Annotation Vocabulary
Collection
15 items • Updated
Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 127 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 10.5k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.89k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.55k ⌀ | Pfam stringlengths 8 224 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 9.11k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 65 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.7k ⌀ | Organism stringlengths 8 196 | av_tokens listlengths 0 247 | av_text listlengths 0 247 | av_provenance listlengths 0 247 | nl_text stringlengths 42 15.3k |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
A0A009IHW8 | ABTIR_ACIB9 | MSLEQKKGADIISKILQIQNSIGKTTSPSTLKTKLSEISRKEQENARIQSKLSDLQKKKIDIDNKLLKEKQNLIKEEILERKKLEVLTKKQQKDEIEHQKKLKREIDAIKASTQYITDVSISSYNNTIPETEPEYDLFISHASEDKEDFVRPLAETLQQLGVNVWYDEFTLKVGDSLRQKIDSGLRNSKYGTVVLSTDFIKKDWTNYELDGLVAREMNGHKMILPIWHKITKNDVLDYSPNLADKVALNTSVNSIEEIAHQLADVILNR | 3.2.2.-; 3.2.2.6 | null | NAD+ catabolic process [GO:0019677]; signal transduction [GO:0007165] | null | NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleosidase activity, cyclic ADP-ribose generating [GO:0061809]; NADP+ nucleosidase activity [GO:0050135] | PF13676; | 3.40.50.10140; | null | null | null | CATALYTIC ACTIVITY: Reaction=NAD(+) = 2'cADPR + nicotinamide + H(+); Xref=Rhea:RHEA:75299, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:194248; Evidence={ECO:0000269|PubMed:36048923}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75300; Evidence={ECO:0000269|PubMed:36048923}; CATALYTIC AC... | null | null | null | null | FUNCTION: NAD(+) hydrolase (NADase) that catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide (PubMed:29395922). In addition to ADPR, also generates a cyclization variant of cyclic ADPR (cADPR), termed 2'cADPR (v-cADPR) (PubMed:29395922, PubMed:36048923). Cleaves NADP(+), but does not cyclize the prod... | Acinetobacter baumannii (strain 1295743) | [
259,
1285,
2363,
7667,
9078,
9193,
9507,
16168,
20078,
20137,
23699
] | [
"ec: EC 3.2.2.6",
"go_bp: signal transduction (GO:0007165)",
"go_bp: NAD+ catabolic process (GO:0019677)",
"go_mf: NAD+ nucleosidase activity (GO:0003953)",
"go_mf: NADP+ nucleosidase activity (GO:0050135)",
"go_mf: NAD+ nucleosidase activity, cyclic ADP-ribose generating (GO:0061809)",
"interpro: Toll/... | [
"UniProtKB=ECO:0000269",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000269",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000269",
"UniProtKB=ECO:0000269",
"InterPro=match:Pfam"
] | Function: NAD(+) hydrolase (NADase) that catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide. In addition to ADPR, also generates a cyclization variant of cyclic ADPR (cADPR), termed 2'cADPR (v-cADPR). Cleaves NADP(+), but does not cyclize the product.
