manufernandezbur/uniprot2025_03 · Datasets at Fast360

300

A0A1D8EJF9

MAAAEMERTMSFDAAEKLKAADGGGGEVDDELEEGEIVEESNDTASYLGKEITVKHPLEHSWTFWFDNPTTKSRQTAWGSSLRNVYTFSTVEDFWGAYNNIHHPSKLIMGADFHCFKHKIEPKWEDPVCANGGTWKMSFSKGKSDTSWLYTLLAMIGHQFDHGDEICGAVVSVRAKGEKIALWTKNAANETAQVSIGKQWKQFLDYSDSVGFIFHDDAKRLDRNAKNRYTV

Eukaryotic translation initiation factor 4E-1 (eIF4E-1) (eIF-4F 25 kDa subunit) (eIF-4F p26 subunit) (mRNA cap-binding protein)

Solanum pimpinellifolium (Currant tomato) (Lycopersicon pimpinellifolium)

4,084

231

26,042

Cytoplasm;Disulfide bond;Host-virus interaction;Initiation factor;Nucleus;Plant defense;Protein biosynthesis;RNA-binding;Translation regulation

GO:0000340; GO:0003723; GO:0003743; GO:0005634; GO:0005737; GO:0006413; GO:0006417; GO:0016281; GO:0051607

Evidence at protein level

5

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm {ECO:0000250|UniProtKB:C6ZJZ3}. Note=Binds to potyvirus viral genome-linked protein (VPg) in the nucleus and with potyvirus nuclear inclusion protein A (NIa-Pro) and nuclear inclusion protein B (NIb) in the cytoplasm. {ECO:0000250|UniProtKB:C6ZJZ3}.

null

PF01652;

IPR023398;IPR001040;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Solanales (order), Solanaceae (family), Solanoideae (subfamily), Solaneae (tribe), Solanum (genus), Solanum subgen. Lycopersicon (subgenus)

eIF4E1

false

301

A0A1D8PCL1

MSSKIERIFSGPALKINTYLDKLPKIYNVFFIASISTIAGMMFGFDISSMSAFIGAEHYMRYFNSPGSDIQGFITSSMALGSFFGSIASSFVSEPFGRRLSLLTCAFFWMVGAAIQSSVQNRAQLIIGRIISGIGVGFGSAVAPVYGAELAPRKIRGLIGGMFQFFVTLGIMIMFYLSFGLGHINGVASFRIAWGLQIVPGLCLFLGCFFIPESPRWLAKQGQWEAAEEIVAKIQAHGDRENPDVLIEISEIKDQLLLEESSKQIGYATLFTKKYIQRTFTAIFAQIWQQLTGMNVMMYYIVYIFQMAGYSGNSNLVASSIQYVINTCVTVPALYFIDKVGRRPLLIGGATMMMAFQFGLAGILGQYSIPWPDSGNDSVNIRIPEDNKSASKGAIACCYLFVASFAFTWGVGIWVYCAEIWGDNRVAQRGNAISTSANWILNFAIAMYTPTGFKNISWKTYIIYGVFCFAMATHVYFGFPETKGKRLEEIGQMWEERVPAWRSRSWQPTVPIASDAELARKMEVEHEEDKLMNEDSNSESRENQA

High-affinity glucose transporter 1

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

237,561

545

60,670

Cell membrane;Glycoprotein;Membrane;Reference proteome;Transmembrane;Transmembrane helix;Transport

GO:0005351; GO:0005886; GO:0008643; GO:0016020; GO:0030447; GO:0034605; GO:0036168; GO:0036178; GO:0036244; GO:0045916; GO:0052067; GO:0055056; GO:1903561; GO:1904659

Evidence at protein level

5

SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.

null

TRANSMEM 29..49; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 72..92; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 100..120; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 125..145; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 157..177; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 192..212; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 291..311; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 317..337; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 345..365; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 395..415; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 433..453; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 460..480; /note="Helical"; /evidence="ECO:0000255"

PF00083;

IPR020846;IPR005828;IPR050360;IPR036259;IPR003663;IPR005829;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida albicans (species)

HGT1 HGT11 CAALFM_C101980WA orf19.4527

false

302

A0A1D8PDV7

MATLSQPQSALPKTKIATTFGLSKDLKSPISVKVCYLECTRNNVSLVPLSTKFEDPTVFKKLSQIYKNSDLFVEIRVYDGKNNNLISTPVRTSYKAFNNKGRTWNQQLKLNIDYNQISIDAYLKFSICEIIDTKPSVFGVSYLSLFSHDSSTLRSGSHKIPVFMEDDPQYSKNIQYGTLIGLTDLEKRLIDYENGKYPRLNWLDKMVLPKVDATFLKTNNKDHDYYLYIELPQFEFPIVYSDIIYQIPTIEPITETTSKIPPDDTLNSNIIINSIDIPMATSHDPSIMKVYDPDFHITANNHLNPNATTFDPVELKYRKLERNIDNNTILDKELKPTPQLRDELLRIMIKPSNAELTDNEKNLIWKFRYYFSKNNSGNDPSNKSVKSFLPKFLRSINWENDYELDHTFKEIIPFYWNVDKLQIGDALELLGDYFNPYTLGKPTYQDDSMTSKSSKMKSDEKRFIKIYNNVCFLRKLAVERLKLANSEELLLYLLQLVQALKYEALIYEKSPPFCERSDQIEDNASSTLKSPLADFLIERAVENEKLGNFFYWYVKVENEDQLNNPHIDGPIKIYMDILNRYIELLKAHCHENRLPYYKHLKHQIWFIKKLTSLVELLRASFKKNEATAKKVEYLREYLANSGNELLKFPEPFPLPLDPSVMICGCYPEESSVFKSSLAPLKITLKTIEKKKHGHATSQLFGKRSRYGKYPLMFKIGDDLRQDQLVIQIIDLMDQLLKNENLDLKLTPYKILATSPISGLIQFVPNETLDSILSKTYPTSVTYSGGGETSDVPPSVSNNGILNYLRLHSQEQQSEEPISKSILSTNTSQSNTEIPVLPRQPKPTITSDLGVSPILMDNYVKSCAGYCVITYILGVGDRHLDNLLLSPNGKFWHADFGYILGRDPKPFPPLMKLPIQVIDGMGGLHHENYNVFKSYCFITYTTLRKNSNLILNLFQLMLDANIPDIQFDPSRVIEKVQEKFCLQMTEEEAILHFQNLINDSVNAFLPVVIDRLHSLAQYWRA

Phosphatidylinositol 3-kinase VPS34 (PI3-kinase VPS34) (PI3K VPS34) (PtdIns-3-kinase VPS34) (EC 2.7.1.137) (Vacuolar protein sorting-associated protein 34)

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

237,561

1,020

117,469

ATP-binding;Endosome;Golgi apparatus;Kinase;Membrane;Nucleotide-binding;Reference proteome;Transferase

GO:0000045; GO:0000280; GO:0000329; GO:0000407; GO:0000425; GO:0004672; GO:0005524; GO:0005737; GO:0005768; GO:0005777; GO:0005794; GO:0006624; GO:0006897; GO:0006914; GO:0007033; GO:0007034; GO:0009267; GO:0010008; GO:0016020; GO:0016192; GO:0016303; GO:0030447; GO:0030473; GO:0032120; GO:0032968; GO:0034271; GO:0034272; GO:0036092; GO:0036170; GO:0036180; GO:0046854; GO:0048015; GO:0051365; GO:0071470; GO:0071561

Evidence at protein level

5

SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P22543}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22543}. Endosome membrane {ECO:0000250|UniProtKB:P22543}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22543}.

null

PF00454;PF00792;PF00613;

IPR016024;IPR035892;IPR011009;IPR000403;IPR036940;IPR018936;IPR002420;IPR001263;IPR042236;IPR008290;IPR015433;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida albicans (species)

null

false

303

A0A1D8PFP2

MTPSSTKKIKQRRSTSCTVCRTIKRKCDGNTPCSNCLKRNQECIYPDVDKRKKRYSIEYITNLENTNQQLHDQLQSLIDLKDNPYQLHLKITEILESSSSFLDNSETKSDSSLGSPELSKSEASLANSFTLGGELVVSSREQGANFHVHLNQQQQQQQPSPQSLSQSSASEVSTRSSPASPNSTISLAPQILRIPSRPFQQQTRQNLLRQSDLPLHYPISGKTSGPNASNITGSIASTISGSRKSSISVDISPPPSLPVFPTSGPTLPTLLPEPLPRNDFDFAPKFFPAPGGKSNMAFGATTVYDADESMVMNVNQIEERWGTGIKLAKLRNVPNIQNRSSSSSSTLIKVNKRTIEEVIKMITNSKAKKYFALAFKYFDRPILCYLIPRGKVIKLYEEICAHKNDLATVEDILGLYPTNQFISIELIAALIASGALYDDNIDCVREYLTLSKTEMFINNSGCLVFNESSYPKLQAMLVCALLELGLGELTTAWELSGIALRMGIDLGFDSFIYDDSDKEIDNLRNLVFWGSYIIDKYAGLIFGRITMLYVDNSVPLIFLPNRQGKLPCLAQLIIDTQPMISSIYETIPETKNDPEMSKKIFLERYNLLQGYNKSLGAWKRGLSREYFWNKSILINTITDESVDHSLKIAYYLIFLIMNKPFLKLPIGSDIDTFIEIVDEMEIIMRYIPDDKHLLNLVVYYALVLMIQSLVAQVSYTNANNYTQNSKFMNQLLFFIDRMGEVLRVDIWLICKKVHSNFQQKVEYLEKLMLDLTEKMEQRRRDEENLMMQQEEFYAQQQQQQQQQQQQPKHEYHDHQQEQEQQEQLQEEHSEKDIKIEIKDEPQPQEEHIHQDYPMKEEEENLNQLSEPQTNEEDNPAEDMLQNEQFMRMVDILFIRGIENDQEEGEEQQQQQQQQEQVQQEQVQQEQVQQDQMELEEDELPQQMPTSPEQPDEPEIPQLPEILDPTFFNSIVDNNGSTFNNIFSFDTEGFRL

Transcription factor ROB1 (Regulator of biofilm 1)

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

237,561

991

113,686

DNA-binding;Metal-binding;Nucleus;Reference proteome;Transcription;Transcription regulation;Zinc

GO:0000785; GO:0000981; GO:0001216; GO:0005634; GO:0006351; GO:0006357; GO:0008270; GO:0030447; GO:0036180; GO:0043565; GO:0044011; GO:1900231; GO:1900445

Evidence at transcript level

5

SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.

null

PF04082;PF00172;

IPR051615;IPR007219;IPR036864;IPR001138;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida albicans (species)

ROB1 CHA4 CAALFM_C113620WA orf19.12465

false

304

A0A1D8PHA3

MFRTAYKTMNQSMVQKFIAGGVGVTGLTASYLLYQDSMTADAMTAAEHGLHPPAYNWPHNGMFETFDHASIRRGFQVYREVCAACHSLDRIAWRNLVGVSHTTSEAKAMAEELEYDDEPDDEGKPRKRPGKLADYIPGPYENEQAARAANQGAYPPDLSLIVKARHGGSDYIFSLLTGYPDEPPAGVVLPEGSNYNPYFPGGAIAMGRVLFDDLVEYEDGTPATTSQMAKDVSTFLNWASEPEHDDRKKWGLKALVVLSSLYLLSIWVKRFKWTPIKNRKFRFDPPKK

Cytochrome b-c1 complex catalytic subunit, mitochondrial (EC 7.1.1.8) (Complex III catalytic subunit)

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

237,561

288

32,221

3D-structure;Electron transport;Heme;Iron;Membrane;Metal-binding;Mitochondrion;Mitochondrion inner membrane;Reference proteome;Respiratory chain;Translocase;Transmembrane;Transmembrane helix;Transport

GO:0005743; GO:0005886; GO:0006122; GO:0008121; GO:0009055; GO:0020037; GO:0045275; GO:0046872

Evidence at protein level

5

SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P07143}; Multi-pass membrane protein {ECO:0000255}.

null

TRANSMEM 12..34; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 250..268; /note="Helical"; /evidence="ECO:0000255"

PF02167;

IPR009056;IPR036909;IPR002326;IPR021157;

7RJA;7RJB;7RJC;7RJD;7RJE;

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida albicans (species)

CYT1 CYT12 CAALFM_C204950CA orf19.11011

false

305

A0A1D8PJA8

MKFSSTTLLAGLSSLTATVSAGCSFEGGNYYCSETKKVIYKGIGFSGTYMDVTNMDESTGKCTQQSYSFSGNLSPLDEELSVHFRGPLTLLQFGVYYPSSSGNSKRQIDDQDCNVKHVHHKHKRATEVVQVTQTVFVDGNGNTVTSQALQTSTVESSPAVSSAAADDNANSGSGSGSSAGSGSGYGSVSALDGEGKAYRSDISTKSAPTSTSAQPSSSETASVDGAWTRDSYYTPGSTDNCVFLNYHGGSGSGVWSAKFGNSLSYANADNSGGSSTPVPLEETTIKSGEEYIIFSGSKCGSSSDCGYYRKGTVAYHGFKGASKIFVFEFEMPSDTNGNGYNQDMPAVWLLNAKIPRTLQYGEATCSCWKTGCGELDLFEVLSSGSNKMISHLHDGQGSSQNSNNGGGGSQDYFERPTSGTFKGVVIFEGDEIHILQVDDETEFGSSLDEETVNAWLKEAGSVATIGY

Probable circularly permuted 1,3-beta-glucanase TOS1 (EC 3.2.1.39) (Secreted protein TOS1)

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

237,561

467

49,230

Cell wall biogenesis/degradation;Glycosidase;Hydrolase;Reference proteome;Secreted;Signal;Virulence

GO:0005576; GO:0009277; GO:0009986; GO:0016798; GO:0030446; GO:0071555

Evidence at protein level

5

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26453650, ECO:0000303|PubMed:17905924}.

SIGNAL 1..21; /evidence="ECO:0000255"

null

PF10287;PF10290;

IPR018805;IPR018807;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida albicans (species)

TOS1 CAALFM_C301550CA orf19.9258

false

306

A0A1D8PJX3

MSSLAFRTLRNGLGLKSSVRALSTTTTTLSNYQQPDYSSYLNNKSGQGSRNFTYFMVGSMGLLSAAGAKSTVEAFLSSFAASADVLAMAKVEVKLGAIPEGKNVIIKWQGKPVFIRHRTADEIEEANQVDIKTLRDPQNDADRVKKPEWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPEYDFTDDETLLVG

Cytochrome b-c1 complex subunit Rieske, mitochondrial (EC 7.1.1.8) (Complex III subunit 7)

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

237,561

213

23,207

2Fe-2S;3D-structure;Disulfide bond;Electron transport;Iron;Iron-sulfur;Membrane;Metal-binding;Mitochondrion;Mitochondrion inner membrane;Reference proteome;Respiratory chain;Transit peptide;Translocase;Transmembrane;Transmembrane helix;Transport

GO:0005743; GO:0005886; GO:0006122; GO:0008121; GO:0016491; GO:0045275; GO:0046872; GO:0051537

Evidence at protein level

5

SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P08067}; Single-pass membrane protein {ECO:0000250|UniProtKB:P08067}.

null

TRANSMEM 48..77; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P08067"

PF00355;PF02921;

IPR037008;IPR017941;IPR036922;IPR014349;IPR005805;IPR004192;IPR006317;

7RJA;7RJB;7RJC;7RJD;7RJE;

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida albicans (species)

RIP1 CAALFM_C304430WA orf19.13314

false

307

A0A1D8PN96

MDTSSSSGTHPSTFNNLTKQQELTGNDPNDTNRKRIRVACDSCRRKKIKCNGSYPCGNCIQAKNTSNCHFTERPVRKKLKPTKQDNKSTANSNGVSKRKYNDTFSGNSINIKTEKQENTTFGINDNKSSDLESRLSRIENSMSRMMHTLENFSQNFMTQAIRNNHSNSSMFNNNSLSPTPSEDFNKSAFDSEEQQTSHSYKNLKDRVKDANELLKLRNWDEFVGTHSITCIFSRESLDWMEKTLGSYGEEYLTPIRNLPLVFHSELKPYIMKWIDPPVVDKLQRKKLLESPFPTDSKLISKLIDLYYEETSMINILVDESRVRSLFAAYYNNFAEPIATKRRRFKLSELLLMTSILLISLSCLTEDDFSEERITTPASSTSSNYSAASANLLGDYNKNRLIALQNSLENSAIFYYHRISVISEGLETVEALLMFIIYVESNWLTSFFNYTIITVTIRFAQEIGLHRAETYNNLDLEEATKRRKIWWFCYFFDIEFSFKSGKPPVINTNDVTTNSDEDLLRVITQLKQYGPLSPKDRMYSPVCHTISTSLLDLSGSDSICLDILKIIQSGDILDDPFYFQFCALLQSRIRSNSYHDLFIASAEKRDFSSISNTLEKLNADMFELAMYLADEAKPRFYNDPKFTSVQASTGTSIRRDTILAMKLTFFSHLMIINRYPLMIATEDSKFDDRVIKFRNLSLDSARTILMLIKGWHRESASALFYNWAIYFPVAAYLVLVAAIINHPQLPESGTNLNLLIETSLSFFKSSKQWNSSNDSQDKQQNSTICVNKIVAIELIVRLMLRVVIKVYELHNNVEILANNPALQNHLQEAEEKFPDIFQNHAEFTSKMIALVGASPFGGCGSRNTSSCNLRDNSTNHGQNNMNPSPTITNNTYNSNINTGSNSTGEPQVCYAQSPSYNASLSNIINNESTGRSPATSTSINQSMMNENYDLFNDYLIDNSAVNLPFSQFNNLPNFFFDNNLGI

Transcription factor TAC1 (Transcriptional activator of CDR genes 1) (Zn(2)-Cys(6) DNA-binding domains containing protein 2)

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

237,561

981

111,696

DNA-binding;Metal-binding;Nucleus;Reference proteome;Transcription;Transcription regulation

GO:0000978; GO:0000981; GO:0001216; GO:0003677; GO:0003713; GO:0005634; GO:0005667; GO:0006351; GO:0006357; GO:0008270; GO:0030447; GO:0034599; GO:0036180; GO:0043565; GO:0045944; GO:0071383; GO:1900445; GO:2001038

Evidence at protein level

5

SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:15590837, ECO:0000269|PubMed:19561319}.

null

PF04082;PF00172;

IPR050987;IPR007219;IPR036864;IPR001138;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida albicans (species)

TAC1 ZNC2 CAALFM_C501840CA orf19.10700

false

308

A0A1D8PNR5

MAQLSSQGNNAIIYLSYAFMLATGLFLAWKFSSNKDFLSSNGTQRGIPLALNFVASAMGVGIITTYAQIANIAGLHGLLVYTICGAIPIVGFAVVGPVIRRKCPDGFILTEWVRHRFGMVTALYLSAFTCLTMFLFMVGELSAIRSAIETLTGLNALGAVIVECVVTTIYTFFGGFRVSFITDNFQGVCVLLLLIICAAGMGSYIEIDTSKIGPSGLLKANKLGWQLVYILFVAIVTNDCFMSGFWLRTFASKTDKDLWIGTSIAAFVTFAICTLIGTTGFLAVWSGDLIVGDENGYDAFFILLSKMPRWLVAFVLIFCIVLSTCTFDSLQSAMVSTISNDVFRNKLHINYVRIMLILIMVPIVVLAVKVADNILQIYLIADLVSAAIIPSVFLGLADTWFWYLRGFDVMAGGLGALLGVFIFGTVYYHSAREGGKLLLIWNGLYDSSDWGPFGAFVIAPVGGVIITLASAALRIAVLYAYSKVTGKEFTALDKPVTVEVENQDHTYGSIDDDESDTKKVV

Spermidine transporter DUR31

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

237,561

521

56,592

Glycoprotein;Membrane;Reference proteome;Transmembrane;Transmembrane helix;Transport

GO:0005886; GO:0009267; GO:0015606; GO:0015848; GO:0030447; GO:0036170; GO:0036180; GO:0044182; GO:0051454; GO:0055085; GO:0071248

Inferred from homology

5

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.

null

TRANSMEM 11..31; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 47..67; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 79..99; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 117..137; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 156..176; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 187..207; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 227..247; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 264..284; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 310..330; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 354..374; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 377..397; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 406..426; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 453..473; /note="Helical"; /evidence="ECO:0000255"

PF00474;

IPR038377;IPR001734;IPR050277;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida albicans (species)

DUR31 CAALFM_C503480CA orf19.6656

false

309

A0A1D8PPK1

MTIESTNSFVVPSDTELIDVTPLGSTKLFQPIKVGNNVLPQRIAYVPTTRFRASKDHIPSDLQLNYYNARSQYPGTLIITEATFASERGGIDLHVPGIYNDAQAKSWKKINEAIHGNGSFSSVQLWYLGRVANAKDLKDSGLPLIAPSAVYWDENSEKLAKEAGNELRALTEEEIDHIVEVEYPNAAKHALEAGFDYVEIHGAHGYLLDQFLNLASNKRTDKYGCGSIENRARLLLRVVDKLIEVVGANRLALRLSPWASFQGMEIEGEEIHSYILQQLQQRADNGQQLAYISLVEPRVTGIYDVSLKDQQGRSNEFAYKIWKGNFIRAGNYTYDAPEFKTLINDLKNDRTIIGFSRFFTSNPDLVEKLKLGKPLNYYNREEFYKYYNYGYNSYDESEKQVIGKPLA

Probable NADPH dehydrogenase (EC 1.6.99.1) (Estrogen-binding protein) (EBP)

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

237,561

407

46,089

Flavoprotein;FMN;NADP;Oxidoreductase;Reference proteome

GO:0000324; GO:0003959; GO:0005496; GO:0008202; GO:0009986; GO:0010181; GO:0030446; GO:0042562; GO:0099130

Evidence at transcript level

5

null

PF00724;

IPR013785;IPR001155;IPR045247;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida albicans (species)

EBP1 orf19.125 CAALFM_C601180CA

false

310

A0A1D8PQ86

MLPQFLLLLLYLTVSTAKTITGVFNSFDSLTWTRSVEYVYKGPETPTWTAVLGWSLNSTTADAGDTFTLIMPCVFKFITSQTSVDLTADGVSYATCDFNAGEEFTTFSSLSCTVNSVSVSYDKASGTVKLPITFNVGGTGSSVDLTDSKCFTAGKNTVTFMDGDTKISTTVDFDASPVSPSGYITSSRIIPSLNKASSLFVSPQCENGYTSGIMGFVTSQGATIDCSNINIGISKGLNDWNFPVSSESFTYTKTCSSSGIIVEYENVPAGYRPFVDAYISSENVEQYTLTYANEYTCKNGNTVVDPFTLTWWGYKNSEADSNGDIIVVTTKTVTASTTAVTTLPFNPTVDKTETIEVLQPIPTTTITTSYIGISTSYETFTATIGGTATVIVDTPYHITTTVTTFWTGSVTTTTTYSNPTGSIDTVIVQIPSPDPTTTITEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTPSVSSFESKTFYSSEAQSSLEIDSSNTFMTSISVSTASSYDESSTIVSSAFPTLHISSYSLSTSFVPPVTLPRYVNTTISSSPSFESSSMYSSVTSAVTSIDNDREVPTSTTTYLHSKLYSESISTVIQTKSSDWSLSLGNSNKPESASTVSEESLHYLSTPGPSSSEYSISFTSEKEGHVSSYVPRVSYTSSVKVSISSTMSSENGMSATHTFGISTNTIPSSTETSIKSATVTTPVSESTNTGMSIFMSTTTESKTTDITTETSVSGEVNLGSATVKVSSSEFISKGTVTRIMPTELTNSESTFTASPSFVLTSTESSVIETPATIEMSSRSSSYSVPLSKLRSEGETTRVIPTSSTATGSTVIGSPSSVSTSNESIITGSSSFVSTTAETISTRSIVTESIVAGSPSLVLTTTVLDTTETTITETSIVGESSSRSLTFKASSLSKGEITGTVTPEMSVSTSKATTGTTSEVSIKESLTTKVPTFTSTTIKPETSETQHSESRTTQIPYSETKGSQLSTANSQVSQTGSSKSSIFESAISKDESTFVSATVKSITTPAVTQYQTSLPNPAVSVSEESGKKSSIIESQTENSATQHSIYFDSIETSTLSNTLANTLVSGAMKNSETTSELTTSDKAIGFSTTTETSIPGATNSALSPSVDSGKSSMLGWSGGIVSTVSTSTRLEDSTATSSSITAANQDSLNPSTVSKYPHGSETIDNGSNGSSHSSSALASTISASHSIKFSAHQTTLSQSLISSSTKTVIASTYDGSGSVIKLHSWFYGLVTIFFLFI

Agglutinin-like protein 9 (Adhesin 9)

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

237,561

1,890

201,290

3D-structure;Cell adhesion;Cell membrane;Cell wall;Disulfide bond;Glycoprotein;GPI-anchor;Lipoprotein;Membrane;Reference proteome;Repeat;Secreted;Signal;Virulence

GO:0005886; GO:0007155; GO:0009986; GO:0030445; GO:0030446; GO:0030448; GO:0043709; GO:0043710; GO:0044011; GO:0098552; GO:0098609; GO:1903561

Evidence at protein level

5

SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. Secreted, cell wall. Note=Identified as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer. {ECO:0000305|PubMed:12845604}.

SIGNAL 1..17; /evidence="ECO:0000255"

null

PF05792;PF11766;

IPR008966;IPR008440;IPR024672;IPR043063;IPR033504;IPR011252;

2Y7L;2Y7M;2Y7N;2Y7O;2YLH;

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida albicans (species)

ALS9 ALS11 CAALFM_C603710WA orf19.13164 orf19.5742

false

311

A0A1D8PQB9

MLLQFLLLSLCVSVATAKVITGIFDSFNSLTWTNAASYSYRGPANPTWTAVIGWSLDGATASAGDTFTLDMPCVFKFITDQTSIDLVADGRTYATCNLNSAEEFTTFSSVSCTVTTTMTADTKAIGTVTLPFSFSVGGSGSDVDLANSQCFTAGINTVTFNDGDTSISTTVDFEKSTVASSDRILLSRILPSLSQAVSLFLPQECANGYTSGTMGFSTAGTGATIDCSTVHVGISNGLNDWNYPISSESFSYTKTCTSTSVLVTYQNVPAGYRPFVDAYVSATRVSSYAMRYTNIYACVGAASVDDSFTHTWSGYSNSQAGSNGITIVVTTRTVTDSTTAVTTLPFNSESDKTKTIEILQPIPTTTITTSYVGVTTSYSTKTAPIGETATVIVDVPYHTTTTVTSEWTGTITTTTTRTNPTDSIDTVVVQVPSPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPNPTVTTTEYWSQSYATTTTVTSPPGGTDIVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPNPTVTTTEYWSQSYATTTTVTSPPGGTDIVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPSPTVTTTEYWSQSYATTTTVTAPPGGTATVIIKEPPNYTVTTTEYWSQSYATTTTITAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPSPTVTTTEYWSQSYATTTTVTAPPGGTATVIIREPPNYTVTTTEYWSQSYATTTTITAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPNPTVTTTEYWSQSYATTLTITAPPGGTNSVIIRVHSSTNDESSESTFSTLSVPSFSGSISIVSTVSRPHYVNSTVTHLPSSSSKPVDIPSSDVVTSTNDNSLTSLTGSENGKTSVAISTTFCDDENGCQTSIPQGSVVRTTATTTATTTTIIGDNNGSGKSKSGELSSTGSVTTNTATPDVPSTKVPSNPGAPGTGVPPPLAPSTETQTTNNVPGSPNIPATGTTDIIRESTTVSHTVTGNGNTGVPMNPNPVLTTSTSLTGATNSATNPSHETSVNTGSGGSTNIVTPPSSATATVVIPGTDNGATTKGQDTAGGGNSNGSTATTNIQGGNNEPGNQPGTNTTGEPVGTTDTQSVESISQPTTLSQQTTSSLISTPLASTFDGSGSIVQHSGWLYVLLTAISIFF

Agglutinin-like protein 4 (Adhesin 4)

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

237,561

2,100

220,888

Cell adhesion;Cell membrane;Cell wall;Disulfide bond;Glycoprotein;GPI-anchor;Lipoprotein;Membrane;Reference proteome;Repeat;Secreted;Signal;Virulence

GO:0005576; GO:0005886; GO:0009277; GO:0009986; GO:0030445; GO:0030446; GO:0030448; GO:0043709; GO:0043710; GO:0044011; GO:0044406; GO:0071502; GO:0098552; GO:0098609; GO:1903561

Evidence at protein level

5

SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:12845604}. Secreted, cell wall {ECO:0000269|PubMed:22106872}. Note=Identified as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer (Probable). Covers the surface of yeast-form cells (PubMed:22106872). {ECO:0000269|PubMed:22106872, ECO:0000305|PubMed:12845604}.

