manufernandezbur/uniprot2025_03 · Datasets at Fast360

100

A0A0C5QRZ2

MDPFPLVAAALFIAATWFITFKRRRNLPPGPFPYPIVGNMLQLGSQPHETFAKLSKKYGPLMSIHLGSLYTVIISSPEMAKEIMHKYGQVFSGRTIAQAVHACDHDKISMGFLPVGAEWRDMRKICKEQMFSHQSMEDSQNLRKQKLQQLLEYAQKCSEEGRGIDIREAAFITTLNLMSATLFSMQATEFDSKVTMEFKEIIEGVASIVGVPNFADYFPILRPFDPQGVKRRADVYFGRLLGLIEGYLNERIEFRKANPNAPKKDDFLETLVDALDAKDYKLKTEHLTHLMLDLFVGGSETSTTEIEWIMWELLASPEKMAKVKAELKSVMGGEKVVDESMMPRLPYLQAVVKESMRLHPPGPLLLPRKAESDQVVNGYLIPKGAQVLINAWAMGRDPSLWKNPDSFEPERFLDQKIDFKGTDYELIPFGSGRRVCPGMPLANRILHTVTATLVHNFDWKLERPEASDAHKGVLFGFAVRRAVPLKIVPIKA

Ferruginol synthase (SfFS) (EC 1.14.14.175) (11-oxomiltiradiene synthase) (EC 1.14.14.-) (Cytochrome P450 76AH24) (Ferruginol monooxygenase) (11-hydroxyferruginol synthase) (EC 1.14.14.60) (Miltiradiene oxidase)

Salvia fruticosa (Greek sage)

268,906

492

55,616

Heme;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Transmembrane;Transmembrane helix

GO:0005506; GO:0016020; GO:0016102; GO:0016712; GO:0020037

Evidence at protein level

5

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

null

TRANSMEM 1..21; /note="Helical"; /evidence="ECO:0000255"

PF00067;

IPR001128;IPR017972;IPR002401;IPR036396;

null

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

CYP76AH24 FS HFS

false

101

A0A0C5XL88

MTTSFWRIATDARTYEADDLSGAGAKITGGRWNEVGVAIVYAASSRALACLETVVHLNSGGLPLNRYLVEIEVPDEVLASAEVATPGNLPVGWDAEPAGRVSISFGSQWAQSQRTALLLVPSVIVPEETNLLINPAHPDAKGIKARKVRKWLYDPRMIRKA

Prs ADP-ribosylating toxin (EC 2.4.2.-) (Mono-ADP-ribosyltransferase) (mART)

Sphingobium sp. (strain YBL2)

484,429

161

17,408

3D-structure;ADP-ribosylation;Glycosyltransferase;NAD;Nucleotidyltransferase;Toxin-antitoxin system;Transferase

GO:0016757; GO:0016779

Evidence at protein level

5

null

PF08808;

IPR014914;

6D0H;6D0I;

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Alphaproteobacteria (class), Sphingomonadales (order), Sphingomonadaceae (family), Sphingobium (genus), unclassified Sphingobium (no rank)

parT yblI TZ53_17660

false

102

A0A0C6DRW4

MTLSPEKQHVRPRDAADNDPVAVARGLAEKWRATAVERDRAGGSATAEREDLRASGLLSLLVPREYGGWGADWPTAIEVVREIAAADGSLGHLFGYHLTNAPMIELIGSQEQEEHLYTQIAQNNWWTGNASSENNSHVLDWKVRATPTEDGGYVLNGTKHFCSGAKGSDLLFVFGVVQDDSPQQGAIIAAAIPTSRAGVTPNDDWAAIGMRQTDSGSTDFHNVKVEPDEVLGAPNAFVLAFIQSERGSLFAPIAQLIFANVYLGIAHGALDAAREYTRTQARPWTPAGIQQATEDPYTIRSYGEFTIALQGADAAAREAAHLLQTVWDKGDALTPEDRGELMVKVSGVKALATNAALNISSGVFEVIGARGTHPRYGFDRFWRNVRTHSLHDPVSYKIADVGKHTLNGQYPIPGFTS

Dibenzothiophene monooxygenase (DBT monooxygenase) (DBT-MO) (EC 1.14.14.21)

Rhodococcus erythropolis (Arthrobacter picolinophilus)

1,833

417

45,096

3D-structure;Cytoplasm;Direct protein sequencing;Flavoprotein;FMN;Monooxygenase;Nucleotide-binding;Oxidoreductase

GO:0004497; GO:0005737; GO:0006552; GO:0008470; GO:0018896; GO:0050660

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|Ref.2}.

null

PF08028;PF02770;PF02771;

IPR013107;IPR006091;IPR046373;IPR036250;IPR013786;IPR037069;IPR009100;IPR049992;

3X0X;3X0Y;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Actinomycetota (phylum), Actinomycetes (class), Mycobacteriales (order), Nocardiaceae (family), Rhodococcus (genus), Rhodococcus erythropolis group (no rank)

dszC

false

103

A0A0D1CKI0

MKYLQFLAAVAAVSAFSGPVLAGSSVENTNQVLPVQLTGALFSQVANGQHAERAIKVDNSAQFVPVQGTIAALSAVLNEQKAGKRSFSVENTNQVLPIDVIIAGLSQVLTEQKAAKRDNIVKNTNQILPIEATIAALSAIANGQKAATKRSTAVDNSSQFIPIQGTLAAFSNVLNSQKATKRNTGKVVDNTNQVVPIQGTLAALSTVLNEQKASKRGVDVDNSSQTLPIEATIAALSTIANGQQAGKRNAPDFDVVKNSNQVLPIQATAALLSQIANGQSVEKRNAPDFDVVKNSNQVLPIQATAALLSQIANGQSVEKRNAPDFDVVKNSNQVLPIQATAALLSQIANGQSVEKRNAPDFDVVKNSNQVLPIQATAALLSQIANGQSVEKRNAPDFDSVKNSNQVVPIQATAALLSAVKNLQSVERNAPDFDSVKNSNQVVPIQATAALLSQIANGQSVEKRNAPDFDSVKNSNQVVPIQGTAALLSVVGNGQSVSKRHEGENNIVDNTNQVIPIQATIAALSTLLNSQKAERSYSVDNTNQVLPIEATLAAFSSVLNSQKAERSYSVENDNEVVPVDLVAAALSQVANGQKVTRRGETKESIKHNVNQVAPAQASLSALSDIVNSAHSRRAMDVKQYETLQYAINALQQALDKTNTGDKTHHVDAMTGTAEHFDERDAGLDPAAFLGSAASGISVPVGNKDLLKSLVKRYAAEEDEAMAKRTPSLNGRGQRPRPRNSSSSEHNNNGQCSVGEAKCCSQVITDEGKKKTLAGLLGFNNLVGDIGLNCQQIPVLGVSLQSICKATPVCCTNVSQDGLVNVGCTSIPIN

Class I hydrophobin hum3 [Cleaved into: Repeat-1; Repeat-2; Repeat-3; Repeat-4; Repeat-5; Repeat-6; Repeat-7; Repeat-8; Repeat-9; Repeat-10; Repeat-11; Repeat-12; Repeat-13; Repeat-14; Repeat-15; Repeat-16; Repeat-17; Linker peptide; Hydrophobin 3]

Mycosarcoma maydis (Corn smut fungus) (Ustilago maydis)

5,270

828

87,229

Cell wall;Cell wall biogenesis/degradation;Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Reference proteome;Secreted;Signal

GO:0005199; GO:0009277

Evidence at protein level

5

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17917743}. Secreted, cell wall {ECO:0000269|PubMed:17917743}.

SIGNAL 1..22; /evidence="ECO:0000255"

null

PF01185;

IPR001338;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Basidiomycota (phylum), Ustilaginomycotina (subphylum), Ustilaginomycetes (class), Ustilaginales (order), Ustilaginaceae (family), Mycosarcoma (genus)

him3 UMAG_04433

false

104

A0A0D1DWQ2

MKLSVSIFVLLAVSAFGGGSAAAVSGKSEAAEIEAGDRLDALRDQLQRYETPIIQTILARSALGGRAPSEQDEVRAALSRNAFEPSEVISEWLQTESGARFRSTRPLPPAVEFITPVVLSRDTVLDKPVVGKGIFPIGRRPQDPTNMDEFLDTSLLSLNQSSTVDLASAVSLDVSLLHLVSARVLLGYPIALAKFDWLHDNFCHILTNTTLSKSQKLANIIQQLTDHKQEVNVLSRVEQKSKSLSHLFRNDIPYPPHTQDRILRLFQAYLIPITTQIEAAAILDHANKCT

Secreted chorismate mutase (EC 5.4.99.5)

Mycosarcoma maydis (Corn smut fungus) (Ustilago maydis)

5,270

290

31,859

3D-structure;Allosteric enzyme;Glycoprotein;Host cytoplasm;Isomerase;Reference proteome;Secreted;Signal;Virulence

GO:0004106; GO:0005576; GO:0009073; GO:0044164; GO:0046417; GO:0140502; GO:0140593

Evidence at protein level

5

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21976020}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:21976020}. Note=Is translocated to host plant cells and spreads to neighboring tissue. The spreading is likely to occur through plasmodesmata. {ECO:0000269|PubMed:21976020}.

SIGNAL 1..21; /evidence="ECO:0000269|PubMed:30651637"

null

IPR036263;IPR037039;

6FPF;6FPG;6TI2;

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Basidiomycota (phylum), Ustilaginomycotina (subphylum), Ustilaginomycetes (class), Ustilaginales (order), Ustilaginaceae (family), Mycosarcoma (genus)

CMU1 UMAG_05731

false

105

A0A0D1DWZ5

MSDSIYAPHNKHKLEAARAADAAADDAATVSALVEPTDSTAQASHAAEQTIDAHQQAGDVEPERCHPHLTRPLLYLSGVDATMTDKELAGLVFDQVLPVRLKIDRTVGEGQTASGTVEFQTLDKAEKAYATVRPPIQLRINQDASIREPHPSAKPRLVKQLPPTSDDAFVYDLFRPFGPLRRAQCLLTNPAGIHTGFKGMAVLEFYSEQDAQRAESEMHCSEVGGKSISVAIDTATRKVSAAAAEFRPSAAAFVPAGSMSPSAPSFDPYPAGSRSVSTGSAASIYATSGAAPTHDTRNGAQKGARVPLQYSSQASTYVDPCNLFIKNLDPNMESNDLFDTFKRFGHIVSARVMRDDNGKSREFGFVSFTTPDEAQQALQAMDNAKLGTKKIIVRLHEPKTMRQEKLAARYNAANADNSDMSSNSPPTEARKADKRQSRSYFKAGVPSDASGLVDEEQLRSLSTVVRNELLSGEFTRRIPKVSSVTEAQLDDVVGELLSLKLADAVEALNNPISLIQRISDAREQLAQKSASTLTAPSPAPLSAEHPAMLGIQAQRSVSSASSTGEGGASVKERERLLKAVISVTESGAPVEDITDMIASLPKKDRALALFNPEFLKQKVDEAKDILDITDESGEDLSPPRASSGSAPVPLSVQTPASAIFKDASNGQSSISPGAAEAYTLSTLAALPAAEIVRLANSQSSSGLPLPKADPATVKATDDFIDSLQGKAAHDQKQKLGDQLFKKIRTFGVKGAPKLTIHLLDSEDLRALAHLMNSYEDVLKEKVQHKVAAGLNK

RNA-binding protein RRM4

Mycosarcoma maydis (Corn smut fungus) (Ustilago maydis)

5,270

792

84,663

3D-structure;Cytoplasm;Cytoskeleton;Endosome;mRNA transport;Reference proteome;Repeat;RNA-binding;Transport

GO:0003730; GO:0005634; GO:0005768; GO:0005829; GO:0005856; GO:0008143; GO:0008266; GO:0010494; GO:0051028; GO:1990904

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17105762, ECO:0000269|PubMed:19494833, ECO:0000269|PubMed:25985087}. Endosome {ECO:0000269|PubMed:22357951, ECO:0000269|PubMed:24355572, ECO:0000269|PubMed:25985087}. Note=Assembles into particles that shuttle along microtubules to both poles (PubMed:17105762, PubMed:19494833). Shuttles with RAB5A-positive endosomes along microtubules (PubMed:22357951, PubMed:25985087). {ECO:0000269|PubMed:17105762, ECO:0000269|PubMed:19494833, ECO:0000269|PubMed:22357951, ECO:0000269|PubMed:25985087}.

null

PF00658;PF00076;

IPR012677;IPR036053;IPR002004;IPR035979;IPR000504;

7PZE;8S6N;8S6O;

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Basidiomycota (phylum), Ustilaginomycotina (subphylum), Ustilaginomycetes (class), Ustilaginales (order), Ustilaginaceae (family), Mycosarcoma (genus)

RRM4 UMAG_10836

false

106

A0A0D1E015

MTIPDPANIIHNDAGTASPHHIWADVGDSTSSSQHEATRSRSDDANGGASASMHAPQHVKANRAAQPTYDSSDLPSFGLSARLTRDSSSFGSKPSSSASDSRRPKFAPYEAENLWATSSTTSHPSKASQSTLSPNASVFKPSRSLQPNHFEPHAVANVHDFDDPLNSAYSSDTVSPRPDHAPLDHEQPQQPSALDPVAVSKVEEQRGDHSIPHQNGLVSAQAQTASDAVSTSKYTTEAADQEEDQDDFVYPGADSPSSGQAAVQDEQQAVTDSQTTKSLTKQESDPEASSTSLSAPAEAEHIVVGSAAEQSLTSSAPAETAVHIDYDTLAQLCSRGPLSDLQSFFHTAQESGLSMFSLSNDPNPGNGLVPLHFAAKDGKTDIVRWLITQAGAIVEMEDREGETALHKAAMAGKLSVASLLLSHGADANAQDADGWTALHNACSRGYLDLVRLLVDRGHAQIDVQGGRGAWTPLMNAASKGHLPVVRHLTAKYHADPFVRNAAGETAFDVAAATFEVYICEILERYEAERWNASKFTTSSPSRSGAIVPGRGPYEPLALHTTIPVILHENQRLDTRLQTLALNGGKPRWSSSSAARAHKPDRRSPSSMPPGPLAPSRTRHVPMRQDDVGLPTRSLPYKLRLRSRVGPAAARRRAAALAAQHTPNPQDCHDDDLASTPTPESVLQARRGTSSVNGASAQHADAESSHFWLCEWQLDTTHPLVDVEHGWQYAQSFDALDDKWSSQPPPPLERLLEGRGLSASVTRAITGGAGFANAQAEQEISSSSWVRRRRWIRVLRRRLDIEFGDDLEACEGATGAGAEHLVLSSESQSNGDGSHGLSTAAIMAAQEAAKSECSQLGPDADYVSRAKALAGPSAASGATPADAMGADRDELARRIARLVMANTELRAAFEDDDVERRSRAEELRKEYALQLGQLREAAGLDEDEDEDAADDDDDEFIYPNSYKDDGASVFTRLVNGETSGTLSRPSLSQRQSSAASMLRNSVAPSEAGTSLAAARSADLAANREFRVPTNEAPNKVVLRHGPTMREQNLQPQWQRDEEAKDCIGCGRHFTFFLRKHHCRRCGRIFCDACSSKRAQLRMAELVVDPSLPSMAASEVLAPTRVCNGCHAELQLPPQLQNMRGADAMMAASRSRGADEVSGRSILETQLEDGAFRSTLAPPSDVSSRASELTECPVCSTTLSALGGSEEQEAHVRNCLENGGGGSMQGGRYLVYKLPEDSPIVGKECSICMEDFVANSTIARLPCLCYFHRGCIDSWFKRGRECPVHARDW

FYVE zinc finger domain protein UPA1 (PAM2 domain-containing protein UPA1)

Mycosarcoma maydis (Corn smut fungus) (Ustilago maydis)

5,270

1,287

138,533

3D-structure;ANK repeat;Cytoplasm;Cytoskeleton;Endosome;Metal-binding;mRNA transport;Reference proteome;Repeat;Transferase;Transport;Ubl conjugation pathway;Zinc;Zinc-finger

GO:0005768; GO:0005856; GO:0008270; GO:0016740; GO:0051028

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:25985087}. Endosome {ECO:0000269|PubMed:25985087}. Note=Shuttles with endosomes along microtubules (PubMed:25985087). the FYVE domain mediates endosomal localization and endosomal targeting is crucial for its function during polar growth and CTS1 secretion (PubMed:25985087). {ECO:0000269|PubMed:25985087}.

null

PF12796;PF13857;PF01363;PF13639;

IPR002110;IPR036770;IPR000306;IPR017455;IPR011011;IPR001841;IPR013083;

8S6U;

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Basidiomycota (phylum), Ustilaginomycotina (subphylum), Ustilaginomycetes (class), Ustilaginales (order), Ustilaginaceae (family), Mycosarcoma (genus)

UPA1 UMAG_12183

false

107

A0A0D2UG83

MAKSKKIVAATSGSRSRSSRAGLAFPVGRVHRLLRKGHFADRIGSGSAVYLAAVLEYLTAEILELAGNAARDNRKTRINPRHIQLAVRNDEELSKLFTGVVIPSGGTLPHIWPALIPNEAKDSSTASASFNAPAKSATVKALAAAKSAGKKPAAVSSSSAAASSSSSASSSSSVAPKKPVRGFTILSKKTLHLGQTLYVVNGDLTEVRCDAVVHPTNGTMSFAGQVGGAIRAAAGAGVDAEVNSYMSEHSQLQVTKAAITSGHNLPSKWIVHVHSPNYSNAATATDALTQTIRNALTLADTKSIKTIAFPSIGSGNNHFPKHIAAQTILQAISAYFMSIMSSSIKEVYFVLFDQESINVYNAELINTN

Histone macroH2A1.1

Capsaspora owczarzaki (strain ATCC 30864)

595,528

368

38,580

3D-structure;Chromatin regulator;Chromosome;DNA-binding;Nucleosome core;Nucleus;Reference proteome

GO:0000786; GO:0003677; GO:0005634; GO:0006325; GO:0010836; GO:0030527; GO:0046982; GO:0072570; GO:0160002; GO:1902688

Evidence at protein level

5

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75367}. Chromosome {ECO:0000250|UniProtKB:O75367}.

null

PF00125;PF16211;PF01661;

IPR009072;IPR002119;IPR007125;IPR032454;IPR032458;IPR002589;IPR043472;

7NY6;7NY7;

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Filasterea (class), Capsaspora (genus), Capsaspora owczarzaki (species)

CAOG_004778

false

108

A0A0D2Y5A7

MLSAALRRRVLAPTHSALRTGFAAHVVRHYASFPEHQVIKMPALSPTMQAGNIGAWQKKPGDSIAPGDVLVEIETDKAQMDFEFQEEGVIAKILKDAGEKDIPVGSPIAVLVEEGTDISAFEKFSIEDAGGDAAKPAAPKKEEKSESKSESASAPEPTPEPQQYQSQGRLQTALDRLPNISASAKRLAREKGISIDGLKGTGKNGQITEEDVKKAISSPAASSAPSATYEDIPISGMRKTIANRLVESTQTNPHFYVTSSISVSKLLKLRQALNSSADGKYKLSVNDFLIKAIAVASRKVPQVNSSWRDGNIRQFNNVDVSVAVSTPTGLITPIVTGVEGRGLEAISSQVKSLAKKARDGKLKPEEYQGGTISISNMGMNPAVDHFTAVINPPQAAILAVGTTKKVAIPAENEAGVEFDDQITLTASFDHKVVDGAVGAEWLKELKQVLENPLELLL

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC 2.3.1.12) (FoDLAT) (DLAT)

Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936) (Fusarium vascular wilt of tomato)

426,428

457

48,774

Acyltransferase;Lipoyl;Mitochondrion;Pyruvate;Reference proteome;Transferase;Transit peptide

GO:0004742; GO:0005739; GO:0005759; GO:0006086; GO:0009060; GO:0045254

Evidence at protein level

5

SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:34927582}.

null

PF00198;PF00364;PF02817;

IPR003016;IPR001078;IPR000089;IPR023213;IPR045257;IPR036625;IPR006257;IPR004167;IPR011053;

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 oxysporum species complex (no rank), Fusarium oxysporum (species), Fusarium oxysporum f. sp. lycopersici (no rank)

LAT1 FOXG_11462

false

109

A0A0D9S1R0

MKVLWAALLVTFLAGCQAAADAPIKVEQPVEPETEPELRPQTEWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSPQVTQELTTLMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRSEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLASQPLQERAQALGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTAPVPSDNH

Apolipoprotein E (Apo-E)

Chlorocebus sabaeus (Green monkey) (Simia sabaea)

60,711

323

36,558

Chylomicron;Endosome;Extracellular matrix;Glycoprotein;HDL;Heparin-binding;Lipid transport;Lipid-binding;Oxidation;Phosphoprotein;Reference proteome;Repeat;Secreted;Signal;Transport;VLDL

GO:0005543; GO:0005615; GO:0008201; GO:0008203; GO:0031012; GO:0031175; GO:0032438; GO:0033344; GO:0033700; GO:0034361; GO:0034362; GO:0034363; GO:0034364; GO:0034380; GO:0034382; GO:0034447; GO:0042158; GO:0042627; GO:0042802; GO:0043395; GO:0050750; GO:0055090; GO:0060228; GO:0070062; GO:0071830; GO:0071831; GO:0097487; GO:0120020; GO:1900223; GO:1905907

Inferred from homology

5

SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P02649}. Note=In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. Colocalizes with CD63 and PMEL at exosomes and in intraluminal vesicles within multivesicular endosomes. {ECO:0000250|UniProtKB:P02649}.

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

null

PF01442;

IPR000074;IPR050163;

null

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

APOE

false

110

A0A0E3D8M9

MLYFLAETIFGFICQYVPIGFWNGYSPAPTDRYRRLDLKSSQGFRAEPNLAPLPTTKPRRERYYGPNQIIRAPLDYLLSIPGKDIRGKLINAFNEWLQLPDDKLAIVKEVINLLHTASLLIDDIQDGSRLRRGRPVAHEVFGVAQTINAANYAYFLQQERLSEIGDPRAFHIFTNALLDLHRGQGMDLYWREAVVCPTEEEYIRMVIYKTGGLFRLALELMQVQSNSTTDFSELVELLGIIFQIRDDYMNLQSGLYAEKKGSMEDLTEGKFSYPVIHSIHAAPENSMLVDILKQRTEDNVVKVRAVHYMESTGSFQYCRENLARLTKQARHHVKELEVSLGPNRGIHAILDLLHVQQPNEKPLV

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

Penicillium janthinellum (Penicillium vitale)

5,079

364

41,736

Isoprene biosynthesis;Magnesium;Metal-binding;Transferase

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

Inferred from homology

5

null

PF00348;

IPR008949;IPR000092;IPR033749;

null

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

janG

false

111

A0A0E3D8P4

MLFLAPGYIFPNVATPVTVAIDFAQAVKQGAYNVLDLKASPIPNPELFQPPSRIIRGPLNYLLSLPGKDIRGKLIDALNEWFRVPEDKLNIIKEIVVILHTASLLIDDIQDSSELRRGNPVAHRIFGVAQTINSANYAYFLAQAKLADLNDSRAFDIFTKGLLKLHRGQGMELYWRDNLICPTEEEYVEMVSCKTGGLFYLAVQLMQLNSEVTVNFSNFINLLGIIFQIRDDYMNLQSGTMTKTKGFSEDLTEGKFGYPIIHSIHAAPNDSQLIQILKLKTKDEVIKQYAVRYIESTGSFVYCREKLDMYLEEANETFRGLEMLLGPSKGIRAILDFLRTR

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

Penicillium crustosum (Blue mold fungus)

36,656

341

38,580

Isoprene biosynthesis;Magnesium;Metal-binding;Transferase

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

Inferred from homology

5

null

PF00348;

IPR008949;IPR000092;IPR033749;

null

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

penG

false

112

A0A0E3JXD9

MTEQMLDYFIVGAGLGGVAFAEVALQHQKSIFVFAGDKPPSSVAAAGVYNAVILKRFTLVSQAQEQINLLKVFYPEIEKRIQKNIIFDLPTYRRLASVEEQNNFIVASDRPLFQLFLSPKIISDKFKAVISPFGFGLMKQTGYVDTKLLLQSYRNYLQQNGCISAETFNYAELIIHPDFVEYKGQKAKQIIFAEGFQMKHNPFFKDLPLEGAKGELLVIRSENLDVNVLLKAGVFVLPIGNDLYKVGATYNWTDKTNKPTQSAKDELISELKELISCDFEVVEHLAGIRPTVKDRKPLVGRHPFHKNIYLLNGLGTRGVMLAPYLSYKLFDFIESDLPLDSSISIERYYNSITSSNK

D-amino-acid oxidase (DAAO) (DAMOX) (DAO) (EC 1.4.3.3)

Unknown prokaryotic organism

2,725

357

40,314

Cell wall;Cytoplasm;FAD;Flavoprotein;Oxidoreductase;Secreted

GO:0003884; GO:0005576; GO:0005737; GO:0009063; GO:0009274

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A5U3S4}. Secreted, cell wall {ECO:0000250|UniProtKB:A5U3S4}.

null

PF01266;

IPR006076;IPR036188;

null

cellular organisms (no rank), Bacteria (domain), environmental samples (no rank)

dao daoE

false

113

A0A0E3KBH3

MAGLKVEWNDWCPGCGNFGILSAEQQAIQELGLDPKKVVLVSGIGCSGKIPHFIRLPASGVHTLHGRALTFAIGIKLANPSLEVIVNGGDGDQLGIGVGHFVSAGRRNVDLTVIVHNNGVYGLTKGQASPTLKLGVKTKSLPKPNINSDINPIALAISSGYTFVARGYAYDVKHLKEIIKKAIKHKGLAMIDVLQPCPTYNDIHTKEYYDKRVYKLDEDPSWDPIVKKPEEMDDKMSKAILKSMEWGDRTPIGIFYQNELVSTYEQRIAERSPSYLDNPPAHDVIEFEGKPTTDVEDILKERRVT

2-oxoacid:ferredoxin oxidoreductase subunit beta (OFOR) (EC 1.2.7.11)

Saccharolobus solfataricus (Sulfolobus solfataricus)

2,287

305

33,616

Iron;Iron-sulfur;Magnesium;Metal-binding;Oxidoreductase;Thiamine pyrophosphate

GO:0000287; GO:0018491; GO:0019164; GO:0030976; GO:0047553; GO:0051539

Evidence at protein level

5

null

PF12367;PF02775;

IPR053399;IPR051457;IPR011896;IPR032686;IPR029061;IPR011766;

null

cellular organisms (no rank), Archaea (domain), Thermoproteati (kingdom), Thermoproteota (phylum), Thermoprotei (class), Sulfolobales (order), Sulfolobaceae (family), Saccharolobus (genus)

SSOP1_2914 SULA_0624 SULB_0626 SULC_0624

false

114

A0A0E3T3B5

MAIQIPSRQLFIDGEWREPVLKKRIPIINPATEQIIGDIPAATAEDVEIAVEAARKALARNKGRDWALAPGAVRAKYLRAIAAKIAERKSEIAKLEAIDCGKPLDEAAWDIDDVSGCFEYYADLAEGLDAQQKTPISLPMEQFKSHVLKEPIGVVGLITPWNYPLLMATWKVAPALAAGCAAILKPSELASVTCLELADVCREVGLPPGVLNILTGLGHEAGAPLASHPHVDKIAFTGSTMTGSKIMTAAAQLVKPVSLELGGKSPIVVFDDVDIDKAAEWTAFGIFWTNGQICSATSRLIIHENIAAKFLDRLVQWCKNIKIADPLEEGCRLGPVVSGGQYEKILKFIATAKSEGARVLSGGARPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSSEDEALELANDSHYGLGAAVISKDLERCERVSKALQAGIVWINCSQPCFCQAPWGGNKRSGFGRELGKWGLDNYLTVKQVTEYVSDDPWGWYKSPSKL

Aminoaldehyde dehydrogenase 2, peroxisomal (MdAMADH2) (EC 1.2.1.-) (Aminobutyraldehyde dehydrogenase AMADH2) (EC 1.2.1.19)

Malus domestica (Apple) (Pyrus malus)

3,750

503

54,661

Metal-binding;NAD;Oxidoreductase;Peroxisome;Sodium

GO:0005777; GO:0019145; GO:0019285; GO:0046872; GO:0102244; GO:0110095

Evidence at protein level

5

SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:26296314}.

null

PF00171;