Catalytic Activity: NAD(+) = 2'cADPR + nicotinam... |
A0A011QK89 | L2HDH_ACCRE | MESIEAVVIGAGVVGLACARELARRGFETVILERHGAFGTETSARNSEVIHAGLYYPTDSLKARLCVAGRQQLYAFCATHAISHQRCGKLVVATSPAQESRLAALQKQGEANGVDDLQRLSAAEARALEPGLACTAALLSPSTGIVDSHGLMLALLGDAETAGAALALHSPLLRGSLDANTPGIVLESGGADGLRFKARRVINAAGLWAPQVAASLAGFPRTLIPANFHAKGSYYALTGRTPFSRLVYPLPEAGGLGVHLTLDLGGQARFGPDVEWLPDPTPGQPIDEPDYRVDPARADAFYAEIRRYWPALPDAALTPA... | 1.1.99.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q9H9P8}; | null | null | (S)-2-hydroxyglutarate dehydrogenase activity [GO:0047545] | PF01266; | 3.30.9.10;3.50.50.60; | L2HGDH family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2; Xref=Rhea:RHEA:21252, ChEBI:CHEBI:13193, ChEBI:CHEBI:16782, ChEBI:CHEBI:16810, ChEBI:CHEBI:17499; EC=1.1.99.2; Evidence={ECO:0000250|UniProtKB:S2DJ52}; | null | null | null | null | FUNCTION: Catalyzes the dehydrogenation of L-2-hydroxyglutarate (L2HG or(S)-2-hydroxyglutarate) to 2-oxoglutarate (alpha-ketoglutarate) (By similarity). Also displays some oxidase activity in vitro on L-2-hydroxyglutarate with O2 as the electron acceptor, but this activity is most likely not physiological (PubMed:34555... | Accumulibacter regalis | [
9050,
11702,
16307,
19943,
21445
] | [
"go_mf: (S)-2-hydroxyglutarate dehydrogenase activity (GO:0047545)",
"interpro: FAD dependent oxidoreductase (IPR006076)",
"interpro: FAD/NAD(P)-binding domain superfamily (IPR036188)",
"cofactor: FAD (CHEBI:57692)",
"pfam: DAO (PF01266)"
] | [
"UniProtKB-GO=ECO:0000250",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000250",
"InterPro=match:Pfam"
] | Function: Catalyzes the dehydrogenation of L-2-hydroxyglutarate (L2HG or(S)-2-hydroxyglutarate) to 2-oxoglutarate (alpha-ketoglutarate) (By similarity). Also displays some oxidase activity in vitro on L-2-hydroxyglutarate with O2 as the electron acceptor, but this activity is most likely not physiological.
Catalytic Ac... |
A0A017SE81 | FOGD_ASPRC | MSTKFALVTGCGQGGIGEALITEYARRGIHAIATVLPAEPSDHLARAGITFFPLDVTNEESVLELKARVQKLTGGRLDVLVNCAGIAYTMTAIDTDVAAVQRMFNVNVFGPMRMVHHFHDMIIKATGAIVNIGSIGGVVPYLYGSSYNATKAALQHWSNTLRVEMAPFDVRVITVISGEVATNILKNDAHRRLPEGSYYSPLAENFRQHVTRTPPRTTDRFQYAANVVAESLRSSPSAWFWYGSQSTLIRFLDMFCWRTVWDSLFWRMFDLGKLKEAHSSKAKKQV | 1.1.1.- | null | phosphatidic acid biosynthetic process [GO:0006654]; secondary metabolite biosynthetic process [GO:0044550]; triglyceride catabolic process [GO:0019433] | endoplasmic reticulum [GO:0005783]; lipid droplet [GO:0005811] | acylglycerone-phosphate reductase (NADP+) activity [GO:0000140]; triacylglycerol lipase activity [GO:0004806] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:32134669}. | null | null | FUNCTION: Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain (PubMed:32134669). The PKS fogA releases the c... | Aspergillus ruber (strain CBS 135680) | [
1075,
2346,
3796,
6563,
6578,
7995,
10628,
14539,
16354,
20610
] | [
"go_bp: phosphatidic acid biosynthetic process (GO:0006654)",
"go_bp: triglyceride catabolic process (GO:0019433)",
"go_bp: secondary metabolite biosynthetic process (GO:0044550)",
"go_cc: endoplasmic reticulum (GO:0005783)",
"go_cc: lipid droplet (GO:0005811)",
"go_mf: triacylglycerol lipase activity (GO... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam"
] | Function: Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. The PKS fogA releases the carboxylic acid (8E... |
A0A017SE85 | FOGI_ASPRC | MDGKTYKLRASCNACNESKVRCSQTKPTCARCERNKTTCVYGLSRRTHKDAPPISLSHSHSHSHSGSQPHSHSGSRRSSVHIPNATATANATTTANYTSTTTPFMPLHENSMTSYPPQPSVDQFFAQQQPHHQQPSTAGPGPGILSPANLDLPSFMTPLPTPNEDHTNSLFSSFGNFAAGVGGVNGSVNNILTPLTGSPGTGTSASTSTDMFQQPQVQECTCHAGVMEQMASMSQPSRNEERRLSLDVQLSQLKRCIIASEASMGCGHHGNGDSEPINIISVAMLIGRIIDEFELMLNERIGRGTTMPERERSLSLDEAT... | null | null | null | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; zinc ion binding [GO:0008270] | PF00172; | 4.10.240.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}. | null | null | null | null | null | FUNCTION: Transcriptional regulator that positively regulates the expression of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. {ECO:00002... | Aspergillus ruber (strain CBS 135680) | [
6494,
7541,
8242,
10010,
16601,
20671,
24954
] | [
"go_cc: nucleus (GO:0005634)",
"go_mf: DNA-binding transcription factor activity, RNA polymerase II-specific (GO:0000981)",
"go_mf: zinc ion binding (GO:0008270)",
"interpro: Zn(2)Cys(6) fungal-type DNA-binding domain (IPR001138)",
"interpro: Zn(2)-C6 fungal-type DNA-binding domain superfamily (IPR036864)",... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000255"
] | Function: Transcriptional regulator that positively regulates the expression of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain.