SIGNAL 1..17; /evidence="ECO:0000255"

null

PF05792;PF11766;

IPR008966;IPR008440;IPR024672;IPR043063;IPR033504;IPR011252;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida albicans (species)

ALS4 ALS12 CAALFM_C604130CA orf19.4555 orf19.4556

false

312

A0A1D8PS71

MVSVSKLINNGLLLTSQSVFQDVATPQQASVQQYNILNFLGGSAPYIQRNGYGISTDIPAGCEIAQIQLYSRHGERYPSKSNGKSLEAIYAKFKNYNGTFKGDLSFLNDYTYFVKDQSNYAKETSPKNSEGTYAGTTNALRHGAAFRAKYGSLYKENSTLPIFTSNSNRVHETSKYFARGFLGDDYEEGKTVKFNIISEDADVGANSLTPRSACSKNKESSSSTAKKYNTTYLNAIAERLVKPNPGLNLTTSDVNNLFSWCAYEINVRGSSPFCDLFTNEEFIKNSYGNDLSKYYSNGAGNNYTRIIGSVILNSSLELLKDTENSNQVWLSFAHDTDLEIFHSALGLLEPAEDLPTSYIPFPNPYVHSSIVPQGARIYTEKLQCGNDAYVRYIINDAVVPIPKCATGPGFSCKLDDFENFVKERIGDVDFIKQCGVNSTYPSELTFYWDYKNVTYNAPLEL

Phytase PHO112 (EC 3.1.3.-) (EC 3.1.3.8) (Histidine acid phosphatase PHO112) (HAP) (Myo-inositol hexakisphosphate phosphohydrolase PHO112) (Myo-inositol-hexaphosphate 3-phosphohydrolase PHO112)

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

237,561

461

51,296

Disulfide bond;Glycoprotein;Hydrolase;Reference proteome;Secreted;Virulence

GO:0003993; GO:0005576; GO:0008707; GO:0009277; GO:0009986; GO:0030287; GO:0030448

Evidence at protein level

5

SUBCELLULAR LOCATION: Secreted {ECO:0000305}.

null

PF00328;

IPR033379;IPR000560;IPR029033;IPR016274;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida albicans (species)

PHO112 CAALFM_CR02400WA orf19.11211

false

313

A0A1D8PT03

MKIAIIQYSTYGHITQLAKAVQKGVADAGYKADIFQVPETLPQEVLDKMHAPAKPTDIPIATNDTLTEYDAFLFGVPTRYGTAPAQFFEFWGATGGLWANGSLAGKPAGVFVSTSGQGGGQETTVRNFLNFLAHHGMPYIPLGYANAFALQSSMEEVHGGSPYGAGTFANVDGSRQPSTLELEIAEKQGEAFVKSATKLVKGSKKTNTTTTSKSAATSDAAGTTSGTAAGTSAATGAATGTSAPKESTKEASSSAKKEATNGTATRTQQSTKAPETAEKSSCSKCIIM

NAD(P)H quinone oxidoreductase YCP4 (EC 1.6.5.2) (Flavodoxin-like protein YCP4) (FLP YCP4)

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

237,561

288

29,783

Cell membrane;Flavoprotein;FMN;Membrane;NAD;Nucleotide-binding;Oxidoreductase;Reference proteome;Virulence

GO:0003955; GO:0005737; GO:0005886; GO:0010181; GO:0016020; GO:0032126; GO:0034599; GO:0062040; GO:0160020

Evidence at transcript level

5

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26325183}; Peripheral membrane protein {ECO:0000269|PubMed:26325183}.

null

PF03358;

IPR008254;IPR029039;IPR010089;IPR005025;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida albicans (species)

YCP4 CAALFM_CR05380CA orf19.5286

false

314

A0A1D8PTL7

MLYRVSGFYKRHTRNFTNIDYGYYIRNFIHHIASKIYPYAKVVLPNFRAAHYFYILTLVILGSILVYPVKTCAYIDVLFFTAGASTQAGLNTVNVNDLSLYQQIVLYLLATLATPIFIHGSLLFVRLYYFERHFDNIKERSLMDYRMRKSATLARLGSAPTMSSTRLNTFNNQVLGFQEREAEKGSSSSPQSSSSQTSQPVSTAYNDQGGNDIEHHSEPSDSDDDESGNGPVTFQEKIHFEEPQRPRSQRRHSRTDSGIKFSALPHPRRRKSIDPEDMYRSINMLQEHKKNQEAKSKGIQFLNIGSPVRRKSRSSNIEAFPEEDTNPSRGDEITPATNSVGTGNNDEDEDDILIIKPPIEIENSDEANPIFTKKKKLASQIQFKETPGKAKKWITTKTRKHYNPWTSKLKKTLSNSSKKGSLSVVPTDTEDDSEDEEYASIDSETSDISDNEHAADNAEGSDVDSVGSYEEDEDEDEHNSDDDDDGEGERRLGNGASLTKAQSHLVLPSKDETGGKKYTKRSNTLDTPQQNTSDGRKIRKKAPKRKTPRTQRNASFNQHSNVSIGDGSIENVDTNDSYQRLSRTMSGNYLSWTPTVGRNSTFIKLTDEQKEELGGIEYRAVKLLIKIIVVYYVGFNIIPGVMLSIWIYCMPHYKNLMISSSISPAWWAFFTSQSSFNDLGLTLTSNSMMSFNQNAFVQILCSFLIVIGNTGFPILLRFIIWVMFKTARPLSLYKESLGFLLDHPRRCFTLLFPSVPTWWLFFILVVLNGFDLVIFCILDLHDDTFKGVDMGYRVLNGLFQAFCTRTVGFSVMDLSQLHAATQVSYLIMMYISVLPIAISVRRTNVYEEQSLGVYAKENAEGVDESAPSNYVGSHLRNQLSYDLWYICLGLFIICIAEGKRLKEQDLRFSIFAVLFEIVSAYGTVGMSMGYPGVDCSLSGEFNVISKLVIIAMMIRGRHRGLPYTIDRAIMLPNAAMKRHDRLQEEHAINRHNTMERTTTLGRVATFGNGPIDGGNNLLTRAITNIEHRLRNRRDGRSESSTVSEDPRYVVRTVSEV

Potassium transporter TRK1

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

237,561

1,056

119,431

Cell membrane;Chloride;Chloride channel;Ion channel;Ion transport;Membrane;Potassium;Potassium transport;Reference proteome;Transmembrane;Transmembrane helix;Transport

GO:0005254; GO:0005886; GO:0006821; GO:0009636; GO:0015079; GO:0015108; GO:0016020; GO:0030007; GO:0034707; GO:0140107; GO:1990573

Evidence at protein level

5

SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:19175416}; Multi-pass membrane protein {ECO:0000255}.

null

TRANSMEM 47..67; /note="Helical; Name=1"; /evidence="ECO:0000305|PubMed:19175416"; TRANSMEM 100..122; /note="Helical; Name=2"; /evidence="ECO:0000305|PubMed:19175416"; TRANSMEM 623..646; /note="Helical; Name=3"; /evidence="ECO:0000305|PubMed:19175416"; TRANSMEM 694..710; /note="Helical; Name=4"; /evidence="ECO:0000305|PubMed:19175416"; TRANSMEM 755..778; /note="Helical; Name=5"; /evidence="ECO:0000305|PubMed:19175416"; TRANSMEM 818..841; /note="Helical; Name=6"; /evidence="ECO:0000305|PubMed:19175416"; TRANSMEM 875..896; /note="Helical; Name=7"; /evidence="ECO:0000305|PubMed:19175416"; TRANSMEM 943..965; /note="Helical; Name=8"; /evidence="ECO:0000305|PubMed:19175416"

PF02386;

IPR003445;IPR004773;IPR015958;IPR051143;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida albicans (species)

TRK1 CAALFM_CR07960CA orf19.8233

false

315

A0A1D9BZF0

MDSGSSSSSSSSGSSSGSCSTSGSGSTSGSSTTSSSSSSSSSSSSSSSSSSKEYMPELPKQRKASCVVIDSESDSDNTSDEKNTTVCEISSGDETSDIDRPGGQKLPLIVIDDDDDGSPDLKNTKQKSDEPQMSVLEKEGVECIGSDSTSPHDVCEIWDVCGSSNQTSSELEPEGEPESEAKGEPESEAKGEPESEAKGEPESEAKGESESEAKGEMETEAKGESESEAKGEMETEAKGESESEAKGEMETEAKGEPESEAKGEMETEAKGEPESEAKGEMETEAKGESESEAKGEMETEAKGESESEAKGEMETEAKGEPESEAKGEMETEAKGEPESEAKGEPEPEAAKGEMETEAAMGEVETEAAMGEPEQEITAEEAKKKRAAYLLAQQRKRKRKNRFICMSSSKPRRKRRRADPQDGADPQDGADPQDRADPQDLADPQDRGDSQDMPSLPGTSDEPIPSGQPVCPRKGMASSRGRGRGRGRGRGRGRGRGRGRGRGAKAGK

Germ cell nuclear acidic protein (Acidic repeat-containing protein) (Germ cell nuclear antigen)

Mus musculus (Mouse)

10,090

507

53,394

Chromosome;Nucleus;Reference proteome

GO:0000793; GO:0006974; GO:0007129; GO:0010032; GO:0016605; GO:0031570; GO:0035825; GO:0106300

Evidence at protein level

5

SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:31839538}. Nucleus, PML body {ECO:0000269|PubMed:31839538}. Nucleus {ECO:0000269|PubMed:27718356}. Note=Co-localizes with SUMO2 at PML bodies in all interphase cells (By similarity). Localizes on condensed chromosomes in spermatocytes in G2 and M during meiotic prophase (PubMed:31839538). {ECO:0000250|UniProtKB:Q96QF7, ECO:0000269|PubMed:31839538}.

null

IPR050972;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Glires (clade), Rodentia (order), Myomorpha (suborder), Muroidea (clade), Muridae (family), Murinae (subfamily), Mus (genus), Mus (subgenus)

Gcna

false

316

A0A1E1FFL0

MAPMIPPRLQRFPATASADEIFAAFQEDGCVVIEGFISPEQVARFSQEVDPAMEKIPVEVTNNGNSNDRTKRFSKCVIASPTFRNEIIESDLMHELCDRVFSKPGEGMGYHFNDNMVIEVQPGAPAQRLHRDQELYPWWNSMGPAGPECVINFFCAVTPFTEENGATRLVPGSHLWPEFTQINERDCPQFGKIETVPAIMQPGDCYLMSGKVIHGAGHNATTTDRRRALALAIIRRELRPMQAFSLSVPMKLAREMSERSQTMFGFRSSVQHCDVDMVHFWGNDGKDIAHHLGLEAPSVHV

Multifunctional dioxygenase prhA (EC 1.14.11.-) (Paraherquonin biosynthesis cluster protein A)

Penicillium brasilianum

104,259

301

33,731

3D-structure;Dioxygenase;Iron;Metal-binding;Oxidoreductase

GO:0046872; GO:0051213; GO:0140874

Evidence at protein level

5

null

PF05721;

IPR008775;

5YBM;5YBN;5YBO;5YBP;5YBQ;5YBR;5YBS;5YBT;

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), Eurotiomycetes (class), Eurotiomycetidae (subclass), Eurotiales (order), Aspergillaceae (family), Penicillium (genus)

prhA

false

317

A0A1E3P8S6

MFFTKVLNNQVANGLKQLPVHKRVQMAYDLHIPNKTVNPNLNIRSHEPIVFVHGIFGSKKNYRHDCQKIANVTHTPVYTIDLRNHGQSMHALPFDYETLAQDVTDFCEDHGLKKVNLIGYSLGAKICMLTMLQNPDLVRSGVIIDNSPIEQPHIEIFLTQFIKSMLHVLNSTKIRADDKDWKSKANQAMRRYIPNGGIRDYLLANLINKVPKGYKSPVINYDDGYIHFQNPVRHMTEVAVKNVSAWPTEHVKGLKFEGQVRFLKGTKSAFIDEKGLEAIKEYFPNYSLSELNATHFILNERPQEYVKLICDFIKVNRYKSLQEHIRHVENFSSAELEARHNAEHERQMEELRQLTQTTPTAEQVKTIDNLASKVDLSATERQQQQNKEITV

Ethanol acetyltransferase 1 (EC 2.3.1.268) (Acetyl-CoA hydrolase) (EC 3.1.2.1) (Acetyl-CoA thioesterase) (Alcohol acetyltransferase) (AAT) (Ethyl acetate esterase) (EC 3.1.1.-)

Wickerhamomyces anomalus (strain ATCC 58044 / CBS 1984 / NCYC 433 / NRRL Y-366-8) (Yeast) (Hansenula anomala)

683,960

391

45,069

Coiled coil;Hydrolase;Mitochondrion;Reference proteome;Transferase;Transit peptide

GO:0003986; GO:0005739; GO:0016740; GO:0052689

Evidence at protein level

5

SUBCELLULAR LOCATION: Mitochondrion.

null

PF00561;

IPR000073;IPR029058;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Saccharomycetes (class), Phaffomycetales (order), Wickerhamomycetaceae (family), Wickerhamomyces (genus), Wickerhamomyces anomalus (species)

EAT1 WICANDRAFT_27004

false

318

A0A1F4

MSNVHQFDTQTMAESPQIRRDMGRLCATWPSKDSEDGAGTALRAATPLTANGATTTGLSVTLAPKDMQRNHLLKMPTATIEKPTITATIASSSSTSTSTTRKSVTATRSLKLNPNILLPTLRILARGLLLPALILAILVGSSQAGFACLSNPCVFGVCIDGLNSSYSCYCIDGYTGIQCQTNWDECWSSPCQNGGTCVDGVAYYNCTCPEGFSGSNCEENVDECMSNPCQNGGLCRDRTNGYICTCQPGYLGSHCELDVAVCETGTGARCQHGGECIEGPGLEFTCDCPAGWHGRICQEEINECASSPCQNGGVCVDKLAAYACACPMGYTGINCEEEILICADNPCQNNALCLMEEGVPTCYCVPDYHGEKCEFQYDECQLGPRCMNGGVCIDGVDTFSCSCPPLLTGMLCECLMVGEESLDCNYTAPATQSPPRRTTTTSTMAPPTVRPVTPPETTVSPSRASEEVEIIVVTTSAPAEVVTSVLSPSSSSSSSEEGVSVEIKTPTVAPPESGSHSISVEQTTAVPAQPEPESEQEPESKPHPESESASESETETEEEIIPGTTARPPTSRSSSSSEESPSIFTTLPPLPGKPQTSASSESSGEVVTSEEYTTVPHFEVSGSKSESGSEEVTTVRPTAAPSITISVDITSSGSSSSSSESVEVFTTPAPVFVQRVTTIETSISIDYVTPTPLPETTTPRVVPVPRPTFAPEPPLDVVETTASTHHLWTEVPTTAAPFFTEYPAEVLITTHRTSAGRFTTVQPPAGVTTTSPTEDSSVELPTPHTPQIVVTILDSNEVIPSLITTTGSPTTHHHHHHHPHHEAEGTTLQPLEEDEHHHHHHHDEFTTPQPVEITTGHPLQTEDLIGVQEPAVVTTESPFAPAETTVVPVVVPATIAPLGTAAPPATPAPVPPATTTPPPSPPSLATETPTLPPTLPPVTLPPVTQPPPTIPPTPPSTQSAQTLPPPTSAINVYTTPDGPPTASQTKPSVTESSEEVEGTNTVSTGGRGSGGVPEEKAGDVDCIKLGCYNGGTCVTTSEGSRCVCRFDRQGPLCELPIIIRNAAFSGDSYVSHRIYKDIGGHESLDAVLPMHIQLKVRTRATNGLIMLAAAQGTKGGHYMALFLQKGLMQFQFSCGLQTMLLSELETPVNTGHEITIRAELDFSRNYTHCNASLLVNDTLAMSGDQPTWLKLLPPRLHTPEAILNTWLHLGGAPQAPIGLIIELPPAQSGSGFTGCLHTLRINGQAREIFGDALDGFGITECGSLACLSSPCRNGAACIKIETNDLDENGEKAEKWKCKCPTGYMGPTCEISVCEDNPCQYGGTCVQFPGSGYLCLCPLGKHGHYCEHNLEVALPSFSGSVNGLSSFVAYTVPIPLEYSLELSFKILPQTMSQISLLAFFGQSGYHDEKSDHLAVSFIQGYIMLTWNLGAGPRRIFTQKPIDFRLDAPRVPYEIKVGRIGRQAWLSVDGKFNITGRSPGSGSRMDVLPILYLGGHEIANFNTLPHDLPLHSGFQGCIYDVQLKAGQVTVPLQETRGVRGRGVGQCGTRECHRHACQHDGACLQHGATFTCICQEGWYGPLCAQPTNPCDSFNNKCYEDATCVPLVNGYECDCPVGRTGKNCEEVIRSLSDVSLTGRRSYLAVRWPYLYDGGDKLGAKRSQMVSYRNFTKKLMPPKPITTPSSHFVMKLLNEVEKQRSFSPVPLMGSKSFEEHHRVQFFFIEFQLRPLSERGLLLYFGTLNNNQDKKIGFVSLSLQGGVVEFRISGPSNHVTVVRSVRMLAIGEWHKIKMAQRGRWLTLWVEGSASSALAPSAEVLVEPDSLLYIGGLKDVSKLPHNAISGFPIPFRGCVRGLVVSGTRIVLNETNIVESRNIRDCDGTACGGDSCESGGHCWLDEKLQPHCICPEYAKGDRCEYSETCKLIPCKNNGRCLRSGRCSCPNGWGGFYCEIAMSKPTTPSFRGNSYLILPPPRIPMKDKRRGPSLYVRPREAIQVSLNFSTIEPDGLLLWSEHERSKFLGLGLEAGHLKLASNLLGSTNDTVRAPASGFIADGAWHWTSVLLDRSRLELQLDGEVIFTERLPEGGRSLGSTTPRSTLAGRRKNSSKEPTISYEDVFYLGGFPNSDSVSRRTKGRFFDPFKGCLQDIQFGAEPTAIISDFSTYQGENIGSCDLHGDEPLTV

Protein eyes shut (Protein spacemaker)

Drosophila melanogaster (Fruit fly)

7,227

2,176

234,104

Calcium;Disulfide bond;EGF-like domain;Glycoprotein;Membrane;Reference proteome;Repeat;Secreted;Transmembrane;Transmembrane helix

GO:0000902; GO:0005201; GO:0005509; GO:0005576; GO:0005615; GO:0009986; GO:0010378; GO:0016020; GO:0031012; GO:0042052; GO:0097730

Evidence at protein level

5

SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:17011488, ECO:0000269|PubMed:17036004}. Note=Secreted by photoreceptor cells, through the stalk membrane into the interrhabdomeral space (IRS). Although secreted, lacks a canonical signal sequence and contains a predicted transmembrane domain. The discrepancy may be explained by protein cleavage after the transmembrane region.

null

TRANSMEM 123..143; /note="Helical"; /evidence="ECO:0000255"

PF00008;PF12661;PF02210;

IPR013320;IPR001881;IPR013032;IPR000742;IPR000152;IPR018097;IPR001791;IPR051022;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Mandibulata (clade), Pancrustacea (clade), Hexapoda (subphylum), Insecta (class), Dicondylia (clade), Pterygota (subclass), Neoptera (infraclass), Endopterygota (cohort), Diptera (order), Brachycera (suborder), Muscomorpha (infraorder), Eremoneura (clade), Cyclorrhapha (clade), Schizophora (no rank), Acalyptratae (no rank), Ephydroidea (superfamily), Drosophilidae (family), Drosophilinae (subfamily), Drosophilini (tribe), Drosophila (genus), Sophophora (subgenus), melanogaster group (no rank), melanogaster subgroup (no rank)

eys spam CG33955

false

319

A0A1I9LMX5

MKLLSITLTSIVISMVFYQTPITTEARSLRKTNDQDHFKAGFTDDFVPTSPGNSPGVGHKKGNVNVEGFQDDFKPTEGRKLLKTNVQDHFKTGSTDDFAPTSPGHSPGVGHKKGNVNVESSEDDFKHKEGRKLQQTNGQNHFKTGSTDDFAPTSPGNSPGIGHKKGHANVKGFKDDFAPTEEIRLQKMNGQDHFKTGSTDDFAPTTPGNSPGMGHKKGDDFKPTTPGHSPGVGHAVKNDEPKA

Precursor of CEP9 (PCEP9) [Cleaved into: C-terminally encoded peptide 9.1 (CEP9.1) (CEP9a); C-terminally encoded peptide 9.2 (CEP9.2) (CEP9b); C-terminally encoded peptide 9.3 (CEP9.3) (CEP9c); C-terminally encoded peptide 9.4 (CEP9.4) (CEP9d); C-terminally encoded peptide 9.5 (CEP9.5) (CEP9e)]

Arabidopsis thaliana (Mouse-ear cress)

3,702

243

26,206

Apoplast;Developmental protein;Direct protein sequencing;Hormone;Hydroxylation;Reference proteome;Secreted;Signal

GO:0005179; GO:0006970; GO:0006995; GO:0009733; GO:0035864; GO:0048046; GO:0048364; GO:0060359; GO:1901371; GO:1901698; GO:1902025; GO:2000023; GO:2000280

Evidence at protein level

5

SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.2]: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:25324386}. Note=Accumulates in xylem sap under nitrogen (N)-starved conditions. {ECO:0000269|PubMed:25324386}.; SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.3]: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:25324386}. Note=Accumulates in xylem sap under nitrogen (N)-starved conditions. {ECO:0000269|PubMed:25324386}.; SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.4]: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:25324386}. Note=Accumulates in xylem sap under nitrogen (N)-starved conditions. {ECO:0000269|PubMed:25324386}.; SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.5]: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:25324386}. Note=Accumulates in xylem sap under nitrogen (N)-starved conditions. {ECO:0000269|PubMed:25324386}.; SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.1]: Secreted, extracellular space, apoplast {ECO:0000305|PubMed:25324386}. Note=Accumulates in xylem sap. {ECO:0000305|PubMed:25324386}.

SIGNAL 1..26; /evidence="ECO:0000255"

null

IPR033250;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), rosids (clade), malvids (clade), Brassicales (order), Brassicaceae (family), Camelineae (tribe), Arabidopsis (genus)

CEP9 At3g50610 T20E23.210

false

320

A0A1I9LN01

MTGWYEFPVMIGFVSAAVFLLISVAYLPLLNDLYWSTLKSLTPPAGIVADLLVTNGTIFTSDSSLPFADSMAIRNGRILKVGSFATLKGFIGDGTMEVNLEGKIVVPGLIDSHVHLISGGLQMAQVGLRGVSQKDEFCKMVKDAVQNAKEGSWILGGGWNNDFWGGELPSASWIDEISPRNPVWLIRMDGHMALANSLALKIAGVISLTEDPVGGTIMRMPSGEPTGLLIDAAMELVTPWVKEISVDERREALFRASKYALTRGVTTVIDLGRYFPGTTDELSWKDFQDVYLYADSSKKMMIRTCLFFPITTWSRLLDLKLQKGSVLSEWLYLGGVKAFIDGSLGSNSALFYEEYIDTPNNYGLEVMDPEKLSNFTMAADKSGLQVAIHAIGDKANDMILDMYESVAAANGDRDRRFRIEHAQHLAPGSANRFGQLHIVASVQPDHLLDDADSVAKKLGSERAVKESYLFQSLLNGNALLALGSDWPVADINPLHSIRTAVKRIPPKWDHAWIPSERISFTDALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTNSWDEFSKDVSASVLATYVGGKQLYP

Protein LONG AFTER FAR-RED 3 (EC 3.5.-.-)

Arabidopsis thaliana (Mouse-ear cress)

3,702

583

63,785

Alternative splicing;Cytoplasm;Glycoprotein;Hydrolase;Membrane;Reference proteome;Transmembrane;Transmembrane helix

GO:0009704; GO:0009845; GO:0010218; GO:0016020; GO:0016810; GO:0048471

Evidence at transcript level

5

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14645728}.

null

TRANSMEM 7..27; /note="Helical"; /evidence="ECO:0000255"

PF07969;

IPR013108;IPR011059;IPR032466;IPR033932;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), rosids (clade), malvids (clade), Brassicales (order), Brassicaceae (family), Camelineae (tribe), Arabidopsis (genus)

LAF3 At3g55850 F27K19.30

false

321

A0A1L3THR9

MLAPLFAALLAGAATASPIQERQSSVPVGTIITACTVPNTFALTFDDGPFAYTSELLDLLSSNGVKATFFLNGQNWGSIYDYTSVVTRMDAEGHQIGSHTWSHADLATLDAAGITSQMTQLETALTSILGKVPTYMRPPYFSTNALALSTLGGLGYHVINANIDTLDYEHDDDTIGVAFTNFQNGLASGGTVSLMHDVHAQTVHVLVQEAINAIKAKGLTPVTVGTCLGDASANWYKSGGGSGTTPPPATGGPSPDDTCGGSNGYVCQNSQCCSQWGWCGTTSEYCAAGCQAAYGPCT

Chitin deacetylase (EC 3.5.1.41)

Pestalotiopsis sp

36,460

298

30,941

Carbohydrate metabolism;Cell wall biogenesis/degradation;Chitin degradation;Chitin-binding;Cobalt;Disulfide bond;Hydrolase;Metal-binding;Polysaccharide degradation;Secreted;Signal;Virulence

GO:0000272; GO:0004099; GO:0005576; GO:0006032; GO:0008061; GO:0042783; GO:0046872; GO:0071555

Evidence at protein level

5

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27901067}.

SIGNAL 1..16; /evidence="ECO:0000255"

null

PF00187;PF01522;

IPR001002;IPR018371;IPR036861;IPR011330;IPR002509;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), sordariomyceta (clade), Sordariomycetes (class), Xylariomycetidae (subclass), Amphisphaeriales (order), Sporocadaceae (family), Pestalotiopsis (genus), unclassified Pestalotiopsis (no rank)

CDA

false

322

A0A1L4BJ46

MTFLILTILATVTPSLYSHVVQRELRVNFEPLAGQRDSWPVARAAMVTFDARSEKAREFSECRMINSMHELSRELMDSPEHTVKRASKEEMDDLVQRCSGSAEGRSWFIWPDTKWCGPGTDAKNESDLGPLEADKCCRTHDHCDYIGAGETKYGLTNKSFFTKLNCKCEAAFDQCLKESIDRAEGSAKSSMEGLHSFYFNTYSPECYEVKCSRKRDAECTNGIAIWKDSYKS

Phospholipase A2 hemilipin (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (Phospholipase A(2)) [Cleaved into: Phospholipase A2 large subunit; Phospholipase A2 small subunit]

Hemiscorpius lepturus (Scorpion)

520,031

232

26,339

Calcium;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Secreted;Signal;Zymogen

GO:0004623; GO:0005576; GO:0006644; GO:0016042; GO:0046872; GO:0050482

Evidence at protein level

5

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26335363}.

SIGNAL 1..18; /evidence="ECO:0000255"

null

PF05826;

IPR016090;IPR036444;IPR033113;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Chelicerata (subphylum), Arachnida (class), Scorpiones (order), Iurida (parvorder), Scorpionoidea (superfamily), Hemiscorpiidae (family), Hemiscorpiinae (subfamily), Hemiscorpius (genus)

null

false

323

A0A1L4BKS3

MKRLRPSDKFFELLGYKPHHVQLAIHRSTAKRRVACLGRQSGKSEAASVEAVFELFARPGSQGWIIAPTYDQAEIIFGRVVEKVERLSEVFPTTEVQLQRRRLRLLVHHYDRPVNAPGAKRVATSEFRGKSADRPDNLRGATLDFVILDEAAMIPFSVWSEAIEPTLSVRDGWALIISTPKGLNWFYEFFLMGWRGGLKEGIPNSGINQTHPDFESFHAASWDVWPERREWYMERRLYIPDLEFRQEYGAEFVSHSNSVFSGLDMLILLPYERRGTRLVVEDYRPDHIYCIGADFGKNQDYSVFSVLDLDTGAIACLERMNGATWSDQVARLKALSEDYGHAYVVADTWGVGDAIAEELDAQGINYTPLPVKSSSVKEQLISNLALLMEKGQVAVPNDKTILDELRNFRYYRTASGNQVMRAYGRGHDDIVMSLALAYSQYEGKDGYKFELAEERPSKLKHEESVMSLVEDDFTDLELANRAFSA

Terminase, large subunit (DNA-packaging protein) (DNA-packaging protein gp80) (Gene product 80) (gp80) [Includes: ATPase (EC 3.6.4.-); Endonuclease (EC 3.1.21.-)]

Thermus phage G20c (Thermus thermophilus phage G20c)

1,406,341

485

55,156

3D-structure;ATP-binding;Endonuclease;Hydrolase;Magnesium;Metal-binding;Nuclease;Nucleotide-binding;Viral genome packaging;Viral release from host cell

GO:0004519; GO:0005524; GO:0016887; GO:0019073; GO:0046872; GO:0051276; GO:0098009

Evidence at protein level

5

null

PF17289;PF03237;

IPR027417;IPR035421;IPR044267;

5M1F;5M1K;5M1N;5M1O;5M1P;5M1Q;

Viruses (no rank), Duplodnaviria (realm), Heunggongvirae (kingdom), Uroviricota (phylum), Caudoviricetes (class), Oshimavirus (genus), unclassified Oshimavirus (no rank)

G20c_80

false

324

A0A1L6Z3A0

MSRFTSATHGLNLSIKMPISVSQVPSIRSNTSKYELQKLRSTGRSVLQTRRQLAIINMTKRSEADDNDGVERRKGVFHPNLWDDGFIQSLSTVYHEQASYRERAERLIGEVKAVFDSISMGDGDQFISPSAYDTAWVARVPAIDGSSRPQFPQAIDWILLNQQQDGSWGSQSHLSLTHRLTDTLACVIALASWKIESVQIDEGLDFITRGVEKLQSESVPAEFEIIFAELLNQAKSLQLSLPYEHSCLQSLWRKQEPILANGLMDSVAKRSLSSLEEMQDHRMNTDSDGTMHVESFLSSPAVAARVLMRTGNPICLAYLNNVLNKFGDYVPGMYPVDLFQRLWMVDNVERLGIDRHFKKEIQVTLDYVYSYWNGKGIGCGRDSLSPDLNSTSLGFRTLRLHGYNVSADVLEHFKDRDGKFVCSSNPTVGEIRSVLNLYRASLLAFPGEKVMEEAETFARRYLEEIVQKIPPSKFSREIEYVLEFGWQSTVPRWEARSYIDFHGLDTYSPWTIYEMASEKFLELAKLEFNIFNSLQHTELQYLSRWWNDSGMSQMRFTRHRNVEYYTMASCIAMEPSQSAFRIGFTKLCGIATCIDDIYDTYGTIDELKLFREAVKRWDPSAIESLPEYMKSVYMVLYELVNEMAQDTERTQGRDTLDYARNAWEAIIDAHLVEAEWIASGHIPTFEEYLENSKVTSGLHIAILPILTLDVPLPDQLPLQEIDTLSRFHHLASTIGRLSGDMNAYKIDLAHGEESSCISCYMKDNPGTTEGDAHNYANVTISYLMKELNLELMGQHNRVSFLRTSKKPAFDIYRASNYMYKYRDGYTIADKETKNLVMRTLVQAVSL

Pseudolaratriene synthase, chloroplastic (EC 4.2.3.180) (Terpene synthase 8) (PxaTPS8)

Pseudolarix amabilis (Golden larch) (Pseudolarix kaempferi)

3,355

846

96,588

Chloroplast;Lyase;Magnesium;Metal-binding;Plastid;Transit peptide

GO:0000287; GO:0009507; GO:0010333; GO:0016102

Evidence at protein level

5

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.

null

PF01397;PF03936;

IPR008949;IPR034741;IPR044814;IPR001906;IPR036965;IPR050148;IPR005630;IPR008930;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Acrogymnospermae (clade), Pinopsida (class), Pinidae (subclass), Conifers I (clade), Pinales (order), Pinaceae (family), Pseudolarix (genus)

TPS8

false

325

A0A1L7NQ96

MKIGCHGLVWTGHFDAEGIRYSVQKTREAGFDLVEFPLMDPFSFDVQTAKSALAEHGLAASASLGLSDATDVSSEDPAVVKAGEELLNRAVDVLAELGATDFCGVIYSAMKKYMEPATAAGLANSKAAVGRVADRASDLGINVSLEVVNRYETNVLNTGRQALAYLEELNRPNLGIHLDTYHMNIEESDMFSPILDTAEALRYVHIGESHRGYLGTGSVDFDTFFKALGRIGYDGPVVFESFSSSVVAPDLSRMLGIWRNLWADNEELGAHANAFIRDKLTAIKTIELH

Ketose 3-epimerase (EC 5.1.3.-) (D-allulose 3-epimerase) (D-AE) (L-ribulose 3-epimerase)

Arthrobacter globiformis

1,665

289

31,406

3D-structure;Carbohydrate metabolism;Cobalt;Isomerase;Magnesium;Manganese;Metal-binding

GO:0005975; GO:0016857; GO:0030145

Evidence at protein level

5

null

PF01261;

IPR050312;IPR036237;IPR013022;

5ZFS;8YEB;8YEC;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Actinomycetota (phylum), Actinomycetes (class), Micrococcales (order), Micrococcaceae (family), Arthrobacter (genus)

DAE

false

326

A0A1L8F5J9

MGTMRLFLLAVLFLFSFARAGCDPKIVNIGAVLSTKKHEQIFREAVNQANKRHFTRKIQLNATSVTHRPNAIQMALSVCEDLISSQVYAILVSHPPAPTDHLTPTPISYTAGFYRIPVIGLTTRMSIYSDKSIHLSFLRTVPPYSHQALVWFEMMRLFNWNHVILIVSDDHEGRAAQKKLETLLEEKESKADKVLQFEPGTKNLTALLLEAKELEARVIILSASEDDATAVYKSAAMLDMTGAGYVWLVGEREISGSALRYAPDGIIGLQLINGKNESAHISDAVAVVAQAIHELFEMENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYPDGVTGRIEFNEDGDRKFANYSIMNLQNRKLVQVGIFNGSYIIQNDRKIIWPGGETERPQGYQMSTRLKIVTIHQEPFVYVRPTTSDGTCREEYTINGDPIKKVICNGPNETIPGRPTVPQCCYGFCVDLLIKLAREMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWFSWGVLLNSGIGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLNILKSHENGFMEELDKTWVRYQECDSRSNAPATLTFENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKASFRSITSTLASSFKRRRSSKDTVNVVV

Glutamate receptor ionotropic, NMDA 1 (GluN1) (N-methyl-D-aspartate receptor subunit NR1) (NMD-R1)

Xenopus laevis (African clawed frog)

8,355

903

101,793

3D-structure;Alternative splicing;Calcium;Cell membrane;Disulfide bond;Glycoprotein;Ion channel;Ion transport;Ligand-gated ion channel;Magnesium;Membrane;Metal-binding;Postsynaptic cell membrane;Receptor;Reference proteome;Signal;Synapse;Transmembrane;Transmembrane helix;Transport;Zinc

GO:0004972; GO:0005886; GO:0007268; GO:0010043; GO:0015280; GO:0017146; GO:0022849; GO:0035235; GO:0035725; GO:0038023; GO:0042391; GO:0043005; GO:0045202; GO:0045211; GO:0046872; GO:0048167; GO:0070588; GO:0098839

Evidence at protein level

5

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19524674, ECO:0000269|PubMed:21677647, ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:26912815, ECO:0000269|PubMed:27135925, ECO:0000269|PubMed:27916457, ECO:0000269|PubMed:28232581}; Multi-pass membrane protein {ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:27062927, ECO:0000269|PubMed:28232581}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P35438}. Postsynaptic density membrane {ECO:0000250|UniProtKB:P35439}. Synaptic cell membrane {ECO:0000250|UniProtKB:P35438}. Note=Synaptic cell membrane targeting is dependent of GRIN2B/GluN2B subunit (By similarity). Association with GRIN3A occurs in the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P35438, ECO:0000250|UniProtKB:P35439}.