IPR016161;IPR016163;IPR016160;IPR029510;IPR016162;IPR015590;

null

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

AMADH2

false

115

A0A0E3T552

MAIQIPSRLLFIDGEWREPVLKKRIPIINPATEEIIGHIPAATAEDVELAVEAARRALSRNKGRDWASAPGAVRAKYLRAIAAKIGERKPEIAKLEAIDCGKPLDEAAWDIDDVSGCFEYYAELAEGLDAQQKAPISLPMEQFKSHVLKEPIGVVGLITPWNYPLLMATWKVAPALAAGCAAILKPSELASVTCLELADVCREVGLPPGVLNILTGLGHEAGAPLVSHPHVDKIAFTGSTMTGSKIMTAAAQLVKPVSLELGGKSPIVVFDDVDIDKAAEWTAFGCFWTNGQICSATSRLILHENIATEFLDRLLKWCKNIKIADPLEEGCRLGPVVSGGQYEKILKSIETAKSEGARVLSGGDRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSSEDEALELANDTHYGLGAAVISKDLERCDRFSKGLQAGIVWINCSQPCFCQAPWGGNKRSGFGRELGKWGLDNYLTVKQVTEYVSDDPWGWYTSPSKL

Aminoaldehyde dehydrogenase 1, peroxisomal (MdAMADH1) (EC 1.2.1.-) (Aminobutyraldehyde dehydrogenase AMADH1) (EC 1.2.1.19)

Malus domestica (Apple) (Pyrus malus)

3,750

503

54,779

Cytoplasm;Metal-binding;NAD;Oxidoreductase;Sodium

GO:0005829; GO:0019145; GO:0019285; GO:0046872; GO:0102244; GO:0110095

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26296314}.

null

PF00171;

IPR016161;IPR016163;IPR016160;IPR029510;IPR016162;IPR015590;

null

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

AMADH1

false

116

A0A0F5HNH9

MKEELDAFHQIFTTTKEAIERFMAMLTPVIENAEDDHERLYYHHIYEEEEQRLSRLDVLIPLIEKFQDETDEGLFSPSNNAFNRLLQELNLEKFGLHNFIEHVDLALFSFTDEERQTLLKELRKDAYEGYQYVKEKLAEINARFDHDYADPHAHHDEHRDHLADMPSAGSSHEEVQPVAHKKKGFTVGSLIQ

Ferritin-like protein (EC 1.16.3.1) (IMEF cargo protein)

Bacillus thermotolerans (Quasibacillus thermotolerans)

1,221,996

192

22,608

3D-structure;Encapsulin nanocompartment;Iron;Iron storage;Oxidoreductase;Reference proteome

GO:0004322; GO:0006879; GO:0140315; GO:0140737

Evidence at protein level

5

SUBCELLULAR LOCATION: Encapsulin nanocompartment {ECO:0000269|PubMed:31194509, ECO:0000269|PubMed:31282860}.

null

PF24309;

IPR030909;

6N63;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Bacillaceae (family), Bacillus (genus)

IMEF QY95_01593

false

117

A0A0F6B5X3

MKTMPQIAIESNERLSLRVSTDAKKLIVRAAAIQQTNLTDFVVSNILPVAQKIVDAAERVYLTERDTKMIMEILDNPPAPNEKLLAAAFALPDMKK

Antitoxin TacA3 (Antitoxin A6)

Salmonella typhimurium (strain 14028s / SGSC 2262)

588,858

96

10,679

3D-structure;DNA-binding;Repressor;Toxin-antitoxin system;Transcription;Transcription regulation

GO:0003677; GO:0006355

Evidence at protein level

5

null

PF08681;

IPR010985;IPR014795;

7AK9;7ZG5;

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Salmonella (genus), Salmonella enterica (species), Salmonella enterica I (subspecies), Salmonella typhimurium (no rank), Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (strain)

tacA3 a6 STM14_3505

false

118

A0A0F6B5X4

MMFTDWHEAAIGKTHNRMNFDCGDADLNQFLQRHARQNHEKGTTKTYVALDNSDVTRIHGFYSVSPASLIYAQVPGAISKGLGRYDVPVFRLGRLAVDKSMQGQGLGAQLLLSAGKRCIQAALQVGGVALLIDAKNKQVCDWYKGFGAVPLNDQPLSLLLSFKTLYAALSASGRL

tRNA-acetylating toxin 3 (TacT3) (EC 2.3.1.-) (Toxin A6)

Salmonella typhimurium (strain 14028s / SGSC 2262)

588,858

175

19,070

3D-structure;Acyltransferase;Repressor;RNA-binding;Toxin-antitoxin system;Transcription;Transcription regulation;Transferase;tRNA-binding

GO:0000049; GO:0016747

Evidence at protein level

5

null

PF00583;

IPR016181;IPR000182;

6G96;7AK9;7ZG5;

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Salmonella (genus), Salmonella enterica (species), Salmonella enterica I (subspecies), Salmonella typhimurium (no rank), Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (strain)

tacT3 a6 STM14_3506

false

119

A0A0F6B8D8

MGRVTAPEPLSAFHQVAEFVSGEAVLDDWLKQKGLKNQALGAARTFVVCKKDTKQVAGFYSLATGSVNHTEATGNLRRNMPDPIPVIILARLAVDLSFHGKGLGADLLHDAVLRCYRVAENIGVRAIMVHALTEEAKNFYIHHGFKSSQTQQRTLFLRLPQ

tRNA-acetylating toxin 1 (TacT1) (EC 2.3.1.-) (Toxin T8) (tRNA-acetylating toxin) (TacT)

Salmonella typhimurium (strain 14028s / SGSC 2262)

588,858

161

17,735

3D-structure;Acyltransferase;Repressor;RNA-binding;Toxin-antitoxin system;Transcription;Transcription regulation;Transferase;tRNA-binding

GO:0000049; GO:0016747

Evidence at protein level

5

null

PF13508;

IPR016181;IPR000182;

5FVJ;7AK8;

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Salmonella (genus), Salmonella enterica (species), Salmonella enterica I (subspecies), Salmonella typhimurium (no rank), Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (strain)

tacT1 t8 STM14_4401

false

120

A0A0F6B8D9

MLYKGCLMKSDVQLNLRAKESQRALIDAAAEILHKSRTDFILETACQAAEKVILDRRVFNFNDEQYEEFINLLDAPVADDPVIEKLLARKPQWDV

Antitoxin TacA1 (Antitoxin A8)

Salmonella typhimurium (strain 14028s / SGSC 2262)

588,858

95

10,951

3D-structure;DNA-binding;Repressor;Toxin-antitoxin system;Transcription;Transcription regulation

GO:0003677; GO:0006355

Evidence at protein level

5

null

PF08681;

IPR010985;IPR014795;

7AK8;7ZG6;

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Salmonella (genus), Salmonella enterica (species), Salmonella enterica I (subspecies), Salmonella typhimurium (no rank), Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (strain)

tacA1 a8 STM14_4402

false

121

A0A0F7G352

MAAKLLFFLLFLVSALSVALAGFEEDNPIRSVTQRPDSIEPAILGVLGSCRHAFHFARFARRYGKSYGSEEEIKKRFGIFVENLAFIRSTNRKDLSYTLGINQFADLTWEEFRTNRLGAAQNCSATAHGNHRFVDGVLPVTRDWREQGIVSPVKDQGSCGSCWTFSTTGALEAAYTQLTGKSTSLSEQQLVDCASAFNNFGCNGGLPSQAFEYVKYNGGIDTEQTYPYLGVNGICNFKQENVGVKVIDSINITLGAEDELKHAVGLVRPVSVAFEVVKGFNLYKKGVYSSDTCGRDPMDVNHAVLAVGYGVEDGIPYWLIKNSWGTNWGDNGYFKMELGKNMCGVATCASYPIVAV

Vanillin synthase, chloroplastic (Ferulate hydratase/lyase) (VpVAN) (EC 4.1.2.65)

Vanilla planifolia (Vanilla)

51,239

356

39,031

Chloroplast;Disulfide bond;Glycoprotein;Lyase;Plastid;Reference proteome;Transit peptide

GO:0006508; GO:0008234; GO:0009507; GO:0009699; GO:0042189; GO:0042802; GO:0042803; GO:0050547; GO:0062116

Evidence at protein level

5

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:29186560}. Note=Localized in chloroplasts and re-differentiated chloroplasts termed phenyloplasts during pod development. {ECO:0000269|PubMed:29186560}.

null

PF08246;PF00112;

IPR038765;IPR025661;IPR000169;IPR025660;IPR013128;IPR000668;IPR039417;IPR013201;

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), Asparagales (order), Orchidaceae (family), Vanilloideae (subfamily), Vanilleae (tribe), Vanilla (genus)

VAN HPP92_025938 HPP92_026221

false

122

A0A0F7KYQ8

MLKVISSLLVYMTASVMAVASPLAHSGEPSGEYPTVNEIPVGEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDELLLIDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAAGVATYASPSTRRLAEAEGNEIPTHSLEGLSSSGDAVRFGPVELFYPGAAHSTDNLVVYVPSANVLYGGCAVHELSSTSAGNVADADLAEWPTSVERIQKHYPEAEVVIPGHGLPGGLDLLQHTANVVKAHKNRSVAE

Metallo-beta-lactamase VIM-1 (EC 3.5.2.6)

Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

208,964

266

28,024

3D-structure;Antibiotic resistance;Hydrolase;Metal-binding;Periplasm;Plasmid;Signal;Zinc

GO:0016787; GO:0042597; GO:0046677; GO:0046872

Evidence at protein level

5

SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P25910}.

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

null

PF00753;

IPR001279;IPR050855;IPR036866;IPR049721;

7UYA;7UYB;7UYC;8Y4I;8Y4K;8Y4M;9C5P;

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Pseudomonadales (order), Pseudomonadaceae (family), Pseudomonas (genus), Pseudomonas aeruginosa group (no rank), Pseudomonas aeruginosa (species)

VIM-1 blaVIM-1

false

123

A0A0G2JDV3

MTQPQMAPICLVENHNEQLSVNQEAIEILDKISQPVVVVAIVGLYRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLDTEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMITINHQALEQLQYVTELTELIRAKSSPNPAGIKNSTEFVSFFPDFVWTVRDFMLELKLNGEDITSDDYLENALKLIPGDKPRMQASNSCRECIRLFFPNRKCFVFDRPTHDKELLQKLDSITEDQLDPKFQEVTKAFVSYIFTYAKIKTLKEGIKVTGNRLGILVTTYVNAINSGAVPCLDDAVTTLAQRENSVAVQKAADHYSEQMAQRLRLPTETLQELLDVHAACEKEAMAVFMEHSFKDENQQFLKKLVELIGENKELFLSKNEEASNKYCQEELDRLSKDFMENISTFFVPCGHKLYMDKREKIEHDYWQVPRKGVKASEVFQSFLQSQAFIESSILQADTALTAGEKAIAEERAQKVAAEKEQELLRQKQKEQQEYMEAQEKSHKENLEQLRRKLEQEREQDIKDHDMMLKKLMKDQKAFLEEGFKKKAEEMNKEIQQLRDVIKDKKRNTDRIKEALLNGFSTVLFHYLVRYLKHL

Guanylate-binding protein 6 (EC 3.6.5.-) (GTP-binding protein 6) (GBP-6) (Guanine nucleotide-binding protein 6) (Macrophage activation 2 like protein)

Mus musculus (Mouse)

10,090

611

70,443

Antimicrobial;Cytoplasmic vesicle;GTP-binding;Hydrolase;Immunity;Innate immunity;Nucleotide-binding;Reference proteome

GO:0003924; GO:0005525; GO:0009617; GO:0020005; GO:0031410; GO:0035458; GO:0042832; GO:0044406; GO:0050830; GO:0071222; GO:0071346

Evidence at transcript level

5

SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:18025219}.

null

PF02263;PF02841;

IPR030386;IPR037684;IPR003191;IPR036543;IPR015894;IPR027417;

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), 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)

Gbp6 Mpa2l

false

124

A0A0G2JTR4

MEPLSHRGLPRLSWIDTLYSNFSYGAEDYDAEGHEEQKGPPEGSETMPYIDESPTMSPQLSARSQGGGESISPTPPEGLAPGVEAGKGLEMRKLVLSGFLASEEIYINQLEALLLPMKPLKATATTSQPVLTIQQIETIFYKIQDIYEIHKEFYDNLCPKVQQWDSQVTMGHLFQKLASQLGVYKAFVDNYKVALETAEKCSQSNNQFQKISEELKVKGPKDSKDSHTSVTMEALLYKPIDRVTRSTLVLHDLLKHTPVDHPDYPLLQDALRISQNFLSSINEDIDPRRTAVTTPKGETRQLVKDGFLVEMSESSRKLRHVFLFTDVLLCAKLKKTSAGKHQQYDCKWYIPLADLVFPSPEESEASPQVHPFPDHELEDMKVKISALKSEIQKEKANKGQSRAIERLKKKMFENEFLLLLNSPTIPFRIHNRNGKSYLFLLSSDYERSEWREAIQKLQKKDLQAFVLSSVELQVLTGSCFKLRTVHNIPVTSNKDDDESPGLYGFLHVIVHSAKGFKQSANLYCTLEVDSFGYFVSKAKTRVFRDTTEPKWDEEFEIELEGSQSLRILCYEKCYDKTKVNKDNNEIVDKIMGKGQIQLDPQTVESKNWHTDVIEMNGIKVEFSMKFTSRDMSLKRTPSKKQTGVFGVKISVVTKRERSKVPYIVRQCIEEVEKRGIEEVGIYRISGVATDIQALKAVFDANNKDILLMLSDMDINAIAGTLKLYFRELPEPLLTDRLYPAFMEGIALSDPAAKENCMMHLLRSLPDPNLITFLFLLEHLKRVAEKEPINKMSLHNLATVFGPTLLRPSEVESKAHLTSAADIWSHDVMAQVQVLLYYLQHPPISFAELKRNTLYFSTDV

Active breakpoint cluster region-related protein

Rattus norvegicus (Rat)

10,116

859

97,693

Cell projection;Coiled coil;GTPase activation;Guanine-nucleotide releasing factor;Phosphoprotein;Reference proteome;Synapse

GO:0002692; GO:0005085; GO:0005096; GO:0005829; GO:0005886; GO:0006909; GO:0007420; GO:0016020; GO:0016477; GO:0030036; GO:0030424; GO:0032496; GO:0035556; GO:0042472; GO:0043114; GO:0043197; GO:0043312; GO:0043314; GO:0050728; GO:0050766; GO:0050804; GO:0050885; GO:0051649; GO:0060313; GO:0098685; GO:0098978; GO:0099092; GO:1905517; GO:1905522

Evidence at protein level

5

SUBCELLULAR LOCATION: Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q5SSL4}. Cell projection, axon {ECO:0000250|UniProtKB:Q5SSL4}. Synapse {ECO:0000269|PubMed:20962234}.

null

PF00168;PF19057;PF00620;PF00621;

IPR037769;IPR037865;IPR000008;IPR035892;IPR035899;IPR000219;IPR001331;IPR011993;IPR001849;IPR008936;IPR000198;

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)

Abr

false

125

A0A0G2JTY4

MTTANCGAHDELDFKLVFGEDGAPTPVSQVSRPADLEPDDCASIYIFNVDPPPSTLNSSLGLPHHGLLQSHSSVLSPSFQLQGFKNYEGTDDISESKYSSLSGPKPFECPSIQITSISPNCHQETDAHEDDLHVNDPEREYLERPSRDHLYLPLEPSYRESSLSPSPASSVSSRSWFSDASSCESLSHIYDDVDSELNEAAARFTLGSPLTSPGGSPGGCPGEESWHQQYGPGHSLSPRQSPCHSPRSSITDENWLSPRPASGPSSRPTSPCGKRRHSSAEVCYAGSLSPHHSPVPSPGHSPRGSVTEDTWLTAPVHTGSGLSPAPFPFQYCVETDIPLKTRKTSDDQAAILPGKLEVCSDDQGSLSPSRETSVDDGLGSQYPLKKDSSGDQFLSVPSPFTWSKPKPGHTPIFRTSSLPPLDWPLPTHFGQCELKIEVQPKTHHRAHYETEGSRGAVKASTGGHPVVKLLGYSEKPINLQMFIGTADDRYLRPHAFYQVHRITGKTVATASQEIIIASTKVLEIPLLPENNMSASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGKVLSLQIASIPVECSQRSAQELPHIEKYSINSCSVNGGHEMIVTGSNFLPESKIIFLEKGQDGRPHWEAEGKIIREKCQGGHIVLEVPPYHNPAVTSAVQVHFYLCNGKRKKSQSQRFTYTPVLMKQEQREDTDLSSVPSLPVPHSAQTQRPSSDTGHPHDSALSAPRSLICPVQPAYASMITSTHLPQLQCRDEGAGKEQHIIPSSVMHQPFQVTPTSPMGSSYQSIQTNMYNGPTCLPMNPASSQEFDPVLFQQDAALSNLVNLGCQPLSPIPFHSSNSDATGHLLAHSPHSVQTPPHLQSMGYHCSSAGQRSLSSPVAAQVTGQPSSHLQPITYCPSHPGSATAASPAASHALSSSPISGPPSPQLQSMPYQSPSSGTASSPSPVTRMHSGQHSTQAQSTGQGGLSVPSSLVCHSLCDPASFPPGGAAVSIKPEPEDQEPNFATIGLQDITLDDVNEIIGRDMSQITVSQGPEVIRDAPLPGPESPDVMSSNSAQ

Nuclear factor of activated T-cells, cytoplasmic 3 (NFATc3) (NFATx) (T-cell transcription factor NFAT4)

Rattus norvegicus (Rat)

10,116

1,076

115,656

Acetylation;Cytoplasm;DNA-binding;Nucleus;Phosphoprotein;Reference proteome;Repeat;Transcription;Transcription regulation;Ubl conjugation

GO:0000976; GO:0000978; GO:0000981; GO:0001227; GO:0001228; GO:0001569; GO:0001666; GO:0001974; GO:0003677; GO:0003682; GO:0003700; GO:0005634; GO:0005667; GO:0005737; GO:0005829; GO:0006355; GO:0006366; GO:0006606; GO:0007507; GO:0010613; GO:0014898; GO:0014902; GO:0014904; GO:0030217; GO:0033173; GO:0035886; GO:0043065; GO:0043565; GO:0045059; GO:0045333; GO:0045429; GO:0045893; GO:0045944; GO:0048538; GO:0048741; GO:0071277; GO:0071285; GO:0097084; GO:1902894; GO:1904157; GO:1905064; GO:1905653; GO:1990837; GO:2001256

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19538478, ECO:0000269|PubMed:30980393}. Nucleus {ECO:0000269|PubMed:19538478, ECO:0000269|PubMed:30980393}. Note=The subcellular localization of NFATC plays a key role in the regulation of gene transcription (By similarity). Rapid nuclear exit of NFATC is thought to be one mechanism by which cells distinguish between sustained and transient calcium signals (By similarity). Cytoplasmic when phosphorylated and nuclear after activation, that is controlled by calcineurin-mediated dephosphorylation (By similarity). Translocation to the nucleus is increased in the presence of calcium in pre-osteoblasts (By similarity). Translocates to the nucleus in the presence of EDN1 following colocalization with F-actin filaments, translocation is ROCK-dependent (PubMed:19538478). Translocates to the nucleus in response to lipopolysaccharide treatment of macrophages (By similarity). {ECO:0000250|UniProtKB:P97305, ECO:0000269|PubMed:19538478}.

null

PF16179;PF00554;

IPR013783;IPR014756;IPR002909;IPR008366;IPR008967;IPR032397;IPR011539;IPR037059;

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)

Nfatc3 Nfat4

false

126

A0A0G2JTZ2

MSSKQATSPFACTVDGEETMTQDLTSREKEEGSDQHPASHLPLHPIMHNKPHSEELPTLVSTIQQDADWDSVLSSQQRMESENNKLCSLYSFRNTSTSPHKPDEGSREREIMNSVTFGTPERRKGSLADVVDTLKQKKLEEMTRTEQEDSSCMEKLLSKDWKEKMERLNTSELLGEIKGTPESLAEKERQLSTMITQLISLREQLLAAHDEQKKLAASQIEKQRQQMDLARQQQEQIARQQQQLLQQQHKINLLQQQIQVQGHMPPLMIPIFPHDQRTLAAAAAAQQGFLFPPGITYKPGDNYPVQFIPSTMAAAAASGLSPLQLQKGHVSHPQINPRLKGISDRLGRNLDPYEHGGGHSYNHKQIEQLYAAQLASMQVSPGAKMPSTPQPPNSAGAVSPTGIKNEKRGTSPVTQVKDETTAQPLNLSSRPKTAEPVKSPTSPTQSLFPASKTSPVNLPNKSSIPSPIGGSLGRGSSLDILSSLNSPALFGDQDTVMKAIQEARKMREQIQREQQQQPHGVDGKLSSMNSMGLSNCRNEKERTRFENLGPQLTGKSSEDGKLGPGVIDLTRPEDAEGSKAMNGSAAKLQQYYCWPTGGATVAEARVYRDARGRASSEPHIKRPMNAFMVWAKDERRKILQAFPDMHNSNISKILGSRWKSMSNQEKQPYYEEQARLSKIHLEKYPNYKYKPRPKRTCIVDGKKLRIGEYKQLMRSRRQEMRQFFTVGQQPQIPITTGTGVVYPGAITMATTTPSPQMTSDCSSTSASPEPSLPVIQSTYGMKMDGASLAGNDMINGEDEMEAYDDYEDDPKSDYSSENEAPEPVSAN

Transcription factor SOX-6

Rattus norvegicus (Rat)

10,116

827

91,816

Activator;Alternative splicing;Coiled coil;Cytoplasm;Developmental protein;Differentiation;DNA-binding;Isopeptide bond;Nucleus;Phosphoprotein;Reference proteome;Repressor;Transcription;Transcription regulation;Ubl conjugation

GO:0000122; GO:0000902; GO:0000976; GO:0000978; GO:0000981; GO:0000987; GO:0001217; GO:0001227; GO:0001502; GO:0001701; GO:0002062; GO:0003677; GO:0003700; GO:0005634; GO:0005737; GO:0006355; GO:0006357; GO:0007417; GO:0007420; GO:0009791; GO:0010467; GO:0010468; GO:0021529; GO:0021778; GO:0030097; GO:0030218; GO:0032332; GO:0042803; GO:0043565; GO:0045165; GO:0045892; GO:0045893; GO:0045944; GO:0048708; GO:0048709; GO:0048821; GO:0051216; GO:0055007; GO:0061036; GO:0071560; GO:2000726; GO:2000741

Evidence at protein level

5

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40645, ECO:0000255|PROSITE-ProRule:PRU00267}. Cytoplasm {ECO:0000250|UniProtKB:P40645}.

null

PF00505;

IPR009071;IPR036910;IPR051356;

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)

Sox6 Sox-6

false

127

A0A0G2JUG7

MACRRRYLSSLETGSSLSTDRYSVEGEAPSSETGTSLDSPSAYHQGPLVPGSSLSPDHYEHTSVGAYGLYAGPGPQQRTRRPRLQHSTSVLRKQAEEEAIKRSRSLSESYELSSDLQDKQVEMLERKYGGRLVTRHAARTIQTAFRQYQMNKNFERLRSSMSENRMSRRIVLSNMRMQFSFEGPEKVHSSYFEGKQVSVTNDGSQLGALVPSECGDLSDPALKSPAPSSDFADAITELEDAFSRQVKSLAESIDDALNCRSLHSEEVPASDTARARDTEPKPGLHGMDHRKLDEMTASYSDVTLYIDEEELSPPLPLSQAGDRPSSTESDLRLRSGGAAQDYWALAHKEDKADTDTSCRSTPSLERPEPRLRVEHLPLLTIEPPSDSSVELSDRSDRSSLKRQSAYERSLGGQQGSPKHGPHGGPPKGLPREEPELRPRPPRPLESHLAINGSANRQSKSESDYSDGDNDSINSTSNSNDTINCSSESSSRDSLREQTLSKQTYHKETRNSWDSPAFSNDVIRKRHYRIGLNLFNKKPEKGIQYLIERGFVPDTPVGVAHFLLQRKGLSRQMIGEFLGNRQKQFNRDVLDCVVDEMDFSAMELDEALRKFQAHIRVQGEAQKVERLIEAFSQRYCVCNPGVVRQFRNPDTIFILAFAIILLNTDMYSPNVKPERKMKLEDFVKNLRGVDDGEDIPRETLIGIYERIRKRELKTNEDHVSQVQKVEKLIVGKKPIGSLHHGLGCVLSLPHRRLVCYCRLFEVPDPNKPQKLGLHQREIFLFNDLLVVTKIFQKKKNSVTYSFRQSFSLYGMQVLLFENQYYPNGIRLTSAVPGADIKVLINFNAPNPQDRKKFTDDLRESVAEVQEMEKHRIESELEKQKGVVRPSMSQCSSLKKESGNGTLSRACLDDSYASGEGLKRSALSSSLRDLSEAGKRGRRSSAGSLESNVEFQPFQPSQPPVLCS

IQ motif and SEC7 domain-containing protein 1

Rattus norvegicus (Rat)

10,116

962

108,080

Coiled coil;Cytoplasm;Cytoplasmic vesicle;Guanine-nucleotide releasing factor;Lipid-binding;Nucleus;Phosphoprotein;Reference proteome;Synapse

GO:0005085; GO:0005634; GO:0008021; GO:0008289; GO:0019901; GO:0030036; GO:0032012; GO:0051549; GO:0051965; GO:0060996; GO:0098685; GO:0098978; GO:0099092; GO:0099149; GO:0099170; GO:0120183

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6DN90}. Nucleus {ECO:0000250|UniProtKB:Q6DN90}. Postsynaptic density {ECO:0000250|UniProtKB:Q8R0S2}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q8R0S2}. Note=At steady state, may be preferentially cytosolic. {ECO:0000250|UniProtKB:Q6DN90}.

null

PF16453;PF01369;

IPR033742;IPR011993;IPR023394;IPR000904;IPR035999;

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)

Iqsec1 Brag2

false

128

A0A0G2JV04

MAEAEGESLESWLNKATNPSNRQEDWEYIIGFCDQINKELEGPQIAVRLLAHKIQSPQEWEAVQALTVLEACMKNCGRRLHNEVGKFRFLNELIKVVSPKYLGDRVSEKVKAKVIELLFSWTLALPEEAKIKDAYHMLKRQGIVQSDPPIPMDRTLIPSPPPRPKNPVFDDEEKSKLLAKLLRSKNPDDLQEANQLIKSMVKEDEARIQKVTKRLHTLEEVNNNVKLLHEMLLHYSQEFSSEADKELMKELFDRCENKRRTLFKLASETEDNDNSLGDILQASDNLSRVINSYKTIIEGQIINGEVTTSTVPDSEGNSHCGNQGALIDLAELDTPSSSSPVLAPAPAPPTSGIPILPPPPQTSGPPRSRSSSQAEAPSGPDSTNNALSLLDEELLCLGLSDPAPTAPKESAGNSPWHLFQNEPSSDLDFFSPRLVSAASCPSEGSLLPPPVSTSSLSQAPLPAAFPAPVVPASAVTHSTGSFTFSSGPAPALVPKAEPEGPEYPSSSISHRLDALDQLLEEAKVTSGLVKPVSCFSPGPTASPLLPASTPARPLLPFSTGPGSPLFQSPAFQSQGSPQKGPELSLASVHVPLESIKPSSALPVTAYDKNGFRILFHFAKECPPGRPDVLVVVVSMLNTAPLPVKSIVLQAAVPKSMKVKLQPPSGTELSPFSPIQPPAAITQVMLLANPMKEKVRLRYKLTFALGEQLSTELGEVDQFPPVEQWGNL

ADP-ribosylation factor-binding protein GGA3 (Golgi-localized, gamma ear-containing, ARF-binding protein 3)

Rattus norvegicus (Rat)

10,116

727

78,759

Endosome;Golgi apparatus;Membrane;Phosphoprotein;Protein transport;Reference proteome;Transport;Ubl conjugation

GO:0005764; GO:0005769; GO:0005802; GO:0006622; GO:0006893; GO:0030163; GO:0031267; GO:0031647; GO:0031648; GO:0031901; GO:0032456; GO:0032991; GO:0034394; GO:0035091; GO:0043001; GO:0043130; GO:0044877; GO:0045732; GO:0055037; GO:0055038; GO:0061462; GO:0140318; GO:1902430