Subcellula... |
A0A017SEF3 | FOGH_ASPRC | MALQTTNTWETLAQLLPSRNHDQDFWWKVTGRQLAVLLEAAGYPIERQYNTLLFHYHWAIPYLGPAPASGVAKWPSQLSVDGSPIEYSWKWNTKSKAPDVRYTMEPMSEFTGTKLDPLNQRAFRELLHKLSQFVPDVDLAPTDYFMSTLFDHDRSVLMKAVDDGVPLQFSSTALAFEFLDKGLLLKTYYAPRKLETGHFVLKDWDTAIRGYYPESKALDIVYEFLKTSPEGELMNPYHLAVDNVKDGRLKFYFQSPHRTFTSVREILTIGGRVQREGLEEQLLSLRDLLNALTGQSPDFPEDGEPPIVEEDVTADLDTDG... | 2.5.1.- | null | alkaloid metabolic process [GO:0009820] | null | prenyltransferase activity [GO:0004659] | PF11991; | null | Tryptophan dimethylallyltransferase family | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.07 mM for violaceoid C {ECO:0000269|PubMed:32134669}; KM=0.09 mM for 2-heptyl-1-(hydroxymethyl)cyclohexa-2,5-diene-3,6-dione {ECO:0000269|PubMed:32134669}; | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:32134669}. | null | null | FUNCTION: Prenyltransferase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain (PubMed:32134669). The PKS fogA releases the carboxyli... | Aspergillus ruber (strain CBS 135680) | [
1741,
7925,
13887,
15962,
23484
] | [
"go_bp: alkaloid metabolic process (GO:0009820)",
"go_mf: prenyltransferase activity (GO:0004659)",
"interpro: Aromatic prenyltransferase, NscD-like (IPR017795)",
"interpro: Aromatic prenyltransferase (IPR033964)",
"pfam: Trp_DMAT (PF11991)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam"
] | Function: Prenyltransferase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. The PKS fogA releases the carboxylic acid (8E,10E,12E... |
A0A017SEX7 | FOGA_ASPRC | MNDDPPCIVGMACRLPGDVRSPSQLWDLVINQKTGQGPTPPIRYNVDGYYHPDGNRSGGINVPGGYFINEDIRQFDNGFFGINNLEATYMDPQQRKLLEVVFECFESTGASMKSMSGSNTGVYVGNFSVDYQPMQTRDADYLHRYTSTGSGATIMSNRISHVFNLHGPSFTLDTACSSSVYALHQALTAIKVGDCESAVVASANLIMSPELHIGAAKSGVLSPTGTCHTFDASADGYGRAEGVNAIYVKRLSAALRDGNQIRAIVRGSAVNANGRTPGIALPSGNLQEAVMRKAYQNAGLDFAETDYVECHGTGTPVGDP... | 2.3.1.- | COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000255|PROSITE-ProRule:PRU00258}; | fatty acid biosynthetic process [GO:0006633]; lactone biosynthetic process [GO:1901336]; secondary metabolite biosynthetic process [GO:0044550] | null | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; oxidoreductase activity [GO:0016491] | PF00698;PF08240;PF13602;PF16197;PF00109;PF02801;PF08659;PF23114;PF21089;PF14765; | 3.40.47.10;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110; | null | null | null | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:32134669}. | null | null | FUNCTION: Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain (PubMed:32134669). FogA releases the... | Aspergillus ruber (strain CBS 135680) | [
1065,
3796,
7782,
8506,
10053,
12505,
12707,
13115,
13321,
13346,
13347,
13354,
13629,
13630,
13632,
14070,
14511,
14512,
15805,
16354,
16550,
17489,
18403,
18428,
19612,
19938,
20613,
21086,
22030,
23079,
23199,
23953
] | [
"go_bp: fatty acid biosynthetic process (GO:0006633)",
"go_bp: secondary metabolite biosynthetic process (GO:0044550)",
"go_mf: 3-oxoacyl-[acyl-carrier-protein] synthase activity (GO:0004315)",
"go_mf: oxidoreductase activity (GO:0016491)",
"interpro: Acyl transferase domain superfamily (IPR001227)",
