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Unnamed: 0
int64
0
562k
Entry
stringlengths
6
10
Sequence
stringlengths
2
35.2k
Protein names
stringlengths
1
2.59k
Organism
stringlengths
8
196
Organism (ID)
int64
14
3.4M
Length
int64
2
35.2k
Mass
int64
260
3.91M
Keywords
stringlengths
3
1.61k
Gene Ontology IDs
stringlengths
10
3.48k
Protein existence
stringclasses
5 values
Annotation
float64
1
5
Subcellular location [CC]
stringlengths
29
6.18k
Signal peptide
stringlengths
11
302
Transmembrane
stringlengths
31
5.51k
Pfam
stringlengths
8
232
InterPro
stringlengths
10
820
PDB
stringlengths
5
11.6k
Taxonomic lineage
stringlengths
49
843
Gene Names
stringlengths
1
583
Toxin
bool
2 classes
0
A0A009IHW8
MSLEQKKGADIISKILQIQNSIGKTTSPSTLKTKLSEISRKEQENARIQSKLSDLQKKKIDIDNKLLKEKQNLIKEEILERKKLEVLTKKQQKDEIEHQKKLKREIDAIKASTQYITDVSISSYNNTIPETEPEYDLFISHASEDKEDFVRPLAETLQQLGVNVWYDEFTLKVGDSLRQKIDSGLRNSKYGTVVLSTDFIKKDWTNYELDGLVAREMNGHKMILPIWHKITKNDVLDYSPNLADKVALNTSVNSIEEIAHQLADVILNR
2' cyclic ADP-D-ribose synthase AbTIR (2'cADPR synthase AbTIR) (EC 3.2.2.-) (NAD(+) hydrolase AbTIR) (EC 3.2.2.6) (TIR domain-containing protein in A.baumannii) (AbTIR)
Acinetobacter baumannii (strain 1295743)
1,310,613
269
30,922
3D-structure;Coiled coil;Hydrolase;NAD
GO:0003953; GO:0007165; GO:0019677; GO:0050135; GO:0061809
Evidence at protein level
5
null
null
null
PF13676;
IPR000157;IPR035897;
7UWG;7UXU;8G83;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Moraxellales (order), Moraxellaceae (family), Acinetobacter (genus), Acinetobacter calcoaceticus/baumannii complex (no rank), Acinetobacter baumannii (species)
J512_3302
false
1
A0A023I7E1
MRFQVIVAAATITMITSYIPGVASQSTSDGDDLFVPVSNFDPKSIFPEIKHPFEPMYANTENGKIVPTNSWISNLFYPSADNLAPTTPDPYTLRLLDGYGGNPGLTIRQPSAKVLGSYPPTNDVPYTDAGYMINSVVVDLRLTSSEWSDVVPDRQVTDWDHLSANLRLSTPQDSNSYIDFPIVRGMAYITANYNNLTPQFLSQHAIISVEADEKKSDDNTSTFSGRKFKITMNDDPTSTFIIYSLGDKPLELRKQDNSNLVASKPYTGVIRVAKLPAPEFETLLDASRAVWPTGGDISARSDDNNGASYTIKWKTNSNEAPLLTYAYAHHLTSIDDSNVKRTDMTLQSATKGPMTALVGNEWTLRETELSPVEWLPLQAAPNPTTINEIMTEINKDIASNYTQETAKEDNYFSGKGLQKFAMLALILNKSDQTQLRNPELAQIALDKLKAAFLPYLQNEQADPFRYDTLYKGIVAKAGLPTSMGGTDDLSAEFGHSYYSDHHYHQGYFVVTAAIIHHLDPTWNADRLKAWTEALIRDVNNANDGDEYFAAFRNWDWFAGHSWAGGIKPDGALDGRDQESVPESVNFYWGAKLWGLATGNTPLTKLASLQLAVTKRTTYEYFWMLDGNKNRPENIVRNKVIGIYFEQKTDYTTYFGRFLEYIHGIQQLPMTPELMEYIRTPEFVSQEWDEKLGAIAPTVQSPWAGVLYLNYAIINPAEAYPALRKVQMDDGQTRSYSLYLTATRPHFFRRSLLAALARHGSTRRPSLPSSGDDDKHEDGFLLRFRRLNPFNLKHRIY
Glucan endo-1,3-beta-D-glucosidase 1 (Endo-1,3-beta-glucanase 1) (EC 3.2.1.39) (Laminarinase) (RmLam81A)
Rhizomucor miehei
4,839
796
89,495
3D-structure;Carbohydrate metabolism;Cell wall;Cell wall biogenesis/degradation;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal
GO:0000272; GO:0005576; GO:0042973; GO:0052861; GO:0071555
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250|UniProtKB:P53753}.
SIGNAL 1..24; /evidence="ECO:0000255"
null
PF17652;PF03639;
IPR005200;IPR040720;IPR040451;
4K35;4K3A;5XBZ;5XC2;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Fungi incertae sedis (no rank), Mucoromycota (phylum), Mucoromycotina (subphylum), Mucoromycetes (class), Mucorales (order), Lichtheimiaceae (family), Rhizomucor (genus)
ENG1 LAM81A
false
2
A0A024B7W1
MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKEKKRRGADTSVGIVGLLLTTAMAAEVTRRGSAYYMYLDRNDAGEAISFPTTLGMNKCYIQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGCVTVMAQDKPTVDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEAYLDKQSDTQYVCKRTLVDRGWGNGCGLFGKGSLVTCAKFACSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHETDENRAKVEITPNSPRAEATLGGFGSLGLDCEPRTGLDFSDLYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKEALVEFKDAHAKRQTVVVLGSQEGAVHTALAGALEAEMDGAKGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGSTIGKAFEATVRGAKRMAVLGDTAWDFGSVGGALNSLGKGIHQIFGAAFKSLFGGMSWFSQILIGTLLMWLGLNTKNGSISLMCLALGGVLIFLSTAVSADVGCSVDFSKKETRCGTGVFVYNDVEAWRDRYKYHPDSPRRLAAAVKQAWEDGICGISSVSRMENIMWRSVEGELNAILEENGVQLTVVVGSVKNPMWRGPQRLPVPVNELPHGWKAWGKSYFVRAAKTNNSFVVDGDTLKECPLKHRAWNSFLVEDHGFGVFHTSVWLKVREDYSLECDPAVIGTAVKGKEAVHSDLGYWIESEKNDTWRLKRAHLIEMKTCEWPKSHTLWTDGIEESDLIIPKSLAGPLSHHNTREGYRTQMKGPWHSEELEIRFEECPGTKVHVEETCGTRGPSLRSTTASGRVIEEWCCRECTMPPLSFRAKDGCWYGMEIRPRKEPESNLVRSMVTAGSTDHMDHFSLGVLVILLMVQEGLKKRMTTKIIISTSMAVLVAMILGGFSMSDLAKLAILMGATFAEMNTGGDVAHLALIAAFKVRPALLVSFIFRANWTPRESMLLALASCLLQTAISALEGDLMVLINGFALAWLAIRAMVVPRTDNITLAILAALTPLARGTLLVAWRAGLATCGGFMLLSLKGKGSVKKNLPFVMALGLTAVRLVDPINVVGLLLLTRSGKRSWPPSEVLTAVGLICALAGGFAKADIEMAGPMAAVGLLIVSYVVSGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEDDGPPMREIILKVVLMTICGMNPIAIPFAAGAWYVYVKTGKRSGALWDVPAPKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGSALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWDGHSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGRREEETPVECFEPSMLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKTRLRTVILAPTRVVAAEMEEALRGLPVRYMTTAVNVTHSGTEIVDLMCHATFTSRLLQPIRVPNYNLYIMDEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIMDTEVEVPERAWSSGFDWVTDHSGKTVWFVPSVRNGNEIAACLTKAGKRVIQLSRKTFETEFQKTKHQEWDFVVTTDISEMGANFKADRVIDSRRCLKPVILDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYLYGGGCAETDEDHAHWLEARMLLDNIYLQDGLIASLYRPEADKVAAIEGEFKLRTEQRKTFVELMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPAEVWTRHGEKRVLKPRWMDARVCSDHAALKSFKEFAAGKRGAAFGVMEALGTLPGHMTERFQEAIDNLAVLMRAETGSRPYKAAAAQLPETLETIMLLGLLGTVSLGIFFVLMRNKGIGKMGFGMVTLGASAWLMWLSEIEPARIACVLIVVFLLLVVLIPEPEKQRSPQDNQMAIIIMVAVGLLGLITANELGWLERTKSDLSHLMGRREEGATIGFSMDIDLRPASAWAIYAALTTFITPAVQHAVTTSYNNYSLMAMATQAGVLFGMGKGMPFYAWDFGVPLLMIGCYSQLTPLTLIVAIILLVAHYMYLIPGLQAAAARAAQKRTAAGIMKNPVVDGIVVTDIDTMTIDPQVEKKMGQVLLIAVAVSSAILSRTAWGWGEAGALITAATSTLWEGSPNKYWNSSTATSLCNIFRGSYLAGASLIYTVTRNAGLVKRRGGGTGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEARRALKDGVATGGHAVSRGSAKLRWLVERGYLQPYGKVIDLGCGRGGWSYYAATIRKVQEVKGYTKGGPGHEEPMLVQSYGWNIVRLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEEARTLRVLSMVGDWLEKRPGAFCIKVLCPYTSTMMETLERLQRRYGGGLVRVPLSRNSTHEMYWVSGAKSNTIKSVSTTSQLLLGRMDGPRRPVKYEEDVNLGSGTRAVVSCAEAPNMKIIGNRIERIRSEHAETWFFDENHPYRTWAYHGSYEAPTQGSASSLINGVVRLLSKPWDVVTGVTGIAMTDTTPYGQQRVFKEKVDTRVPDPQEGTRQVMSMVSSWLWKELGKHKRPRVCTKEEFINKVRSNAALGAIFEEEKEWKTAVEAVNDPRFWALVDKEREHHLRGECQSCVYNMMGKREKKQGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMGRENSGGGVEGLGLQRLGYVLEEMSRIPGGRMYADDTAGWDTRISRFDLENEALITNQMEKGHRALALAIIKYTYQNKVVKVLRPAEKGKTVMDIISRQDQRGSGQVVTYALNTFTNLVVQLIRNMEAEEVLEMQDLWLLRRSEKVTNWLQSNGWDRLKRMAVSGDDCVVKPIDDRFAHALRFLNDMGKVRKDTQEWKPSTGWDNWEEVPFCSHHFNKLHLKDGRSIVVPCRHQDELIGRARVSPGAGWSIRETACLAKSYAQMWQLLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLVVWNRVWIEENDHMEDKTPVTKWTDIPYLGKREDLWCGSLIGHRPRTTWAENIKNTVNMVRRIIGDEEKYMDYLSTQVRYLGEEGSTPGVL
Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (NS5)]
Zika virus (isolate ZIKV/Human/French Polynesia/10087PF/2013) (ZIKV)
2,043,570
3,423
379,113
3D-structure;4Fe-4S;Acetylation;Activation of host autophagy by virus;Alternative initiation;ATP-binding;Capsid protein;Clathrin-mediated endocytosis of virus by host;Cleavage on pair of basic residues;Disulfide bond;Fusion of virus membrane with host endosomal membrane;Fusion of virus membrane with host membrane;Glycoprotein;GTP-binding;Helicase;Host cytoplasm;Host endoplasmic reticulum;Host membrane;Host nucleus;Host-virus interaction;Hydrolase;Inhibition of host innate immune response by virus;Inhibition of host interferon signaling pathway by virus;Inhibition of host STAT1 by virus;Inhibition of host STAT2 by virus;Inhibition of host TYK2 by virus;Interferon antiviral system evasion;Iron;Iron-sulfur;Isopeptide bond;Membrane;Metal-binding;Methyltransferase;mRNA capping;mRNA processing;Nucleotide-binding;Nucleotidyltransferase;Phosphoprotein;Protease;RNA-binding;RNA-directed RNA polymerase;S-adenosyl-L-methionine;Secreted;Serine protease;Suppressor of RNA silencing;Transcription;Transcription regulation;Transferase;Transmembrane;Transmembrane helix;Ubl conjugation;Viral attachment to host cell;Viral envelope protein;Viral immunoevasion;Viral penetration into host cytoplasm;Viral RNA replication;Virion;Virus endocytosis by host;Virus entry into host cell;Zinc
GO:0003724; GO:0003725; GO:0003968; GO:0004252; GO:0004482; GO:0004483; GO:0005198; GO:0005524; GO:0005525; GO:0005576; GO:0005813; GO:0006508; GO:0008289; GO:0016020; GO:0016887; GO:0019028; GO:0019031; GO:0019062; GO:0039502; GO:0039520; GO:0039563; GO:0039564; GO:0039574; GO:0039654; GO:0039694; GO:0042025; GO:0044167; GO:0044220; GO:0045824; GO:0046872; GO:0046983; GO:0051539; GO:0055036; GO:0060090; GO:0075512
Evidence at protein level
5
SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000269|PubMed:36594413}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q32ZE1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q32ZE1}; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-ProRule:PRU00860}.; SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q32ZE1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q32ZE1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q32ZE1}. Host nucleus {ECO:0000269|PubMed:32699085}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
null
TRANSMEM 105..125; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 250..269; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 275..290; /note="Helical"; /evidence="ECO:0000305"; TRANSMEM 746..767; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 774..794; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1178..1198; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1221..1241; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1271..1291; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1296..1316; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1346..1366; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1374..1394; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1398..1418; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 2171..2191; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 2219..2239; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 2345..2365; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 2376..2396; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 2442..2462; /note="Helical"; /evidence="ECO:0000255"
PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949;
IPR043502;IPR000069;IPR038302;IPR013755;IPR001122;IPR037172;IPR011492;IPR027287;IPR026470;IPR038345;IPR011998;IPR001157;IPR000752;IPR000487;IPR001850;IPR000404;IPR001528;IPR046811;IPR002535;IPR038688;IPR047530;IPR000208;IPR000336;IPR014412;IPR036253;IPR038055;IPR013756;IPR014001;IPR001650;IPR014756;IPR026490;IPR049486;IPR027417;IPR009003;IPR007094;IPR002877;IPR029063;
5GOZ;5GP1;5H30;5H32;5H37;5IRE;5IZ7;5JMT;5KQR;5KQS;5KVE;5LBS;5LBV;5LCV;5M5B;5MRK;5NJU;5NJV;5U4W;5UHY;5ULP;5Y0A;5Y6M;5Y6N;6CO8;6I7P;6JFH;6JFI;6LD1;6LD2;6LD3;6LD4;6LD5;6NIP;6NIU;6PLK;6RWZ;6S0J;6UM3;7A3N;7A3U;7BSD;7BU8;7BUA;7M1V;7T17;7V2Z;7YAR;7YW7;7YW8;8EE5;8EE8;8EED;8EEE;
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Kitrinoviricota (phylum), Flasuviricetes (class), Amarillovirales (order), Flaviviridae (family), Orthoflavivirus (genus), Orthoflavivirus zikaense (species), Zika virus (no rank)
null
false
3
A0A024RXP8
MYRKLAVISAFLATARAQSACTLQSETHPPLTWQKCSSGGTCTQQTGSVVIDANWRWTHATNSSTNCYDGNTWSSTLCPDNETCAKNCCLDGAAYASTYGVTTSGNSLSIGFVTQSAQKNVGARLYLMASDTTYQEFTLLGNEFSFDVDVSQLPCGLNGALYFVSMDADGGVSKYPTNTAGAKYGTGYCDSQCPRDLKFINGQANVEGWEPSSNNANTGIGGHGSCCSEMDIWEANSISEALTPHPCTTVGQEICEGDGCGGTYSDNRYGGTCDPDGCDWNPYRLGNTSFYGPGSSFTLDTTKKLTVVTQFETSGAINRYYVQNGVTFQQPNAELGSYSGNELNDDYCTAEEAEFGGSSFSDKGGLTQFKKATSGGMVLVMSLWDDYYANMLWLDSTYPTNETSSTPGAVRGSCSTSSGVPAQVESQSPNAKVTFSNIKFGPIGSTGNPSGGNPPGGNPPGTTTTRRPATTTGSSPGPTQSHYGQCGGIGYSGPTVCASGTTCQVLNPYYSQCL
Exoglucanase 1 (EC 3.2.1.91) (1,4-beta-cellobiohydrolase) (Cellobiohydrolase 7A) (Cel7A) (Exocellobiohydrolase I) (CBHI) (Exoglucanase I)
Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei)
1,344,414
514
54,111
Carbohydrate metabolism;Cellulose degradation;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Pyrrolidone carboxylic acid;Secreted;Signal
GO:0005576; GO:0016162; GO:0030245; GO:0030248
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P62694}.
SIGNAL 1..17; /evidence="ECO:0000255"
null
PF00734;PF00840;
IPR035971;IPR000254;IPR013320;IPR001722;IPR037019;
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), Hypocreales (order), Hypocreaceae (family), Trichoderma (genus), Hypocrea jecorina (species)
cbh1 M419DRAFT_125125
false
4
A0A024SC78
MRSLAILTTLLAGHAFAYPKPAPQSVNRRDWPSINEFLSELAKVMPIGDTITAACDLISDGEDAAASLFGISETENDPCGDVTVLFARGTCDPGNVGVLVGPWFFDSLQTALGSRTLGVKGVPYPASVQDFLSGSVQNGINMANQIKSVLQSCPNTKLVLGGYSQGSMVVHNAASNLDAATMSKISAVVLFGDPYYGKPVANFDAAKTLVVCHDGDNICQGGDIILLPHLTYAEDADTAAAFVVPLVS
Cutinase (EC 3.1.1.74)
Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei)
1,344,414
248
25,924
3D-structure;Disulfide bond;Hydrolase;Secreted;Serine esterase;Signal
GO:0005576; GO:0016052; GO:0050525
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000255|RuleBase:RU361263}.
SIGNAL 1..17; /evidence="ECO:0000255"
null
PF01083;
IPR029058;IPR000675;IPR043580;IPR043579;IPR011150;
4PSC;4PSD;4PSE;
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), Hypocreales (order), Hypocreaceae (family), Trichoderma (genus), Hypocrea jecorina (species)
M419DRAFT_76732
false
5
A0A024SH76
MIVGILTTLATLATLAASVPLEERQACSSVWGQCGGQNWSGPTCCASGSTCVYSNDYYSQCLPGAASSSSSTRAASTTSRVSPTTSRSSSATPPPGSTTTRVPPVGSGTATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAAAAVAKVPSFMWLDTLDKTPLMEQTLADIRTANKNGGNYAGQFVVYDLPDRDCAALASNGEYSIADGGVAKYKNYIDTIRQIVVEYSDIRTLLVIEPDSLANLVTNLGTPKCANAQSAYLECINYAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFANVYKNASSPRALRGLATNVANYNGWNITSPPSYTQGNAVYNEKLYIHAIGPLLANHGWSNAFFITDQGRSGKQPTGQQQWGDWCNVIGTGFGIRPSANTGDSLLDSFVWVKPGGECDGTSDSSAPRFDSHCALPDALQPAPQAGAWFQAYFVQLLTNANPSFL
Exoglucanase 2 (EC 3.2.1.91) (1,4-beta-cellobiohydrolase) (Cellobiohydrolase 6A) (Cel6A) (Exocellobiohydrolase II) (CBHII) (Exoglucanase II)
Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei)
1,344,414
471
49,653
Carbohydrate metabolism;Cellulose degradation;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Pyrrolidone carboxylic acid;Secreted;Signal
GO:0005576; GO:0016162; GO:0030245; GO:0030248
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07987}.
SIGNAL 1..18; /evidence="ECO:0000255"
null
PF00734;PF01341;
IPR016288;IPR036434;IPR035971;IPR000254;IPR001524;
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), Hypocreales (order), Hypocreaceae (family), Trichoderma (genus), Hypocrea jecorina (species)
cbh2 M419DRAFT_122470
false
6
A0A026W182
MMKMKQQGLVADLLPNIRVMKTFGHFVFNYYNDNSSKYLHKVYCCVNLFMLLLQFGLCAVNLIVESADVDDLTANTITLLFFTHSIVKICYFAIRSKYFYRTWAIWNNPNSHPLFAESNARYHAIALKKMRLLLFLVGGTTMLAAVAWTVLTFFEHPIRKIVDPVTNETEIIELPQLLIRSFYPFDAGKGITHVLVLVYQFYWVLFMLIDANSLDVLFCSWLLFACEQLQHLKQIMKPLMELSATLDTVVPNSSELFKAGSADHLRDGDNPPPPPPPQSDNMLDLDLRNIYSNRQDFTATFRPTAGMTFNGGVGPNGLTKKQEALVRSAIKYWVERHKHIVRLVTAVGDAYGFALLLHMLTTTITLTLLAYQATKVNGINVYAASTIGYILYTFGQVFLFCIFGNRLIEESTSVMEAAYSCHWYDGSEEAKTFVQIVCQQCQKAMSISGAKFFTVSLDLFASVLGAVVTYFMVLVQLK
Odorant receptor coreceptor
Ooceraea biroi (Clonal raider ant) (Cerapachys biroi)
2,015,173
478
54,109
Behavior;Cell membrane;Glycoprotein;Membrane;Olfaction;Receptor;Reference proteome;Sensory transduction;Transducer;Transmembrane;Transmembrane helix
GO:0004984; GO:0005549; GO:0005886; GO:0007165; GO:0007469; GO:0019236; GO:0035176; GO:0042048; GO:0043695; GO:0050911
Evidence at protein level
5
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
null
TRANSMEM 44..64; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 74..94; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 134..154; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 191..211; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 350..370; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 383..403; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 455..475; /note="Helical; Name=7"; /evidence="ECO:0000255"
PF02949;
IPR004117;
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), Hymenoptera (order), Apocrita (suborder), Aculeata (infraorder), Formicoidea (superfamily), Formicidae (family), Dorylinae (subfamily), Ooceraea (genus)
Orco X777_12371
false
7
A0A044RE18
MYWQLVRILVLFDCLQKILAIEHDSICIADVDDACPEPSHTVMRLRERNDKKAHLIAKQHGLEIRGQPFLDGKSYFVTHISKQRSRRRKREIISRLQEHPDILSIEEQRPRVRRKRDFLYPDIAHELAGSSTNIRHTGLISNTEPRIDFIQHDAPVLPFPDPLYKEQWYLNNGAQGGFDMNVQAAWLLGYAGRNISVSILDDGIQRDHPDLAANYDPLASTDINGHDDDPTPQDDGDNKHGTRCAGEVASIAGNVYCGVGVAFHAKIGGVRMLDGPVSDSVEAASLSLNRHHIDIYSASWGPEDDGRTFDGPGPLAREAFYRGVKAGRGGKGSIFVWASGNGGSRQDSCSADGYTTSVYTLSVSSATIDNRSPWYLEECPSTIATTYSSANMNQPAIITVDVPHGCTRSHTGTSASAPLAAGIIALALEANPNLTWRDMQHIVLRTANPVPLLNNPGWSVNGVGRRINNKFGYGLMDAGALVKLALIWKTVPEQHICTYDYKLEKPNPRPITGNFQMNFSLEVNGCESGTPVLYLEHVQVLATFRFGKRGDLKLTLFSPRGTSSVLLPPRPQDFNSNGIHKWPFLSVQTWGEDPRGKWTLMVESVSTNRNVGGTFHDWSLLLYGTAEPAQPNDPRHSSVVPSSVSAESPFDRITQHIASQEKKKKQRDSRDWQPKKVENKKSLLVSAQPELRV
Endoprotease bli (EC 3.4.21.75) (Blisterase)
Onchocerca volvulus
6,282
693
76,800
Autocatalytic cleavage;Calcium;Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen
GO:0000139; GO:0004252; GO:0005576; GO:0005634; GO:0005802; GO:0007635; GO:0031638; GO:0040002; GO:0045887; GO:0046872; GO:0090472; GO:1902075
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:12855702}.