Evidence at protein level

5

SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9NZ52}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NZ52}. Endosome membrane {ECO:0000250|UniProtKB:Q9NZ52}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NZ52}. Early endosome membrane {ECO:0000269|PubMed:26446845}; Peripheral membrane protein {ECO:0000305}. Recycling endosome membrane {ECO:0000269|PubMed:26446845}; Peripheral membrane protein {ECO:0000305}.

null

PF02883;PF03127;PF18308;PF00790;

IPR008152;IPR013041;IPR008942;IPR008153;IPR004152;IPR044111;IPR038425;IPR027422;IPR041198;IPR002014;IPR046996;

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)

Gga3

false

129

A0A0G2JXN2

MAEGEDMQTFTSIMDALVRISTSMKNMEKELLCPVCQEMYKQPLVLPCTHNVCQACAREVLGQQGYIGHGGDPSSEPTSPASTPSTRSPRLSRRTLPKPDRLDRLLKSGFGTYPGRKRGALHPQTILFPCPACQGDVELGERGLSGLFRNLTLERVVERYRQSVSVGGAILCQLCKPPPLEATKGCSECRATFCNECFKLFHPWGTQKAQHEPTLPTLSFRPKGLMCPDHKEEVTHYCKTCQRLVCQLCRVRRTHSGHKITPVLSAYQALKDKLTKSLAYILGNQDTVQTQICELEETIRHTEVSGQQAKEEVSQLVRGLGAVLEEKRSSLLQAIEECQQERLSRLSAQIHEHQSLLDGSGLVGYAQEVLKETDQPCFVQAAKQLHNRIARATEALQTFRPAASSSFRHCQLDVGREMKLLTELNFLRVPEAPVIDTQRTFAYDQIFLCWRLPPHSPPAWHYTVEFRRTDVPAQPGPTRWQRREEVRGTSALLENPDTGSVYVLRVRGCNKAGYGEYSEDVHLHTPPAPVLHFFLDGRWGASRERLAISKDQRAVRSIPGLPLLLAAERLLTGCHLSVDVVLGDVAVTQGRSYWACAVDPASYLVKVGVGLESKLQESFQGAPDVISPRYDPDSGHDSGAEDAAVEALPPFAFLTIGMGKILLGSGASSNAGLTGRDGPAASCTVPLPPRLGICLDYERGRVSFLDAVSFRGLLECPLDCSGPVCPAFCFIGGGAVQLQEPVGTKPERKVTIGGFAKLD

Tripartite motif-containing protein 46

Rattus norvegicus (Rat)

10,116

759

83,431

Cell projection;Coiled coil;Cytoplasm;Cytoskeleton;Metal-binding;Phosphoprotein;Reference proteome;Repeat;Zinc;Zinc-finger

GO:0000226; GO:0001578; GO:0001764; GO:0005856; GO:0007409; GO:0008270; GO:0030517; GO:0032880; GO:0043194; GO:0044304; GO:0048490; GO:0099612; GO:1901953; GO:1904115; GO:1990769

Evidence at protein level

5

SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:26671463}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26671463}. Note=Microtubule-associated. Localizes to the proximal part of the axon. {ECO:0000269|PubMed:26671463}.

null

PF18568;PF00643;PF13445;

IPR001870;IPR043136;IPR013320;IPR017903;IPR050617;IPR003961;IPR036116;IPR013783;IPR040859;IPR035731;IPR027370;IPR000315;IPR001841;IPR013083;IPR017907;

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)

Trim46

false

130

A0A0G2JXT6

MEHIRTTKVEQVKLLDRFSTNNKSLTGTLYLTATHLLFIDAHQKETWILHHHIASVEKLALTTSGCPLVIQCKNFRIVHFIVPRERDCHDIYNSLLQLSKQAKYEDLYAFSYNPKQNDTERLNGWQLIDLAAEYERMGVPNANWQLSDANREYKVCETYPRELYVPRTASRPVIVGSSNFRSKGRLPVLSYCQQGTEAAICRCSQPLSGFSARCLEDEHLLQAISKANPGNRYMYVVDTRPKLRMQSWWDTQKDIGRIIVRISSKIWNDEKIRESDEKKRLNAMANRAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQKLLEVNGSKGLSVNDFYSGLESSGWLRHIKAVLDAAIFLAKAIVVENASVLVHCSDGWDRTSQVCSLGSLLLDSYYRTMKGFMVLIEKDWISFGHKFSERCGHLDGDPKEVSPVFTQFLECVWHLTEQFPQAFEFNEAFLLQIHEHIHSCQFGNFLGNCQKEREELRLKEKTYSLWPFLLADKKKYLNPLYSSKSQRLTVLEPNTASFNFKFWRNMYHQFDRTLHPRQSVLNIIMNMNEQNKQLEEDVKDLEAKIKQCKSGILTKDLLHAVHPESPSLKTSLCLKEQSLLPVKDTLRAVEGSSPADNRYCDYTEEFSKSEPAVVSLEYGVARMTC

Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR6 (EC 3.1.3.95) (Myotubularin-related protein 6) (Phosphatidylinositol-3-phosphate phosphatase)

Rattus norvegicus (Rat)

10,116

655

75,577

Cell membrane;Cell projection;Coiled coil;Cytoplasm;Endocytosis;Endoplasmic reticulum;Hydrolase;Lipid metabolism;Membrane;Phosphoprotein;Reference proteome

GO:0004438; GO:0005635; GO:0005737; GO:0005783; GO:0005793; GO:0006897; GO:0032587; GO:0046856; GO:0048471; GO:0052629; GO:0106018

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23188820}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y217}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q8VE11}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:23188820}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Y217}. Note=Localizes to ruffles during EGF-induced macropinocytosis (By similarity). Colocalizes with MTMR9 to the perinuclear region (By similarity). Partially localizes to the endoplasmic reticulum (By similarity). Co-localizes with RAB1B to the endoplasmic reticulum-Golgi intermediate compartment and to the peri-Golgi region (PubMed:23188820). {ECO:0000250|UniProtKB:Q8VE11, ECO:0000250|UniProtKB:Q9Y217, ECO:0000269|PubMed:23188820}.

null

PF06602;PF21098;

IPR035998;IPR030564;IPR010569;IPR011993;IPR029021;IPR016130;IPR003595;

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)

Mtmr6

false

131

A0A0G2JZ79

MIGTDPRTILKDLLPETIPPPELDDMTLWQIVINILSEPPKRKKRKDINTIEDAVKLLQECKKIIVLTGAGVSVSCGIPDFRSRDGIYARLAVDFPDLPDPQAMFDIEYFRKDPRPFFKFAKEIYPGQFQPSLCHKFIALSDKEGKLLRNYTQNIDTLEQVAGIQRIIQCHGSFATASCLICKYKVDCEAVRGDIFNQVVPRCPRCPADEPLAIMKPEIVFFGENLPEQFHRAMKYDKDEVDLLIVIGSSLKVRPVALIPSSIPHEVPQILINREPLPHLHFDVELLGDCDVIINELCHRLGGEYAKLCCNPVKLSEITEKPPRTQKELVHLSELPPTPLHISEDSSSPERTVPQDSSVIATLVDQTIKNKVDDLEVSEPKSCVEEKSQEVQTYRNVESINVENPDFKAVGSSTGDKNERTSVAETVRKCWPNRLAKEQISKRLDGNQYLFVPPNRYIFHGAEVYSDSEDDALSSSSCGSNSDSGTCQSPSLEEPLEDESEIEEFYNGLEDDADRPECAGGSGADGGDQEAVNEAIAMKQELTDVNCTPDKSEHY

NAD-dependent protein deacetylase sirtuin-1 (EC 2.3.1.286) (NAD-dependent protein deacylase sirtuin-1) (EC 2.3.1.-)

Rattus norvegicus (Rat)

10,116

555

62,059

Acetylation;Apoptosis;Biological rhythms;Cytoplasm;Developmental protein;Differentiation;Metal-binding;Methylation;Myogenesis;NAD;Nucleus;Phosphoprotein;Reference proteome;S-nitrosylation;Transcription;Transcription regulation;Transferase;Ubl conjugation;Zinc

GO:0000012; GO:0000122; GO:0000183; GO:0000720; GO:0000731; GO:0000785; GO:0000791; GO:0000792; GO:0000978; GO:0001525; GO:0001542; GO:0001678; GO:0001938; GO:0002039; GO:0002821; GO:0003713; GO:0003714; GO:0004407; GO:0005634; GO:0005635; GO:0005637; GO:0005654; GO:0005677; GO:0005730; GO:0005737; GO:0005739; GO:0005829; GO:0006325; GO:0006642; GO:0006974; GO:0006979; GO:0007005; GO:0007179; GO:0007283; GO:0007346; GO:0007517; GO:0007623; GO:0008047; GO:0008284; GO:0008630; GO:0009267; GO:0010046; GO:0010460; GO:0010628; GO:0010629; GO:0010659; GO:0010667; GO:0010824; GO:0010868; GO:0010875; GO:0010883; GO:0010898; GO:0010906; GO:0010918; GO:0010976; GO:0014858; GO:0016239; GO:0016567; GO:0016605; GO:0016922; GO:0017136; GO:0019213; GO:0019899; GO:0019904; GO:0030225; GO:0030424; GO:0030426; GO:0030512; GO:0031393; GO:0031507; GO:0031648; GO:0031667; GO:0032007; GO:0032041; GO:0032436; GO:0032720; GO:0032868; GO:0032922; GO:0032991; GO:0033210; GO:0033553; GO:0033558; GO:0034391; GO:0034979; GO:0035098; GO:0035331; GO:0035356; GO:0035358; GO:0035774; GO:0042127; GO:0042149; GO:0042220; GO:0042311; GO:0042393; GO:0042542; GO:0042595; GO:0042632; GO:0042771; GO:0042802; GO:0042981; GO:0043065; GO:0043066; GO:0043124; GO:0043161; GO:0043398; GO:0043422; GO:0043425; GO:0043518; GO:0043524; GO:0043536; GO:0044321; GO:0045348; GO:0045471; GO:0045599; GO:0045722; GO:0045739; GO:0045766; GO:0045786; GO:0045892; GO:0045944; GO:0046015; GO:0046628; GO:0046872; GO:0046969; GO:0046970; GO:0050872; GO:0051019; GO:0051152; GO:0051402; GO:0051658; GO:0051897; GO:0051898; GO:0055089; GO:0060125; GO:0060766; GO:0060907; GO:0061051; GO:0061773; GO:0070301; GO:0070403; GO:0070857; GO:0070914; GO:0071236; GO:0071303; GO:0071356; GO:0071456; GO:0071479; GO:0089720; GO:0090335; GO:0090400; GO:0097009; GO:0097193; GO:0106230; GO:0106231; GO:0140297; GO:0140861; GO:0140937; GO:0141050; GO:0141208; GO:0160012; GO:1900181; GO:1901797; GO:1902166; GO:1902176; GO:1902237; GO:1902617; GO:1903427; GO:1904178; GO:1904179; GO:1904373; GO:1904638; GO:1904639; GO:1904644; GO:1904646; GO:1904648; GO:1904710; GO:1990254; GO:1990830; GO:1990841; GO:2000111; GO:2000270; GO:2000614; GO:2000655; GO:2000773; GO:2000774; GO:2000781; GO:2001171

Inferred from homology

5

SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000250|UniProtKB:Q96EB6}. Cytoplasm {ECO:0000250|UniProtKB:Q96EB6}. Nucleus {ECO:0000250|UniProtKB:Q96EB6}. Note=Recruited to the nuclear bodies via its interaction with PML. Colocalized with APEX1 in the nucleus. May be found in nucleolus, nuclear euchromatin, heterochromatin and inner membrane (By similarity). Shuttles between nucleus and cytoplasm (By similarity). Colocalizes in the nucleus with XBP1 isoform 2 (By similarity). {ECO:0000250|UniProtKB:Q923E4, ECO:0000250|UniProtKB:Q96EB6}.

null

PF02146;

IPR029035;IPR050134;IPR003000;IPR026591;IPR026590;

null

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

Sirt1

false

132

A0A0G2K047

MKPSWLQCRKVTGAGTLGAPLPGSPSVRGAGVARRALVAGFGGRGCRALTTSSGGGEYKTHFAASVADPERFWGKAAEQISWYKPWTKTLENRYPPSTSWFVEGMLNICYNAIDRHIENGQGDKIAIIYDSPVTDTKATISYKEVLEQVSKLAGVLVKQGVKKGDTVVIYMPMIPQAIYAMLACARIGAIHSLIFGGFASKELSTRIDHVKPKVVVTASFGIEPGRKVEYMPLLEEALRIGQHKPDRLLIYNRPNMEKVPLMSGRDLDWEEEMAKAQSHDCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGSPITASCIGLGNSKTPPPGQAGKCVPGYNVMILDDNMQKLKARSLGNIVVKLPLPPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESVLSHGTVTDCAVVGKEDPLKGHVPLALCVLKKDVNATEEQVLEEIVKHVRQSIGPVAAFRNAVFVKQLPKTRSGKIPRSTLSALVNGKPYKVTPTIEDPSIFGHIEEVLKQAL

Acyl-CoA synthetase short-chain family member 3, mitochondrial (EC 6.2.1.1) (Acetate--CoA ligase 3) (Acyl-CoA synthetase short-chain family member 3) (Propionate--CoA ligase) (EC 6.2.1.17)

Rattus norvegicus (Rat)

10,116

683

74,675

Acetylation;ATP-binding;Ligase;Lipid metabolism;Mitochondrion;Nucleotide-binding;Reference proteome;Transit peptide

GO:0003987; GO:0005524; GO:0005759; GO:0006629; GO:0031956; GO:0050218

Evidence at protein level

5

SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:28003429}.

null

PF16177;PF00501;PF13193;

IPR032387;IPR025110;IPR045851;IPR020845;IPR000873;IPR042099;

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)

Acss3

false

133

A0A0G2K1Q8

MVVLRQLRLLLWKNYTLKKRKVLVTVLELFLPLLFSGILIWLRLKIQSENVPNATVYPDQHIQELPLFFSFPPPGGSWELAYVPSHSDAARTITEAVRREFMIKMRVHGFSSEKDFEDYVRYDNHSSNVLAAVVFEHTFNHSKDPLPLAVRYHLRFSYTRRNYMWTQTGNLFLKETEGWHTASLFPLFPSPGPREPSSPDGGEPGYIREGFLAVQHAVDKAIMHYHANASAHQLFQKLTVITKRFPFPPYISDPFLIAIQYQLPLLLMLSFTYTSLTIIRAVVQEKEKKLKEYMRMMGLSSWLHWSAWFLMFLLFSLIVVSFMTLLFCVKVKKDIAVLSNSDPSLVLAFLLCFAISSISFSFMVSTFFSKANMAATVGGFLYFFTYTPYFFVAPRYNWMTLSQKLLSCLLSNVAMAMGAQLIGKFEAKGTGIQWCDLLNPVNVDDDFCFGQVLGMLLLDSVLYGLVTWYVEAVFPGQFGVPQPWYFFLMPSYWCGNPRTVVGKEEEGGDPEKAFRTEYFEAEPEDLAAGIKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSMLTGLFPPTSGHAYIRGYEISQDMVQIRKSLGLCPQHDVLFDNLTVAEHLYFYAQLKGLSVQKCPEEVKQMLHTLGLEDKRDSRSKFLSGGMKRKLAIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGSSLFLKQKYGAGYHMTLVKEPHCNPEGISQLVHHHVPNAMLESHAGAELSFILPKESTHRFESLFAKLEKKQKELGIASFGASVTTMEEVFLRVGKLVDTSMDIQAIQLPALQYQHERRASDWALDSNLCGVMDPTNGIGALIEEEEVLVKLNTGLALHCQQFWAMFLKKAAYSWREWRMVAAQILVPVTCLTLALLAINYTSEIFDDPPLKLSLNEYGTTVVPFSVPGTSRLGQQLSEHLRDMLQAERQEPREVLGDLEEFLVFRASVEGGGFNERCLVATSFKDSGERTVVTALFNNQAYHSPATALAIVDNLLFKLLCGPRASIEISNYPQPRSTLQVAKDQFNEGRKGFDIALNLLIAMAFLASTFSILAVSERAVQAKHVQFVSGVHVATFWLSALLWDLISFLVPSLLLLVVFRAFDVHAFTRDGHMADLLLLLMLYGWAIIPLMYLLSFFFSAASTAYTRLTIFNILSGIATFIVVTIMRIPAVKLEELSRTLDHVFLVLPNHCLGMAVSNFYENYETRRYCTSSEVATHYCKKYNIQYQENFYAWSTPGIGKFVTSMAASGGIYLTLLFLIETNLLWRLRTFVCAFRRRWTLAELQNRTSVLPEDQDVADERSRVLVPSLDSMLDTPLIINELSKVYDQRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMGYCPQFDALLDHMTGREMLVMYARLRGIPERLIDACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFGSGYSLQAKVRSEGKQEVLEEFKAFVDLTFPGSVLEDEHQDMVHYHLPGCDLSWAKVFGILEKAKEKYGVDDYSVSQISLEQVFLSFAHLQPPTTEDGR

Phospholipid-transporting ATPase ABCA3 (EC 7.6.2.1) (ATP-binding cassette sub-family A member 3) (Xenobiotic-transporting ATPase ABCA3) (EC 7.6.2.2) [Cleaved into: 150 Kda mature form]

Rattus norvegicus (Rat)

10,116

1,704

191,767

ATP-binding;Cytoplasmic vesicle;Disulfide bond;Endosome;Glycoprotein;Lipid transport;Lysosome;Membrane;Nucleotide-binding;Reference proteome;Repeat;Translocase;Transmembrane;Transmembrane helix;Transport

GO:0005319; GO:0005524; GO:0005765; GO:0005770; GO:0005886; GO:0006855; GO:0006869; GO:0008559; GO:0010875; GO:0015914; GO:0016887; GO:0030324; GO:0030659; GO:0032368; GO:0032464; GO:0032585; GO:0042599; GO:0042626; GO:0042908; GO:0043129; GO:0043231; GO:0046470; GO:0046471; GO:0046618; GO:0046890; GO:0051384; GO:0055091; GO:0070925; GO:0097208; GO:0097232; GO:0097233; GO:0120019; GO:0140345; GO:0150172; GO:1902995; GO:2001140

Evidence at protein level

5

SUBCELLULAR LOCATION: Endosome, multivesicular body membrane {ECO:0000250|UniProtKB:Q99758}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q99758}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q99758}. Late endosome membrane {ECO:0000250|UniProtKB:Q99758}. Lysosome membrane {ECO:0000250|UniProtKB:Q99758}. Note=Localized in the limiting membrane of lamellar bodies in lung alveolar type II cells. Trafficks via the Golgi, sorting vesicles (SVs) and late endosome/multivesicular body network directly to the outer membrane of lamellar bodies in AT2 lung epithelial cells or to lysosomes and lysosomal-related organelles (LROs) in other cells where undergoes proteolytic cleavage and oligosaccharide processing from high mannose type to complex type. Oligomers formation takes place in a post-endoplasmic reticulum compartment. {ECO:0000250|UniProtKB:Q99758}.

null

TRANSMEM 22..42; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 251..271; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 307..327; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 344..364; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 373..393; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 405..425; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1100..1120; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1144..1164; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1183..1203; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1213..1233; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1245..1265; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1310..1330; /note="Helical"; /evidence="ECO:0000255"

PF12698;PF00005;PF23321;

IPR003593;IPR013525;IPR003439;IPR017871;IPR026082;IPR027417;IPR056264;

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)

Abca3

false

134

A0A0G2K2P5

MSARAAAAKSTAMEETAIWEQHTVTLHRAPGFGFGIAISGGRDNPHFQSGETSIVISDVLKGGPAEGQLQENDRVAMVNGVSMDNVEHAFAVQQLRKSGKNAKITIRRKKKVQIPVSHPDPDPVSDNEDDSYDEDVHDPRSGRGALANRRGEKSWARDRSASRDRSLSPRSDRRSVASSQPAKPTKVTLVKSRKNEEYGLRLASHIFVKEISQDSLAARDGNIQEGDVVLKINGTVTENMSLTDAKTLIERSKGKLKMVVQRDERATLLNVPDLSDSIHSANASERDDISEIQSLASDHSVRSHDRPPRRSQSRSPDQRSEPSDHSTQSPQQPSNGSLRSREEERMSKPGAVSTPVKHVDDHTPKAVEEVTVEKHEKQTPTLPEPKPVYAQVGQPDVDLPVSPSDGVLPNSTHEDGILRPSMKLVKFRKGDSVGLRLAGGNDVGIFVAGVLEDSPAAKEGLEEGDQILRVNNVDFTNIIREEAVLFLLDLPKGEEVTILAQKKKDVYRRIVESDVGDSFYIRTHFEYEKESPYGLSFNKGEVFRVVDTLYNGKLGSWLAIRIGKNHKEVERGIVPNKNRAEQLASVQYTLPKTAGGDRADFWRFRGLRSSKRNLRKSREDLSAQPVQTKFPAYERVVLREAGFLRPVTIFGPIADVAREKLAREEPDIYQIAKSEPRDAGTDHRSSGIIRLHTIKQIIDQDKHALLDVTPNAVDRLNYAQWYPIVVFLNPDSKQGVKTMRMRLCPESRKSARKLYERSHKLRKNNHHLFTTTINLNSMNDGWYGALKEAIQQQQNQLVWVSEGKADGATSDDLDLHDDRLSYLSAPGSEYSMYSTDSRHTSDYEDTDTEGGAYTDQELDETLNDEVGTPPESAITRSSEPVREDSSGMHHENQTYPPYSPQAQPQAIHRIDSPGLKTASQQKAEASSPVPYLSPETNPASSASAVKHNVNLTNVNLEEPTPAPPTSHVSQADCLGAPSPEAPHTMLRDEGVSLPSHVDPAKVYRKEPYPEEMMRQNHILKQPALGHPGQRLDKEPNPAYDPQLPYVEKQASRDLEQPPYRYESSSYTDQFSRNYDHRLRFEDRVPTYEDQWSYYDDKQPYPTRPFDTQHPRDLDSRQHPEEASERGYFQRFEEPAPLPYDSRPRYEQLPRTSTLRHEEQPTSGYEVHNRYRPEAQPYAPAGPKSSEPKQYFDQYPRSYEQVPPPGFTSKTGHYEPLHGAAVVPPLIPSSQHKPEVLPSATKPQPPPPALTEEEEDPAMKPQSVLTRVKMFENKRSASLENKKDVNDTASFKPPEVASKPPSASLVGPKPVSQTQFSEHDKTLYRLPEPQKPQAKPPEDIVRSNHYDPEEDEEYYRKQLSYFDRRSFESKPPAHIPAGHHSEPAKPVHSQSQPNFSSYSSKGKPETDAMDRSFSEKRYDPTQAMPPPPPLPSQYSQPVPPLSNSSLHIHSKAAQSEGNSVSLDFQNSYISKPDPPPSQSKPATFRPPTREDPPQTFYPQKSFPDKASVNGAEQTQKTITPAYNRFTPKPYTSSARPFERKFESPKFNHNLLPSETVHKPELSSKPPPSPKTLMKAHSSTQPPEFDSGVETFSVHTDKPKYQINNISTMPKAVPVSPSAVEEDEDEDGHTVVATARGIFNSNGGVLSSIETGVSIIIPQGAIPEGIEQEIYFKVCRDNSILPPLDKEKGETLLSPLVMCGPHGLKFLKPVELRLPHCASMTPDGWSFALKSSDSSSGDPKTWQNKCLPGDPNYLVGANCVSVLIDHF

Tight junction protein ZO-1 (Tight junction protein 1) (Zona occludens protein 1) (Zonula occludens protein 1)

Rattus norvegicus (Rat)

10,116

1,765

197,148

ATP-binding;Cell junction;Cell membrane;Gap junction;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Reference proteome;Repeat;SH3 domain;Tight junction;Transferase

GO:0001825; GO:0005524; GO:0005634; GO:0005737; GO:0005886; GO:0005911; GO:0005912; GO:0005921; GO:0005923; GO:0007605; GO:0008013; GO:0008284; GO:0009410; GO:0009986; GO:0014704; GO:0016020; GO:0016301; GO:0016323; GO:0016324; GO:0016327; GO:0019904; GO:0030036; GO:0030054; GO:0030335; GO:0031032; GO:0031410; GO:0032496; GO:0032991; GO:0034334; GO:0036305; GO:0043066; GO:0043116; GO:0043296; GO:0044325; GO:0045177; GO:0045216; GO:0045471; GO:0046581; GO:0050839; GO:0051493; GO:0051497; GO:0070160; GO:0070830; GO:0071000; GO:0071253; GO:0071277; GO:0071333; GO:0071896; GO:0090557; GO:0098609; GO:0150105; GO:1901888; GO:1902396; GO:1903672; GO:1905605; GO:2000049; GO:2000810

Evidence at protein level

5

SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q07157}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q07157}; Cytoplasmic side {ECO:0000250|UniProtKB:Q07157}. Cell junction, tight junction {ECO:0000269|PubMed:3528172, ECO:0000269|PubMed:9707407}. Cell junction {ECO:0000250|UniProtKB:P12830}. Cell junction, gap junction {ECO:0000250|UniProtKB:Q07157}. Note=Moves from the cytoplasm to the cell membrane concurrently with cell-cell contact (By similarity). Distributed over the entire lateral surface of the plasma membrane and other actin-rich structures (By similarity). Detected at the leading edge of migrating and wounded cells (By similarity). Colocalizes with SPEF1 at sites of cell-cell contact in intestinal epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q07157, ECO:0000269|PubMed:3528172, ECO:0000269|PubMed:9707407}.

null

PF00625;PF00595;PF07653;PF00791;

IPR008145;IPR008144;IPR027417;IPR001478;IPR036034;IPR036028;IPR001452;IPR005417;IPR005418;IPR035597;IPR000906;

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)

Tjp1

false

135

A0A0G2K309

MKSNPAIQAAIDLTAGAAGGTACVLTGQPFDTMKVKMQTFPDLYRGLTDCCLRTYSQVGFRGFYKGTSPALIANIAENSVLFMCYGFCQQVVRKVVGLDRQAKLSDLQNAAAGSFASAFAALVLCPTELVKCRLQTMYEMETSGKIAASQNTVWSVVKEIFRKDGPLGFYHGLSSTLLREVPGYFFFFGGYELSRSFFASGRSKDELGPIPLMLSGGFGGICLWLAVYPVDCIKSRIQVLSMTGKQTGLIRTFLSIVKNEGITALYSGLKPTMIRAFPANGALFLAYEYSRKLMMSQLEAC

Mitochondrial ornithine transporter 1 (Solute carrier family 25 member 15)

Rattus norvegicus (Rat)

10,116

301

32,797

Antiport;Membrane;Mitochondrion;Mitochondrion inner membrane;Reference proteome;Repeat;Transmembrane;Transmembrane helix;Transport

GO:0000064; GO:0005739; GO:0005743; GO:0015189; GO:0015297; GO:0061459; GO:1903401; GO:1903826; GO:1990575

Evidence at protein level

5

SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q12375}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:15057822}; Multi-pass membrane protein {ECO:0000255}.

null

TRANSMEM 5..25; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 68..88; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 110..130; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 168..188; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 207..227; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 237..257; /note="Helical; Name=6"; /evidence="ECO:0000255"

PF00153;

IPR050567;IPR018108;IPR023395;

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)