SIGNAL 1..20; /evidence="ECO:0000255"

TRANSMEM 558..578; /note="Helical"; /evidence="ECO:0000269|PubMed:25008524"; TRANSMEM 629..645; /note="Helical"; /evidence="ECO:0000269|PubMed:25008524"; TRANSMEM 811..831; /note="Helical"; /evidence="ECO:0000269|PubMed:25008524"

PF01094;PF00060;PF10613;

IPR001828;IPR019594;IPR001508;IPR015683;IPR001320;IPR049872;IPR049873;IPR028082;

3QEK;3QEL;3QEM;4TLL;4TLM;5B3J;5EWJ;5EWL;5EWM;5IOU;5IOV;5IPQ;5IPR;5IPS;5IPT;5IPU;5IPV;5TPW;5TPZ;5TQ0;5TQ2;5UN1;5UOW;5UP2;6E7R;6E7S;6E7T;6E7U;6E7V;6E7W;6E7X;7TE6;

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amphibia (class), Batrachia (superorder), Anura (order), Pipoidea (superfamily), Pipidae (family), Xenopodinae (subfamily), Xenopus (genus), Xenopus (subgenus)

grin1

false

327

A0A1L8FDW4

MAMRGLIEAECGGSNPLMKLTNHFTQDKALREEGLQHVSWPPGATVVSKPLGEATEDELVSEFLHTRAPSLQSRAPHTFKMDGLLAEMQEIEQSSFRPEPLRAPGVADLALSEQWSAEFLGVEVDPVEEEDWSREFTEQADPHASPSRWAEEYLQQSEEKLWLGESEGAMAEKWTEEYQPEDDLQREAKSLVSQVTDPKLANTQFLQFVKRIGDGELSFSHAPSTPSQTVSQAEQWSEQFVHEQAEQWVDQFAPLEKDFEKAKAAVESDVDFWDKLQEEWEEMAKRDAEAHPWLSDFQDLSSKSIDKGYMFEDNNPFSEVSLPFEEGLKHLREGDLPSAVRLFEVAVKRDPQHMEAWQYLGTTQAENEQELAAISALRRCIDLKPDNLSALMALAVSYTNECLQQQACHTLREWLRHNPKYSHLVKEESSSNASRARSFGTLLSDSVFSDVRELFLSAVNSDPSQVDPDVQCGLGVLFNLSGEYQKAVDCFTAALGQRPDDYLLWNKLGATLANGNDSEAAVEAYRRALQLQPGFIRSRYNLGIACINLGAHREAIEHFLEALSMQQQSGGCESAMSDNIWSTLRMALSMIGQSDLYSSADARDLATLQAAFPPHSAAQ

Peroxisomal targeting signal 1 receptor (PTS1 receptor) (PTS1R) (PTS1-BP) (Peroxin-5)

Xenopus laevis (African clawed frog)

8,355

619

69,403

Cytoplasm;Isopeptide bond;Peroxisome;Protein transport;Receptor;Reference proteome;Repeat;Thioester bond;TPR repeat;Translocation;Transport;Ubl conjugation

GO:0000425; GO:0005052; GO:0005778; GO:0005782; GO:0005829; GO:0016560; GO:0016561; GO:0016562; GO:0044721; GO:0140597

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:35931083}. Peroxisome matrix {ECO:0000269|PubMed:35931083}. Note=Cycles between the cytosol and the peroxisome matrix (PubMed:35931083). Following binding to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, recruited to the docking complex, composed of pex13 and pex14, leading to translocation into the peroxisome matrix along with cargo proteins (PubMed:35931083). Export and recycling to the cytosol is initiated by binding to the pex2-pex10-pex12 ligase complex via its unstructured N-terminus that inserts into the ligase pore and emerges in the cytosol (PubMed:35931083). Cys-11 of pex5 is then monoubiquitinated, promoting its extraction from peroxisomal membrane by the pex1-pex6 AAA ATPase complex (PubMed:35931083). Extraction is accompanied by unfolding of the TPR repeats and release of bound cargo in the peroxisome matrix (PubMed:35931083). The TPR repeats refold in the cytosol and ubiquitination is removed by deubiquitinating enzymes, resetting pex5 for a subsequent import cycle (PubMed:35931083). {ECO:0000269|PubMed:35931083}.

null

PF13432;PF13181;

IPR024111;IPR011990;IPR019734;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amphibia (class), Batrachia (superorder), Anura (order), Pipoidea (superfamily), Pipidae (family), Xenopodinae (subfamily), Xenopus (genus), Xenopus (subgenus)

pex5.S

false

328

A0A1L8G2K9

MGDMQMSVVDPTWELLDPNPDIRALFLEFNDTFFWGQLSGVEVKWSARMTLCAGVCSYEGRGGLCSIRLSEPLLKLRPRKDLVETLLHEMIHALLFVTHNNKDHDSHGPEFCKHMERINGRTGANISVYHNFHDEVDEYRKHWWLCNGPCQKRKPYFGYVKRAMNRAPSSLDPWWADHQRTCGGSFVKVKEPENYPQKRKRKNDPTISEVNSSSHVKGKSNGVDIRTVIPFSGTGYKLFEPNKSDAPLKILNINPTKDKAAVPLLNHTPPSTNINGTFLTNKIGSAKSTPAQSILTKVSVANTKVFINLNGSPIKLPSGSKNKSHQISSKQKSVLPFFKMQKDNSFDLTLPSPSIQSTSQKPQKDISFGFTLPSQSFPSTSPGSNSENKEPLYKKLQMNDRESFIIHSGNKTNVNDNKSCTGPAATTASGLNHTIKVSCPVCGTEVLECKINDHLDTCTSSGPQKDILLDVSLPLQSFPSTSQGSNSAIKEPLYKKLQINDKDSFIIHSGNKTNVNDNKSCTRPAATTASGFNHTIKVCCPVCGTDVLQDKINDHLDTCLQNCNT

DNA-dependent metalloprotease SPRTN (EC 3.4.24.-) (Protein with SprT-like domain at the N terminus) (Spartan)

Xenopus laevis (African clawed frog)

8,355

565

62,607

Autocatalytic cleavage;Chromosome;DNA damage;DNA repair;Hydrolase;Isopeptide bond;Metal-binding;Metalloprotease;Nucleus;Protease;Reference proteome;Repeat;Zinc;Zinc-finger

GO:0000785; GO:0003690; GO:0003697; GO:0004222; GO:0005634; GO:0006508; GO:0006974; GO:0008270; GO:0016540; GO:0031593; GO:0106300

Evidence at protein level

5

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H040}. Chromosome {ECO:0000269|PubMed:30595436}. Note=Localizes to sites of UV damage via the PIP-box (By similarity). Recruited to stalled replication forks at sites of replication stress (By similarity). {ECO:0000250|UniProtKB:Q9H040}.

null

PF10263;PF22934;

IPR006642;IPR044245;IPR006640;IPR055220;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amphibia (class), Batrachia (superorder), Anura (order), Pipoidea (superfamily), Pipidae (family), Xenopodinae (subfamily), Xenopus (genus), Xenopus (subgenus)

sprtn XELAEV_18029135mg

false

329

A0A1L8GSA2

MMETQPTSLPHVLPQDVYEFCDDRKSLGRLRVSEMPAESNGDGGGSKGDGAAVVAKEVPEQSNKKRKRCGVCVPCLRKEPCGACYNCVNRSTSHQICKMRKCEQLKKKRVVPLKGVEAVNKDDSKNQAKEQVPNVKNCSESILVDGPKTDQMEAGPVNHVQEGRLKKECDSTLPSKACEDLANQLLMEANSWLSNTAAPQDPCNKLNWDKPTIPNHTAATNNSNLEDAKNLVAFSAVAEAMSNYGMPASGTPSSVSMQLYEKFNYETNRDSSGHPEGNAPSCPEDLNTLKTALALAKHGVKPPNCNCDGPECPDYLEWLENKIKSSQKDSQESSFPGLGQVSKELVQKSYPKEEVLNLENKNLCPSGNLPFSQNALSLAKEKNISLQTAIAIEALTQLSSALPQTNNECPNSSSQPLINTCDQLTHFPTAKGNQLPIFPMACNELFQNQQSQLYTGKNALPVPQSPRQTSWEQNKKPSYQEGQYIPENLSQSSSVLPSDASTPQKTEFLQQWIQNADLLKSPSDPMTGLKQLLGNTDEYIKSVFKGPEALPNKIKHVKTKRTIKSIKKKSSDFLKMSPDQQLSQLLQENDFHHNAQAALQQHLHHKRNLFVDPNTMEACAQEQQNWWVPKSQKLPVSKTTENPVKERKKRRQRSPSQKQVEPKPKPPRKQVQIKKPRMKEGNAVFMPVSQISLDAFRGAEKEENQLKEMNLEKSLSNNIQPDLLESQSILVTGSQANIENRKTVNTQETCNENQASNGKASNFALCVNQANSLGAKDSCPTPSTDDASSSSGQGDSANQHTNVGDVPGQNDLSCLDDKFEDLLRQFEAEFGEDFSLPGSEAPSQNGVGPPKQQISGDPQFKMPFPSQLLPSENSTRPDAHSNPALSNNPISHNVSHNLDSLFSSKSPKKIKIESSGAITVVSTTCFYSEENQHLDGTPTKSDLPFNPTLSGFLESPLKYLTSPTKSLIDTPAKMAQAEFPTCDCVEQINEKDEGPYYTHLGSGPTVASIRELMEDRFGEKGEAIRIEKVIYTGKEGKSSRGCPIAKWVIRRQSEDEKLMCLVRQRAGHHCENAVIIILIMAWEGIPRALGDSLYSDITETITKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWSMYFNGCKYARSKTPRKFRLIGDNPKEEEFLNDNFQDLATKVAPVYQMLAPQSYENQVNNEEVAIDCRLGLKEGRPFSGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRTIGRIPEDEQLHVLPLYKVSSTDEFGSEDGQAEKIRKGGIQVLASFPREVRKLSEPAKSCRQRQLDAKKAAAEKKKLQKEKLVSPDKTKQEPADTKMCQQNPGVPQQQTKPCVKVEPSNHYNTYKYNGNGVVESYSVLGSCRPSDPYSMNSVYSYHSFYAQPNLPSVNGFHSKFALPPFGFYGFPNNPVVPNQFMNYGTSDARNSGWMNNSFEKKPDVQSLADGMNQSYGSELPEQSYRRSSEVPHHYSLQNPNSQKSFNISHRTTPSPMETTPYSNLPCYNKVIKKEPVCDPLVDPFQRANSVHSQSPGVNHSLQTSDLPFKANGALPSSGRSNAEGPCSMSLPNDKSGLEKRDYFGVHSNVPALKDKQWTPYGTDVPVGQRDSLDAQSPGKVWSSCKLSDSPAVLPSFASTQTKNWNGRQASLNQGLKEPMPFQEKLWNSVAASDRCSVTPSDRSSVTPCAELQDKNWASFPNPVGNSLKTESSQNHWDPYSLDDNMDDGQSKSVKEEEDEEEIWSDSEHNFLDKNIGGVAVAPGHGSILIECARRELHATTPLKKPNRCHPARISLVFYQHKNLNQPNHGLALWEAKMKLLAERARVKEEEAARLGIKQEVKSLGKKRKWGGAATTETPPVEKKDFIPTRQATTILTDSATTAFSYAYTKVTGPYSRFI

Methylcytosine dioxygenase tet3-A (EC 1.14.11.80)

Xenopus laevis (African clawed frog)

8,355

1,925

213,144

Chromatin regulator;Chromosome;Coiled coil;Developmental protein;Dioxygenase;DNA-binding;Iron;Metal-binding;Nucleus;Oxidoreductase;Reference proteome;Zinc;Zinc-finger

GO:0000978; GO:0001654; GO:0005634; GO:0005694; GO:0007399; GO:0008270; GO:0008327; GO:0044029; GO:0045944; GO:0070579; GO:0141167

Evidence at protein level

5

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A0JP82}. Chromosome {ECO:0000250|UniProtKB:A0JP82}. Note=Detected on chromatin, where it binds to target gene promoters. {ECO:0000250|UniProtKB:A0JP82}.

null

PF12851;PF02008;

IPR024779;IPR040175;IPR046942;IPR002857;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amphibia (class), Batrachia (superorder), Anura (order), Pipoidea (superfamily), Pipidae (family), Xenopodinae (subfamily), Xenopus (genus), Xenopus (subgenus)

tet3-a XELAEV_18020377mg

false

330

A0A1L8GVF0

MSKIEKMSIQGVRSFGINDKNKQVIQFFTPLTILVGPNGAGKTTIIECLKYMTTGDFPSGSKGNTFVYHPKLAHETDVRAQICLQLKDVNGEPVAVQRSIICRQKGKSTECKTVDCVITRIKHGGPVSLRPKCEEMNKEMISALGVSSAVLNNVIFCHQEDSNWPLSEGKRLKGKFDEIFSITRYSKALETLRDVRMKEDQNVSNYQEEIKYLKENKEKAREIQDNLQSKEKQLTVSKENVKSIESQLEPLKDRLADIQRNLFKVIRLENEIKALESRKRTMEQDNQDLMEKMEKVFQGTDEELNEMYQNQCFVREKERKLNDHQREMDRACKESQRLNREKGELLVQQGHLQLEADNHQRYIKTRDSLIKSLAVQLELDGFELTPFNQRQTSNFQMLVKERQEEVEAHANQILREFSEREAMQQRQIDEIRDKKTGLERTIELKSSTESKKHTDLKKVKYDLQQLEGTSDRLHELDEELQKTAHALENVEKSCNLEALKGEVVQLQTQKSELDRNVRELDQEMEQLNKHTMTRTQMDMLKNDKADKDEQIRKMKSRHNDELISLYEYFPNKKQLEDWLYSKREDINQTRDKLARLTKELVAAEQNSNHLSNELCQKEKQSASFEEKVFDVCGSQDFNSDLSQLLEDIEKTSKQRAMLAGATAVYTQFITTLTEENQPCCPVCQRTFPSEAEVQDVINDMQSKLCLVPDKLKAAEDELKRKEKRKDEMMELKPMRQMLSDLKEKEIPEIRNKLEAINREIKRLQNDVEEQESLIVTFVSEEARAEACLQDISLMEQYQMELRDVDQKIAHYATKLLGVDLNRTVQQVNQEKLEKHHSLDNVSRRIELLQNHLQNQQEQVQQLKSRVNELTAEKLHISSNLQQRQQLEEQNVELTTELHCLSIEIKESREQVFPLESTLQKLQQEKQALLQRKESSYREAQEKVNDIKEKVKKINLHTKDIEKYIQDGKEEFKEQKESELQELTVRLNECEELKEKINREMVTIRQDIDTQKIQERCLQDNLTLRKRIEELKQVEEERDQLLKEMGQMKVTQMEKEYQELENKRETLKTNHSLTLGRQKGFEDEILRFKNELNEPKYKDAEEEYREKMIVMRTTELAIKDLDIYFKTMDQAIMKFHSIKMEEINKIIRDLWCSTYRGQDIEYIEIQSEPDEGISAADNRRTYNYRVVMIKGDTELDMRGHCSAGQKVLASLIIRLALAEIFCSNCGVLALDEPTTNLDHENIDSLAHALVEIIKSRSRQRNFQLIVITHNEDFVELLGRSEYVEHFYRIKKNIDQCSEIIRCSVSSLASYLH

DNA repair protein RAD50.S (EC 3.6.-.-)

Xenopus laevis (African clawed frog)

8,355

1,311

153,773

ATP-binding;Chromosome;Coiled coil;DNA damage;DNA repair;Hydrolase;Magnesium;Meiosis;Metal-binding;Nucleotide-binding;Nucleus;Reference proteome;Telomere;Zinc

GO:0000722; GO:0000729; GO:0000781; GO:0000794; GO:0003691; GO:0005524; GO:0006302; GO:0007004; GO:0016887; GO:0030870; GO:0035861; GO:0043047; GO:0043539; GO:0046872; GO:0051310; GO:0051880; GO:0062176; GO:0070192; GO:0110025

Evidence at protein level

5

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92878}. Chromosome, telomere {ECO:0000250|UniProtKB:Q92878}. Chromosome {ECO:0000250|UniProtKB:Q92878}. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents. Localizes to DNA double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q92878}.

null

PF13476;PF04423;PF13558;

IPR027417;IPR038729;IPR004584;IPR013134;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amphibia (class), Batrachia (superorder), Anura (order), Pipoidea (superfamily), Pipidae (family), Xenopodinae (subfamily), Xenopus (genus), Xenopus (subgenus)

rad50.S

false

331

A0A1L8GXM0

MSKIEKMSIQGVRSFGIEDKNKQVIQFFTPLTVLVGPNGAGKTTIIECLKYITTGDFPPGSKGKTFVHDPKVAHETDVRAQIRLQLKDVNGELVAVQRSMICTQKGKSTEFKTLEGVITRIKHGEKVSLSTKCAEMDKEMISALGVSAAVLNNVIFCHQEDSNWPLSEGRQLKVKFDEIFSATRYIKALETLKKVRTQQAHNVREYQVEIKYLKQNKEKAREIQDNLQSKEKQLAVSKENVKSIESQLEPLKDRLADIQRNLSKVMRLDNEIKALESRKRTMEQDNQDLEEKMEKVFQGTDEELNGMYQNHQRSVREKERKLNDQQREMDRACKESQRLNREKGELLVQQGRLQLEADHHQQYIKTRDSLIKSLAAQLELDGFERTPFNQRQTSNFQMLVKERQEKDEAHANQILREFSEREAMKQRQLDEMRDKKTGLERTIELKSSTQSKKHTDLKNVKYELQQLEGSSDRLQELDEELQKTERELENVEKSCNLEALRGEVLQLQNQKSELDRNVRKLDQEMEQMNTHTMTRTQMDMLKKDKADKDEQIRKIKSRHNDELSLLLGYFPNKKQLEDWLYSKRKDINQTRDKLARLTKELVAAEQNKNHLSNELRRKEEQSASFEEKVFDVCGSQDFDSDLSRLQDDIEKTSKQRAMLAGATAVYTQFITTLTEENQPCCPVCQRIFPSEAELQDVINDMQSKLRLVPDKLKSAEGELKRKEKRKDDMMELKPMRQMLADLKEKEIPEIRNKLVTINREIQRLKNDVDEQETLIATFASEEESAKACLQDISLMERYQMELRDVERKIAQYATKLQGVDLNRTVQQVSQEKQEKQHNLDNVSGKIELLRKRIQDQQEQVQQLKSAVNELTAEKLHISSNLQRRQQLEDQNVELTTELQCLAREIKEAREQLFPLESTLQKLQQEKQELLQRKESSYREAQEKVNDIKEKVKKINLLTKDIEKYSQDGKEEFKEQKESELQELIGRLNECEKLKEKVNREMVTIRQDIDTQKIQERCLQDNLTLRKRIEELKRVEEERHQLLKEMGQMKVVQMKNEYQELENKSESLKTNHSLALGRQKGFEDEILRFKKELRESQYKEAEEKYREKMIVMRTTELAIKDLDIYYKTLDQAIMKYHSIKMEEINKIVRDLWRSTYRSQDIEYIEIQSDADESVTAADKRRTYNYRVVMIKGDTALDMRGRCSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIIKSRSRQRNFQLIVITHDEDFVELLGRSEYVEHFYRIKKNIDQCSEIIRCSVNSLASYVH

DNA repair protein RAD50.L (EC 3.6.-.-)

Xenopus laevis (African clawed frog)

8,355

1,312

153,910

ATP-binding;Chromosome;Coiled coil;DNA damage;DNA repair;Hydrolase;Magnesium;Meiosis;Metal-binding;Nucleotide-binding;Nucleus;Reference proteome;Telomere;Zinc

GO:0000722; GO:0000729; GO:0000781; GO:0000794; GO:0003691; GO:0005524; GO:0006302; GO:0007004; GO:0016887; GO:0030870; GO:0035861; GO:0043047; GO:0043539; GO:0046872; GO:0051310; GO:0051880; GO:0062176; GO:0070192; GO:0110025

Evidence at protein level

5

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92878}. Chromosome, telomere {ECO:0000250|UniProtKB:Q92878}. Chromosome {ECO:0000250|UniProtKB:Q92878}. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents. Localizes to DNA double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q92878}.

null

PF13476;PF04423;PF13558;

IPR027417;IPR038729;IPR004584;IPR013134;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amphibia (class), Batrachia (superorder), Anura (order), Pipoidea (superfamily), Pipidae (family), Xenopodinae (subfamily), Xenopus (genus), Xenopus (subgenus)

rad50.L

false

332

A0A1L8HU22

MEALPPQVLKPLDCMSIYSRHREPENRHNELSTGRCGRGHVIFSSMKALQPQVLKPTGSHANLQQVLYAPAATIITAPASSHNDLSSLTGCSYAGVETLGKELFIYFGLKAMRVHFGMNGSMRINQPMKKGQENGRPIPIAVLEVQLTKDLICFYESTVDVRNASECQEKIRFFEELDVCSSKFSFPRAECEIKKQRTRMLCDILLDQMILPGVGNIIKNEALFDSGLHPGVQAGLLTDEQVSHLVKMTRDFTLLFYKCRKSGSALYKHYKVYKRPNCGQCGTKITVCRLGEHNRMTYFCPKCQKDKPQHVDVSKLPTRNSLIGWVQRTASNANEHVATSKEEHWACAVCTLINKPSDKQCDACLTLRPEVSSLAVSDEAAELNTDLVKYPCNNFAKVLPELKLNRRTAFGNTTLVLTDFGAKEGLADKNSQQNILNRSTFDVPLNNKYYHTKTPSNKRSNENEHWTNTLNAVNGHSAASNNVFNHPQKKLKTGHTTSNTIHLSSTISSPQSKMTGDAAAKTGNPQCSAHNVPCALQVVRKEGENKGRSFYTCSLPRERRCQYFEWADLHFPFCNHGKRCIVRTVLKIGPNNGKNFYVCPMGKDKQCNFFEWAKTE

Endonuclease 8-like 3 (EC 3.2.2.-) (EC 4.2.99.18) (DNA glycosylase/AP lyase Neil3) (Endonuclease VIII-like 3) (Nei-like protein 3)

Xenopus laevis (African clawed frog)

8,355

616

69,092

Chromosome;DNA damage;DNA repair;DNA-binding;Glycosidase;Hydrolase;Lyase;Metal-binding;Multifunctional enzyme;Nucleus;Reference proteome;Repeat;Zinc;Zinc-finger

GO:0003684; GO:0003906; GO:0005634; GO:0005654; GO:0005694; GO:0006284; GO:0008270; GO:0019104; GO:0036297; GO:0140078; GO:1904931

Evidence at protein level

5

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TAT5}. Chromosome {ECO:0000269|PubMed:30842657}. Note=Recruited to replication stress sites via interaction with ubiquitinated CMG helicase. {ECO:0000269|PubMed:30842657}.

null

PF06831;PF06839;

IPR015886;IPR015887;IPR035937;IPR010979;IPR000214;IPR010666;IPR001876;IPR036443;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amphibia (class), Batrachia (superorder), Anura (order), Pipoidea (superfamily), Pipidae (family), Xenopodinae (subfamily), Xenopus (genus), Xenopus (subgenus)

neil3 XELAEV_18005394mg

false

333

A0A1L8HV70

MATPPKRICIDVPASPSGNKCKVKRISIEGNIAAGKSTFVNILKKANEEWDVVPEPIARWCNIQSCKDEFEELTTSQKSGGNLLQMMYEKPERWSFTFQSYACLSRIRAQLKALGGKLKEAENPVLFFERSVYSDRYIFASNLYEAECMNETEWTVYQDWHDWMNSQFGADLELDGIIYLRAIPEKCLNRVYTRGREEEQGIPMEYLEKLHYKHETWLHHRTLRTDFEYLQEIPILTLDVNEDFRDNKQKQESLIEKVKEFLSTL

Deoxycytidine kinase 1 (XldCK) (EC 2.7.1.74) (Deoxyadenosine kinase 1) (EC 2.7.1.76) (Deoxyguanosine kinase 1) (EC 2.7.1.113)

Xenopus laevis (African clawed frog)

8,355

265

31,112

ATP-binding;Kinase;Nucleotide-binding;Nucleus;Reference proteome;Transferase

GO:0004136; GO:0004137; GO:0004138; GO:0005524; GO:0005634; GO:0005737; GO:0005739; GO:0009157

Evidence at protein level

5

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27707}.

null

PF01712;

IPR002624;IPR050566;IPR031314;IPR027417;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amphibia (class), Batrachia (superorder), Anura (order), Pipoidea (superfamily), Pipidae (family), Xenopodinae (subfamily), Xenopus (genus), Xenopus (subgenus)

dck.1.L dck XELAEV_18005792mg

false

334

A0A1M4XLJ3

MTITLDGASLTLADIDAVARGGAKVAITGDADVLARVHGSRDVIARAVERGEEIYGVTTLFGGMADVHVTRDQLIDVQKIALWQHKSTTGPRLPDADVRAAMLLRANSLMRGASGVRIALIERLVAFLNAGASPQVYQRGSIGASGDLVPLTYIGASILGLSPEFLVDLDGETLDCHTVLAKLGFTPMDPDPKEGLALNNGTGACTGVAANVMARALDAATMALGVHALFAQALLATDQSFDPYIHAQKPHPGQVWSAARMAELLTGGRTIRSEAGGDRARRKGDLIQDRYGIRCLPQFFGPIVDGLSTAARQIETEANTANDNPLINPATGETFHTGNFLAQYTAIAMDSTRYLIGLMCKHIDSQIALMITPAFSNGLTPALVGNMDTGVNVGLKSLHIGMNQMSTQISYLGQSVADRFPTHAEMYNQNINSQAMNAANLARDQMDVTEHFLAAALLTGVQAVEVRSRVETGSCDARDILSPATVPLYEAARVAAAGRPDKARTIVWDDMDGFLQPKVEGLLADIGSRGNVHAALQALRSSLDTFRA

Aromatic ammonia-lyase (AAL) (EC 4.3.1.-) (LaAAL)

Loktanella atrilutea

366,533

548

58,150

Lyase;Phenylalanine catabolism;Phenylpropanoid metabolism;Reference proteome

GO:0006559; GO:0009698; GO:0016841

Evidence at protein level

5

null

PF00221;

IPR001106;IPR024083;IPR008948;

null

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Alphaproteobacteria (class), Rhodobacterales (order), Roseobacteraceae (family), Loktanella (genus)

pal SAMN05444339_102525

false

335

A0A1P8AQ95

MTKNMTKKKMGLMSPNIAAFVLPMLLVLFTISSQVEVVESTGRKLSWAFNGAPIVFTPPSSSCGGSPAAVMASEWMPRRPCRRTRPPGTNIPVSQSP

Secreted transmembrane peptide 4 (Phytocytokine STMP4) (Precursor of secreted transmembrane peptide 4)

Arabidopsis thaliana (Mouse-ear cress)

3,702

97

10,464

Apoplast;Cell membrane;Cleavage on pair of basic residues;Membrane;Reference proteome;Secreted;Signal

GO:0005886; GO:0009414; GO:0009651; GO:0009723; GO:0009751; GO:0009753; GO:0030275; GO:0033612; GO:0048046

Evidence at transcript level

5

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31001913}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:31001913}. Note=The precursor of STMP4 accumulates at the plasma membrane and is proteolytically cleaved to release the STMP4 in the apoplasm. {ECO:0000269|PubMed:31001913}.

SIGNAL 1..33; /evidence="ECO:0000255"

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), rosids (clade), malvids (clade), Brassicales (order), Brassicaceae (family), Camelineae (tribe), Arabidopsis (genus)

STMP4 At1g65486 F5I14

false

336

A0A1P8ASY1

MPPRKKPKSSALKSNKQSSANHSSQPSTFGIQQLFLRHIQNSQSTSNSHTSTADPVDQQNVNGLASDTAVLTPQNPLGTSNEKPDESKDMDQQLTEASPKISKNLKRFSPGMLIKQSQDDCGGEITWKISPVNERLRAAAKNIPKMMDLTENSLGVKSSTIRPCSLNKLVQKQCPTSGITSKVEQWLSSPSKKASKRPAFATNRVMERVNPSPDAEFEIVNTSSSGNSPFQTPPSLSCPHNKLPCTVTCSGACGSMGAGQHKKALLELLDQVEDVIAVDDKTTDDVGIVMPQARVKDDIISSVVDCAVDEGPVSLPKMQNSINPDSYFLVLEVSEKRGSGSSSKGQCPYKVLRLLDEHTGVECALYLWDEWFYSTVSPGDSINVIGEFDGDGKCDVDRQNNFLIVHPDTLVAGTRVAASFGCPRRTVLDERLRSNEHATVALLGTLQHQVFQAGLSQESPSVDGLQEYASTVIEKSIESLYACGVHEGDVRSTLFKAIPKMLNWIEHFRYSKDSEVSKVDFGSTIGKKAVKVSEVIDIEEMSWAPKYGLKGMIDASVRVIVESDMNTVNEKIMPLEFKSGKAPSGQSSIEHSAQVILYTLLMSERYLKHIDNGLLYYLQSDQTQGISVQRSDLVGLIIRRNELANDILVASTTQQLPPMLRNPNICRNCRHLDVCTIYHKADGGNTESSGLGDVFDTHVSHLSTLHFNFLRHWDRLIDLEGREMQLLRKDIAHPHGSKGSHSASYLSSMVLDVTNGFQHHNSHKETRFIYRFVRQKSSESRERVTSEDMIRTGNLATDDLDCKLRTGDRVILRTEVSHLTVANGIIADISRTHISVSLSKRLRLPWSEPSSEVSNLSHELWRIYKDEFMTSFSVMRFNLMQLFVQNGHNIRKMIVDLEPPRFDNGSILSQDPAISYIWSEKSLNNDQRQAILKILTAKDYALILGMPGTGKTSTMVHAVKALLIRGSSILLASYTNSAVDNLLIKLKAQGIEFLRIGRDEAVHEEVRESCFSAMNMCSVEDIKKKLDQVKVVASTCLGINSPLLVNRRFDVCIIDEAGQIALPVSIGPLLFASTFVLVGDHYQLPPLVQSTEARENGMGISLFRRLSEAHPQAISVLQNQYRMCRGIMELSNALIYGDRLCCGSAEVADATLVLSTSSSTSPWLKKVLEPTRTVVFVNTDMLRAFEARDQNAINNPVEASIIAEIVEELVNNGVDSKDIGIITPYNSQASLIQHAIPTTPVEIHTIDKYQGRDKDCILVSFVRSREKPRSSASSLLGDWHRINVALTRAKKKLIMVGSQRTLSRVPLLMLLLNKVKEQSGILNLLPGDLKP

DNA replication ATP-dependent helicase/nuclease JHS1 (Protein EMBRYO DEFECTIVE 2411) (Protein JING HE SHENG 1) [Includes: DNA replication nuclease JHS1 (EC 3.1.-.-); DNA replication ATP-dependent helicase JHS1 (EC 3.6.4.12)]

Arabidopsis thaliana (Mouse-ear cress)

3,702

1,331

147,286

4Fe-4S;Alternative splicing;ATP-binding;Chromosome;DNA damage;DNA repair;DNA replication;DNA-binding;Helicase;Hydrolase;Iron;Iron-sulfur;Metal-binding;Multifunctional enzyme;Nuclease;Nucleotide-binding;Nucleus;Reference proteome

GO:0003677; GO:0004518; GO:0005524; GO:0005634; GO:0005694; GO:0006260; GO:0006281; GO:0006974; GO:0010073; GO:0016887; GO:0017116; GO:0046872; GO:0051539

Evidence at transcript level

5

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26951435}. Chromosome {ECO:0000250|UniProtKB:P51530}. Note=Localized to nuclear foci in response to DNA damage. {ECO:0000269|PubMed:26951435}.

null

PF13086;PF13087;PF08696;

IPR026851;IPR045055;IPR041679;IPR041677;IPR014808;IPR027417;IPR011604;IPR047187;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), rosids (clade), malvids (clade), Brassicales (order), Brassicaceae (family), Camelineae (tribe), Arabidopsis (genus)