SIGNAL 1..20; /evidence="ECO:0000255"
null
PF01483;PF00082;PF16470;
IPR008979;IPR034182;IPR002884;IPR000209;IPR036852;IPR023827;IPR022398;IPR023828;IPR015500;IPR032815;IPR038466;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Nematoda (phylum), Chromadorea (class), Rhabditida (order), Spirurina (suborder), Spiruromorpha (infraorder), Filarioidea (superfamily), Onchocercidae (family), Onchocerca (genus)
Bli
false
8
A0A059TC02
MRSVSGQVVCVTGAGGFIASWLVKILLEKGYTVRGTVRNPDDPKNGHLRELEGAKERLTLCKADLLDYQSLREAINGCDGVFHTASPVTDDPEQMVEPAVIGTKNVINAAAEANVRRVVFTSSIGAVYMDPNRDPETVVDETCWSDPDFCKNTKNWYCYGKMVAEQAAWEEAKEKGVDLVVINPVLVQGPLLQTTVNASVLHILKYLTGSAKTYANSVQAYVDVKDVALAHILLYETPEASGRYLCAESVLHRGDVVEILSKFFPEYPIPTKCSDVTKPRVKPYKFSNQKLKDLGLEFTPVKQCLYETVKSLQEKGHLPIPTQKDEPIIRIQP
Cinnamoyl-CoA reductase 1 (Ph-CCR1) (EC 1.2.1.44) (Coniferylaldehyde synthase) (Coumaroyl-CoA reductase) (Feruloyl-CoA reductase) (Sinapoyl-CoA reductase)
Petunia hybrida (Petunia)
4,102
333
36,886
3D-structure;Cytoplasm;Disulfide bond;Lignin biosynthesis;NADP;Nucleotide-binding;Oxidoreductase;Phenylpropanoid metabolism
GO:0000166; GO:0005737; GO:0007623; GO:0009699; GO:0009809; GO:0010597; GO:0016616; GO:0016621
Evidence at protein level
5
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24985707}.
null
null
PF01370;
IPR001509;IPR036291;IPR050425;
4R1S;4R1T;
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), Petunioideae (subfamily), Petunia (genus)
CCR1
false
9
A0A059WI14
MKYAHVGLNVTNLEKSIEFYSKLFGAEPVKVKPDYAKFLLESPGLNFTLNLRDEVNGNQVGHFGIQVESTEEVVAHKNRLAENGILSQYDEINTTCCYALQDKFWIHDPDGNEWEFFYTKTTVEENSTHPPTCCVNEPNVEKAECCSPTASSNKDTSNCCS
Trivalent organoarsenical cleaving enzyme (EC 1.13.11.-) (Arsenic inducible gene ArsI) (C-As lyase) (Methylarsonous acid demethylase) (MAs(III) demethylase)
Bacillus sp. (strain MD1)
1,501,233
161
18,109
Detoxification;Dioxygenase;Iron;Metal-binding;Oxidoreductase
GO:0008168; GO:0032259; GO:0046686
Evidence at protein level
5
null
null
null
PF00903;
IPR052393;IPR029068;IPR004360;IPR037523;IPR049789;
null
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Bacillaceae (family), Bacillus (genus), unclassified Bacillus (in: firmicutes) (no rank)
arsI
false
10
A0A060A682
MKFLAFGLIYFHFCILNRCEYITSSTIQKCYNSSNEPNNCSQKAVIVLSLENGQIANTEQVVATLNQLSDSGVNKQLQNSFIFEVTKSPVTALFPLIYLQDFNSQPLEQVIATTLFSCKDGFYDSSPTCKFQYDSKGQKILDSQGYCCYCSLSDILGMGNDLSRGKVCYALNLGAGSATAHCLKFSPLWYSAFKIQQYQLYFEVNINIYTVDSQNQKNLKQTLKLSTSNPTMKSSDNSTISKIIGTFTPTQPPADLSSYYLVKPSFPATDPRVLQGISSWMFVDKTMFTLDGTQCNKIGVSYSGFRQQSSSCSQPVGSCLQNQLENLYQSDLILLSQNKQPKYLLESQGNFNQVQFQGQTILQQGLSGSASTLITIEIDAAQIKFVTNLGIGCISQCSINNFESHSGNGKLVALVQNQGNYSAEFVLGFNCSSNVQPIQGQKLFLTANQLYNFNCSVSVNSDISAINNNCTINLYDAIGNQLDSKNILFNTTSTNHTSNQGNNTGQQQSSQEYKSSQSCSDKCSSFWSFWCYFSAGCIKEAFKSIASIAGVASALALVIFLAKNGYLVPIIRFLCCCCCKSKKKENEKNKDKTDKKSIQESCSYDRSCCSHSISQSYQVENKNKYKRSKIQRSFSSESCQDKSKKIINELSNLEETFEANKLYANIDKNSSIFEYFGFKKSFTFILYERNDILFLPQNSTILDMIGALQPQKGSYLAQKFLEIVNKNALKVVSTSPLYLLIE
Hapless 2 (Generative cell specific-1)
Tetrahymena thermophila
5,911
742
82,663
Cell junction;Cell membrane;Disulfide bond;Fertilization;Lipid-binding;Membrane;Signal;Transmembrane;Transmembrane helix
GO:0005886; GO:0005911; GO:0007338; GO:0008289; GO:0009566; GO:0045026; GO:0140522
Evidence at protein level
5
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:25155508, ECO:0000305|PubMed:28238660}; Single-pass type I membrane protein {ECO:0000255}. Cell junction {ECO:0000269|PubMed:25155508, ECO:0000269|PubMed:28238660}. Note=Detected at the mating junction. {ECO:0000269|PubMed:25155508, ECO:0000269|PubMed:28238660}.
SIGNAL 1..19; /evidence="ECO:0000255"
TRANSMEM 541..561; /note="Helical"; /evidence="ECO:0000255"
PF10699;
IPR040326;IPR018928;
null
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Ciliophora (phylum), Intramacronucleata (subphylum), Oligohymenophorea (class), Hymenostomatida (order), Tetrahymenina (suborder), Tetrahymenidae (family), Tetrahymena (genus)
HAP2 GCS1
false
11
A0A061ACU2
MTVPPLLKSCVVKLLLPAALLAAAIIRPSFLSIGYVLLALVSAVLPPIRKSLALPKLVGTFVIITFLFCLAVALGVGSYQISEQVVHKNDRTYICNRSDTTLFRSIGLVRFHPTGTFESTRAFLPEIIATSAALLTIIIVMFLSHRDEQLDVVGDVVTVRSESGREQRRQRKLAAIMWSAIGNSLRRLTNFVLFLFTAYVGIVKPSLSNSIYFLAFLFISTWWSTYTPLRHGVYNQIKKFLIFYSALHFLVLYTYQIPIVHHSWLPTGSFLPRLFGLTVLMDSSCPEWWKFPFVAPDFNDDDLIMKWPLYANPIVVLVFFYLTVAQYKFTRNGSREYIDDNEYGSSVHEERFVSAGTVETNVDDVGQLISISESTASAPSGRGRGNTLLLSNASSSANDDEQGRARSRSPLRNGEEQGSIPLRKVTSQVVDRNKLSNIFNTTAPGDKESAASKGMIAVMTFVIFHSYSIALTAMMTWALLYHSIFGLILLILTCILWIFRDTRKSSFAMAPIILMYIEFLLILQYFLSMDIHAEIGDPAWMNFVGIEWTTLPVHAVIILCVQTLLTLPVFLLLRLARREKFYESLSDYERQRRINSYGTFGASKTGAGGVAVAKFQDPKSRKFAAFVEYLSNKVSVYFIFVVSVVLLVVSTCFAPNFYNILFFALWALNLIYLKFSFRLYRGLAYAFWLTLTFYTSIVIIALYIYQFPGVSQWIIRNTSLSQEWLNAIGLVDFRAIGESGALFLQLLAPIALFVVTMLQLKFFHGPWSRATSPRRAENDPPTSTTEAAAVASTSGTQGRAHAAGDTLVKKLHKLANQTIELLWRFFEVHISKIVFVIIAIFIANNINALYIPLVILLSLAICLPSAADGIFSLFMCAYLFLVALSKMIYQLDIVPELSQIDRGVGADNCSHGNISMPEWFGLKKEVEGTEPIYMLFGVIVSIIALAFQSIVIYRQRHYRASLGLPESMRAKVFPDFHHSHFDRSLKNAIQFLIDYGFYKFGLEITMIAIGIDIFNRMDALAAIQCFWLVLFALNKRVFVRRIWVFYVIYMAILYPLQFFSYVGLPPDSCIEYPWSYWIPSYSDDARFNLSYLLNLSIYGVNWPSAYLIGDFFVLLLASCQLAVFRREGEDNDSIYNDGNFVIKPENPQYDFIDTKKSYVDYFKSFVFHYGHWITLMSTLAAGIAGTSLFALGYIIFTLTMLWSGNNLYVMNSTLRSFEHTLKRWNALLGYTLFTITMKVCLQIFGCVFLSWFDQSGGWGKTLCIVRQLFSITCVNNECHVLKELEDFSKACAVETKEGNIGFDVIALSFLVFQIRIFHSWYFQHCMVEYRSEVILANRGAVLKNQLIEKEMKEQNEQQKAKFNDIRRRTEAIRERYQKQIERGAAERDFEPVTYGHAKRAGDYYMFKYDPENDDLVEPVDSFVPEVDPKATAYDRLDPGQIMYAATAHDLDLAKTVQQVKKGDTIKDPDSRALIAVSEPEARKPGGTEETDGDEDEDNKDSKVESTAKFIQKMIASALDLCSVTLNKLCREHRYVGFVLSKEKQKLKSGHSESLSNTSRKLTDIRSAVDLPSLQLVQSANDVEKMETAVSVDWQQKSSATRLLNAVVNCIGAHTDILCYFFAIMTQVMTGGLITLPLPLMSLFWGNLSNPRPSKFFWVTMITYTECVIVIKFVCQFAFMPYNSITWRTEHQMDPMSLDKLFGVSQRDSFALWDIVLLFSLFFHRYMLRKLGLWKDANLTDTFTLKEEPRSASGSDTGSPKKIAQEPKVVVTQSDTLEGTSGGEIVIPSDPNAVSNMEELDCEPPIPEKQSGPIGRFIHQLFHPKFRYIRDLYPIMFGIDVICFLIMTFGYSAFGEGGSGNVLDDVKASRIPVTLVVMLVGMTLAIIIDRALYLRKSVVGKLIYQVLMIAFLHIWVFLVLPNMTRRSAISNHVAQALYVIKSCYFLVSAWQIRNGYPELCIGNLLTHSYGMTNMIAFKVFMNIPFLFELRTAIDWTWTDTSMPLFDFFNMENFYAHIFNIKCARQFEAAYPAPRGIPKGKLVKYMMGFPIIIGVVIFIFSPLLLWSLLNQIGTISMPEKVTLRISIEGYPPLYEMEAQGSNHDNAELGMIKPDQLASLNQALTDSYTTRDTNSILRSRMSVSYLKGYTYEDILIVRFRPESEIYWPISQDSRNAMIDKLSRNTSVNFEVSLEFTRPYDPNENAALKHSKSWLVPISLDMTIRAKIQSALRGDPGHPILIPQSIPAFIQVPNQGELTLPTSIGNTIINDGNPRINTTGMEKSDEARAWFDSLTLNLEQGKSQNEKMWIATSEHPGDQNAKLWIKTANTTYSGRPYLQVVGFIDRAFPSFLAKVFKGGVIAVYLSVILVVGRGLVRGIFTTSPSTVMFTELPNADHLLKICLDIYLVREAKDFMLEQDLFAKLIFLFRSPATLIEWTRMSKKKQE
Piezo-type mechanosensitive ion channel component 1
Caenorhabditis elegans
6,239
2,442
276,793
3D-structure;Alternative initiation;Alternative splicing;Cell membrane;Glycoprotein;Ion channel;Ion transport;Membrane;Reference proteome;Transmembrane;Transmembrane helix;Transport
GO:0005261; GO:0005886; GO:0008381; GO:0009612; GO:0030317; GO:0042391; GO:0050982; GO:0060279; GO:0071260; GO:0090727; GO:0098655
Evidence at protein level
5
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32490809}; Multi-pass membrane protein {ECO:0000255}.
null
TRANSMEM 6..26; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 28..48; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 57..77; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 123..143; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 174..196; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 199..219; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 240..260; /note="Helical; Name=7"; /evidence="ECO:0000255"; TRANSMEM 304..324; /note="Helical; Name=8"; /evidence="ECO:0000255"; TRANSMEM 455..475; /note="Helical; Name=9"; /evidence="ECO:0000255"; TRANSMEM 479..499; /note="Helical; Name=10"; /evidence="ECO:0000255"; TRANSMEM 507..527; /note="Helical; Name=11"; /evidence="ECO:0000255"; TRANSMEM 553..573; /note="Helical; Name=12"; /evidence="ECO:0000255"; TRANSMEM 634..654; /note="Helical; Name=13"; /evidence="ECO:0000255"; TRANSMEM 657..677; /note="Helical; Name=14"; /evidence="ECO:0000255"; TRANSMEM 684..704; /note="Helical; Name=15"; /evidence="ECO:0000255"; TRANSMEM 740..760; /note="Helical; Name=16"; /evidence="ECO:0000255"; TRANSMEM 833..853; /note="Helical; Name=17"; /evidence="ECO:0000255"; TRANSMEM 875..895; /note="Helical; Name=18"; /evidence="ECO:0000255"; TRANSMEM 932..952; /note="Helical; Name=19"; /evidence="ECO:0000255"; TRANSMEM 991..1011; /note="Helical; Name=20"; /evidence="ECO:0000255"; TRANSMEM 1013..1033; /note="Helical; Name=21"; /evidence="ECO:0000255"; TRANSMEM 1042..1062; /note="Helical; Name=22"; /evidence="ECO:0000255"; TRANSMEM 1097..1117; /note="Helical; Name=23"; /evidence="ECO:0000255"; TRANSMEM 1161..1181; /note="Helical; Name=24"; /evidence="ECO:0000255"; TRANSMEM 1188..1210; /note="Helical; Name=25"; /evidence="ECO:0000255"; TRANSMEM 1232..1252; /note="Helical; Name=26"; /evidence="ECO:0000255"; TRANSMEM 1300..1320; /note="Helical; Name=27"; /evidence="ECO:0000255"; TRANSMEM 1616..1636; /note="Helical; Name=28"; /evidence="ECO:0000255"; TRANSMEM 1655..1675; /note="Helical; Name=29"; /evidence="ECO:0000255"; TRANSMEM 1707..1727; /note="Helical; Name=30"; /evidence="ECO:0000255"; TRANSMEM 1834..1854; /note="Helical; Name=31"; /evidence="ECO:0000255"; TRANSMEM 1867..1887; /note="Helical; Name=32"; /evidence="ECO:0000255"; TRANSMEM 1901..1921; /note="Helical; Name=33"; /evidence="ECO:0000255"; TRANSMEM 1931..1951; /note="Helical; Name=34"; /evidence="ECO:0000255"; TRANSMEM 2047..2067; /note="Helical; Name=35"; /evidence="ECO:0000255"; TRANSMEM 2347..2367; /note="Helical; Name=36"; /evidence="ECO:0000255"
PF12166;PF24874;PF24871;PF15917;PF23188;
IPR027272;IPR031334;IPR056770;IPR056769;IPR031805;IPR056768;
4PKE;4PKX;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Nematoda (phylum), Chromadorea (class), Rhabditida (order), Rhabditina (suborder), Rhabditomorpha (infraorder), Rhabditoidea (superfamily), Rhabditidae (family), Peloderinae (subfamily), Caenorhabditis (genus)
pezo-1 C10C5.1
false
12
A0A061I403
MPMASVIAVAEPKWISVWGRFLWLTLLSMALGSLLALLLPLGAVEEQCLAVLRSFHLLRSKLDRTQHVVTKCTSPSTELSVTSGDVGLLTVKTKTSPAGKLEAKAALNQALEMKRQGKREKAHKLFLHALKMDPGFVDALNEFGIFSEEEKDIIQADYLYTRALTISPFHEKALVNRDRTLPLVEEIDQRYFSIIDSKVKKVMSIPKGSSALRRVMEETYYHHIYHTVAIEGNTLTLSEIRHILETRYAVPGKSLEEQNEVIGMHAAMKYINTTLVSRIGSVTIDDMLEIHRRVLGYVDPVEAGRFRRTQVLVGHHIPPHPRDVEKQMQEFTQWLNSEDAMNLHPVEFAALAHYKLVYIHPFIDGNGRTSRLLMNLILMQAGYPPITILKEQRSEYYHVLEVANEGDVRPFIRFIAKCTEVTLDTLLLATTEYSVALPEAQPNHSGLKETLPVRP
Protein adenylyltransferase FICD (EC 2.7.7.108) (AMPylator FICD) (De-AMPylase FICD) (EC 3.1.4.-) (FIC domain-containing protein) (Huntingtin-interacting protein E)
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
10,029
455
51,477
ATP-binding;Endoplasmic reticulum;Glycoprotein;Hydrolase;Magnesium;Manganese;Membrane;Nucleotide-binding;Nucleotidyltransferase;Phosphoprotein;Reference proteome;Repeat;Signal-anchor;TPR repeat;Transferase;Transmembrane;Transmembrane helix;Unfolded protein response
GO:0005524; GO:0005789; GO:0006986; GO:0018117; GO:0030544; GO:0034976; GO:0042803; GO:0044602; GO:0044603; GO:0051087; GO:0070733; GO:1903894
Evidence at protein level
5
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BVA6}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9BVA6}.
null
TRANSMEM 21..41; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255"
PF02661;
IPR003812;IPR036597;IPR040198;IPR011990;
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), Cricetidae (family), Cricetinae (subfamily), Cricetulus (genus)
FICD HYPE H671_4g11989 I79_014982
false
13
A0A067CMC7
MLEVPVWIPILAFAVGLGLGLLIPHLQKPFQRFSTVNDIPKEFFEHERTLRGKVVSVTDGDTIRVRHVPWLANGDGDFKGKLTETTLQLRVAGVDCPETAKFGRTGQPFGEEAKAWLKGELQDQVVSFKLLMKDQYSRAVCLVYYGSWAAPMNVSEELLRHGYANIYRQSGAVYGGLLETFEALEAEAREKRVNIWSLDKRETPAQYKARK
Endonuclease Htp3 (EC 3.1.31.-) (Host targeting protein 3) (RxLR effector protein Htp3)
Saprolegnia parasitica (strain CBS 223.65)
695,850
211
23,841
Calcium;Endonuclease;Glycoprotein;Host cytoplasm;Hydrolase;Metal-binding;Nuclease;Reference proteome;Secreted;Signal;Virulence
GO:0004519; GO:0005576; GO:0005737; GO:0044164; GO:0046872
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29904064}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:29904064}. Note=Uptake into host cells is more efficient at a lower pH of 5.5. S.parasitica acidifies the pH of its environment, which likely leads to the exposure of a gp96 protein to the host cell surface. The gp96 protein is working as a receptor and mediates the translocation of Htp3 via lipid rafts into the cell. Finally, Htp3 is released from vesicles with the help of other effector proteins, such as Htp1, into the cytosol where it is functionally active as a nuclease. {ECO:0000269|PubMed:29904064}.
SIGNAL 1..20; /evidence="ECO:0000255"
null
PF00565;
IPR035437;IPR016071;
null
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Stramenopiles (clade), Oomycota (phylum), Saprolegniales (order), Saprolegniaceae (family), Saprolegnia (genus), Saprolegnia parasitica (species)
HTP3 SPRG_03573
false
14
A0A067XGX8
MALTATATTRGGSALPNSCLQTPKFQSLQKPTFISSFPTNKKTKPRTKHISAVQSPPSTTKWNLESWKTKPAFQLPDYPDKVELESVLKTLSTYPPIVFAGEARNLEEKLGEAALGNAFLLQGGDCAESFKEFSANNIRDTFRVMLQMGVVLMFGGQMPVIKVGRMAGQFAKPRSDPFEEKDGVKLPSYRGDNVNGDAFDEKSRIPDPHRMVRAYTQSVATLNLLRAFASGGYAAMQRVNQWNLDFTDQSEQGDRYRELAHRVDEAMGFMTAAGLTVDHTIMTTTDFWTSHECLLLPYEQALTREDSTSGLYYDCSAHMIWVGERTRQLDGAHVEFLRGIANPLGIKVSHKMDPDELVKLIDILNPQNKPGRITVITRMGADNMRVKLPHLIRAVRGAGQIVTWVSDPMHGNTTKAPCGLKTRSFDSIRAELRAFFDVHEQEGSYPGGVHLEMTGQNVTECVGGSRTITYNDLSSRYHTHCDPRLNASQALELAFAIAERLRRRRLGPKFSL
Phospho-2-dehydro-3-deoxyheptonate aldolase 2, chloroplastic (EC 2.5.1.54) (3-deoxy-D-arabino-heptulosonate 7-phosphate synthase 2) (DAHP synthase 2) (PhDAHP2) (Phospho-2-keto-3-deoxyheptonate aldolase 2)
Petunia hybrida (Petunia)
4,102
512
57,062
Amino-acid biosynthesis;Aromatic amino acid biosynthesis;Chloroplast;Manganese;Metal-binding;Plastid;Transferase;Transit peptide
GO:0003849; GO:0008652; GO:0009073; GO:0009423; GO:0009507; GO:0046872
Evidence at transcript level
5
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:24815009}.
null
null
PF01474;
IPR013785;IPR002480;
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), Petunioideae (subfamily), Petunia (genus)
DAHP2 DHS2
false
15
A0A067XH53
MALSTNSTTSSLLPKTPLVQQPLLKNASLPTTTKAIRFIQPISAIHSSDSSKNTPIVSAKPSSPPAATSTAAATAVTKQEWSIDSWKTKKALQLPEYPNQEELKNVLKTIEDFPPIVFAGEARHLEEKLGEAAMGRAFLLQGGDCAESFKEFNANNIRDTFRILLQMGAVLMFGGQMPVIKVGRMAGQFAKPRSDNFEEKNGVKLPSYRGDNVNGDAFDLKSRTPDPQRLIRAYCQSAATLNLLRAFATGGYAAMQRVTQWNLDFTEHSEQGDRYRELANRVDEALGFMNAAGLTTDHPIMTTTEFWTSHECLLLPYEQSLTRLDSTSGLYYDCSAHFLWVGERTRQLDGAHVEFLRGIANPLGIKVSDKMDPSALVKLIEILNPQNKAGRITIITRMGAENMRVKLPHLIRAVRGAGQIVTWVSDPMHGNTIKAPCGLKTRPFDSIRAEVRAFFDVHEQEGSHPGGVHLEMTGQNVTECIGGSRTVTFDDLSSRYHTHCDPRLNASQSLELAFIIAERLRKRRLGSQSVLGQ
Phospho-2-dehydro-3-deoxyheptonate aldolase 1, chloroplastic (EC 2.5.1.54) (3-deoxy-D-arabino-heptulosonate 7-phosphate synthase 1) (DAHP synthase 1) (PhDAHP1) (Phospho-2-keto-3-deoxyheptonate aldolase 1)
Petunia hybrida (Petunia)
4,102
533
58,894
Amino-acid biosynthesis;Aromatic amino acid biosynthesis;Chloroplast;Manganese;Metal-binding;Plastid;Transferase;Transit peptide
GO:0003849; GO:0008652; GO:0009073; GO:0009423; GO:0009507; GO:0010597; GO:0046872
Evidence at transcript level
5
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:24815009}.
null
null
PF01474;
IPR013785;IPR002480;
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), Petunioideae (subfamily), Petunia (genus)
DAHP1 DAHPS DHS1
false
16
A0A067XR63
MNAEGGNLHREFEITWGDGRARIHNNGGLLTLSLDRASGSGFRSKNEYLFGRIEIQIKLVAGNSAGTVATYYLSSEGPTHDEIDFEFLGNSSGEPYTLHTNVFSQGKGNREQQFFLWFDPTMDFHTYTILWNPQRIIFYVDETPIREFKNLERHGIPFPRSQAMRVYSSMWNADDWATRGGLVKTDWTKAPFTASYRSYKADACVWSGEASSCGSQDSNPSDKWWMTEELNATRMKRLRWVQKKYMVYNYCVDKMRFPEGLAPECNIS
Xyloglucan endotransglucosylase protein 7 (XET protein 7) (EC 2.4.1.207) (DkXTH7) (Xyloglucan endotransglucosylase/hydrolase protein 7) (XTH protein 7)
Diospyros kaki (Kaki persimmon) (Diospyros chinensis)
35,925
268
30,834
Cell wall biogenesis/degradation;Cytoplasm;Disulfide bond;Fruit ripening;Glycoprotein;Glycosidase;Glycosyltransferase;Hydrolase;Transferase
GO:0004553; GO:0005737; GO:0009835; GO:0010411; GO:0016762; GO:0048046; GO:0070726
Evidence at protein level
5
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27242828}. Note=Dispersed throughout the cell. {ECO:0000269|PubMed:27242828}.
null
null
PF00722;PF06955;
IPR044791;IPR008264;IPR013320;IPR000757;IPR008263;IPR010713;IPR016455;
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), Ericales (order), Ebenaceae (family), Diospyros (genus)
XTH7
false
17
A0A067XRK9
MASSLTLPMAMAFTLLALSFASAMGGSMNSSRFDELFQPSWAFDHFVYEGEVLKMKLDNYSGAGFSSKGKYLFGKVTVQIKLVEGDSAGTVTAFYMSSDGTNHNEFDFEFLGNTTGEPYLVQTNVYVNGVGNREQRLNLWFDPTKDFHSYSLLWNQRQVVFMVDETPIRVHSNLEHRGIPFPKDQPMGVYSSIWNADDWATQGGRIKTDWSHAPFVASYQGFAIDACECPAAVAATDNARRCSSSAEKQFWWDMPTLSELSLHQSHQLIWVRANHLVYDYCTDTARFPVTPAECEHHRH
Xyloglucan endotransglucosylase protein 6 (XET protein 6) (EC 2.4.1.207) (DkXTH6) (Xyloglucan endotransglucosylase/hydrolase protein 6) (XTH protein 6)
Diospyros kaki (Kaki persimmon) (Diospyros chinensis)
35,925
299
33,764
Apoplast;Cell wall;Cell wall biogenesis/degradation;Disulfide bond;Fruit ripening;Glycoprotein;Glycosidase;Glycosyltransferase;Hydrolase;Secreted;Signal;Transferase
GO:0004553; GO:0009835; GO:0010411; GO:0016762; GO:0042546; GO:0048046; GO:0071555
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:27242828}. Secreted, extracellular space, apoplast {ECO:0000255|RuleBase:RU361120}.
SIGNAL 1..25; /evidence="ECO:0000255|RuleBase:RU361120"
null
PF00722;PF06955;
IPR044791;IPR008264;IPR013320;IPR000757;IPR010713;IPR016455;
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), Ericales (order), Ebenaceae (family), Diospyros (genus)
XTH6
false
18
A0A067YMX8
MAASPYSIFAVQLLLLASWMLSSSSSNFNQDFNIAWGGGRARILNNGELVTLSLDKASGSGFRSKNLYLFGKIDMQLKLVPGNSAGTVTTYYLSSEGSVRDEIDFEFLGNLTGEPYTLHTNVYSHGKGEREQQFRLWFDPAADFHTYSILWNSKTIVFYVDQTPVREFKNMESIGVPYLRQPMRLFSSIWNADEWATRGGLIKTDWTQAPFTTSYRNFRADNACVWAAKASSCGLAAGGNAWLSVELDAKSRGRLRWVRRNQMIYDYCVDGKRFPRGVPPECKLNLHI
Xyloglucan endotransglucosylase protein 8 (XET protein 8) (EC 2.4.1.207) (DkXTH8) (Xyloglucan endotransglucosylase/hydrolase protein 8) (XTH protein 8)
Diospyros kaki (Kaki persimmon) (Diospyros chinensis)
35,925
288
32,526
Apoplast;Cell wall;Cell wall biogenesis/degradation;Disulfide bond;Fruit ripening;Glycoprotein;Glycosidase;Glycosyltransferase;Hydrolase;Secreted;Signal;Transferase
GO:0004553; GO:0009737; GO:0009835; GO:0016762; GO:0030247; GO:0042546; GO:0048046; GO:0071370; GO:0071555; GO:2000899
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:27966647}. Secreted, extracellular space, apoplast {ECO:0000255|RuleBase:RU361120}.