Slc25a15

false

136

A0A0G2K344

MPPRPSSGELWGIHLMPPRILVECLLPNGMIVTLECLREATLVTIKHELFKEARKYPLHQLLQDESSYIFVSVTQEAEREEFFDETRRLCDLRLFQPFLKVIEPVGNREEKILNREIGFVIGMPVCEFDMVKDPEVQDFRRNILNVCKEAVDLRDLNSPHSRAMYVYPPNVESSPELPKHIYNKLDKGQIIVVIWVIVSPNNDKQKYTLKINHDCVPEQVIAEAIRKKTRSMLLSSEQLKLCVLEYQGKYILKVCGCDEYFLEKYPLSQYKYIRSCIMLGRMPNLMLMAKESLYSQLPIDSFTMPSYSRRISTATPYMNGETATKSLWVINSALRIKILCATYVNVNIRDIDKIYVRTGIYHGGEPLCDNVNTQRVPCSNPRWNEWLNYDIYIPDLPRAARLCLSICSVKGRKGAKEEHCPLAWGNINLFDYTDTLVSGKMALNLWPVPHGLEDLLNPIGVTGSNPNKETPCLELEFDWFSSVVKFPDMSVIEEHANWSVSREAGFSYSHTGLSNRLARDNELRENDKEQLRALCTRDPLSEITEQEKDFLWSHRHYCVTIPEILPKLLLSVKWNSRDEVAQMYCLVKDWPPIKPEQAMELLDCNYPDPMVRSFAVRCLEKYLTDDKLSQYLIQLVQVLKYEQYLDNLLVRFLLKKALTNQRIGHFFFWHLKSEMHNKTVSQRFGLLLESYCRACGMYLKHLNRQVEAMEKLINLTDILKQEKKDETQKVQMKFLVEQMRQPDFMDALQGFLSPLNPAHQLGNLRLEECRIMSSAKRPLWLNWENPDIMSELLFQNNEIIFKNGDDLRQDMLTLQIIRIMENIWQNQGLDLRMLPYGCLSIGDCVGLIEVVRNSHTIMQIQCKGGLKGALQFNSHTLHQWLKDKNKGEIYDAAIDLFTRSCAGYCVATFILGIGDRHNSNIMVKDDGQLFHIDFGHFLDHKKKKFGYKRERVPFVLTQDFLIVISKGAQEYTKTREFERFQEMCYKAYLAIRQHANLFINLFSMMLGSGMPELQSFDDIAYIRKTLALDKTEQEALEYFTKQMNDAHHGGWTTKMDWIFHTIKQHALN

Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform (PI3-kinase subunit alpha) (PI3K-alpha) (PI3Kalpha) (PtdIns-3-kinase subunit alpha) (EC 2.7.1.137) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha) (PtdIns-3-kinase subunit p110-alpha) (p110alpha) (Phosphoinositide-3-kinase catalytic alpha polypeptide) (Serine/threonine protein kinase PIK3CA) (EC 2.7.11.1)

Rattus norvegicus (Rat)

10,116

1,068

124,354

Angiogenesis;ATP-binding;Kinase;Nucleotide-binding;Phagocytosis;Proto-oncogene;Reference proteome;Serine/threonine-protein kinase;Transferase

GO:0001525; GO:0001889; GO:0004674; GO:0005524; GO:0005737; GO:0005829; GO:0005886; GO:0005942; GO:0005943; GO:0005944; GO:0006006; GO:0006909; GO:0008286; GO:0010468; GO:0010629; GO:0014704; GO:0014823; GO:0014870; GO:0016303; GO:0016477; GO:0030027; GO:0030036; GO:0030295; GO:0030835; GO:0032869; GO:0035005; GO:0035994; GO:0036092; GO:0038084; GO:0040014; GO:0043201; GO:0043457; GO:0043491; GO:0043524; GO:0043560; GO:0046854; GO:0046934; GO:0048009; GO:0048015; GO:0048661; GO:0051897; GO:0055119; GO:0060612; GO:0071333; GO:0071464; GO:0071548; GO:0086003; GO:0097009; GO:0106310; GO:0110053; GO:0141068; GO:1903544; GO:1905477; GO:2000270; GO:2000811

Evidence at protein level

5

null

PF00454;PF00792;PF02192;PF00794;PF00613;

IPR016024;IPR035892;IPR011009;IPR000403;IPR036940;IPR018936;IPR002420;IPR003113;IPR001263;IPR042236;IPR000341;IPR037704;IPR015433;IPR029071;

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)

Pik3ca

false

137

A0A0G2KQY6

MTLRRASGCRQLTLTIGLALTLGLLQWPIGDVRGQDGASPAQVLQELLTRYGDNASISVPQLRSLLVRLNGGQSEDHDSKTQPTRTNASKCLAADTLAVYGMSEQSRIDERGLQQICPTMIQQLDSQACKTQPNQESESSPRPTEAEVWGYGLLCVTVISLCSLVGASVVPFMRKTFYKRLLLYFIALAIGTLYSNALFQLIPEAFGFDPMEDYYVPKSAVVFGGFYLFFFTEKILKMILKPKDTGGHGHGHSHFPAERYANSNGDLEDGVMEKLQNGEAGGAALPRAEADGRGVGEDDKMLSTGQTVQDTQSSGGGGTGGCYWLKGRAYSDIGTLAWMITLSDGLHNFIDGLAIGASFTASVFQGISTSVAILCEEFPHELGDFVILLNAGMSIQQALFFNFLSACCCYLGMGFGILAGNNFSPNWIFALAGGMFLYIALADMFPEMNEVSREEEEAGGSGFLLTFALQNAGLLTGFAIMLVLTIYSGQIQLG

Metal cation symporter ZIP14 (Solute carrier family 39 member 14) (Zrt- and Irt-like protein 14) (ZIP-14)

Danio rerio (Zebrafish) (Brachydanio rerio)

7,955

494

53,266

Cell membrane;Endosome;Ion transport;Lysosome;Membrane;Reference proteome;Signal;Transmembrane;Transmembrane helix;Transport;Zinc;Zinc transport

GO:0005381; GO:0005384; GO:0005385; GO:0005765; GO:0005886; GO:0006829; GO:0006882; GO:0015086; GO:0015296; GO:0016323; GO:0016324; GO:0030003; GO:0031901; GO:0031902; GO:0032869; GO:0033212; GO:0034755; GO:0045745; GO:0055071; GO:0071333; GO:0071421; GO:0071577; GO:0071578; GO:0098662; GO:0098739; GO:0140410

Evidence at transcript level

5

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27231142}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}.

SIGNAL 1..34; /evidence="ECO:0000255"

TRANSMEM 153..173; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 182..202; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 220..240; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 398..418; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 427..447; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 463..483; /note="Helical"; /evidence="ECO:0000255"

PF02535;

IPR003689;IPR050799;

null

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

slc39a14 zip14

false

138

A0A0G2KTI4

MSASPPISAGDYLSAPEPDALKPAGPTPSQSRFQVDLVTESAGDGETTVGFDSSPPEYVAEPPPDGLRDSVSGGEEAKGRFRVVNFAASSPDAAPAETAQNGDTVMSEGSLHSSTGGQQHHHYDTHTNTYYLRTFGHNTIDAVPKIDFYRQTAAPLGEKLIRPTLSELHDELDKEPFEDGFANGEELTPAEESAAKDVSESKGVVKFGWIKGVLVRCMLNIWGVMLFIRMTWIVGQAGIAYSCIIVIMATVVTTITGCSTSAIATNGFVRGGGAYYLISRSLGPEFGGSIGLIFAFANAVAVAMYVVGFAETVVELLMDSGLLMIDQTNDIRVIGTITVILLLGISVAGMEWEAKAQIFLLVILITAIFNYFIGSFIAVDSKKKFGFFSYDAGILAENFGPDFRGQTFFSVFSIFFPAATGILAGANISGDLADPQMAIPKGTLLAILITGLVYVGVAISAGACIVRDATGIESNFTLISNCTDAACKYGYDFSSCRPTVEGEVSSCKFGLHNDFQVMSVVSGFSPLISAGIFSATLSSALASLVSAPKVFQALCKDNIYPGIAIFGKGYGKNNEPLRGYFLTFGIALAFILIAELNVIAPIISNFFLASYALINFSVFHASLANSPGWRPSFKYYNMWASLAGAILCCVVMFIINWWAALLTNVIVLSLYIYVSYKKPDVNWGSSTQALTYHQALTHSLQLCGVADHIKTFRPQCLVMTGAPNSRPAILHLVHAFTKNVGLMLCGHVRISSRRPNFKELNSDMLRYQRWLLNNNSKAFYTCVVAEDLRQGTQYMLQAAGLGRLRPNTLVIGFKNDWRTGDIKEVETYINLIHDAFDFQYGVVILRLREGLDISHIQGQDDSSGMKDVVVSVDISKDSDGDSSKPSSKATSVQNSPAVQKDEDDDGKAHTQPLLKKDKKSPTVPLNVADQRLLDASQQFQQKQGKGTVDVWWLFDDGGLTLLIPYLIANKKKWKDCKIRVFIGGKINRIDHDRRAMATLLSKFRIDFSDITVLGDINTKPKSEGLTEFAEMIEPYKLREDDMEQEAAEKLKSEEPWRITDNELELYKAKGNRQIRLNELLKEHSSTANLIVMSMPLARKGAVSSALYMAWLDTLSKDLPPILLVRGNHQSVLTFYS

Solute carrier family 12 member 2 (Bumetanide-sensitive sodium-(potassium)-chloride cotransporter 2) (BSC2) (Na-K-Cl cotransporter 1) (NKCC1)

Danio rerio (Zebrafish) (Brachydanio rerio)

7,955

1,136

124,112

3D-structure;Alternative splicing;Cell membrane;Chloride;Disulfide bond;Glycoprotein;Ion transport;Membrane;Metal-binding;Phosphoprotein;Potassium;Potassium transport;Reference proteome;Sodium;Sodium transport;Symport;Transmembrane;Transmembrane helix;Transport

GO:0006884; GO:0008511; GO:0008519; GO:0015377; GO:0016323; GO:0016324; GO:0035725; GO:0042472; GO:0042802; GO:0043583; GO:0046872; GO:0048798; GO:0055064; GO:0055075; GO:0055078; GO:0072488; GO:1902476; GO:1990573

Evidence at protein level

5

SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:19633174, ECO:0000305|PubMed:31367042}; Multi-pass membrane protein {ECO:0000305|PubMed:31367042}.

null

TRANSMEM 209..234; /note="Discontinuously helical; Name=1"; /evidence="ECO:0000269|PubMed:31367042, ECO:0007744|PDB:6NPL"; TRANSMEM 239..261; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:31367042, ECO:0007744|PDB:6NPL"; TRANSMEM 286..314; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:31367042, ECO:0007744|PDB:6NPL"; TRANSMEM 328..351; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:31367042, ECO:0007744|PDB:6NPL"; TRANSMEM 352..376; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:31367042, ECO:0007744|PDB:6NPL"; TRANSMEM 408..427; /note="Discontinuously helical; Name=6"; /evidence="ECO:0000269|PubMed:31367042, ECO:0007744|PDB:6NPL"; TRANSMEM 439..462; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:31367042, ECO:0007744|PDB:6NPL"; TRANSMEM 524..551; /note="Helical; Name=8"; /evidence="ECO:0000269|PubMed:31367042, ECO:0007744|PDB:6NPL"; TRANSMEM 577..595; /note="Helical; Name=9"; /evidence="ECO:0000269|PubMed:31367042, ECO:0007744|PDB:6NPL"; TRANSMEM 596..619; /note="Helical; Name=10"; /evidence="ECO:0000269|PubMed:31367042, ECO:0007744|PDB:6NPL"; TRANSMEM 637..656; /note="Helical; Name=11"; /evidence="ECO:0000269|PubMed:31367042, ECO:0007744|PDB:6NPL"; TRANSMEM 657..672; /note="Helical; Name=12"; /evidence="ECO:0000269|PubMed:31367042, ECO:0007744|PDB:6NPL"

PF00324;PF08403;PF03522;

IPR004841;IPR013612;IPR002444;IPR018491;IPR002443;IPR004842;

6NPH;6NPJ;6NPK;6NPL;

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

slc12a2 nkcc1

false

139

A0A0G2L7I0

MMEDEDFLLALRLQEQFDQETPAAGWPDEDCPSSKRRRVDPSGGLDVIPFTQPRAERPLSIVDESWETLDPNPDVRAMFLQFNDKFFWGKLSGVEVKWSPRMTLCAGVCSYEGRGGLCSIRLSEPLLKLRPRKDLVQTLLHEMIHALLFVTQNNRDRDGHGPEFCKHMNRINQASGTNITIYHSFHDEVDVYRQHWWRCNGPCQNRRPFFGYVKRAMNRPPSARDPWWADHQRSCGGTYTKIKEPENYGKTGKSDKQRDKMPATEMPKKSKPPSSTSSSGSQDIRNIIPFSGRGFVLGGNAQIPTNKQIQSPPKAPPEPLHSPPDSPLLPRLQLNEDNLKRLSSGTSNIPRKRSVGNTNAFINVNGSPVRISNGNGSGGKQRSVRDLFQAIVLKSPDRGASAVGSSKSSTDASTADYRSNSALDAKPSGKTSLITDHLSYTISGPKTLSAESNISKYFGGSAKTDVQDSKLKTFGSPQKSAIGTPGYVSKAFGSNQRPDSTSSGIRNTGSPQRSHASATSGSSFKHFRGPAKPESNFPSPRNIGSPRTSGTTPSGAKKRSWEEHNSERVFDYFQRTVGESATSTDKKREEVRSEAPPPVRDQQANNPPAQITVHCPVCHIRLPESTINDHLDSCLL

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

Danio rerio (Zebrafish) (Brachydanio rerio)

7,955

636

70,224

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

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

Inferred from homology

5

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H040}. Chromosome {ECO:0000250|UniProtKB:A0A1L8G2K9}. Note=Localizes to sites of UV damage via the PIP-box. Recruited to stalled replication forks at sites of replication stress. {ECO:0000250|UniProtKB:Q9H040}.

null

PF10263;PF22934;

IPR006642;IPR044245;IPR006640;IPR055220;

null

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

sprtn

false

140

A0A0G2Q9D6

MGKNEARRSALAPDHGTVVCDPLRRLNRMHATPEESIRIVAAQKKKAQDEYGAASITILEGLEAVRKRPGMYIGSTGERGLHHLIWEVVDNAVDEAMAGYATTVNVVLLEDGGVEVADDGRGIPVATHASGIPTVDVVMTQLHAGGKFDSDAYAISGGLHGVGVSVVNALSTRLEVEIKRDGYEWSQVYEKSEPLGLKQGAPTKKTGSTVRFWADPAVFETTEYDFETVARRLQEMAFLNKGLTINLTDERVTQDEVVDEVVSDVAEAPKSASERAAESTAPHKVKSRTFHYPGGLVDFVKHINRTKNAIHSSIVDFSGKGTGHEVEIAMQWNAGYSESVHTFANTINTHEGGTHEEGFRSALTSVVNKYAKDRKLLKDKDPNLTGDDIREGLAAVISVKVSEPQFEGQTKTKLGNTEVKSFVQKVCNEQLTHWFEANPTDSKVVVNKAVSSAQARIAARKARELVRRKSATDIGGLPGKLADCRSTDPRKSELYVVEGDSAGGSAKSGRDSMFQAILPLRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDIGKLRYHKIVLMADADVDGQHISTLLLTLLFRFMRPLIENGHVFLAQPPLYKLKWQRSDPEFAYSDRERDGLLEAGLKAGKKINKEDGIQRYKGLGEMDAKELWETTMDPSVRVLRQVTLDDAAAADELFSILMGEDVDARRSFITRNAKDVRFLDV

DNA gyrase subunit B (EC 5.6.2.2)

Mycobacterium bovis (strain BCG / Pasteur 1173P2)

410,289

714

78,456

ATP-binding;Cytoplasm;DNA-binding;Isomerase;Magnesium;Metal-binding;Nucleotide-binding;Topoisomerase

GO:0003677; GO:0005524; GO:0005694; GO:0005737; GO:0006261; GO:0006265; GO:0034335; GO:0046872

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01898}.

null

PF00204;PF00986;PF02518;PF01751;

IPR002288;IPR011557;IPR036890;IPR020568;IPR014721;IPR001241;IPR013760;IPR000565;IPR013759;IPR013506;IPR018522;IPR006171;IPR034160;

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), Mycobacterium bovis (biotype), Mycobacterium tuberculosis variant bovis BCG (no rank)

gyrB1 BCG_0005; gyrB2 BCG_0035

false

141

A0A0G2Q9F8

MTDTTLPPDDSLDRIEPVDIQQEMQRSYIDYAMSVIVGRALPEVRDGLKPVHRRVLYAMFDSGFRPDRSHAKSARSVAETMGNYHPHGDASIYDTLVRMAQPWSLRYPLVDGQGNFGSPGNDPPAAMRYTEARLTPLAMEMLREIDEETVDFIPNYDGRVQEPTVLPSRFPNLLANGSGGIAVGMATNIPPHNLRELADAVFWALENHDADEEETLAAVMGRVKGPDFPTAGLIVGSQGTADAYKTGRGSIRMRGVVEVEEDSRGRTSLVITELPYQVNHDNFITSIAEQVRDGKLAGISNIEDQSSDRVGLRIVIEIKRDAVAKVVINNLYKHTQLQTSFGANMLAIVDGVPRTLRLDQLIRYYVDHQLDVIVRRTTYRLRKANERAHILRGLVKALDALDEVIALIRASETVDIARAGLIELLDIDEIQAQAILDMQLRRLAALERQRIIDDLAKIEAEIADLEDILAKPERQRGIVRDELAEIVDRHGDDRRTRIIAADGDVSDEDLIAREDVVVTITETGYAKRTKTDLYRSQKRGGKGVQGAGLKQDDIVAHFFVCSTHDLILFFTTQGRVYRAKAYDLPEASRTARGQHVANLLAFQPEERIAQVIQIRGYTDAPYLVLATRNGLVKKSKLTDFDSNRSGGIVAVNLRDNDELVGAVLCSADDDLLLVSANGQSIRFSATDEALRPMGRATSGVQGMRFNIDDRLLSLNVVREGTYLLVATSGGYAKRTAIEEYPVQGRGGKGVLTVMYDRRRGRLVGALIVDDDSELYAVTSGGGVIRTAARQVRKAGRQTKGVRLMNLGEGDTLLAIARNAEESGDDNAVDANGADQTGN

DNA gyrase subunit A (EC 5.6.2.2)

Mycobacterium bovis (strain BCG / Pasteur 1173P2)

410,289

838

92,345

Antibiotic resistance;ATP-binding;Cytoplasm;DNA-binding;Isomerase;Nucleotide-binding;Topoisomerase

GO:0003677; GO:0005524; GO:0005694; GO:0005737; GO:0006261; GO:0006265; GO:0009330; GO:0034335; GO:0046677

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897}.

null

PF03989;PF00521;

IPR005743;IPR006691;IPR035516;IPR013760;IPR013758;IPR013757;IPR002205;IPR050220;

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), Mycobacterium bovis (biotype), Mycobacterium tuberculosis variant bovis BCG (no rank)

gyrA1 BCG_0006; gyrA2 BCG_0036

false

142

A0A0G2QC33

MDAATLTYDTLRFAEFEDFPETSEPVWILGRKYSIFTEKDEILSDVASRLWFTYRRNFPAIGGTGPTSDTGWGCMLRCGQMIFAQALVCRHLGRDWRWTQRKRQPDSYFSVLNAFLDRKDSYYSIHQIAQMGVGEGKSIGQWYGPNTVAQVLKKLAVFDTWSSLAVHIAMDNTVVMEEIRRLCRASLPCAGAAALSMESERHCNGLPAGAEVTNRPLAWRPLVLLIPLRLGLTDINEAYVETLKHCFMMPQSLGVIGGKPNSAHYFIGYVGEELIYLDPHTTQPAVELTDSCFIPDESFHCQHPPCRMGIGELDPSIAVGFFCKTEEDFNDWCQQVKKLSQLGGALPMFELVEQQPSHLACQDVLNLSLDSSDVERLERFFDSEDEDFEILSL

Cysteine protease ATG4B (EC 3.4.22.-) (Autophagy-related protein 4 homolog B)

Rattus norvegicus (Rat)

10,116

393

44,364

Acetylation;Alternative splicing;Autophagy;Cytoplasm;Cytoplasmic vesicle;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Isopeptide bond;Mitochondrion;Phosphoprotein;Protease;Protein transport;Reference proteome;S-nitrosylation;Thiol protease;Transport;Ubl conjugation;Ubl conjugation pathway

GO:0000045; GO:0000421; GO:0000423; GO:0004175; GO:0004197; GO:0005737; GO:0005739; GO:0005783; GO:0005829; GO:0006508; GO:0006914; GO:0008233; GO:0008234; GO:0009267; GO:0015031; GO:0016237; GO:0016485; GO:0019786; GO:0031173; GO:0031410; GO:0034497; GO:0034727; GO:0035973; GO:0045732; GO:0097110

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4P1}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y4P1}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q9Y4P1}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y4P1}. Mitochondrion {ECO:0000250|UniProtKB:Q9Y4P1}. Note=Mainly localizes to the cytoplasm, including cytosol. A samll potion localizes to mitochondria; phosphorylation at Ser-34 promotes localization to mitochondria. {ECO:0000250|UniProtKB:Q9Y4P1}.

null

PF20166;PF03416;

IPR046793;IPR038765;IPR005078;IPR046792;

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)

Atg4b

false

143

A0A0G2UGT2

MTTFLIKHKASGKYFHPKGGTSNPPNGTNLVLHSDIHERMYFQFEVVNERWRYIKHVASEKIVHPFGGKADPLNGTNMVLHQDRHDRALFAMDFFNDNIRHKGGKYIHPKGGSKNPSNGNLTVMHGDEHGAMEFIFVSPKNKDKRVLVYA

D-galactose-binding lectin (GalNAc/Gal-specific lectin) (MTL)

Mytilus trossulus (Blue mussel)

6,551

150

17,111

Glycoprotein;Hemagglutinin;Lectin

GO:0005534; GO:0016045; GO:0034117; GO:0042834; GO:0045087; GO:0050830; GO:0050832; GO:0051260; GO:0098630; GO:0140460

Evidence at protein level

5

null

cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Spiralia (clade), Lophotrochozoa (clade), Mollusca (phylum), Bivalvia (class), Autobranchia (subclass), Pteriomorphia (clade), Mytilida (order), Mytiloidea (superfamily), Mytilidae (family), Mytilinae (subfamily), Mytilus (genus)

null

false

144

A0A0G4P2K0

MKDMDCIPGPKPLPVVGNLFDLDLDNALQSIIRMADEFGPLFQITINGQKQIFATSQALVDELCDETRFHKAVMGGVEKLRMLAQDGLFTAHHGERGWGIAHRILMPAFGPLRIRDMFEDMSDVAHQLCFKWARQGSSASINIAEDFTRLTLDTIALCTMSFRLNSYYNSETMHPFVQSMLYVLKEADLQATLPGVANCVRVKAQRRMSKHIQAMRNIAGDIIKGRRDKPEPVDDLLNTLLNGRDPVTGEGMSDELIISNIITFLVAGHETTSGLLSFTFYYLLQHPHVLEQARNEVDEVVGVGPITVQHLAKLPYIDAVMKESLRLMPTAPAFTVTPKKPEVVGGKWMVNTGQSVHVLLPVCLRDEAVFGPDAGEFRPTRMLEENFSKLPPNSWKPFGNGERGCIGRAFAWQEAQLVVASVLQTFDLVAEDPYYKLRIKETLTIKPDGFRVRATLRRGQSATALSQHNMSAGATASPGSSTHLAGDENGQDTAGGQPISFFYGSNSGTCKALAHRLASTMMTRGFTDQHLAQLDSAVDNLPRDQPTIIVTTTYDGQPTDDAKKFLAWLESGNVPSLHGVSYAVFGCGHQDWTKTFYRIPILIDDLMHKAGATRLTTRGTANAAVSDLFSDLEVWEETNLLPALREKFYLCNSSDFEPLDPHQLQISISKPARVGMHRDLVEGKVTAIRTLTSPGVPEKRHVEFQIPSEMALRPGDHVNILPVNPPCSVLRALARFSLASDHSITFESSNALDLPQATPVSAAELFSSYLELSQPATRINLKSLASATPSDDDKKELLHFHDSYDSLIRDKRVSVLDLLEHFTSITLPIATFISMLPVLRVRTYSLSMAPSFKPLHCSLTFSVVNEPAWSGNGRYLGVGSNYLASLTPGSILYVSPRPAKDAFHLPTDQSSNPIIMICAGSGLAPFRSFIQDRMAWLQQGKPLAKALLFFGCRGPHLDDLYHDELSEFESAGVVEVRRAYSKVPNHYLAKGCRYAQHRLLTETETIQDMWAHNATLYLCGSANLAKGVKAVLENMLGTLSEERYITEIF

Self-sufficient cytochrome P450 monooxygenase CYP505E4 (Bifunctional cytochrome P450/NADPH--P450 reductase CYP505E4) [Includes: Cytochrome P450 monooxygenase (EC 1.14.14.1); NADPH--cytochrome P450 reductase (EC 1.6.2.4)]

Penicillium camemberti (strain FM 013)

1,429,867

1,049

116,032

Electron transport;FAD;Flavoprotein;FMN;Heme;Iron;Metal-binding;Monooxygenase;NADP;Oxidoreductase;Reference proteome;Transport

GO:0003958; GO:0005506; GO:0005829; GO:0010181; GO:0020037; GO:0043386; GO:0050660; GO:0070330

Evidence at protein level

5

null

PF00667;PF00258;PF00175;PF00067;

IPR023206;IPR003097;IPR001128;IPR017972;IPR002401;IPR036396;IPR017927;IPR008254;IPR029039;IPR039261;IPR023173;IPR001433;IPR017938;

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), Penicillium camembertii (species)

CYP505E4 PCAMFM013_S004g000414

false

145

A0A0H2UNG0

MRKTPSHTEKKMVYSIRSLKNGTGSVLIGASLVLLAMATPTISSDESTPTTNEPNNRNTTTLAQPLTDTAAGSGKNESDISSPGNANASLEKTEEKPAASPADPAPQTGQDRSSEPTTSTSPVTTETKAEEPIEDNYFRIHVKKLPEENKDAQGLWTWDDVEKPSENWPNGALSFKDAKKDDYGYYLDVKLKGEQAKKISFLINNTAGKNLTGDKSVEKLVPKMNEAWLDQDYKVFSYEPQPAGTVRVNYYRTDGNYDKKSLWYWGDVKNPSSAQWPDGTDFTATGKYGRYIDIPLNEAAREFGFLLLDESKQGDDVKIRKENYKFTDLKNHSQIFLKDDDESIYTNPYYVHDIRMTGAQHVGTSSIESSFSTLVGAKKEDILKHSNITNHLGNKVTITDVAIDEAGKKVTYSGDFSDTKHPYTVSYNSDQFTTKTSWRLKDETYSYDGKLGADLKEEGKQVDLTLWSPSADKVSVVVYDKNDPDKVVGTVALEKGERGTWKQTLDSTNKLGITDFTGYYYQYQIERQGKTVLALDPYAKSLAAWNSDDSKIDDAHKVAKAAFVDPAKLGPQDLTYGKIHNFKTREDAVIYEAHVRDFTSDPAIAKDLTKPFGTFEAFIEKLDYLKDLGVTHIQLLPVLSYYFVNELKNHERLSDYASSNSNYNWGYDPQNYFSLTGMYSSDPKNPEKRIAEFKNLINEIHKRGMGAILDVVYNHTAKVDLFEDLEPNYYHFMDADGTPRTSFGGGRLGTTHHMTKRLLIDSIKYLVDTYKVDGFRFDMMGDHDAASIEEAYKAARALNPNLIMLGEGWRTYAGDENMPTKAADQDWMKHTDTVAVFSDDIRNNLKSGYPNEGQPAFITGGKRDVNTIFKNLIAQPTNFEADSPGDVIQYIAAHDNLTLFDIIAQSIKKDPSKAENYAEIHRRLRLGNLMVLTAQGTPFIHSGQEYGRTKQFRDPAYKTPVAEDKVPNKSHLLRDKDGNPFDYPYFIHDSYDSSDAVNKFDWTKATDGKAYPENVKSRDYMKGLIALRQSTDAFRLKSLQDIKDRVHLITVPGQNGVEKEDVVIGYQITAPNGDIYAVFVNADEKAREFNLGTAFAHLRNAEVLADENQAGPVGIANPKGLEWTEKGLKLNALTATVLRVSQNGTSHESTAEEKPDSTPSKPEHQNEASHPAHQDPAPEARPDSTKPDAKVADAENKPSQATADSQAEQPAQEAQASSVKEAVRNESVENSSKENIPATPDKQAELPNTGIKNENKLLFAGISLLALLGLGFLLKNKKEN

Pullulanase A (EC 3.2.1.41) (Alpha-dextrin endo-1,6-alpha-glucosidase) (Pullulan 6-glucanohydrolase)

Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)

170,187

1,280

142,619

3D-structure;Calcium;Cell wall;Glycosidase;Hydrolase;Metal-binding;Peptidoglycan-anchor;Reference proteome;Secreted;Signal;Virulence

GO:0005509; GO:0005576; GO:0009986; GO:0010303; GO:0030247; GO:0030979; GO:0051060; GO:2001066; GO:2001067; GO:2001069

Evidence at protein level

5

SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}. Cell surface {ECO:0000250|UniProtKB:Q9F930}. Note=Localizes to cytoplasm in the lung alveolar type II cells of the mouse and human hosts. {ECO:0000269|PubMed:17187076, ECO:0000269|PubMed:21565699}.