JHS1 EMB2411 At1g08840 F7G19.26

false

337

A0A1P8AUY4

MAIDGSFNLKLALETFSVRCPKVAAFPCFTSILSKGGEVVDNEEVIHALGDAFLHPEFTVPLVHCFLPIIRNVVDRVVGLLRLVDDLKSSIDYSDDVSSVLDNAMTEGISVIDFYVRRGQRLELHECACLAFSRALHFNTSLLGSILNYFEKAPPPYERILVKDIVSESRMEATDAYLLCLRVSYRFLVIRPEVFSKLWDWSCYLDSMKRLSECPRQQRHFLEKYRDAVWCGIQILSVVLRCSDRLAGCFGFEEEEALSCLLRWEEFCQDIEIEKAGLYIQLPTYTALKSLQQFNTLVPGINKRQSAGLEADEPQMKIRRLDTWDVNSFSEPFEIHSRVKKSFEMVSLAVSQKRPVLLYGPSGSGKSALIRKLADESGNHVVFIHMDDQLDGKTLVGTYVCTDQPGEFRWQPGSLTQAIMNGFWVVLEDIDKAPSDVPLVLSSLLGGSCSFLTSQGEEIRIAETFQLFSTISTPECSVSHIRDAGNSLSPLWRRIVVYPPDRESLQSILGARYPNLGPVAEKLIETFETINSALRPQFSSSTTENSATFSSPSRFSLRDLLKWCERVHGLPSYDGHAVYQEAADIFSASNMSVKNRVAVSEIVASIWNVAVPESQDKPPIQEFSGILKIGRVSLPLGETASHDRSRFVETRTSTRLLEKIARSVEYNEPVLLVGETGTGKTTLVQNLAHWIGQKLTVLNLSQQSDIVDLLGGFKPIDPKLMCTMVYNEFNELARDLKIKDDSKIMKWLQDNFRAKKWHTFLTGLLDIIKGIEGRITERMEGKIGEARSRSGRKRKKPEEELKNCACLRTKVNKIRQQIHSGGMVFTFVEGAFVTALREGHWVLLDEVNLAPPEILGRLIGVLEGVRGSLCLAERGDVMGIPRHLNFRLFACMNPATDAGKRDLPFSFRSRFTEYAVDDDICDDDLEIFVRRFLGGRGSDSKLVANIVWFYKEAKRLSEESLQDGANQKPQYSLRSLYRALEYAIKAEAIGGFQKALYDGFSMFFLSLLDASSAKIVEPIIKRISGENIRSQPLQRYLGELKGSSDKFVGSYVKTKSVIDHLNHLAHAIFIKRYPVLLQGPTSSGKTSLVKYLAAISGNKFVRINNHEQTDIQEYLGSYMTDSSGKLVFHEGALVKAVRGGHWIVLDELNLAPSDVLEALNRLLDDNRELFVPELSETISAHPNFMLFATQNPPTLYGGRKILSRAFRNRFVEIHVDEIPEDELSEILTTKCSIANSHASKMVEVMKDLQRNRQSSKAFAGKHGYITPRDLFRWAYRFRTYDGTSHEELAREGYYILAERLRDDTEKVVVQEVLERHFRVSLAKDDLYNMELPRLDSIQNRKFTWTQSMRRLFFLIDRSYKLREPVLLVGDTGGGKTTICQILSDVKKKRLHILNCHQYTETSDFLGGFFPVRDRSKLITEYENQVKQLELSQALTPFGQDIVICGDISRAEVSIKSVEVALEKYKNGSVIGVAATPQDVDFLEKIRNNMVMLYQKWRAIFVWQDGPLVEAMRAGNIVLVDEISLADDSVLERMNSVLETDRKLSLAEKGGPVLEEVVAHEDFFVLATMNPGGDYGKKELSPALRNRFTEIWVPPITDTEELRSIAFSGLSSLKESNVVDPIINFWEWFNRLHTGRTLTVRDLLSWVAFVNMATESLGPAYAILHGAFLVLLDGLSLGTGFSGRDGQDLREKCFAFLLQQLELFASDTLPLELSRMELYGWGDSKAICEKSKSVRHEGMFGIDPFFISKGDENPEIGGFEFLAPTTHRNVLRVLRAMQLSKPILLEGSPGVGKTSLILALGKYSGHKVVRINLSEQTDMMDLLGSDLPVESDEDMKFAWSDGILLQALKEGSWVLLDELNLAPQSVLEGLNAILDHRAQVFIPELGCTFECPPTFRVFACQNPSTQGGGRKGLPKSFLNRFTKVYVDELVEDDYLFICRSLYPSVPSPLLSKLIALNRQLHDGTMLYRKFGHDGSPWEFNLRDVIRSCQFMQEAIHDLEVESFLNVLYIQRMRTATDRKEVLRIYKAIFDKTPSINPYPRVQLNPAYLVVGTAAIKRNLNQSNIASEQLKLLPEIRQNLEAVAHCVQNKWLCILVGPSSSGKTSVIRILAQLTGYPLNELNLSSATDSSDLLGCFEQYNAFRNFRLVMTRVEHLVDEYNSLLLQSSQEALFSNRSGLVSRWLSYLNKIDSSLVENPLFFLNDSETLSTLEEVVEDLEQVLKEGVLPVSWSKKYLEQISKTILQLQTHEKKQSTKFEWVTGMLIKAIEKGEWVVLKNANLCNPTVLDRINSLVEPCGSITINECGIVNGEPVTVVPHPNFRLFLSVNPKFGEVSRAMRNRGVEVFMMGPHWQLNEDGSNCEELVLRGVERFLALSGIPGYKLVTSMAKAHVHAWLNGQSFGVRITYLELEQWVHLFQLLLMNGNQLLWSLQLSWEHIYLSSLGVTDGKEVVDFVRETYLSDVELSELDSFMGGDLYLPGGWPKPFNLRDLTWYSRETTVRQNCMYLEFLGAQYASHQPKISDNVKSRDRELAAGEPRIIYSIDSWTLKKVLFPKALIGSSCAPDAANFENDLASKMLLFAANWTIEQATEEDIQLYLAWFSWFGSRLQQHCPFLLCFLNTLKVEFEHPIWNHISRCRKNLKFLCRLDPDAVPIPMLSSKLIDVAASNDQSKPYSKSLFESLNSVGVLRRSYQQWLVESNDNHTDVSTFTRFLDSLRVLEKKILCEIVGAPSFSVLIQLYTEVIDNHSFFWSGLVSSSDEYLLFSFWSLIKSIKKMHSFFPGEVQVVLEESKNINNIVLHGHPEKSMLWAYGGHPSLPVSAELFHKQQEFLQLCSTVWPLKSESDEHGNDHLTKAIPFSGPELCLLALEGLCISSYIADEDDVDYVAAVQLDEIYQTFLERLKLEKKRLEDKMGFSEIDNTENITASCCVFCPEIVTTGSGFSSWVKTCFIASSESCSLDVELLAALQHLLVARPTEHQDLVDIRKLLKPALEYSLSSTRPPQTLVAHQKLLWAIDAHASELGVDTKIAGFALEIWYWWHSVLWKNSQIGLMNISDTGNCQILSPSMLIQPVKTATVAQILENVFSVKDYSVQSMKLLSASRYLWKSSQPYQEMPGSLLSIARSLFQQIIYTHQKSFESETFVAIKSVFHAIEKKQNKMDGIQNLISLIGSSSHNKLKSVTHSFVGPLAKRLYSDSSSNALCPTFVEFYCNLGLAWLYLGGLRFHLLNSLDVIDPAMKITCKLLKLEEKISSLELNIKVRGECGYLSGLLYSGNNDESSEHTLSKLKTEHKRLQRKVIFRSDPKKYQDLRRALDEFAGFLTRPISLVNDIEVLDWNQVVEQVFNWQETAISFIDRMSSDYSEYVDITQPIQVSVYEMKLGLSLFVSGALLGKLLNRFDIDMVDSVMETIYALMRFPRDSSIASTTYTECLPPLHLSHGANSRAKSLGLDVGLLHKLISVSSAEDSRKASELQLKVALYKNLHARVLQFVANTGLLDEASFELLDKIYVELARIWMEMKFQAKTKADNLPGLYKFRSRDFKIDSVMEVDISALGKYFPNESFSEWQEYLADDDTKNVKDMTHIDQDEENLEDDWDLIQEHLDSIYSTHNELFGFCDLSEKSGRFCITDSRRLDSFTDSYELGVSMIKGLRGLFTSSLDAKLVPEHLLRLCLENKKNFTSNYQSASKYNFYKDLDGPELGKMVKFLTPLQQRINSLLQEREDHPGLQKLSGVLQMLLAIPSSTPLAKALSGLQFLLCKVHKLQEEGCKLPISDLLEPIISLASSWQKVEFERWPTLLDEVQDQYELNARKLWLPLFSVLFQKDAVEISEHENESISQSLVEFIETSNVGEFRRRLQLLFCFLLQLSMGSSLGIYSSDSHKRRVEMCYNIFGFYIQFLPVVMEQLDLNRKNVETELKEVLKLCRWERPDNYLYNETTKRTRQKVKKLIQKFTDMLRLPVMLVKPDLTKERAQFLPLLDPDLMDGASDMRIEVLVSALDAEQLRDRSSWYVVWWNKLKESVGRFHQEMHYKTLLMGAEHQYSSPVYQGDWKNLWSTVARIGETIAGCSDLWRNSDRDVAKKRALFELLKLLESSGLQKHKFENIEMSNHFKGLLYQPAYDPKHLLLLTHTKSNIHPSMGVEDQNKENSLVEWRVANEFYFKSLASVQLMLNIDRKHSDVTAEQVKRAISFLNHLVEIQRQQRKSAYAFAELFNRFRQCVLSLARLLGDSVGADRKDDSVFSFPQNQHAVFNCLWLQKQLFDNITAMLLEESALLRTVGSTHLDSCQAVKTSSRSLLSFIEILIPIAQNSKASLDRLLLDCNGFIITPSSSLKQFVTQHMVQVLRQNFDQLTDLENQISSFCENNEKSYCRDVLLSQFSPVFKEGKLLAENLNCLLNVRDQSTGMEPKERLFLEENLASIFANVKDVIGKLCSYKDGSLSQEEEMNITTWDGLFKKAENDLNLDNLCKLLSESFGSIEQLLNSSGVLSAGVGDQLKQLQAFLDLLLSFGDCYLKEFLAISKTVSLITHVLASVLADLFTKGFGISKNEEDDDSKVDKSEAAEGTGMGDGVGAKDVSDQIEDEDQLHGTDKKEEEEKEQDDVLGKNKGIEMSDEFDGKEYSVSEDEEEDKEDEGSEDEPLDNGIGDVGSDAEKADEKPWNKDEEDEEENMNEKNESGPSIVDKDTRSRELRAKDDGVETADEPEESNTSDKPEEGNDENVEQDDFDDTDNLEEKIQTKEEALGGLTPDVDNEQIDDDMEMDKTEEVEKEDANQQEEPCSEDQKHPEEGENDQEETQEPSEENMEAEAEDRCGSPQKEEPGNDLEQEPETEPIEGKEVMSEDMMKPNFRNDNISGVESGSQNPHGSNVLGAGSTAPQENLSATDVTDELTDSMDLPSSSNTEMNLMMTNMANGETLTDNLPKMEFPQNQSSTAQQTKVNPYRNVGDALKEWKERVRISSDLGEKQEAENEMEDPDASEYGFASQFDAGTSQALGPALPEQVNTDMREGESEEEKLAGNQDDVSPMDIDDLNPENKPAVQSKPSISNSIAEQVQEPDTDRTHQENSPIHNFGDGNSRMDSMVSVDNTFLGEEACNLDRMQVTDNDSESNQDNQEDPDARSNAVVLWRRCELLTAKPSQELAEQLRLILEPTLASKLSGDYRTGKRINMKKVIPYIASHYRKDKIWLRRTKPNKRDYQVVIAVDDSRSMSESGCGDFAIRALATVCRAMSQLELGSLAVASFGKQGSIKMLHDFGQSFTTESGIKMISNLTFKQENLIEDQPVVNLLRNMNEMLENLASTRRQSYGSNPLQQLVLIIGDGKFHEREKLKRTVRSFLQQKRMVVYLLLDDAEQSVFDLADYVYDGERRPYKKMNYLDSFPFPYYIVLRDIEALPRTLGDVLRQWFELMQSSRD

Midasin (AtMDN1) (Dynein-related AAA-ATPase MDN1) (MIDAS-containing protein 1) (Protein DWARF AND SHORT ROOT 1)

Arabidopsis thaliana (Mouse-ear cress)

3,702

5,400

611,889

Abscisic acid signaling pathway;Alternative splicing;ATP-binding;Chaperone;Coiled coil;Nucleotide-binding;Nucleus;Reference proteome

GO:0000027; GO:0000055; GO:0005524; GO:0005634; GO:0005654; GO:0005730; GO:0005737; GO:0009506; GO:0009553; GO:0009738; GO:0009941; GO:0016887; GO:0048638

Evidence at protein level

5

SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q12019}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q12019}.

null

PF07728;PF17865;PF17867;PF21108;

IPR003593;IPR040848;IPR011704;IPR048617;IPR012099;IPR041190;IPR027417;IPR025662;IPR002035;IPR036465;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), rosids (clade), malvids (clade), Brassicales (order), Brassicaceae (family), Camelineae (tribe), Arabidopsis (genus)

MDN1 DSR1 At1g67120 F5A8.11

false

338

A0A1P8AW69

MAKRGYKLQEFVAHSGNVNCLSIGKKTSRLLLTGGDDYKVNLWSIGKTTSPMSLCGHTSPVDSVAFNSEEVLVLAGASSGVIKLWDLEESKMVRAFTGHRSNCSAVEFHPFGEFLASGSSDTNLRVWDTRKKGCIQTYKGHTRGISTIEFSPDGRWVVSGGLDNVVKVWDLTAGKLLHEFKCHEGPIRSLDFHPLEFLLATGSADRTVKFWDLETFELIGTTRPEATGVRAIAFHPDGQTLFCGLDDGLKVYSWEPVICRDGVDMGWSTLGDFCINEGKFIGCSYYRNSVGIWVSDISELEPYGAVSEDKNECMVKRFSVLNDQSERMGSGPRGSVSPDYETREIKNIYVDCGNLNVAQNPGSLKATLPLESGKVATMVSEKQNAAYFGPAGDKYSSTSRDSDSGEESSYSERESIPFSRTKSGMLLRPAHVRKTLAKFEESKQSAVVQSATRKKSGLAVEEEPQTQNAFLSEQNASKPFDAEDSIIKGITNKFEKALSSEPPTDEANRMFLKPPRIHRSSNSKYNDTRRAMSADPATFGKGGMENSGDVEDIPSKTERVLSREKPGDEQKNTEYPSGSRELNPVKIVEGVNVVSGRTRSLVEKFERGEKTTHTEGASTTIEQNNNAVQEDPRKTSRQTGETPVISTRRARSTPARVMPIVLNRDSNVTSDEPPLTQPARTSSFPVMPVILNQASNVTYDEPSVALTQESRTSHARILPVTFNQATNITSEEASVTLRRQRRNSAARVRPVLLSQATSHECPVTSVRPLRTSPARVMPTKLNQSVNMTSDTSHIASMHRVSPTQMLATPTVIDQVADMTLDETHATQIQPACDNMPQKEEPNISDREDDSDITENLMLTHNEFLSTLQSRLTKLQIVRHFWERSDVKGAIGALRKLTDQSVQADVISILTEKIEILTLDMFSQLVPVLTSLLGSRTERPVNVSLDMLLKLVAVFGTVIRSTVSAPRIVGVDLHANERLEICQICSAGLHKIQRILPVLARRGGLITRKAQELNLVLQEP

Katanin p80 WD40 repeat-containing subunit B1 homolog KTN80.1

Arabidopsis thaliana (Mouse-ear cress)

3,702

1,019

112,385

Cytoplasm;Cytoskeleton;Microtubule;Reference proteome;Repeat;WD repeat

GO:0005737; GO:0005874; GO:0008017; GO:0008352; GO:0015630; GO:0051013; GO:0051510

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000269|PubMed:28978669}. Note=Present in dynamic discrete particles specifically localized to microtubule (MT) crossovers and branching nucleation sites. {ECO:0000269|PubMed:28978669}.

null

PF13925;PF00400;

IPR020472;IPR028021;IPR026962;IPR015943;IPR019775;IPR036322;IPR001680;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), rosids (clade), malvids (clade), Brassicales (order), Brassicaceae (family), Camelineae (tribe), Arabidopsis (genus)

KTN80.1 At1g11160 T28P6.17

false

339

A0A1R3RGK0

MTFTSHPQSEPLAIIGLACKYANDINSPLDLYQQVMAARSMHGPMPPSRMDAAFYYHPSSEATGTTYAKGGYFLQSDLNAFDSPFFQLSEIDVLAMDPQQKMLLENVYHALENAGIPLKDAVSSSTSVFVGCSNNDHLALANADLLLALKGKGTGTSPSILANRISWFYDFQGTSQTIDTACSSSLVAFHQGCMDVRAGKSTMSIISGVNLMEHPAPTMYLSSLGVLSPDGRSMSFDARANGYGRGEGLGTVIIKPLTAALRDGNRIRAIVRSTGSNQDGRTPGITVPSPTAQERLIREVYKAADLDPSRTGYVEAHGTGTPVGDPLEVQAISAALGMSRDSPLYVGSVKSVVGHLEGGAGMAGLISATMAVESKTIPPVAGLQTLNPRIPQRPDLKFAKEATPWPREDVRRASINSFGFGGTNAHVVLEDVEGFFSDLFGQQLPGALQLSEVTSKALVPSAMKSAVNGIPADQPPKESSVNRLFVISAFDEAGIQRNAASLASHLESMRAITGSDGEERLLNDLCHTLNEKRTRFDWRSYHVADSIDSLRNSLQNPRPIRQSPAEKVVRFIFTGQGANWAGMAYDLLVYPLFRRRIQEAAIFLKELGSDWDLYERIASQSGELDEPTFAQSSCVAVQVALVDLLASWNVTPQTVVGHSSGEIAAAYCAGQISRQAAWKVAFCRGQVCARRTDGQGRMLAAAMPVTQLEQLVARVNKGQSTAVKVGCYNSPKNLTLTGRAEDILRAKLELDDVGALNRLLPVKVAYHSDYMRDAAPEYLDLLGDLDFGDSIHADAGIKMVSSVTGRAVSAGEAQQPSYWVDNLVSPVRFSTALLASMDDPSATGAREDALIEIGPHSTLRTAIKETFADVREFQSIQYGSLLKRYETDGSTILRTFGMLVCSGHKISLAAINDRRVGAKKTPRLLTGLPSYAFDHSRSMRGTSRRIEQAKFPAYKRHELLGVPVEDTNPVEQRWRNILRPDDLPWLRMNRMNGQIHFPGVAYLLMATEAAIQRVGNTVAISGVRLGNVSMLAPLPIPDSAAGVEIQFSIYPMKIHANSGTDWSTFRIVSYDSAEKTWTEHCVGSVRVETGPHESHEPHPGNATREECTESVDIAQMYSRFTTAGMDFGEYLRNIQEMKLSPDHQACTATITAPDIPCQAHDHYSLHPCTFESILHALLHLCKSSQGPMVTTYIEEVLVLSPQDTGVCGFEACAQTQRASATTWRSDVTITANTGRQQIRVTGLDLVQLPPSEDASDAESFYVVKWKPDVKLLTSVDALRDSASMYVAQHLPTLDEHEGFQLASGIFLLDTMDYVTRTGLPALPQHHQAFMQWMEKECRSIADGTVPLLDTALFEGIRASPDRRRELLARVAQLSARGELLVRVGTQMVPILEQKIDCLEVMFGPDNLMDRTYEEGLPGQIAPSVAGYLHCLAHAQTGIKVLEVGAGTGSATKVILDSLKPTERQDGGGLVSSVSTYHFTDISAAFFEKARARFPDWADILRPKVLNIELDPADQGFEMGSYDLVIATHVLHATADLSVSLKNIRGLLKEGGDLIVIENIQPDLMCSPLAFGLLPGWWRSVEPYRKTNPLITKDQWDQELRNAGLQSRLLIDDTDEGVNEMTAFVASRVREPPATQHVCSIIYSSRYGGQYELASQVARDLPPSCTASLVDLADISPEHTSTIGIVLVGYQGLDLSELSAHEYDRVNFLLTAFHRLLWVTCDEDEVPKSAMASGLVRTARWERDHDGVNFILLGISHRVPSASAAVSQMIRVCDHAFFSHELVPRNAEFRLEGSVLLTNRLFPATGINECIASSSRPRSKQVALEAVQHPVKLTSIGPHQPNGFHFVEDPQVDEPLLPDEVKIQIRAVGLDESDVEEMNRLIPGESAGSQGTGVVVEVGPAVHDIHVGDRVMALRTGHSGSLQTVLRTHSSAVTQVPEGLSLADAAAVPLPFTTAYHGLVNVARLEPQDTILIHNAGGATGQAAVQFACMLGATVYATVESDAQRQALLDYGVDRSRLLDGPSFAQQLARRGAKGSVDVLFNLSRESLEDRDLACLSQFGRLVGVHGQGSLPAGPTNRSYATVSIRELVQVRPKALHGTLRTISDLLTSRAIRPITPVRAGYSELQTVLSQIRQGNAGPWVLEPRANDTIPVAMKPLGDYQFDPCASYLLIGGFGGIGRSVVRWMLTRGAKNFIFLSRSGASSVPAKQLCADLLDAGCGVSDTVCDVTDATAVENALQQCGKSMPPIRGCLQCSMVLEDSMLSNMSHAQFLNAITPKVQGTIHVASALSSVKSNLDFFVLLSSSAGIIGNRGQANYSAANAFLDAFAAHLVSRGYPATSISLGSVLSVGWVAENQDRLPIALSYGAISEDLLLAILEYHMDPSWGAAQSPGTCHTVAGVRSARDFQRQSIPLPGFMAYPLFSPLRAIAGASQTAEEVAEAPIAQGLRGATSMEDAVELVTRAIVYKLARIMALSAKEIDAQRSLASYGVDSLVTVDLKAWFQREVGATVASGDLLGDSTIVQLAQQAAGGSRLVSVAMKGTE

Highly reducing polyketide synthase otaA (EC 2.3.1.-) (Ochratoxin A biosynthesis cluster protein A)

Aspergillus carbonarius (strain ITEM 5010)

602,072

2,541

274,798

Acyltransferase;Methyltransferase;Multifunctional enzyme;NADP;Oxidoreductase;Phosphopantetheine;Phosphoprotein;Reference proteome;S-adenosyl-L-methionine;Transferase

GO:0004312; GO:0004315; GO:0006633; GO:0008168; GO:0016218; GO:0016491; GO:0031177; GO:0032259; GO:1900818

Evidence at protein level

5

null

PF23297;PF00698;PF08240;PF16197;PF00109;PF02801;PF08659;PF08242;PF21089;PF14765;

IPR001227;IPR036736;IPR014043;IPR016035;IPR013154;IPR011032;IPR018201;IPR014031;IPR014030;IPR016036;IPR013217;IPR036291;IPR032821;IPR020841;IPR042104;IPR020807;IPR049551;IPR049552;IPR020843;IPR013968;IPR049900;IPR050091;IPR020806;IPR009081;IPR029063;IPR016039;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), Eurotiomycetes (class), Eurotiomycetidae (subclass), Eurotiales (order), Aspergillaceae (family), Aspergillus (genus), Aspergillus subgen. Circumdati (subgenus), Aspergillus carbonarius (species)

otaA OTApks ASPCADRAFT_173482

false

340

A0A1R4LHH9

MKFTAIVGTTSPKSYNRTLLQFMQAHFKDKADIELLEIDQVPMFNQDQPSTNPQLLEINQKIIASDGVIIATPEYNHSIPSSLKSVLEWLSYELHPLDGKPVMILGASIDAQGSSRAQLHLRQILDAPGVNANVMPGYEFLLGNAHQAFDDKGQLNNEATIDFLEICFFRFMRFAKISNQLNVEEDFSFAPGTYEVHALGHGGALPMQVSFSEKKIESIHIDTAGETEGLADVVFVRIPDKIIEGQTLNVDALSGASETSHAVIDGVAKAVKLAGVNPDILKKRPKPASSLNRDDEEYSCDVVVIGGGGAGLSAAATVLQAGKNAIVLEKFPAVGGNTIRTGGPINAADPEWQRTFDENPGERHTIEALLSTDESEIHPEYLADFRALKEEFAAYQQQFGDQKGYLFDSPLLHRMQTYFGGKRTDLEGNSIYGQYDLVKILTDHALESVQWLEEIGVEYDKEVVFAPVGALWRRGHKPVKRYGTAFILALSRYIESMSGTILTDSPAKEFLIEDGEIKGVIATGVNGQKITIHAKAVVLASGGFGANTKMLQQYNTYWSHIADDIKTTNSYAMTGDGIVLGQSVGAGLIGMGFTQMMPVADPNTGELFSGLQVPPENFVIVNQQGKRFVNEFAGRDVLTKAALAEGGLFYLIADDEIKKTAANTSQEKIDRQVEAGTLFRADTLEELAVQVGMEPDVLVETINKYNRYVEAGHDPEFHKDTFSLKVEKAPFYATPRQPAVHHTMGGLKIDTATRVLNENNRPIKHLYAAGEVAGGIHAGNRLGGNALADIFTFGRIAGKTAMSEMD

NADH:(hydroxy)cinnamate reductase subunit CrdB (EC 1.3.1.-) (NADH:cinnamate reductase subunit CrdB)

Vibrio ruber (strain DSM 16370 / JCM 11486 / BCRC 17186 / CECT 7878 / LMG 23124 / VR1)

1,123,498

806

87,942

FAD;Flavoprotein;FMN;NAD;Oxidoreductase;Phosphoprotein;Reference proteome

GO:0010181; GO:0016020; GO:0043786

Evidence at protein level

5

null

PF00890;PF04205;PF03358;

IPR003953;IPR050315;IPR036188;IPR010960;IPR029039;IPR007329;IPR005025;IPR027477;

null

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Vibrionales (order), Vibrionaceae (family), Vibrio (genus), Vibrio ruber (species)

crdB urdA VR7878_01556

false

341

A0A1S3PBB7

MKLGVRLCVLVVFSLQLWGPGQGQELEPEQVLAFCDDKDVEAAVDLALVKYNQKLPYGNQLALYQILESSKAQNDSCTQYFVEFNSRVTDCPAGGDKVWRDCDYLPTGNKVPRPCKATVHMSETDKKVLAVFCDPVEAPVVAERTTCLGCPREIDVESEDLKDPLTYSITRFNADSDSSHHFILNSVGFATRQVVAGFRYRLMFDMRKSNCSKADHKELNDECHPDPDVELAHCNSTVDVAPWRHETAEANVECAPGPLDNFDVFRRRPPGWSPLRNFNNFAEVKTTQASTASAKEESSEESQERSPSAVTMANPEPALPSVAPTTAAESPFHCPSKPWKQFVPPTTLRPAQEKSPTPLPVVEEGLSDLDLLGKK

Kininogen [Cleaved into: Bradykinin]

Salmo salar (Atlantic salmon)

8,030

375

41,560

Cleavage on pair of basic residues;Cytoplasm;Direct protein sequencing;Disulfide bond;Glycoprotein;Protease inhibitor;Reference proteome;Signal;Thiol protease inhibitor;Vacuole

GO:0004869; GO:0005737; GO:0005773; GO:0007204; GO:0030195; GO:0072562

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12397376}. Vacuole {ECO:0000269|PubMed:12397376}.

SIGNAL 1..23; /evidence="ECO:0000269|PubMed:10583403"

null

PF00031;

IPR000010;IPR046350;IPR027358;IPR050735;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Actinopterygii (superclass), Actinopteri (class), Neopterygii (subclass), Teleostei (infraclass), Osteoglossocephalai (clade), Clupeocephala (no rank), Euteleosteomorpha (cohort), Protacanthopterygii (clade), Salmoniformes (order), Salmonidae (family), Salmoninae (subfamily), Salmo (genus)

LOC106584303

false

342

A0A1S3X835

MYKPQQQQQLFDLQDNNGAAFDNGGTDPSCWLSHENEISRTDSSLSSSNVDPLLFNDLVQIVPLVQSLIDRKEKSSFTRRGSMTYTKMPSRESLYKKTSEVKGRNAGQSTATKKHRDQNKNVSSSQDGYAENFSTPSSTSSLTEKDREELMTLREKVEDLQKKLLEKDELLKEAEILKNEITATNAELDEMKKDISEKDFLVKTTQVQLSDALVKLADKKAAVEKLEWEAMTSSKKVERLQEDLDLLQGEISSFIQFVHALTGNDSRDSAEECNVIPYPWDQNVEIDKLNERDLQKMEAAREAYIAAVAAAKENPDEASLSAASTARSYLQSLVLRT

Protein MICROTUBULE BINDING PROTEIN 2C (NtMBP2C) (Movement protein binding protein 2C) (TMV-MP30 binding protein 2C)

Nicotiana tabacum (Common tobacco)

4,097

337

37,930

Alternative splicing;Coiled coil;Cytoplasm;Cytoskeleton;Host-virus interaction;Plant defense;Reference proteome;RNA-binding

GO:0002230; GO:0003723; GO:0005737; GO:0006952; GO:0008017; GO:0010497; GO:0015630; GO:0046740; GO:0051224; GO:0051493

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12913144}. Note=Microtubule-associated (PubMed:12913144). Localized in cytosolic punctae when associated with KN-1 (PubMed:17965274). {ECO:0000269|PubMed:12913144, ECO:0000269|PubMed:17965274}.

null

IPR040289;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Solanales (order), Solanaceae (family), Nicotianoideae (subfamily), Nicotianeae (tribe), Nicotiana (genus)

MBP2C LOC107762219

false

343

A0A1S3XSG2

MATTKQKVTAPSSSTAPCCPSTSILRREATAAVAGVGDGLQNWNNVPSVDDKQKKTASSALASLASTEPLSSNTSTKGIQIMTRAQTCHPLDPLSAAEISVAVATVRAAGETPEVRDGMRFIEVVLLEPDKSVVALADAYFFPPFQSSLMPRTKGGSLIPTKLPPRRARLIVYNKKTNETSIWIVELNEVHAAARGGHHRGKVISSNVVPDVQPPIDAQEYAECEAVVKSYPPFRDAMRRRGIDDLDLVMVDPWCVGYHSEADAPSRRLAKPLVFCRTESDCPMENGYARPVEGIYVLVDVQNMQIIEFEDRKLVPLPPADPLRNYTAGETRGGVDRSDVKPLHIIQPEGPSFRISGNYIEWQKWNFRIGFTPREGLVIHSVAYLDGSRGRRPIAHRLSFVEMVVPYGDPNDPHYRKNAFDAGEDGLGKNAHSLKRGCDCLGYIKYFDAHFTNFTGGVETTENCVCLHEEDHGMLWKHQDWRTGLAEVRRSRRLTVSFVCTVANYEYAFYWHFYQDGKIEAEVKLTGILSLGALQPGEYRKYGTTILPGLYAPVHQHFFVARMNMAVDCKPGEAHNQVVEVNVKVEEPGKENVHNNAFYAEETLLRSELQAMRDCDPFSARHWIVRNTRTVNRTGQLTGYKLVPGPNCLPLAGPEAKFLRRAAFLKHNLWVTQYAPGEEFPGGEFPNQNPRVGEGLASWVKQDRPLEESDIVLWYIFGITHVPRLEDWPVMPVEHIGFVLQPHGFFNCSPAVDVPPPSACDSESRDSDVTETSVAKSTATSLLAKL

Diamine oxidase [copper-containing] 1, peroxisomal (NtDAO1) (EC 1.4.3.-) (Copper methylamine oxidase) (EC 1.4.3.21) (N-methylputrescine oxidase 2, peroxisomal) (NtMPO2) (EC 1.4.3.-)

Nicotiana tabacum (Common tobacco)

4,097

786

87,421

Alkaloid metabolism;Copper;Disulfide bond;Manganese;Metal-binding;Oxidoreductase;Peroxisome;Reference proteome;TPQ

GO:0005507; GO:0005777; GO:0008131; GO:0009308; GO:0009447; GO:0009820; GO:0042179; GO:0048038; GO:0050232

Evidence at protein level

5

SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:24287136}.

null

PF01179;PF02727;PF02728;

IPR000269;IPR015798;IPR036460;IPR016182;IPR015800;IPR015802;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Solanales (order), Solanaceae (family), Nicotianoideae (subfamily), Nicotianeae (tribe), Nicotiana (genus)

DAO1 MPO2 LOC107768026

false

344

A0A1S3YCW2

MPALGCCVDAAVSPPPGYSFLWDSSLPAPEIFPSGVPPSTNTAVATTTTTHWSPAHSSALYSIDGWGAPYFTVNSSGDISVKPHGTDTLPHQEIDLLKVVKKASDPKNLGGLGLQFPLVVRFPDILKNRLESLQSVFDYAVQSQGYEAHYQGVYPVKCNQDRFVVEDIVKFGSGFRFGLEAGSKPELLLAMSCLCKGSHEGLLVCNGFKDAEYISLALVARKLMLNTVIVLEQEEELDLVIDISKKMAVRPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTTQIVRVVKKLEESGMLDCLQLLHFHIGSQIPSTALLADGVGEAAQIYCELVRLGAGMKYIDCGGGLGIDYDGTKSCDSDCSVGYGLQEYASTVVQAVRFVCDRKNVKHPVICSESGRAIVSHHSVLIFEAVSSTTTRSQELSSVDLQSFVEKLNDDARADYRNLSAAAIRGEYDTCVLYADQLKQRCVEQFKDGDLDIEQLAAVDGICDFVSKAIGASDPVRTYHVNLSIFTSVPDFWAIDQLFPIVPIHKLDERPVVRGILSDLTCDSDGKIDKFIGGESSLPLHELGSNGGGGGDGGKYYLGMFLGGAYEEALGGLHNLFGGPSVLRVSQSDSPHSFAVTCAVPGPSCADVLRAMQHEPELMFETLKHRAEEFVHNDDEQEEDKGLAFASLASSLAQSFNNMPYLVTNSSCCLTAAANNGGYYYCNDENIVGVGAESAAAEEELWPYCVA

Arginine decarboxylase 1A, chloroplastic (EC 4.1.1.19)

Nicotiana tabacum (Common tobacco)

4,097

733

79,045

Alkaloid metabolism;Chloroplast;Decarboxylase;Lyase;Magnesium;Plastid;Pyridoxal phosphate;Reference proteome;Spermidine biosynthesis;Transit peptide

GO:0006527; GO:0008295; GO:0008792; GO:0009507; GO:0009820; GO:0042179

Evidence at protein level

5

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.

null

PF02784;

IPR009006;IPR002985;IPR022657;IPR022644;IPR022653;IPR000183;IPR029066;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Solanales (order), Solanaceae (family), Nicotianoideae (subfamily), Nicotianeae (tribe), Nicotiana (genus)

ADC1A ADC LOC107774919

false

345

A0A1S3Z5Y0

MDGSGQQTDTMMSDAGAEQPPPAPQPVAGMDNIPATLSYGGRFIQYNIFGNIFEVTAKYKPPILPIGKGAYGIVCSALNSETIENVAIKKIANAFDNKIDAKRTLREIKLLRHMDHENIVAIRDIIPPPQREAFNDVYIAYELMDTDLHQIIRSNQGLSEEHCQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARVTSETDFMTEYVVTRWYRPPELLLNSSDYTAAIDIWSVGCIFTELMDRKPLFPGRDHVHQLRLIMELIGTPSEAEMEFLNENAKRYIRQLPLYRRQSFTEKFPHVHPAAIDLVEKMLTFDPRRRITVEGALAHPYLNSLHDISDEPICMTPFSFDFEQHALTEEQMKELIYRESLAFNPEYQHM

Mitogen-activated protein kinase SIPK (EC 2.7.12.2) (Salicylic acid-induced protein kinase)

Nicotiana tabacum (Common tobacco)

4,097

393

45,139

ATP-binding;Kinase;Nucleotide-binding;Plant defense;Reference proteome;Serine/threonine-protein kinase;Transferase

GO:0004674; GO:0004707; GO:0004713; GO:0005524; GO:0005634; GO:0005737; GO:0006952; GO:0035556; GO:0106310

Evidence at protein level

5

null

PF00069;

IPR011009;IPR050117;IPR003527;IPR000719;IPR017441;IPR008271;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Solanales (order), Solanaceae (family), Nicotianoideae (subfamily), Nicotianeae (tribe), Nicotiana (genus)

SIPK LOC107772177 LOC107783427

false

346

A0A1S4AUX8

MAGQTIIVSGLNPAAILQSTIGGGASPTAAAAENGTRKVIPLSRDALQDFMLSIITQKLQDEKQPFYVLDLGEVVSLIDQWKSALPNIRPFYAVKCNPEPSFLSILSAMGSNFDCASRAEIEYVLSLGISPDRIVFANPCKPESDIIFAAKVGVNLTTYDSEDEVYKIRKHHPKSELLLRIKPMFDGNARCPMGPKYGALPEEVEPLLRAAQAARLTVSGVSFHIGSGDADSNAYLGAIAAAKEVFETAAKLGMSKMTVLDVGGGFTSGHQFTTAAVAVRSALKQHFDDQPELTIIAEPGRFFAETAFTLATTIIGKRVRGELREYWINDGLYGSMNCVLYDHATVNATPLAVLSNRTNVTCGGSKTFPTTVFGPTCDALDTVLRDYQLPELQVNDWLVFPNMGAYTKAAGSNFNGFNTSAIVTHLAYAYPS

Ornithine decarboxylase 1A, chloroplastic (EC 4.1.1.17)

Nicotiana tabacum (Common tobacco)

4,097

432

46,538

Alkaloid metabolism;Chloroplast;Lyase;Plastid;Pyridoxal phosphate;Reference proteome;Transit peptide

GO:0004586; GO:0005737; GO:0006596; GO:0009507; GO:0009611; GO:0009820; GO:0033387; GO:0042179; GO:1901695

Evidence at transcript level

5

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.

null

PF02784;PF00278;

IPR009006;IPR022643;IPR022657;IPR022644;IPR022653;IPR000183;IPR002433;IPR029066;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Solanales (order), Solanaceae (family), Nicotianoideae (subfamily), Nicotianeae (tribe), Nicotiana (genus)

ODC1A ODC ODC1 LOC107801491

false

347

A0A1S4BDC4

MATTKQKVTAPSPSPSSSTASCCPSTSILRREATAAIAVVGDGLQNWTNIPSVDEKQKKTASSALASLPTTEPLSTNTSTKGIQIMTRAQTCHPLDPLSAAEISVAVATVRAAGETPEVRDGMRFIEVVLVEPDKSVVALADAYFFPPFQSSLMPRTKGGSQIPTKLPPRRARLIVYNKKTNETSIWIVELNEVHAAARGGHHRGKVIASNVVPDVQPPIDAQEYAECEAVVKSYPPFRDAMRRRGIDDLDLVMVDPWCVGYHSEADAPSRRLAKPLVFCRTESDCPMENGYARPVEGIYVLVDVQNMQIIEFEDRKLVPLPPVDPLRNYTAGETRGGVDRSDVKPLHIIQPEGPSFRISGNYVEWQKWNFRIGFTPREGLVIHSVAYLDGSRGRRPIAHRLSFVEMVVPYGDPNDPHYRKNAFDAGEDGLGKNAHSLKRGCDCLGYIKYFDAHFTNFTGGVETTENCVCLHEEDHGMLWKHQDWRTGLAEVRRSRRLTVSFVCTVANYEYAFYWHFYQDGKIEAEVKLTGILSLGALQPGEYRKYGTTILPGLYAPVHQHFFVARMNMAVDCKPGEAHNQVVEVNVKVEEPGKENVHNNAFYAEETLLRSELQAMRDCDPFSARHWIVRNTRTVNRTGQLTGYKLVPGPNCLPLAGPEAKFLRRAAFLKHNLWVTQYAPGEDFPGGEFPNQNPRVGEGLASWVKQDRPLEESDIVLWYIFGITHVPRLEDWPVMPVEHIGFVLQPHGYFNCSPAVDVPPPFACDSESRDSDVTETSVAKSTATSLLAKL

N-methylputrescine oxidase 1, peroxisomal (NtMPO1) (EC 1.4.3.-) (Copper methylamine oxidase) (EC 1.4.3.21)

Nicotiana tabacum (Common tobacco)

4,097

790

87,966

Alkaloid metabolism;Copper;Disulfide bond;Manganese;Metal-binding;Oxidoreductase;Peroxisome;Reference proteome;TPQ

GO:0005507; GO:0005777; GO:0008131; GO:0009308; GO:0009733; GO:0009753; GO:0009820; GO:0042179; GO:0042802; GO:0042803; GO:0048038; GO:0052595; GO:0052597

Evidence at protein level

5

SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:24287136}.

null

PF01179;PF02727;PF02728;

IPR000269;IPR015798;IPR036460;IPR016182;IPR015800;IPR015802;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Solanales (order), Solanaceae (family), Nicotianoideae (subfamily), Nicotianeae (tribe), Nicotiana (genus)

MPO1 LOC107807126

false

348

A0A1S4EWW7

MASHVIVKFITAAILIGSCYANYCDQSLCRRGPHVACNAPTQFGSACGQEPKFVKMDARMKNLLLKKHNELRAEIACGKHGFPQAARMPTLVWDDELAHIASFNARKCIFAHDKCRNTREFKFAGQNLAITAFAGYNFQAADRAENFTQEWFNEHKDCPKSYVDSYPMSHSGPQIGHFTQMVNDRAWKMGCSMVHYKNGRVIKYYLVCNYSMTNMIEEPIYTRGSAGSKCQTGQNPQYRGLCSPREKVRSESYRG

Venom allergen-1 (AaVA-1)

Aedes aegypti (Yellowfever mosquito) (Culex aegypti)

7,159

255

28,897

Glycoprotein;Host endosome;Host mitochondrion;Reference proteome;Secreted;Signal

GO:0005576; GO:0033650; GO:0044174

Evidence at protein level

5

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31937766}. Host endosome {ECO:0000269|PubMed:31937766}. Host mitochondrion {ECO:0000269|PubMed:31937766}. Note=Delivered into the human immune cells by endocytosis in a RhoA-dependent manner; escapes from host endosomes to mitochondria. {ECO:0000269|PubMed:31937766}.