SIGNAL 1..25; /evidence="ECO:0000255|RuleBase:RU361120"
null
PF00722;PF06955;
IPR044791;IPR013320;IPR000757;IPR008263;IPR010713;IPR016455;
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), Ericales (order), Ebenaceae (family), Diospyros (genus)
XTH8
false
19
A0A068J840
MKSELIFLPAPAIGHLVGMVEMAKLFISRHENLSVTVLIAKFYMDTGVDNYNKSLLTNPTPRLTIVNLPETDPQNYMLKPRHAIFPSVIETQKTHVRDIISGMTQSESTQVVGLLADLLFINIMDIANEFNVPTYVYSPAGAGHLGLAFHLQTLNDKKQDVTEFRNSDTELLVPSFANPVPAEVLPSMYVDKEGGYDYLFSLFRRCRESKAIIINTFEELEPYAINSLRMDSMIPPIYPVGPILNLNGDGQNSDEAAVILGWLDDQPPSSVVFLCFGSYGSFQENQVKEIAMGLERSGHRFLWSLRPSIPKGETKLQLKYSNLKEILPVGFLDRTSCVGKVIGWAPQVAVLGHESVGGFLSHCGWNSTLESVWCGVPVATWPMYGEQQLNAFEMVKELGIAVEIEVDYKKDYFNMKNDFIVRAEEIETKIKKLMMDENNSEIRKKVKEMKEKSRAAMSENGSSYNSLAKLFEEIM
UDP-glycosyltransferase 1 (UGTPg1) (EC 2.4.1.363)
Panax ginseng (Korean ginseng)
4,054
475
53,374
Glycosyltransferase;Isoprene biosynthesis;Transferase
GO:0016114; GO:0035251
Evidence at protein level
5
null
null
null
PF00201;
IPR050481;IPR002213;IPR035595;
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), Apiales (order), Apiineae (suborder), Araliaceae (family), Panax (genus)
UGT1
false
20
A0A068Q5Q5
MALIRLVAPERVFSDLASMVAYPNFQVQDKITLLGSAGGDFTFTTTASVVDNGTVFAVPGGYLLRKFVGPAYSSWFSNWTGIVTFMSAPNRHLVVDTVLQATSVLNIKSNSTLEFTDTGRILPDAAVARQVLNITGSAPSVFVPLAADAAAGSKVITVAAGALSAVKGTYLYLRSNKLCDGGPNTYGVKISQIRKVVGVSTSGGVTSIRLDKALHYNYYLSDAAEVGIPTMVENVTLVSPYINEFGYDDLNRFFTSGISANFAADLHIQDGVIIGNKRPGASDIEGRSAIKFNNCVDSTVKGTCFYNIGWYGVEVLGCSEDTEVHDIHAMDVRHAISLNWQSTADGDKWGEPIEFLGVNCEAYSTTQAGFDTHDIGKRVKFVRCVSYDSADDGFQARTNGVEYLNCRAYRAAMDGFASNTGVAFPIYRECLAYDNVRSGFNCSYGGGYVYDCEAHGSQNGVRINGGRVKGGRYTRNSSSHIFVTKDVAETAQTSLEIDGVSMRYDGTGRAVYFHGTVGIDPTLVSMSNNDMTGHGLFWALLSGYTVQPTPPRMSRNLLDDTGIRGVATLVAGEATVNARVRGNFGSVANSFKWVSEVKLTRLTFPSSAGALTVTSVAQNQDVPTPNPDLNSFVIRSSNAADVSQVAWEVYL
Depolymerase, capsule K1-specific (EC 4.-.-.-) (Gene product 34) (gp34) (K1-ORF34 protein) (Probable tail spike protein)
Klebsiella phage NTUH-K2044-K1-1 (Bacteriophage NTUH-K2044-K1-1)
1,194,091
651
69,928
3D-structure;Degradation of host capsule during virus entry;Degradation of host cell envelope components during virus entry;Host-virus interaction;Lyase;Reference proteome;Viral attachment to host adhesion receptor;Viral attachment to host cell;Viral tail protein;Virion;Virus entry into host cell
GO:0016829; GO:0098015; GO:0098671; GO:0098994; GO:0098996
Evidence at protein level
5
SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=Tail appendage. {ECO:0000305}.
null
null
PF24146;PF24145;PF24149;
IPR056204;IPR012334;IPR011050;
7W1C;7W1D;7W1E;
Viruses (no rank), Duplodnaviria (realm), Heunggongvirae (kingdom), Uroviricota (phylum), Caudoviricetes (class), Autographiviridae (family), Slopekvirinae (subfamily), Drulisvirus (genus), Drulisvirus K244 (species)
ORF34
false
21
A0A072ULZ1
MEENKKTVDGSVDFTEEQEALVVKSWNAMKNNSCDLSLKFFTKILEIAPPAKQMFSFLKDSNVPLEQNPKLKPHAMSVFLMTCESAVQLRKAGKVRVRESNLKKLGATHFKTGVQDEHFEVTKQALLETIEEAIPEMWSLAMKNAWAEAHDQLANAIKVEMKEAHDQMDNANLIINMEENTGSCFTEEQEALVVKSWNAIKYNSGDLSLKFFKKILEIAPPAKQLFSFLKDSNVPLEHNPKLKPHAMSVFLMTCESAVQLRKAGKVTVRESNLKKLGATHFKTGVKDEHFEVTKQALLETIKEALPEMWSPAMENAWGEAHDQLANAIKAEMKKTDHDHQTNVEDKSKPSS
Anaerobic nitrite reductase Glb1-2 (EC 1.7.2.-) (Non-symbiotic hemoglobin 1-2) (MtGlb1-2) (Phytoglobin 1.2) (Phytogb1.2)
Medicago truncatula (Barrel medic) (Medicago tribuloides)
3,880
351
39,609
Alternative splicing;Cytoplasm;Heme;Iron;Metal-binding;Nodulation;Nucleus;Oxidoreductase;Oxygen transport;Reference proteome;Repeat;Transport
GO:0001666; GO:0005344; GO:0005634; GO:0005737; GO:0009609; GO:0009877; GO:0010167; GO:0016491; GO:0019825; GO:0020037; GO:0046872; GO:0060359; GO:0071731
Evidence at protein level
5
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2XE98}. Nucleus {ECO:0000250|UniProtKB:A2XE98}.
null
null
PF00042;
IPR000971;IPR009050;IPR012292;IPR001032;IPR019824;
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), Fabales (order), Fabaceae (family), Papilionoideae (subfamily), 50 kb inversion clade (clade), NPAAA clade (clade), Hologalegina (clade), IRL clade (clade), Trifolieae (tribe), Medicago (genus)
Glb1-2 MTR_4g068870 Medtr4g068870 MtrunA17_Chr4g0034311
false
22
A0A072UR65
MANILNLKHLLTLALILLALATKSSTSSSSSITRVKGIYWLENPFFPPTTVDTSLFTHIFYSFLTPNNITYKLEISSSQILSLNTFTKTFKTKSPPAATLFSIGGAGSNSSLLAFIASDPPACAAFINSTIDVARTFGFDGIDLDWEFPKNTKEMNDLGEMLFQWRKAISDEGATTGRPPLLLTAAVYFAVNFSIYGEPRMYPVNSINENLDWVNVMSYELRGPRSNKTGAPSGTFDPKSNVSVVSGLLSWIHSGVVPEKLVMGMPLYGKSWKLRDPNVHGIGAPSVGSGPGVNGLMAYFQVLDFNRQKSAKVEYDVDTASVYSYSGSTWIGYDNPFTVSIKVGFAQALKLRGYFFWVAGLDTLDWKIATQASKAWKLV
Class V chitinase CHIT5b (MtCHIT5b) (EC 3.2.1.14)
Medicago truncatula (Barrel medic) (Medicago tribuloides)
3,880
379
41,526
Carbohydrate metabolism;Chitin degradation;Glycoprotein;Glycosidase;Hydrolase;Plant defense;Polysaccharide degradation;Reference proteome;Signal
GO:0000272; GO:0004568; GO:0005576; GO:0006032; GO:0008061; GO:0008843; GO:0050832
Evidence at protein level
5
null
SIGNAL 1..26; /evidence="ECO:0000255"
null
PF00704;
IPR011583;IPR029070;IPR001223;IPR001579;IPR017853;IPR050314;
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), Fabales (order), Fabaceae (family), Papilionoideae (subfamily), 50 kb inversion clade (clade), NPAAA clade (clade), Hologalegina (clade), IRL clade (clade), Trifolieae (tribe), Medicago (genus)
CHIT5B MTR_4g117000
false
23
A0A072VDF2
MPAATAAAAAESSSVSGETICVTGAGGFIASWMVKLLLEKGYTVRGTLRNPDDPKNGHLKKLEGAKERLTLVKVDLLDLNSVKEAVNGCHGVFHTASPVTDNPEEMVEPAVNGAKNVIIAGAEAKVRRVVFTSSIGAVYMDPNRSVDVEVDESCWSDLEFCKKTKNWYCYGKAVAEAAAWDVAKEKGVDLVVVNPVLVLGPLLQPTINASTIHILKYLTGSAKTYANATQAYVHVRDVALAHILVYEKPSASGRYLCAETSLHRGELVEILAKYFPEYPIPTKCSDEKNPRVKPHIFSNKKLKDLGLEFTPVSECLYETVKSLQDQGHLSIPNKEDSLAVKS
Cinnamoyl-CoA reductase 1 (Mt-CCR1) (EC 1.2.1.44) (Caffeoyl-CoA reductase) (EC 1.2.1.-) (Coumaroyl-CoA reductase) (Feruloyl-CoA reductase) (Sinapoyl-CoA reductase)
Medicago truncatula (Barrel medic) (Medicago tribuloides)
3,880
342
37,113
Cytoplasm;Disulfide bond;NADP;Oxidoreductase;Reference proteome
GO:0005737; GO:0009699; GO:0009809; GO:0016616; GO:0016621
Evidence at protein level
5
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A059TC02}.
null
null
PF01370;
IPR001509;IPR036291;IPR050425;
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), Fabales (order), Fabaceae (family), Papilionoideae (subfamily), 50 kb inversion clade (clade), NPAAA clade (clade), Hologalegina (clade), IRL clade (clade), Trifolieae (tribe), Medicago (genus)
CCR1 MTR_2g104960 MtrunA17_Chr2g0333781
false
24
A0A072VIM5
MSLEETLRSLSLDYLNLLINGQAFSDVTFQVEGRLVHAHRCILAARSLFFRKFFCGPDPPSGLDPIGGGSSRQPTVRPGVIPVNSVGYEVFLLLLQFLYSGQVSIVPQKHEPRPNCGERGCWHTHCTSAVDLALDTLAAARYFGVEQLALLTQKQLVSMVEKASIDDVMKVLIASRKQEMPQLWTTCSHLVAKSGLPPEILAKHLSIDVVAKIEELRLKSSLARRSLMPLHHHHHHHHHHDFGDLEDQKIRRMRRALDSSDVELVKLMVMGEGLNLDEALALHYAVENCSREVVKALLELGAADVNYPAGPAGKTSLHVAAEMVSPEMVAVLLDHHADPTVRTVDGVTPLDILRTLTSDFLFKGAVPGLNHIEPNKLRLCLELVQSAALVLSREENNASNNNNNNNNASSSAAPVYPPMSEDHSSSSSGNNNNNNNSIGNLNLDSRLVYLNLGATQMGGDDDNRHNNSHREAMNRQGGHGCDPSMYHHSHDF
BTB/POZ domain and ankyrin repeat-containing protein NOOT2 (Protein NODULE ROOT 2) (MtNOOT2)
Medicago truncatula (Barrel medic) (Medicago tribuloides)
3,880
492
54,118
ANK repeat;Cell membrane;Cytoplasm;Membrane;Metal-binding;Nodulation;Nucleus;Reference proteome;Repeat;Ubl conjugation pathway;Zinc;Zinc-finger
GO:0000976; GO:0005634; GO:0005737; GO:0005886; GO:0006355; GO:0008270; GO:0009864; GO:0009877; GO:0099402
Evidence at transcript level
5
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:G3LSH3}. Cytoplasm {ECO:0000250|UniProtKB:G3LSH3}. Cell membrane {ECO:0000250|UniProtKB:G3LSH3}; Peripheral membrane protein {ECO:0000250|UniProtKB:G3LSH3}; Cytoplasmic side {ECO:0000250|UniProtKB:G3LSH3}.
null
null
PF12796;PF00651;PF11900;
IPR002110;IPR036770;IPR000210;IPR044284;IPR024228;IPR011333;
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), Fabales (order), Fabaceae (family), Papilionoideae (subfamily), 50 kb inversion clade (clade), NPAAA clade (clade), Hologalegina (clade), IRL clade (clade), Trifolieae (tribe), Medicago (genus)
NOOT2 MTR_1g051025
false
25
A0A075BSX9
MTEKIYDAIVVGAGFSGLVAARELSAQGRSVLIIEARHRLGGRTHVVNFLGRPVEIGGAGVHWCQPHVFAEMQRYGFGFKEAPLADLDKAYMVFADGQKIDVPPATFDEEYTTAFEKFCSRSRELFPRPYSPLDNHEVSNLDGVSARDHLESLGLNELQLASMNAELTLYGGAPTTELSYPSFVKFHALASWDTITFTDSEKRYHVQGGTNALCQAIFDDCRADSEFGVPVEAVAQTDNGVTVTLADKRVFRALTCVLTLPTKVYADVRFEPPLPPEKRAFIEHAEMADGAELYVHVRQNLGNTFTFCDDPNPFNAVQTYAYDDELGTILKITIGRQSLINLENFDAIAAEIRKIHGDVEVLEALPYNWAMDEYARTSYPAMRKGWFSRYKDMAKPENRLFFAGSATADGWHEYIDGAIESGIRVGREIRHFMKATA
(S)-6-hydroxynicotine oxidase ((S)-6HN oxidase) (EC 1.5.3.5) (6-hydroxy-L-nicotine oxidase) (6-HLNO) (L-hydroxynicotine oxidase) (LHNO)
Shinella sp. (strain HZN7)
879,274
437
48,736
3D-structure;Alkaloid metabolism;FAD;Flavoprotein;Nucleotide-binding;Oxidoreductase;Plasmid
GO:0000166; GO:0009820; GO:0018531; GO:0019608
Evidence at protein level
5
null
null
null
PF01593;
IPR002937;IPR036188;IPR001613;IPR050703;
6CR0;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Alphaproteobacteria (class), Hyphomicrobiales (order), Rhizobiaceae (family), Shinella (genus), unclassified Shinella (no rank)
nctB shn_30305
false
26
A0A075D5I4
MAEKQQAVAEFYDNSTGAWEVFFGDHLHDGFYDPGTTATIAGSRAAVVRMIDEALRFANISDDPAKKPKTMLDVGCGIGGTCLHVAKKYGIQCKGITISSEQVKCAQGFAEEQGLEKKVSFDVGDALDMPYKDGTFDLVFTIQCIEHIQDKEKFIREMVRVAAPGAPIVIVSYAHRNLSPSEGSLKPEEKKVLKKICDNIVLSWVCSSADYVRWLTPLPVEDIKAADWTQNITPFYPLLMKEAFTWKGFTSLLMKGGWSAIKVVLAVRMMAKAADDGVLKFVAVTCRKSK
Picrinine-N-methytransferase (RsPiNMT) (EC 2.1.1.-) (Gamma-tocopherol-like methyltransferase PiNMT) (RsTLMT)
Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum)
4,060
290
31,987
Alkaloid metabolism;Membrane;Methyltransferase;S-adenosyl-L-methionine;Transferase;Vacuole
GO:0008170; GO:0008757; GO:0009705; GO:0009821; GO:0032259; GO:1900985
Evidence at protein level
5
SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:35166361}.
null
null
PF08241;
IPR050447;IPR013216;IPR025774;IPR029063;
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)
PiNMT Rs8692
false
27
A0A075D657
MYTCSIIIYILTFWQLSKIKKQVAAAEKQVMTVTEKQEAVAEFYDKSTDAWEVFFGEHLHDGFYEPGTTATIPGSKVAVVRMIDELLRFAGISDDPEKKPKTMLDVGCGLGGTCLHVAKKYDIKCTGITISPEQVKCAQDLAATQGLESKVSFDVGDALDMPYKDGTFDLVFTIQCIEHIQDKEKFIREMVRVAAPGAPVVIAGYAARNLSPSEESLKPEEKMVLEKICDHIVLSWLCSTGDYVKWLTPLPVQDIKVWDLTQNITPFYPLCIKEAFTWKSFTSLLKMGGWSAIKVVFAVKMMAMAAEEGLLKFAAVTCRKSK
Picrinine-N-methytransferase (VmPiNMT) (EC 2.1.1.-) (Gamma-tocopherol-like methyltransferase PiNMT) (VmTLMT)
Vinca minor (Common periwinkle)
60,093
322
35,867
Alkaloid metabolism;Cytoplasm;Methyltransferase;S-adenosyl-L-methionine;Transferase
GO:0005829; GO:0008170; GO:0008757; GO:0009821; GO:0032259; GO:1900985
Evidence at protein level
5
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:35166361}.
null
null
PF08241;
IPR050447;IPR013216;IPR025774;IPR029063;
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), Vincinae (subtribe), Vinca (genus)
PiNMT Vm130
false
28
A0A075F7E9
MVALLLFPMLLQLLSPTCAQTQKNITLGSTLAPQGPASSWLSPSGDFAFGFRPVEGNTSFYLIAVWFNKISDKTVVWYAKNTDQDPSIVEVPSDSFLQLTNDGALSLKDRSGQEGWNPQVTGVAYASMRDTGNFVLLGADGTTKWQTFDMPSDTILPTQVIPCNKTRNKSLRARLDIDDYSSGRFLLDVQTDGNLALYLVAVPSGSKYQQYWSTDTTGNGSELVFSETGKVYFALTDGTQINISSDAGIGSMADYFHRATLDPDGVFRQYVYPKKANAGILGGETWTALSMQPQNICHAIVSDVGSGVCGFNSYCTFDGTRNQIASCQCPPWYKFFDEQKKYKGCKQDFQPHSCDLEEATALAQFELRPIYGVDWPLSDYEKYEPIGQDDCGRLCVIECFCAMAVYNQSTSTCWKKKLPLSNGNMADYVQRTVLLKVPSSNSSQFMISTSSNKWKRNRKHWVLGSSLILGTSILVNFALISIFLFGTYCRITTKKNIPLSQASSKSQLPLKTFTYKELEKATAGFHEILGAGASGVVYKGQLEDELKTNIAVKTIHKLQPETEKEFMVEVETIGQTFHKNLVRLLGFCNERAERLLVYEFMTNGPLNRLLFDNSRPHWNTRVHIALGVARGFLYLHDECSKQIIHCDIKPQNILLDDNLVAKISDFGLAKLLLTNQTRTKTGIRGTRGYVAPEWFKNIGISTKVDVYSFGVILLELVCCRRNVELEVVDEEQTIVTYWANDCYRSGRIDLLVEGDDEAIYDIKKVERFVTVALWCLQEDPSMRPNMLKVTQMLDGAVAIPSPPDPCSFISSLP
G-type lectin S-receptor-like serine/threonine-protein kinase LECRK1 (OsLecRK1) (EC 2.7.11.1) (OsRLCK134)
Oryza sativa subsp. indica (Rice)
39,946
813
90,770
ATP-binding;Disulfide bond;EGF-like domain;Glycoprotein;Kinase;Lectin;Membrane;Nucleotide-binding;Plant defense;Receptor;Reference proteome;Serine/threonine-protein kinase;Signal;Transferase;Transmembrane;Transmembrane helix
GO:0004674; GO:0005524; GO:0006952; GO:0016020; GO:0030246; GO:0051707; GO:0106310
Evidence at protein level
5
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
SIGNAL 1..19; /evidence="ECO:0000255"
TRANSMEM 467..487; /note="Helical"; /evidence="ECO:0000255"
PF01453;PF00069;
IPR001480;IPR036426;IPR051343;IPR011009;IPR000719;IPR017441;IPR008271;IPR024171;
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), Liliopsida (clade), Petrosaviidae (subclass), commelinids (clade), Poales (order), Poaceae (family), BOP clade (clade), Oryzoideae (subfamily), Oryzeae (tribe), Oryzinae (subtribe), Oryza (genus), Oryza sativa (species)
LECRK1 LECRK OsI_14840
false
29
A0A075F932
MVSESHHEALAAPPATTVAAAPPSNVTEPASPGGGGGKEDAFSKLKEKFMNELNKIPLPPWALIAIAIVAVLLILTCCFCLCKKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQDDDAETGLTDGEEKEEPKEVEKLGKIQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKYETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEYKVAMNTVDFGHVTEEWRDLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQIVVTVLDYDKIGKNDAIGKVFVGYNSTGAELRHWSDMLANPRRPIAQWHTLQPEEEVDAMLAVKK
Synaptotagmin-1 (Synaptotagmin I) (SytI)
Anser cygnoides (Swan goose)
8,845
421
47,208
Calcium;Cytoplasm;Cytoplasmic vesicle;Differentiation;Glycoprotein;Lipoprotein;Membrane;Metal-binding;Palmitate;Reference proteome;Repeat;Synapse;Transmembrane;Transmembrane helix
GO:0000149; GO:0001786; GO:0005509; GO:0005543; GO:0005544; GO:0005737; GO:0005886; GO:0008021; GO:0017158; GO:0030154; GO:0030276; GO:0030424; GO:0030672; GO:0031045; GO:0042584; GO:0046883; GO:0048488; GO:0048791; GO:0051592; GO:1903305; GO:1903861
Evidence at transcript level
5
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P21707}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:P21707}; Single-pass membrane protein {ECO:0000250|UniProtKB:P21707}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane {ECO:0000250|UniProtKB:P21707}; Single-pass membrane protein {ECO:0000250|UniProtKB:P21707}. Cytoplasm {ECO:0000250|UniProtKB:P21707}. Note=Synaptic vesicles and chromaffin granules. {ECO:0000250|UniProtKB:P21707}.
null
TRANSMEM 61..81; /note="Helical"; /evidence="ECO:0000255"
PF00168;
IPR000008;IPR035892;IPR001565;
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), Sauropsida (clade), Sauria (clade), Archelosauria (clade), Archosauria (clade), Dinosauria (clade), Saurischia (clade), Theropoda (clade), Coelurosauria (clade), Aves (class), Neognathae (infraclass), Galloanserae (superorder), Anseriformes (order), Anatidae (family), Anserinae (subfamily), Anser (genus)
SYT1
false
30
A0A075FBG7
MSITFNLKIAPFSGPGIQRSKETFPATEIQITASTKSTMTTKCSFNASTDFMGKLREKVGGKADKPPVVIHPVDISSNLCMIDTLQSLGVDRYFQSEINTLLEHTYRLWKEKKKNIIFKDVSCCAIAFRLLREKGYQVSSDKLAPFADYRIRDVATILELYRASQARLYEDEHTLEKLHDWSSNLLKQHLLNGSIPDHKLHKQVEYFLKNYHGILDRVAVRRSLDLYNINHHHRIPDVADGFPKEDFLEYSMQDFNICQAQQQEELHQLQRWYADCRLDTLNYGRDVVRIANFLTSAIFGEPEFSDARLAFAKHIILVTRIDDFFDHGGSREESYKILDLVQEWKEKPAEEYGSKEVEILFTAVYNTVNDLAEKAHIEQGRCVKPLLIKLWVEILTSFKKELDSWTEETALTLDEYLSSSWVSIGCRICILNSLQYLGIKLSEEMLSSQECTDLCRHVSSVDRLLNDVQTFKKERLENTINSVGLQLAAHKGERAMTEEDAMSKIKEMADYHRRKLMQIVYKEGTVFPRECKDVFLRVCRIGYYLYSSGDEFTSPQQMKEDMKSLVYQPVKIHPLEAINV
9,13-epoxylabda-14-ene synthase, chloroplastic (EC 4.2.3.189) (Manoyl oxide synthase) (EC 4.2.3.190) (Miltiradiene synthase) (EC 4.2.3.131)
Marrubium vulgare (White horehound)
41,230
580
67,098
Chloroplast;Lyase;Magnesium;Metal-binding;Plastid;Transit peptide
GO:0000287; GO:0009507; GO:0009686; GO:0010333; GO:0062205; GO:0062206; GO:0106239; GO:1901946
Evidence at protein level
5
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
null
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), Lamioideae (subfamily), Marrubieae (tribe), Marrubium (genus)
ELS
false
31
A0A075QQ08
MVDEVEKPASLEESKTNTREVEEGAEEVIESDDTMSSLGNPCKAMKHPLEHSWTFWFDNPSGKSKQAAWGSSIRPIYTFSTVEDFWSVYNNIHHPSKLAVGADFHCFKNKIEPKWEDPVCASGGKWTMSFSRGKSDTCWLYTLLAMIGEQFDCGDEICGAVINVRVRQEKIALWTRNAANETAQVSIGKQWKEFLDYNDSIGFIFHDDAKKLDRAAKNRYSV
Eukaryotic translation initiation factor 4E-1 (NteIF4E1) (eIF4E-1) (Eukaryotic translation initiation factor 4E2-T) (eIF4E2-T) (eIF-4F 25 kDa subunit) (eIF-4F p26 subunit) (mRNA cap-binding protein)
Nicotiana tabacum (Common tobacco)
4,097
222
25,217
Cytoplasm;Disulfide bond;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 transcript level
5
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:K0P2S0}. Cytoplasm {ECO:0000250|UniProtKB:K0P2S0}.
null
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), Nicotianoideae (subfamily), Nicotianeae (tribe), Nicotiana (genus)
eIF4E EIF4E2-T T015277 LOC107829212
false
32
A0A075TJ05
MVRRIASATPMVQSPMSPLGTTYCVRPNPVSLNLQRRPLVIASTDEAKVTIIYAGLLIPGDGEPLRNAALVISDKIIAFVGSEADIPKKYLRSTQSTHRVPVLMPGLWDCHMHFGGDDDYYNDYTSGLATHPASSGARLARGCWEALQNGYTSYRDLAGYGCEVAKAINDGTIVGPNVYSSGAALSQTAGHGDIFALPAGEVLGSYGVMNPRPGYWGAGPLCIADGVEEVRRAVRLQIRRGAKVIKVMASGGVMSRDDNPNFAQFSPEELKVIVEEAARQNRIVSAHVHGKAGIMAAIKAGCKSLEHVSYADEEVWELMKEKGILYVATRSVIEIFLASNGEGLVKESWAKLQALADSHLKAYQGAIKAGVTIALGTDTAPGGPTALELQFAVERGGMTPLEAIKAATANAPLSVGPQAPLTGQLREGYEADVIALEENPLEDIKVFQEPKAVTHVWKGGKLFKGPGIGPWGEDARNPFL
Ochratoxinase (OTase) (EC 3.4.17.-) (Amidohydrolase 2) (Amidase 2) (Carboxypeptidase Am2)
Aspergillus niger
5,061
480
51,200
Carboxypeptidase;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Zinc
GO:0004180; GO:0005576; GO:0006508; GO:0008237; GO:0016810; GO:0046872
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24947135}.