SIGNAL 1..44; /evidence="ECO:0000255"

null

PF00128;PF02922;PF00746;PF03714;PF18033;PF04650;

IPR013784;IPR005323;IPR014755;IPR006047;IPR004193;IPR013780;IPR017853;IPR013783;IPR014756;IPR019931;IPR011838;IPR040806;IPR005877;

2J44;2YA0;2YA1;2YA2;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pneumoniae (species)

spuA SP_0268

false

146

A0A0H2URG7

MTIYNINLGIGWASSGVEYAQAYRAGVFRKLNLSSKFIFTDMILADNIQHLTANIGFDDNQVIWLYNHFTDIKIAPTSVTVDDVLAYFGGEESHREKNGKVLRVFFFDQDKFVTCYLVDENKDLVQHAEYVFKGNLIRKDYFSYTRYCSEYFAPKDNVAVLYQRTFYNEDGTPVYDILMNQGKEEVYHFKDKIFYGKQAFVRAFMKSLNLNKSDLVILDRETGIGQVVFEEAQTAHLAVVVHAEHYSENATNEDYILWNNYYDYQFTNADKVDFFIVSTDRQNEVLQEQFAKYTQHQPKIVTIPVGSIDSLTDSSQGRKPFSLITASRLAKEKHIDWLVKAVIEAHKELPELTFDIYGSGGEDSLLREIIANHQAEDYIQLKGHAELSQIYSQYEVYLTASTSEGFGLTLMEAIGSGLPLIGFDVPYGNQTFIEDGQNGYLIPSSSDHVEDQIKQAYAAKICQLYQENRLEAMRAYSYQIAEGFLTKEILEKWKKTVEEVLHD

UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit (EC 2.4.1.-) (Glycosyltransferase GtfA) (O-linked N-acetyl-D-glucosamine (O-GlcNAc) transferase)

Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)

170,187

503

57,782

3D-structure;Cell membrane;Cytoplasm;Glycosyltransferase;Membrane;Nucleotide-binding;Reference proteome;Transferase

GO:0000166; GO:0005737; GO:0005886; GO:0016757; GO:0017122; GO:0018242

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01472}. Cell membrane {ECO:0000250|UniProtKB:A1C3L9, ECO:0000255|HAMAP-Rule:MF_01472}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01472}. Note=Cell membrane association requires GtfB. {ECO:0000250|UniProtKB:A1C3L9, ECO:0000255|HAMAP-Rule:MF_01472}.

null

PF13692;PF22145;

IPR014267;IPR054396;

4PQG;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pneumoniae (species)

gtfA SP_1758

false

147

A0A0H2URJ6

MRNTKRAVVFAGDYAYIRQIETAMKSLCRHNSHLKIYLLNQDIPQEWFSQIRIYLQEMGGDLIDCKLIGSQFQMNWSNKLPHINHMTFARYFIPDFVTEDKVLYLDSDLIVTGDLTDLFELDLGENYLAAARSCFGAGVGFNAGVLLINNKKWGSETIRQKLIDLTEKEHENVEEGDQSILNMLFKDQYSSLEDQYNFQIGYDYGAATFKHQFIFDIPLEPLPLILHYISQDKPWNQFSVGRLREVWWEYSLMDWSVILNEWFSKSVKYPSKSQIFKLQCVNLTNSWCVEKIDYLAEQLPEVHFHIVAYTNMANELLALTRFPNVTVYPNSLPMLLEQIVIASDLYLDLNHDRKLEDAYEFVLKYKKPMIAFDNTCSENLSEISYEGIYPSSIPKKMVAAIRSYMR

Glycosyltransferase GlyE (PsrP glycosyltransferase GlyE)

Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)

170,187

406

47,412

3D-structure;Glycosyltransferase;Manganese;Metal-binding;Nucleotide-binding;Reference proteome;Transferase

GO:0000166; GO:0006486; GO:0016757; GO:0046872

Evidence at protein level

5

null

PF01501;

IPR002495;IPR050748;IPR029044;

5GVV;5GVW;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pneumoniae (species)

glyE SP_1766

false

148

A0A0H2URK1

MTETVEDKVSHSITGLDILKGIVAAGAVISGTVATQTKVFTNESAVLEKTVEKTDALATNDTVVLGTISTSNSASSTSLSASESASTSASESASTSASTSASTSASESASTSASTSISASSTVVGSQTAAATEATAKKVEEDRKKPASDYVASVTNVNLQSYAKRRKRSVDSIEQLLASIKNAAVFSGNTIVNGAPAINASLNIAKSETKVYTGEGVDSVYRVPIYYKLKVTNDGSKLTFTYTVTYVNPKTNDLGNISSMRPGYSIYNSGTSTQTMLTLGSDLGKPSGVKNYITDKNGRQVLSYNTSTMTTQGSGYTWGNGAQMNGFFAKKGYGLTSSWTVPITGTDTSFTFTPYAARTDRIGINYFNGGGKVVESSTTSQSLSQSKSLSVSASQSASASASTSASASASTSASASASTSASASASTSASVSASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASESASTSASASASTSASESASTSASASASTSASASASTSASGSASTSTSASASTSASASASTSASASASISASESASTSASESASTSTSASASTSASESASTSASASASTSASASASTSASASASTSASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASVSASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASISASESASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASESASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASTSASESASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASISASESASTSASASASTSASVSASTSASASASTSASESASTSASASASTSASESASTSASASASTSASASASISASESASTSASASASTSASASASTSASASASTSASESASTSTSASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASVSASTSASESASTSASASASTSASASASTSASESASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASISASESASTSASASASTSASASASTSASVSASTSASASASTSASASASISASESASTSASASASTSASASASTSASASASTSASASASISASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASVSASTSASESASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASASTSASASASTSASASASTSASASASISASESASTSASESASTSTSASASTSASESASTSASASASTSASASASTSASASASTSASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASVSASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASISASESASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASESASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASTSASESASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASISASESASTSASASASTSASVSASTSASASASTSASESASTSASASASTSASESASTSASASASTSASASASISASESASTSASASASTSASASASTSASASASTSASESASTSTSASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASVSASTSASESASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASASTSASASASTSASASASTSASASASISASESASTSASASASASTSASASASTSASASASTSASASASISASESASTSASESASTSTSASASTSASESASTSASASASTSASASASTSASASASTSASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASVSASTSASASASTSASASASTSASESASTSASASTSASESASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASESASTSASASASTSASESASTSASASASTSASASASTSASGSASTSTSASASTSASASASTSASASASISASESASTSASESASTSTSASASTSASESASTSASASASTSASASASTSASASASTSASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASVSASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASISASESASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASESASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASTSASESASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASISASESASTSASASASTSASVSASTSASASASTSASESASTSASASASTSASESASTSASASASTSASASASISASESASTSASASASTSASASASTSASASASTSASESASTSTSASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASVSASTSASESASTSASASASTSASASASTSASESASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASISASESASTSASASASTSASASASTSASVSASTSASASASTSASASASISASESASTSASASASTSASASASTSASASASTSASASASISASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASISASESASTSASASASTSASASASTSASASASTSASESASTSTSASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASVSASTSASESASTSASASASTSASASASTSASESASTSASASASTSASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASISASESASTSASASASTSASASASTSASVSASTSASASASTSASASASISASESASTSASASASTSASASASTSASASASTSASASASISASESASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSASASASTSVSNSANHSNSQVGNTSGSTGKSQKELPNTGTESSIGSVLLGVLAAVTGIGLVAKRRKRDEEE

Pneumococcal serine-rich repeat protein (PsrP) (Adhesin PsrP) (Serine-rich repeat protein PsrP)

Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)

170,187

4,776

412,239

3D-structure;Cell adhesion;Cell wall;DNA-binding;Glycoprotein;Peptidoglycan-anchor;Reference proteome;Repeat;Secreted;Signal;Virulence

GO:0003677; GO:0005576; GO:0007155; GO:0009275; GO:0009986; GO:0044010; GO:0052031

Evidence at protein level

5

SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000269|PubMed:19627498}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}. Cell surface {ECO:0000269|PubMed:19627498}.

SIGNAL 1..72; /evidence="ECO:0000305|PubMed:16861665"

null

PF00746;

IPR050252;IPR019931;IPR026465;

3ZGH;3ZGI;5JUI;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pneumoniae (species)

psrP SP_1772

false

149

A0A0H2URU9

MKKMMTFLKKAKVKAFTLVEMLVVLLIISVLFLLFVPNLTKQKEAVNDKGKAAVVKVVESQAELYSLEKNEDASLRKLQADGRITEEQAKAYKEYNDKNGGANRKVND

Competence protein ComGC (Major pilin ComGC)

Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)

170,187

108

12,177

3D-structure;Cell membrane;Competence;Fimbrium;Membrane;Methylation;Reference proteome;Secreted;Signal;Transmembrane;Transmembrane helix

GO:0005576; GO:0005886; GO:0009289; GO:0009986; GO:0015627; GO:0015628; GO:0030420

Evidence at protein level

5

SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P25955}; Single-pass membrane protein {ECO:0000250|UniProtKB:P25955, ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:P25955}. Fimbrium {ECO:0000250|UniProtKB:Q8DN88}. Secreted {ECO:0000269|PubMed:24550320}. Note=The unprocessed form is an integral membrane protein with its C-terminus outside the membrane. Upon cleavage, it is translocated to the outer face of the membrane (By similarity). ComGC release into culture supernatant is probably physiological because it is still observed in an autolysis-deficient lytA mutant background (PubMed:24550320). {ECO:0000250|UniProtKB:P25955, ECO:0000269|PubMed:24550320}.

SIGNAL 1..13; /evidence="ECO:0000255"

TRANSMEM 16..36; /note="Helical"; /evidence="ECO:0000255"

PF07963;

IPR000983;IPR016940;IPR012902;IPR045584;

5NCA;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pneumoniae (species)

comGC cglC SP_2051

false

150

A0A0H2USC0

MIKSTNIQVIGSGIMHQINNIHSLTLFSLPVSLSPSCNEYYLKVWSEWERNGTPGEQRNIAFNRLKICLQNQEAELNLSELDLKTLPDLPPQITTLEIRKNLLTHLPDLPPMLKVIHAQFNQLESLPALPETLEELNAGDNKIKELPFLPENLTHLRVHNNRLHILPLLPPELKLLVVSGNRLDSIPPFPDKLEGLALANNFIEQLPELPFSMNRAVLMNNNLTTLPESVLRLAQNAFVNVAGNPLSGHTMRTLQQITTGPDYSGPQIFFSMGNSATISAPEHSLADAVTAWFPENKQSDVSQIWHAFEHEEHANTFSAFLDRLSDTVSARNTSGFREQVAAWLEKLSASAELRQQSFAVAADATESCEDRVALTWNNLRKTLLVHQASEGLFDNDTGALLSLGREMFRLEILEDIARDKVRTLHFVDEIEVYLAFQTMLAEKLQLSTAVKEMRFYGVSGVTANDLRTAEAMVRSREENEFTDWFSLWGPWHAVLKRTEADRWAQAEEQKYEMLENEYSQRVADRLKASGLSGDADAEREAGAQVMRETEQQIYRQLTDEVLA

E3 ubiquitin-protein ligase IpaH2.5 (EC 2.3.2.27) (Invasion plasmid antigen 2.5)

Shigella flexneri

623

563

63,587

3D-structure;Host cytoplasm;Leucine-rich repeat;Plasmid;Reference proteome;Repeat;Secreted;Transferase;Ubl conjugation;Ubl conjugation pathway;Virulence

GO:0005576; GO:0016567; GO:0030430; GO:0061630; GO:0090729

Evidence at protein level

5

SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8VSC3}. Host cytoplasm {ECO:0000250|UniProtKB:Q8VSC3}. Note=Secreted via Mxi-Spa type III secretion system (T3SS), and delivered into the host cytoplasm. {ECO:0000250|UniProtKB:Q8VSC3}.

null

PF12468;PF14496;

IPR001611;IPR051071;IPR032675;IPR032674;IPR029487;

7YA8;

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Shigella (genus)

ipaH2.5 CP0054 SF_p0054

false

151

A0A0H2USG1

MIKSTNIQAIGSGIMHQINNVYSLTPLSLPMELTPSCNEFYLKTWSEWEKNGTPGEQRNIAFNRLKICLQNQEAELNLSELDLKTLPDLPPQITTLEIRKNLLTHLPDLPPMLKVIHAQFNQLESLPALPETLEELNAGDNKIKELPFLPENLTHLRVHNNRLHILPLLPPELKLLVVSGNRLDSIPPFPDKLEGLALANNFIEQLPELPFSMNRAVLMNNNLTTLPESVLRLAQNAFVNVAGNPLSGHTMRTLQQITTGPDYSGPQIFFSMGNSATISAPEHSLADAVTAWFPENKQSDVSQIWHAFEHEEHANTFSAFLDRLSDTVSARNTSGFREQVAAWLEKLSASAELRQQSFAVAADATESCEDRVALTWNNLRKTLLVHQASEGLFDNDTGALLSLGREMFRLEILEDIARDKVRTLHFVDEIEVYLAFQTMLAEKLQLSTAVKEMRFYGVSGVTANDLRTAEAMVRSREENEFTDWFSLWGPWHAVLKRTEADRWAQAEEQKYEMLENEYSQRVADRLKASGLSGDADAEREAGAQVMRETEQQIYRQLTDEVLALRLSENGSNHIA

E3 ubiquitin-protein ligase IpaH1.4 (EC 2.3.2.27) (Invasion plasmid antigen 1.4)

Shigella flexneri

623

575

64,859

3D-structure;Host cytoplasm;Leucine-rich repeat;Plasmid;Reference proteome;Repeat;Secreted;Transferase;Ubl conjugation;Ubl conjugation pathway;Virulence

GO:0005576; GO:0016567; GO:0030430; GO:0061630; GO:0085034; GO:0090729

Evidence at protein level

5

SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8VSC3}. Host cytoplasm {ECO:0000250|UniProtKB:Q8VSC3}. Note=Secreted via Mxi-Spa type III secretion system (T3SS), and delivered into the host cytoplasm. {ECO:0000250|UniProtKB:Q8VSC3}.

null

PF12468;PF14496;

IPR001611;IPR051071;IPR032675;IPR032674;IPR029487;

3CKD;7V8E;7V8G;7V8H;7YA7;

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Shigella (genus)

ipaH1.4 CP0265 SF_p0265

false

152

A0A0H2V871

MYAREYRSTRPHKAIFFHLSCLTLICSAQVYAKPDMRPLGPNIADKGSVFYHFSATSFDSVDGTRHYRVWTAVPNTTAPASGYPILYMLDGNAVMDRLDDELLKQLSEKTPPVIVAVGYQTNLPFDLNSRAYDYTPAAESRKTDLHSGRFSRKSGGSNNFRQLLETRIAPKVEQGLNIDRQRRGLWGHSYGGLFVLDSWLSSSYFRSYYSASPSLGRGYDALLSRVTAVEPLQFCTKHLAIMEGSATQGDNRETHAVGVLSKIHTTLTILKDKGVNAVFWDFPNLGHGPMFNASFRQALLDISGENANYTAGCHELSH

Apo-salmochelin esterase (EC 3.1.1.107) (Enterobactin hydrolase IroE)

Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)

199,310

318

35,444

3D-structure;Cell inner membrane;Cell membrane;Hydrolase;Membrane;Reference proteome;Serine esterase;Transmembrane;Transmembrane helix

GO:0005886; GO:0052689

Evidence at protein level

5

SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:16076215}; Single-pass membrane protein {ECO:0000255}; Periplasmic side {ECO:0000305|PubMed:16076215}.

null

TRANSMEM 13..32; /note="Helical"; /evidence="ECO:0000255"

PF00756;

IPR029058;IPR000801;IPR052558;

2GZR;2GZS;

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Escherichia (genus), Escherichia coli (species)

iroE c1251

false

153

A0A0H2V8B5

MIAYENIEFFICLVNVLGNNMYNILFFIFLSIAIPFLLFLAWKQHLKTKEIRSYLLKEGYNIIFNGEGNSYLAFNISNATFRAGNLTSNDYFQASISYIHDYRWEWKEVEAKKINNIFIIYISNIDFPSQKLFYRNNKSLAEIDWAKLQAIFHQPYEIQNDVMQDNNNTHYDFFISHAKEDKDTFVRPLVDELNRLGVIIWYDEQTLEVGDSLRRNIDLGLRKANYGIVILSHNFLNKKWTQYELDSLINRAVYDDNKIILPIWHNINAQEVSKYSHYLADKMALQTSLYSVKEIARELAEIAYRRR

NAD(+) hydrolase TcpC (EC 3.2.2.6) (NADP(+) hydrolase TcpC) (EC 3.2.2.-) (TIR domain-containing protein in E.coli) (tcpC)

Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)

199,310

307

36,426

Hydrolase;Membrane;NAD;Reference proteome;Secreted;Transmembrane;Transmembrane helix;Virulence

GO:0003953; GO:0005576; GO:0007165; GO:0016020; GO:0019677; GO:0034125; GO:0050135; GO:0061809

Evidence at protein level

5

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18327267}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.

null

TRANSMEM 22..42; /note="Helical"; /evidence="ECO:0000255"

PF13676;

IPR000157;IPR035897;

null

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Escherichia (genus), Escherichia coli (species)

TcpC c2398

false

154

A0A0H2VG78

MKANKYLIFILGALGGLLYGYDNGVISGALLFIHKDIPLNSTTEGIVVSSMLIGAIVGAGSSGPLADKLGRRRLVMLIAIVFIIGALILAASTNLALLIIGRLIIGLAVGGSMSTVPVYLSEMAPTEYRGSLGSLNQLMITIGILAAYLVNYAFADIEGWRWMLGLAVVPSVILLVGIYFMPESPRWLLENRNEEAARQVMKITYDDSEIDKELKEMKEINAISESTWTVIKSPWLGRILIVGCIFAIFQQFIGINAVIFYSSSIFAKAGLGEAASILGSVGIGTINVLVTIVAIFVVDKIDRKKLLVGGNIGMIASLLIMAILIWTIGIASSAWIIIVCLSLFIVFFGISWGPVLWVMLPELFPMRARGAATGISALVLNIGTLIVSLFFPILSDALSTEWVFLIFAFIGVLAMIFVIKFLPETRGRSLEEIEYELRERTGARTE

Glucose transporter GlcP (Glucose/H(+) symporter)

Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200)

176,280

446

48,375

3D-structure;Cell membrane;Membrane;Sugar transport;Symport;Transmembrane;Transmembrane helix;Transport

GO:0005886; GO:0015293

Evidence at protein level

5

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24127585}; Multi-pass membrane protein {ECO:0000269|PubMed:24127585}.

null

TRANSMEM 7..31; /note="Helical"; /evidence="ECO:0000305|PubMed:24127585"; TRANSMEM 39..64; /note="Helical"; /evidence="ECO:0000305|PubMed:24127585"; TRANSMEM 71..90; /note="Helical"; /evidence="ECO:0000305|PubMed:24127585"; TRANSMEM 95..122; /note="Helical"; /evidence="ECO:0000305|PubMed:24127585"; TRANSMEM 130..152; /note="Helical"; /evidence="ECO:0000305|PubMed:24127585"; TRANSMEM 155..180; /note="Helical"; /evidence="ECO:0000305|PubMed:24127585"; TRANSMEM 235..269; /note="Helical"; /evidence="ECO:0000305|PubMed:24127585"; TRANSMEM 273..295; /note="Helical"; /evidence="ECO:0000305|PubMed:24127585"; TRANSMEM 304..324; /note="Helical"; /evidence="ECO:0000305|PubMed:24127585"; TRANSMEM 330..363; /note="Helical"; /evidence="ECO:0000305|PubMed:24127585"; TRANSMEM 371..399; /note="Helical"; /evidence="ECO:0000305|PubMed:24127585"; TRANSMEM 402..420; /note="Helical"; /evidence="ECO:0000305|PubMed:24127585"

PF00083;

IPR020846;IPR005828;IPR036259;IPR050814;IPR003663;IPR005829;IPR047984;

4LDS;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Staphylococcaceae (family), Staphylococcus (genus), Staphylococcus epidermidis (species)

glcP SE_0247

false

155

A0A0H2WWV6

MKKIFMMVHELDVNKGGMTSSMFNRSKEFYDADIPADIVTFDYKGNYDEIIKALKKQGKMDRRTKMYNVFEYFKQISNNKHFKSNKLLYKHISERLKNTIEIEESKGISRYFDITTGTYIAYIRKSKSEKVIDFFKDNKRIERFSFIDNKVHMKETFNVDNKVCYQVFYDEKGYPYISRNINANNGAVGKTYVLVNKKEFKNNLALCVYYLEKLIKDSKDSIMICDGPGSFPKMFNTNHKNAQKYGVIHVNHHENFDDTGAFKKSEKYIIENANKINGVIVLTEAQRLDILNQFDVENIFTISNFVKIHNAPKHFQTEKIVGHISRMVPTKRIDLLIEVAELVVKKDNAVKFHIYGEGSVKDKIAKMIEDKNLERNVFLKGYTTTPQKCLEDFKLVVSTSQYEGQGLSMIEAMISKRPVVAFDIKYGPSDFIEDNKNGYLIENHNINDMADKILQLVNNDVLAAEFGSKARENIIEKYSTESILEKWLNLFNS

Poly(ribitol-phosphate) alpha-N-acetylglucosaminyltransferase (EC 2.4.1.70) (WTA GlcNAc-transferase)

Staphylococcus aureus (strain COL)

93,062

493

57,275

3D-structure;Cell wall biogenesis/degradation;Cytoplasm;Glycosyltransferase;Teichoic acid biosynthesis;Transferase

GO:0005737; GO:0019350; GO:0047269; GO:0071555

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:20185825}.

null

PF00534;

IPR001296;

4WAC;4WAD;4X6L;4X7M;4X7P;4X7R;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Staphylococcaceae (family), Staphylococcus (genus), Staphylococcus aureus (species)

tarM SACOL1043

false

156

A0A0H2WZ38

MHELTIYHFMSDKLNLYSDIGNIIALRQRAKKRNIKVNVVEINETEGITFDECDIFFIGGGSDREQALATKELSKIKTPLKEAIEDGMPGLTICGGYQFLGKKYITPDGTELEGLGILDFYTESKTNRLTGDIVIESDTFGTIVGFENHGGRTYHDFGTLGHVTFGYGNNDEDKKEGIHYKNLLGTYLHGPILPKNYEITDYLLEKACERKGIPFEPKEIDNEAEIQAKQVLIDRANRQKKSR

Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD (EC 6.3.5.13) (Lipid II isoglutaminyl synthase glutaminase subunit) (EC 3.5.1.2)

Staphylococcus aureus (strain COL)

93,062

243

27,430

3D-structure;Cell shape;Cell wall biogenesis/degradation;Glutamine amidotransferase;Hydrolase;Ligase;Peptidoglycan synthesis

GO:0004359; GO:0008360; GO:0009236; GO:0009252; GO:0071555; GO:0140282

Evidence at protein level

5

null

PF07685;

IPR029062;IPR033949;IPR011698;IPR043702;

5N9M;7Q8E;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Staphylococcaceae (family), Staphylococcus (genus), Staphylococcus aureus (species)

gatD SACOL1950

false

157

A0A0H2X5R2

MHYLDNLLLNTDSYKASHWLQYPPGTDASFFYVESRGGVYDQTAFFGLQSILKEAINRPVTHADIDDAKALLAAHGEPFNEAGWRDIVDRLGGQLPIRIRAVPEGCVVPTHNVLMTIESTDAKAFWVPSYLETLLLRVWYPVTVATVSWQVKQIVRDFLQRTSDDPEGQLPFKLHDFGARGVSSLGSAALGGAAHLVNFLGTDTLSALLLARAHYHTPVAGYSIPAAEHSTITSWGREREVDAYRNMLTQFARPGAIVAVVSDSYDIYRAIREHWGTTLREEIIASGATVVIRPDSGDPVDVVEQCLLLLDEAFGHQVNGKGYKVLNHVRVIQGDGINPQSLRAILERITAAGYAADNVAFGMGGALLQKVDRDTQKFALKCSAVRVDGAWIDVYKDPITDQGKQSKRGRLTLLRDRATGQYRSALLDEVATHAGDSDDALVTVWENGQMLREWTLEQVRAHADAARL

Nicotinamide phosphoribosyltransferase (NAM phosphoribosyltransferase) (NAMPT) (EC 2.4.2.12)

Xanthomonas campestris pv. campestris (strain 8004)

314,565

468

51,602

3D-structure;Glycosyltransferase;Phosphoprotein;Pyridine nucleotide biosynthesis;Transferase

GO:0009435; GO:0047280

Evidence at protein level

5

null

PF18127;PF04095;

IPR013785;IPR041529;IPR041525;IPR016471;IPR036068;

7YQO;7YQP;7YQQ;7YQR;8IGZ;

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Lysobacterales (order), Lysobacteraceae (family), Xanthomonas (genus), Xanthomonas campestris (species), Xanthomonas campestris pv. campestris (no rank)

XC_0719

false

158

A0A0H2Z7X0

MNRRRRYTGSNPSLRRVLYRAHLGVALVAVFTAGLAVTLVGLLTLRAYADPNQQLIARSISYTVEAAVVFGDAQAAEESLALIASSEEVSSAIVYDRQGQPLASWHRESTGPLHLLEQQLAHWLLSAPTEQPILHDGQKIGSVEVKGSGGSLLRFLLTGFAGMVLCLLLTALGAFYLSRRLVRGIVGPLDQLAKVAHTVRRERDFEKRVPEAGIAELSQLGEDFNALLDELESWQARLQDENASLAHQAHHDSLTSLPNRAFFEGRLSRALRDASEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRESDLVARLGGDEFAVLLAPLASGADALRIADNIIASMQAPIRLSDGSTVSTSLTIGIALYPEHADTPAALLHDADMAMYIAKRQARGSRRLAELNDPRILQEEKEIDSATPEAPPK

Diguanylate cyclase TpbB (EC 2.7.7.65)

Pseudomonas aeruginosa (strain UCBPP-PA14)

208,963

435

47,483

Cell inner membrane;Cell membrane;GTP-binding;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Phosphoprotein;Transferase;Transmembrane;Transmembrane helix

GO:0005525; GO:0005886; GO:0007165; GO:0016740; GO:0046872

Evidence at protein level

5

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

null

TRANSMEM 23..43; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 155..175; /note="Helical"; /evidence="ECO:0000255"

PF17152;PF00990;PF00672;

IPR033417;IPR052163;IPR000160;IPR003660;IPR029787;IPR043128;

null

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Pseudomonadales (order), Pseudomonadaceae (family), Pseudomonas (genus), Pseudomonas aeruginosa group (no rank), Pseudomonas aeruginosa (species)

tpbB yfiN PA14_49890

false

159

A0A0H2ZFK2

MHRSPLAWLRLLLAAVLGAFLLGGPLHAAETAAPRSPAWAQAVDPSINLYRMSPTLYRSALPNAQSVALLQRLQVKTVVSFIKDDDRAWLGQAPVRVVSLPTHADRVDDAEVLSVLRQLQAAEREGPVLMHCKHGNNRTGLFAAMYRIVVQGWDKQAALEEMQRGGFGDEDDMRDASAYVRGADVDGLRLAMANGECSPSRFALCHVREWMAQALDRP

Dual specificity protein phosphatase TpbA (DUSP) (EC 3.1.3.16) (EC 3.1.3.48) (Dual specific tyrosine phosphatase) (Protein tyrosine phosphatase) (Tyrosine phosphatase related to biofilm formation)

Pseudomonas aeruginosa (strain UCBPP-PA14)

208,963

218

23,993

3D-structure;Hydrolase;Periplasm;Protein phosphatase;Signal

GO:0004721; GO:0042597

Evidence at protein level

5

SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:19543378}.