SIGNAL 1..21; /evidence="ECO:0000255"

null

PF00188;

IPR014044;IPR035940;IPR001283;IPR034763;IPR002413;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Mandibulata (clade), Pancrustacea (clade), Hexapoda (subphylum), Insecta (class), Dicondylia (clade), Pterygota (subclass), Neoptera (infraclass), Endopterygota (cohort), Diptera (order), Nematocera (suborder), Culicomorpha (infraorder), Culicoidea (superfamily), Culicidae (family), Culicinae (subfamily), Aedini (tribe), Aedes (genus), Stegomyia (subgenus)

AAEL000793

false

349

A0A1S4F020

MIPRIVVVLLSVLAVVTARRSYEGYKVYGIVPESPDEAEILYQIRQSNPDLDFWHLTKQPGDEARVLVAPKDQRSFLIKLIRHGLHYQEVISDVEGTLAPYNEPRTRGMSLDRDVSTSYLRHNEINEYLQTLSQKYPSLVSVEEAGTSYEGRSIKTITINKKPGNAVVFLDAGIHAREWIAPATALYAIEQLVEHSSENQEVLSNLTWVIMPVVNPDGYEFSHETDRFWRKTRKPTGKTCKGTDGNRNFDYHWGEVGASTQACADTFRGETAFSEPETRAVRDAVMKLKGSCKFYLSLHSYGNYILYPWGWTSKLPETWEAIDEVAQAGAEAIKQSTGSRYTVGSSTNVLYAAAGGSDDWAFAVAEVPISITMELPGGGNGGFNPPPSSIEKIVNESWVGIKAMALKVAQMF

Carboxypeptidase B1 (AaCPB-I) (CPBAe1) (EC 3.4.17.2)

Aedes aegypti (Yellowfever mosquito) (Culex aegypti)

7,159

412

45,840

3D-structure;Carboxypeptidase;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Zinc;Zymogen

GO:0004181; GO:0005615; GO:0005783; GO:0006508; GO:0008270

Evidence at protein level

5

SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:25521592}.

SIGNAL 1..18; /evidence="ECO:0000255"

null

PF00246;PF02244;

IPR036990;IPR003146;IPR000834;

7EQX;7EQZ;

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Mandibulata (clade), Pancrustacea (clade), Hexapoda (subphylum), Insecta (class), Dicondylia (clade), Pterygota (subclass), Neoptera (infraclass), Endopterygota (cohort), Diptera (order), Nematocera (suborder), Culicomorpha (infraorder), Culicoidea (superfamily), Culicidae (family), Culicinae (subfamily), Aedini (tribe), Aedes (genus), Stegomyia (subgenus)

CPB1 CPB-I

false

350

A0A1S4FPC9

MLRIKEVKKYNNRLGFPAGKEVRIRPLLEAGGFARGPIYVKYGRELSKHDPSSRSMAWNATVFDTALNHPTRPWTVTVVGGKKMVLGVRKEGLGFSEDDPPRSLNVKGGDDMADENYGGGNSTIVLVKSGGKDFAIGLDDLKELNSFGIGAGNGKLSLALGNPVNVLTGVVLPVEQRDGSVAYVAVNSDTKSVIYKVDAKGLQKNQKIDVNVRASAEKILLTKNNELLHISPQGLNVYSVQGSASTFKYFCPYFSSFGGWSRRFVDTVTLMDEGGNQEALIGTGPKGIEYMPVDEKCKNYVVEGVQDAKHAVVAPGATKEGNDIKVLGVYNGELCLLTLEVVDAVEPKLDQGSPAKPSAERVKATKSSKVTVRSGALSKPVSWLRDSLDEASFKNIVDKLSGKIRFSFPLVDLQGRMGLPIKLVVYYDESDGEDMSVLGRHWTLGRDCIVLDHGNTVFEDKQDYYLVKDQMKIRLERDWTKPSANGKVLFNMVGNKDATFEYTAREEKWEVSDGKIRYVYGMNNQGVVSVPGWADWYGPSANYDSKKIHSVQWNLVEISSVAHRDVKLKYTYTPLDPSTHTMHLLSITDDSNKTTIKFSYKTIEGLGKQVSSGLVKEHKFINNKLLEKVEIDSPSTAQVLKLTSTKIDSLYYLESIKQDDDPDPVLGFEYNKDDKLKPRVQQIRLPSKSVVDFKYTKQAIATQQFEQEIAKMADLYTGNEYSLEIEKTVGETDLYVRLKDSAGKNDFIKNQSIRIESYRGFKIKSYSPFMMHSYIAILVRYAEEKEKLHNKIYILNKGEDDSWKLDTTNNNSRVSEDKKFKYDFQEDSFVYYHSKKVHFEYKKSGTKVWSYTSKDIGDVDAFTLMNRGAVYCKNDLVLIRWDALGKLQQETLSDAKSKPSISDVDTFFEYIDVQGTFPEDEAEAKKEVDDYKRDLKESLSDYGLILYNNVVALRTIKLSFTGRITVKVLLYLLKHDYTVSSRSSIELQGGDLAKFNLTLDVFDEHKTKNTNDLDKYRFEFKKQGSKFKLTYIEATDKDNKPTKPSSQNEKLIGQYERRMKIPLDFEKYMMQVNQEGIIVNDHQIIHDNGNFIAKQLDRDTLKLTKFKIPLGAFSNFKKDSDGDEIKLCTKTEQERTESCVSLQTNSARNVSIKYPYYLVTQKKNDIKVLPLKINSRGWEDSVDYRGEILHGSSSHAAMVTTRMSDQKTIVRPLKALNKINKIYAQVISEEKLTTPYDSYVIKYEYEDPVVSMNQVAFKTTIVVPGGGKSATGYYRETNDLQDNQQIVQVMTADNQVFDPEYVKRMNEMQQEEDKQRDGAQLDAEQTITDKSGYHPILKTTPYSANQELVQFLGFEDYEDMTGWTVNRRPIQESNIRRNEFSATGRNFLLLRKGEELIAEFPNTAYYDTFIASTWIRTTQETAVGSTTDMLSLYVDNKPMKGTIKQTIDEWIYVEADSREIAVPESTAVKRVHFKIIVKPTGADDVHVDHVRLSPVNFNFEGSVYDARIGQRTATIQTNGFVSRRLYDAYNRRIAEVDETGNIKYLASYSKRVGNKKDEKKREGGISSRLQMRAKHSWVESFSPYTMEKRWQIGGAATVEPNQAILQGQIISKEKFSSESICIRLVYSMSGSSQLSLTIGKTTVVVKPNAVQYKGHTATTPSNAELVIFATPKLTSIWVDGHLRIEAPETHAKFNNEAVSLQTSGPVGIKDVIVMEDAEIQVSYLNRDSKPLQEILLLDSSNVLIRQMMYDVIGRRVAETVWVQKSLIDGRSTAFKAFQYHDDFVSNDNPTDRNYFLNTGPMQGYVATATNTIYEGYPYSQTVYYNNPLEIRHKVGHPGVKNSIKGAFVHQYAIASDLAFIQRNYPKNEGYRQEEEKSPNGKKHVVVYNRRNKKVAEYTQVKDYNNILTTYIYDQHGNQIQMLPPSYYHEKSRSGDYQPEKQVVASPWAVTSKYDSTGEFITSKETPDGGRVEFIYNEYNQLRYQIHYKEDKQADKIVYFLYNIFGRMCEAGQVPANPTTLQQVRETTKSHQAIPNRDQAVYFDYGETESEPSLRGRIQRTVKKNKEVLFSEVMFFDEESNIIRKSYISPTTNETLSLVYLQENDKVSGIQYPFGVDGKQLILKYKHNLRGEIVEVARVEQKTSGQTEFIPIAGIDHDAEGKVTKISHNYGDSKFDQTYKYVAPGYLVEIANNFLTEKLYYTEKGYGCEPTGDGSILRTEFKASWHDKCDQNLIPLTARAFVSGGIDFTTAETCFDALLNLGYIDTTGRPVKTFYPDLETGLPMKCATPSNWRYISEKMLEQGYPEHYGHAYDYGSHGELIAAKSFVGKEKDSLTAPLSKASFANAGMKSHELDRFWDSLSRSINKVEGTKAIFEGTQQLTTGLVGSVIHKPKLESLLEGKGGDSSICTPWSSGDRTEEAKCKREYQQAFDKLKLKQVIQSLQEPVRKNVLRILKNTLASMLGNSPGDVESFSIDPNGNHGVFYTGFKRFELKYKHQKNQIATIKEGTKQQEKMIVHDDEGNVIKALHKKIDKIEYDPLTQRVSRIEMSDRSRTLEFGYDFRGERTFKRVRNKDNDIISVNYYVRDNKGNVLVEYKQEYPNPKDTNKPINTVTAYIHGPLGLLGFFRNNKYYNVLLDHEGSTRLVIHQGKVVAAYDYLPYGQMIRKYGSNPEAHIAFRYTGQEFDEETGLYNYHARLYDPDIGRFFQMDPMEQYASPYKYAGNSPVSQIDPDGQIAVTLVLMIIGAIVGAYLGAASANNSWNPAKWAWGDKKTWIGLFAGAIMGAFAVYGGAATFSYFTAMFGGSMIAGALATGVISVAGAFLGAAAASNQWNPAKWDWTSPAVWNGLLSGASIAVSFPSGFVGITRSFMSISSNLVKMIYASLMVGGFLLFVYLGGGMANNFNFQISQWDWKSPRTWFGMIEGASTIFMGTAGTAKHGAAKVYNVVKPNGLKMIWHKVNIPSKAFTMRRVKDTIILTWYKNGQSISKQILKTTVKADLAKIPKDFIMIHRGFFMPYQRIGYAAIAMPSMAGLMFKKNQYFFTNHPNGTLTKHVRKKRSAPMSSSAASPSVSNFLNDFFENMSELFDSFFSQTEHSHQDSQSSLSIGASYGRPSNESYHKSFQKLCYSPDSDGNQIICPQRESTVNIFSKGETFAPEAFGQDLFSRCLPLTWHDRPSIACDGEQTTFIYTPNQNIRVFDMVDGWLMLARIAPAALRNLKAGFSFLRDVVFSDEREQTVQVNDLSRCKQDLEVELLDLKRVMLKKQPNEVKWAQPILNDLEDDIGEFLSERKPSEKEFELLQERLSALREEIMENSSVATELNLSTLIGDMLKKMDGVNVGLNGDVRDMISTLSGMVPFSSSNLLA

Salivary gland surface protein 1 (SGS1) (aaSGS1) (Tox-SGS domain-containing protein)

Aedes aegypti (Yellowfever mosquito) (Culex aegypti)

7,159

3,364

379,959

3D-structure;Cell membrane;Disulfide bond;Glycoprotein;Membrane;Reference proteome;Secreted;Transmembrane;Transmembrane helix

GO:0005615; GO:0005886

Evidence at protein level

5

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16367875}; Multi-pass membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:17913537}.

null

TRANSMEM 2734..2754; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 2774..2794; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 2805..2825; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 2844..2864; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 2878..2898; /note="Helical"; /evidence="ECO:0000255"

PF15651;

IPR022385;IPR050708;IPR028901;

8FJP;

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Mandibulata (clade), Pancrustacea (clade), Hexapoda (subphylum), Insecta (class), Dicondylia (clade), Pterygota (subclass), Neoptera (infraclass), Endopterygota (cohort), Diptera (order), Nematocera (suborder), Culicomorpha (infraorder), Culicoidea (superfamily), Culicidae (family), Culicinae (subfamily), Aedini (tribe), Aedes (genus), Stegomyia (subgenus)

null

false

351

A0A1S4GMJ4

MCILTLVERKHLKNMVHVRLLVMMHILIIYSTFGAVRRPINIRVLEGNSCDTPQVIGGKCMNISLCDPAFVHSIAYQEHTPVCQQNAFYRVICCQPFLDFCENSKQFQIMHGIEAEPGMFPHLARLGLKSEEDGIAWTCSANIISERFLLTAAHCNPVNIAGLGCAESMQCDQQNTVKSFISNPKYKTSFKYHDIALVELEQNIRFNKRVLPICPYISKTDLHESEDLVIAGWGATESHFQSPRLMFATVRTVLQNDCKDHYASLLKASPNKKLHQGITDEMYCAQGALVDNVTEYIDACSGDSGGPLQTKQNNNLYLIGVISTGFGCGSSSPGLYTRVASYFGWIKETVSATRDN

CLIP domain-containing serine protease C9 (EC 3.4.21.-) [Cleaved into: CLIP domain-containing serine protease C9 subunit p12; CLIP domain-containing serine protease C9 subunit p30]

Anopheles gambiae (African malaria mosquito)

7,165

356

39,687

Disulfide bond;Glycoprotein;Hydrolase;Immunity;Innate immunity;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen

GO:0004252; GO:0005615; GO:0006508; GO:0035008; GO:0042742; GO:0045087; GO:0140546

Evidence at protein level

5

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33045027}. Note=Secreted into the hemolymph (PubMed:33045027). Recruited by CLIPA8 to microbial surfaces where it is cleaved into the two chain active form (PubMed:33045027). {ECO:0000269|PubMed:33045027}.

SIGNAL 1..?; /evidence="ECO:0000305"

null

PF00089;

IPR051333;IPR009003;IPR043504;IPR001314;IPR001254;IPR018114;IPR033116;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Mandibulata (clade), Pancrustacea (clade), Hexapoda (subphylum), Insecta (class), Dicondylia (clade), Pterygota (subclass), Neoptera (infraclass), Endopterygota (cohort), Diptera (order), Nematocera (suborder), Culicomorpha (infraorder), Culicoidea (superfamily), Culicidae (family), Anophelinae (subfamily), Anopheles (genus), Cellia (subgenus), Pyretophorus (clade), gambiae species complex (no rank)

CLIPC9 AGAP004719

false

352

A0A1S4H5M5

MKVLLFCIVISLTTLIASGQDIEEELRCPGGYCVSKYLCPNGTFIDDIKHAQTTQLIGLRAGLDIDDFDDCNDYLLVCCQSAPAPTATSTEKPATSDELIEPPPSTNLACGQANEGGLIYDLRNNETLSQYAEYPWVVYILALKKQEANSGDFVCGGTLIHSRLVVTTAHNTDGKTDLVARFGEWDISTTKEPFPQQDIDVAEVIKHPQYVFNPIQNDIALLVLAENVQYAAHIRPICLPQPTDEFVGQRCVSNGWGKERGVYANVMKKLTLPVIGRANCTRMLRYAGLGPFYTLREGFLCAGGEVAVDMCKGDGGSPLACQTESGTYVLAGIVSWGIGCGGFNTPGVYVAVNRYVQWLNEHIVDQALNESFDIKL

Inactive CLIP domain-containing serine protease A28 [Cleaved into: Inactive CLIP domain-containing serine protease A28 light chain; Inactive CLIP domain-containing serine protease A28 heavy chain]

Anopheles gambiae (African malaria mosquito)

7,165

376

41,034

Disulfide bond;Glycoprotein;Immunity;Innate immunity;Reference proteome;Secreted;Serine protease homolog;Signal

GO:0004252; GO:0005615; GO:0006508; GO:0010954; GO:0035008; GO:0042742; GO:0045087

Evidence at protein level

5

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31765430, ECO:0000269|PubMed:33045027}. Note=Secreted into the hemolymph. {ECO:0000269|PubMed:31765430, ECO:0000269|PubMed:33045027}.

SIGNAL 1..19; /evidence="ECO:0000255"

null

PF00089;

IPR009003;IPR043504;IPR001314;IPR001254;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Mandibulata (clade), Pancrustacea (clade), Hexapoda (subphylum), Insecta (class), Dicondylia (clade), Pterygota (subclass), Neoptera (infraclass), Endopterygota (cohort), Diptera (order), Nematocera (suborder), Culicomorpha (infraorder), Culicoidea (superfamily), Culicidae (family), Anophelinae (subfamily), Anopheles (genus), Cellia (subgenus), Pyretophorus (clade), gambiae species complex (no rank)

CLIPA28 AGAP010730

false

353

A0A1S4H5S2

MPSWWCCCCLVVLLYAQRMIVPSSAQNDGSDELQECPGGFCSPKYLCPNGTYNEANAQNQEIIMLRFGEEDVCQDYMQVCCSNATSMRYELVTNNEPVEYGCGISNPGGLIYQVEGNRTYAQYGEFPWVVAILEAFYSSNEQQFTYVGGGTLIHPRFVVTAAHIFNKTENLVASFGEWDMNRDENVYPKQNIDIDRTIIVHPEYNSVGLLNDIALAQLKQNVVYDKHIRPICLPNPTDRFDDQLCISTGWGIEALTSAYANVLKRVDLPVIARASCKKLFAETRLGPFFRLHKSVLCAGGEEGADMCDGDGGSGLACPNESGAYVLAGIVSWGLSCHQQNVPGAYVNVARFVTWINATIEGIL

Inactive CLIP domain-containing serine protease A8 [Cleaved into: Inactive CLIP domain-containing serine protease A8 light chain; Inactive CLIP domain-containing serine protease A8 heavy chain]

Anopheles gambiae (African malaria mosquito)

7,165

363

40,130

Disulfide bond;Glycoprotein;Immunity;Innate immunity;Reference proteome;Secreted;Serine protease homolog;Signal

GO:0004252; GO:0005615; GO:0006508; GO:0010954; GO:0035008; GO:0042742; GO:0045087; GO:0140546

Evidence at protein level

5

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17537726, ECO:0000269|PubMed:33045027}. Note=Secreted into the hemolymph. {ECO:0000269|PubMed:17537726, ECO:0000269|PubMed:33045027}.

SIGNAL 1..25; /evidence="ECO:0000255"

null

PF18322;PF00089;

IPR009003;IPR043504;IPR001314;IPR041515;IPR001254;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Mandibulata (clade), Pancrustacea (clade), Hexapoda (subphylum), Insecta (class), Dicondylia (clade), Pterygota (subclass), Neoptera (infraclass), Endopterygota (cohort), Diptera (order), Nematocera (suborder), Culicomorpha (infraorder), Culicoidea (superfamily), Culicidae (family), Anophelinae (subfamily), Anopheles (genus), Cellia (subgenus), Pyretophorus (clade), gambiae species complex (no rank)

CLIPA8 AGAP010731

false

354

A0A1S4HE51

MAFSLRIGIRTTDSKRCLVLLVLVVLLTVLACLPPSVEGNFPVGKFRRCNNNKGICVSREQCLNGQINTVGHTQIEPRLLNDDDIDECDVYGMQCCNLPSTNVPADSDEEEQEEEEKEKKGGTVTTTTTEEPDDPDWSRQCGQRTDVTERADQDGETNRFEFPWSVALFSKAQFFGKVRKEFLCGGTLIDDYLVLTAARCVNQKDRNTLVVQLGRWNLDAGKESRMQEIAVEELIIHRGYVLSSHLHNVALLVLANGAQLGRAANRVCLPDHSVQFGPDTLCYVVGWSNSPSPNTSNRQLKLRSMVAPVQECTATIRRSTGAWDFRLLSENICTTYLDDTVPCERAPGSGFVCESPTLPGQYFLVGIASYAVRQCHKYRAHDVFVHVPDYIEWVDGHVVNQSRQTSFYRPDPISFD

Inactive CLIP domain-containing serine protease A30 (Inactive CLIP domain-containing serine protease SPCLIP1)

Anopheles gambiae (African malaria mosquito)

7,165

416

46,590

Disulfide bond;Glycoprotein;Immunity;Innate immunity;Reference proteome;Secreted;Serine protease homolog;Signal

GO:0004252; GO:0005576; GO:0005615; GO:0006508; GO:0010954; GO:0035008; GO:0042742; GO:0048023; GO:0140367; GO:0140546

Evidence at protein level

5

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24039584, ECO:0000269|PubMed:33045027}. Note=Secreted into the hemolymph. {ECO:0000269|PubMed:24039584, ECO:0000269|PubMed:33045027}.

SIGNAL 1..39; /evidence="ECO:0000255"

null

PF18322;PF00089;

IPR009003;IPR043504;IPR041515;IPR051487;IPR001254;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Mandibulata (clade), Pancrustacea (clade), Hexapoda (subphylum), Insecta (class), Dicondylia (clade), Pterygota (subclass), Neoptera (infraclass), Endopterygota (cohort), Diptera (order), Nematocera (suborder), Culicomorpha (infraorder), Culicoidea (superfamily), Culicidae (family), Anophelinae (subfamily), Anopheles (genus), Cellia (subgenus), Pyretophorus (clade), gambiae species complex (no rank)

SPCLIP1 CLIPA30 AGAP028725

false

355

A0A1S5RW73

MSFATSLPRPTTTGAAGFGLPLATCISLSVSHSFSPKFGICNNTSLRLKSKAGSGCYEGIHRSQLAASTILEGHTPINPEVESEKIRLIERIRLMFRSMDDGEISVSPYDTAWVALVEDIGGSGGPQFPTSLEWISNNQLDDGSWGDRKFVLYDRILNTLACVVALTTWKMHPNKCEKGLRFISDNIEKLADEDEELMPVGFEIALPSLIDLAKRLCIEIPDNSASIKNIYAKRDSKLKRIPMDLMHKKPTSLLFSLEGMEGLNWDKLLDFQSEGSFLSSPSSTAYALHHTKDELCLEYLLKAVKKFNGGVPNAYPVDMFEHLWSVDRLRRLGISRYFQVEIDECLDYVYRYWTNKGICWARNMCVQDSDDSSMGFRLLRLYGYDVSIDVFKQFEEGGQFCSIPGQMTHAITGMYNLYRASQLMFPQEHILADARNFTANLLHQKRVTNSIVDKWIITKDLPGEVAYALDVPFYASLPRLEARFFLEQYGGDDDVWIGKTLYRMLYVNCNTYLELAKLDYKHCQTVHQLEWNSMQTWYRECNLGEFGLSERSLLLAYYIAASTAFEPEKSSERLAWAITTILVETIMSQELSDEQKREFVDEFVNISIINNQNGGRYKPGNRLVEVLINTVTLMAEGRGTDQQLSNAWKNWLKTWEEGGDLGEAEARLLLHTIHLSSGLDESSFSHPKYQQLLEATSKVCHQLRLFQNLKANDAQGSTSRLVTVTTFQIEAGMQELVKLIFTKTLEDLTSATKQSFFNIARSFYYTAYCPADTIDSHINKVLFEKIV

(-)-kolavenyl diphosphate synthase, chloroplastic (SdKPS) (EC 5.5.1.28) (Clerodienyl diphosphate synthase) (Kolavenyl diphosphate synthase CPS2) (SdCPS2)

Salvia divinorum (Maria pastora) (Diviner's sage)

28,513

787

89,377

Chloroplast;Isomerase;Magnesium;Metal-binding;Plastid;Transit peptide

GO:0000287; GO:0009507; GO:0009686; GO:0010333; GO:0016102; GO:0016853

Evidence at protein level

5

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.

null

PF01397;

IPR008949;IPR001906;IPR036965;IPR050148;IPR008930;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Lamiales (order), Lamiaceae (family), Nepetoideae (subfamily), Mentheae (tribe), Salviinae (subtribe), Salvia (genus), Salvia subgen. Calosphace (subgenus)

KPS CPS2

false

356

A0A1S6M251

MRVRRGLLRLPRRSLLAALFFFSLSSSLLYFVYVAPGIVNTYLFMMQAQGILIRDNMRTIGAQVYEQVVRSAYAKRNSSVNDSDYPLDLNHSETFLQTTTFLPEDFTYFANHTCPERLPSMKGPIDINMSEIGMDTIHELFSKDPAIKLGGHWKPSDCVPRWKVAILIPFRNRHEHLPVLLRHLIPMLQRQRLQFAFYVVEQVGTQPFNRAMLFNVGFQEAMKDLDWDCLVFHDVDHIPENDRNYYGCGQMPRHFATKLDKYMYLLPYNEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNRVQNAGYSVSRPEGDTGKYKSIPYHHRGEVQFLGRYALLRKSKERQGLDGLNNLNYFANITYDALYKNITVNLTPELAQVTEY

Beta-1,4-galactosyltransferase 5 (Beta-1,4-GalTase 5) (Beta4Gal-T5) (b4Gal-T5) (EC 2.4.1.-) (Beta-1,4-GalT II) (Glucosylceramide beta-1,4-galactosyltransferase) (EC 2.4.1.274) (Lactosylceramide synthase) (LacCer synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 5) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 5)

Sus scrofa (Pig)

9,823

388

45,046

Disulfide bond;Glycoprotein;Glycosyltransferase;Golgi apparatus;Lipid biosynthesis;Lipid metabolism;Manganese;Membrane;Metal-binding;Reference proteome;Signal-anchor;Sphingolipid metabolism;Transferase;Transmembrane;Transmembrane helix

GO:0003945; GO:0005794; GO:0005975; GO:0006486; GO:0008489; GO:0009101; GO:0010706; GO:0021955; GO:0022010; GO:0030311; GO:0031647; GO:0032580; GO:0040019; GO:0042551; GO:0046872; GO:0070085

Evidence at protein level

5

SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P15291}; Single-pass type II membrane protein. Golgi apparatus {ECO:0000269|PubMed:29546034}. Note=Trans cisternae of Golgi stack. {ECO:0000250|UniProtKB:P15291}.

null

TRANSMEM 15..35; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255"

PF02709;PF13733;

IPR003859;IPR027791;IPR027995;IPR029044;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Artiodactyla (order), Suina (suborder), Suidae (family), Sus (genus)

B4GALT5

false

357

A0A1S7LCW6

MKLKGTTIVALGMLVVAIMVLASMIDLPGSDMSATPAPPDTPRGAPIVGGQGQAMGLPVAMQRRRGEQRAPVPALSDANGGFVAPNVQFSEAHWQGMEALPLSIELKRKLKLPLDLEGLLIDETSLNAAVSGLLAGDVLVAINGRKVKTLKKMQKETRRVQMDRRASLTVYRKGRLLTLTLSEEKNLGLAQVETAPMILPGDIMPHPYRGPCTQCHAIGTTGHITPDPDGIVLPPGPIRAGAKMPHRDRGPCAACHAIIQ

Multi-heme protein MamP (EC 1.-.-.-) (Magnetochrome MamP) (Magnetosome-associated protein MamP)

Magnetococcus massalia (strain MO-1)

451,514

260

27,638

3D-structure;Biomineralization;Cell inner membrane;Cell membrane;Heme;Iron;Membrane;Metal-binding;Oxidoreductase;Transmembrane;Transmembrane helix

GO:0005886; GO:0016491; GO:0046872

Evidence at protein level

5

SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250|UniProtKB:Q2W8Q1}; Single-pass membrane protein {ECO:0000305|PubMed:24097349}. Note=Not seen in magnetosome membranes. {ECO:0000250|UniProtKB:Q2W8Q1}.

null

TRANSMEM 8..21; /evidence="ECO:0000305|PubMed:24097349"

PF18509;PF13180;

IPR040963;IPR001478;IPR036034;

4JJ0;4JJ3;

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Alphaproteobacteria (class), Magnetococcales (order), Magnetococcaceae (family), Magnetococcus (genus)

mamP MAGMO_0521

false

358

A0A1U8F5V2

MATEAPPPVDTTEVPPFTAAETAVKQPHKLERKWTFWFDNQSKPKQGAAWGSSLKKAYTFDTVEEFWSLYDQIFKPSKLTVNADFHLFKAGIEPKWEDPECANGGKWTVTSSRKANLETMWLETLMALVGEQFDDSEDICGVVASVRRSQDKLSLWTKTATNEAAQMGIGRKWKEIIDTEKISYSFHDDSKRERSAKSRYTV

Eukaryotic translation initiation factor isoform 4E (eIF(iso)-4E) (eIF(iso)4E) (eIF-(iso)4F 25 kDa subunit) (eIF-(iso)4F p28 subunit) (mRNA cap-binding protein)

Capsicum annuum (Capsicum pepper)

4,072

202

23,037

Cytoplasm;Disulfide bond;Initiation factor;Nucleus;Protein biosynthesis;RNA-binding;Translation regulation

GO:0003723; GO:0003743; GO:0005634; GO:0005737; GO:0006417; GO:0009615

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A445AGS0}. Nucleus {ECO:0000250|UniProtKB:A0A445AGS0}.

null

PF01652;

IPR023398;IPR001040;IPR019770;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Solanales (order), Solanaceae (family), Solanoideae (subfamily), Capsiceae (tribe), Capsicum (genus)

eIFiso4E LOC107853558

false

359

A0A1U8GR65

MATAEMEKTTTFDEAEKVKLNANEADDEVEEGEIVEETDDTTSYLSKEIATKHPLEHSWTFWFDNPVAKSKQAAWGSSLRNVYTFSTVEDFWGAYNNIHHPSKLVVGADLHCFKHKIEPKWEDPVCANGGTWKMSFSKGKSDTSWLYTLLAMIGHQFDHEDEICGAVVSVRGKGEKISLWTKNAANETAQVSIGKQWKQFLDYSDSVGFIFHDDAKRLDRNAKNRYTV

Eukaryotic translation initiation factor 4E-1 (eIF4E-1) (eIF-4F 25 kDa subunit) (eIF-4F p26 subunit) (mRNA cap-binding protein)

Capsicum annuum (Capsicum pepper)

4,072

228

25,908

Cytoplasm;Disulfide bond;Host-virus interaction;Initiation factor;Nucleus;Plant defense;Protein biosynthesis;Reference proteome;RNA-binding;Translation regulation

GO:0000340; GO:0003723; GO:0003743; GO:0005634; GO:0005737; GO:0006413; GO:0006417; GO:0016281; GO:0051607

Evidence at protein level

5

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm {ECO:0000250|UniProtKB:C6ZJZ3}.

null

PF01652;