null
null
PF01979;
IPR006680;IPR011059;IPR032466;IPR051781;
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)
Am2
false
33
A0A075TMP0
MASTTPSTYKQAVFKEQGAGLTLEEVALTLPKRDEILVKVEACGVCHSDHFAQTNLMGGGFPLVPGHEIIGRVAAVGEGETVWKEGDRIGGAWHGGHDGTCGACKKGFFQMCDNEQVNGISRNGGYAEYCIIRREAAVHIPDHVNAAKYAPMLCAGVTVFNAMRHMKIPPGELVAIQGLGGLGHLALQYANKFGYRVVALSRDSTKEEFARKLGAHEYIDTSREDPVAALQKLGGASLIVSTAPVPEIINPLIQGLGVMGKLLILSIVGGIEVHTGLLVGKGKSIWSWPSGHATDSEDAIAFADLHGIDCLIEEFPLDKCNEAFAAMMEGSVRFRAVITM
Alcohol dehydrogenase patD (EC 1.1.1.-) (Patulin biosynthesis cluster protein D)
Penicillium expansum (Blue mold rot fungus)
27,334
340
36,280
Cytoplasm;Metal-binding;NAD;NADP;Oxidoreductase;Reference proteome;Zinc
GO:0004022; GO:0005829; GO:0008106; GO:0016218; GO:0016491; GO:0046872; GO:0140723
Evidence at protein level
5
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}.
null
null
PF08240;PF00107;
IPR013149;IPR013154;IPR011032;IPR036291;IPR020843;
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)
patD PEX2_082780
false
34
A0A075TMP8
MDILQLAPTHLLAILLSSTSALFLITYLLRAGHRPSDLPNGPPTVPLFGNELQVPKSDAHFQFSRWAKEYGGFFTLKRYNNTTIVISDQKLIKTLLDKKSNIYSHRPASLVSHLITQSDHLLVMQYGERWRMLRKTIHQYFMEPRCERDHWKVQEAEAKQMLHDYLTMPEDHMLHPKRYSNSITNSLVFGIRTKTVHDEYMKKLFYLMDKWSLVQELGATPPVDSFALLRYVPQWMLGNWRNRAVEVGDLMQSLYQTVLDQVKERRQRGIQRDSFMDRVLDTLKQTPLSENELRFLGGVLMEGGSDTSSSLILTIIQAMTKYPEVQAKAHAQIDSIIGHNRSPAWSDWSKLPYINMIIKESHRWRPVSPLGVPHAVAEDDHIDGKLIPQGSSIVLNVWGMHHDSDRWQEPEHFQPERFADFPALASGYAGSERRDHLGYGAGRRICPGIHLAERNLIIGIAKLLWAFEFLEPLGSDSDISAHSGASKGFLHCPKDYGCVIRLRSPEKRETIMREFAEAQEVFARFD
Cytochrome P450 monooxygenase patI (EC 1.-.-.-) (Patulin biosynthesis cluster protein I) (m-hydroxybenzyl alcohol hydroxylase)
Penicillium expansum (Blue mold rot fungus)
27,334
526
60,437
Endoplasmic reticulum;Glycoprotein;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Reference proteome;Transmembrane;Transmembrane helix
GO:0004497; GO:0005506; GO:0005783; GO:0005789; GO:0016218; GO:0016705; GO:0020037; GO:0140723
Evidence at protein level
5
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30680886}; Single-pass membrane protein {ECO:0000269|PubMed:30680886}.
null
TRANSMEM 7..29; /note="Helical"; /evidence="ECO:0000255"
PF00067;
IPR001128;IPR002401;IPR036396;IPR050364;
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)
patI PEX2_082860
false
35
A0A075TR33
MRLHQSPPRLLVCILSVLQVSAGLSSNCRCMPGDSCWPSLNDWARFNTSIGGRLVDTQPLGQPCHDPFYTASECNELKQQWTHPELHDASSSSIMSAAVANETCDAFTPRSKPCTLGAMVRYAVNASSPDDFVQTIRFSQERNIRLVIRNTGHDYAGKSTGAGALSIWTHSLKEIDFLNYTSAHYTGPAVRMTAGIQGTDINPAAHKKGLVIVGGECATVGPVGGFTQGGGHSALSSRFGLAADQVLEWEVVDGMGRLLTASPTQNPDLYWALSGGGGGTFGVVYAVTVKTFPDFAVTGVVLQFENIDPSSNRFFEAVGHYHRHLPTYTSAGGMAIAQITNSSFLLTPLTLPAYTAAATKKLLGPFLQDLHQLNISYTLNVTESASYFQHYMKLIEPNPTQLVQNAQYGGRLLPLDLIERNNSQLTDAVQKLTADGVTFVGIGLNVSSSVTGDIWNSVLPGWRTAAMTVILTTSWPLGANLTKMKILADKMTTKWVPILTALSPESGCYMSEADPQQPDWKQTFYGRNYDSLYAIKTKYDPLQTFYATTAVGSEDWQVEAGGRLCQATRKN
FAD-linked oxidoreductase patO (EC 1.-.-.-) (Patulin biosynthesis cluster protein O)
Penicillium expansum (Blue mold rot fungus)
27,334
571
61,945
FAD;Flavoprotein;Glycoprotein;Oxidoreductase;Reference proteome;Signal;Vacuole
GO:0000328; GO:0005773; GO:0016218; GO:0016491; GO:0071949; GO:0140723
Evidence at protein level
5
SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:30680886}.
SIGNAL 1..23; /evidence="ECO:0000255"
null
PF08031;PF01565;
IPR012951;IPR016166;IPR036318;IPR016169;IPR050432;IPR006094;
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)
patO PEX2_082840
false
36
A0A075TR41
MAPFVPYHYSAGQSTIVKFGGLLTTEFLEPPPGRCFLFRQTYRHTIEGSIPENLRKLINSPDRPKGPPPHFHQFQTEYFRVENGVLGISVDGVVRRITPEDGEISVKAGSVHNFFIHPDSPENMTVYLSASDSGNDYQLDRVFFENWYGYWHDALLHDGGIDWIQFLAIQDGGDAYTPAPAWVPFRRQVGYWTCVIVGRWIGGLLGYKPFFREYTTDWDFAVAKMKGSFFQRHLVHAAFEEEKSWTKQAELEPKGKPENAEFEPWTEDMSPAPLSLGPVAYEQGLFHGVQPGSVNGSNGHSTGVESKLEQLGSRAQRRVVIDDAGK
Probable oxidoreductase patJ (EC 1.-.-.-) (Patulin biosynthesis cluster protein J)
Penicillium expansum (Blue mold rot fungus)
27,334
326
36,772
Cytoplasmic vesicle;Oxidoreductase;Reference proteome;Vacuole
GO:0000328; GO:0005773; GO:0016218; GO:0016491; GO:0060205; GO:0140723
Evidence at protein level
5
SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:30680886}. Cytoplasmic vesicle lumen {ECO:0000269|PubMed:30680886}.
null
null
null
IPR014710;IPR011051;
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)
patJ PEX2_082870
false
37
A0A075TRB3
MVLTTGLKGAHVLITGGTRGMGEAMVHKFLQEEANVSYCARTVTNTEYDDFYSTLAEGNTARAVGTAFDVASKDSLVKWVESSAERLGRIDVIIANASPMHMEGETEHWESSFAIDVMGFVELVKAATPYLEKSPQASIIVQSSFMGREFYRSPPAAYGPCKAAQLQHVQELSHFLGPKGIRVNAISPGPVLCKGGPWELYSKINPEWVEEQRLKIPLKRLGGPTEVANVAVFLASPLASFVSGTNMLVDGGIHVGTQF
Isoepoxydon dehydrogenase patN (IDH) (EC 1.1.1.-) (Patulin biosynthesis cluster protein N)
Penicillium expansum (Blue mold rot fungus)
27,334
259
28,033
Cytoplasm;NADP;Oxidoreductase;Reference proteome
GO:0005829; GO:0006633; GO:0016218; GO:0016491; GO:0016616; GO:0048038; GO:0140723
Evidence at protein level
5
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}.
null
null
PF13561;
IPR036291;IPR002347;
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)
patN PEX2_082830
false
38
A0A075TRC0
MHSVSPSTYPSGGTSPAPADTPGTEYSEYEFSNDVAVVGMACRVAGGNHNPELLWQSLLSQKSAVGEIPEMRWEPYYRRDPRNAKELKKTTSRGYFLDRLEDFDCQFFGISPKEAEQMDPQQRVSLEVASEALEDAGIPAKSLSGSDTAVFWGVNSDDYSKLVLEDLPNVEAWMGIGTAYCGVPNRISYHLNLMGPSTAVDAACASSLVAVHHGVQAIRLGESQVAIVGGVNALCGPGLTRVLDKAGAISSDGSCKSFDDDAHGYARGEGAGALVLKSLHRALLDHDNVLAVIKGSAVAQDGKTNGIMAPNAKAQQLAARTALNVAGVDPSTVRYVEAHATSTPLGDPTEISAIAGVYGTNRPADDPCYIGSIKPNIGHLEAGAGVMGFIKAILTIQKGVLPPQANLTNLNSRIDWKTAGVKVVQEATPWPSSDPIRRAGVCSYGYGGTVSHAVIEEFNPILRPDPLDDGAATGPGLLLLSGPQEKRLALQAKTLREWMTADGKDNNLSEILTTLATRRDHHDYRAALVVDDHLDATQVLQALANGTDHSFTTQSRVLGADVSKDVVWVFSGHGAQWPDMGKQLIHNPVFFAAIQPLDELIQAEIGLSPIELLRTGDFESSDRVQILTYLMQIGLSAILQSNGITPQAVIGHSVGEIAASVVAGALTSAEGALIVTRRALLYRQVMGKGGMILVNLPSAETEEILGRRQDLVVAIDSSPSSCVVAGDKDIVAETAEAFKARGVKTFTVKSDIAFHSPTLNVLMDPLRDALGQALAPTVHIKLYSTALVDPRGQDVRDLEYWTGNMVNRVRLTSAIQAAVEDGYRLFLEVSTHPVVSHSINETLMDAGLEDFAVIPTLLRKKPTEKHILHSIAQLHCRGAEVNWAAQMPGRWATGLPTTTWMHKPIWRKIETAPLHTGLTHDVEKHTLLGQRIPVPGTDTFVYTSRLDNETKPFPGSHPLHGTEIVPAAGLINTFLKGTGGQMLQNVVLRVPVAINAPRSVQVVVQQDQVKVVSRLISSDPSLSDDDASWVTHTTAYWDRKVLGSADRIDLAAVKARLTTKLADNFSIDYLDKVGVSAMGFPWAVTEHYRDTKQMLARVDVNPAVLGDDPLPWDSSSWAPVLDAATSVGSTVFQTAALRMPAQIERVEIFTSEDPPKISYLFVEEASDSVPTSHVSVLSETGEVLAKFTAMRFSEIEGTPGVSGSMESLVHQIAWPPATPAEEPLLITKVILVSPDATARAQYAATLPTQVQSFQFSTTEDFFSNASSLPLEKGTVVAYIPGEVASLAEVPAASESFTWNLLELIKFIVNGSLPIKVFTLTSSVGDGQTPTALAQSPLIGLARIIASEHPDLGSLIDIEEPKIPLSTMRYIQGADVIRISDGIARVSRFRSLPRTKLRPASEGPRLLPRPDGTYLITGGLGILGLEVADFLVEKGARRLLLISRRALPPRRTWDQVSEDLQPTIAKIRLLESRGASVHVLPLDITKPDAVEQLSTALDRLSLPAVQGVVHAAGVLDNEMVLQTTRDAFNRVLAPKIAGALALHEVFPPKSVDFFVMFSSCGNLVGFTGQASYGSGNAFLDTLATHRARLGDSGAVAFQWTAWRGLGMGSSTDFINAELEAKGITDVTRDEAFAAWQHLAKYDIDHGVVLRSLAIDDGEPVPVPILNDIVVRRVSELSGSAQAAAGSSGNDAVPSSGPELKAYLDEKIRGCVAKVLQMTAEDVDSKAALADLGVDSVMTVTLRRQLQQTLKIPVPPTLTWSHPTVSHLVVWFAEKIGK
6-methylsalicylic acid synthase (6MSAS) (EC 2.3.1.165) (Non-reducing polyketide synthase patK) (Patulin biosynthesis cluster protein K)
Penicillium expansum (Blue mold rot fungus)
27,334
1,776
190,701
Cytoplasm;Multifunctional enzyme;NADP;Phosphopantetheine;Phosphoprotein;Reference proteome;Transferase
GO:0004312; GO:0004315; GO:0005829; GO:0006633; GO:0016218; GO:0031177; GO:0050641; GO:0140723
Evidence at protein level
5
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}.
null
null
PF00698;PF16197;PF00109;PF02801;PF08659;PF21089;PF00550;
IPR001227;IPR036736;IPR014043;IPR016035;IPR018201;IPR014031;IPR014030;IPR016036;IPR036291;IPR032821;IPR020841;IPR042104;IPR020807;IPR049552;IPR013968;IPR049900;IPR050091;IPR020806;IPR009081;IPR006162;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)
patK PEX2_082880
false
39
A0A075TRK9
MRLTSGIFHAAIAVAAVGAVLPEGPSSSKTHRNEYARRMLGSSFGIPKNQTFDYLVIGGGTAGLTIATRLAEQGVGSVAVIEAGGFYELNNGNLSQIPAQDAFYVGTDLDDWQPGIDWGFHTTPQAGAYDRVSHYARGKCLGGSSARNYMAYQRGTKAAHQRWADTVGDSSYTWEQFLPFFEKSLHFTPANDALRGANASVVSDPSVLGNGDGPLSVTYPHYAQAFATWAKHAFIEIGLQIRSGFQSGALLGQSYGLYTINATTMHRESSETSFLRKGLADPNLTVFQSALAKRIRFQDKRAVGVDVETMGRAYTLSARKEIVLSAGAFQSPQLLMVSGVGPAATLKAHNIPLVADRPGVGQNMQDHIIYAPSYRVNVITQSALLNEEFEAQANRDYNERAAGIYANPTSDILAWEKIPEPKRSAWFSNHTRQVLAEYPDDWPEVEFLTMGGYFGYQRNYIRDNPSDGYNYASLAVSLCTPRSRGNVTITSPDAGVPPVINPNWLTDPVDVELAVAAFKRTRDFFNTTAIKPILIGPEYFPGSQVATDAEILDHVRKSFDTIFHASCTCAMGLANDTQAVVDSKARVIGVEALRVVDASALPFLPPGHPQSTLYALAEKIACEISGNC
Patulin synthase (EC 1.1.-.-) (Dehydrogenase patE) (Patulin biosynthesis cluster protein E)
Penicillium expansum (Blue mold rot fungus)
27,334
628
68,132
3D-structure;Cell wall;Cytoplasm;FAD;Flavoprotein;Glycoprotein;Oxidoreductase;Reference proteome;Secreted;Signal;Vacuole
GO:0005576; GO:0005773; GO:0005938; GO:0016218; GO:0016491; GO:0016614; GO:0031012; GO:0050660; GO:0140723
Evidence at protein level
5
SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:30680886}. Vacuole {ECO:0000269|PubMed:30680886}. Secreted {ECO:0000269|PubMed:30680886}. Secreted, cell wall {ECO:0000269|PubMed:30680886}.
SIGNAL 1..19; /evidence="ECO:0000255"
null
PF05199;PF00732;
IPR036188;IPR012132;IPR000172;IPR007867;
8BXL;
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)
patE PEX2_082770
false
40
A0A075TRL5
MEPFLLLLLVLLPAIVLVRYAFTYGHRTSTMPIGPPTLPFIGNIHQITKKYTHIKFTEWAAQYGGLYMLKIGNGNMAVITDRRLVKEVLDRKSGIYSHRPHSFVSHDLITKGNHLLVMHYGDQWRTFRRLVHQHLMETMVENHHTKIVNAEAIQLVRDYMIDPEHHMAHPKRYSNSITNSIVFGIRTANREGANMRRLYKLMEEWSEVMETGATPPVDLFPWLKLLPQWLFNNYIDRAKAIGVQMETLYVDILNKVIKRREDGHNNGTFMDKVLDSQEKHNLPWHQLAFIGGVLMEGGSDTSSSLTLAIVQALIQNPDVQRKAHAEIDAVVGHNRSPVWEDFEKLPYINMIIKEGHRWRPILPLCFPHALGEDDWVDGKFLPKGTIVVVNTWGMHMDPSQPDDPAAFIPERFAKHPQLAPDYVPGTWERRDHYGYGVGRRICPGIHLAERNMFLGIAKLLWAFDFQPGEGPIDSDPVTGYHNGFLYCAKDYSCRPVIRNEVIRDTIEREYATATADVFSRFTEG
Cytochrome P450 monooxygenase patH (EC 1.-.-.-) (Patulin biosynthesis cluster protein H) (m-cresol hydrolase)
Penicillium expansum (Blue mold rot fungus)
27,334
524
60,202
Endoplasmic reticulum;Glycoprotein;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Reference proteome;Transmembrane;Transmembrane helix
GO:0004497; GO:0005506; GO:0005783; GO:0005789; GO:0016218; GO:0016705; GO:0020037; GO:0140723
Evidence at protein level
5
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30680886}; Single-pass membrane protein {ECO:0000269|PubMed:30680886}.
null
TRANSMEM 5..22; /note="Helical"; /evidence="ECO:0000255"
PF00067;
IPR001128;IPR002401;IPR036396;IPR050364;
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)
patH PEX2_082740
false
41
A0A075TXZ1
MAKIDVHHHFYPPAMRQALDRAGGDPSGWYIPPWTLELDQDITRQMKVTTTILSVTAPGPGIEPDVTKAAALARSCNESAAAIRDAKPQQYGFFASVPSLFDTAAVLKEIEYACTTLRADGVTLFTRYGKGSNYLGHAAFRPIWADLSRRGAVVFIHPTHPVDTQLINTWLPQPMFDYPHETGRAAMDLLTSGILQDYPGCKIILSHAGGTLPYLIHRAATMLPLMPRTLGLSTEELVEAARTFYFDTAISSNPVTLKALFEFAAPGHVLFGSDFPNAPHDAILRFTNFLEAYELPEETKRQVDSGAALELFPRLKGILDKAKL
6-methylsalicylic acid decarboxylase (EC 4.1.1.52) (Patulin biosynthesis cluster protein G)
Penicillium expansum (Blue mold rot fungus)
27,334
324
35,653
Cytoplasm;Decarboxylase;Hydrolase;Lyase;Metal-binding;Reference proteome;Zinc
GO:0005829; GO:0016218; GO:0016787; GO:0046872; GO:0047596; GO:0140723
Evidence at protein level
5
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}.
null
null
PF04909;
IPR032465;IPR006680;IPR032466;
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)
patG PEX2_082750
false
42
A0A076FFM5
MPFPMEVLQASSLSFPLLRRHSRNNLINKFRNPTLPRIDIPRQNIDLKTFAATTPTVACPPSDPEIIPEKKEDKFDWYENWYPVATVCDLDKRRPHGRKVIGIDVVVWWDRKENAWKVFDDTCPHRLAPLSEGRIDQWGRLQCVYHGWCFDGVGACKFIPQAPHDGPPVETSKKACVKGVYPSCVRNGIVWFWPNSDPKYKDIYLTNKPHYIPELDDPSFTCTTITREVPYGYEILAENLMDPSHVPYAHYGILELEKVKESSKRDREGGHEMEISVGTIDVNGFSAKHVSADYYFVPPYVYYGRITPNAATKTKDATLPVVPEEKTAMIVFYCIPVTPGYSRLIYAGARNFAVQIDRFVPRWITHMSHNLIFDSDLFLLHVEEQKLKDLDWHKSCYIPTKADGQVVAFRRWLNKYGGTQVDWRNNFTPALPPTPSREQLFDRYWSHTAECSSCSVACKRLNALEIGLQAMSLVFVAMAAAVSAPATRYSMVAMAVLSFLASKWLSHFIHKTFYNHGYDHAFV
Flavonoid 8-hydroxylase 1, chloroplastic (ObF8H-1) (EC 1.14.15.-)
Ocimum basilicum (Sweet basil)
39,350
523
59,910
2Fe-2S;Chloroplast;Cytoplasm;Iron;Iron-sulfur;Membrane;Metal-binding;Oxidoreductase;Plastid;Transit peptide;Transmembrane;Transmembrane helix
GO:0004497; GO:0005737; GO:0009507; GO:0009812; GO:0010277; GO:0031969; GO:0046872; GO:0051537
Evidence at protein level
5
SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000269|PubMed:25139498}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:25139498}.
null
TRANSMEM 466..486; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 489..509; /note="Helical"; /evidence="ECO:0000255"
PF08417;PF00355;
IPR050584;IPR013626;IPR017941;IPR036922;
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), Ociminae (subtribe), Ocimum (genus)
F8H-1
false
43
A0A078CGE6
MARQMTSSQFHKSKTLDNKYMLGDEIGKGAYGRVYIGLDLENGDFVAIKQVSLENIVQEDLNTIMQEIDLLKNLNHKNIVKYLGSLKTKTHLHIILEYVENGSLANIIKPNKFGPFPESLVTVYIAQVLEGLVYLHEQGVIHRDIKGANILTTKEGLVKLADFGVATKLNEADVNTHSVVGTPYWMAPEVIEMSGVCAASDIWSVGCTVIELLTCVPPYYDLQPMPALFRIVQDDSPPIPDSLSPDITDFLRQCFKKDSRQRPDAKTLLSHPWIRNSRRALQSSLRHSGTIRYMKGADSSSEKDGEGSQDIAESVSAEKVGMSKTNSKSKLGVGSFRSEKDQSSASDIGEERADSEDDIMSDQGPTLSIHDNKSSLQSSTCSISSDAKGTSQDGKSEPDGNLEMEASEGRRKASATKQVGKESSIQMQQRSHSFGPKGEDRGLRKAVKTPSSYGGNELTRFSDPPGDACLHDLFHPLNKVPEGKLNEASASTPASNANQGDSPVADGGKNDLATKLRARIAQKQMEGETGHSNDGGDLFRLMMGVLKDDVIDIDGLVFDEKASPDNLLPLQAVEFSRLVSSLRPSETEDAIVTSCQKLVAMFRHRPEQKVVFVTQHGFLPVMDLLDSPKSRVTCAVLQLINEIIKDNIDFQENACLVGLIPLVMSFAGPERDRSREIRKEAAYFLQQLCQSSSLTLQMFIACRGIPVLVGFLEADYAKYRSMVHLAIDGMWQVFKLKRSTPRNDFCRIAAKNGILLRLINTLYSLNEATLLASEGRSGQLDQHEALLSVIDHPDVLKTRPGGGEEPSNSQRSDLYQPDGDRPRSSSAALDATEDVKQHHRISISSNRTSTDKIQKLAESASNGYAVTQPEQVRPLLSLLEKEPPSRHVSGQLDYVKHIAGLEKHESILPLLRASIDTMPRYFSKTMSKKVMAIEGAASASGVLSGSGVLNARLGSDTSSGLLSHMVTTLSAEVASQYLEKVADLLLEFARADTTVKSYMCSQSLLSRLFHMFNRVEPPILLKILKCTNHLSTDPNCLESLQRADAIKHLIPNLEVKEGNLVDQIHHEVLSALFNLCKINKRRQEQAAENGIIPHLMLFVMSDSPLKQYALPLLCDMAHASRNSREQLRSHGGLDVYLSLLDDEYWSVIALDSIAVCLAQDNDNRKVEQALLKDDAIYTLVNFFQSCPERHFVHILEPFLKIITKSSRINTTLAVNGLTPLLIARLDHQDAIARLNLLKLIKAVYEHHPRPKQLIVENDLPQRLQNLIEERREGQHLGGQVLVKQMATSLLKALHINTVL
MAP3K epsilon protein kinase 1 (BnM3KE1) (EC 2.7.11.1)
Brassica napus (Rape)
3,708
1,299
143,609
ATP-binding;Cell cycle;Cell division;Cell membrane;Cytoplasm;Cytoskeleton;Kinase;Membrane;Nucleotide-binding;Nucleus;Phosphoprotein;Repeat;Serine/threonine-protein kinase;Transferase
GO:0004674; GO:0005524; GO:0005730; GO:0005737; GO:0005815; GO:0005886; GO:0046777; GO:0051301; GO:0051302; GO:0106310
Evidence at protein level
5
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q8T2I8}. Nucleus, nucleolus {ECO:0000269|PubMed:15292395}. Cell membrane {ECO:0000250|UniProtKB:Q9LJD8}. Note=Accumulates in the nucleolus during interphase (PubMed:15292395). Localized to the plasma membrane in developing pollen grains (By similarity). {ECO:0000250|UniProtKB:Q9LJD8, ECO:0000269|PubMed:15292395}.