SIGNAL 1..28; /evidence="ECO:0000255"

null

PF03162;

IPR029021;IPR004861;IPR016130;IPR000387;

2M3V;

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Pseudomonadales (order), Pseudomonadaceae (family), Pseudomonas (genus), Pseudomonas aeruginosa group (no rank), Pseudomonas aeruginosa (species)

tpbA PA14_13660

false

160

A0A0H2ZL64

MRKTPSHTEKKMVYSIRSLKNGTGSVLIGASLVLLAMATPTISSDESTPTTNEPNNRNTTTLAQPLTDTAADSGKNESDISSPRNANASLEKTEEKPATEPTTSTSPVTTETKAEEPIEDNYFRIHVKKLPEENKDAQGLWTWDDVEKPSENWPNGALSFKDAKKDDYGYYLDVKLKGEQAKKISFLINNTAGKNLTGDKSVEKLVPKMNEAWLDQDYKVFSYEPQPAGTVRVNYYRTDGNYDKKSLWYWGDVKNPSSAQWPDGTDFTATGKYGRYIDIPLNEAAREFGFLLLDESKQGDDVKIRKENYKFTDLKNHSQIFLKDDDESIYTNPYYVHDIRMTGAQHVGTSSIESSFSTLVGAKKEDILKHSNITNHLGNKVTITDVAIDEAGKKVTYSGDFSDTKHPYTVSYNSDQFTTKTSWHLKDETYSYDGKLGADLKEEGKQVDLTLWSPSADKVSVVVYDKNDPDKVVGTVALEKGERGTWKQTLDSTNKLGITDFTGYYYQYQIERQGKTVLALDPYAKSLAAWNSDDAKIDDAHKVAKAAFVDPAKLGPQDLTYGKIHNFKTREDAVIYEAHVRDFTSDPAIAKDLTKPFGTFEAFIEKLDYLKDLGVTHIQLLPVLSYYFVNELKNHERLSDYASSNSNYNWGYDPQNYFSLTGMYSSDPKNPEKRIAEFKNLINEIHKRGMGAILDVVYNHTAKVDIFEDLEPNYYHFMDADGTPRTSFGGGRLGTTHHMTKRLLVDSIKYLVDTYKVDGFRFDMMGDHDAASIEEAYKAARALNPNLIMLGEGWRTYAGDENMPTKAADQDWMKHTDTVAVFSDDIRNNLKSGYPNEGQPAFITGGKRDVNTIFKNLIAQPTNFEADSPGDVIQYIAAHDNLTLFDIIAQSIKKDPSKAENYAEIHRRLRLGNLMVLTAQGTPFIHSGQEYGRTKQFRDPAYKTPVAEDKVPNKSHLLRDKDGNPFDYPYFIHDSYDSSDAVNKFDWTKATDGKAYPENVKSRDYMKGLIALRQSTDAFRLKSLQDIKDRVHLITVPGQNGVEKEDVVIGYQITAPNGDIYAVFVNADEKAREFNLGTAFAHLRNAEVLADENQAGSVGIANPKGLEWTEKGLKLNALTATVLRVSQNGTSHESTAEEKPDSTPSKPEHQDPAPEARPDSTKPDAKVADAENKPSQATADSQAEQPAQEAQASSVKEAVQNESVENSSKKNIPATPDRQAELPNTGIKNENKLLFAGISLLALLGLGFLLKNKKEN

Pullulanase A (EC 3.2.1.41) (Alpha-dextrin endo-1,6-alpha-glucosidase) (Pullulan 6-glucanohydrolase)

Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)

373,153

1,256

140,279

Calcium;Cell wall;Glycosidase;Hydrolase;Metal-binding;Peptidoglycan-anchor;Reference proteome;Secreted;Signal;Virulence

GO:0005576; GO:0005975; GO:0009986; GO:0030246; GO:0046872; GO:0051060

Inferred from homology

5

SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}. Cell surface {ECO:0000250|UniProtKB:Q9F930}. Note=Localizes to cytoplasm in the lung alveolar type II cells of the mouse and human hosts. {ECO:0000250|UniProtKB:A0A0H2UNG0}.

SIGNAL 1..44; /evidence="ECO:0000255"

null

PF00128;PF02922;PF00746;PF03714;PF18033;PF04650;

IPR013784;IPR005323;IPR014755;IPR006047;IPR004193;IPR013780;IPR017853;IPR013783;IPR014756;IPR019931;IPR011838;IPR040806;IPR005877;

null

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pneumoniae (species)

spuA SPD_0250

false

161

A0A0H2ZLQ1

MSEKSREEEKLSFKEQILRDLEKVKGYDEVLKEDEAVVRTPANEPSAEELMADSLSTVEEIMRKAPTVPTHPSQGVPASPADEIQRETPGVPSHPSQDVPSSPAEESGSRPGPGPVRPKKLEREYNETPTRVAVSYTTAEKKAEQAGPETPTPATETVDIIRDTSRRSRREGAKPAKPKKEKKSHVKAFVISFLVFLALLSAGGYFGYQYVLDSLLPIDANSKKYVTVGIPEGSNVQEIGTTLEKAGLVKHGLIFSFYAKYKNYTDLKAGYYNLQKSMSTEDLLKELQKGGTDEPQEPVLATLTIPEGYTLDQIAQTVGQLQGDFKESLTAEAFLAKVQDETFISQAVAKYPTLLESLPVKDSGARYRLEGYLFPATYSIKESTTIESLIDEMLAAMDKNLSPYYSTIKSKNLTVNELLTIASLVEKEGAKTEDRKLIAGVFYNRLNRDMPLQSNIAILYAQGKLGQNISLAEDVAIDTNIDSPYNVYKNVGLMPGPVDSPSLDAIESSINQTKSDNLYFVADVTEGKVYYANNQEDHDRNVAEHVNSKLN

Endolytic murein transglycosylase (EC 4.2.2.29) (Peptidoglycan lytic transglycosylase) (Peptidoglycan polymerization terminase)

Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)

373,153

551

60,797

Cell membrane;Cell wall biogenesis/degradation;Lyase;Membrane;Reference proteome;Transmembrane;Transmembrane helix

GO:0005886; GO:0008932; GO:0009252; GO:0071555

Evidence at protein level

5

SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_02065, ECO:0000305|PubMed:26933838}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02065}. Note=Localizes separately from FtsZ with the peripheral PG synthesis machine. {ECO:0000269|PubMed:26933838}.

null

TRANSMEM 188..208; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_02065"

PF02618;

IPR003770;

null

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pneumoniae (species)

mltG SPD_1346

false

162

A0A0H2ZMF9

MKLDKLFEKFLSLFKKETSELEDSDSTILRRSRSDRKKLAQVGPIRKFWRRYHLTKIILILGLSAGLLVGIYLFAVAKSTNVNDLQNALKTRTLIFDREEKEAGALSGQKGTYVELTDISKNLQNAVIATEDRSFYKNDGINYGRFFLAIVTAGRSGGGSTITQQLAKNAYLSQDQTVERKAKEFFLALELSKKYSKEQILTMYLNNAYFGNGVWGVEDASKKYFGVSASEVSLDQAATLAGMLKGPELYNPLNSVEDSTNRRDTVLQNMVAAGYIDKNQETEAAEVDMTSQLHDKYEGKISDYRYPSYFDAVVNEAVSKYNLTEEEIVNNGYRIYTELDQNYQANMQIVYENTSLFPRAEDGTFAQSGSVALEPKTGGVRGVVGQVADNDKTGFRNFNYATQSKRSPGSTIKPLVVYTPAVEAGWALNKQLDNHTMQYDSYKVDNYAGIKTSREVPMYQSLAESLNLPAVATVNDLGVDKAFEAGEKFGLNMEKVDRVLGVALGSGVETNPLQMAQAYAAFANEGLMPEAHFISRIENASGQVIASHKNSQKRVIDKSVADKMTSMMLGTFTNGTGISSSPADYVMAGKTGTTEAVFNPEYTSDQWVIGYTPDVVISHWLGFPTTDENHYLAGSTSNGAAHVFRNIANTILPYTPGSTFTVENAYKQNGIAPANTKRQVQTNDNSQTDDNLSDIRGRAQSLVDEASRAISDAKIKEKAQTIWDSIVNLFR

Penicillin-binding protein 2a (PBP2a) (Cell wall synthase PBP2a) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.99.28) (Peptidoglycan TGase) (Peptidoglycan glycosyltransferase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase)]

Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)

373,153

731

80,799

Acyltransferase;Antibiotic resistance;Carboxypeptidase;Cell membrane;Cell shape;Cell wall;Cell wall biogenesis/degradation;Glycosyltransferase;Hydrolase;Membrane;Multifunctional enzyme;Peptidoglycan synthesis;Protease;Reference proteome;Secreted;Signal-anchor;Transferase;Transmembrane;Transmembrane helix

GO:0005576; GO:0005886; GO:0006508; GO:0008360; GO:0008658; GO:0008955; GO:0009002; GO:0009252; GO:0016746; GO:0030288; GO:0046677; GO:0071555

Evidence at protein level

5

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29487215}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8DNB6}. Secreted, cell wall {ECO:0000305}. Note=Localizes to sites of new peptidoglycan (PG) synthesis at midcell independently of MacP. {ECO:0000269|PubMed:29487215}.

null

TRANSMEM 57..77; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000250|UniProtKB:Q8DNB6, ECO:0000255"

PF00912;PF00905;

IPR012338;IPR053473;IPR001264;IPR050396;IPR023346;IPR036950;IPR001460;

null

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pneumoniae (species)

pbp2a SPD_1821

false

163

A0A0H2ZNH9

MLDLLKQTIFTRDFIFILILLGFILVVTLLLLENRRDNIQLKQINQKVKDLIAGDYSKVLDMQGGSEITNITNNLNDLSEVIRLTQENLEQESKRLNSILFYMTDGVLATNRRGQIIMINDTAKKQLGLVKEDVLNRSILELLKIEENYELRDLITQSPELLLDSQDINGEYLNLRVRFALIRRESGFISGLVAVLHDTTEQEKEERERRLFVSNVSHELRTPLTSVKSYLEALDEGALCETVAPDFIKVSLDETNRMMRMVTDLLHLSRIDNATSHLDVELINFTAFITFILNRFDKMKGQEKEKKYELVRDYPINSIWMEIDTDKMTQVVDNILNNAIKYSPDGGKITVRMKTTEDQMILSISDHGLGIPKQDLPRIFDRFYRVDRARSRAQGGTGLGLSIAKEIIKQHKGFIWAKSEYGKGSTFTIVLPYDKDAVKEEVWEDEVED

Sensor histidine protein kinase/phosphatase WalK (EC 2.7.13.3) (EC 3.9.1.-)

Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)

373,153

449

51,712

Hydrolase;Kinase;Membrane;Phosphoprotein;Reference proteome;Transferase;Transmembrane;Transmembrane helix;Two-component regulatory system;Virulence

GO:0000155; GO:0004673; GO:0004721; GO:0005886; GO:0006355; GO:0007165; GO:0016036

Evidence at protein level

5

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

null

TRANSMEM 14..34; /note="Helical"; /evidence="ECO:0000255"

PF22610;PF02518;PF00512;PF00989;

IPR050351;IPR003660;IPR036890;IPR005467;IPR003661;IPR036097;IPR000014;IPR000700;IPR035965;IPR013767;IPR004358;IPR054693;

null

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pneumoniae (species)

walK SPD_1084

false

164

A0A0H2ZQ76

MKKKILASLLLSTVMVSQVAVLTTAHAETTDDKIAAQDNKISNLTAQQQEAQKQVDQIQEQVSAIQAEQSNLQAENDRLQAESKKLEGEITELSKNIVSRNQSLEKQARSAQTNGAVTSYINTIVNSKSITEAISRVAAMSEIVSANNKMLEQQKADKKAISEKQVANNDAINTVIANQQKLADDAQALTTKQAELKAAELSLAAEKATAEGEKASLLEQKAAAEAEARAAAVAEAAYKEKRASQQQSVLASANTNLTAQVQAVSESAAAPVRAKVRPTYSTNASSYPIGECTWGVKTLAPWAGDYWGNGAQWATSAAAAGFRTGSTPQVGAIACWNDGGYGHVAVVTAVESTTRIQVSESNYAGNRTIGNHRGWFNPTTTSEGFVTYIYAD

Peptidoglycan hydrolase PcsB (EC 3.2.1.-)

Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)

373,153

392

41,697

3D-structure;Cell membrane;Coiled coil;Hydrolase;Membrane;Reference proteome;Secreted;Signal

GO:0005576; GO:0005886; GO:0016787; GO:0030428

Evidence at protein level

5

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17449619}; Peripheral membrane protein {ECO:0000305|PubMed:22006325}; Extracellular side {ECO:0000305|PubMed:22006325}. Cell septum {ECO:0000269|PubMed:22006325}. Secreted {ECO:0000269|PubMed:17449619}. Note=Localizes to outer membrane surface, probably due to hydrophobic interactions. {ECO:0000305|PubMed:22006325}.

SIGNAL 1..27; /evidence="ECO:0000255"

null

PF24568;PF05257;

IPR007921;IPR038765;IPR009148;

4CGK;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pneumoniae (species)

pcsB SPD_2043

false

165

A0A0H2ZQB9

MTNLIATFQDRFGDWLTALSQHLQLSLLTLLLAILLAIPLAVYLRYHEKLADWVLQIAGIFQTIPSLALLGLFIPLMGIGTLPALTALVIYAIFPILQNTITGLKGIDPSLQEAGIAFGMTRWERLKKFEIPLAMPVIMSGIRTAAVLIIGTATLATLIGAGGLGSFILLGIDRNNASLILIGALSSAVLAIAFNFLLKVMEKAKLRTIFSGFALMALLLGLSYSPALLAQKEKENLIIAGKIGPEPEILANMYKLLIEENTSMTATVKPNFGTTSFLYEALKKGDIDIYPEFTGTVTESLLQPSPKVSHEPEQVYQVARDGIAKQDHLAYLKPMSYQNTYAVAVPKKIAQEYGLKTISDLKKVEGQLKAGFTLEFNDREDGNKGLQSMYGLNLNVATMQPALRYQAIHSGDIQITDAYSTDAELERYDLQVLEDDKQLFPPYQGAPLMKEALLKKHPELERVLNTLAGKITESQMSQLNYQVGVEGKSAKQVAKEFLQEQGLLKK

Ergothioneine transporter EgtUBC

Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)

373,153

506

55,544

3D-structure;Cell membrane;Membrane;Reference proteome;Transmembrane;Transmembrane helix;Transport

GO:0006865; GO:0015418; GO:0015697; GO:0031460; GO:0043190

Evidence at protein level

5

SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|RuleBase:RU363032}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU363032}.

null

TRANSMEM 23..43; /note="Helical"; /evidence="ECO:0000255, ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 49..69; /note="Helical"; /evidence="ECO:0000255, ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 70..90; /note="Helical"; /evidence="ECO:0000255, ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 148..168; /note="Helical"; /evidence="ECO:0000255, ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 178..198; /note="Helical"; /evidence="ECO:0000255, ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 209..229; /note="Helical"; /evidence="ECO:0000255"

PF00528;PF04069;

IPR007210;IPR051204;IPR000515;IPR035906;

7TXK;7TXL;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pneumoniae (species)

egtUBC proWX SPD_1642

false

166

A0A0H2ZQL5

MDLGDNELTLTPIPGKSGKAYMGSYPDGKRIFVKMNTSPILPGLAREQIAPQLLWSRRLADGRDMCAQEWLTGKILTPYDMNRKQIVNILTRLHRSRPLMTQLSRLGYAMETPVDLLQSWQETAPDALRKNHFISEVMADLRQTIPGFREDHATIVHGDVRHSNWIETDSGLIYLVDWDSVRLTDRMFDVAHMLCHYISEHQWKEWLTYYGYKYNQTVLSKLYWYGQLSYLSQISKYYMNQDLENVNREIHGLRHFRDKYGKRR

Cell cycle regulator CcrZ (EC 2.7.1.15) (EC 2.7.1.229) (Cell cycle regulator protein interacting with FtsZ)

Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)

373,153

264

31,105

ATP-binding;Cell cycle;Cell division;Cytoplasm;DNA damage;DNA replication;Kinase;Nucleotide-binding;Reference proteome;Transferase

GO:0004747; GO:0005524; GO:0005737; GO:0006270; GO:0006974; GO:0016773; GO:0019200; GO:0032153; GO:0051301; GO:0051726

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:34373624}. Note=Localizes at mid-cell, forming a patchy ring. Disassembles from the old septum to assemble at the newly formed division site. Colocalizes with FtsZ during the full cell cycle. Colocalizes with DnaA in newborn cells. {ECO:0000269|PubMed:34373624}.

null

PF01636;

IPR002575;IPR052077;IPR011009;

null

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pneumoniae (species)

ccrZ SPD_0476

false

167

A0A0H3AMJ9

MEAILNKNMKILIVDDFSTMRRIVKNLLRDLGFNNTQEADDGLTALPMLKKGDFDFVVTDWNMPGMQGIDLLKNIRADEELKHLPVLMITAEAKREQIIEAAQAGVNGYIVKPFTAATLKEKLDKIFERL

Chemotaxis protein CheY-3 (Chemotaxis response regulator CheY-3)

Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)

345,073

130

14,748

3D-structure;Chemotaxis;Cytoplasm;Flagellar rotation;Magnesium;Metal-binding;Phosphoprotein;Two-component regulatory system

GO:0000160; GO:0005737; GO:0006935; GO:0046872; GO:0097588

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.

null

PF00072;

IPR011006;IPR001789;IPR052048;

4JP1;4LX8;

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

cheY-3 VC0395_A1653

false

168

A0A0H3C8X0

MPFDSTNADLSVIPVKTPAELKRFIALPARLNAKDPNWITPLFMERTDALTPKTNPFFDHAEVQLFLATRGGRDVGRISAQIDQLTPQPTEGRLDGHFGMIAAEDDPAVFNVLFRAAEDWLRARGRTHAVGPFNLSINEEVGLLVWGFDTPPMVLMGHDPVYAGPRVEEQGYAKAQDLFAYKADETGDIPEIAQRRVKRGLPSGVVLRQLDMSRYDQEVQTLTEILNDAWSDNWGFTPTTEAETRQLAKSLKQVIDQRLVWFSEIDGEAAGVVVFLPNVNEAIADLKGKLLPFGWAKLLWRLKVKGVKSARIPLMGVKKKFQTSQRGRMLPFWMMKASRDMAMSLGYNRYEISWVLEANKAMTHIAENVGGTHYKTYRVYEKAL

Bacterial ceramide synthase (EC 2.3.1.-)

Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus)

565,050

384

43,279

Acyltransferase;Cytoplasm;Lipid metabolism;Reference proteome;Transferase

GO:0005737; GO:0006665; GO:0016020; GO:0016746

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:34969973}.

null

IPR016181;IPR039968;

null

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Alphaproteobacteria (class), Caulobacterales (order), Caulobacteraceae (family), Caulobacter (genus), Caulobacter vibrioides (species)

bcerS CCNA_01212

false

169

A0A0H3GDH9

MKIRWIRLSLVAILIIAVVFIGVIGFQKYQFSKSRNKVIMQMDRLMKDQDGGNFRRLDKKENGVEIISYIPKTTEKKDNEIIQKEIGKATDAEVKKLNRDKETQGIIFYTYQKHRMAEQAISYKAVQSEYVKEGRTKFVLKDKKDICKNIVTDAETGALLTLGEVLIKSNQTKLNLKTAVEEELIKTGDFSLKDVGNLGKIKSLVKWNQTDFEITNSEIILPVKIPGAPEPKKVKVKLADIASSVNKRYLPSSVKVPEVPKAKTNKRIALTFDDGPSSSVTPGVLDTLKRHNVKATFFVLGSSVIQNPGLVKRELEEGHQVGSHSWDHPQLTKQSTQEVYNQILKTQKAVFDQTGYFPTTMRPPYGAVNKQVAEEIGLPIIQWSVDTEDWKYRNAGIVTKKVLAGATDGAIVLMHDIHKTTAASLDTTLTKLKSQGYEFVTIDELYGEKLQIGKQYFDKTDSRMVK

Peptidoglycan-N-acetylglucosamine deacetylase PgdA (Peptidoglycan GlcNAc deacetylase) (EC 3.5.1.104) (N-acetylglucosamine deacetylase Pgd) (Peptidoglycan N-deacetylase) (PG N-deacetylase) (Petptidoglycan deacetylase) (PG deacetylase)

Listeria monocytogenes serotype 1/2a (strain 10403S)

393,133

466

52,496

Cell membrane;Cell wall;Hydrolase;Membrane;Metal-binding;Secreted;Transmembrane;Transmembrane helix;Virulence;Zinc

GO:0001896; GO:0005576; GO:0005886; GO:0005975; GO:0008270; GO:0009275; GO:0042545; GO:0042783; GO:0042803; GO:0050119; GO:0060241; GO:0141043

Evidence at transcript level

5

SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8Y9V5}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8Y9V5, ECO:0000255}; Extracellular side {ECO:0000250|UniProtKB:Q8Y9V5}. Secreted, cell wall {ECO:0000250|UniProtKB:A0A3Q0NBH7}.

null

TRANSMEM 6..26; /note="Helical"; /evidence="ECO:0000255"

PF01522;

IPR011330;IPR002509;IPR017219;IPR050248;

null

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Listeriaceae (family), Listeria (genus), Listeria monocytogenes (species)

pgdA LMRG_00107

false

170

A0A0H3GGY3

MKLAKKWRDWYIESGKKYLFPLLLVCFAVIAYFLVCQMTKPESYNVKLFQVAEKTIRSPQTVEDTEKTKEERTKASDAVEDVYVYNRETGQNRVALIQSLFAYVNEVNAEAQEKDTKNKEKAKKENKPAPAPTSTEDKLKNLKDKLSSNVSEKITSNISDEVFTTLIEAKSKDFNVMEDVVTTEVEKSMENKIRDENLNSVKIRARDDIELSAIPAYYKNVSKALVSYAIVPNEVYDEEQTDARRKEAAQSVVPVKILQGQVIVQEGQIVDRETYRQLKMLHLLDQKMPVKQYAGFAIFIIALAAILFLYTKKQTQPKAKKMQTMLIFSSVYLVSLFMLFIILFLETQNIANIAFLFPAAFAPMILKILLNEKYAFLSVIFIAVTSLLTFQNDATSGITIFILLSGATSVVMLRDYSRRSAIMLSGFMVGLINMIYVLLLLLINNSTLLQVSTLMALGYAFLGGFGAFILGVGVIPLFETIFGLLTTSRLVELANPNHPLLKKILMKAPGTYHHSMMVANLAEACADKIGANSLLVRVGCFYHDIGKTLRPPYFVENQLQGINPHDRLTPEQSRDIILSHTKDGAEILKENHMPQPIIDIALQHHGTTLLKYFYFKAKETNPDVKEADYRYSGPKPQTKEIAIINISDSVEAAVRSSTEPTMAKITEIIDGIIKDRFLDGQFTECDITIQEIKIIRDTLIATLNGIYHQRIQYPDDKD

Cyclic-di-AMP phosphodiesterase PgpH (c-di-AMP phosphodiesterase) (EC 3.1.4.59)

Listeria monocytogenes serotype 1/2a (strain 10403S)

393,133

718

81,112

3D-structure;Cell membrane;Hydrolase;Manganese;Membrane;Metal-binding;Nucleotide-binding;Transmembrane;Transmembrane helix

GO:0000166; GO:0005886; GO:0016787; GO:0046872; GO:0106409

Evidence at protein level

5

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

null

TRANSMEM 18..38; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 290..310; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 325..345; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 350..370; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 371..391; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 393..413; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 422..442; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 458..478; /note="Helical"; /evidence="ECO:0000255"

PF07698;PF07697;PF01966;

IPR003607;IPR006674;IPR006675;IPR011624;IPR011621;IPR052722;

4S1B;4S1C;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Listeriaceae (family), Listeria (genus), Listeria monocytogenes (species)

pgpH LMRG_00918

false

171

A0A0H3JN63

MHELTIYHFMSDKLNLYSDIGNIIALRQRAKKRNIKVNVVEINETEGITFDECDIFFIGGGSDREQALATKELSKIKTPLKEAIEDGMPGLTICGGYQFLGKKYITPDGTELEGLGILDFYTESKTNRLTGDIVIESDTFGTIVGFENHGGRTYHDFGTLGHVTFGYGNNDEDKKEGIHYKNLLGTYLHGPILPKNYEITDYLLEKACERKGIPFEPKEIDNEAEIQAKQVLIDRANRQKKSR

Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD (EC 6.3.5.13) (Lipid II isoglutaminyl synthase glutaminase subunit) (EC 3.5.1.2)

Staphylococcus aureus (strain N315)

158,879

243

27,430

3D-structure;Cell shape;Cell wall biogenesis/degradation;Glutamine amidotransferase;Hydrolase;Ligase;Peptidoglycan synthesis

GO:0004359; GO:0008360; GO:0009236; GO:0009252; GO:0071555; GO:0140282

Evidence at protein level

5

null

PF07685;

IPR029062;IPR033949;IPR011698;IPR043702;

6GS2;6H5E;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Staphylococcaceae (family), Staphylococcus (genus), Staphylococcus aureus (species)

gatD SA1707

false

172

A0A0H3JNB0

MKKVSVIMPTFNNGEKLHRTISSVLNQTMKSTDYELIIIDDHSNDNGETLNVIKKYKGLVRFKQLKKNSGNASVPRNTGLKMSKAEYVFFLDSDDLLHERALEDLYNYGKENNSDLIIGKYGVEGKGRSVPKAIFEKGNVAKADIIDNSIFYALSVLKMFKKSVIDKNKIKFKTFSKTAEDQLFTIEFLMNSKNYSIKTDYEYYIVVNDFESSNHLSVNKSTGNQYFATINEIYKAIYKSPIYKNQEKRHQLAGKYTTRLLRHGQKKNFANSKMKYEDKIEWLNNFSKTINKVPRDSDKYVTQIFNLKLEAIRQNDLLAVMIADKLL

Poly(ribitol-phosphate) beta-N-acetylglucosaminyltransferase TarP (EC 2.4.1.-) (WTA glycosyltransferase)

Staphylococcus aureus (strain N315)

158,879

327

37,812

3D-structure;Cell wall biogenesis/degradation;Glycosyltransferase;Manganese;Metal-binding;Teichoic acid biosynthesis;Transferase;Virulence

GO:0016758; GO:0019350; GO:0046872; GO:0071555

Evidence at protein level

5

null

PF00535;PF22181;

IPR001173;IPR029044;IPR054028;

6H1J;6H21;6H2N;6H4F;6H4M;6HNQ;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Staphylococcaceae (family), Staphylococcus (genus), Staphylococcus aureus (species)

tarP SA1808

false

173

A0A0H3JPC6

MMKFSVIVPTYNSEKYITELLNSLAKQDFPKTEFEVVVVDDCSTDQTLQIVEKYRNKLNLKVSQLETNSGGPGKPRNVALKQAEGEFVLFVDSDDYINKETLKDAAAFIDEHHSDVLLIKMKGVNGRGVPQSMFKETAPEVTLLNSRIIYTLSPTKIYRTALLKDNDIYFPEELKSAEDQLFTMKAYLNANRISVLSDKAYYYATKREGEHMSSAYVSPEDFYEVMRLIAVEILNADLEEAHKDQILAEFLNRHFSFSRTNGFSLKVKLEEQPQWINALGDFIQAVPERVDALVMSKLRPLLHYARAKDIDNYRTVEESYRQGQYYRFDIVDGKLNIQFNEGEPYFEGIDIAKPKVKMTAFKFDNHKIVTELTLNEFMIGEGHYDVRLKLHSRNKKHTMYVPLSVNANKQYRFNIMLEDIKAYLPKEKIWDVFLEVQIGTEVFEVRVGNQRNKYAYTAETSALIHLNNDFYRLTPYFTKDFNNISLYFTAITLTDSISMKLKGKNKIILTGLDRGYVFEEGMASVVLKDDMIMGMLSQTSENEVEILLSKDIKKRDFKNIVKLNTAHMTYSLK

Poly(ribitol-phosphate) beta-N-acetylglucosaminyltransferase TarS (EC 2.4.1.355) (Beta-O-GlcNAc transferase) (Beta-O-GlcNAc-WTA transferase) (WTA glycosyltransferase) (Wall teichoic acid beta-glycosyltransferase)

Staphylococcus aureus (strain Mu50 / ATCC 700699)

158,878

573

66,257

3D-structure;Antibiotic resistance;Cell wall biogenesis/degradation;Glycosyltransferase;Manganese;Metal-binding;Teichoic acid biosynthesis;Transferase;Virulence

GO:0016758; GO:0019350; GO:0046677; GO:0046872; GO:0071555

Evidence at protein level

5

null

PF00535;PF18674;PF22377;PF22181;

IPR001173;IPR029044;IPR054028;IPR041038;IPR054531;