IPR023398;IPR001040;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Solanales (order), Solanaceae (family), Solanoideae (subfamily), Capsiceae (tribe), Capsicum (genus)

eIF4E PVR1 PVR2 LOC107868427 T459_11130

false

360

A0A1U8QK63

MALEEVPSVSRDLDHSALRALSSASPSSLPSSCSRSTTSLLFQSKGIEFRLSIPDTFLSLVEPHRNAFLASYSTQGNTQSPLELALSFLYFLLDQKVSPLVLSSVLRAFNLEFLGNRSEIHSLIADLTPIPKQRQRWLGIYYRFLEASDDKRAEIPLSSIFQHARTNEFQLMAVFGGQGECSRTCLNEFAELYSSYEPMLRRLVGVIGPCLYNLSTSDEYSSYYRNQPLDLKAWITDENHVPDLGFVASAPVSVPVIGALSLARYCVTCHITGCNPGLMRSMLRTATGHSQGLLAAIVVAVSHSWDSFYQATEEVIELLFRLGWECHHAAPCSMVPAANYADVDGANGPSYMLSLRGLKRQETEATIDHVNASLPEDKRLYLALINAYDQFVVAGPVASLLRLESHLVEITSKDIDQSRIPFRDRKPYIQHSFLPVSTPFHTPYLTRAAARVKKQFAARPIPTRRLAIPVYHTHTGLDLRKQGGCALSIAIDAIASEPCNWPCAVASYHASHILTFDRGGLAPLIKRVREGCGVRVVQVADLDTRDSEMATMRDLFATKLLPTSTKLQSWGQQFRPGLASGPKIQLETRLNRVLGAPPIMVAGMTPTTVHPDFVAAIMNAGYHAELAGGGYHNASAMEAAIYDLVSSIPKERGITCNLIYANPRSISWQIELLRRLSNGNVRIDGLTIGAGVPSLTVASEYIETLGLRHISFKPGSVAAIRKVVEIAREHPDFPVILQWTGGRGGGHHSFEDFHAPIIATYGIIRQEPNVYLVAGSGFGDSDSVYPYLTGSWSVAMGHPAMPFDGILLGSRMMVAKEAHTSPAVRRIIAATPGVSDSEWEKTYSGPAGGVITVTSEMGEPIHKIATRGVCLWADLDKTVFSLSRRDRLTYLAQHRRSIIQRLNADFAKPWFGCNSDGEAVDLEDMTYLEVLKRLTALMFVPNKQWIDASYIEFTMTIAQRWLQRLQFDSEAAASLTISLLRKAPDRFLAIFADVCPTAEGDLLNPEDISFFLMQCKTPGRKPVNFIPALDDDFEFYFKKDSLWQAEDVDAVLDQDAERVCILHGPIAARYSKSDSEPAGYILDSILNGVVARLRETSTAEMLLPKLERGHTTPASWSTLSLTERDTSEETSDTSITSLSELIENHSFSSGGVDSVPRPSHPLWMRALLEDDVVLQGTLRQKNPFRDLIQSSPNTVVNYNQDSSELMVTAQEPYHISSFMRAVCHDGVMDKRNERIKSFYSLLWFGHDCDTSQSLNGVFYGPDITLTEDLLDEYNATIGPAYSDHRQMVPSTDVLPISMGIIIAWDVISRPLILRQIGGDLLRLVHRSNTFEYYSDTRLRLGDSVSSRSEVQAVYDDDGGRVVIVEAQILRSRVPVMTVTSTFLFRGSKGTTVPAFRRAREQKWTYDVTSEFEESILLSRNWFRPCDPSLTLVGKSMIFDLNSLVKYHDDGNMELHVQGTAMSQTNGQQQKLAIVDFRNTCTGNPVLDFLQRRGKLAEPRTEFKIPGWAGKSTMDIQMPPSNEPYAQLSKDFNPIHTSPIFSSLAGVPGTLCHGMCTSAIAERVLEHLGLGGDRERLRRFEARFTDMVMPLEKLVVEIKHTGMVDGRMCFSILAKRKETDERVLEGDAEVEQPRTAYLFTGQGSQSKGMGMDLYKTSTGQFLLTNKGGLFWTSCKTTQSPLPIRQKYLDITTEVVLPNGKRVQKPVFPGLTPTSTSYTFRHPRGLLYSTQFAQPAILLFEAAAFAELRAKGYVSHGAVYAGHSLGEFGALSALSRSVPTGALVELAFYRGSVMQASVASDNDGGTTYGMVAMNPKRVGTFFTQTTLDRLVSQIAAQSQELLEIVNFNIEGEQYVCSGTIDRPISGGTWPSLSG

Fatty acid synthase beta subunit pkiC (EC 2.3.1.86) [Includes: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9); [Acyl-carrier-protein] acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] malonyltransferase (EC 2.3.1.39); S-acyl fatty acid synthase thioesterase (EC 3.1.2.14) (Pki biosynthesis cluster protein C)]

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)

227,321

1,872

207,117

Hydrolase;Lyase;Multifunctional enzyme;NAD;NADP;Oxidoreductase;Reference proteome;Transferase

GO:0004312; GO:0004313; GO:0004314; GO:0004318; GO:0004321; GO:0005835; GO:0016297; GO:0019171; GO:0042759

Evidence at protein level

5

null

PF00698;PF08354;PF13452;PF22235;PF01575;PF16073;

IPR001227;IPR014043;IPR016035;IPR013785;IPR039569;IPR016452;IPR013565;IPR003965;IPR050830;IPR029069;IPR002539;IPR032088;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), Eurotiomycetes (class), Eurotiomycetidae (subclass), Eurotiales (order), Aspergillaceae (family), Aspergillus (genus), Aspergillus subgen. Nidulantes (subgenus), Emericella nidulans (species)

pkiC AN3381

false

361

A0A1U8QLG8

MSPPLDSALEPLSEYKETAFPRTEKDPSQYKEHDLVTPEKEIQTGYFSPRGSHSSHGSHDSSASSNISLDDARMSDVNNSPNVFHDDPDTIDEKLSMYWKAANETVIREPYDYIAGIPGKEIRRKLLEAFNHWYKVDEQSCQAIATTVGMAHNASLLIDDIQDSSKLRRGVPCAHEVFGIAQTINSANYVYFLAQNQLFRLRSWPQAISVFNEEMVNLHRGQGMELFWRDNLLPPSMDDYLQMIANKTGGLFRMIVRLLQTSSRQVIDVEQLVDVLGLYFQILDDYKNIREEKMAAQKGFFEDLTEGKFSFPICHAIGEGAKNRTALLHMLRLKTDDMKIKQEAVCILDNAGSLDYTREVLYGLDRKARSLLREFKTPNPFMEALLDAMLSSLQACH

Geranylgeranyl pyrophosphate synthase AN1592 (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10) (Pimaradiene biosynthesis cluster protein AN1592)

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)

227,321

397

45,185

Isoprene biosynthesis;Magnesium;Metal-binding;Reference proteome;Transferase

GO:0004161; GO:0004311; GO:0004337; GO:0008299; GO:0016114; GO:0043386; GO:0046165; GO:0046872

Evidence at transcript level

5

null

PF00348;

IPR008949;IPR000092;IPR033749;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), Eurotiomycetes (class), Eurotiomycetidae (subclass), Eurotiales (order), Aspergillaceae (family), Aspergillus (genus), Aspergillus subgen. Nidulantes (subgenus), Emericella nidulans (species)

AN1592 ANIA_01592

false

362

A0A1U8QWA2

MAIIDTTKDLSALFTQQVRASPNALALEDDKTSYTYAELDKEVEELSRRLRSYGVSRDSLVGVLLPRSAHFVIACLAALRAGGAFLVLELAYPPDLLADVLEDATPAVVVTHRSETGKIKGSVPVISLDEPPVDANGHTVEPGPLPVDDDLDRLAFVSYSSGTTGKPKGIANPHRAPVLSYNLRFGVQDLQPGDRVACNVFFIWEILRPLIRGATVVAVPDDHSYDPAALVDLLASRHITETLMTPTLLATILSRHSDIGARLPELRTLWLNGEVVTTDLARRAIRALPNTRLLNCYSACETHEIACGDIKEIVSDESQYCPVGPLLDPKHAYIVNEQGEKVEEGVSGELCVGGPMLARGYINRPETTAKAFIPDPFSNSPGAVMYRTGDRARMLPSGLLEITGRVGAMIKLRGYSVVPGKVENDIVKHLAVRQCAVVAHGEGLERQLVAYIVADQEHSEERPTVEINSSGHSPGARRALTKFLAHYMIPALWVQVDELPTHEVSGKIDLKRLPPPPTEVLANGNGKKEDPIGIEDIAAIWAVALKVPKATLKPEDNFFDLGGHSLSIADLSSRLSRKFGFRIPIVRLAENSTLSGHLDTVRAIRDGHTAAVQADLPAVLRTDATLDEEIRSDAKICSLTDAKTVLLTGVTGFLGAFLLKDLVDSTSAHIICLVRFNEPEDDDQPGGVARIRRNLLDLGLWNDSIMERVEILPGNLSRSRFGLTPDAFQELAQRVDVIVHAAASVNLVYPYAALRAANVGGTREILRLASQGGATVQYVSTNGVLPPSGEKGWPEDTMLDMKDVPTKLLDGYGQTKWVAEQLVLEAGRRGLPVRVHRIGTVSGHSQSGAANAWDLLTALIVESIKLGKYPDVEGWRAEMTPVDFVSKAIIHLANQTAVEQTVFHIGDPDPVNTRSVFEDLKTLGYPTEPLSWDDWVALWTSQRGHVKGGDGGFTVDILRSGMPSIEFLRGIVVLDNSATRPIRREVERPKVDRFLLETYTRHWFARGWLKRPPIRQRQLSPIPKGPLSGKVAVVTGASSGIGAAVATALAREGAHVALGARRLDALESLKEKLSASGVKVVTCKTDVTDRKQVEGLVKAATEELGPVDILVACAGVMYFTMMANTQMDEWERTVDVNCKGILNSLASTVPGMLARGKGHVVAISSDAGRKVFPGLGVYSASKFFVEATLQALRLETAGQGLRVTAVQPGNTATDLLGMSTDAEAIKKYGEPSGAQILDPEDVANSIIYALRQPEHVAMNEILIEPRDEPI

Glycine betaine reductase ATRR (Nonribosomal peptide synthetase-like protein ATRR) [Includes: Carboxylic acid reductase (EC 1.2.1.-); Aldehyde reductase (EC 1.1.1.-)]

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)

227,321

1,270

137,536

Multifunctional enzyme;Oxidoreductase;Phosphopantetheine;Phosphoprotein;Reference proteome;Repeat

GO:0009058; GO:0016491; GO:0031177

Evidence at protein level

5

null

PF00106;PF00501;PF07993;PF00550;

IPR036736;IPR045851;IPR020845;IPR000873;IPR042099;IPR013120;IPR036291;IPR020806;IPR009081;IPR006162;IPR002347;IPR010080;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), Eurotiomycetes (class), Eurotiomycetidae (subclass), Eurotiales (order), Aspergillaceae (family), Aspergillus (genus), Aspergillus subgen. Nidulantes (subgenus), Emericella nidulans (species)

ATRR AN5318 ANIA_05318

false

363

A0A1V0E492

MACVSDLVAFTQPLIIGAKPLEIVRRSAAFHPNVWGDYFLKLSQDEKKLESMRERAKVLKEKVLKKLSTIEGGERLELIDTLYHLGVAYNFEKEIEEALEKIYKAYDEDATQDNLCTLALRFRLLRQHGWNASSDVFNKFKETKNGNFKESVASDVLGMLSLYEASYVGTKEDKILEEAISFTTRNLSAALPNMEPLLAERVAHSLELPLHKRLQRLEARYFITMYEKNNAHDEMLLEYAKLDYNLLQALHQNEMKELTKWWTKIDLVGKMKFPRDRVTECYFWPLGAFFEPQHSRGRIFATKITQLTSIIDDLYDVYGTQEELQLFTDVIQRWDMNAKKSLPDYIKPLYEALLSTLKDFEEELSLEGNAYRASFMQQAMKNICMAYFDEAKWYNRGTTPKVEEYLNSAEISCGYPVVATACFTGAGEITTKKLLEWIQSQPKYMKDTCRLCRIVDDIKTYKFEEERGHVASVVACYMEEHKCNEDEALEKLNEDVMNTWKDINKACMRPTPFPMVVMNIIRNLSRVMEILYQFGDGYTFADTVTKERLNLLLKDPIPV

Terpene synthase 1 (PnTPS1) (Alpha-humulene synthase) (EC 4.2.3.104) (Beta-caryophyllene synthase) (PnCPS) (EC 4.2.3.57)

Piper nigrum (Black pepper)

13,216

559

64,936

Lyase;Magnesium;Metal-binding

GO:0000287; GO:0010333; GO:0010597; GO:0016102; GO:0051762; GO:0080017; GO:1901937

Evidence at protein level

5

null

PF01397;PF03936;

IPR008949;IPR034741;IPR044814;IPR001906;IPR036965;IPR050148;IPR005630;IPR008930;IPR019734;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), Magnoliidae (clade), Piperales (order), Piperaceae (family), Piper (genus)

TPS1

false

364

A0A1V0E4A6

MDAVSCAINALSAQAPPKHLGGNNVGRKSVTFPKDIWGDYFLKISPNEEKLDSWRVRAKELKEKVFDILSCAKGAEQVHIIDALYHLGVSYQFEKEIEEALKNMLTTYNDDTSTEDDLYTLALRFRLLRQNGFHASTKALNKFKDAHGSFREDLASDVMGLLSLYEASYAGTVDDLILDEALAFTKIHLKAALPHLDSHLAQRVSHSLELPLHKRIQRLEAREFISLCEKDDSIVIKELLEFAKLDYNILQALHQWELKELTKWWKKLNLVGKMTFARDRMTEIYFYVSGFFFEPQYSRGRIISSKILAICSVVDDEYDVYGTLDELQVFTDAICRLDVAAMENLPEYVKPLYEAIFFSLKEFEEELAREGNAYRVNYLREEVKNLCKSYLQETKWLHQRYIPTLEEYLLVSEISSTYTVIFNGCFVGCGEIATKEVFEWFQAFPKLLSDSARIGRIADDIMSCKFEQSRGHCPSAVECCMEEHQCTKEVALGNLDGVLGRAWKDMNKACMRPTPFPMEVLRPIVNLARMAEISYQYEDGYTFSGGKTKERISMLYKDPIPV

Terpene synthase 2 (PnTPS2) (Cadinene synthase) (PnCDS) (EC 4.2.3.-) (Cadinol synthase) (PnCO) (EC 4.2.3.-)

Piper nigrum (Black pepper)

13,216

562

64,564

Lyase;Magnesium;Metal-binding

GO:0000287; GO:0010333; GO:0010597; GO:0016102; GO:0047461; GO:0051762; GO:1901928

Evidence at protein level

5

null

PF01397;PF03936;

IPR008949;IPR034741;IPR044814;IPR001906;IPR036965;IPR050148;IPR005630;IPR008930;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), Magnoliidae (clade), Piperales (order), Piperaceae (family), Piper (genus)

TPS2

false

365

A0A1V0QSG0

MSLSGLISTTTFKEQPAIVRRSGNYKPPLWDAHFIQSLQVIYTEESYGKRINELKEDVRRILEKEAENPLVKLEQINDLSRLGISYHFEDQIKAILNLTYNNNNALWKKDNLYATALHFKLLRQYGFNPVSSEIFNAFKDEKKEFKESLSKDVKGMVCLYEASFYSFRGEPILDEARDFTTKHLKQYLMMTRQGQNVDHDDDNDLMVKLVEHALELPVHWRMKRLEARWFIDMYAEMSHHHHMNSTFLQLAKLDFNVVQSTYQEDLKHVVRWWKTTSLGERLPFARDRIVEIFLWSVGLKFEPQFRYCRKMLTKIGQLVTTMDDIFDVYGTLDELSLFQHALGRWDINTIDQLPDYMKIFFLATYNVVNEMAYDVLKQNGILIIKYLKKTWTDLCKCYMLEANWYHSGYTPSLEEYIKNGWISIAEPLILVNLYCLITNPIKEDDIDCLLQYPTFIRISGIIARLVDDLGTSSDELKRGDNPKSIQCYMKENGICDEKNGREHIRNLISETWKEMNEARVGESPFSQAFIETAIDFVRTAMMIYQKEQDGVGTNIDHYTKDGIISLFFTSIPI

Myrcene synthase TPS5FN (EC 4.2.3.15) ((+)-alpha-pinene synthase TPS5FN) (EC 4.2.3.121) ((-)-limonene synthase TPS5FN) ((-)-(4S)-limonene synthase) (EC 4.2.3.16) (Camphene synthase TPS5FN) (EC 4.2.3.-) (Sabinene synthase TPS5FN) (EC 4.2.3.-) (Terpene synthase 5FN) (CsTPS5FN) (Terpinolene synthase TPS1) (EC 4.2.3.113)

Cannabis sativa (Hemp) (Marijuana)

3,483

573

67,232

Lyase;Magnesium;Metal-binding;Reference proteome

GO:0000287; GO:0010333; GO:0016102

Evidence at protein level

5

null

PF01397;PF03936;

IPR008949;IPR034741;IPR044814;IPR001906;IPR036965;IPR050148;IPR005630;IPR008930;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), rosids (clade), fabids (clade), Rosales (order), Cannabaceae (family), Cannabis (genus)

TPS5FN F8388_001483 G4B88_022052

false

366

A0A1V0QSH2

MCSLAKSPSSDTSTIVRRSANYDPPIWSFDFIQSLPCKYKGEPYTSRSNKLKEEVKKMLVGMENSLVQLELIDTLQRLGISYHFENEIISILKKYFTNISTNKNPKYDLYATALEFRLLREYGYAVPQEIFNDFKDETGKFKASIKNDDIKGVLALYEASFYVKNGENILEEARVFTTEYLKRYVMMIDQNMILNDNMAILVRHALEMPLHWRTIRAEAKWFIEEYEKTQDKNGTLLEFAKLDFNMLQSIFQEDLKHVSRWWEHSKLGKNKMVYARDRLVEAFLWQVGIRFEPQFSHFRRISARIYALITIIDDIYDVYGTLEELELFTKAVERWDVKTVDELPDYMKLPFFTLFNTVNEMAYDVLEEHNFVSVEYLKNSWAELCRCYLEEAKWFYSGYKPTLKKYIENASLSIGGQVIFVYAFFSLTKSITNEALESLQEGHYAACRQGSLMLRLADDLGTSSDELKRGDILKSVQCYMHETGVSEDEAREHIKFLISEIWKEMNDEDEYNSIFSKEFVQACKNLGRMSLFMYQHGDGHASQDSHSRKRISDLIINPIPL

(+)-alpha-pinene synthase TPS2FN (EC 4.2.3.121) ((-)-limonene synthase TPS2FN) ((-)-(4S)-limonene synthase) (EC 4.2.3.16) (Camphene synthase TPS2FN) (EC 4.2.3.-) (Isoterpinolene synthase TPS2FN) (EC 4.2.3.-) (Sabinene synthase TPS2FN) (EC 4.2.3.-) (Terpene synthase TPS2FN) (CsTPS2FN) (beta-phellandrene synthase TPS2FN) (EC 4.2.3.-)

Cannabis sativa (Hemp) (Marijuana)

3,483

561

65,771

Lyase;Magnesium;Metal-binding

GO:0000287; GO:0010333; GO:0016102

Evidence at protein level

5

null

PF01397;PF03936;

IPR008949;IPR034741;IPR044814;IPR001906;IPR036965;IPR050148;IPR005630;IPR008930;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), rosids (clade), fabids (clade), Rosales (order), Cannabaceae (family), Cannabis (genus)

TPS2FN

false

367

A0A1W2P872

MEPEAPDSRKRPLETPPEVVCTKRSNTGEEGEYFLKVLIPSYAAGSIIGKGGQTIVQLQKETGATIKLSKSKDFYPGTTERVCLVQGTAEALNAVHSFIAEKVREIPQAMTKPEVVNILQPQTTMNPDRAKQAKLIVPNSTAGLIIGKGGATVKAVMEQSGAWVQLSQKPEGINLQERVVTVSGEPEQVHKAVSAIVQKVQEDPQSSSCLNISYANVAGPVANSNPTGSPYASPADVLPAAAAASAAAASGLLGPAGLAGVGAFPAALPAFSGTDLLAISTALNTLASYGYNTNSLSLGLNSAAASGVLAAVAAGANPAAAAAANLLASYAGDAGAGPGAGAAPPPPPPPGALGSFALAAAANGYLGAGAGGAAGAGGAPLVAAAAAAGAAGGFLTAEKLAAESAKELVEIAVPENLVGAILGKGGKTLVEYQELTGARIQISKKGEFLPGTRNRRVTITGSPAATQAAQYLISQRVTYEQGVRASNPQKVG

RNA-binding protein Nova-2

Mus musculus (Mouse)

10,090

492

49,067

Alternative splicing;Isopeptide bond;mRNA processing;mRNA splicing;Neurogenesis;Nucleus;Reference proteome;Repeat;RNA-binding;Ubl conjugation

GO:0000381; GO:0003723; GO:0003729; GO:0005634; GO:0006397; GO:0008380; GO:0021954; GO:0030182; GO:0051252; GO:0120163; GO:1902667; GO:1990825

Evidence at protein level

5

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30638744}.

null

PF00013;

IPR047275;IPR047276;IPR047274;IPR004087;IPR004088;IPR036612;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Glires (clade), Rodentia (order), Myomorpha (suborder), Muroidea (clade), Muridae (family), Murinae (subfamily), Mus (genus), Mus (subgenus)

Nova2

false

368

A0A1W5T1U1

MAPSQAPREPIAIVGSGCRFPGESSSPSKLWELLQAPRDVQTEIPPTRFNPHGFYHPDNLHHGTSNVRHSYLLTEDHRHFDAQFFGIKPAEAHCIDPQQRLLMETVYESLESAGLRLEDLRGSETAVYVGLMCGDYADIVLRDPESFPMYLSTGTARSIMSNRISYFFDWHGPSMTIDTACSSSLVAVHEAVQTLRLGRSRVAVAAGSNLCLSPEPYIAESKLQMLSPTGRSRMWDIQADGYARGDGVAAVVLKTLSAALADGDHIECLIRETSVNQDGRTRGITMPSSEAQTRLIQDTYARAGLDPLKPQERCQYFEAHGTGTPTGDPLEAAAIRQAFFPGDNNQDRGCLFVGSIKTVVGHTEGTAGLAGVLKASLALRNGIIPPNLLFNQLNPKIKPFYTNLEIATAAKPWPVLPAGVPRRASVNSFGFGGTNAHAIIEAYEPALTAPSKSTEPDIAFIPFVFSAASESALRRMLELYAQHLSKNPTINARDLGWTLQARRSRFPFSIAVPGATTDQLRSNLETRLNSTDARQPLKIVKQESRPENPRILGVFTGQGAQWATMGRALYQSPKVRQIIQELDASLQALPVGERPSWTLASELTADASVSRIKAAEISQPMCTAVQVVLVQLLQSAGVVFDAVVGHSSGEIAAAYAAGFLSGTDAIRIAYYRGLCARLAQGAHGEKGAMMAVGTGVEDALELCAEPEFRGRMSVAAVNSSASVTLSGDADAITQAKEILDEEKKFARVLVVDKAYHSHHMQACSGRYLSCLAKARIAVSAPTDTKCVWYSTVRQGPVTEADLADLTGPYWNDNMVSPVLFAQAVETALAARGPFNMAVEVGPHPALRGPAQQTVQDVLETSLPYTPTLQRGMNDVEAMAECLGLLWQGLAPGFVDLSSYDAFLSQGAVSRVIKDLPRYSWDHDRVFWYESRVSRATRQRIAASHPILGTRCPDGVEQEFRWRNFLSLKELPWLTGHRIQGQIIFPGAGYISAAVDSARAMSSNESIQLVELQELLIRQAIVFEDENASVEILVSITDVTHHSKDMVRAQFSFYSAVGKESTQMTLNASGRLVITYGPVRKDALPVQRPSLVDMVDVPSERFYNALDPLGYSYTGRFRALKSMQRKLGIATGLVTRQEAADLSSVTLDPAMLDAAIQAVLLAKSFPGDGELWCSQVPKVIHRIAVNPTLCDPSGNGVESTFPLDAVLTMMKASDTQGDVDVYSADGQYTMIRMEGIHAVPLEATNADRDRPFFSGVVWGPAAPDSQTVNFDATATPEEYELAYVLERVATFYLRKIHLAFPMDHSARHEGPYVGLLNYATYVTQQVASGYHRYTQPHWARDTVAVIKSESQRFPNNIDLAVMHIIGEHMVDVISTRATILEHLTKDNLLSRYYEQAMGIGHFSDYLASVVEQIVHRYPQMKVLEIGAGTGMATKKVIQRVGHSFGSYTFTDISSGFFENAREIFASHQDQMVYKVLDAEKDPVAQGFGEQSYDLIVASFVLHATSHLETTLHNLRRLLKPGGYVVMLEVTNLEQSRLGYIFGSLPGWWLGANDGRILSPCVPTEEWDRLLKLTGFSGVDTFTSDADALPYPASAIVSQAVDETVDFLRNPLGTPSDFVNRATPVVLIGGASSSVRVIRDVVKRHLDTRFDQVQVVDRLSDFVAISPAVSNGLLTLNLSDLEEPVFQNMTADSLAALKLLYERSNYVLWVTEDARAGNPHQNQSLGFGRSMMVEMPHVQSQFLDLDRITETSSVASRIVDAALRFVGVNMPDRGGDVASAGLLWSTEPEIAVIGGRELLPRIKLNRSQNLRYNASRRAIAEDVDMDQKSVQLVRNGNAYVLEQGSTSGFGNQTPGYTRIRVDVSSLKSLHLGRGNALYLVAGTVLATGEKVIGFADKNSSIVDIPPSWMSHRPDISMAALILSIIARLFSRAILSSISPGGVLVVAEPDELLAPVLEWQASQQKIRVVFVTTQEDAPERPNWVVLHSQVHVRSLPKLAPTEPVTILDLSTGEEPSALALKLRNSLHPASAFERLTYWFSDHARRGEIHIPAEAMLTMYRPPMSPPASDSVIASHSFPVTDVSQIPAARCPLAVVDWQSTSHVPALIRPVDHYPMLKSNKTYWLVGLTGSLGLSLCAWMIHQGAQNVVLTSRNPKIDQIILQELRSLGARVEVYAGDVTNQESLRGVYDRICQTLPPVAGVGQGAMVLIDTMIKDMEIDAMQSVLQPKVKGSINLDELFSAERPLDFFIFFSSATCVTGNIGQSNYAAANMFMTGLAANRNRRGLAGSVMNIGAIMGVGYVTRETSEALQRNLLKSGHVWMSEQDFHTIFAEAILAGTPGSDANVEITCGLRITNASEEQRPLWSFNPRFQHLVVMEEQVEETYEQDKKGMSLKLQLREARTTDEIYEVIKECFIVKLQIMLGLDDAATNSITSKAADDLGIDSLNTVEIRSWFLKEMKVDIPVLRILGGATIGEIIKFVLEKLPSDMTPSLGLSPPTGAASKATSQPNPKPKVVVERRNVPRLEKKIVHSAGSRTSSSVTGTSKSVSPARSMDTASSQTSEAASPSIHTEEITKPLKPLAPLLKADVVSSNLGKVITPVEQTAALSVRKEPLSFGQSRFWFLKLYLEDQTTFNITCLLRMTGPLSVDSLSRAVTAVGQRHEALRTCFTVEDGQSPVQTILPESTLKLERQEYRTMADVNTATKKLTQHVYEMESGRLMRVILLSSAPNSSVHYVLVGYHHINMDGVSLEVFLHDLEKAYRGQPLSSDLLQYPDYAAKQRQERNQGAWQDDLTFWKNEMVGSNLEIPLLPLASVAIRKPLTQYRHHRVEQRLDARLGAQIRQLCQSIKATPSHFYLATFTTLLARLTRTREIWVGMADANRIQAETADSIGNYLNLLALRMQYDPDQPFVASVQAARKKSYGALAHSRIPFDVLLSELQVPRSSTHSPLFQVFMDYRHDVREKRMFGDCQLEGVEYEMGRTAYDIALDVVDTADDGPLIIMGLQESLYSPDTAQMLLNSFLEMVRAFAQDSKQPGGHVSLFSASDLEKALALGNGSVVASQWPATLSHRIDDMAKQYPQKLALNDGDNLRLTFQQMSQRADSIASALLSANVSRQQRVAVFQHPSSDCICSILAILRIGATYVPLDLRLELARLRSIVQDCEPTVFLVDSHTQSQAPDLMLTRPAMTINIADLPRIAPFPVMNRAAAEDEAVILYTSGSTGNPKGVPLTHENLRVNIEGNQAEFQFGPDDCLLQQIAFSFDFSVWQIFMALANGASLFIAPSTHRGDPVALMDLVVREDITITGATPSEYRSWFQHGDLARLKTSQWKTAVSAGEAMTTNMIRDFQALNKSDLRLVNGYGPTEASMSSNKLVVPYLTNKDHPEEWMEKGAVVAGYTAPNYSIYIVDEAMNLLPIGLPGQILIGGPGIASGYLNNKELSCIRFINDKYASPEQRACGWRWAHLTGDRGRIGADGRLRIEGRIEGDTQVKLRGYRIDLQDVEAAMLKASPGAFKDLVVSLHQATQALVAHVVFSQHYPAHKHSQALEIKSLELPRYMWPARTVSIDQMPVTVHGKLDRKALQTMDLPAIEPMKQTSTAHLNEAQAQMVQLWEEVISKDILAAHHIVAESDFFAVGGTSMLLVDLQRQIKSWFKMEIALAELFSANTLEKMALLIKPQEDIATPAAVDAAPPSSPSPLALTASLPPAPTTINWSEEVQLPRVLREQTSSGTTVSVPEKTSGLRLVLTGATGFIGQALLQQLTANPAISTVHCIAVRDPSAIPAHEKILVHAGDLTHAALGLAPVEAQAIFREVDAVIHNGADVSFMKSYHSLRRTNVESTIALIQNSLSRQIPFHYISSSGIANLAGTTTFAEVSAASFIPPTDGSQGYLATKWVSERLLEEAHREFGLPVYIHRPSSVTGSNAPPLDLMDNLMTYARRLKAVPMPERSSWKGYLDFVPVEQVVRDVTGDVLSAAGTVPSARASKVHYIHHLGRQVSLTGLHRYLERETGAVYRVLKMGEWLEEATQVGMDALLRTYLESMDKEDVKVVFPRLVAGKRHASTVGVAKGVKIGESWLEKGKTLLFSW

Hybrid PKS-NRPS synthetase poxE (PKS-NRPS) (EC 2.3.1.-) (EC 6.3.2.-) (Oxaleimides biosynthesis cluster protein E)

Penicillium oxalicum

69,781

4,080

447,924

Ligase;Methyltransferase;Multifunctional enzyme;Oxidoreductase;Phosphopantetheine;Phosphoprotein;Repeat;Transferase

GO:0004312; GO:0004315; GO:0006633; GO:0008168; GO:0009403; GO:0016491; GO:0016874; GO:0030639; GO:0031177; GO:0032259; GO:1901336

Evidence at transcript level

5

null

PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765;

IPR001227;IPR036736;IPR014043;IPR016035;IPR045851;IPR020845;IPR000873;IPR042099;IPR023213;IPR001242;IPR013120;IPR018201;IPR014031;IPR014030;IPR016036;IPR013217;IPR036291;IPR032821;IPR020841;IPR042104;IPR020807;IPR049551;IPR049552;IPR013968;IPR049900;IPR050091;IPR020806;IPR009081;IPR006162;IPR029063;IPR016039;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), Eurotiomycetes (class), Eurotiomycetidae (subclass), Eurotiales (order), Aspergillaceae (family), Penicillium (genus)

poxE

false

369

A0A1W6QDI7

MSLAFNLRVIPFSGHTIQSRRGLFPVHESPMITTKPFAAVKCSLTTSTDLMGKIKEKFNGKVHTSLPAITTHSADTPSNLCIIDTLQRLGVDRYFQSEIDSILDDTYRLWQLKKEDIFSDITTHAMAFRLLRVKGYQVSSEELAPYADQEHVNLQEIDVPTVIELYRAAQERVTEEDSTLKKLYVWTSTFLKQQLLTDAIPDKKLHEQVDYYLKNYHGILDRMGVRRSLDLYDVGHYKTLKAADGFSNLCNEDFLAFARQDFNISQAQHQKELQQLQRWYSDCRLDTLKFGRDVVRVSNFLTSAMSGDPELSDVRLAFAKHIVLVTRIDDFFDHGGSKEESYKILELVKEWKEKPAGEYGSEEVEILFTAVYNTVNELAEMAHIEQGRSVKDLLIKLWVEILSMFKIELDTWSDDTALTLDEYLSSSWVSIGCRICILISMQFLGVKLTDEMLLSEECTDLCRHVSMVDRLLNDVQTFEKERKENTGNSVSLLLAAHKDERAINEEEAITKAKDLAEYNRRKLMQIVYKTGTIFPRKCKDMFLKVCRIGCYLYSSGDEFTTPQQMMEDMKSLVYEPLTIHPPEANNVVGKKTELCQQLVKPYVCHTFCKKYTVSRPSNVMMTCYID

Miltiradiene synthase KSL1, chloroplastic (EC 4.2.3.131) (Kaurene synthase 1) (IrKSL1) (Terpene synthase 4) (IrTPS4)

Isodon rubescens (Rabdosia rubescens)

587,669

626

72,049

Alternative splicing;Chloroplast;Lyase;Magnesium;Metal-binding;Plastid;Transit peptide

GO:0000287; GO:0009507; GO:0009686; GO:0010333; GO:0016114; GO:0062205; GO:1901946

Evidence at protein level

5

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.

null

PF01397;PF03936;

IPR008949;IPR001906;IPR036965;IPR050148;IPR005630;IPR008930;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Lamiales (order), Lamiaceae (family), Nepetoideae (subfamily), Ocimeae (tribe), Isodoninae (subtribe), Isodon (genus)

KSL1 TPS4

false

370

A0A1W7HCY1

MSGHSFFEHLFEHSQHVTPYLHGAIKPRPERCAEHGFIHIEHASSDHIRALYESLKLAHPEAGAAYWLTRTWTLLCWQPLYVAFIAIYSCQGLPKLSSMGQHVQPRFVSGYQFDDDEYRQGSEQELIAHAGKELCALFDYFRQEMSLWTRIRPGFTQHLFADGVFGCLVKLSQFYPTLSGDYFLEQARLWLAACQLPEKLIQSLRYDETSRQLSLVRTSCCLVYKCQGRELCRDCPRHPDNKRE

Ferric aerobactin reductase IutB (EC 1.16.1.10) (Ferric chelate reductase) (FCR) (Ferric reductase)

Vibrio vulnificus

672

244

28,349

2Fe-2S;Cytoplasm;Iron;Iron-sulfur;Metal-binding;NAD;NADP;Oxidoreductase

GO:0005737; GO:0010106; GO:0046872; GO:0051537; GO:0052851; GO:0140618

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28150143}.

null

PF11575;

IPR023998;IPR024726;

null

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Vibrionales (order), Vibrionaceae (family), Vibrio (genus)

iutB

false

371

A0A1Y3DYH2

MNILQEPIDFLKKDELKNIDLSQMDKKERYKIWKRIPKCELHCHLDLCFSADFFLSCVRKYNLQPNLSDEEVLDYYLFAKGGKSLGEFVEKAIRVADIFQDYEMIEDLAKHAVFNKYKEGVVLMEFRYSPTFVAFKHNLDIELIHQAIVKGIKEVVELLDHKIDVTLLCIGDTGHRAADIKASADFCLKHKADFVGFDHGGHEVDLKPYKEIFDYVKEGGMHLTVHAGEDVTLPNLNTLYSAIQVLKVERIGHGIRVSESQELIDMVKENNILLEVCPISNVLLKNAKSFDTHPIRKLYDAGVKVSVSSDDPGMFLTNINDDYEKLYTHLHFTLEDFMKMNEWALEKSFIGCDIKEKIKKLYF

Adenosine deaminase (EC 3.5.4.4) (S-methyl-5'-thioadenosine deaminase) (EC 3.5.4.31)

Plasmodium knowlesi

5,850

363

41,906

Hydrolase;Metal-binding;Purine salvage;Zinc

GO:0004000; GO:0005829; GO:0006154; GO:0006166; GO:0009168; GO:0009897; GO:0043103; GO:0046103; GO:0046872; GO:0060169; GO:0090614

Evidence at protein level

5

null

PF00962;

IPR006650;IPR001365;IPR006330;IPR032466;

null

cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Aconoidasida (class), Haemosporida (order), Plasmodiidae (family), Plasmodium (genus), Plasmodium (Plasmodium) (subgenus)

ADA PKNOH_S03329100

false

372

A0A1Z2R986

MKSICCVLVLCLLLCRRSTASESICELKDVSGNSNDWIVLREKPLGCWTDFQTENGTEVHIINLEDNPSVFTVNLLKANKSVVIFTSSSAQSSHAMLFDNPAVSIYVTNKTSLTFIHPTQKPLQILTAPPAGNVSAVLRWAAETFGGVTSVTNARNPKTITFTGVKGSQNSSRCELMPETPTEKPFIHLELNEPIEALKSCYMKHEGEKLHIINIPDGVTIRHVSVHLLSDCNVVLRGPAGTHWIIKNSLRIGILSNNQIHLQSFPLRPRMAISDNPTDIRQKALSYFSSGFISSYSEIRLNVTNVELWITDYSISSAPTEVEKTTPSPTSPPFPVQMQLFSSPDFTTPIDNNSRVLSDKRVYAEISSQTFREASIRVSSCWVRSTPVTREMPFREEPCFIKDCPKRLSFSFQILQDLPAGSWDLECAVKLCGVKRINNEESCTSETPVKRNVQVKPFTPTTNSCFEFGLSAVLGIAFGGFLIGVLLTGALWFIKIRTGHPVALGMRSTAAELSVLSISGCPCGLTKRQPVPTHPSPSENSSANASIGSTQSTPTSSMA

Endoglin

Danio rerio (Zebrafish) (Brachydanio rerio)

7,955

559

61,300

Angiogenesis;Cell membrane;Disulfide bond;Glycoprotein;Membrane;Reference proteome;Signal;Transmembrane;Transmembrane helix

GO:0001525; GO:0001568; GO:0001837; GO:0001886; GO:0005024; GO:0005114; GO:0005539; GO:0005886; GO:0007179; GO:0007507; GO:0016477; GO:0017015; GO:0048514; GO:0071260

Evidence at transcript level

5

SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17813}; Single-pass type I membrane protein {ECO:0000255}.