null
null
PF00069;
IPR011989;IPR016024;IPR052441;IPR011009;IPR000719;IPR017441;IPR001245;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), rosids (clade), malvids (clade), Brassicales (order), Brassicaceae (family), Brassiceae (tribe), Brassica (genus)
M3KE1 BnaA03g30290D GSBRNA2T00111755001
false
44
A0A080WMA9
MATPSKKRCGVLGATGAVGTRFILLLSQHPLLELVAVGASDRSSGKKYRDAVRWKQSAPMPAKVADLTVRCCDPAEFSDCDIIFSGLDPDAAGEIEMAFLKANFAVFSNAKNYRLDPMVPLVVPLVNAGHIDVIPAQRKHFGLDKGMLVCNSNCAVVGLVVPAKALIQKFGPIESVSMVTMQAVSGAGYPGVSSMDIFDNIVPYIPGEEGKISSEARKILGDLNSDLAGFSDQKPLQISVACNRVPVLDGHTVCASLRFVNRPPPTASQVREALREYKPEVQTLGCPSAPKMSIHVMDEVDRPQPRLDRETEGGYACTVGRIREDDSDVFDIQFVALSHNTVLGASGSSILNAESAILKGFV
Aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) (TrASADH)
Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot fungus)
559,305
362
38,742
3D-structure;Amino-acid biosynthesis;Cytoplasm;Methionine biosynthesis;NADP;Nucleus;Oxidoreductase;Reference proteome;Threonine biosynthesis
GO:0004073; GO:0005634; GO:0005829; GO:0009088; GO:0009089; GO:0046983; GO:0050661; GO:0051287; GO:0071266
Evidence at protein level
5
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P13663}. Nucleus {ECO:0000250|UniProtKB:P13663}.
null
null
PF01118;PF02774;
IPR051823;IPR000319;IPR005676;IPR036291;IPR000534;IPR012280;
4ZHS;4ZIC;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), Eurotiomycetes (class), Eurotiomycetidae (subclass), Onygenales (order), Arthrodermataceae (family), Trichophyton (genus), Trichophyton rubrum (species)
TERG_03598
false
45
A0A087WPF7
MDGPTRGHGLRKKRRSRSQRDRERRSRAGLGTGAAGGIGAGRTRAPSLASSSGSDKEDNGKPPSSAPSRPRPPRRKRRESTSAEEDIIDGFAMTSFVTFEALEKDVAVKPQERAEKRQTPLTKKKREALTNGLSFHSKKSRLSHSHHYSSDRENDRNLCQHLGKRKKMPKGLRQLKPGQNSCRDSDSESASGESKGFQRSSSRERLSDSSAPSSLGTGYFCDSDSDQEEKASDASSEKLFNTVLVNKDPELGVGALPEHNQDAGPIVPKISGLERSQEKSQDCCKEPVFEPVVLKDPHPQLPQLPSQAQAEPQLQIPSPGPDLVPRTEAPPQFPPPSTQPAQGPPEAQLQPAPLPQVQQRPPRPQSPSHLLQQTLPPVQSHPSSQSLSQPLSAYNSSSLSLNSLSSRSSTPAKTQPAPPHISHHPSASPFPLSLPNHSPLHSFTPTLQPPAHSHHPNMFAPPTALPPPPPLTSGSLQVPGHPAGSTYSEQDILRQELNTRFLASQSADRGASLGPPPYLRTEFHQHQHQHQHTHQHTHQHTFTPFPHAIPPTAIMPTPAPPMFDKYPTKVDPFYRHSLFHSYPPAVSGIPPMIPPTGPFGSLQGAFQPKTSNPIDVAARPGTVPHTLLQKDPRLTDPFRPMLRKPGKWCAMHVHIAWQIYHHQQKVKKQMQSDPHKLDFGLKPEFLSRPPGPSLFGAIHHPHDLARPSTLFSAAGAAHPTGTPFGPPPHHSNFLNPAAHLEPFNRPSTFTGLAAVGGNAFGGLGNPSVTPNSVFGHKDSPSVQNFSNPHEPWNRLHRTPPSFPTPPPWLKPGELERSASAAAHDRDRDVDKRDSSVSKDDKERESVEKRHPSHPSPAPPVPVSALGHNRSSTDPTTRGHLNTEAREKDKPKEKERDHSGSRKDLTTEEHKAKESHLPERDGHSHEGRAAGEEPKQLSRVPSPYVRTPGVDSTRPNSTSSREAEPRKGEPAYENPKKNAEVKVKEERKEDHDLPTEAPQAHRTSEAPPPSSSASASVHPGPLASMPMTVGVTGIHAMNSIGSLDRTRMVTPFMGLSPIPGGERFPYPSFHWDPMRDPLRDPYRDLDMHRRDPLGRDFLLRNDPLHRLSTPRLYEADRSFRDREPHDYSHHHHHHHHPLAVDPRREHERGGHLDERERLHVLREDYEHPRLHPVHPASLDGHLPHPSLLTPGLPSMHYPRISPTAGHQNGLLNKTPPTAALSAPPPLISTLGGRPGSPRRTTPLSAEIRERPPSHTLKDIEAR
Autism susceptibility gene 2 protein homolog
Mus musculus (Mouse)
10,090
1,261
138,920
Alternative splicing;Cell projection;Cytoplasm;Cytoskeleton;Nucleus;Phosphoprotein;Reference proteome;Transcription;Transcription regulation
GO:0001764; GO:0003682; GO:0005634; GO:0005737; GO:0005856; GO:0010592; GO:0030036; GO:0030426; GO:0035022; GO:0045944; GO:0048675; GO:0060013; GO:0097484; GO:0098582
Evidence at protein level
5
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19948250, ECO:0000269|PubMed:25519132, ECO:0000269|PubMed:25533347}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:25533347}. Cell projection, growth cone {ECO:0000269|PubMed:25533347}. Note=Detected both in cytoplasm and nucleus (PubMed:25533347). Colocalizes with RAC1 at actin-rich growth cones (PubMed:25533347). Detected on the promoter region of actively transcribed genes (PubMed:25519132). {ECO:0000269|PubMed:25519132, ECO:0000269|PubMed:25533347}.
null
null
PF15336;
IPR023246;
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)
Auts2 Kiaa0442
false
46
A0A087X1C5
MGLEALVPLAMIVAIFLLLVDLMHRHQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREAMVTRGEDTADRPPAPIYQVLGFGPRSQGVILSRYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFADQAGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLPHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAKKEKAKGSPESSFNDENLRIVVGNLFLAGMVTTSTTLAWGLLLMILHLDVQRGRRVSPGCPIVGTHVCPVRVQQEIDDVIGQVRRPEMGDQAHMPCTTAVIHEVQHFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWKKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQPRPSHSRVVSFLVTPSPYELCAVPR
Cytochrome P450 2D7 (EC 1.14.14.1)
Homo sapiens (Human)
9,606
515
57,489
Cytoplasm;Glycoprotein;Heme;Iron;Membrane;Metal-binding;Mitochondrion;Monooxygenase;Oxidoreductase;Reference proteome;Transmembrane;Transmembrane helix
GO:0005506; GO:0005737; GO:0005739; GO:0006805; GO:0016020; GO:0016712; GO:0019369; GO:0020037; GO:0042178; GO:0043231; GO:0070330
Evidence at protein level
5
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000305|PubMed:15051713}. Mitochondrion {ECO:0000269|PubMed:18838503}.
null
TRANSMEM 3..23; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 302..322; /note="Helical; Name=2"; /evidence="ECO:0000255"
PF00067;
IPR001128;IPR017972;IPR002401;IPR008069;IPR036396;IPR050182;
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), Catarrhini (parvorder), Hominoidea (superfamily), Hominidae (family), Homininae (subfamily), Homo (genus)
CYP2D7
false
47
A0A088MLT8
MRLEELKRLQNPLEQVDDGKYLLENHQLAMDVENNIENYPLSLQPLESKVKIIQRAWREYLQRQDPLEKRSPSPPSVSSDKLSSSVSMNTFSDSSTPDYREDGMDLGSDAGSSSSSRASSQSNSTKVTPCSECKSSSSPGGSLDLVSALEDYEEPFPVYQKKVIDEWAPEEDGEEEEEEDDRGYRDDGCPAREPGDVSARIGSSGSGSRSAATTMPSPMPNGNLHPHDPQDLRHNGNVVVAGRPNASRVPRRPIQKTQPPGSRRGGRNRASGGLCLQPPDGGTRVPEEPPAPPMDWEALEKHLAGLQFREQEVRNQGQARTNSTSAQKNERESIRQKLALGSFFDDGPGIYTSCSKSGKPSLSARLQSGMNLQICFVNDSGSDKDSDADDSKTETSLDTPLSPMSKQSSSYSDRDTTEEESESLDDMDFLTRQKKLQAEAKMALAMAKPMAKMQVEVEKQNRKKSPVADLLPHMPHISECLMKRSLKPTDLRDMTIGQLQVIVNDLHSQIESLNEELVQLLLIRDELHTEQDAMLVDIEDLTRHAESQQKHMAEKMPAK
IQCJ-SCHIP1 readthrough transcript protein
Mus musculus (Mouse)
10,090
559
61,917
Alternative splicing;Cell projection;Coiled coil;Cytoplasm;Reference proteome
GO:0005516; GO:0005737; GO:0008366; GO:0030506; GO:0033268; GO:0043194; GO:0044325; GO:0051494
Evidence at protein level
5
SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:18550753}. Cytoplasm {ECO:0000250|UniProtKB:B3KU38}. Note=Localizes to the axon initial segments (AIS) and nodes of Ranvier of neurons and is absent from dendrites. {ECO:0000269|PubMed:18550753}.
null
null
PF15157;PF10148;
IPR029362;IPR039045;IPR015649;
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)
Iqcj-Schip1 Iqschfp Schip1
false
48
A0A089QRB9
MRTATATSVAVIGMACRLPGGIDSPQRLWEALLRGDDLVGEIPADRWDANVYYDPEPGVPGRSVSRWGAFLDDVGGFDCDFFGLTEREATAIDPQHRLLLEVSWEAIEHAGVDPATLAESQTGVFVGLTHGDYELLSADCGAAEGPYGFTGTSNSFASGRVAYTLGLHGPAVTVDTACSSGLTAVHQACRSLDDGESDLALAGGVVVTLEPRKSVSGSLQGMLSPTGRCHAFDEAADGFVSGEGCVVLLLKRLPDAVRDGDRVLAIVRGTAANQDGRTVNIAAPSAQAQIAVYQQALAAAGVEASTVGMVEAHGTGTPVGDPVEYASLAAVYGTEGPCALTSVKTNFGHLQSASGPLGLMKTILALRHGVVPQNLHFCRLPDQLAEIDTELFVPQANTSWPDNTGQPRRAAVSSYGMSGTNVHAILEQAPVSEPAASGPELTPEAGGLALFPVSATSAEQLHVTAARLADWVDQNGNAGSRVSMRDLGYTLSCRRAHRPVRTVVTASSFDELSAALRDVAGDQIPYQPAVGHDDRGPVWVFSGQGSQWPGMGTELLVAEPVFAATVAAMEPVIARESGFSVTEAMSAPQTVSGIDRVQPTIFAVQVALAAALKSYGVRPGAIIGHSLGEAAAAVVAGALSLHDGLRVICRRSRLMSRIAGSGAMASVELPGQQVLSELAIRGISDVVLSVVASPTSTVVGGATQSIRDLVAAWEQQDVLAREVAVDVASHTPQVDPILDELLEVLAEVDPTAPEIPYYSATLWDPRERPSFTGEYWVENLRYTVRFAAAVQAALKDGYRVFGELAPHPLLTYAVEQNAASLDMPIATLAAMRRGEQLPFGLRGFVADVHNAGAKVDFSVQYPDGRLVDAPLPSWTHRTLMLSREDSHRSHTGAVQAVHPLLGAHVHLLEEPERHVWQAGVGTGAHPWLGDHRIHNVAAFPGAAYCEMALAAARTTLGELSEVRDIKFEQTLLLDEQTVVSSAATIAAPGILQFAVESHQEGEPARRASAMLHALEEMPQPPGYDTNALTAAHESSMSGEELRKMFNSLGIQYGPAFSGLVAVHTARGDVTTVLAEVALPGAIRSQQSAYASHPALLDACFQSVLVHPEVQKATVGGLMLPVGVRRLRNYHSTRSAHYCLARVTSSSRAGECEADLDVFDQAGTVLLTVEGLRLAAGISEHERANRVFDERLLTIEWERGELPEVPQIDAGSWLLLSASEADPLTAQLADALNAVGAQSTSVASASDVAQLRSLLGGRLTGVVVVTGPPTGGLTQCGRDYVSQLVGIARELAELPGEPPRLFVVTRSAASVLPSDLANLEQAGLRGLMRVIDSEHPHLGATAIDVDNDETVAALVASQLQSGSQEDETAWRNGIWYTARLRPGPLRPAERRTAVVEYRRDGMRLQIRTPGDLESLEFVTFDRVAPGPGEIEVAVTASSVNFADVLVAFGRYPTFEGYRQQLGIDFAGVVTAVGPDVTEHRIGDHVGGMSANGCWSTFVRCDARLAVTLPPELPVAAAAAVPTASATAWYALHDLARICSDDKVLIHSGTGGVGQAAIAIARAAGCEIFATAGSAQRRQLLHDMGVEHVYDSRSTEFAEQIRGDTDGYGVDVVLNSLPGAAQRAGIELLAFGGRFVEIGKRDIYGDTRLGLFPFRRNLSLYAVDLALLTHSHPHTVRRLLKTVYQHTVEGTLPVPQTTHYPIHDAAVAIRLVGGAGHTGKVVLDVPRTGEGVAVVPPEQVRTSRPDGAYLVTGGLGGLGLFLAGELAAAGCGRIVLNSRSTPSPHATRVIERLRAAGADIQVECGDIADAATAHRVVAVATASGLPVRGVLHAAAVVEDATLANVTDELIDRCWAPKVHGAWNIHRATAAQPLEWFCLFSSAAALVGSPGQGAYAAANSWLDAFAHWRRAQGLPATSIAWGAWAEIGRATALAEGTGAAIAPAEGARAFQTLLRYGRAYSGYAPIMGTPWLTAFAQRSRFAEAFHATGQNQPATGKFLAELGSLPREEWPRTVRRLVSDQISLLLRRTIDPDRPLSDYGLDSLGNLELRTRIETETGIRVSPTKITTVRGLAEHVCDELAAAQSAPV
Mycolipanoate synthase (EC 2.3.1.252) (Mycocerosic acid synthase-like polyketide synthase) (MAS-like PKS) (Mycolipanoic/mycolipenic acids synthase-like polyketide synthase)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
83,332
2,085
220,462
Acyltransferase;Cell membrane;Direct protein sequencing;Lipoprotein;Membrane;Multifunctional enzyme;NADP;Palmitate;Phosphopantetheine;Phosphoprotein;Reference proteome;Signal;Transferase
GO:0004315; GO:0005886; GO:0006633; GO:0016491; GO:0031177; GO:0034081; GO:1902321
Evidence at protein level
5
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
SIGNAL 1..15; /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
null
PF00698;PF08240;PF00107;PF16197;PF00109;PF02801;PF08659;PF21089;PF00550;PF14765;
IPR001227;IPR036736;IPR014043;IPR016035;IPR013149;IPR013154;IPR011032;IPR018201;IPR014031;IPR014030;IPR016036;IPR053386;IPR036291;IPR032821;IPR020841;IPR042104;IPR020807;IPR049551;IPR049552;IPR020843;IPR013968;IPR049900;IPR050091;IPR020806;IPR009081;IPR016039;
null
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Actinomycetota (phylum), Actinomycetes (class), Mycobacteriales (order), Mycobacteriaceae (family), Mycobacterium (genus), Mycobacterium tuberculosis complex (no rank), Mycobacterium tuberculosis (species)
msl3 pks3 pks4 Rv1180/Rv1181
false
49
A0A095AMW7
MNTTGYDILRNPFLNKGTAFSEAERQQLGLTGTLPSQIQTIEEQAEQAYKQFQAKSPLLEKRIFLMNLFNENVTLFYHLMDQHVSEFMPIVYDPVVAESIEQYNEIYTNPQNAAFLSVDRPEDVENALKNAAAGRDIKLVVVTDAEGILGMGDWGVNGVDIAVGKLMVYTAAAGIDPATVLPVSIDAGTNNKELLHNPLYLGNKHERIAGEQYLEFIDKFVTAEQNLFPESLLHWEDFGRSNAQVILDKYKESIATFNDDIQGTGMIVLAGIFGALNISKQKLVDQKFVTFGAGTAGMGIVNQIFSELKQAGLSDDEARNHFYLVDKQGLLFDDTEGLTAAQKPFTRSRKEFVNPEQLINLETIVKELHPTVLIGTSTQPGTFTETIVKSMAENTERPIIFPLSNPTKLAEATAEDLIKWTGGKALVATGIPAADVDYKGVTYKIGQGNNALIYPGLGFGLVASTAKLLTQETISAAIHALGGLVDTDEPGAAVLPPVSNLTDFSQKIAEITAQSVVNQGLNREKIVDPKQAVQDAKWSAEY
Malolactic enzyme (MLE) (EC 4.1.1.101)
Leuconostoc mesenteroides
1,245
542
59,205
Lyase;Manganese;Metal-binding;NAD
GO:0004470; GO:0005829; GO:0006108; GO:0016616; GO:0016831; GO:0030145; GO:0043464; GO:0043883; GO:0051287
Evidence at protein level
5
null
null
null
PF00390;PF03949;
IPR046346;IPR015884;IPR012301;IPR037062;IPR012302;IPR001891;IPR048182;IPR036291;
null
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Lactobacillaceae (family), Leuconostoc (genus)
mleS LH61_04880
false
50
A0A095C6S0
MSFDAVVIGSGVIGLSIARELDNRGLKVAMVARDLAEDSLSVGFASPWAGCNWYSFAEGGTPAAEWDAITFSKLAKLAEDHPDLCEKIPFCSVWDLPKSDSESEPWFKDLVFEYKKLKSTPGQHLAGGKKFGYSFKSYVLHAPNYIRHLSSEIRARGIPIHRYRLSSIDEAYNLPGIGKVSLVVNASGLGAKSLIGVEDEKVYSGRGQTVLVRAPGFKACIMHTEGFYADLDESGREITPPPPAYIIPRPGPEGHVVLGGVYQKDNWSTLPDLKEAERILKDCYNLAPELAGPNGKSWKDIEIISHNVGLRPAREGEPRLEIEEREVGTGANGGNGYEVAPKFGCEGERRKVAVVHAYGIGSAGFQASLGMAEKASDLVEKYLSGRRTSAKL
D-amino-acid oxidase 2 (DAAO) (DAMOX) (DAO) (EC 1.4.3.3) (CgDAO2)
Cryptococcus deuterogattii (strain R265) (Cryptococcus gattii VGII (strain R265))
294,750
392
42,599
FAD;Flavoprotein;Oxidoreductase;Peroxisome
GO:0003884; GO:0005782; GO:0019478; GO:0019740; GO:0071949; GO:1990748
Evidence at protein level
5
SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:P80324}.
null
null
PF01266;
IPR006181;IPR023209;IPR006076;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Basidiomycota (phylum), Agaricomycotina (subphylum), Tremellomycetes (class), Tremellales (order), Cryptococcaceae (family), Cryptococcus (genus), Cryptococcus gattii species complex (no rank), Cryptococcus deuterogattii (species)
DAO2 CNBG_2060
false
51
A0A096MJN4
MIKHFLEDNSDDAELSKFVKDFPGSEPCHPTESKTRVARPQILEPRPQSPDLCDDDVEFRATLWSQPSDSQQYFCPPAPLSPSSRPRSPWGKLDPYDSSEDDKEYVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVNSLFLTDLYRDRKLLGAEERIMQTVEITKHAVDIEEKGVRLRLTIVDTPGFGDAVNNTECWRPVAEYIDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPLDVEFMKALHQRVNIVPILAKADTLTPSEVDRKKCKIREEIEHFGIKIYQFPDCDSDEDEDFKLQDQALKESIPFAVIGSNTVVEARGRRVRGRLYPWGIVEVENPGHCDFVKLRTMLVRTHMQDLKDVTRETHYENYRAQCIQSMTRLVVKERNRNKLTRESGTDFPIPAVPPGTDPETEKLIREKDEELRRMQEMLHKIQRQMKETH
Septin-4 (Apoptosis-related protein in the TGF-beta signaling pathway) (Arts) (Bradeion beta) (Brain protein H5) (CE5B3 beta) (Cell division control-related protein 2) (hCDCREL-2) (Peanut-like protein 2)
Rattus norvegicus (Rat)
10,116
459
53,083
Cell cycle;Cell division;Cell projection;Cilium;Coiled coil;Cytoplasm;Cytoplasmic vesicle;Differentiation;Flagellum;GTP-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;Spermatogenesis
GO:0000287; GO:0001764; GO:0003924; GO:0005525; GO:0005737; GO:0005739; GO:0005940; GO:0007286; GO:0007420; GO:0008021; GO:0008104; GO:0015630; GO:0017157; GO:0030317; GO:0030382; GO:0030424; GO:0030425; GO:0031105; GO:0031398; GO:0031514; GO:0032153; GO:0036126; GO:0042802; GO:0042995; GO:0043065; GO:0043204; GO:0043679; GO:0048240; GO:0048515; GO:0048729; GO:0060090; GO:0061484; GO:0061640; GO:0097227; GO:0098691; GO:0098793; GO:2000647; GO:2001244
Evidence at protein level
5
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28661}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:P28661}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:O43236}. Cell projection, axon {ECO:0000250|UniProtKB:P28661}. Cell projection, dendrite {ECO:0000250|UniProtKB:P28661}. Perikaryon {ECO:0000250|UniProtKB:P28661}. Note=Found in the sperm annulus, a fibrous ring structure connecting the midpiece and the principal piece of the sperm flagellum (By similarity). In platelets, found in areas surrounding alpha-granules (By similarity). Expressed and colocalized with SLC6A3 and SNCA in axon terminals, especially at the varicosities (By similarity). {ECO:0000250|UniProtKB:O43236, ECO:0000250|UniProtKB:P28661}.
null
null
PF00735;
IPR030379;IPR027417;IPR016491;
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), Rattus (genus)
Septin4 Arts Bh5 Gm11492 Pnut12 Sep4 Sept4
false
52
A0A096MJY4
MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVETLRKKGLNGCDSPDPDADDSVGHSPESEDKYRKINEDIDLMISRQRLCAVPPPNFEMPVTIPVSSHNSLVYSNPVSSLGNPNLLPLAHPSLQRNSMSPGVTHRPPSAGNTGGLMGGDLTSGAGTSAGNGYGNPRNSPGLLVSPGNLNKNIQAKSPPPMNLGMNNRKPDLRVLIPPGSKNTMPSVSEDVDLLLNQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTTYGTEYSLSSADLSSLSGFNTASALHLGSVTGWQQQHLHNMPPSALSQLGACTSTHLSQSSNLSLPSTQSLNIKSEPVSPPRDRTTTPSRYPQHTRHEAGRSPVDSLSSCSSSYDGSDREDHRNEFHSPIGLTRPSPDERESPSVKRMRLSEGWAT
Myocyte-specific enhancer factor 2C (Myocyte enhancer factor 2C)
Rattus norvegicus (Rat)
10,116
473
51,217
Acetylation;Activator;Apoptosis;Cytoplasm;Developmental protein;Differentiation;DNA-binding;Isopeptide bond;Neurogenesis;Nucleus;Phosphoprotein;Reference proteome;Transcription;Transcription regulation;Ubl conjugation
GO:0000122; GO:0000165; GO:0000976; GO:0000977; GO:0000978; GO:0000981; GO:0000987; GO:0001228; GO:0001568; GO:0001649; GO:0001764; GO:0001782; GO:0001947; GO:0001958; GO:0001974; GO:0002062; GO:0002467; GO:0002634; GO:0002931; GO:0003138; GO:0003139; GO:0003151; GO:0003185; GO:0003211; GO:0003677; GO:0003680; GO:0003682; GO:0003700; GO:0005634; GO:0005737; GO:0005829; GO:0006355; GO:0006915; GO:0006959; GO:0007411; GO:0007507; GO:0007519; GO:0007521; GO:0007611; GO:0010467; GO:0010613; GO:0010628; GO:0010629; GO:0014033; GO:0014898; GO:0014902; GO:0016528; GO:0016607; GO:0021542; GO:0030017; GO:0030154; GO:0030182; GO:0030220; GO:0030224; GO:0030279; GO:0030318; GO:0030501; GO:0030890; GO:0031667; GO:0032991; GO:0033197; GO:0035050; GO:0035914; GO:0035984; GO:0042100; GO:0042826; GO:0043410; GO:0043523; GO:0043524; GO:0043537; GO:0043565; GO:0045165; GO:0045652; GO:0045663; GO:0045666; GO:0045669; GO:0045893; GO:0045944; GO:0046928; GO:0046982; GO:0048167; GO:0048643; GO:0048666; GO:0048667; GO:0048703; GO:0048704; GO:0050680; GO:0050853; GO:0051145; GO:0051963; GO:0051966; GO:0055007; GO:0055012; GO:0060021; GO:0060025; GO:0060045; GO:0060079; GO:0060290; GO:0060297; GO:0060536; GO:0060998; GO:0061333; GO:0061629; GO:0071222; GO:0071277; GO:0071300; GO:0071333; GO:0071363; GO:0071374; GO:0071466; GO:0071498; GO:0071560; GO:0071837; GO:0071838; GO:0071864; GO:0072102; GO:0072160; GO:0097492; GO:0098794; GO:0098989; GO:0098990; GO:0140297; GO:1902287; GO:1904706; GO:1904753; GO:1905563; GO:1990837; GO:2000111; GO:2000727; GO:2000987; GO:2001013; GO:2001016
Evidence at protein level
5
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15862299}. Cytoplasm, sarcoplasm {ECO:0000269|PubMed:15862299}.