5TZ8;5TZE;5TZI;5TZJ;5TZK;5U02;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Staphylococcaceae (family), Staphylococcus (genus), Staphylococcus aureus (species)

tarS SAV0258

false

174

A0A0H3JRU9

MKQIKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYLVGSDLGPAESYLNIERIIDVAKQANVDAIHPGYGFLSENEQFARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLMIKATSGGGGKGMRIVREESELEDAFHRAKSEAEKSFGNSEVYIERYIDNPKHIEVQVIGDEHGNIVHLFERDCSVQRRHQKVVEVAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLVSGDEFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAAGADLFGEEINMPQQKDITTLGYAIQCRITTEDPLNDFMPDTGTIIAYRSSGGFGVRLDAGDGFQGAEISPYYDSLLVKLSTHAISFKQAEEKMVRSLREMRIRGVKTNIPFLINVMKNKKFTSGDYTTKFIEETPELFDIQPSLDRGTKTLEYIGNVTINGFPNVEKRPKPDYELASIPTVSSSKIASFSGTKQLLDEVGPKGVAEWVKKQDDVLLTDTTFRDAHQSLLATRVRTKDMINIASKTADVFKDGFSLEMWGGATFDVAYNFLKENPWERLERLRKAIPNVLFQMLLRASNAVGYKNYPDNVIHKFVQESAKAGIDVFRIFDSLNWVDQMKVANEAVQEAGKISEGTICYTGDILNPERSNIYTLEYYVKLAKELEREGFHILAIKDMAGLLKPKAAYELIGELKSAVDLPIHLHTHDTSGNGLLTYKQAIDAGVDIIDTAVASMSGLTSQPSANSLYYALNGFPRHLRTDIEGMESLSHYWSTVRTYYSDFESDIKSPNTEIYQHEMPGGQYSNLSQQAKSLGLGERFDEVKDMYRRVNFLFGDIVKVTPSSKVVGDMALYMVQNDLDEQSVITDGYKLDFPESVVSFFKGEIGQPVNGFNKDLQAVILKGQEALTARPGEYLEPVDFEKVRELLEEEQQGPVTEQDIISYVLYPKVYEQYIQTRNQYGNLSLLDTPTFFFGMRNGETVEIEIDKGKRLIIKLETISEPDENGNRTIYYAMNGQARRIYIKDENVHTNANVKPKADKSNPSHIGAQMPGSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEIEKATD

Pyruvate carboxylase (EC 6.4.1.1)

Staphylococcus aureus (strain Mu50 / ATCC 700699)

158,878

1,150

128,558

3D-structure;ATP-binding;Biotin;Ligase;Manganese;Metal-binding;Nucleotide-binding;Pyruvate

GO:0004736; GO:0005524; GO:0005737; GO:0006094; GO:0042802; GO:0046872

Evidence at protein level

5

null

PF02785;PF00289;PF00364;PF02786;PF00682;PF02436;

IPR013785;IPR011761;IPR005481;IPR011764;IPR005482;IPR000089;IPR003379;IPR005479;IPR055268;IPR016185;IPR000891;IPR005930;IPR011054;IPR011053;

3BG5;3HB9;3HBL;3HO8;4HNT;4HNU;4HNV;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Staphylococcaceae (family), Staphylococcus (genus), Staphylococcus aureus (species)

pycA SAV1114

false

175

A0A0H3JUU7

MRQWTAIHLAKLARKASRAVGKRGTDLPGQIARKVDTDVLRKLAEQVDDIVFISGTNGKTTTSNLIGHTLKANNIQIIHNNEGANMAAGITSAFIMQSTPKTKIAVIEIDEGSIPRVLKEVTPSMMVFTNFFRDQMDRFGEIDIMVNNIAETISNKGIKLLLNADDPFVSRLKIASDTIVYYGMKAHAHEFEQSTMNESRYCPNCGRLLQYDYIHYNQIGHYHCQCGFKREQAKYEISSFDVAPFLYLNINDEKYDMKIAGDFNAYNALAAYTVLRELGLNEQTIKNGFETYTSDNGRMQYFKKERKEAMINLAKNPAGMNASLSVGEQLEGEKVYVISLNDNAADGRDTSWIYDADFEKLSKQQIEAIIVTGTRAEELQLRLKLAEVEVPIIVERDIYKATAKTMDYKGFTVAIPNYTSLAPMLEQLNRSFEGGQS

Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT (EC 6.3.5.13)

Staphylococcus aureus (strain N315)

158,879

437

49,192

3D-structure;ATP-binding;Cell shape;Cell wall biogenesis/degradation;Ligase;Metal-binding;Nucleotide-binding;Peptidoglycan synthesis;Zinc

GO:0005524; GO:0008270; GO:0008360; GO:0009252; GO:0016881; GO:0071555; GO:0140282

Evidence at protein level

5

null

PF08245;PF08353;

IPR043703;IPR036565;IPR013221;IPR013564;

6GS2;6H5E;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Staphylococcaceae (family), Staphylococcus (genus), Staphylococcus aureus (species)

murT SA1708

false

176

A0A0H3K686

MKKKNIYSIRKLGVGIASVTLGTLLISGGVTPAANAAQHDEAQQNAFYQVLNMPNLNADQRNGFIQSLKDDPSQSANVLGEAQKLNDSQAPKADAQQNNFNKDQQSAFYEILNMPNLNEAQRNGFIQSLKDDPSQSTNVLGEAKKLNESQAPKADNNFNKEQQNAFYEILNMPNLNEEQRNGFIQSLKDDPSQSANLLSEAKKLNESQAPKADNKFNKEQQNAFYEILHLPNLNEEQRNGFIQSLKDDPSQSANLLAEAKKLNDAQAPKADNKFNKEQQNAFYEILHLPNLTEEQRNGFIQSLKDDPSVSKEILAEAKKLNDAQAPKEEDNNKPGKEDNNKPGKEDNNKPGKEDNNKPGKEDGNKPGKEDNKKPGKEDGNKPGKEDNKKPGKEDGNKPGKEDGNKPGKEDGNGVHVVKPGDTVNDIAKANGTTADKIAADNKLADKNMIKPGQELVVDKKQPANHADANKAQALPETGEENPFIGTTVFGGLSLALGAALLAGRRREL

Immunoglobulin G-binding protein A (IgG-binding protein A) (Staphylococcal protein A) (SpA)

Staphylococcus aureus (strain Newman)

426,430

508

55,554

Cell wall;Direct protein sequencing;Peptidoglycan-anchor;Repeat;Secreted;Signal;Virulence

GO:0005576; GO:0019865

Evidence at protein level

5

SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000269|PubMed:17416657, ECO:0000269|PubMed:24434550}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000269|PubMed:17416657, ECO:0000269|PubMed:24434550}. Secreted {ECO:0000269|PubMed:24434550}. Note=Released from the cell wall in a glycan-free form by LytM; released early in log growth, almost no release occurs after 3 hours growth (PubMed:24434550). Anchored to the cell wall by sortase A (By similarity). {ECO:0000250|UniProtKB:P02976, ECO:0000269|PubMed:24434550}.

SIGNAL 1..36; /evidence="ECO:0000255, ECO:0000269|PubMed:24434550"

null

PF02216;PF00746;PF01476;PF03373;PF04650;

IPR009063;IPR019931;IPR018392;IPR036779;IPR005038;IPR003132;IPR005877;

null

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Staphylococcaceae (family), Staphylococcus (genus), Staphylococcus aureus (species)

spa NWMN_0055

false

177

A0A0H3KB22

MTYAVKEIFYTLQGEGANAGRPAVFCRFAGCNLWSGREEDRAQAVCRFCDTDFVGTDGENGGKFKDADALVATIAGLWPAGEAHRFVVCTGGEPMLQLDQPLVDALHAAGFGIAIETNGSLPVLESIDWICVSPKADAPLVVTKGNELKVVIPQDNQRLADYAKLDFEYFLVQPMDGPSRDLNTKLAIDWCKRHPQWRLSMQTHKYLNIP

7-carboxy-7-deazaguanine synthase (CDG synthase) (EC 4.3.99.3) (Queuosine biosynthesis protein QueE)

Burkholderia multivorans (strain ATCC 17616 / 249)

395,019

210

23,148

3D-structure;4Fe-4S;Iron;Iron-sulfur;Lyase;Magnesium;Metal-binding;Queuosine biosynthesis;Reference proteome;S-adenosyl-L-methionine

GO:0000287; GO:0008616; GO:0016840; GO:0042802; GO:0042803; GO:0051539; GO:1904047

Evidence at protein level

5

null

IPR024924;IPR013785;IPR030977;IPR007197;

4NJG;4NJH;4NJI;4NJJ;4NJK;

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Burkholderiaceae (family), Burkholderia (genus), Burkholderia cepacia complex (no rank), Burkholderia multivorans (species)

queE Bmul_3115 BMULJ_00116

false

178

A0A0H3KZS3

MVTYSMIPQISQAPGLIQRVLTFLETLKAQGFTGDTATSYADRLSLSTDNSIYQLLPDAVLFPRSTADVALIARLAGEAAFSSLVFTPRGGGTGTNGQSLNQGIIVDMSRHMNRILEINTEQRWVRVEAGVVKDQLNAYLKPFGFFFSPELSTSNRATLGGMINTDASGQGSLVYGKTSDHVLGLRAVLLGGDILDTRPVPTALAENLAQTPTPEGRIYQQVLTRCREHRELILEKFPKLNRFLTGYDLRHVFSDDMQTFDLTRLLCGAEGTLAFISEARLDITPLPKVRRVVNIKYDAFDSALRNAPLMVEAQALSVETVDSKVLNLAREDIVWHSVRELITAIPDKEMLGLNIVEFAGDDAGQIDRQITQLCARLDTLMTQQQGGVIGYQLCDDLDGIERIYNMRKKAVGLLGNAKGRAKPIPFVEDTAVPPEHLADYIVEFRALLDSHGLSYGMFGHVDAGVLHVRPALDMCDPHQEMMMKQISDEVVALTARYGGLLWGEHGKGFRAQYSPAFFGETLFNELRRIKAAFDPHNRLNPGKICTPFDSEAAMMQVDATKRGSYDRQIPLQVRETWRGALECNGNGLCFNFDARSPMCPSMKITRNRIHSPKGRATLTREWLRLLAEQGADPVMLEKKLPESSLSLRALISRMRNTWYANKGEYDFSHEVKEAMSGCLACKACSTQCPIKIDVPAFRSRFLQLYHTRYLRPLSDHLVAGVESYAPLMAKAPGVFNFFLKQPWATSFSKTHIGMVDLPLLSSPTLKQQLSGHPAMNMTLEQLEALSETQRAQKVLVVQDPFTSFYEAKLVHDFIRLIEKLGYQPVLLPFSPNGKAQHVKGFLQRFARTASKTADFLNRVAKLGMPMVGIDPATVLCYRDEYHQMLGEARGDFNVLLVHEWLHQALQEREVQVTSGEAWYLFAHCTEVTALPGTPGQWQAIFSRFGAKLENINVGCCGMAGTYGHESQNLENSLGIYALSWHPQLQKLPRQRCLATGFSCRSQVKRVEGNGMRHPLQALLELI

D-2-hydroxyglutarate dehydrogenase (D2HGDH) (EC 1.1.99.39)

Pantoea ananatis (strain AJ13355)

932,677

1,022

113,963

4Fe-4S;FAD;Flavoprotein;Iron;Iron-sulfur;Metal-binding;Oxidoreductase

GO:0004458; GO:0008720; GO:0046872; GO:0051539; GO:0071949; GO:1903457

Evidence at protein level

5

null

PF02913;PF01565;PF13183;

IPR017896;IPR017900;IPR004113;IPR016166;IPR036318;IPR016169;IPR016164;IPR006094;IPR016171;

null

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Erwiniaceae (family), Pantoea (genus), Pantoea ananas (species)

ydiJ PAJ_1060

false

179

A0A0H3LKL4

MQGKPRIAVIGAGLGGTAGAALMARAGFNVRLYEQAPAFSRLGAGIHLGPNVMKIMRRIGIEDELNRQGSHPDYWYSRDWQSGAELARIPLGDYAVSHYGATYLTVHRGDFHALMTAALPAGLLQFNKRLTRVDEDDDVVRLHFADGSVEEAEIVIGADGVNSRLREHLLGAELPKYTGYVAHRAVFPTPLDSGSLPFDMCVKWWSDDRHMMVYFVTGKRDEIYYVTGVPEQQWDMGKSWVPSSKAEMRAAFAGWHPTVQALIEATPEVSKWPLLERDPLPLWSRGRIVLLGDACHPMKPHMAQGAAMAIEDAAMLTRIFEQTGLQDHAAAFRLYEDNRAERASRVQRVSHDNTWLRTNENPDWCFGYDVYAEPLVEGRRAAA

6-hydroxynicotinate 3-monooxygenase (6-HNA monooxygenase) (EC 1.14.13.114)

Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)

257,310

383

42,803

Aromatic hydrocarbons catabolism;FAD;Flavoprotein;Monooxygenase;NAD;Oxidoreductase;Signal

GO:0009056; GO:0043731; GO:0071949

Evidence at protein level

5

null

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

null

PF01494;

IPR002938;IPR050493;IPR036188;

null

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Alcaligenaceae (family), Bordetella (genus), Bordetella bronchiseptica (species)

nicC BB1778

false

180

A0A0H3LM39

MNQPSSLAADLRGAWHAQAQSHPLITLGLAASAAGVVLLLVAGIVNALTGENRVHVGYAVLGGAAGFAATALGALMALGLRAISARTQDAMLGFAAGMMLAASAFSLILPGLDAAGTIVGPGPAAAAVVALGLGLGVLLMLGLDYFTPHEHERTGHQGPEAARVNRVWLFVLTIILHNLPEGMAIGVSFATGDLRIGLPLTSAIAIQDVPEGLAVALALRAVGLPIGRAVLVAVASGLMEPLGALVGVGISSGFALAYPISMGLAAGAMIFVVSHEVIPETHRNGHETTATVGLMAGFALMMFLDTALG

Zinc transporter ZIPB (BbZIP)

Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)

257,310

309

30,988

3D-structure;Cadmium;Cell inner membrane;Cell membrane;Ion transport;Membrane;Transmembrane;Transmembrane helix;Transport;Zinc;Zinc transport

GO:0005385; GO:0005886

Evidence at protein level

5

SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.

null

TRANSMEM 23..50; /note="Helical"; /evidence="ECO:0000269|PubMed:35857505"; TRANSMEM 56..81; /note="Helical"; /evidence="ECO:0000269|PubMed:28875161"; TRANSMEM 84..119; /note="Helical"; /evidence="ECO:0000269|PubMed:28875161"; TRANSMEM 122..145; /note="Helical"; /evidence="ECO:0000269|PubMed:28875161"; TRANSMEM 166..190; /note="Helical"; /evidence="ECO:0000269|PubMed:28875161"; TRANSMEM 193..222; /note="Helical"; /evidence="ECO:0000269|PubMed:28875161"; TRANSMEM 225..251; /note="Helical"; /evidence="ECO:0000269|PubMed:28875161"; TRANSMEM 256..275; /note="Helical"; /evidence="ECO:0000269|PubMed:28875161"; TRANSMEM 288..308; /note="Helical"; /evidence="ECO:0000269|PubMed:28875161"

PF02535;

IPR003689;

5TSA;5TSB;6PGI;7Z6M;7Z6N;8CZJ;8GHT;8J1M;

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Alcaligenaceae (family), Bordetella (genus), Bordetella bronchiseptica (species)

BB2405

false

181

A0A0H3M5A8

MKLGAWVAAQLPTTRTAVRTRLTRLVVSIVAGLLLYASFPPRNCWWAAVVALALLAWVLTHRATTPVGGLGYGLLFGLVFYVSLLPWIGELVGPGPWLALATTCALFPGIFGLFAVVVRLLPGWPIWFAVGWAAQEWLKSILPFGGFPWGSVAFGQAEGPLLPLVQLGGVALLSTGVALVGCGLTAIALEIEKWWRTGGQGDAPPAVVLPAACICLVLFAAIVVWPQVRHAGSGSGGEPTVTVAVVQGNVPRLGLDFNAQRRAVLDNHVEETLRLAADVHAGLAQQPQFVIWPENSSDIDPFVNPDAGQRISAAAEAIGAPILIGTLMDVPGRPRENPEWTNTAIVWNPGTGPADRHDKAIVQPFGEYLPMPWLFRHLSGYADRAGHFVPGNGTGVVRIAGVPVGVATCWEVIFDRAPRKSILGGAQLLTVPSNNATFNKTMSEQQLAFAKVRAVEHDRYVVVAGTTGISAVIAPDGGELIRTDFFQPAYLDSQVRLKTRLTPATRWGPILQWILVGAAAAVVLVAMRQNGWFPRPRRSEPKGENDDSDAPPGRSEASGPPALSESDDELIQPEQGGRHSSGFGRHRATSRSYMTTGQPAPPAPGNRPSQRVLVIIPTFNERENLPVIHRRLTQACPAVHVLVVDDSSPDGTGQLADELAQADPGRTHVMHRTAKNGLGAAYLAGFAWGLSREYSVLVEMDADGSHAPEQLQRLLDAVDAGADLAIGSRYVAGGTVRNWPWRRLVLSKTANTYSRLALGIGIHDITAGYRAYRREALEAIDLDGVDSKGYCFQIDLTWRTVSNGFVVTEVPITFTERELGVSKMSGSNIREALVKVARWGIEGRLSRSDHARARPDIARPGAGGSRVSRADVTE

Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthase [Includes: Apolipoprotein N-acyltransferase (ALP N-acyltransferase) (EC 2.3.1.269); Polyprenol monophosphomannose synthase (PPM synthase) (Polyprenol-P-Man synthase) (Ppm1) (EC 2.4.1.-) (Dolichol-phosphate mannose synthase) (EC 2.4.1.83)]

Mycobacterium bovis (strain BCG / Pasteur 1173P2)

410,289

874

93,824

Acyltransferase;Cell membrane;Hydrolase;Membrane;Transferase;Transmembrane;Transmembrane helix

GO:0004582; GO:0005886; GO:0016410; GO:0016787; GO:0042158

Evidence at protein level

5

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

null

TRANSMEM 23..42; /note="Helical"; /evidence="ECO:0000250|UniProtKB:A0QZ13"; TRANSMEM 72..89; /note="Helical"; /evidence="ECO:0000250|UniProtKB:A0QZ13"; TRANSMEM 94..115; /note="Helical"; /evidence="ECO:0000250|UniProtKB:A0QZ13"; TRANSMEM 177..194; /note="Helical"; /evidence="ECO:0000250|UniProtKB:A0QZ13"; TRANSMEM 206..223; /note="Helical"; /evidence="ECO:0000250|UniProtKB:A0QZ13"; TRANSMEM 509..526; /note="Helical"; /evidence="ECO:0000250|UniProtKB:A0QZ13"

PF00795;PF00535;PF20154;

IPR004563;IPR003010;IPR036526;IPR039528;IPR001173;IPR045378;IPR029044;

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), Mycobacterium bovis (biotype), Mycobacterium tuberculosis variant bovis BCG (no rank)

lnt ppm1 BCG_2070c

false

182

A0A0H3MDW1

MAGPKHVLLVSEHWDLFFQTKELLNPEEYRCTIGQQYKQELSADLVVCEYSLLPREIRSPKSLEGSFVLVLLDFFDEETSVDLLDRGFWYLIRPITPRILKSAISLFLSQHSLHSVPESIRFGPNVFYVLKLTVETPEGSVHLTPSESGILKRLLINKGQLCLRKHLLEEIKNHAKAIVARNVDVHIASLRKKLGAYGSRIVTLRGVGYLFSDDGDKKFSQQDTKLS

Atypical response regulator protein ChxR (Transcriptional regulatory protein)

Chlamydia trachomatis serovar L2 (strain ATCC VR-902B / DSM 19102 / 434/Bu)

471,472

227

25,835

3D-structure;Activator;DNA-binding;Transcription;Transcription regulation;Two-component regulatory system

GO:0000160; GO:0000976; GO:0003677; GO:0003700; GO:0042802; GO:0042803; GO:0043565; GO:0045893

Evidence at protein level

5

null

PF22368;PF00486;

IPR011006;IPR055158;IPR001867;IPR016032;IPR001789;IPR036388;

2M1B;3Q7R;3Q7S;3Q7T;

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), PVC group (clade), Chlamydiota (phylum), Chlamydiia (class), Chlamydiales (order), Chlamydiaceae (family), Chlamydia/Chlamydophila group (no rank), Chlamydia (genus), Chlamydia trachomatis (species)

chxR CTL0894

false

183

A0A0H3PEK7

MRFDFFVSKRLNISRNKALELIENEEVLLNGKSFKASFDVKNFLENLKKTQDLNPEDILLTDGLKLDLLSEIYVSRAALKLKNFLEENGIEIKHKNCLDIGSSTGGFVQILLENQALKITALDVGNNQLHLSLRTNEKIILHENTDLRTFKSEEKFELITCDVSFISLINLLYYIDNLALKEIILLFKPQFEVGKNIKRDKKGVLKDDKAILKARMDFEKACAKLGWLLKNTQKSSIKGKEGNVEYFYYYIKN

23S rRNA (cytidine-2'-O)-methyltransferase TlyA (EC 2.1.1.226) (23S rRNA (cytidine1920-2'-O)-methyltransferase) (Hemolysin A)

Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176)

354,242

253

29,175

Methyltransferase;RNA-binding;rRNA processing;S-adenosyl-L-methionine;Transferase;Virulence

GO:0000451; GO:0003723; GO:0008649; GO:0016032; GO:0042256; GO:0048870; GO:0071236

Evidence at protein level

5

null

PF01728;

IPR002877;IPR036986;IPR029063;IPR047048;

null

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Campylobacterota (phylum), Epsilonproteobacteria (class), Campylobacterales (order), Campylobacteraceae (family), Campylobacter (genus), Campylobacter jejuni (species), Campylobacter jejuni subsp. jejuni (subspecies)

tlyA CJJ81176_0616

false

184

A0A0H3PJK4

MQINLLNDFIKAYENTYSVSFDDSFKGRIQELCKELNEPFMHASYALENELKELVFSLDKNVNIAIIGQFSSGKSSLLNLILGRDCLPTGVVPVTFKPTFLRYAKEYFLRVEFEDGSDIITNIEKLAFYTDQRNEVKQAKSLHIFAPIPLLEKITLVDTPGLNANENDTLTTLDELKNIHGAIWLSLIDNAGKKSEEDAIKANLELLGENSICVLNQKDKLSAEELDNVLNYAKSVFLKYFNELIAISCKEAKDEQSYEKSNFQSLLDFLTQLDTTVLKEKFVKRKILNLCEILEDENQLFVGIFDRLLNQFQSYEKHLLLAYENFLKEIEILNHQILEQLKSISERISSEIFASVKEKDAYFYKESKGFLKKDLYTRYDYKAPYISSDDAFLAMFYNSDVMSKEFKKIKNELYKSFEEIKMKLKDFINILEREILLFKAEFSNIQKDHIFQSDKNFSELRAFCNASDEYFLKDFKELLFKSILELDLFFEKLNLKAFTNYENATKLSLAFFSRKINESRVLYELDSSEFVLFYPKKSEIYERVLNELNVYEFETLLINKPILTKIAKNFLEQSQNLIQEKNKFLDLKKAELQKRRAQILNVRESIKED

Dynamin-like protein 2 (DLP2)

Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176)

354,242

609

71,304

3D-structure;Cytoplasm;Hydrolase

GO:0005829; GO:0016787

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30131557}.

null

PF00350;

IPR022812;IPR045063;IPR027417;IPR051943;

5OWV;5OXF;

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Campylobacterota (phylum), Epsilonproteobacteria (class), Campylobacterales (order), Campylobacteraceae (family), Campylobacter (genus), Campylobacter jejuni (species), Campylobacter jejuni subsp. jejuni (subspecies)

dlp2 cj0412 CJJ81176_0436

false

185

A0A0H5BMX5

MSIVSFCSSLPAGPHGFKHGRGTRDMVHMPCIVRRTARSPAQACRLLRWNKYHCAAVPTNSSLSPSPTPLDVEIELDLEPFLIKYKSGRIERLGRFGDRTDYVEASLDPATEVTSRDAITDTGVPVRIYLPKVDDSPPNSLRVLVYFHGGAFLVEDSASPPYHNYLNNLASKANILIVSVNYRLAPEYPLPVAYDDCMEALNWVNKHSDGTGQEDWINKHGDFDHLFISGDSAGGNITHNIAMSTDAPKNIEGIALVHPYFFGKVALETELQDPTNLLLHRKLWSFITPESEGLDDPRVNPLGPTAPSLEKIKCKRAVVFVAGEDFHSERGRKYSEKLKSEFKGEVPLLCNHDGVGHVYHLSVDATEEEIESAAAWKMMTDLLKFYKDNDVVLEGSIVESLKAKTTEGIKKMKEIEKGMSERMMEQLVAFYNGKPVPYSS

Tuliposide B-converting enzyme 1, amyloplastic (TgTCEB1) (EC 4.2.99.23)

Tulipa gesneriana (Garden tulip)

13,306

440

49,023

Amyloplast;Direct protein sequencing;Lyase;Plant defense;Plastid;Transit peptide

GO:0006952; GO:0009501; GO:0016787; GO:0016829

Evidence at protein level

5

SUBCELLULAR LOCATION: Plastid {ECO:0000269|PubMed:25997073}. Plastid, amyloplast {ECO:0000305}.

null

PF07859;

IPR013094;IPR029058;IPR050466;IPR033140;

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), Liliales (order), Liliaceae (family), Tulipa (genus)

TCEB1

false

186

A0A0J5ZXG5

MALADDLKKWVGETFTGKWEVQETTSVPNPEDLRLNSNHAKDLKAATVLYADLDGSTDMVNTKKWQFSAQIYKTFLKCASDIIRDEGGNITAYDGDRVMAVFTGNSKNTSAARCALKINSAVLDIIQPAIAKKWQTDFVLRHVVGIDTSQLRTARIGIRGDNDLVWIGRAANYAAKLTNLAGKPTRITADVYNKLADKLKYANGVDMWAPEHWDDMGIWTYTSTWKWTV

Uridylate cyclase (EC 4.6.1.26) (BcPycC) (Cyclic UMP synthase) (cUMP synthase)

Burkholderia cepacia (Pseudomonas cepacia)

292

229

25,594

3D-structure;Antiviral defense;Cytoplasm;Lyase;Manganese;Metal-binding;Nucleotide-binding

GO:0000166; GO:0004016; GO:0005737; GO:0009190; GO:0035556; GO:0046872; GO:0051607

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.

null

PF00211;

IPR001054;IPR029787;

7R65;

cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Burkholderiaceae (family), Burkholderia (genus), Burkholderia cepacia complex (no rank)

pycC VL15_12785

false

187

A0A0J9SZQ5

MKKSSKEISSSQSLKNGGSDHFFNTSLMYVLAACLASFIFGYQVSVLNTIKNFIVIEFGWCTGNKVECDDSTLKSSFLLASVFIGAVVGSGFSGYLVQHGRRFSLLVIYNFFILVSILTSITHHFHTILFSRLLSGFGIGLITVSVPMYISEMTHKDKKGAYGVLHQLFITFGIFVAVLLGMAMGEAPDAKSVDALGEFQKIWWRLMFFFPCLISILGIVLLTFFYKEETPYYLFENGKIEESKKILKKIYGTDNVDEPLKAIKDAVEQNEAAKKNSISLMRAMQIPSYRNVILLGCILSGLQQFTGINVLVSNSNELYKEFLSNKLITTLSVIMTVVNFLMTFPAIYIVEKLGRKTLLLCGCAGVICAFLPTAIANQIDSTSAFVKNLSIAATFVMIISFAVSYGPVLWIYLHEMFPSEIKDSAASLASLVNWVCAIIVVFPSDIIIKKSPTILFFIFSGMSILSFLFIFFFIKETKGGEIGTSPYITMEERQKHMGKSAV

Hexose transporter 1 (PvHT) (Facilitative hexose transporter)

Plasmodium vivax (strain Brazil I)

1,033,975

502

55,779

Cell membrane;Disulfide bond;Membrane;Sugar transport;Transmembrane;Transmembrane helix;Transport

GO:0005886; GO:0015149

Evidence at protein level

5

SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q7KWJ5}; Multi-pass membrane protein {ECO:0000255}.

null

TRANSMEM 27..47; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 77..97; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 103..123; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 133..153; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 164..184; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 206..226; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 292..312; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 330..350; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 357..377; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 391..411; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 428..448; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 454..474; /note="Helical"; /evidence="ECO:0000255"