SIGNAL 1..20; /evidence="ECO:0000255"

TRANSMEM 474..494; /note="Helical"; /evidence="ECO:0000255"

null

IPR042235;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Actinopterygii (superclass), Actinopteri (class), Neopterygii (subclass), Teleostei (infraclass), Osteoglossocephalai (clade), Clupeocephala (no rank), Otomorpha (cohort), Ostariophysi (subcohort), Otophysi (clade), Cypriniphysae (superorder), Cypriniformes (order), Cyprinoidei (suborder), Danionidae (family), Danioninae (subfamily), Danio (genus)

eng

false

373

A0A218NGS0

MDLLQILLAIAGLLAILLLQKQWRTKTSPGAKAGRKLPPEPAGAWPVIGHLHKLGGPNPIYRNLAEWSDKYGPVMTLKLGMQNAVVVSDREAIKECFTTNDKALADRPPSSIGLHLGFNYAAIGAAPYGPYWRDMRKLVLLEVLSSRRLEMLRNVRISEIGTSIKELYSNIIRSSGGSGPAKVVISHWIEQLTLNYILRTIAGRRFSDDSSKDAQYVKGVINDFMYFAGQFVVSDVIPIPLLRWLDPQGHLKGMKRVAKEVDTMCEAWIQEHVQRRMREKPGPGQEQDFIDVLLNNRDVMRKAQEEIDNHVGKERWVDETDLKHLVYLQAIVKEGLRLYPPGPLGAPHRAIEDCQVGGYFIPKGTQLLVNVWKLHRDPRVWSEPEKFMPERFLTRQAEVDVFGHHFELLPFGSGRRACPGITFAVQVMHLTVARLLQGFDMTTPSNLPVDMTEGPGVTMPKAHPVEVLMMPRLPSALYEP

Vinorine hydroxylase (RsVH) (EC 1.14.14.104) (Cytochrome P450 5437) (RsCYP5437) (Cytochrome P450 82S18) (Perakine synthase) (Vomilenine isomerase)

Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum)

4,060

480

54,063

Alkaloid metabolism;Heme;Iron;Isomerase;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Transmembrane;Transmembrane helix

GO:0004497; GO:0005506; GO:0016020; GO:0016853; GO:0020037; GO:0035835; GO:0050596

Evidence at protein level

5

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.

null

TRANSMEM 3..23; /note="Helical"; /evidence="ECO:0000255"

PF00067;

IPR001128;IPR017972;IPR002401;IPR036396;IPR050651;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Gentianales (order), Apocynaceae (family), Rauvolfioideae (subfamily), Vinceae (tribe), Rauvolfiinae (subtribe), Rauvolfia (genus)

VH CYP5437 CYP82S18

false

374

A0A248QE08

MASITSRASARASCSQANTRAGRVALSGGALLRPARPARSFVPARKQQQGAVRRGGALSARASAVEDIRKVLSDSSSPVAGQKYDYILVGGGTAACVLANRLSADGSKRVLVLEAGPDNTSRDVKIPAAITRLFRSPLDWNLFSELQEQLAERQIYMARGRLLGGSSATNATLYHRGAAGDYDAWGVEGWSSEDVLSWFVQAETNADFGPGAYHGSGGPMRVENPRYTNKQLHTAFFKAAEEVGLTPNSDFNDWSHDHAGYGTFQVMQDKGTRADMYRQYLKPVLGRRNLQVLTGAAVTKVNIDQAAGKAQALGVEFSTDGPTGERLSAELAPGGEVIMCAGAVHTPFLLKHSGVGPSAELKEFGIPVVSNLAGVGQNLQDQPACLTAAPVKEKYDGIAISDHIYNEKGQIRKRAIASYLLGGRGGLTSTGCDRGAFVRTAGQALPDLQVRFVPGMALDPDGVSTYVRFAKFQSQGLKWPSGITMQLIACRPQSTGSVGLKSADPFAPPKLSPGYLTDKDGADLATLRKGIHWARDVARSSALSEYLDGELFPGSGVVSDDQIDEYIRRSIHSSNAITGTCKMGNAGDSSSVVDNQLRVHGVEGLRVVDASVVPKIPGGQTGAPVVMIAERAAALLTGKATIGASAAAPATVAA

Fatty acid photodecarboxylase, chloroplastic (CvFAP) (EC 4.1.1.106)

Chlorella variabilis (Green alga)

554,065

654

68,824

3D-structure;Chloroplast;FAD;Flavoprotein;Lyase;Plastid;Reference proteome;Transit peptide

GO:0008812; GO:0009507; GO:0016020; GO:0016829; GO:0019285; GO:0050660

Evidence at protein level

5

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.

null

PF05199;PF00732;

IPR036188;IPR012132;IPR000172;IPR007867;

5NCC;6YRU;6YRV;6YRX;6YRZ;6YS1;6YS2;6ZH7;7AV4;7R33;7R34;7R35;7R36;

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Chlorophyta (phylum), core chlorophytes (clade), Trebouxiophyceae (class), Chlorellales (order), Chlorellaceae (family), Chlorella clade (clade), Chlorella (genus)

FAP CHLNCDRAFT_28598

false

375

A0A250YGJ5

MSVNYAAGLSPYADKGKCGLPEIFDPPEELERKVWELARLVRQSSNVVFHTGAGISTASGIPDFRGPHGVWTMEERGLAPKFDTTFENARPTQTHMALVQLERVGLLHFVVSQNVDGLHVRSGFPRDKLAELHGNMFVEECAKCKTQYVRDTVVGTMGLKTTGRLCTVAKARGLRACRGELRDTILDWEDALPDRDLALADEASRNADLSITLGTSLQIRPSGNLPLATKRRGGKLVIVNLQPTKHDRHADLRIHGYVDDVMTQLMKHLGLEIPAWDGPRVLEKALPPLPRPPTPKLEPTDKSLAQLNGSVPADSKPEPCTWHNGSQPASPKREQPDSPAPRRPPKRVKAEVTPS

NAD-dependent protein deacylase sirtuin-6 (EC 2.3.1.-) (NAD-dependent protein deacetylase sirtuin-6) (EC 2.3.1.286) (Protein mono-ADP-ribosyltransferase sirtuin-6) (EC 2.4.2.-)

Castor canadensis (American beaver)

51,338

355

39,068

Acetylation;Acyltransferase;Chromatin regulator;Chromosome;Developmental protein;DNA damage;DNA repair;DNA-binding;Endoplasmic reticulum;Glycosyltransferase;Hydrolase;Isopeptide bond;Metal-binding;NAD;Nucleotidyltransferase;Nucleus;Phosphoprotein;Reference proteome;RNA-binding;Telomere;Transferase;Tumor suppressor;Ubl conjugation;Zinc

GO:0000122; GO:0000781; GO:0000785; GO:0003684; GO:0003714; GO:0003723; GO:0005634; GO:0005783; GO:0006302; GO:0008340; GO:0010526; GO:0010569; GO:0016779; GO:0016787; GO:0019216; GO:0031490; GO:0031491; GO:0031508; GO:0031648; GO:0032024; GO:0032922; GO:0034244; GO:0034979; GO:0042181; GO:0042308; GO:0042752; GO:0042803; GO:0045600; GO:0045721; GO:0045820; GO:0046827; GO:0046872; GO:0046969; GO:0050994; GO:0051697; GO:0055007; GO:0070403; GO:0097372; GO:0106274; GO:0120162; GO:0120187; GO:0140612; GO:0140765; GO:0140773; GO:0140774; GO:1904841; GO:2000738; GO:2000781

Evidence at protein level

5

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P59941}. Chromosome {ECO:0000250|UniProtKB:Q8N6T7}. Chromosome, telomere {ECO:0000250|UniProtKB:Q8N6T7}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P59941}. Note=Predominantly nuclear. Associated with pericentric heterochromatin and telomeric heterochromatin regions. Localizes to DNA damage sites: directly recognizes and binds double-strand breaks (DSBs) sites via a tunnel-like structure that has high affinity for DSBs (By similarity). A fraction localizes to the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P59941, ECO:0000250|UniProtKB:Q8N6T7}.

null

PF02146;

IPR029035;IPR050134;IPR003000;IPR026590;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Glires (clade), Rodentia (order), Castorimorpha (suborder), Castoridae (family), Castor (genus)

SIRT6

false

376

A0A261GRE4

MKTRQNVYELKDDTLSWYSRAVEEMKSRDINDPTSWWYQGAIHGYATYPSALTYWHDATGYPPSQQTVNSGFWNRCQHGTWYFLPWHRMYLFYFEEIVAKAIRDMGGPADWTLPYWNYCEAYNTSASPSNQQQALQIPPEFGSSQGPNADFASLWIKNRRNYVLNKNNVNPWPAMNEAEFTNSGGDISFGGGVTGFAHSGGQTGQLESLPHNVVHTDINGAMGNPDTAALDPIFWLHHANIDRLWQVWLAQAGRSNPVVNAWKDFRFKFHDANGQPVEIAVKDVETTQLLGYVYTPAFPLSSTTPARRSVPAMDVVGATSASFSVGDHMAPLDLTMVPQPARGARLLAARGGDEKRTILRISNVKGKGATSPIDLFITNRDNEEGNEENFVGCIGLFGLENASTPSVESDGSGLNFAIDISDTINKLRQRDDWDEDNIRVQLIPQSKQDSDVEINVGRVSLHSEID

Tyrosinase HcTyr1 (EC 1.14.18.1)

Hahella sp. (strain CCB-MM4)

1,926,491

466

51,989

3D-structure;Copper;Metal-binding;Oxidoreductase;Reference proteome

GO:0004097; GO:0046872

Evidence at protein level

5

null

PF25271;PF12142;PF00264;

IPR008922;IPR057190;IPR022739;IPR050316;IPR002227;

8B74;

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Oceanospirillales (order), Hahellaceae (family), Hahella (genus), unclassified Hahella (no rank)

BTA51_09820

false

377

A0A286R227

MGVRHSASKDYIAGRPLVPGEAPLDKKNSNFSSWKPVTEIDDRDAKCADNWVPRHPDLIRLTGKHPFNSEPPHADVMKEGWLTPVSMHFVRNHGAVPRLEWGSHRITITGLVERPMEITMDDIAKLPAVTVPCLLTCCGNRRKEVNMVKNSQGFSWGPGAVSVNNWTGARLSDVLKLVGVKSQAQGAKYVHFCGPKGELPKGVDGSYGTALTLGHALDPSMDVLIAYKQNGQFLHPDHGFPCRMLIPGWIGGRSVKWLSHLHVSDKDSQNWYHFHDNKVLPPHVDAESAAKQGWWKDPSFILKELNINSTISSPGHDERILMDQNRRYTMKGYAYSGGGRKIVRVEVSFNGGETWSHPAKIIVTETPNQAGKHWTWVHWELPVDTSQFFTATEVVCRAWDESQNTQPAVLTWTLLGQGNNSMFRLRLHKEVDPQGRLCIRFQQPAPILPGPLGNVGWREQEAGSAVPSAPAAVAAAAPGLDSTKKYVTKAMLEQHVEEASVWFAYKGKVYDGTKFLDDHPGGADSILMAGGEDATEDFDAVHSDSAKKQLEQFYIAELAPEGVPVPANLLYGGVDAAVVVMPGTAAAPLPAIDVDAPFLNPKKQKAAELKEKIKISHDVTLFRFGLEHDEQLLGLPTGKHMLIRKKVTNAEGDEEVVMRAYTPTTANETRGHFDLVVKIYKANVHPKFPEGGKFSQILEALEVGDTVEVKGPIGHFHYDRPGHYKNHKLESEVKRINMIAGGTGLTPMYQVMKAILSNPSDLTEIRLLYANQTEADILLRPELEALAKSHPDRVKIHYTVDRPTPGWKYSSGFIDLDMCERALFRYEPGTISVLCGPPPMLKFACHPNLEKMGFEKGVTSIEF

Nitrate reductase [NADH] (NR) (EC 1.7.1.1)

Ulva prolifera (Green seaweed) (Enteromorpha prolifera)

3,117

863

95,563

3D-structure;FAD;Flavoprotein;Heme;Iron;Metal-binding;Molybdenum;Nitrate assimilation;Oxidoreductase

GO:0006790; GO:0008482; GO:0008940; GO:0009703; GO:0020037; GO:0030151; GO:0042126; GO:0042128; GO:0043546; GO:0071250; GO:0071949

Evidence at protein level

5

null

PF00173;PF00970;PF03404;PF00175;PF00174;

IPR008333;IPR001199;IPR036400;IPR018506;IPR017927;IPR001709;IPR039261;IPR014756;IPR005066;IPR008335;IPR001433;IPR000572;IPR036374;IPR022407;IPR017938;

5YLY;

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Chlorophyta (phylum), Ulvophyceae (class), OUU clade (clade), Ulvales (order), Ulvaceae (family), Ulva (genus)

null

false

378

A0A286Y9D1

MDRGSKRRQVKPLADSLLDALDYDSSDDSDFKVGESSGSEGTGNGSDEEGSKESAAGSESDSDAAAASADEEGIDDLETKDLNQEDDEEEKVKESFSEETSSKETGGSSRSRKKGEKSSDMEPNGSATTEENSAEPKKWNLRRNRPMLDFTTMEELNEMDDYDSEDDNDWRPTQGKKKGKASSGKEKEGSGEEDDDDDDGGSDEEDNEDDNDDDDDDDDEGNDDESSSSDSEEEGKKPKKKAGKNTGAFDEEETNDSHSTSHGKGNEDSLLERPQTWSSQRMEHILICCVCLGDNSEDADEIIQCDNCGVTVHEGCYGVDGESDSIMSSASENSTEPWFCDACKNGVSPSCELCPSQDGIFKETDAGRWVHVVCALYVPGVAFGDIDKLRPVTLTEMNYSKYGAKECSLCEDTRFARTGVCISCDAGMCRSFFHVTCAQREGLLSEAAAEEDIADPFFAYCKQHADRFDRKWKRKNYLALQSYCKVSLQEREKQLTPEAQARITTRLQQYRAKAELSRNTRPQAWVPREKLPRPLTSSASAIRKLMRKAELMGISTDIFPVDTSDISASVDGRRKHKQPALTADFVNYYLERNMRMIQIQDNIVEQKNLKDKLESEQEKLHMEYDKLCESLEDLQNVNGQLRTEGQSIWSMMGGIVGQKLNVPAVLKAPKERKPSKKEGGSPGKSSSLPAMLYSCGICKKNQDQHLLLLCDTCKLHYHLGCLDPPLTRMPKKTKNSYWQCSECDQASSDEADIAMETLPDGTKRSRRQIKGPIKFIPQEMSPEPKKPQVRGTRTRGQKRKRMSICEEEKMEEPLPRERRQRQSTLQKKPKADDTRTECTTCKGPGDNENLVRCDECRLCYHFGCLDPPLKKSPKQTGYGWICQECDTSSSKEEEAQEVEEESVNEETAEQEIPD

PHD finger protein 14

Danio rerio (Zebrafish) (Brachydanio rerio)

7,955

914

102,272

3D-structure;Coiled coil;Metal-binding;Nucleus;Reference proteome;Repeat;Transcription;Transcription regulation;Zinc;Zinc-finger

GO:0000122; GO:0005634; GO:0006357; GO:0008270; GO:0008285; GO:0010463; GO:0042393; GO:0048286; GO:0060916; GO:0072201; GO:0140566; GO:2000584; GO:2000791

Evidence at protein level

5

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9D4H9}.

null

PF00628;PF13831;PF13832;

IPR034732;IPR050701;IPR019786;IPR011011;IPR001965;IPR019787;IPR013083;

7D86;7D87;7D8A;

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Actinopterygii (superclass), Actinopteri (class), Neopterygii (subclass), Teleostei (infraclass), Osteoglossocephalai (clade), Clupeocephala (no rank), Otomorpha (cohort), Ostariophysi (subcohort), Otophysi (clade), Cypriniphysae (superorder), Cypriniformes (order), Cyprinoidei (suborder), Danionidae (family), Danioninae (subfamily), Danio (genus)

phf14

false

379

A0A287B8J2

MAQSKRHVYSRTPSGSRMSAEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKVLRREGTDSNAKTSKLRGPKPKKAPTARKTTTRRPKPTRPASTGVAGASSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFDLSENCSERPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDSTMQLADHIKFTQSALDCMSVEVGRLRAFLQGGQEASDIALLLRDLETSCSDIRQFCKKIRRRMPGTDAPGIPAALAFGAQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLPVAALEELAFKASEQIYGTPSSSPYECLRQSCNILISTMNKLATAMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLEETQALLRKKEKEFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIEGIRGPPPSGIATLVSGIAGEEQQRGGAPGQAPGIVPGPGLVKDSPLLLQQISAMRLHISQLQHENSVLKGAQMKASLAALPPLHVAKLSLPPHEGPGSELAAGALYRKTNQLLETLNQLSTHTHVVDITRSSPAAKSPSAQLLEQVTQLKSLSDTIEKLKDEVLKETVSQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGLGQRHRLVLTQEQLHQLHDRLIS

Dynactin subunit 1 (150 kDa dynein-associated polypeptide) (p150-glued)

Sus scrofa (Pig)

9,823

1,281

141,818

3D-structure;Cell cycle;Cell division;Coiled coil;Cytoplasm;Cytoskeleton;Dynein;Microtubule;Mitosis;Nucleus;Phosphoprotein;Reference proteome;Transport;Ubl conjugation

GO:0000132; GO:0000776; GO:0000922; GO:0005635; GO:0005813; GO:0005814; GO:0005829; GO:0005875; GO:0005938; GO:0007097; GO:0007528; GO:0008017; GO:0010457; GO:0019901; GO:0021517; GO:0030286; GO:0030424; GO:0030904; GO:0031252; GO:0032402; GO:0034454; GO:0035371; GO:0036064; GO:0042147; GO:0043025; GO:0045171; GO:0050905; GO:0051081; GO:0051301; GO:0060236; GO:0061744; GO:0070050; GO:0072686; GO:0090063; GO:0120103; GO:1904398; GO:1905515; GO:1990535

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q14203}. Nucleus envelope {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q14203}. Note=Localizes to microtubule plus ends. Localizes preferentially to the ends of tyrosinated microtubules. Localization at centrosome is regulated by SLK-dependent phosphorylation. Localizes to centrosome in a PARKDA-dependent manner. Localizes to the subdistal appendage region of the centriole in a KIF3A-dependent manner. PLK1-mediated phosphorylation at Ser-179 is essential for its localization in the nuclear envelope. {ECO:0000250|UniProtKB:Q14203}.

null

PF01302;PF12455;

IPR036859;IPR000938;IPR022157;

6ZNL;7Z8F;8PQW;8PQZ;8PR0;8PR5;8PTK;

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Artiodactyla (order), Suina (suborder), Suidae (family), Sus (genus)

DCTN1

false

380

A0A291NUG3

MLHSSLHPSIPQPRGRRAKKAAFVLLSVCLVVLWDLGERPEHILQWLMLHLASLQLGLLFKGVCSLVEELRHVHSRYQGSYWKAVRACLGCPIRCGTLLLLSCYFYTPFPNTTHLPFTWTLALLGLSQALSILLDLQDLAPAEVSAVCERRNLNVAQGMAWSFYIGYLRLILPGLPARIHSYNQHHNNLLRGAGSHRLYILFPLDCGVPDDLSMVDPNIRFLHELPLQKADRAGIKSRVYTNSVYELLENGRPVGACVLEYATPLQTLFAMSQDSRAGFSREDRLEQAKLFCKTLEDILADAPECQNNCRLVVYQEPAEGGNFSLSQEILRHLKQEEKEEVTVDSARTSVMPDPSMLPQGPELLISSMDQPLPLRTDVF

Stimulator of interferon genes protein (STING)

Pteronotus parnellii (Parnell's mustached bat)

59,476

379

42,654

Cell membrane;Cytoplasm;Cytoplasmic vesicle;Endoplasmic reticulum;Golgi apparatus;Immunity;Innate immunity;Ion channel;Ion transport;Lipoprotein;Membrane;Mitochondrion;Mitochondrion outer membrane;Nucleotide-binding;Palmitate;Phosphoprotein;Transmembrane;Transmembrane helix;Transport

GO:0000045; GO:0000139; GO:0000421; GO:0005741; GO:0005789; GO:0005886; GO:0015252; GO:0016239; GO:0031410; GO:0032481; GO:0033116; GO:0035438; GO:0035591; GO:0045087; GO:0048471; GO:0051607; GO:0061507; GO:0061709; GO:0140896

Evidence at protein level

5

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post-Golgi vesicles, where the kinase TBK1 is recruited (By similarity). Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis (By similarity). Localizes in the lysosome membrane in a TMEM203-dependent manner. {ECO:0000250|UniProtKB:Q3TBT3, ECO:0000250|UniProtKB:Q86WV6}.

null

TRANSMEM 18..38; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 43..63; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 89..109; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 114..134; /note="Helical"; /evidence="ECO:0000255"

PF15009;PF23417;

IPR029158;IPR047191;IPR038623;IPR055432;IPR055434;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Chiroptera (order), Yangochiroptera (suborder), Mormoopidae (family), Pteronotus (genus)

STING1 STING

false

381

A0A291NUI4

MPHSSLHPSIPRPRGHRAKKAAFVLLSTCLAALWELGEPADHILRWLVLHLASEQLGLLFKGLCSLAEEIRHVHSRYQGSYWRAFRACLGCPIRCGVLLLLSCYCYTFLPNTAGLPFAWIVALLGLSQALNILLDLQGLAPAVVSTVCEQGNFNVAHGLAWSYYIGYLRLILPGLQARIHTYNQRHNNTVRGTGVHKLYILLPLDCGVPDDLSVADPNIRFLHELPKQSADRAGIKGRVYTNSIYEILENGKPVGTCVLEYATPLQTLFAMSQDSRAGFSREERLEQAKLFCQTLGDILADVPESQYCRLIVYLDAAEGSSFSLSQEILKHLKQEEKEEVTVGTMGSSGVLESSTLDKEPQLLISGMDQPLPLRTDVF

Stimulator of interferon genes protein (STING)

Rhinolophus ferrumequinum (Greater horseshoe bat)

59,479

378

41,911

Cell membrane;Cytoplasm;Cytoplasmic vesicle;Endoplasmic reticulum;Golgi apparatus;Immunity;Innate immunity;Ion channel;Ion transport;Lipoprotein;Membrane;Mitochondrion;Mitochondrion outer membrane;Nucleotide-binding;Palmitate;Phosphoprotein;Reference proteome;Transmembrane;Transmembrane helix;Transport

GO:0000045; GO:0000139; GO:0000421; GO:0005741; GO:0005789; GO:0005886; GO:0015252; GO:0016239; GO:0031410; GO:0032481; GO:0033116; GO:0035438; GO:0035591; GO:0045087; GO:0048471; GO:0051607; GO:0061507; GO:0061709; GO:0140896

Evidence at protein level

5

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post-Golgi vesicles, where the kinase TBK1 is recruited (By similarity). Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis (By similarity). {ECO:0000250|UniProtKB:Q86WV6}.

null

TRANSMEM 21..41; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 46..66; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 89..109; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 114..134; /note="Helical"; /evidence="ECO:0000255"

PF15009;PF23417;

IPR029158;IPR047191;IPR038623;IPR055432;IPR055434;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Chiroptera (order), Yinpterochiroptera (suborder), Rhinolophoidea (superfamily), Rhinolophidae (family), Rhinolophinae (subfamily), Rhinolophus (genus)

STING1 STING

false

382

A0A291NUI5

MSHSSLHPSIPWPRGHKAKVAAFVLLIVCLAALWKLGEPSDHLLQWLVLHLASLHLRLLFKRVCCLAEELCHIHPRYQGNYSRAVRACLGCPIRYGAVLLLSCYFYVSLPNTVDLPLTWMLAHLGLSEALNILLGLQSLTPAEISTICEQRNFNVAHGLAWSYYIGYLQLILPGLRARIHTYNQLHSNTLQGVGSHRLYILFPLDCGVLDDLSAADPNIRFLHELPRQSADRAGIKGRVYTNSVYELLEKGKPVGTCVLEYATPLQTLFAMSQDGRAGFSQEDRLEQAKLFCRTLEDILADAPESQKNCRLIVYQEPTEESDFSLSQEILKHLRQEEREEVTMGTAGTFVAPGSSTLHQEPELLISGMDQPLPLRTDIF

Stimulator of interferon genes protein (STING)

Eidolon helvum (Straw-colored fruit bat)

77,214

379

42,537

Cell membrane;Cytoplasm;Cytoplasmic vesicle;Endoplasmic reticulum;Golgi apparatus;Immunity;Innate immunity;Ion channel;Ion transport;Lipoprotein;Membrane;Mitochondrion;Mitochondrion outer membrane;Nucleotide-binding;Palmitate;Phosphoprotein;Transmembrane;Transmembrane helix;Transport

GO:0000045; GO:0000139; GO:0000421; GO:0005741; GO:0005789; GO:0005886; GO:0015252; GO:0016239; GO:0031410; GO:0032481; GO:0033116; GO:0035438; GO:0035591; GO:0045087; GO:0048471; GO:0051607; GO:0061507; GO:0061709; GO:0140896

Evidence at protein level

5

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post-Golgi vesicles, where the kinase TBK1 is recruited (By similarity). Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis. Localizes in the lysosome membrane in a TMEM203-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q3TBT3, ECO:0000250|UniProtKB:Q86WV6}.

null

TRANSMEM 20..40; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 87..107; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 115..135; /note="Helical"; /evidence="ECO:0000255"

PF15009;PF23417;

IPR029158;IPR047191;IPR038623;IPR055432;IPR055434;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Chiroptera (order), Yinpterochiroptera (suborder), Pteropodoidea (superfamily), Pteropodidae (family), Pteropodinae (subfamily), Eidolon (genus)

STING1 STING

false

383

A0A2B7ICX0

MFDIPYQVPSRRTFLSLSALSAIAIAASPEMPDAFASPDPDIWSALCEKWTDIITGRNAAKTADPRARAIIAKTDKRVATILTDLASSSSRTTVLLSANLQKEESSFITTTARAISSIACAWATPGSAYHAEPHVLSACIDALKDFCRLRYHPSQDEYGNWWDWEDGASRAIGDVMCILHDALPTDVMAAAAAGIDHFVPDPWYQQPESVKPTAHPTQPVISTGANRMDLTRAVICRSIATGDESKLRHAVQGLPDSWRTVAEGDGFRADGGFIQHSHVPYTGSYGDVLLSGLAMLLPLVAGTRFDITDSAQANLLSQVERGIVPVMYGGQILDCVRGRSISRIDEPAAMHGMSIARSMLLMANAIPAHRAELWRGTVHGWMTRNTFDHLSEPASLRDIDLFDTAANVRPIPESSTPTYFASIDRLVHRTPNWLIAVSNCSNRISWYEYGNSENEWASRTSQGMRYLMLPEDMGQYEDGFWATVDYSAPTGTTVDSTPLKRAVGTAWAERTPDNEWSGGLASGEWSAAASQITSQDSTLKARRLWVGLKDALLELTTDVSTDASKATTVVEHRKVGKTPPELLVDGITITSKTSFDNPHWAHLRGVGGYVFATDVDLTAQLEKRKGSWIDVNPARTVKGFNEAIERNYASLHVTHHNRPVAWAVLPTASRSQTMALAQRPVDNLFIVLSNDRMVQAVRSTGCLLTKDPTVVTTYAFWKPATCAGMTADAPAIIQTQAQGSRVEVIMSEPTQKRPSLTVAIEGVWTVENSSDRISVSRSDKTTTLRINTADLGGQSIRVTLSPALPKPTKPSLRASSYPLGLPHTSS

Hyaluronate lyase HylA (EC 4.2.2.1) (Hyaluronate lyase) (Hyaluronidase) (HYase)

Cutibacterium acnes (Propionibacterium acnes)

1,747

826

90,014

3D-structure;Lyase;Secreted;Signal;Virulence

GO:0005576; GO:0005975; GO:0030246; GO:0030340

Evidence at protein level

5

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:38052825}.