"int... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match"... | Function: Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. FogA releases the carboxylic acid (... |
A0A017SEY2 | FOGG_ASPRC | MAVTFDISPEKEAGVLRLFHSQLFVTPPPLTRRDVDLSGKTAIVTGANGGLGLETAHQLLDLGCKVILAVRRVERGEAARQKLLEGRDAQATEIEVWPLDLSSYESVVGFAERAKTLSRLDIAILNAGLYKVNQTMTASTGYEESIHVNYLANALLITLLAPIFKNKKTGNTPGRIVLVSSDLAAWAKFKERKSNPILPTFKQKMTPKWDYLERYGTSKVLGQFFVTELAKRVSPDAVLVTTTNCGLCHGSELSREGQGHLIGYVFNVVSRLFGRSCSVGARVFVHAAANPVLGASVHGQYVEDAKLKPMSPLIYKPGDL... | 1.1.1.- | null | null | null | null | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:32134669}. | null | null | FUNCTION: Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain (PubMed:32134669). The PKS fogA releases the c... | Aspergillus ruber (strain CBS 135680) | [
10628,
16354,
20610
] | [
"interpro: Short-chain dehydrogenase/reductase SDR (IPR002347)",
"interpro: NAD(P)-binding domain superfamily (IPR036291)",
"pfam: adh_short (PF00106)"
] | [
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam"
] | Function: Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. The PKS fogA releases the carboxylic acid (8E... |
A0A017SFB8 | FOGE_ASPRC | MITASSAILLVALIAALWRLSLIGQRPKDYPPGPPTLPILGNLHQIPKARRHIQFEKWARQYGPVYSLILGTKVMIVLNTEDAIRELVDKRGAIYASRPESFIAQDTISGGLRILWMHNGETWKMVRKLAHRILNITTARTYVPYQDLETKRMLVDFLEKPDSFIEHMRRFSTSLTTQMTFGFRTTTIHDPRFKESFDIFDESWELVASPVAALMDFFPFLRKIPDFLLPVKREAKKLHQREITLFRDHYFETRRKLQDGTAKPCVCVDLMKLQKEESFSDNLAAYIGGSLLQAGSETTAGVLVGFIQAITIFPSVAKIA... | 1.-.-.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | null | membrane [GO:0016020] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:32134669}. | null | null | FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain (PubMed:32134669). The PKS fogA releases t... | Aspergillus ruber (strain CBS 135680) | [
6727,
7856,
8157,
8525,
8657,
10002,
10647,
16401,
19936,
20574,
24930,
25105
] | [
"go_cc: membrane (GO:0016020)",
"go_mf: monooxygenase activity (GO:0004497)",
"go_mf: iron ion binding (GO:0005506)",
"go_mf: oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen (GO:0016705)",
"go_mf: heme binding (GO:0020037)",
"interpro: Cytochrome P450 ... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000250",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. The PKS fogA releases the carboxylic acid... |
A0A017SGC7 | FOGF_ASPRC | MRRNILTALACSWLTAHAASVDLKSLLLESDIQWASDTVISFSDTPEFEDATVRWNSYNAPTYAGAISPADEEDVVKVVKLAKEHNVPFLATGGRHGCTDMVGLQEGLAIDLSQINSYEVDSDDATVTVGAGSTFGQFQNAIHDAGFMIQSGSVTCPGFIGITLGGGIGRYTGIFGLEIDALISARIVTADGEVLTISETENAELFWGVRGAGFNFGIVTSATYKLHKLADNNNGEILTADFIIPANKTLFYFDWLESLGETMPPNAAGVSRFQFDSIAKEGQIGANWVFIGPEDEGREFLSPILDLQPSVAMLSYVPWN... | 1.-.-.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q5BEJ5}; | null | null | FAD binding [GO:0071949]; oxidoreductase activity [GO:0016491] | PF08031;PF01565; | 3.30.465.10;3.40.462.20; | Oxygen-dependent FAD-linked oxidoreductase family | null | null | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:32134669}. | null | null | FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain (PubMed:32134669). The PKS fogA releases the c... | Aspergillus ruber (strain CBS 135680) | [
8506,
9248,
11713,
13034,
13688,
13690,
16364,
18616,
19943,
21598,
23036
] | [