PF00083;

IPR045263;IPR020846;IPR005828;IPR036259;IPR003663;IPR005829;

null

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

HT1 PVBG_05140

false

188

A0A0J9UMG2

MAMSLPQLGGAGGPHTQPSLPSLPAHLQSDTHLTAHLASRFHVSHPTARLSSHALISLNTYTNSSKGPDGGKEGSAMAGAEEIADRAFLRLGHRSENQAVVFLGESGAGKSTIRAHLLTALLNKSSTPLSTKLSLAAYVFDSLTTTKTATTPTASKSGLFYELQYDTSATTNPVLIGGKLLDHRLERSRIADVPTGERNFHVLYYLLAGTSEAEKSHLGLDGGSATGTTQKRWKYLGHPTQLKVGINDAEGFQVFKNALRKLEFPRAEIAEICQILASILHIGQLEFETTSQTSVTGDDSGGFSHEGGTTITAVKNKDVLSIIAAFLGVSAADLQTTLGYKTKMIHRERVTVMLDPNGARAHAGELARTLYSLLVAWILETINQRLCAPEESIANTVSIVDFPGFCQQTPTGSALDQLLNNAATECIYNLTLQNFFDRKADMLESEEVSVAATSYFDNSDAVRGILKPGNGLLSILDDQTRRNRTDMQFLEALRRRFDGKNAAIEVGSAQAKLPGSNFMTENTSAVFTVKHFAGEVDYPVKGLIEENGEIISGDLLNMINGTKSEFVARLFGQDALQTVTHPNERTTVMQATVSSKPMRAPSVMSRKTHRTGRPSTAYKRQQQEAMEELDQQSQAGESKKNAKMTLEQGASGQFLASLDNVQKAVTDPGTNSYFVFCLKPNDRRIANQFDSKCVRMQVQTFGIAEISQRLRSADFSLFLPFGEFLGMTDAETILVGSERERAEMVIEEKQWPQNEVRVGATGVFLSERCWMEIAQLGEAVSVSGRYGGLPSSDAGDGLTPAESMAFGASKEHLVSGGNTPLMYGEKAKGGYFTDDTRSEAGVSAFGGGDMFKNLDTREQMAERGNEKSLEEVEEYRDKPSRKRWVALVFFLTWFIPDFAIRLIGRMPRKDVRMAWREKVAINMLIWLMCAVAAFFMVGFPMLICPKQYVYSSNELSSYDGDKGSKGAYVAIRGFVIDLNAFIPNHYPGSNLVSEDTLLNYAGKDISALFPIQVSALCQGKDGQIPPEVTLDNRNTNITGQPQLLASRDIDVNSVYHDFRYFTNDSRPDWYFEQMYTFKHVYLKGRMGYSPKYVKKLARDSSWNVVTIHGKVYDMTKYLQGGLRLKAKAGKPTPNIPGATDFMEDSVVQLFRSAKGQDVSKYWDNIKLSPVKKQRMETCLNNLFYIGDSDTRNSTRCQFATYFILAISVMLASILVFKFLAALQFGGKNVPENLDKFVMCMIPAYTEDEDSLRRAIDSLSRMKYDDKRKLLVVVCDGMIIGQGNDRPTPRIVLDILGVSETVDPEPLSFESLGEGMKQHNMGKIYSGLYEVQGHIVPFMVIVKVGKPSEVSRPGNRGKRDSQMVLMRFLNRVHYNLAMSPMELEMYHQIRNIIGVNPTFYEYLFQIDADTVVAADSATRMISAFIDDTRLIACCGETALTNAKGSFITMIQVYEYWISHNLSKAFESLFGSVTCLPGCFSMYRIRAAETGKPLFVSKEIVEDYSTIRVDTLHMKNLLHLGEDRYLTTLLLKYHSKYKTKYLFSAQAWTIAPDSWSVFLSQRRRWINSTVHNLAELIPLAQLCGFCCFSMRFVVFIDLLSTIVQPVIVMYIVYLIYQVATNPSVVPITAFLLLGAIYGLQAVIFILRRKWEMVGWMIMYIAAIPVFSFGLPLYSFWHMDDFNWGNTRVIAGEAGKKIVVSDEGKFDPNSIPRKKWEEYQAELWETQTQTARDDVRSEISGYSYATKAQGPFSEYGGGYQPSRPGSTAGFGHQNMSRMSLAHSEMPGNRASQFGGSQFFSPEDLVGMPSDDALLAEIRDILKTADLMTVTKKGIKQELERRFNVPLDAKRAYINSATEALLSGQL

Chitin synthase V (EC 2.4.1.16) (Chitin-UDP acetyl-glucosaminyl transferase V) (Class-V chitin synthase V)

Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936) (Fusarium vascular wilt of tomato)

426,428

1,862

206,926

Actin-binding;ATP-binding;Cell membrane;Glycoprotein;Glycosyltransferase;Membrane;Motor protein;Myosin;Nucleotide-binding;Reference proteome;Transferase;Transmembrane;Transmembrane helix;Virulence

GO:0003774; GO:0003779; GO:0004100; GO:0005524; GO:0005886; GO:0006031; GO:0016459; GO:0030428; GO:0031505

Evidence at transcript level

5

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

null

TRANSMEM 884..904; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 923..943; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1202..1222; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1590..1610; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1623..1643; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1650..1670; /note="Helical"; /evidence="ECO:0000255"

PF03142;PF00173;PF08766;PF00063;

IPR004835;IPR001199;IPR036400;IPR014876;IPR036961;IPR001609;IPR036037;IPR029044;IPR027417;

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 oxysporum species complex (no rank), Fusarium oxysporum (species), Fusarium oxysporum f. sp. lycopersici (no rank)

chsV FOXG_04162

false

189

A0A0J9UVG7

MRLLRPTPRLSSIFSSKTATSNLRFFTAMAPHNDVGAFHEALRSSKRILALCGAGLSASSGLPTFRGAGGLWRNHDATSLATLSAFKNDPGLVWLFYNYRRHMCLRAEPNPAHYALAALAEKNKDFLCLTQNVDNLSQQAGHPQDQLRTLHGSLFDIKCTNCDWIQRGNYDDPFCPALAPASVDVEPGKPFPLLDASLPLDPISPDDIPKCPQCKIGFQRPGVVWFGENLDEVMMMGITNWLLEDKVDLMLVIGTSAQVYPAAGYIDKAKRKGARIAVINPEAENEEEMYKVKPGDFAFGKDAAEYLPLLLEPVIGKLETDKKERS

NAD-dependent protein deacylase SIR5 (EC 2.3.1.-) (FoSIR5) (NAD-dependent protein deacetylase SIR5) (EC 2.3.1.286) (Protein decrotonylase SIR5) (EC 2.3.1.-)

Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936) (Fusarium vascular wilt of tomato)

426,428

326

36,006

Chromatin regulator;Chromosome;Cytoplasm;Metal-binding;Mitochondrion;NAD;Nucleus;Reference proteome;Transferase;Transit peptide;Zinc

GO:0005634; GO:0005694; GO:0005739; GO:0005829; GO:0017136; GO:0036054; GO:0036055; GO:0046872; GO:0070403; GO:0160011; GO:0160012; GO:1901856

Evidence at protein level

5

SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:34927582}. Cytoplasm, cytosol {ECO:0000269|PubMed:34927582}. Nucleus {ECO:0000269|PubMed:34927582}. Chromosome {ECO:0000269|PubMed:34927582}.

null

PF02146;

IPR029035;IPR050134;IPR003000;IPR026591;IPR027546;IPR026590;

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 oxysporum species complex (no rank), Fusarium oxysporum (species), Fusarium oxysporum f. sp. lycopersici (no rank)

SIR5 FOXG_05932

false

190

A0A0J9X285

MRPTVLCFSGLDPSGGAGLQADIEAIGQSGAHAAIACTALTIQNSQQVFGFEATSKELLLAQANAVVGDLPIKCVKSGMLGTTDNIAALAEFLRAHPDYQYVLDPVLVANSGGSLGDQATLVKAFVELIPLATLITPNTVELRALTGVTDLDQATQKLFEMGAKAVLVKGGHEDTPDFIKNSLYIDGELAASSTCPRLEGEYHGSGCSLASFIAGRLALGDSLKIAVQHAETWLFGVLKNAETPVLNGQKIPKRF

Hydroxylmethylpyrimidine kinase (HMP kinase) (HMPK) (EC 2.7.1.49) (AbHMPK)

Acinetobacter baumannii (strain IS-123)

903,899

255

26,709

3D-structure;ATP-binding;Disulfide bond;Kinase;Nucleotide-binding;Thiamine biosynthesis;Transferase

GO:0005524; GO:0005829; GO:0008902; GO:0008972; GO:0009228; GO:0009229

Evidence at protein level

5

null

PF08543;

IPR004399;IPR013749;IPR029056;

4YL5;4YWR;

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)

ACINIS123_0279

false

191

A0A0K0JFP3

MLGLLTITSVFRNWRNSLQRKEDYDECHMRGINNENEISGKSEKNFKLDEPPISLETVMAEFKLSNETLRRMMAHMSRNMDKGLEGGPENSTISMLPSFVPELPNGTEEGRFIAMDLGGTNLRVMLMDIKPGEELKTEQFNTRIPNWAMRGTGEQLFDYITKCLAEFLIEKGIENDGLPVGFTFSYPCDQKSLRSATLLRWTKGFETTGVVGEDVVELLEQSIARRGDIKVEVVALINDTVGTMVAAAHESGGECHIGVIIATGTNASYMEDTSKIKYGLSKAIAAYNYPEMIIDTEWGGFGDRSEADYILTQYDKIVDSRSEHPGVNTFDKLVGGKCMGEVVRVVLEKLTRARVLFNGKGSDALFQQDSFPTKYISEILRDESGSYVHTRDILGELGIDHYSFSDMLLLREVCVVVSRRSANLGAAAIACVLNRVRKQNMVVGIDGSTYKYHPFFDFWVHDKLKELVDPGLKFKLLQTADGSGKGAALITAIVARLKKRNLKQQQQQQQQQQQHVTMVEQNVVEQIAETKGSREQFMNGNQKINLVTNDIPIYDSFNGDIENGVIHLSTDH

Hexokinase (BmHK) (EC 2.7.1.1)

Brugia malayi (Filarial nematode worm)

6,279

572

64,043

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

GO:0001678; GO:0004340; GO:0005524; GO:0005536; GO:0005739; GO:0005829; GO:0006006; GO:0006096; GO:0008865; GO:0019158; GO:0019318

Evidence at protein level

5

null

PF00349;PF03727;

IPR043129;IPR001312;IPR022673;IPR022672;

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), Brugia (genus)

Bm4678

false

192

A0A0K0MJN3

MCDQFVGTWKFLSSENFEDYMKELGVGFATRKMAGVAKPNVTISINGDVITIKTESTFKNTEVSFRLGEEFDETTADDRKTKNVITLDNGILNQVQKWDGKETVIKRKVMDGNLVVECTMNTVTSKRVYERA

Fatty acid-binding protein, adipocyte (Adipocyte lipid-binding protein) (ALBP) (Adipocyte-type fatty acid-binding protein) (AFABP) (Fatty acid-binding protein 4)

Pygoscelis papua (Gentoo penguin)

30,457

132

14,944

3D-structure;Cytoplasm;Lipid-binding;Nucleus;Transport

GO:0005324; GO:0005634; GO:0005737; GO:0015909; GO:0070538; GO:0070539; GO:0070540; GO:0071399

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04117}. Nucleus {ECO:0000250|UniProtKB:P04117}. Note=Depending on the nature of the ligand, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus. Subject to constitutive nuclear export. {ECO:0000250|UniProtKB:P04117}.

null

PF00061;

IPR012674;IPR000463;IPR031259;IPR000566;

5BVQ;5BVS;

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), Neoaves (clade), Aequornithes (clade), Sphenisciformes (order), Spheniscidae (family), Pygoscelis (genus)

FABP4

false

193

A0A0K0PU92

MSLEDSLRSLSLDYLNLLINGQAFSDVTFSVEGRLVHAHRCILAARSLFFRKFFCGGSDPSASSGLIDQTGIRVNPSGSPRSSNGVLVIPVNSVGYEVFLLLLQFLYSGQVSIVPQKHEARPNCGERGCWHTHCSSAVDLALDTLAAARYFGVEQLALLTQKQLASMVEKASIEDVMKVLLASRKQDMQQLWTTCSHLVAKSGLPPEVLAKHLPIEIVAKIEELRLKSSIARRSMMPHHHHHHHQHDLNAAADLEDQKIRRMRRALDSSDVELVKLMVMGEGLNLDEALALHYAVENCSREVVKALLELGAADVNYPAGPAGKTPLHIAAEMVSPDMVAVLLDHHADPNVRTVDNVTPLDILRTLTSDFLFKGAIPGLTHIEPNKLRLCLELVQSAALVLSREEGNANNNPPSSTTTTLPMYHHPMNDDHNSSSSSGNNHNIANLNLDSRLVYLNLGATVGSGQMSDDHGGRHGDPAMYHHSHHDY

BTB/POZ domain and ankyrin repeat-containing protein NBCL (NOOT-BOP-COCH-like protein) (LaNBCL) (Protein ABSCISSION DEFICIENT) (Protein DELAYED ABSCISSION) (Delabs) (Protein STIPULE DEFICIENT)

Lupinus angustifolius (Narrow-leaved blue lupine)

3,871

486

53,262

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 protein 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

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), genistoids sensu lato (clade), core genistoids (clade), Genisteae (tribe), Lupinus (genus)

NBCL ABS STIP TanjilG_11814

false

194

A0A0K0PVW1

MKSELIFLPVPAFGHLVGMVEMAKLFISRHENLSVTVLISKFFIDTGIDNYNKSLLAKPTPRLTIINLPEIDPQKYLLKPRCAIFPSLIENQKTHVRDVMSRMTQSESTRVVGLLADILFVDIFDIADEFNVPTYVYSPAGAGFLGLAFHLQTLNDDKKQDVTEFRNSDTELLVPSFANPVPAEFLPSIFLEKDGRHDVLLSLYWRCREAKGIIVNTFEELEPYAINSLRMDSMIPPIYPVGPILNLNGEGQNSDEAAVILGWLDDQPPSSVVFLCFGSFGSFPENQVKEIAMGLERSGHRFLWSLRPCISEGETTLQLKYSNLELPAGFLDRTSCVGKVIGWAPQMAILAHEAVGGFVSHCGWNSVLESVWYGMPVATWPMYGEQQLNAFEMVKELGLAVEIEVDYRNEYNKSDFIVKADEIETKIKKLMMDGKNSKIRKKVKEMKEKSRVAMSENGSSYTSLAKLFEEIM

UDP-glycosyltransferase 100 (UGTPg100) (EC 2.4.1.367)

Panax ginseng (Korean ginseng)

4,054

472

53,131

Glycosyltransferase;Hydrolase;Isoprene biosynthesis;Transferase

GO:0002238; GO:0016114; GO:0016787; GO:0035251

Evidence at protein level

5

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)

UGT100

false

195

A0A0K2JL82

MTRPPAPPPGAPGADELLDCGLLSPVRAGTPVEALVCDSAWLQAMLDAEAALTRAQARTGFLPAAAAEAITAAARADRIDLLAVARGARETANPVVGLVAALTAAVRRDDPAAAEYVHRGSTSQDVLDTGAMLVARRALRLIGDDLDRAADALAALAADHRDTPMAGRTLALHAVPTTFGLKAAGWLELVSEAAGRVARLRDGLPFSLGGAAGTLAGYFGDRTDRGDPAVLLDRLLDAYAAETGLARPVLPWHVLRTPVADLAAVLAFTAGALGKIAVDVQSLARTEVAEVAEPAVEGRGASSAMPHKRNPVLSTLIRSAALQVPALATGLTQCLVSEDERSAGAWHAEWQPLRECLRLTGGAARTAVELAAGLEVDAARMRANLDLTDGRIVSESVAVALTPLLGRQAAKELLTRAAFTAGHEGRTLGEVLGELPELDGVLPKERWEALLDPARATGVAGALVDGALARRRPPAR

Nitrosuccinate lyase (EC 4.3.99.5)

Streptomyces cremeus

66,881

476

49,261

3D-structure;Antibiotic biosynthesis;Lyase

GO:0016829; GO:0017000; GO:0019619

Evidence at protein level

5

null

PF10397;PF00206;

IPR019468;IPR024083;IPR000362;IPR022761;IPR008948;IPR012789;

5XNY;5XNZ;

cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Actinomycetota (phylum), Actinomycetes (class), Kitasatosporales (order), Streptomycetaceae (family), Streptomyces (genus)

creD

false

196

A0A0K2S4Q6

MTQRAGAAMLPSALLLLCVPGCLTVSGPSTVMGAVGESLSVQCRYEEKYKTFNKYWCRQPCLPIWHEMVETGGSEGVVRSDQVIITDHPGDLTFTVTLENLTADDAGKYRCGIATILQEDGLSGFLPDPFFQVQVLVSSASSTENSVKTPASPTRPSQCQGSLPSSTCFLLLPLLKVPLLLSILGAILWVNRPWRTPWTES

Protein CD300H (CD300 antigen-like family member H)

Homo sapiens (Human)

9,606

201

21,806

Alternative splicing;Disulfide bond;Glycoprotein;Immunoglobulin domain;Membrane;Reference proteome;Secreted;Signal;Transmembrane;Transmembrane helix

GO:0004888; GO:0005576; GO:0005886; GO:0007165; GO:0030593; GO:0045088

Evidence at protein level

5

SUBCELLULAR LOCATION: [Isoform 1]: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:26221034}.

SIGNAL 1..24; /evidence="ECO:0000255"

TRANSMEM 169..189; /note="Helical"; /evidence="ECO:0000255"

PF07686;

IPR050671;IPR007110;IPR036179;IPR013783;IPR003599;IPR013106;

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)

CD300H

false

197

A0A0K3AUE4

MGREYKFTGIAAKLNPLNCRLKLEIAEDLDERVPTTSTSCSVASVAAATATINTTAPTVLTKSELQKTLQKTSSSFSSSLATTTTTSSHLNAPVESMEGHSSLASYSHHHPSSSHHHHPGQQQSSSSSSSSHLQDFQSPPSASHPYYHQQQPQHQHQQAQQYGQATGSTNGGGQQQMTSMYGGNDYDQHQLHHQNQQHQASTSTQQFHHPQRPPPPQYDQPSSSTGSSLPPLHTVRYEQLPPPPSNQRTPTQQLQYPVKVVEAGGQAYAQQVQQAQQSNRSGAAGVNSALQPKPLPPLSSITSISSSAAGSSISAPSTSQPSTTSSLITSPPSTSSSSMAPRKTPPNASSSSLIKRQSQDVQEQQRVDFEVARNVSQIMSKNGLKVMHEPLLTGSLPQLAPLAPLPPPKSGVYQCPNCNRNLANARNLQRHRQTCGSAQHAAPQLAAMLQRSPPPCASAPPVAPPTAPSTSFQHHNSTGNLTLSYSSSSSRHQSSLYSPQLEHQDLVGNPNVMLSDGYEYKDDPMLYQGPSGLSDSIWSRDDSFHSEPPSASHDQLDMDHLGFPDPLQDPLHHLDSFDSADHRKETPRECHEPDELMTLDPTPPQCGSERFYGINIDDMPLSLDCDEPLMRSESASLSSSSQGRNTPAAVFTCEACKKSVSSERSLRRHYNTCKMFQTELAASGEERPPTTKRKPATKRPSKKKEASEGPEKNSAILAALRKEPAAPQQPQQLQFQQNYQPSPQFQAPYGGGSLPSISASWLHSASTSAAAAAPERSEMFTSPIVTSAPNPYIHQLPHQQPQQQKSSPLEDLLNEQDESADDDGDSRSSSGTVSNSTTTTTTATTTSSKSTGNPLFTCEHCARQLCSMSNLKRHRATCKVAASSSSNSAASRPPSQPSTPATAPATPMLQASQAPQPLQAPPQSPMETTATVTYTKTTVPPSVANTWNTEKAQLISPKPRSQTIFSEASSSMTVGDALRAQQHQQKMDQQIQIQFQQQQQQRFQHHQQQQQAGRIPPRPPNPILNQVQNPPQQVQHNQHQNQMLNPIRQPLLQSPPPPPPKKGLIEHKNTDLVLITSEPLAERMDAKRRSSEGLVAVTSTPLPPIQLPQRSQAPAPSRQQQQQPPVAYQVQFNGRPLPPMQLPPLQNPHNQQQQHQMLHQSQMNYQQVQQVQQVQHVQQQQNLQNQHHHQQQHHQQNQQQAPGNRSRSHSNVGKMEQEAQRQGSPLDSIITSVPLSIEVHHHIMKPGPLEQGQSSVDSQSTAEPSPRKASQQAYICPECKKTYASRKNVKRHRMAVHKLTLDEILANPEQPALDPLSAVGGAGRRHTVAGLETPDSALKPAPTKRKASEAPSAGVATKKGKAMAASVDEIQVKEEEEDQKEETVGSVERQEPPKKPVADDHKSAIAPLPPANTIMPPPPPYNQASAVPLNPPRTALPPLQLPPLQPLQSESPSWASMSAPPTALIPRTPRSSEFADEEDTRAMAKIAAELKRSAEDWPVLAVIEGVAAEPTNGEDIDEDEILIKRLRQGGVLEDVGDVSDLLRDVQGGVDGEPFSEDMLLEKNLSTASSVGLPSLASPGEQFGYQQYSQHPQQHPQQHPQQHPQQQQQVWNPNYEFQGYMQQQHPPMPVSQQFQQPLLQRPASQPPPARPIVKNSRRPSTTPKPPPNLTCSGCKKILGSDYSLRRHRAGCADVQQALNPEYPRPPKRKAAREAQKINEAEILASMPDPQMVAERSAAVAEAAAAEAAVERIGALPPPSVVHEIVHQVNADRQSMKKHNKTTSPPPAQEAPPTCAPDDPMSSSSSSSTSSASPLQGGAKPSTNQARHYCQFPECGKNFSSEWNLARHTRESCKMTTRAHSYEPTSAADKIDLIFMDKSKRRVSRTFLCTVSSLISYWLGEQGDRLELDTKWEHFQLLLDVHTLKVAITADNINLIAEQSKKYQLEHVIRMADQFMMNTNYTTPPTHVQL

Signal element on autosome protein 2

Caenorhabditis elegans

6,239

1,968

215,234

Alternative splicing;Cytoplasm;Differentiation;DNA-binding;Metal-binding;Nucleus;Reference proteome;Repeat;RNA-binding;Sexual differentiation;Transcription;Transcription regulation;Translation regulation;Zinc;Zinc-finger

GO:0003677; GO:0003713; GO:0003725; GO:0003727; GO:0005634; GO:0005737; GO:0006417; GO:0007548; GO:0007549; GO:0008270; GO:0008340; GO:0009408; GO:0010629; GO:0016592; GO:0030154; GO:0040034; GO:0045944

Evidence at protein level

5

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21471153, ECO:0000269|PubMed:23666922}. Cytoplasm {ECO:0000269|PubMed:21471153}. Note=In embryos, diffusely accumulates in the nucleus at the 20- to 30-cell stage, but nuclear localization decreases after the 200-cell stage (PubMed:23666922). Diffusely localized in the nucleus and cytoplasm during the L3 larval stage (PubMed:21471153). {ECO:0000269|PubMed:21471153, ECO:0000269|PubMed:23666922}.

null

PF00096;

IPR050888;IPR036236;IPR013087;

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), Rhabditina (suborder), Rhabditomorpha (infraorder), Rhabditoidea (superfamily), Rhabditidae (family), Peloderinae (subfamily), Caenorhabditis (genus)

sea-2 K10G6.3

false

198

A0A0K3AUJ9

MSLAPKMSKAFIGKPAPQFKTQAVVDGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAWINQPRKHGGLGEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQFVEKHGEVCPAGWTPGSDTIKPGVKESQEYFKKH

Peroxiredoxin prdx-2 (EC 1.11.1.24) (2-Cys peroxiredoxin 2)

Caenorhabditis elegans

6,239

201

22,413

Alternative splicing;Antioxidant;Cytoplasm;Disulfide bond;Oxidoreductase;Peroxidase;Redox-active center;Reference proteome

GO:0000122; GO:0005737; GO:0005829; GO:0006979; GO:0008340; GO:0008379; GO:0010038; GO:0010286; GO:0019430; GO:0042542; GO:0042744; GO:0045454; GO:0070301; GO:0090727; GO:1902882

Evidence at protein level

5

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19064914}.

null

PF10417;PF00578;

IPR000866;IPR050217;IPR024706;IPR019479;IPR036249;IPR013766;

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), Rhabditina (suborder), Rhabditomorpha (infraorder), Rhabditoidea (superfamily), Rhabditidae (family), Peloderinae (subfamily), Caenorhabditis (genus)

prdx-2 prx2 tag-56 F09E5.15

false

199

A0A0K3AV08

MEQASVPSYVNIPPIAKTRSTSHLAPTPEHHRSVSYEDTTTASTSTDSVPEVRIRSESSQVSRESPPIRASKAFVASYEYEAQKDDELNLPLGAIITLVTVETNEDGWYRGELNGKVGLFPSNYAREVTYKDNLVEFKQDEIMLPVAVRTLSDCQIGHGATATVFKMDIKIKKELQNGRMGEAVGDQMKAALKRFNRHASNFRADVVSTDEQLEQLKREANLVNGLSHNNIVRLLGICLEDPYFGLLLELCEGSSLRNVCRNLNSDAAIPLGVLIDWATQVAEGMEYLTKQGYVHRDLKADNVLVKEEVCLCMDEEMFQYAYCLKCGKRPFDKLQLKITDFGVTRKMTADANRFSTAGTYAWLAPEAFKEGTWSEASDVWSYGVVLWELLTREEPYQGHIPATIAFQIANKGQNLSIGDSCPDRWKKLMQDCWNLEPNFRPKFSTLAISFKQYAKEFKDTHLQRAPSKMAVKELYSECFADKTKEEFEKRFHDLYAGSGDINRKNRHSIAPETKARRLKHHKPKKADITGPTEVKHILSVQKDDKNFRVKTYDQSSTGGTLPRLNERQSTLSLSSPDLFHISNLISGSNTVGHSAHRISRKNAIRHKKNQHRMFESPVVSPTMDDSNTFSTIDNADEVDPNHSKESKKGGTLSRAWAKLPWNKRDSKEDHDERAVAGSISSRSSSTTSSNRLITGQTTRGASAAGLLEIGARSRAQSTADGWEDPNTTKKHKVSPSDKRPVKTTNQTERYVKDLEKDTPLRPAQLPPTHRKSALDQTIPASPNSPDSINNFHPMPLSSRRTTANSSSDGAPCYDALVSHSYGAGHGHKNHFGLSDTIPLFPEEPTHYDMGPGRPFGTNGRAIVNQGGDYYGNISGQNYEGFGHGRSINQSTQYYPVGGGCDDYIPIVQKTVIKPTVGEVGNSPYSENIRCATRNVQNPQYIQCKKNQNPRRIPALPMKIQSESNLVTSGMVFTPRDEQLNGIGNSLSSLSLNEPPDIPAPLPPVVTYPIPASLISPSNRVSMSPPTRMAPVLPLGAMSSPRIMDKEILKNSSVEGTEIY

Mitogen-activated protein kinase kinase kinase mlk-1 (EC 2.7.11.25) (Mixed lineage kinase homolog 1)

Caenorhabditis elegans

6,239

1,059

117,635

Alternative splicing;ATP-binding;Coiled coil;Kinase;Magnesium;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;SH3 domain;Stress response;Transferase;Ubl conjugation

GO:0000165; GO:0001934; GO:0004672; GO:0004709; GO:0005080; GO:0005524; GO:0005737; GO:0007165; GO:0007254; GO:0008340; GO:0019901; GO:0030971; GO:0031103; GO:0038066; GO:0042594; GO:0046688; GO:0046872; GO:0048680; GO:0048691; GO:0050829; GO:0097110; GO:0106310

Evidence at protein level

5

null

PF07714;PF14604;

IPR011009;IPR000719;IPR050122;IPR001245;IPR008271;IPR036028;IPR001452;

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), Rhabditina (suborder), Rhabditomorpha (infraorder), Rhabditoidea (superfamily), Rhabditidae (family), Peloderinae (subfamily), Caenorhabditis (genus)

mlk-1 K11D12.10

false