SIGNAL 1..36; /note="Tat-type signal"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"

null

PF02278;PF02884;PF08124;

IPR008929;IPR011013;IPR014718;IPR038970;IPR011071;IPR012970;IPR004103;IPR003159;IPR006311;

8FYG;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Actinomycetota (phylum), Actinomycetes (class), Propionibacteriales (order), Propionibacteriaceae (family), Cutibacterium (genus)

hylA B1B09_04880 COH10_04915

false

384

A0A2C9JXL4

MAPISHYIGKTSLTTLAIGIAIGITVSNIVKFSSTQRRHFSSSGYIPDSPHSHGENDFVEGPDDSLSWHDEHSHSHKFENDSVARQLFKKVRVLCWVMTNPNNIHTKARHVKATWGKRCNVLLFMSSRADRDLPALALNVQEGRDNLWAKTKEAFKLIHSKYLETADWFIKCDDDTFLVLENLRYFLQDKSPSEPVYYGRKFKPIVQQGYMSGGAGYVLSKESLVRLVTQGIGHKEDCRADSGGAEDVEMGRCLQSVNVQAGDSRDELGRERFHPFVPEHHLIPDILPPDMWYWSYNFYPAKQGQECCSDYAISFHYVPPNMMYVLEYLVYHLKPYGITSAYESTEEQDHGSSHKDTDAMKPEGKGMEDKEDEETNISLAQTDSKHIS

Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1 (EC 2.4.1.122) (Glycoprotein-N-acetylgalactosamine beta-1,3-galactosyltransferase) (Beta-1,3-galactosyltransferase) (T-synthase)

Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail)

6,526

388

44,162

Disulfide bond;Glycoprotein;Glycosyltransferase;Manganese;Membrane;Metal-binding;Nucleotide-binding;Reference proteome;Signal-anchor;Transferase;Transmembrane;Transmembrane helix

GO:0000166; GO:0006486; GO:0016020; GO:0016263; GO:0016267; GO:0030145

Evidence at protein level

5

SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9JJ05}; Single-pass type II membrane protein {ECO:0000305}.

null

TRANSMEM 13..30; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255"

PF02434;

IPR026050;IPR003378;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Spiralia (clade), Lophotrochozoa (clade), Mollusca (phylum), Gastropoda (class), Heterobranchia (subclass), Euthyneura (clade), Panpulmonata (clade), Hygrophila (clade), Lymnaeoidea (superfamily), Planorbidae (family), Biomphalaria (genus)

null

false

385

A0A2H1A768

MSEKPFVDAPPPEDGVAHQVSPHDNGSLSEEANSINEYTGFGAHQEGEIRELARTFTNMSHDSGHDLSKTNTSQDLLKYLSHMSEVPGVEPFDPEQISEQLNPDSPNFNAKFWVKNMRKLFDSNPDYYKPSKLGLAYRNLRAYGVAADSDYQPTVSNGLWKMAVDYWHDMRKIDESRCFDILKTMDGYFKPGEVTVVLGRPGSGCSTLLKTIACNTYGFHIGEESQISYDGMTPDEIHKHHRGDVVYSAETDVHFPHLSVGDTLEFAAKLRTPQNRGEVSRLEHAKHMASVTMATYGLSHTRNTPVGNDFVRGVSGGERKRVSIAEVSLSGANIQCWDNATRGLDAATALEFIRALKTSAAILDATPLIAIYQCSQDAYDLFDNVIVLYEGYQIFFGKASEAKQFFLDMGYECPQRQTTADFLTSLTNPEERVVKPGFENKVPRTAKEFSDYWRNSSNYKVLTAGIDKYLAEVADGSQREAYRASHVAKQSDHTRPSSPYTVSFFMQTRYIIGRNFLRMKGDPSIVIFSIFGQGVMGLILSSVFYNLQPTTGSFYYRGAAMFFAVLFNAFASLLEIMSLFEARPIVEKHKKYALYRPSADALASIISELPVKLCMSTCFNFSFYFMVHFRRDPGRFFFYWLFCGLCTLCMSHMFRSLGAVSTSLAAAMTPATSVLLAMVIFTGFVIPIPSMLGWCRWIQYINPVSYVFESLMVNEFHGRKFECAQFVPSGGPYDQVAAVNRVCSTAGARPGEDFVDGTAYLQTSFEYVNAHKWRNLGIVVAYIVVFLGVYIALTEFNKGAMQKGEIALFLRGSLKKVRKQREQNEAKVNDVENNLPNEKISYSDAMEKDSGESSTSDDKLPNQRQIFHWKDLTYQVKIKAENRVILNHVDGWVKPGQITALMGASGAGKTTLLNCLSERLTTGTVTDGVRMVNGHGLDSSFQRSIGYVQQQDIHLATSTVREALTFSAYLRQPSHVSKKEKDEYVDYVIDLLEMGAYSDALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLANHGQAILCTIHQPSAILLQEFDRLLFLQKGGKTVYFGDLGKNCQGLIDYFEKHGAHPCPPDANPAEWMLEVVGAAPGSKAAQDYFEVWRNSEEYQEVQRELAYMENELGKLPVDEDPESRKKYATSLIKQYFIVTWRTFQQYWRSPGYIYSKFFLVITASLFNGFAFFHSGTSQQGLQNQMFSMFMFYMPLQTLIQQMLPYYVMQREIYEVREAPSRTFSWFAFIASQITTEIPFQVVLGTVAFFCWYYPVGLYQNATPTDTVHERGALMWLLVTAFYVYTISLGQMVVAFMEIADNAANMVNLMFIMCLNFCGVLATPEALPGFWIFMYRCNPFTYLIQAMLSTGLANTKIVCSSREILHFQPPSGQTCGQYMQQFISAAGGYLLDESATDQCDFCAMSQTNTFLDSVHAVYSERWRNFGIFIAFIAINMIGTIFFYWLARVPKSSKSKNH

Pleiotropic ABC efflux transporter of multiple drugs CDR1

Candidozyma auris (Yeast) (Candida auris)

498,019

1,508

169,964

ATP-binding;Cell membrane;Membrane;Nucleotide-binding;Repeat;Transmembrane;Transmembrane helix;Transport

GO:0005524; GO:0005886; GO:0016020; GO:0016887; GO:0140359; GO:1990961

Evidence at protein level

5

SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:30718246}; Multi-pass membrane protein {ECO:0000255}.

null

TRANSMEM 525..545; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 560..580; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 609..629; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 634..654; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 674..694; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 776..796; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1204..1224; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1240..1260; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1289..1309; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1327..1347; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1363..1383; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1476..1496; /note="Helical"; /evidence="ECO:0000255"

PF01061;PF00005;PF14510;PF06422;

IPR003593;IPR013525;IPR029481;IPR003439;IPR017871;IPR034001;IPR034003;IPR005285;IPR027417;IPR010929;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Metschnikowiaceae (family), Candidozyma (genus)

CDR1 B9J08_000164

false

386

A0A2H1K3G9

MIAVNSRNSLNADMTSLHPETLMVHGGMKGLTEAGVHVPAIDLSTTNPVNDVATGGDSYEWLATGHTLKDGDSAVYQRLWQPGVARFETALAGLEHAEEAVAFATGMAAMTAALLAAVSAGTPHIVAVRPLYGGSDHLLETGLLGTTVTWAKEADIASAIQDDTGLVIVETPANPSLDLVDLDSVVSAAGNVPVLVDNTFCTPVLQQPISHGAALVLHSATKYLGGHGDAMGGIIATNADWAMRLRQVRAITGALLHPMGAYLLHRGLRTLAVRMRAAQTTAGELAERLDAHPAISVVHYPGLKGQDPRGLLGRQMSGGGAMIAMELAGGFDAARSFVEHCNLVVHAVSLGGADTLIQHPASLTHRPVAATAKPGDGLIRLSVGLEHVDDLADDLIAALDASRAAA

L-methionine gamma-lyase (MGL) (EC 4.4.1.11) (Homocysteine desulfhydrase) (EC 4.4.1.2) (MGL-BL929)

Brevibacterium aurantiacum

273,384

406

41,994

Lyase;Pyridoxal phosphate

GO:0004123; GO:0005737; GO:0018826; GO:0019343; GO:0019346; GO:0030170

Evidence at protein level

5

null

PF01053;

IPR000277;IPR015424;IPR015421;IPR015422;

null

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Actinomycetota (phylum), Actinomycetes (class), Micrococcales (order), Brevibacteriaceae (family), Brevibacterium (genus)

BAUR9175_03070 BAUR920_03040 BAURA63_02933 BAURA86_00394

false

387

A0A2H4DGV8

MEPFTTFSLVASSLILLICWALVKANKPAKNLPPGPPKLPIIGNMHQLESQSPHRVLRKLSRKYGPIMHLQLGQVPTVVISTPRLVEEVVKHHDINFADRPTNTTSQIFYYNNQNVAWSSYGNYWRQIKKIVTLELLSVKKVRSFSSIRAEELTRAVKSVEPSVGSTINFRDLTSQTVNNMVSRATLGDVCKERHILLDTMNDILKTFNSFNVVNFFPSLQFLNVITGKKAKWLKIHKQLDHILENILEEHKSKPKGNQDDEDLIDVLLRVKDAGGQELPITNDNVKAITLEMLTAGTSSSSMTIEWAFCELMRHPEVMKKVQSDVRSAVKGNKVTEDDIQNMHYLKLVVKETLRLHGVPILVPRQNREDCNVLGYHIPAKTKILINAWACGTDPDTWEDPESFIPERFEKSSVSYFGTDFQLIPFGTGRRICPGVNFGIGTVEAVLSNFLYHFDWKLPDGVKPQDIDMTEVTGISTLPKYPLHIVPVSTVSQQK

Germacrene A acid 8-beta-hydroxylase (Ih8H) (IhG8H) (EC 1.14.14.168) (Cytochrome P450 71BL6) (Germacrene A acid 8-alpha-hydroxylase) (EC 1.14.14.170)

Inula hupehensis (Inula helianthus-aquatilis subsp. hupehensis)

1,805,964

495

55,963

Glycoprotein;Heme;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Signal-anchor;Transmembrane;Transmembrane helix

GO:0005506; GO:0009753; GO:0016020; GO:0016114; GO:0020037; GO:0051762; GO:0102614

Evidence at protein level

5

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}.

null

TRANSMEM 3..23; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255"

PF00067;

IPR001128;IPR017972;IPR002401;IPR036396;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), campanulids (clade), Asterales (order), Asteraceae (family), Asteroideae (subfamily), Inuleae (tribe), Inulinae (subtribe), Inula (genus)

CYP71BL6 G8H

false

388

A0A2I0BVG8

MGCSQSSNVKDFKTRRSKFTNGNNYGKSGNNKNSEDLAINPGMYVRKKEGKIGESYFKVRKLGSGAYGEVLLCREKHGHGEKAIKVIKKSQFDKMKYSITNKIECDDKIHEEIYNEISLLKSLDHPNIIKLFDVFEDKKYFYLVTEFYEGGELFEQIINRHKFDECDAANIMKQILSGICYLHKHNIVHRDIKPENILLENKHSLLNIKIVDFGLSSFFSKDNKLRDRLGTAYYIAPEVLRKKYNEKCDVWSCGVILYILLCGYPPFGGQNDQDIIKKVEKGKYYFDFNDWKNISEEAKELIKLMLTYDYNKRITAKEALNSKWIKKYANNINKSDQKTLCGALSNMRKFEGSQKLAQAAILFIGSKLTTLEERKELTDIFKKLDKNGDGQLDKKELIEGYNILRSFKNELGELKNVEEEVDNILKEVDFDKNGYIEYSEFISVCMDKQILFSEERLRDAFNLFDTDKSGKITKEELANLFGLTSISEQMWNEVLGEADKNKDNMIDFDEFVNMMHKICDNKSS

Calcium-dependent protein kinase 1 (EC 2.7.11.1) (PfCDPK1)

Plasmodium falciparum (isolate NF54)

5,843

524

60,800

ATP-binding;Calcium;Cell membrane;Cell projection;Cilium;Cytoplasm;Flagellum;Host cell membrane;Host membrane;Kinase;Lipoprotein;Magnesium;Membrane;Metal-binding;Myristate;Nucleotide-binding;Palmitate;Phosphoprotein;Repeat;Serine/threonine-protein kinase;Transferase

GO:0005509; GO:0005524; GO:0005737; GO:0005886; GO:0007292; GO:0009931; GO:0020002; GO:0020005; GO:0036126; GO:0048232

Evidence at protein level

5

SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P62344}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}. Cell membrane {ECO:0000269|PubMed:29311293}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}; Cytoplasmic side {ECO:0000250|UniProtKB:P62344}. Parasitophorous vacuole membrane {ECO:0000250|UniProtKB:P62344}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}. Cytoplasm {ECO:0000269|PubMed:29311293}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:29311293}. Host cell membrane {ECO:0000250|UniProtKB:P62344}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}. Note=Localizes to the host erythrocytic membrane at low level (By similarity). Localizes to the cell membrane in the nascent merozoites contained within the late-stage schizonts and in free merozoites. Colocalizes with MTIP around developing merozoites in segmented schizonts, also localizes in membranes around the mature food vacuole/residual body of the schizonts. Ser-64 phosphorylated form localizes at the apical pole in punctate structures in merozoites within late schizonts in free merozoites. In trophozoites and schizonts, localizes to the parasitophorous vacuole (PV) and in membranous systems derived from the PV including intraparasitic vacuoles and the tubovesicular system, an extension of the parasitophorous vacuole membrane into the host cell cytoplasm. Localization to the cytoplasm in trophozoite or schizonts is minimal (By similarity). In female stage V gametocytes and gametes, localizes to the cell membrane. In stage V male gametocytes, localizes to the cell membrane and in the cytoplasm. In male gametes, localizes to the residual body, cell membrane and in the flagella (PubMed:29311293). Calcium and/or autophosphorylation does not affect membrane localization (By similarity). {ECO:0000250|UniProtKB:P62343, ECO:0000250|UniProtKB:P62344, ECO:0000269|PubMed:29311293}.

null

PF13499;PF00069;

IPR050205;IPR011992;IPR018247;IPR002048;IPR011009;IPR000719;IPR017441;IPR008271;

null

cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Aconoidasida (class), Haemosporida (order), Plasmodiidae (family), Plasmodium (genus), Plasmodium (Laverania) (subgenus), Plasmodium falciparum (species)

PDCK1 CK202_3261

false

389

A0A2I0C265

MFFINFKKIKKKQFPIYLTQHRIITVFLIFIYFINLKDCFHINNSRILSDVDKHRGLYYNIPKCNVCHKCSICTHENGEAQNVIPMVAIPSKRKHIQDINKEREENKYPLHIFEEKDIYNNKDNVVKKEDIYKLRKKKKQKKNCLNFLEKDTMFLSPSHDKETFHINHMNKIKDEKYKQEYEEEKEIYDNTNTSQEKNETNNEQNLNINLINNDKVTLPLQQLEDSQYVGYIQIGTPPQTIRPIFDTGSTNIWIVSTKCKDETCLKVHRYNHKLSSSFKYYEPHTNLDIMFGTGIIQGVIGVETFKIGPFEIKNQSFGLVKREKASDNKSNVFERINFEGIVGLAFPEMLSTGKSTLYENLMSSYKLQHNEFSIYIGKDSKYSALIFGGVDKNFFEGDIYMFPVVKEYYWEIHFDGLYIDHQKFCCGVNSIVYDLKKKDQENNKLFFTRKYFRKNKFKTHLRKYLLKKIKHQKKQKHSNHKKKKLNKKKNYLIFDSGTSFNSVPKDEIEYFFRVVPSKKCDDSNIDQVVSSYPNLTYVINKMPFTLTPSQYLVRKNDMCKPAFMEIEVSSEYGHAYILGNATFMRYYYTVYRRGNNNNSSYVGIAKAVHTEENEKYLSSLHNKINNL

Plasmepsin IX (EC 3.4.23.-) (Plasmepsin 9)

Plasmodium falciparum (isolate NF54)

5,843

627

74,183

Aspartyl protease;Cytoplasmic vesicle;Hydrolase;Membrane;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zymogen

GO:0004190; GO:0016020; GO:0016485; GO:0020008; GO:0031410; GO:0085017

Evidence at protein level

5

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, rhoptry {ECO:0000269|PubMed:29074774}. Note=In schizonts, localizes to the bulb of rhoptries. {ECO:0000269|PubMed:29074774}.

null

TRANSMEM 14..34; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255"

PF00026;

IPR001461;IPR034164;IPR033121;IPR021109;

null

cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Aconoidasida (class), Haemosporida (order), Plasmodiidae (family), Plasmodium (genus), Plasmodium (Laverania) (subgenus), Plasmodium falciparum (species)

PMIX CK202_0216

false

390

A0A2I2F2I5

MLRSRQATNALRAVGQTRPLRSQTAVAFTQSLNKVPSNRRSEATVATASSTASGAFNSQVRPTPSPTFNQYDSKVQPLTGMSRNVTDESFIGKTGGEIFHDMMLRQGVKHIFGYPGGAILPVFDAIYNSTHFDFILPRHEQGAGHMAEGYARASGKPGVVLVTSGPGATNIVTPMQDALLDGTPMVVFCGQVPTTSIGSDAFQEADIVGISRPCTKWNVMVKNIAELPRRINEAFQIATTGRPGPVLVDLPKDVTAGILRRAIPTDAAIPSLPSASIQDAMDLNHKQLEASIARVAKLVNMAKQPVIYAGQGVIQSESGPELLKKLSDLASIPVTTTLQGLGGFDELDYKSLHMLGMHGSAYANMAMQEADLIIALGGRFDDRVTLNVSKFAPGARAAAAENRGGIVQFEIMPKNINKVVEATEAIVGDVGANLRLLLPHVESRSTDDRSAWYTKIDAWKKKWPLSDYQKTERHGLIKPQTLIEELSNLCADRKEKTYITTGVGQHQMWTAQHFRWRHPRTMITSGGLGTMGYGLPAAIGAKVAQPDALVVDIDGDASFNMTLTELSTAAQFNIGVKVIVLNNEEQGMVTQWQNLFYEDRYAHTHQANPDFIKIADAMGIQGQRVADPTKIKESLQWLIDTDGPALLEVITDKKVPVLPMVPGGCGLHEFIVFNPEDEKTRRGLMRERTCGLHG

Acetolactate synthase catalytic subunit, mitochondrial (EC 2.2.1.6) (Acetohydroxy-acid synthase catalytic subunit) (AHAS) (ALS) (Chlorflavonin biosynthesis cluster protein L)

Aspergillus candidus

41,067

694

75,426

Amino-acid biosynthesis;Branched-chain amino acid biosynthesis;FAD;Flavoprotein;Magnesium;Metal-binding;Mitochondrion;Reference proteome;Thiamine pyrophosphate;Transferase;Transit peptide

GO:0000287; GO:0003984; GO:0004737; GO:0005739; GO:0005948; GO:0009097; GO:0009099; GO:0030976; GO:0050660

Inferred from homology

5

SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.

null

PF02775;PF00205;PF02776;

IPR012846;IPR039368;IPR029035;IPR029061;IPR012000;IPR012001;IPR000399;IPR045229;IPR011766;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), Eurotiomycetes (class), Eurotiomycetidae (subclass), Eurotiales (order), Aspergillaceae (family), Aspergillus (genus), Aspergillus subgen. Circumdati (subgenus)

cfoL BDW47DRAFT_70763

false

391

A0A2I7G3B0

MSSGANGNSKSLAYDIKFTKLFINGEFVDSISGSTFETIDPATEEVLATVAEGREEDVDLAVKAAREAFDNGPWPRLSGEARRKILLKFADLIEENADEIATLEVIDTGKPFQIARYVENSWTSETFRYFAGAADKIRGATLKMSSDFQAYTLREPIGVVGHIIPWNAPAYLFAMKVAPALAAGCTVVIKPAENTPLVGLFMAYLSKLAGVPDGVINVVNGFGSTAGAAVSSHMDIDAVTFTGSTKVGRTIMQAAAASNLKPVSLELGGKSPFIVFDDADIEKAAEIAVLGVLSNKGELCVAGSRVFVHEGIYDAFVKKLEATVKNWATGDRFDAATRHGPQNNKQQYEKVLSYIELGKKEGATLVTGGKPFGNKGYYIEPTLFTNVTDEMTIAKEEIFGPVIMVLKFKTIEEVIRRANATTYGLAAGIMTKNIDIANTVTRSIRAGSVWVNCYLALDRDTPFGGYKMSGFGREQGLEALEHYLQVKTVTTPIYNSPWL

Aldehyde dehydrogenase 1 (TcALDH1) (EC 1.2.1.5) (Trans-chrysanthemic acid synthase) (EC 1.2.1.-)

Tanacetum cinerariifolium (Dalmatian daisy) (Chrysanthemum cinerariifolium)

118,510

499

53,988

NAD;Oxidoreductase

GO:0004029; GO:0008299; GO:0033721

Evidence at protein level

5

null

PF00171;

IPR016161;IPR016163;IPR029510;IPR016162;IPR015590;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), campanulids (clade), Asterales (order), Asteraceae (family), Asteroideae (subfamily), Anthemideae (tribe), Anthemidinae (subtribe), Tanacetum (genus)

ALDH1

false

392

A0A2I7G3B3

MSLNTPDVIICKAAVVRELGRSVMVEEIKVDPPKATEVRIKMLFASICHTDMLCFDGFPTPLFPRIPGHEGVGMVESVGEDIKTKLKPGDIVMPLFMGECGQCLNCKSKRTNLCHAYPLTLSGLLLDGTSRMSIAKTEETIYHHLSCSTWSEYMVIDINYVLKIDPKMHLPYASFLSCGFTTGFGAPWKETQITKGSIVAVFGLGAVGLGAIKGAQMQGASIIIGVDINENKAAKGKAFGMTHFINPKDHPNQLVSDMVRDITDGLGVDYCFECTGIASLLKEIIEASKIGFGTTILIGAAPDNVPISSLSLINGRTLKGTTFGGVRTRSDLPIILQKCMNEEIELDELMSHEIRLENIHEIFEILKKPDCVKILINFD

Alcohol dehydrogenase 2 (TcADH2) (EC 1.1.1.144) (EC 1.1.1.347) (Trans-chrysanthemal synthase) (EC 1.1.1.-)

Tanacetum cinerariifolium (Dalmatian daisy) (Chrysanthemum cinerariifolium)

118,510

379

41,397

Isoprene biosynthesis;Metal-binding;NAD;Oxidoreductase;Zinc

GO:0005829; GO:0008270; GO:0008299; GO:0018457; GO:0046294; GO:0051903

Evidence at protein level

5

null

PF08240;PF00107;

IPR013149;IPR013154;IPR002328;IPR011032;IPR036291;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), campanulids (clade), Asterales (order), Asteraceae (family), Asteroideae (subfamily), Anthemideae (tribe), Anthemidinae (subtribe), Tanacetum (genus)

ADH2

false

393

A0A2J6L8Y7

MVEEIMKSEEQKLIDVNKHRGVRSDGEEDEQLEEGEIVGGDADTLSSSSSSRPGTAIAQHPLEHSWTFWFDTPSAKSKQVAWGSSMRPIYTFSSVEEFWSLYNNIHRPSKLAQGADFYCFKNKIEPKWEDPVCANGGKWTMTFTKAKSDTCWLYTLLAMIGEQFDHGDDICGAVVNVRARQEKIALWTKNAANESAQLSIGKQWKEFIDYNDTIGFIFHEDAKTLDRSAKNKYTV

Eukaryotic translation initiation factor 4E-1 (Ls-eIF4E-1) (eIF-4E-1) (eIF-4F 25 kDa subunit) (eIF-4F p26 subunit) (mRNA cap-binding protein)

Lactuca sativa (Garden lettuce)

4,236

235

26,678

Cytoplasm;Disulfide bond;Host-virus interaction;Initiation factor;Nucleus;Plant defense;Protein biosynthesis;RNA-binding;Translation regulation

GO:0003723; GO:0003743; GO:0005634; GO:0005737; GO:0006413; GO:0006417; GO:0051607

Evidence at protein level

5

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm {ECO:0000250|UniProtKB:C6ZJZ3}.

null

PF01652;

IPR023398;IPR001040;IPR019770;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), campanulids (clade), Asterales (order), Asteraceae (family), Cichorioideae (subfamily), Cichorieae (tribe), Lactucinae (subtribe), Lactuca (genus)

eIF4E LSAT_4X27581

false

394

A0A2J8C362

MQTSALLLAAQALVASAGLIERQSCPSIHVFGARETTVGPGYGSAGTVVNLILNAYPGSTAEAIVYPACGGQSSCGGISYGNSAMQGTNAVASAVNSFNQRCPNTQIVLVGYSQGGQIMDNALCGGGDPGSGITNTAVPLTASAVTAVKAAILMGSPRYRAGFPYNVGTCTAQGFAARPAGFVCPSGSKIQNYCDSPDPYCCTGNNQAVHQGYGGVYGQAALTFVRSKLNSGGSPPTTPPTTPPTTPPTTPPTTPPPSGSCAALYGQCGGQGWNGATCCSQGTCRASNQWYSQCL

Cutinase 11 (EC 3.1.1.74) (VdCUT11)

Verticillium dahliae (Verticillium wilt)

27,337

295

29,632

Disulfide bond;Hydrolase;Reference proteome;Secreted;Signal;Virulence

GO:0005576; GO:0005975; GO:0030248; GO:0044409; GO:0052689

Evidence at protein level

5

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29068240}.

SIGNAL 1..17; /evidence="ECO:0000255"

null

PF00734;PF01083;

IPR029058;IPR035971;IPR000254;IPR000675;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), sordariomyceta (clade), Sordariomycetes (class), Hypocreomycetidae (subclass), Glomerellales (order), Plectosphaerellaceae (family), Verticillium (genus)

VD0003_g7577 VDGD_07784 VDGE_07784 VEDA_01118

false

395

A0A2K1ZPK4

MPVEENYQPLLQEEEERAYDSDEKVLIIGVDSDTESGGSTVLPPFSWKKLWLFTGPGFLMSIAFLDPGNLEGDLQAGAIAGYSLLWLLLWATAMGLLVQLLSARLGVATGRHLAELCREEYPTWASMVLWIMAELALIGADIQEVIGSAIAIKILSNGFVPLWAGVTITACDCFIFLFLENYGVRKLEAVFAVLIGIMAVTFGWMFADAKPSASELFLGILIPKLSSRTIQQAVGVVGCIIMPHNVFLHSALVQSREIDHNKKDRVQEALRYYSIESTTALVISFVINLFVTTVFAKGFYGTELANSIGLVNAGQYLQDKYGGGFFPILYIWGIGLLAAGQSSTITGTYAGQFIMGGFLNLRLKKWLRALITRSCAIIPTMIVALVFDTSEDSLDVLNEWLNVLQSIQIPFALIPLLCLVSKEQIMGTFKIGPILKMVAWLVAALVMVINGYLLLDFFFNEVTGVAFTTVVCGFTGAYVAFIIYLISRGFTCFSRCCPSKQIEVE

Metal transporter Nramp3.2 (PotriNRAMP3.2) (PtNRAMP3.2) (Natural resistance-associated macrophage protein 3.2)

Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa)

3,694

505

55,464

Ion transport;Membrane;Reference proteome;Transmembrane;Transmembrane helix;Transport;Vacuole

GO:0005384; GO:0005774; GO:0006826; GO:0006828; GO:0006879; GO:0009705; GO:0015086; GO:0034755; GO:0042742; GO:0046873; GO:0071421; GO:1903335; GO:2000379

Evidence at protein level

5

SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:35700212}; Multi-pass membrane protein {ECO:0000255}.

null

TRANSMEM 50..70; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 78..98; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 127..147; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 159..179; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 187..207; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 233..253; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 280..300; /note="Helical; Name=7"; /evidence="ECO:0000255"; TRANSMEM 321..341; /note="Helical; Name=8"; /evidence="ECO:0000255"; TRANSMEM 369..389; /note="Helical; Name=9"; /evidence="ECO:0000255"; TRANSMEM 400..420; /note="Helical; Name=10"; /evidence="ECO:0000255"; TRANSMEM 439..459; /note="Helical; Name=11"; /evidence="ECO:0000255"; TRANSMEM 466..486; /note="Helical; Name=12"; /evidence="ECO:0000255"

PF01566;

IPR001046;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), rosids (clade), fabids (clade), Malpighiales (order), Salicaceae (family), Saliceae (tribe), Populus (genus)

NRAMP3.2 Potri.007G050600

false

396

A0A2K3D5Z7

MSVALASEYQLVQNAQLPQRWSQSARKSLAILEATARKEATAQMEAAGGSFCGQFPVDPAFKVLSLEYSAPNPDIARAIRRVDSVPNPPLPSHVVAIQSTAVDADLSLAMGVSLTPGRHTSYLVDARALQQSNSAAVAARKADGDKWGPACDEMFRGCRCVTGQEVVFYTAVKEPAGEVEGGEGSLFKPSFDGPAFRPSWGELSGKATGVVACVLQVPIGKETDIICAEYDNLVSKGQFATVDRFGGDHTVNMTGNALIQNDGKAISKGYAVAHRARVTSNVYGKANDVSLQRLAETVWSVVEKRLSFMPAYRDLVITEQGKPFMLGATATNIISLTENQGVMLHLDTDDGVWTIILWFHRHSGIIAGGEFVLPSLGISFQPLDFTIVVFAANTIVHGTRPLQTTGKIIRWGSSHFLRFKDVNALAQLGAAYGVDELDAKQRDQLEEVDAANSKDGVGAARRVASCMAAERKAAIEAQKAACVRGVVMNPCTGRMPSLLFWQVWRKPPALAVRANAVAGKKRAAADVDFCGA

5-methylcytosine-modifying enzyme 1 (5mC-modifying enzyme 1) (EC 1.14.99.-) (Ten-eleven translocation 1 gene protein homolog) (CrTET1)

Chlamydomonas reinhardtii (Chlamydomonas smithii)

3,055

532

56,994

3D-structure;Dioxygenase;Iron;Metal-binding;Nucleus;Oxidoreductase;Reference proteome

GO:0005506; GO:0005634; GO:0010109; GO:0051213; GO:0120204; GO:0141167

Evidence at protein level

5

SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.

null

7CY4;7CY5;7CY6;7CY7;7CY8;

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Chlorophyta (phylum), core chlorophytes (clade), Chlorophyceae (class), CS clade (clade), Chlamydomonadales (order), Chlamydomonadaceae (family), Chlamydomonas (genus)

CMD1 CHLRE_12g553400v5

false

397

A0A2K3DU55

MRSVPGPSPPCTRSLAHSCRAAARGPCGSARPRARSVSARAHSSEASDMARVQQNFNSAGVGLFFSLFGGNQSLALPHLAAPDIRHVDWRALKAAGFKGLVFDKDNTLSLPFALEVEPRLQPALAGCLEAFGGRAVLYSNSAGLQQYDPEGKEAAALEAALGIPVLRHADKKPGGGCAELEAHFGCPAPQLIMVGDRYLTDIAFGNRHGMLTVHVQPLTTSGEPFGVVMARRIEEFWVARWTSFGVHPPAHSLAPHDTLAAYVKDQPIA

Phosphatidylglycerophosphate phosphatase 1, chloroplastic (CrPGPP1) (PGP phosphatase 1) (EC 3.1.3.27)

Chlamydomonas reinhardtii (Chlamydomonas smithii)

3,055

269

28,620

Chloroplast;Hydrolase;Lipid biosynthesis;Lipid metabolism;Phospholipid biosynthesis;Phospholipid metabolism;Plastid;Reference proteome;Transit peptide

GO:0005737; GO:0006655; GO:0008962; GO:0009507; GO:0009658; GO:0010027; GO:0015979; GO:0016791; GO:0046486; GO:0046839

Evidence at protein level

5

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.

null

PF09419;

IPR036412;IPR023214;IPR027706;IPR010021;

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Chlorophyta (phylum), core chlorophytes (clade), Chlorophyceae (class), CS clade (clade), Chlamydomonadales (order), Chlamydomonadaceae (family), Chlamydomonas (genus)

PGPP1 Cre04.g219900 CHLRE_04g219900v5

false

398

A0A2K3DZC4

MNSAALNARTASVAPQPQACHACKCRQLLSRRVPPAQRQVECSAIAPETLQDIIVGGAVVGAVSVALYAGLKKDPVPCSLCQGTGGIRCFACGGDGRNATVSRDDLYDSKALGGGVAPPKRDPLGRTINPRDCKVCRGAGLVLCSQCKGTGFQSAF

Protein BUNDLE SHEATH DEFECTIVE 2, chloroplastic (CrBSD2)

Chlamydomonas reinhardtii (Chlamydomonas smithii)

3,055

156

16,059

Chaperone;Chloroplast;Metal-binding;Plastid;Reference proteome;Repeat;Transit peptide;Zinc

GO:0009570; GO:0044183; GO:0046872; GO:0061077; GO:0101031; GO:0110102

Evidence at protein level

5

SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:25124725}. Note=Associates with chloroplastic polysomes. {ECO:0000269|PubMed:25124725}.

null

cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Chlorophyta (phylum), core chlorophytes (clade), Chlorophyceae (class), CS clade (clade), Chlamydomonadales (order), Chlamydomonadaceae (family), Chlamydomonas (genus)

BSD2 ZNJ2 CHLRE_03g201050v5 CHLREDRAFT_183954

false

399

A0A2K5EJU6

MKAAVLIWLFLMGSQARHFWQQDEPPQSPWDRVKDLATVYVDSVKDSGRDYVSQFETSTLGKQLNLKLLDNWDSLTSTVNKLREQLGPVTQEFWDNLEKETEELRQEMSKDLEEVKAQVQPYLDNFQKNWQEEMNLYSQKLEPLRTELQEGALQKLQDLQEKLSPLAEQVRDRARAHVNTLRTQLAPYSDELRQRLATRLEALKENSGASLAEYHAKASEHLSALGEKAKPALDDLRQGLLPVLESFKVSFLSALEEYTKKLSSQ

Apolipoprotein A-I (Apo-AI) (ApoA-I) (Apolipoprotein A1) [Cleaved into: Proapolipoprotein A-I (ProapoA-I); Truncated apolipoprotein A-I]

Aotus nancymaae (Ma's night monkey)

37,293

265

30,577

Cholesterol metabolism;HDL;Lipid metabolism;Lipid transport;Lipoprotein;Oxidation;Palmitate;Phosphoprotein;Reference proteome;Repeat;Secreted;Signal;Steroid metabolism;Sterol metabolism;Transport

GO:0001540; GO:0001935; GO:0002719; GO:0005543; GO:0006656; GO:0006695; GO:0007186; GO:0007229; GO:0008035; GO:0008211; GO:0010804; GO:0010875; GO:0010903; GO:0015485; GO:0019899; GO:0019915; GO:0030139; GO:0030300; GO:0030325; GO:0031072; GO:0032489; GO:0032691; GO:0033344; GO:0033700; GO:0034115; GO:0034191; GO:0034205; GO:0034361; GO:0034362; GO:0034366; GO:0034375; GO:0034380; GO:0035025; GO:0042158; GO:0042627; GO:0042632; GO:0042803; GO:0043534; GO:0043691; GO:0045499; GO:0050728; GO:0050766; GO:0050821; GO:0051180; GO:0051496; GO:0055091; GO:0060228; GO:0060354; GO:0070328; GO:0070508; GO:0070653; GO:0071402; GO:0090205; GO:0120020; GO:1900026; GO:1902995; GO:1903561

Inferred from homology

5

SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02647}.

SIGNAL 1..16; /evidence="ECO:0000255"

null

PF01442;

IPR000074;IPR050163;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Primates (order), Haplorrhini (suborder), Simiiformes (infraorder), Platyrrhini (parvorder), Aotidae (family), Aotus (genus)

APOA1

false