null
null
PF12347;PF00319;
IPR022102;IPR033896;IPR002100;IPR036879;
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), Rattus (genus)
Mef2c
false
53
A0A096MK47
MTSCVLAGSIETTPKVSPGDSEAKPLIFTFVPTLRRLPTHIQLADTSKFLVKIPEEPTDKNPETVNRFEYSDHMTFSCESKEERDQRILDYPSEVSGKNSQRKEFNTKEPQGMQKGDLFKAEYVFIVDSDGEDEATCRQGEQGPPGATGNIATRPKSLAISSSLASDVVRPKVRGVDVKVSSHPEIPHGIAPQQKHGQLTSPTTSEQLAHKPPAFSFVSPTNQKTPPVPAKVSGTTVLEEFHIRRLDVHGASEEETATYFHTTAHDSPLPAWKGASTLVFSPSAQLPGSSLCGSNVADHTRGLAPEAQKKVSTSSALNPREDVRTSPSPASGASLRSPSASYIPVRIVMHSLSPSPKPLTSSSHGSLSTVCSQTSSSGNLSKSGLKSPVPSRLSLLTAILKSNPSHQRPLSPASCPTFSLNSLASSTLTLDQKIKQTPSTPKKSLSSCSLTTGSTEQEQASAESHQPCHLSFFSKTTPLSQAQPPSPPALASSSYAATDTEKIPGSTLRSSTTPPQSQTDLFSLADVPSVTPGLSPLSSSKGRKDGDLRAPEKNRNICTRPSTLSFIPPINESTALSSSGKCFHPSPALSDLIDRSKRTCSQRHSDQRPNPSALPTPPVSRAGSASHPHLGYSILPPESSLTQALQRSPSALHPSCGSATCPSRTGMPDSTASNRSSRVSTPSLPVSLTRTKELISPCALSMSAGPENKKPKQYKTKSSYKAFAAIPTNTLLLEQKALDEPARTESNSKASVSDLPVELCFPAQLRQQTEELCATIDKVLQDSLSMHSSDSPSRPSQTMLGSETIKTPTTHPRAAGRETKYANLSSSSSTTSESQLTKPGVIRPVPIKSKLFLKKEEEVYEPNPFSKYLEDSSGLFSEQDMAIPHKPVSLHPLYQSKLYPPAKSLLRPQTLSHADCLTPGPFSHLSSFSLRDEQEKSPTLLSQDTYNKPGHPMVTIPEHDTLDSKE
Muscular LMNA-interacting protein (Cardiac Isl1-interacting protein) (CIP)
Rattus norvegicus (Rat)
10,116
966
103,653
Alternative splicing;Cell membrane;Cytoplasm;Membrane;Nucleus;Phosphoprotein;Reference proteome
GO:0000122; GO:0003714; GO:0005521; GO:0005634; GO:0005635; GO:0005829; GO:0006366; GO:0010614; GO:0016605; GO:0031981; GO:0042383; GO:0045944; GO:1903243
Evidence at protein level
5
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5FW52}. Nucleus envelope {ECO:0000250|UniProtKB:Q5FW52}. Nucleus, PML body {ECO:0000250|UniProtKB:Q5FW52}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5FW52}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q5FW52}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5FW52}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5FW52}.
null
null
PF15274;
IPR029331;
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), Rattus (genus)
Mlip Cip
false
54
A0A096P8D3
MTRVERGRVLARAIERAVAHRASARRWTTTTRTPAWMVTGWMGGRGVDRSTAMTRFERCGSTASSKITAAPMVYVRGEEMTAYVMDLIRSRWIEPRVDVGGWETFDLRAKNRDDTEDRVLRDVIEAGKRIKAIFKEPTVTPTADQVKRLGLRKSWGSPNGAMRRGWNGITISRDTIHIDGVELGYKKPVLFERHAVGGEYSAGYKNVGKGKLTTTFTPSEGPDAGKTVVVDEREIVDEEAAVVTYHNPYDNVHDLARFFFGRCLEAKVTPYVVTKKTVFKWQEPFWQIMRTVFDEEFKAQFVAAGVMKEGEELVHLLSDAATMKLVQWRQGGFGMAAHNYDGDVLTDELAQVHKSPGFITSNLVGVHEDGTLIKEFEASHGTVADMDEARLRGEETSLNPLGMVEGLIGAMNHAADVHNIDRDRTHAFTTKMRTVIHQLFREGKGTRDLCGPSGLTTEQFIDAVAERLDA
Isocitrate dehydrogenase (NAD(+)), mitochondrial (OtIDH) (EC 1.1.1.41)
Ostreococcus tauri
70,448
470
52,553
3D-structure;Magnesium;Manganese;Metal-binding;Mitochondrion;NAD;Oxidoreductase;Reference proteome;Transit peptide;Tricarboxylic acid cycle
GO:0000287; GO:0004449; GO:0004450; GO:0005739; GO:0006099; GO:0006102; GO:0006739; GO:0019674; GO:0042803
Evidence at protein level
5
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
null
null
PF00180;
IPR004790;IPR024084;
6IXL;6IXN;6IXT;7E2W;
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Chlorophyta (phylum), Mamiellophyceae (class), Mamiellales (order), Bathycoccaceae (family), Ostreococcus (genus)
IDH Ot_13g02940 BE221DRAFT_192402
false
55
A0A097PTA8
MKLSTSLLAIVAVASTFIGNALSATTVPGCFAECIDKAAVAVNCAAGDIDCLQASSQFATIVSECVATSDCTALSPGSASDADSINKTFNILSGLGFIDEADAFSAADVPEERDLTGLGRVLPVEKRQNCPTRRGLCVTSGLTACRNHCRSCHRGDVGCVRCSNAQCTGFLGTTCTCINPCPRC
Fungal defensin copsin
Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata)
5,346
184
18,954
3D-structure;Antibiotic;Antimicrobial;Cleavage on pair of basic residues;Defensin;Direct protein sequencing;Disulfide bond;Lipid-binding;Membrane;Pyrrolidone carboxylic acid;Secreted;Signal;Target cell membrane;Target membrane
GO:0005576; GO:0008289; GO:0016020; GO:0042742; GO:0044218
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25342741, ECO:0000305|PubMed:28825809}. Target cell membrane {ECO:0000269|PubMed:25342741, ECO:0000305|PubMed:28825809}. Note=specific localization at active cell wall synthesis sites. {ECO:0000269|PubMed:25342741}.
SIGNAL 1..23; /evidence="ECO:0000255"
null
PF18251;
IPR041284;
2MN5;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Basidiomycota (phylum), Agaricomycotina (subphylum), Agaricomycetes (class), Agaricomycetidae (subclass), Agaricales (order), Agaricineae (suborder), Psathyrellaceae (family), Coprinopsis (genus)
null
false
56
A0A098D6U0
MAPNKKTILLFGDQTDSWVDGIDRLYQDAASIPWLQSFLDDLTHTFKTHTVGMDAVLRNSLGDFANLQELAEKYRYTTDDVGMAQAFLIYAVRAGILLKWAKYEPSLLSTDENQPEWVGISGGLISLSVLAVAETFEKLYEACLEVAGLLARLCRFTSVKSRSMEDRSGAWGWTVLGIGANELRNALDQYQQSMGIPPIKRAQVAVTGHRWNTIVGPPSILQLIVKECPAIRSLPKNELNIHALQHTVVTSRADLDYIVGDSTLLSQPLSLTFTLWGMDDPRAHYTTWGDMLRAICSQALSRPLDITHVVDQLSSKLRSFPQLDVKSIGPCSHLSYLTNVLKSAGRTVSVADDHPPSTPPKQLPGRIAIVGMAGRGPGSDNVEEFWNVIMSKLDLCEEIPEDRFNLSEFYRSKHDSGCTTTTKFGCFMDKPGHFDNRFFHISPREALLMDPGHRQFLMTTYEALEMAGYSDGATRAVDPARIATFFGQCNDDWHDVSHHTLGCDAYTLQGVQRAFGAGRIAFQFKWEGPTYSLDSACASTASSIHLACTSLLAKETDMAVAGAANVVGYPHSWTSLSKSGVLSDTGNCKTFRDDADGYCRADFVGTVVLKRLEDAIAHNDNILAVVAASGRNHSGNSSSITTSDAKAQEKLYRKMMHNARVSPNDISYVEMHGTGTKVGDPAEMGALASLFSHRRTPKPVVVGGVKANVGHSESKQAAGVASLLKCIMMFQKNILPPQAGMPHALNPNFPPLSEINIEIPSEPSTFESPVSQPRRILLNNFDAAGGNACILLEDFGNNMVKKSDPRVHHTVVTSSRTQASYHGNKAKLLQWLRQNPGARIEDVAYTTTARRTHHPIRFAVTASSTQELISKLEADTADSPAAKESPVVFVFTGQGSHYAGMGSELYETSPVFRETVNLCATICEEQNFPPFLDLITQSDSEMSDKTTLEVQLAVLTLEIGLAALWRSIGIQPSVVIGHSLGEYAALHVSGVLSLADVLYLVGQRALLILQRCEVNTSAMLSVAMPVTDTHAFLEAQADPSCEIACVNSTNASVISGSIENITELQAGLKARSKMLSVPYGFHSSQMDPILADYAALAGGVTFSEPKIPVASTLLASLVDTSGTFHAGYMARQCRQPVNFVGALEAIQSNYSDPIWLEIGPSQVCSSFVRATLSPPPSKILSTLDKGTNAWLSLGKCMSSLYKHGATIDWLALHQPYVDNLSLLNLPTYAWDLKEFWIRYTETKDQLPTSTTNGHETFKANISTCAQQVVEHISPPNMKVTFRASLSDPGFKALIDGHRLRDRSVCPGSVFSEAGLAAVTYVLQLHHSKSLKLPALVLRNLSLKRPLTYDLVGPDGELITVVAPGGSSNDTFKVAWKASKGNVSYSLGDCMVAACDGQLIQARWDKVSYFIRSRVDEIVASSKSGISHRLQPQILYGLFANTVKYDAAFKCIQEAYISSDFQEAAAVIVLNSDPVGTKFVASPYWGESLVHLAGFVVNSNPSRQSHDTTFMMDGFESFEQTVIPEPGKPYHTYVRVTGNESASVVCDVYIFDDDKLIMHCAGLHFHEVENAVLDQLLGGTNTSNTTRDQPAPIMSRKEVPKPVDTTEKVEAVSNDSQSDAHVLDSILKIISKETGSDLADFQDDTLIADLGVDSIMAIEIASQVTEETGMDLLPSFIIDYPAIGDLRRVFAPKSTHISLDNDLSRPSLVDDTSQALQSSGSESFDQPPTSVTSTSDSGSIVKIDLGPDVDSPAPKIKITLLQGRPGNGRTPFYLIADGTGTIATYIHLPQFKSQIPIYGIDSPFLRCPTRFTTDVGITGAARFITEALMKAQPEGTFVLGGFSGGAMLAYEVCRQLAAANRKVDSLMLIDMCSPRSKTVEDKNDIGWAIFESISRQNGLWRSTDMTRQHLQAIFAAVATYHPQPLKASERPKRTAIIWAEKGMIDRCAGDSELMQKLAKRGIPTEPYPKFMEDSELGPVAWGLPHKTKNDLGPNGWERYVGDALCLSMPADHLEMPMPGHVHLLHEKMTRAFEFFNEAG
Non-reducing polyketide synthase ZEA1 (EC 2.3.1.-) (Macrolactone megasynthetase) (Polyketide synthase 13) (PKS13) (Zearalenone biosynthesis polyketide synthase 1)
Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum)
229,533
2,038
222,411
Multifunctional enzyme;Phosphopantetheine;Phosphoprotein;Reference proteome;Transferase
GO:0004312; GO:0004315; GO:0006633; GO:0016218; GO:0031177; GO:0106150
Evidence at protein level
5
null
null
null
PF00698;PF22621;PF00109;PF02801;PF00550;PF16073;PF00975;
IPR029058;IPR001227;IPR036736;IPR014043;IPR016035;IPR018201;IPR014031;IPR014030;IPR016036;IPR020841;IPR042104;IPR049900;IPR050091;IPR020806;IPR009081;IPR006162;IPR030918;IPR032088;IPR001031;IPR016039;
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), Hypocreales (order), Nectriaceae (family), Fusarium (genus), Fusarium sambucinum species complex (no rank), Gibberella zeae (species)
ZEA1 PKS13 FGRAMPH1_01T05749 FGSG_02395
false
57
A0A0A0LLY1
MASSSVEFRCFVGGLAWATDSNSLEKAFSVYGEIVEAKIVSDRETGRSRGFGFVTFLEEEAMRSAIEAMNGHILDGRNITVNEAQQRGGGGGGGYNRGGGYGGRRDGGGFSRGGGGGYGGGGGGGYGGGRDRGYGGGGGYGGGRDSRGSGGGGSEGGWRN
Small RNA binding protein 1 (CsSRBP1)
Cucumis sativus (Cucumber)
3,659
160
15,973
Plant defense;Reference proteome;RNA-binding;Secreted
GO:0003727; GO:0003729; GO:0005615; GO:0006858; GO:0006952; GO:0035197; GO:0035198; GO:0050658; GO:0050688; GO:1990428
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31812689}. Note=Observed in the phloem translocation stream. {ECO:0000269|PubMed:31812689}.
null
null
PF00076;
IPR012677;IPR035979;IPR048289;IPR000504;IPR052462;
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), Cucurbitales (order), Cucurbitaceae (family), Benincaseae (tribe), Cucumis (genus)
SRBP1 Csa_2G247040
false
58
A0A0A1C3I2
MDVRRRLPPKLRRPLPITESSHHHRKTPFPADVDRSPSPTPKASDALPLPLYLTNGIFFTLFFSVAYYLLHRWRDKIRSSTPLHIVTLSELAAIVSLIASFIYLLGFFGIDFVQSFVSRADVDVDIDVEPDILEADRRPCSKLMDQPPPPPVVMSSEEDEEIVKSVVSGKTPSYSLESKLGDCYRAASIRREAVQRTTGRSLLGLPLDGFDYESILGQCCEMPIGYVQIPVGIAGPLLLNGCEYVVPMATTEGCLVASTNRGCKAIYACGGATGILLKDGMTRAPVVRFSTAKRASDLKFFLEDPLNFDTLAVVFNKSSRFARLQSIQCSMAGKNLYIRFCCSTGDAMGMNMVSKGVQNVLEFLQSDFPDMDVIGISGNFCSDKKPAAVNWIEGRGKSVVCEAIITDDVVKKVLKTTVPALVELNMLKNLAGSAVAGALGGFNAHAANIVSAVFIATGQDPAQNIESSHCITMMEAINNGKDLHISVTMPSIEVGTVGGGTQLASQSACLNLLGVKGANKESHGSNSRLLATIVAGSVLAGELSLMSAIAAGQLVRSHMKYNRSSRDMSKIGS
3-hydroxy-3-methylglutaryl coenzyme A reductase 1 (HMG-CoA reductase 1) (Hydroxymethylglutaryl-CoA reductase) (PgHMGR1) (EC 1.1.1.34)
Panax ginseng (Korean ginseng)
4,054
573
61,680
Chloroplast;Endoplasmic reticulum;Glycoprotein;Isoprene biosynthesis;Membrane;NADP;Oxidoreductase;Peroxisome;Plastid;Transmembrane;Transmembrane helix
GO:0004420; GO:0005778; GO:0005789; GO:0009646; GO:0009753; GO:0015936; GO:0016104; GO:0016126; GO:0016135; GO:0031969
Evidence at transcript level
5
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24569845}; Multi-pass membrane protein {ECO:0000255}. Plastid, chloroplast membrane {ECO:0000269|PubMed:24569845}; Multi-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:24569845}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in intracellular vesicles. {ECO:0000269|PubMed:24569845}.
null
TRANSMEM 46..66; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 93..113; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 529..549; /note="Helical"; /evidence="ECO:0000255"
PF00368;
IPR002202;IPR023074;IPR023076;IPR004554;IPR023282;IPR009023;IPR009029;
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), Apiales (order), Apiineae (suborder), Araliaceae (family), Panax (genus)
HMGR1 HMGR
false
59
A0A0A1C930
MDVRRRPVKSLSSAKTATAGEPPKSQQQHPKASDALPLPLYLTNGLFFTMFFSVMYFLLHRWREKIRNSTPLHVVTLSELAALVLLMASVIYLLGFFGIGFVRSVIRPSPDAWDILEDDNAINEEDSRREPCAEAIDCSLPPKPKIVHMVPQKALNPKSAFADMMVEQPALAIAPLTEEDEEIVKSVVTGKIPSYSLESKLGDCKKAASIRREALQRITGKSLAGLPLDGFDYKSILGQCCEMPVGYVQIPVGIAGPLLLNETEYSVPMATTEGCLVASTNRGCKAIYASGGATSVLLRDGMTRAPVVRFSTVKRAAELKFFLEEPLNYDTPAHVFNKSSRFGRLQGIKCAVAGKNLYIRFTCSTGDAMGMNMVSKGVQNVLDFLQSDFPDMDVMGISGNYCSDKKPAAVNWIEGCGKSVVCEAIIKEEVVKKVLKTNVAALVELNMLKNLAGSAVAGALGGFNAHASNIVSAVYISTGQDPAQNVESSHCITMMEAVNNGKDLHISVTMPSIEVGTVGGGTQLASQSACLNLLGVKGASKESPGSNSRLLASIVAGSVLAGELSLMSALAAGQLVKSHMKYNRSSKDITKLSS
3-hydroxy-3-methylglutaryl coenzyme A reductase 2-A (HMG-CoA reductase 2) (Hydroxymethylglutaryl-CoA reductase) (PgHMGR2) (EC 1.1.1.34)
Panax ginseng (Korean ginseng)
4,054
594
63,621
Chloroplast;Endoplasmic reticulum;Glycoprotein;Isoprene biosynthesis;Membrane;NADP;Oxidoreductase;Peroxisome;Plastid;Transmembrane;Transmembrane helix
GO:0004420; GO:0005778; GO:0005789; GO:0009753; GO:0015936; GO:0016104; GO:0016126; GO:0016135; GO:0031969
Evidence at transcript level
5
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A0A1C3I2}; Multi-pass membrane protein {ECO:0000255}. Plastid, chloroplast membrane {ECO:0000250|UniProtKB:A0A0A1C3I2}; Multi-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000250|UniProtKB:A0A0A1C3I2}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in intracellular vesicles. {ECO:0000269|PubMed:24569845}.
null
TRANSMEM 38..58; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 82..102; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 550..570; /note="Helical"; /evidence="ECO:0000255"
PF00368;
IPR002202;IPR023074;IPR023076;IPR004554;IPR023282;IPR009023;IPR009029;
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), Apiales (order), Apiineae (suborder), Araliaceae (family), Panax (genus)
HMGR2
false
60
A0A0A1H8I4
MFPRLPTLALGALLLASTPLLAAQPVTTLTVLSSGGIMGTIREVAPAYEKATGVKLDIAAAPSMGDTPQAIPNRLARNEPADVVLMVGSALDKLVASGQVAKDSRVDLGQSFIAMAVRQGAPKPDISNMDAFKQTLEKAQSVAYSDSASGVYLSRILFPRMQLDKSFMAKARMIPAEPVGAVVARGEAQLGFQQLSELKAVPGIDIVGLIPDQAQKMTLYSGAMVSKSQHPEAARALLQYLASKDAAKAIEDSGLKPVPAQP
Aconitate isomerase (AI) (EC 5.3.3.7)
Pseudomonas sp
306
262
27,449
Direct protein sequencing;Isomerase;Signal
GO:0015689; GO:0030973; GO:0046680; GO:0046689; GO:0047614; GO:0071277; GO:0071281; GO:0071286; GO:0071287; GO:0071289; GO:0071292
Evidence at protein level
5
null
SIGNAL 1..22; /evidence="ECO:0000269|PubMed:26293748"
null
PF13531;
IPR050682;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Pseudomonadales (order), Pseudomonadaceae (family), Pseudomonas (genus), unclassified Pseudomonas (no rank)
ais
false
61
A0A0A1HA03
MMGDLTTSFPATTLTTNDQPHVVVCSGAGMGHLTPFLNLASALSSAPYNCKVTLLIVIPLITDAESHHISSFFSSHPTIHRLDFHVNLPAPKPNVDPFFLRYKSISDSAHRLPVHLSALSPPISAVFSDFLFTQGLNTTLPHLPNYTFTTTSARFFTLMSYVPHLAKSSSSSPVEIPGLEPFPTDNIPPPFFNPEHIFTSFTISNAKYFSLSKGILVNTFDSFEPETLSALNSGDTLSDLPPVIPIGPLNELEHNKQEELLPWLDQQPEKSVLYVSFGNRTAMSSDQILELGMGLERSDCRFIWVVKTSKIDKDDKSELRKLFGEELYLKLSEKGKLVKWVNQTEILGHTAVGGFLSHCGWNSVMEAARRGVPILAWPQHGDQRENAWVVEKAGLGVWEREWASGIQAAIVEKVKMIMGNNDLRKSAMKVGEEAKRACDVGGSSATALMNIIGSLKR
UDP-glycosyltransferase 708C1 (EC 2.4.1.360) (C-glucosyltransferase a) (FeCGTa) (UDP-glucose:2-hydroxyflavanone C-glucosyltransferase)
Fagopyrum esculentum (Common buckwheat) (Polygonum fagopyrum)
3,617
457
50,375
3D-structure;Direct protein sequencing;Glycosyltransferase;Transferase
GO:0035251; GO:0120514
Evidence at protein level
5
null
null
null
PF00201;
IPR050481;IPR002213;IPR035595;
6LLG;6LLW;6LLZ;7CYW;
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), Caryophyllales (order), Polygonaceae (family), Polygonoideae (subfamily), Fagopyreae (tribe), Fagopyrum (genus)
UGT708C1 CGTa
false
62
A0A0A1I6E7
MEIKYLLTVFLVLLIVSDHCQAFLFSLIPHAISGLISAFKGRRKRDLDGQIDRFRNFRKRDAELEELLSKLPIY
Antimicrobial peptide AcrAP1
Androctonus crassicauda (Arabian fat-tailed scorpion)
122,909
74
8,679
Amidation;Antibiotic;Antimicrobial;Cleavage on pair of basic residues;Fungicide;Membrane;Secreted;Signal;Target cell membrane;Target membrane
GO:0005576; GO:0016020; GO:0031640; GO:0042742; GO:0044218; GO:0050832
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25332684}. Target cell membrane {ECO:0000250}. Note=Forms a helical membrane channel in the prey. {ECO:0000250}.
SIGNAL 1..22; /evidence="ECO:0000269|PubMed:25332684"
null
null
null
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), Buthida (parvorder), Buthoidea (superfamily), Buthidae (family), Androctonus (genus)
null
false
63
A0A0A1I6N9
MEIKYLLTVFLVLLIVSDHCQAFLFSLIPNAISGLLSAFKGRRKRNLDGQIDRFRNFRKRDAELEELLSKLPIY
Antimicrobial peptide AcrAP2
Androctonus crassicauda (Arabian fat-tailed scorpion)
122,909
74
8,655
Amidation;Antibiotic;Antimicrobial;Cleavage on pair of basic residues;Fungicide;Membrane;Secreted;Signal;Target cell membrane;Target membrane
GO:0005576; GO:0016020; GO:0031640; GO:0042742; GO:0044218; GO:0050832
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25332684}. Target cell membrane {ECO:0000250}. Note=Forms a helical membrane channel in the prey. {ECO:0000250}.
SIGNAL 1..22; /evidence="ECO:0000269|PubMed:25332684"
null
null
null
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), Buthida (parvorder), Buthoidea (superfamily), Buthidae (family), Androctonus (genus)
null
false
64
A0A0A6ZFY4
MDNQNGRISIALLPFLAHGHISPFFELAKQLAKRNCNVFLCSTPINLSSIKDKDSSASIKLVELHLPSSPDLPPHYHTTNGLPSHLMLPLRNAFETAGPTFSEILKTLNPDLLIYDFNPSWAPEIASSHNIPAVYFLTTAAASSSIGLHAFKNPGEKYPFPDFYDNSNITPEPPSADNMKLLHDFIACFERSCDIILIKSFRELEGKYIDLLSTLSDKTLVPVGPLVQDPMGHNEDPKTEQIINWLDKRAESTVVFVCFGSEYFLSNEELEEVAIGLEISTVNFIWAVRLIEGEKKGILPEGFVQRVGDRGLVVEGWAPQARILGHSSTGGFVSHCGWSSIAESMKFGVPVIAMARHLDQPLNGKLAAEVGVGMEVVRDENGKYKREGIAEVIRKVVVEKSGEVIRRKARELSEKMKEKGEQEIDRALEELVQICKKKKDEQ
UDP-glucosyltransferase 29 (UGTPg29) (EC 2.4.1.365) (UDP-glucosyltransferase 94B1) (PgUGT94B1) (UDP-glucosyltransferase 94Q2) (PgUGT94Q2)
Panax ginseng (Korean ginseng)
4,054
442
49,133
3D-structure;Glycosyltransferase;Isoprene biosynthesis;Transferase
GO:0002238; GO:0008194; GO:0016114; GO:0016135; GO:0046246
Evidence at protein level
5
null
null
null
PF00201;
IPR002213;IPR035595;
8JZQ;8K08;8K09;
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), Apiales (order), Apiineae (suborder), Araliaceae (family), Panax (genus)
UGT29 UGT94B1 UGT94Q2
false
65
A0A0A7EPL0
MVIPATSRFGFRAEFNTKEFQASCISLANEIDAAIGRNEVPGNIQELALILNNVCRRKCDDYQTRAVVMALMISVKSACQLGWFPERETQELLAIIDLMWNGFSCPENVTSCVNSPVTLISQVIERFYPCVKLGHILVSFEAKPESKMMMKDFHISKKMPHSPKQKVGLFVVRTEDISRSNCIVHPQGVSFLLNGKGIDKRVNISMESGPQLPTNVTALLNLGANLLQAIGCFGGSYLIAIAFMDVIPLPNKPLLKDYVHPEVVGSNSDCDIIEGPSRISLSCPISRTRIKLPVKGHVCKHLQCFDFWNYVNMNTRRPSWRCPHCNQSVCYTDIRVDQKLRKILEEVGRNAADVVISADGTWMVETENDEDVELVPETTHDHGDPNSFINLGPTVKNPARDENEMETSTQVEEHNPCLSEIQGPSNDTHRPASDYTMLNQSHTSTNTLPQLPRTLNAFDGQQFVNLPQVINTRDSPASQALPMTFSPTPSPQDILATNAANFGTSMPAAQSSQFQGSHVTSLGNCEGRTSDLMARWNHIYGRVQTQFPPAPLSHHHYSMQNQSPSPAQQRPVPSYIAHPQTFHVNYGENADQRWMPSSIAHPQTLPVNYGGNTNQRPIPSSIAHPQTLPVNYRGNTDHRSTPYSITHLQTLLNYGGNADQRPMPSSITNLQTLPATYGGYAHQRPMSSSITHPRTSPVNYGGTPDQRPMPSSITHPQTLPVSYGGTTDQILNPGGAMGQFSSREFMNLTPANTENWRPQSRMRGSVAPGTGYDHMIIHPTRPVHPQAQTPPAPLSTSYDGADEIQAFIGHPSYPVSNNETQAGTSSLPVAEGLGYSGSFWSMPPETW
E4 SUMO-protein ligase PIAL1 (EC 2.3.2.-) (Protein EMBRYO DEFECTIVE 3001) (Protein INHIBITOR OF ACTIVATED STAT-LIKE 1)
Arabidopsis thaliana (Mouse-ear cress)
3,702
847
93,475
Alternative splicing;Ligase;Metal-binding;Nucleus;Reference proteome;Repeat;Transferase;Ubl conjugation pathway;Zinc;Zinc-finger
GO:0005634; GO:0006970; GO:0008270; GO:0009651; GO:0009737; GO:0016874; GO:0016925; GO:0019789; GO:0051176; GO:0060966
Evidence at protein level
5
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
PF02891;
IPR004181;IPR013083;
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)
PIAL1 EMB3001 At1g08910 F7G19.21
false
66
A0A0A7EQR3
MFKPSFVALALVSYATAQASAPQWGQCGGIGWTGPTACPSGWACQQLNAYYSQCLQGAAPAPARTTAAPPPPPATTAAPPPPTTSAPTGSSPVAGACGAIASTVPNYNNAKLPDPFTFANGTALRTKADWSCRRAEISALIQNYEAGTLPPKPPVVTASFSKSGNTGTLAITAGLSNSQTIKFSPTISYPSGTPPANGWPLIIAYEGGSIPIPAGVATLTYSNSDMAQQNSASSRGQGLFYQLYGSTHSASAMTAWVWGVSRIIDALEMTPTAQINTQRIGVTGCSRDGKGALMAGAFEERIALTIPQESGSGGDACWRLSKYEIDNGNQVQDAVEIVGENVWFSTNFNNYVQKLPTVPEDHHLLAAMVAPRAMISFENTDYLWLSPMSSFGCMTAAHTVWQGLGIADSHGFAQVGGHAHCAWPSSLTPQLNAFINRFLLDQSATTNVFTTNNQFGKVQWNAANWITWTTPTLT
4-O-methyl-glucuronoyl methylesterase (EC 3.1.1.117) (Glucuronoyl esterase) (GE)
Cerrena unicolor (Canker rot fungus) (Daedalea unicolor)
90,312
474
49,910
3D-structure;Disulfide bond;Glycoprotein;Hydrolase;Lignin degradation;Secreted;Serine esterase;Signal
GO:0005576; GO:0005975; GO:0030248; GO:0046274; GO:0052689
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25425346}.
SIGNAL 1..17; /evidence="ECO:0000255"
null
PF00734;PF22244;
IPR029058;IPR035971;IPR000254;IPR054579;
6RTV;6RU1;6RU2;6RV7;6RV8;6RV9;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Basidiomycota (phylum), Agaricomycotina (subphylum), Agaricomycetes (class), Agaricomycetes incertae sedis (no rank), Polyporales (order), Cerrenaceae (family), Cerrena (genus)
null
false
67
A0A0A7GEY4
MISEIIKDRAKLVNEKIEELLKEQEPEGLYRAARHYLKAGGKRLRPVITLLSAEALGEDYRKAIHAAIAIETVHNFTLVHDDIMDEDEMRRGVKTVHTLFGIPTAILAGDTLYAEAFEILSMSDAPPENIVRAVSKLARVCVEICEGQFMDMSFEERDSVGESEYLEMVRKKTGVLIGISASIPAVLFGKDESVEKALWNYGIYSGIGFQIHDDLLDISGKGKIGKDWGSDILEGKKTLIVIKAFEEGIELETFGKGRASEEELERDIKKLFDCGAVDYARERAREYIEMAKKNLEVIDESPSRNYLVELADYLIERDH
Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10)
Geoglobus acetivorans
565,033
319
35,918
3D-structure;Isoprene biosynthesis;Magnesium;Metal-binding;Transferase
GO:0004161; GO:0004311; GO:0004337; GO:0033384; GO:0033386; GO:0045337; GO:0046872
Evidence at protein level
5
null
null
null
PF00348;
IPR008949;IPR000092;IPR033749;
5JFQ;
cellular organisms (no rank), Archaea (domain), Methanobacteriati (kingdom), Methanobacteriota (phylum), Archaeoglobi (class), Archaeoglobales (order), Archaeoglobaceae (family), Geoglobus (genus)
GACE_1337
false
68
A0A0A7HFE1
MKKEKIDLFYGALLHDIGKVIQRATGERKKHALVGADWFDEIADNQVISDQIRYHMANYQSDKLGNDHLAYITYIADNIASGVDRRQSNEESDEDASAKIWDTYTNQADIFNVFGAQTDKRYFKPTVLNLKSKPNFASATYEPFSKGDYAAIATRIKNELAEFEFNQAQIDSLLNLFEAILSFVPSSTNSKEIADISLAEHSRLTAAFALAIYDYLEDKGRHNYKEDLFTKASAFYEEEAFLLASFDLSGIQDFIYNIATSGAAKQLKARSLYLDFMSEYIADSLLDKLGLNRANLLYVGGGHAYFVLANTEKTVETLVQFEKDFNQFLLANFQTRLYVAFGWGSFAAKDIMSELNSPESYRQIYQKASRMISEKKISRYDYRTLMLLNRGGKSSERECEICHSVENLVSYHDQKVCDICRGLYQFSKEIAHDHFIITENEGLPIGPNACLKGVAFEKLSQESFSRVYVKNDYKAGTIKATHVFVGDYQCDEIHKYAALSKNEDGLGIKRLAVVRLDVDDLGAAFMAGFSRQGNGQYSTLSRSATFSRSMSLFFKVYINQFASDKKLSIIYAGGDDVFAIGSWQDIIAFTVELRQNFIKWTNGKLTLSAGIGLFADKTPISLMAHQTGELEEAAKGNEKDSISLFSSDYTFKFDRFITNVYDDKLEQIRYFFNHQDERGKNFIYKLIELLRNYESEEKMNVARLAYYLTRLEELTDKDERDKFKQFKKLFFKWYTNNESDRKEAELALLLYVYEIRKD
CRISPR system single-strand-specific deoxyribonuclease Cas10/Csm1 (subtype III-A) (ssDNase Cas10) (EC 3.1.-.-) (Cyclic oligoadenylate synthase) (EC 2.7.7.-) (StCas10)
Streptococcus thermophilus
1,308
758
86,822
3D-structure;Antiviral defense;ATP-binding;Endonuclease;Exonuclease;Hydrolase;Nuclease;Nucleotide-binding;RNA-binding;Transferase
GO:0003723; GO:0004519; GO:0004527; GO:0005524; GO:0016740; GO:0051607
Evidence at protein level
5
null
null
null
PF22335;PF20824;PF18211;PF01966;
IPR054767;IPR013408;IPR052117;IPR048693;IPR041062;IPR000160;IPR006674;IPR043128;
6NUD;6NUE;
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus)
cas10 csm1
false
69
A0A0A7HIF0
MTFAKIKFSAQIRLETGLHIGGSDAFAAIGAIDSPVIKDPITNIPIIPGSSLKGKMRTLLAKVYNEKVAEKPSDDSDILSRLFGNSKDKRFKMGRLIFRDAFLSNADELDSLGVRSYTEVKFENTIDRITAEANPRQIERAIRNSTFDFELIYEITDENENQVEEDFKVIRDGLKLLELDYLGGSGSRGYGKVAFEKLKATTVFGNYDVKTLNELLTAEV
CRISPR system Cms endoribonuclease Csm3 (Csm3 RNase) (EC 3.1.-.-) (CRISPR type III A-associated RAMP protein Csm3)
Streptococcus thermophilus
1,308
220
24,569
3D-structure;Antiviral defense;Endonuclease;Hydrolase;Nuclease;RNA-binding
GO:0003723; GO:0004519; GO:0051607
Evidence at protein level
5
null
null
null
PF03787;
IPR013412;IPR052216;IPR005537;
6NUD;6NUE;
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus)
csm3
false
70
A0A0A7HIX6
MKILISAVGTTDPISNNHDAALLHIARNYRPDKIVLVYSQEMMVKQDLINKVLLSIEGYNPIIEIDSTILNNDEVFLFDKMYEVMGQIVQKYTNDDNEIILNLSSGTPQIISALFALNRINDYNTQAIQVATPKNRANREYTALTESEIDALIMENQDNRLDFVDRSIKDKSEKFTQALVKRHLRSLIASFDYQAAEAIINRKEYNKLLSKKKIAYIREKLYDFSRVFKNQSILSDILSFPLDDSQKKALNYYLMIDVLKEREHIADVLIKAKSLAEFVIEETIKKDHEGLIVFDGNLPKLNPSFPDCEAILDDIDKKMKKSRGIEDTEERIFSVQSTLNLLSYLNILEFYEYDSQLQTAINGILSLNGERNKVAHGLSEIDTRLLSRKKLKQLSENLRLLLVDCLGIDSSYFNYYDKQNKELIKMLE
CRISPR system endoribonuclease Csm6 (EC 3.1.-.-) (CRISPR type III-A associated protein Csm6-1)
Streptococcus thermophilus
1,308
428
49,361
Antiviral defense;Endonuclease;Hydrolase;Nuclease;Nucleotide-binding;RNA-binding
GO:0000166; GO:0003723; GO:0004519; GO:0051607
Evidence at protein level
5
null
null
null
PF22208;PF09659;
IPR013489;IPR053955;IPR053941;
null
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus)
csm6
false
71
A0A0A8IDB7
MRSSSLAWALGLVALANAQGSPTQWYDSITGVTFSRFYQQDTDASWGYIFPSASGGQAPDEFIGLFQGPASAGWIGNSLGGSMRNNPLLVGWVDGSTPRISARWATDYAPPSIYSGPRLTILGSSGTNGNIQRIVYRCQNCTRWTGGAGGIPTTGSAVFGWAFHSTTKPLTPSDPSSGLYRHSHAAQYGFDIGNARTTLYDYYLQQLTNAPPLSGGAPTQPPTQQPPTTTAPPPPPPSSTFVSCPGAPQPRYQMNVANGFRVAPVLGGLTMPRGITLDTRGNLLVVERGRGLTGHTLDANGCVTSSKVVIQDTQINHGIDVHPSGRRIIASSGDIAWSWDYDPATMTATNRRTLVTGMNNFYHFTRTVHISRKYPNLFALNVGSDGNIDVPTRQQNSGRAQIRVFDYDQLPQNGVPFVSQYGRVLGYGLRNDVGITEDRAGNIHSIENSLDNAYRMVNGQRRDIHTNNPAEKVYNLGDPSNPRAIFGGYPDCYTVWEPSDFTDSPKQPGDWFTQDNSGQYTDAWCNANAVKPTLLLPPHTAPLDMKFGLGNDTNLYVALHGSWNRQPPQGYKVVVVPGQYSASGEWSPTAPLAQSRTAWSDLLTNRNENQCSGFGNANCFRPVGLVWSADGQNLYVSSDTSGEVFIIKRMSGPIVQPPITQPPITTSPPTPTTPPVVQPPTTVAPPQASQTLWGQCGGQGWTGPTLCPANSVCRESNQWYSQCVPA
Pyrroloquinoline quinone-dependent pyranose dehydrogenase (PDH) (EC 1.1.99.-) (AA12 family sugar dehydrogenase) (Pyrroloquinoline quinone-dependent sugar dehydrogenase) (SDH)
Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata)
5,346
726
78,379
Calcium;Disulfide bond;Glycoprotein;Heme;Iron;Metal-binding;Oxidoreductase;Secreted;Signal
GO:0005576; GO:0005975; GO:0016491; GO:0030248; GO:0046872
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25121592}.
SIGNAL 1..18; /evidence="ECO:0000255"
null
PF00734;PF16010;PF22807;
IPR011042;IPR035971;IPR015920;IPR000254;IPR005018;IPR054539;IPR011041;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Basidiomycota (phylum), Agaricomycotina (subphylum), Agaricomycetes (class), Agaricomycetidae (subclass), Agaricales (order), Agaricineae (suborder), Psathyrellaceae (family), Coprinopsis (genus)
PDH SDH
false
72
A0A0B0QJR1
MTNIEPVIIETRLELIGRYLDHLKKFENISLDDYLSSFEQQLITERLLQLITQAAIDINDHILSKLKSGKSYTNFEAFIELGKYQILTPELAKQIAPSSGLRNRLVHEYDDIDPNQVFMAISFALQQYPLYVRQINSYLITLEEEND
tRNA nuclease HepT (EC 3.1.27.-) (Toxin HEPN) (tRNA nuclease HEPN)
Aphanizomenon flos-aquae (strain 2012/KM1/D3)
1,532,906
147
17,110
3D-structure;Endonuclease;Hydrolase;Nuclease;Nucleotide-binding;Phosphoprotein;Toxin-antitoxin system
GO:0000166; GO:0004519; GO:0004540; GO:0110001
Evidence at protein level
5
null
null
null
PF01934;
IPR008201;IPR037038;IPR052379;
7AE2;7AE6;7AE8;7AE9;
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Cyanobacteriota/Melainabacteria group (clade), Cyanobacteriota (phylum), Cyanophyceae (class), Nostocales (order), Aphanizomenonaceae (family), Aphanizomenon (genus), Aphanizomenon flos-aquae (species)
hepT hepn OA07_26455
false
73
A0A0B4J1F4
MGGEAGADGPRGRVKSLGLVFEDESKGCYSSGETVAGHVLLEAAEPVALRGLRLEAQGRATSAWGPSAGARVCIGGGSPAASSEVEYLNLRLSLLEAPAGEGVTLLQPGKHEFPFRFQLPSEPLATSFTGKYGSIQYCVRAVLERPQVPDQSVRRELQVVSHVDVNTPPLLTPMLKTQEKMVGCWLFTSGPVSLSVKIERKGYCNGEAIPIYAEIENCSSRLVVPKAAIFQTQTYLASGKTKTVRHMVANVRGNHIGSGSTDTWNGKMLKIPPVTPSILDCCIIRVDYSLAVYIHIPGAKRLMLELPLVIGTIPYSGFGRRNSSVASQFSMDMCWLALALPEQPEAPPNYADVVSEEEFSRHVPPYPQPSDCDGEACYSMFACIQEFRFQPPPLYSEVDPHPGDAQETQPVSFIL
Arrestin domain-containing protein 4
Mus musculus (Mouse)
10,090
415
44,970
Alternative splicing;Cell membrane;Cytoplasmic vesicle;Endosome;Membrane;Reference proteome;Repeat
GO:0005768; GO:0005769; GO:0005886; GO:0015031; GO:0016567; GO:0032728; GO:0070534; GO:0140112; GO:1903561; GO:1990756
Evidence at protein level
5
SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:19605364}. Cell membrane {ECO:0000269|PubMed:19605364, ECO:0000269|PubMed:27462458}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle {ECO:0000269|PubMed:19605364}. Note=Also found in extracellular vesicles different from exosomes. {ECO:0000269|PubMed:27462458}.
null
null
PF02752;PF00339;
IPR014752;IPR011021;IPR011022;IPR050357;IPR014756;
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)
Arrdc4
false
74
A0A0B4J1G0
MWQLLLPTALVLTAFSGIQAGLQKAVVNLDPKWVRVLEEDSVTLRCQGTFSPEDNSIKWFHNESLIPHQDANYVIQSARVKDSGMYRCQTALSTISDPVQLEVHMGWLLLQTTKWLFQEGDPIHLRCHSWQNRPVRKVTYLQNGKGKKYFHENSELLIPKATHNDSGSYFCRGLIGHNNKSSASFRISLGDPGSPSMFPPWHQITFCLLIGLLFAIDTVLYFSVRRGLQSPVADYEEPKIQWSKEPQDK
Low affinity immunoglobulin gamma Fc region receptor III-A (IgG Fc receptor III-A) (CD16-2) (FcgammaRIV) (CD antigen CD16a)
Mus musculus (Mouse)
10,090
249
28,398
Cell membrane;Disulfide bond;Glycoprotein;IgE-binding protein;IgG-binding protein;Immunity;Immunoglobulin domain;Membrane;Phosphoprotein;Receptor;Reference proteome;Repeat;Signal;Transmembrane;Transmembrane helix
GO:0002468; GO:0005886; GO:0009986; GO:0019767; GO:0019770; GO:0019863; GO:0019864; GO:0042119; GO:0043320; GO:0045780; GO:0140375; GO:0160006
Evidence at protein level
5
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16039578, ECO:0000269|PubMed:17558411, ECO:0000269|PubMed:28389502}; Single-pass type I membrane protein {ECO:0000255}.
SIGNAL 1..20; /evidence="ECO:0000255"
TRANSMEM 204..224; /note="Helical"; /evidence="ECO:0000255"
PF13895;PF13927;
IPR007110;IPR036179;IPR013783;IPR050488;IPR003599;IPR003598;
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)
Fcgr4 Fcgr3a
false
75
A0A0B4J1N3
MRLLALSGLLCMLLLCFCIFSSEGRRHPAKSLKLRRCCHLSPRSKLTTWKGNHTRPCRLCRNKLPVKSWVVPGALPQI
Protein GPR15LG (Protein GPR15 ligand) (Protein GPR15L)
Mus musculus (Mouse)
10,090
78
8,899
Antibiotic;Antimicrobial;Chemotaxis;Cytokine;Disulfide bond;Reference proteome;Secreted;Signal
GO:0001664; GO:0005615; GO:0007186; GO:0008009; GO:0010837; GO:0043029; GO:0043303; GO:0048018; GO:0048247; GO:0050830; GO:0050832; GO:0051782; GO:1902807; GO:2000404
Evidence at transcript level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q6UWK7}.
SIGNAL 1..24; /evidence="ECO:0000250|UniProtKB:Q6UWK7"
null
PF15854;
IPR031713;
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)
Gpr15lg Gpr15l
false
76
A0A0B4J2F0
MFRRLTFAQLLFATVLGIAGGVYIFQPVFEQYAKDQKELKEKMQLVQESEEKKS
Protein PIGBOS1 (PIGB opposite strand protein 1)
Homo sapiens (Human)
9,606
54
6,313
Direct protein sequencing;Membrane;Mitochondrion;Mitochondrion outer membrane;Proteomics identification;Reference proteome;Transmembrane;Transmembrane helix;Unfolded protein response
GO:0005739; GO:0005741; GO:0006986; GO:1900101
Evidence at protein level
5
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:31653868}; Single-pass membrane protein {ECO:0000255}.
null
TRANSMEM 5..25; /note="Helical"; /evidence="ECO:0000255"
PF23670;
null
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), Catarrhini (parvorder), Hominoidea (superfamily), Hominidae (family), Homininae (subfamily), Homo (genus)
PIGBOS1
false
77
A0A0B4K692
MQTVIQNPNWWRRRNKLEKSLLVSLGIMFVVLATGFGLWIGKVLRTSPPSNPQATALHGDSTTINQVPTGTASKGKSGDSGDVCLTQECIHTASTVLRKMKPEVEPCDNFYEFACGTYLEEENIPDDKVSISTFSVISDKLQEQLKDIITAERPETEPKHFRLPNLLYKACMNKTLIETLGPEPITRVAERLGGWPLIKGDSWNADDSWTWQEQVKKFRTAGFSMDYIIDFSIGVDLQNSTKRLIDLDQSSLALSREYLVKGFNETLVTAYYKYMVDIAVLFGANRDLAKTELLLSLEFEMALANISWPNEKRRNSSELYNLRTPAQLQAAYPYVQWVDYMNALLPEGLNVAEDEMINLSVPSFFEDLGKLLAKTPKRVIANYMFWRIHGFSVGFLSEEFRKRQLQYATALSGRQEQEARWKECVDIATSSMDEVCEDDFDSLGISVGSLYVGKHFHKDSKANALEMVNEIRNVFNDILDEVNWMDAKTKKEAKLKLHSMATHIGYPDEMLDNEKLAAYYAKLDIDPDKYFESFLGMNIFGTDYSFNKLRLPVNKTDWVRHARPAIVNAFYSSLENSIQFPAGILQGHFFNAQRPKYMNFGAIGYVIGHEITHGFDDQGRQFDVKGNLRDWWHPDTQKAYLAKAKCIIEQYGNYTERATGLNLNGINTQGENIADNGGVKESYIAYRRWAEKHGPEAKLPGLDYTPEQMFWVAAGQTWCAKYRKESLKMRITTGVHSPSEFRVLGSLSNMKDFAKDFHCPEGSPMNPVQKCEVW
Neprilysin-2 (EC 3.4.24.11) [Cleaved into: Neprilysin-2, soluble form]
Drosophila melanogaster (Fruit fly)
7,227
774
88,125
Alternative splicing;Cell membrane;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal-anchor;Transmembrane;Transmembrane helix;Zinc
GO:0004175; GO:0004222; GO:0005615; GO:0005886; GO:0006508; GO:0008237; GO:0016020; GO:0016485; GO:0046692; GO:0046872
Evidence at protein level
5
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:15554877, ECO:0000269|PubMed:17157960}. Note=A secreted form exists that is probably produced by proteolytic cleavage (Probable). In embryos, adult Malpighian tubules and testes, detected in the soluble fraction but is not detected in the membrane fraction (PubMed:15554877, PubMed:17157960). {ECO:0000269|PubMed:15554877, ECO:0000269|PubMed:17157960, ECO:0000305|PubMed:15554877, ECO:0000305|PubMed:17157960}.
null
TRANSMEM 21..41; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255"
PF01431;PF05649;
IPR024079;IPR000718;IPR018497;IPR042089;IPR008753;
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)
Nep2 CG9761
false
78
A0A0B4K7J2
MFTTRKEVDAHVHKMLGKLQPGRERDIKGLAVARLYMKVQEYPKAIEYLNGYLRVRDDAVGHNMIATCYSRLNPPDVTEALQHYQRSIQIDPRQSEVVIDACELLVKENNASITECARYWLDQANSLDLSGNKQVFNLRMRVNLADSNGERDDTSGGDGEQNTLEILMYKELQARPQDVNIRIQLLRSYVEKMKIDQAFNYALKTELESKNCTSQSNEWYEQIWMVLFKIEMAKDVKKNWRFWHFALHTLDRLVQLSLEGSGLADSSKQLFRLDQYLFKFSTSIERSGDAPQRDLHQACIDHFTGQLLLHAVTLIFKREVLANKNKWMSTLRSALPLLLLGYQVRPIDDSSTNQWIKHCDAEQKQLIQMWRPQGAFRCAQLGRTLLGCLDRSQMEIKNDRENAEFDENKNSGNSMPGLFADSEELLASAHQQCLDKSWRSQIYQQLFTHAEHKLKDTSSHLVRNLRLQLPLFEWPNLAHIENYELQALVLPPHSLAQHVYLALGTDPNKLGDAPRVVFYEGFQRDVKQNLNYCGQDSISQVDVDLYLYATTIQTRRKLQIQREVYDSSNLGNRNAAARPHMMPFANLVGQLGAPEQSNWWDLVVRLNSNQLITEGNRAEQRAQLQHGLEAVRGVNGPKADAIIIFQLGKILNSRSDRSSLEARIDTLYRQGFSILRHQHNQQMESYVRVFKYGSAGSTAAWQDLQSLAEEAVTYFSEKMFRIGQYEQFLDEVRGLHLPMAYFLQSEACHHLEESSKLPRTSRDRYSERRRECLQKTQKLIKNDDKHPLIAAMHRHQQDRNSRGIDNSFGSPDVHNNSSAYEDAEDDFYSHAAFSANRSRRQLEVTPVTPIVMAQPSQEMEQAVKQISKSLCVLKDDVSVGMEAMRQDIKVLTEKFTGLEDLLKKIKISSRDTPTRDVDPAAALGLDDLFIIEDALAEHQQQQQHQQQQSHNQGAIHPVVPNPYTSGFYNGMPNTPSAQERFLQGPYGSPMFNQNQMYNYYAAQAQAQAQAQFLRTPPAPGSIPPPNMFGPRNPNFGLPSMFPPPTVPSVAPYIDAMGNFTQPPPSLIPPPAQPAAPPAPLNILESKPVVALPTPGFFNTTTPVFGASPIQVPQSKPLTVPTVPIPSTAPAPPIAGTVNPPATTAVPPPVHIPQVAPSVPAQPPAPAPVSVPSMFNRALNNQPVEKEPPANVVITSSDPLPKPTTASVQPTLSVTIPAQHIKPSLVQAPEQPAQSAQPAQPSVSGVGSLSFNFGSKSSESPFSFKTQVAKAAAEKQKEQEEAEQNQSGATDPNKTLPQDTSADDYDPRPDFKPIIPLPDEVEVRTGEEGEDIKFTSRAKLFRYVDKEWKERGTGVIKILCDKATGVSRVLMRRDQTHKVCANHTITADITINVANQDKDKKSLLWAANDFADEQVTLERFLVRFKTGELAEEFRVAFTKASEAAKSKETVKPTVNTAEKGSTATAPAAFKSFVTSTPAANSLINKPQEQTKTQPNPDPPATAAKSLFGTLSVSAAPATSAPASATPFASFSFTPNGSSGFGTSTASPFGNLSFGTASAVGSGNNTTLFTTALIKDNTVQGKTLQQESQLNKSNSSDAEEEYVPTAQFVPVIALPDIVEVVTGEENEDVLFEHRAKLLRWDKEANEWKERGLGNMKLLRDRTDPNKVRLLMRREQVHKLCCNQRLLPETKFTYATNCKAAVTWGAQDYSDEELTTALLAVRFKSQDICQQFLEAVQKAQQSIGNEPKKEEVPSAAGEKEKPIKGFGDAFKPKAGSWNCQACYTNNGQDQLYCLACQEPKDATVPPKQSGLDQGNALNLTTSSSNKFSFGFASSATLPATGGFSFGGATQPKEKPAVAVVTASASAPTSVQTAALGFGKSSMTSGFGDAFKPAVGSWSCSACYVNNPGESLYCSACDAPKNDTVPQKEKSLGSGLNLPPTSKFSFGFGAAAAGDKDQAGDGATFNFAAMPAAVAPTTSIGSSSFTFSMTKPKPDQQQPNSTAAKEDEDNDSQEVEEEENNTYFSPVIPLPDKIDVKTGEEDEELLYVHKAKLYRLNESDWKERGLGDVKILRHRQTKKLRVVMRREQVFKICLNHVLNENVVYREKTETSWMFAVHDFSEGESVLERFTLRFKNKEVAQGFMEAIKNALNETAKPIEDSPVVGSVSQSTEANKPSQKNDGAAKSRGGESEVLDVGKTSSVRPTTHEVIPPLPMTLPLLTLPQPLAKPNDYQTPATILFKGSSLSRNNSSASEASKTPSSAFIFGSTDKSEPGKDAGPLANLQKLASGEGQGNVLGSIFRSGSSNENSSDGSVKFFFGGGNKAAEQQKKDSSESVFGGNKADSQSPATQEAPKLAFGGIAAPVFGDANPFGGHKVNLQKSDGKEEPKSIIGGTPLLFGGSNAFGIPKIETQSPAKDFVFGSAPAFGQMATFSFTAAKNEKEKDITSNNTTDLKAEGKEKKELVPETTSTFADLAKTGSTFADLASNPGGTFADLANKTGNDFANLSANSQGTTVGFNKSAGGGFYNLTHQNAFKNFESPQATEECDDDGDATTDDNYDPHYDAIVELPDEIVVTTGEENETKLFGERAKLYRYDAESKQWKERGVGEIKVLEHPELQTFRLIMRQEQIHKLVLNMNISASLQMDYMNAQMKSFLWAGYNYAVDAEGKVDTEGVLERLACRFAKEEIASEFLNTVNSCIKRAKALQGDEENKNDDAPEEQASS
E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358)
Drosophila melanogaster (Fruit fly)
7,227
2,718
298,931
Alternative splicing;Isopeptide bond;Metal-binding;mRNA transport;Nuclear pore complex;Nucleus;Phosphoprotein;Protein transport;Reference proteome;Repeat;TPR repeat;Transferase;Translocation;Transport;Ubl conjugation pathway;Zinc;Zinc-finger
GO:0005642; GO:0005643; GO:0005737; GO:0006606; GO:0006607; GO:0007281; GO:0007419; GO:0008270; GO:0008284; GO:0010628; GO:0019789; GO:0032880; GO:0035626; GO:0046833; GO:0051028; GO:0051292; GO:1900182
Evidence at protein level
5
SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P49792}. Note=Localizes to annulate lamellae, stacked membrane sheets of the endoplasmic reticulum. Localizes to granules which travel from nurse cells into the ooplasm through ring canals connecting the cytoplasm of the two cell types. {ECO:0000269|PubMed:31626769}.
null
null
PF00638;PF00641;
IPR011993;IPR000156;IPR045255;IPR011990;IPR001876;IPR036443;
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)
Nup358 RanBP2 CG11856
false
79
A0A0B4KEE4
MSENTYQIETRRRSRSKTPFLRSSCDHENCEHAGEEGHVHHLKRKSAAPNVQTIIEEHIVESSISKKTRAKAFAQLTSDYSSDDMTPDAKRKQNSITATVTSILTKRSGGATSTPRNRSQLETTQNTLNSAQEKLNQSNGNLSSGNVSDYLAYIEYRDAGEYWNKTPKTDYTYSELSPHRRQLAPGIVAMPNMSRKSLENHNDRVNYMVQQNPAQEEFIRRRYQSKYTQQVNYDSADELDATFGQQKQSWWLIRLIQLVVSSITTVWSRVTNLSATETTAYQNYHAKRQQSQQVGLWWKIVQTIGGGLASLLRYLYVFIGSVLSLDTWLLRSSDAENKSKKRFLIFLLILLPLLLLSGWLLLQEDQRSAYVQRAEALLPLPLSIFGSLRSRFSNAGATLKSWMEVPTVRSPQREAEAIKVNMASIEQNIQKALTAEEYENILNHVNSYVQQLVELKMQQHSKELAPQQIELFVKLMKENLKQIMYKTELSEKDLSDLAIKLKLELQSSGGWQDGAKLSQANLEEITKLIKAEVHLHESHYTIQLDRIDFASLLERILAAPALADFVDARISLRVGELEPKESSGSSDAEVQIERLNREIAFIKLALSDKQAENADLHQSISNLKLGQEDLLERIQQHELSQDRRFHGLLAEIENKLSALNDSQFALLNKQIKLSLVEILGFKQSTAGGSAGQLDDFDLQTWVRSMFVAKDYLEQQLLELNKRTNNNIRDEIERSSILLMSDISQRLKREILLVVEAKHNESTKALKGHIREEEVRQIVKTVLAIYDADKTGLVDFALESAGGQILSTRCTESYQTKSAQISVFGIPLWYPTNTPRVAISPNVQPGECWAFQGFPGFLVLKLNSLVYVTGFTLEHIPKSLSPTGRIESAPRNFTVWGLEQEKDQEPVLFGDYQFEDNGASLQYFAVQNLDIKRPYEIVELRIETNHGHPTYTCLYRFRVHGKPPAT
Klaroid protein
Drosophila melanogaster (Fruit fly)
7,227
965
109,725
Coiled coil;Cytoplasm;Cytoskeleton;Membrane;Reference proteome;Transmembrane;Transmembrane helix
GO:0000724; GO:0005635; GO:0005815; GO:0007097; GO:0034399; GO:0034993; GO:0043495; GO:0048471; GO:0051647
Evidence at transcript level
5
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:32066907}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18820457, ECO:0000269|PubMed:32066907}. Note=Lam is required for perinuclear localization of Koi (PubMed:18820457). In the fat body, localizes to a perinuclear non-centrosomal microtubule-organizing centers (ncMTOCs) (PubMed:32066907). {ECO:0000269|PubMed:18820457, ECO:0000269|PubMed:32066907}.
null
TRANSMEM 303..323; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 343..363; /note="Helical"; /evidence="ECO:0000255"
PF07738;
IPR045119;IPR012919;
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)
koi CG44154
false
80
A0A0B4KGY6
MESIMKVAMDKAAEQLIQQFGFDYLQQQLQLQHQNQHNSSPQQPQHQQLEPENEHLTYQYQQSKPTHMQQLACNYQPRHSTTTSSPSSTHSLASGGGSSSNSSNSSSSDSSSINISHISNISNISNIGNISNSNHSNAAYSLAVHSYQKQIESPANPSHVPHHQMDLSPLSENGSPNGTPGAQTPTATASGNTAAALASAAAAAAAATSGGNGSSITNCNSNNSSSSSNAQQQLQLGNYKTNSCWCYGESVCSGIEVEIENNNNNHIHHGETTYHMKILVPAVASGAIIGKGGETIASLQKDTGARVKMSKSHDFYPGTTERVCLITGSTEAIMVVMEFIMDKIREKPDLTNKIVDTDSKQTQERDKQVKILVPNSTAGMIIGKGGAFIKQIKEESGSYVQISQKPTDVSLQERCITIIGDKENNKNACKMILSKIVEDPQSGTCLNVSYADVSGPVANFNPTGSPYATNQNAINSSTASLNSTLGTTIGGANSAASLLVNGTGINLSINLGSPNPAPNLAVATQLLEHIKVAMRGSGYSETVTNEVVAALSVLAKYGVLGMGVGVSHTNGAHSTLGNFLGVTTLDQQTAAAASAATASNVFGAVGQVNLEQYAAAVASAAAASRPTQSQLDAAAVQFDPFRHLGSATAPAATPVSLNNNSFGLTATTGTATTAQLGGLSKSPTPGDLSSKDSKNVEVPEVIIGAILGPSGRSLVEIQHVSGANVQISKKGIFAPGTRNRIVTITGQPSAIAKAQYLIEQKINEEETKRARQIPLTTVVN
RNA-binding protein Pasilla
Drosophila melanogaster (Fruit fly)
7,227
780
81,403
Alternative splicing;Cytoplasm;mRNA processing;mRNA splicing;Nucleus;Reference proteome;Repeat;RNA-binding
GO:0000381; GO:0000398; GO:0003729; GO:0005634; GO:0005737; GO:0005829; GO:0033120; GO:0097157
Evidence at protein level
5
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11784037, ECO:0000269|PubMed:28525754}. Cytoplasm {ECO:0000269|PubMed:28525754}. Note=Localizes to synaptoneuropil region of neurons. {ECO:0000269|PubMed:28525754}.
null
null
PF00013;
IPR047275;IPR047276;IPR047274;IPR004087;IPR004088;IPR036612;
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)
ps l(3)10615 NOVA1 CG42670
false
81
A0A0B4LFY9
MAIASNVVEAGNAVRAEKGRKYFYFRKMIGDYIDTSIRIVATVFLADLLLRLYRCVVEYGSNGRYYLPEDRLWIILRRSCTYNNRSIYLIVGFLLVAFFRISVTGNYRNVMPTTLFLFQMPLYWIWSFTDMDQSTLSYSHWIRDSHGLDYAAGMASNYFHGYLKLSLPERKDDGLKHRLAMYEDKNNVTFGIKRLVILIPDEMFVNGVLESHLLDKAEPLETQFINRAGVYRPFKHDVYRMNKKVNGRTYYFAVEGATPMISFFDATYSNLSGTWQMQELKREIWIKFYKHLKELITTWPETRDLVELIIYNSHDSKGNLVDVGELLVAHMQNKTKTIDEISN
Stimulator of interferon genes protein homolog (dSTING) (dmSTING)
Drosophila melanogaster (Fruit fly)
7,227
343
40,183
Antiviral defense;Endoplasmic reticulum;Glycoprotein;Immunity;Innate immunity;Membrane;Nucleotide-binding;Reference proteome;Transmembrane;Transmembrane helix
GO:0000045; GO:0002807; GO:0005776; GO:0005789; GO:0016239; GO:0032481; GO:0035438; GO:0042742; GO:0045087; GO:0051607; GO:0061507; GO:0061709; GO:0098586; GO:0140367; GO:0140374; GO:0140460; GO:0140704; GO:0140896
Evidence at protein level
5
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30119996}; Multi-pass membrane protein {ECO:0000255}.
null
TRANSMEM 87..107; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 109..129; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 195..215; /note="Helical"; /evidence="ECO:0000255"
PF15009;PF23417;
IPR029158;IPR033952;IPR038623;IPR055432;IPR055434;
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)
Sting CG1667
false
82
A0A0B5A051
MELSSVSSFSLGTNPFISIPHNNNNNLKVSSYCCKSKSRVINSTNSKHCSPNNNNNNNTSNKTTHLLGLYGQSRCLLKPLSIFSCKDQRGNSIRASAQIEDRPPESGNLSALTNVKDFVSVCWEYVRPYTAKGVIICSSCLFGRELLENPNLFSWPLIFRALLGMLAILGSCFYTAGINQIFDMDIDRINKPDLPLVSGRISVESAWLLTLSPAIIGFILILKLNSGPLLTSLYCLAILSGTIYSVPPFRWKKNPITAFLCILMIHAGLNFSVYYASRAALGLAFVWSPSFSFITAFITFMTLTLASSKDLSDINGDRKFGVETFATKLGAKNITLLGTGLLLLNYVAAISTAIIWPKAFKSNIMLLSHAILAFSLFFQARELDRTNYTPEACKSFYEFIWILFSAEYVVYLFI
2-acylphloroglucinol 4-prenyltransferase (EC 2.5.1.136) (Aromatic prenyltransferase PT1L) (Humulus lupulus prenyltransferase-1-like) (HlPT1L)
Humulus lupulus (European hop)
3,486
414
45,929
Chloroplast;Membrane;Plastid;Transferase;Transit peptide;Transmembrane;Transmembrane helix
GO:0004659; GO:0031969
Evidence at protein level
5
SUBCELLULAR LOCATION: Plastid {ECO:0000269|PubMed:25564559}. Plastid, chloroplast membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
null
TRANSMEM 153..173; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 201..221; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 229..249; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 256..276; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 281..301; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 336..356; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 359..379; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 394..414; /note="Helical"; /evidence="ECO:0000255"
PF01040;
IPR044502;IPR000537;IPR044878;
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), Humulus (genus)
PT1L
false
83
A0A0B5A886
MMKVIWFSSLICLVIQCSGDSGPIICAGPIHSNKSAGIPHLLGYSEKICQIDRLIHVSSWLRNHSQFQGYVGQRGGRSQVSYYPAENSYSRWSGLLSPCDADWLGMLVVKKAKESDMIVPGPSYKGKVFFERPTFDGYVGWGCGSGKSRTESGELCSSDSGTSSGLLPSDRVLWIGDVACQPMTPIPEETFLELKSFSQSEFPDICKIDGIVFNQCEGESLPQPFDVAWMDVGHSHKIIMREHKTKWVQESSSKDFVCYKEGTGPCSESEEKACKTSGSCRGDMQFCKVAGCEHGEEASEAKCRCSLVHKPGEVVVSYGGMRVRPKCYGFSRMMATLEVNPPEQRIGQCTGCHLECINGGVRLITLTSELRSATVCASHFCSSASSGKKSTEIHFHSGSLVGKTAIHVKGALVDGTEFTFEGSCMFPDGCDAVDCTFCREFLKNPQCYPAKKWLFIIIVILLGYAGLMLLTNVLKAIGVWGSWVIAPVKLMFAIIKKLMRTVSCLVGKLMDRGRQVIHEEIGENGEGNQDDVRIEMARPRRVRHWMYSPVILTILAIGLAEGCDEMVHADSKLVSCRQGSGNMKECITTGRALLPAVNPGQEACLHFTAPGSPDSKCLKIKVKRINLKCKKSSSYFVPDARSRCTSVRRCRWAGDCQSGCPPHFTSNSFSDDWAGKMDRAGLGFSGCSDGCGGAACGCFNAAPSCIFWRKWVENPHGIIWKVSPCAAWVPSAVIELTMPSGEVRTFHPMSGIPTQVFKGVSVTYLGSDMEVSGLTDLCEIEELKSKKLALAPCNQAGMGVVGKVGEIQCSSEESARTIKKDGCIWNADLVGIELRVDDAVCYSKITSVEAVANYSAIPTTIGGLRFERSHDSQGKISGSPLDITAIRGSFSVNYRGLRLSLSEITATCTGEVTNVSGCYSCMTGAKVSIKLHSSKNSTAHVRCKGDETAFSVLEGVHSYIVSLSFDHAVVDEQCQLNCGGHESQVTLKGNLIFLDVPKFVDGSYMQTYHSTVPTGANIPSPTDWLNALFGNGLSRWILGVIGVLLGGLALFFLIMFLLKLGTKQVFRSRTKLA
Envelopment polyprotein (M polyprotein) [Cleaved into: Glycoprotein N (Gn) (Glycoprotein G1); Glycoprotein C (Gc) (Glycoprotein G2)]
SFTS phlebovirus (isolate SFTSV/Human/China/HB29/2010) (Severe fever with thrombocytopenia virus)
992,212
1,073
116,636
3D-structure;Disulfide bond;Fusion of virus membrane with host endosomal membrane;Fusion of virus membrane with host membrane;Glycoprotein;Host endoplasmic reticulum;Host Golgi apparatus;Host membrane;Host-virus interaction;Lipoprotein;Membrane;Palmitate;Reference proteome;Signal;Transmembrane;Transmembrane helix;Viral attachment to host cell;Viral attachment to host entry receptor;Viral penetration into host cytoplasm;Virion;Virus entry into host cell
GO:0016020; GO:0039654; GO:0044167; GO:0044178; GO:0046718; GO:0055036; GO:0098670
Evidence at protein level
5
SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host Golgi apparatus membrane {ECO:0000269|PubMed:27855227, ECO:0000269|PubMed:29467349}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:27855227, ECO:0000269|PubMed:29467349}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Note=Interaction between Glycoprotein N and Glycoprotein C is essential for proper targeting of Glycoprotein C to the Golgi complex, where virion budding occurs. {ECO:0000269|PubMed:27855227}.; SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host Golgi apparatus membrane {ECO:0000269|PubMed:27855227, ECO:0000269|PubMed:29467349}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:27855227, ECO:0000269|PubMed:29467349}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Note=Interaction between Glycoprotein N and Glycoprotein C is essential for proper targeting of Glycoprotein C to the Golgi complex, where virion budding occurs. {ECO:0000269|PubMed:27855227}.
SIGNAL 1..19; /evidence="ECO:0000255"
TRANSMEM 454..474; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1037..1057; /note="Helical"; /evidence="ECO:0000255"
PF19019;PF07243;PF07245;
IPR043603;IPR010826;IPR009878;
8WSU;
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Negarnaviricota (phylum), Polyploviricotina (subphylum), Ellioviricetes (class), Bunyavirales (order), Phenuiviridae (family), Bandavirus (genus), Bandavirus dabieense (species)
GP
false
84
A0A0B5AC19
MSLSKCSNVDLKSVAMNANTVRLEPSLGEYPTLRRDLVECSCSVLTLSMVKRMGKMTNTVWLFGNPKNPLHQLEPGLEQLLDMYYKDMRCYSQRELSALRWPSGKPSVWFLQAAHMFFSIKNSWAMETGRENWRGLFHRITKGQKYLFEGDMILDSLEAIEKRRLRLGLPEILITGLSPILDVALLQIESLARLRGMSLNHHLFTSPSLRKPLLDCWDFFIPVRKKKTDGSYSVLDEDDEPGVLHGYPHLMAHYLNRCPFHNLIRFDEELRTAALNTIWGRDWPAIGDLPKEV
Non-structural protein NS-S (NSs)
SFTS phlebovirus (isolate SFTSV/Human/China/HB29/2010) (Severe fever with thrombocytopenia virus)
992,212
293
33,793
Host cytoplasm;Host cytoplasmic vesicle;Host G2/M cell cycle arrest by virus;Host-virus interaction;Inhibition of host innate immune response by virus;Inhibition of host interferon signaling pathway by virus;Inhibition of host RIG-I by virus;Inhibition of host RLR pathway by virus;Inhibition of host STAT2 by virus;Inhibition of host TBK1 by virus;Inhibition of host TLR pathway by virus;Interferon antiviral system evasion;Modulation of host cell cycle by virus;Reference proteome;Viral immunoevasion
GO:0039502; GO:0039540; GO:0039564; GO:0039592; GO:0039722; GO:0039723; GO:0044161
Evidence at protein level
5
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:24478431}. Host cytoplasmic vesicle {ECO:0000269|PubMed:24335286, ECO:0000269|PubMed:28680969, ECO:0000269|PubMed:30598516}. Note=Localizes to the viral cytoplasmic occlusion bodies. {ECO:0000269|PubMed:24335286, ECO:0000269|PubMed:27226560, ECO:0000269|PubMed:28680969, ECO:0000269|PubMed:30598516}.
null
null
null
null
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Negarnaviricota (phylum), Polyploviricotina (subphylum), Ellioviricetes (class), Bunyavirales (order), Phenuiviridae (family), Bandavirus (genus), Bandavirus dabieense (species)
NSS
false
85
A0A0B5JC15
MVAFSSLFLGASIAATALAAPGELPGMHLNKRQTYTQSATGTHDGYYFSFWTDGGPNVRYTNEAGGQYSVTWSGNGNWVGGKGWNPGAARTINYTGTYQPNGNSYLAVYGWTRNPLVEYYVVENFGTYDPSTGAQRLGSINVDGSTYNVYRTRRTNAPSIEGTRSFDQYWSVRVNKRVGGSVDMNAHFNAWRQAGLTLGTHDYQIVATEGYFSSGSARINVGGGSTGGGNNGGGNNGGNPGGNPGGNPGGNPGGNCSPRWGQCGGQGWNGPTCCESGTTCRQQNQWYSQCL
Endo-1,4-beta-xylanase 11B (Xylanase 11B) (EC 3.2.1.8) (1,4-beta-D-xylan xylanohydrolase 11B)
Humicola insolens (Soft-rot fungus)
85,995
291
30,839
Carbohydrate metabolism;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal;Xylan degradation
GO:0005576; GO:0030248; GO:0031176; GO:0045493
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:25629035}.
SIGNAL 1..19; /evidence="ECO:0000255"
null
PF00734;PF00457;
IPR035971;IPR000254;IPR013320;IPR013319;IPR018208;IPR033119;IPR033123;IPR001137;
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), Sordariomycetidae (subclass), Sordariales (order), Chaetomiaceae (family), Mycothermus (genus)
Xyn11B Xyl2
false
86
A0A0B5KYT4
MESLSLTWITAIAVVLYLVQRYVRSYWRLKDIPGPVLAKLTDLQRVWWVKTGRAHEFHRDMHAMYGPIVRFGPNMVSVSDPRVIPTIYPSRPGFPKGDFYRTQKPYTRNKGAMPAVFNTQDEDLHKQLRSPIASLYSMTNVVRLEPLVDETLTVLSKQLDERFVGTNDKPFDLGDWLQYFAFDSMGTLTFSRRYGFLEQGRDMHGILQEIWNFMTRVAVMGQIPWFDEIWNKNSFITLFKRPTGFGVLKVVDNFISQRVSSRENDEKADEKDMLSQFLNIQASNPHSIMPWAPRAWTFSNVMAGSDSTANVMRTMMYNLLVDRDTLKSLRAELLEAESSNGLSRSLPSWDGVRSLPYLDACVLEALRLHPPFCLPFERVVPEGGITVCETYLPAGTVVGISPYLANRDKQTFGDDADKWRPSRWLDLSREDRVKLENSILTFGAGRRTCLGKNIAILEIKKLFPMLLLNYEIEIVNPENYQTTNAWFFRQWGLHAVIRKLPAPERDDTIEQKASIPPALNIPPSSSTVDVRIIDSGTLLDLRPDLFWTPDLPGLLKVTAPTYCFLISNGSRHVLFDLAVRQDWENLPPSIVAMIKSQTVIQEPRNISDVLDSDESSLGIRSKDIEAIIWSHAHFDHIGDPSTFPPSTELVVGPGIRDTHWPGFPTNPDAINLNTDIQGRNVREISFEKTQKGATKIGSFDAMDYFGDGSFYLLDAAGHSVGHIGALARVTTSPDSFVFMGGDSCHHAGVLRPTKYLPCPLDSGDTSLPCKSDSVFTLSPALPTDYTAALRTVENIKELDACEDVFVVLAHDATLKGKVDFYPSKINDWKAKEYGKKTKWLFYKDIENAIEGQK
Cytochrome P450 monooxygenase mpaDE' (EC 1.-.-.-) (Mycophenolic acid biosynthesis cluster protein DE')
Penicillium brevicompactum
5,074
853
96,352
Endoplasmic reticulum;Heme;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Transmembrane;Transmembrane helix
GO:0004497; GO:0005506; GO:0005783; GO:0005789; GO:0016114; GO:0016218; GO:0016705; GO:0020037; GO:0140722
Evidence at protein level
5
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:31209052}; Single-pass membrane protein {ECO:0000255}.
null
TRANSMEM 7..29; /note="Helical"; /evidence="ECO:0000255"
PF00753;PF00067;
IPR001128;IPR017972;IPR002403;IPR036396;IPR050121;IPR001279;IPR036866;
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)
mpaDE'
false
87
A0A0B5L781
MSAASPASIIQELASAAKQYENNESGAREALIAQSRALIASLEVPSEFIQHTFWSQPALSAIVRLATDVNLFQYLKDAQEEGLNAEALASKTGMDVSLFARLARHLVAMNVITSRNGVFYGTALSNGLAAENYQQSIRFCHDVSRPSFGAFPSFFKGNGYKTPALGTTDGPFQSAHKVDISFPQWLVGNPPYLQYFNSYMSAYRAGKPNWCDNGFYPVADRLLNGFDASVSDVLLVDVGGGRGHDIATFGSQFSPLPGRLVLQDREQVINSIPADESRQFEATTHDIFTTQPVKHARAYYMHSVPHGFGDEDAVKIMANLVPALAKGYSRVLLNEIVVDEERPVMSATNMDLIMLAHMGAKERTEADWRSILTRAGLKVVNIYSYPGVAESLIEAELA
O-methyltransferase mpaG' (EC 2.1.1.-) (Mycophenolic acid biosynthesis cluster protein G')
Penicillium brevicompactum
5,074
398
43,553
3D-structure;Cytoplasm;Methyltransferase;S-adenosyl-L-methionine;Transferase
GO:0005829; GO:0008168; GO:0008171; GO:0016114; GO:0016218; GO:0032259; GO:0140722
Evidence at protein level
5
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:31209052}.
null
null
PF00891;
IPR016461;IPR001077;IPR029063;IPR036388;IPR036390;
8XTE;8XTF;8XTG;
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)
mpaG'
false
88
A0A0B5LB55
MSTEKFTITEHLVPGSHIREYPGSTVNQEDVLKIHVKQYTPKREGPVPDDAITFIATHGVGLPKELYEPLWDELLDQASGFHIRAIWMADVASMNQSGIHNEDKLSMDCSWMDHARDLLLMINHFRDQMPRPLVGIGHSFGGNIITNLAYLHPRLFTTLLLLDPLIQLSPPSLGFGTDAPSAINYTLWRDDVWPSREVAIRANRAIMQGMDPRCLDRMTKHFFRDLPTPLYPDVEAIKALFGTTADSTTTPVTLTTPKYHELVAQIRQNFNARDPKTGRIEVPRDTHADMDPLVAYIPLYRPEPRSTFRRLETLRPSCLWVIAGATFLNIDEIREGVKICGSGIGGSGGVPDGRVREVVLPGFGHLMPFQEVKTVAETCIVWLQQEMDRFRQTERQWKEDRDGKSHLAVEENWYKVLKPIPSGRKKRNDKGKL
Type I acyl-CoA thioesterase mpaH' (EC 3.1.1.-) (Mycophenolic acid biosynthesis cluster protein H')
Penicillium brevicompactum
5,074
433
49,147
3D-structure;Hydrolase;Peroxisome
GO:0005782; GO:0016114; GO:0016218; GO:0016787; GO:0047617; GO:0140722
Evidence at protein level
5
SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:31209052}. Note=The mpaH' location in peroxisomes is required for the unique cooperation between biosynthetic and beta-oxidation catabolism machineries to produce final MPA. {ECO:0000269|PubMed:31209052}.
null
null
PF12697;
IPR000073;IPR029058;
7DBI;7DBL;
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)
mpaH'
false
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