"go_mf: oxidoreductase activity (GO:0016491)",
"go_mf: FAD binding (GO:0071949)",
"interpro: FAD linked oxidase, N-terminal (IPR006094)",
"interpro: Berberine/berberine-like (IPR012951)",
"interpro: FAD-binding domain, PCMH-type (IPR016166)",
"interpro: FAD-binding, type PCMH, subdomain 2 (IPR016169)",
... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000250",
"InterPro=match:Pfam",
"InterPro=match:Pfam"
] | Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. The PKS fogA releases the carboxylic acid (8E... |
A0A017SP50 | ECPT1_ASPRC | MPSEVLTSYYDYPTHDQEAWWRDTGPLFGRFLKGAGYDVHTQYQYLVFFIKNILPSLGPYPARWRSTITPTGLPIEYSLNFQLNSRPLLRIGFEPLSRFSGTPQDPYNKIAAADLLNQLSKLQLHEFDTQLFNHFTNEFELSKSESESLQKQGGINGKSTVRSQTAFGFDLKGGRVAVKGYAFAGLKNRATGTPVGQLISNSIRNLEPQMHCWDSFSILNSYMEESDGWNEYSFVSWDCVDIERSRLKLYGVHNAVTWDKVKEMWTLGGRIENNATIKTGLELLQHMWSLLQINEGDRDYKGGFAADNGGKTLPIIWNYE... | 2.5.1.- | null | alkaloid metabolic process [GO:0009820] | null | transferase activity, transferring alkyl or aryl (other than methyl) groups [GO:0016765] | PF11991; | null | Tryptophan dimethylallyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=cyclo(L-tryptophyl-L-alanyl) + dimethylallyl diphosphate = preechinulin + diphosphate; Xref=Rhea:RHEA:73767, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:193002, ChEBI:CHEBI:193003; Evidence={ECO:0000269|PubMed:29072465, ECO:0000269|PubMed:33381959}; PhysiologicalDirection=left-to-righ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.09 mM for cyclo-L-Trp-L-Ala {ECO:0000269|PubMed:29072465}; KM=0.18 mM for dimethylallyl diphosphate (DMAPP) {ECO:0000269|PubMed:29072465}; | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:29072465, ECO:0000269|PubMed:33381959}.; PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:29072465, ECO:0000269|PubMed:33381959}. | null | null | FUNCTION: Prenyltransferase; part of the gene cluster that mediates the biosynthesis of echinulin family alkaloid (PubMed:29072465, PubMed:33381959). The pathway begins with the biosynthesis of the cyclic dipeptide cyclo-L-Trp-L-Ala (cyclo-TA) by the NRPS echPS via condensation of L-alanine and L-tryptophan (By similar... | Aspergillus ruber (strain CBS 135680) | [
1741,
8537,
13887,
15962,
23484
] | [
"go_bp: alkaloid metabolic process (GO:0009820)",
"go_mf: transferase activity, transferring alkyl or aryl (other than methyl) groups (GO:0016765)",
"interpro: Aromatic prenyltransferase, NscD-like (IPR017795)",
"interpro: Aromatic prenyltransferase (IPR033964)",
"pfam: Trp_DMAT (PF11991)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam"
] | Function: Prenyltransferase; part of the gene cluster that mediates the biosynthesis of echinulin family alkaloid. The pathway begins with the biosynthesis of the cyclic dipeptide cyclo-L-Trp-L-Ala (cyclo-TA) by the NRPS echPS via condensation of L-alanine and L-tryptophan (By similarity). The prenyltransferase echPT1 ... |
A0A017SPL2 | ECPT2_ASPRC | MQPYHTLSRVLPFPDANQKAWWDKLGPMLLKAMQSQGYDTEAQYAQLGMVYKCVLPYLGEFPTVENDATRWKSFLCPYGIPIEPSLNISQGILRYAFEPIGPDVGTEKDPQNMNIIQDCLKGLTQHDDRIDTTLHAEFSSRLLLTEEESRQFATTGQFNFGPGQGMHGFAVDLKGSRPMFKGYFCAGIKSVVTGIPTGKLMLDAVREVDTEGRITQPLDKLEEYSANGIGKLMLCFMSVDMVNPHDARIKMYGLQQEVSREGIVDLWTLGGRVNTPTNQEGLELLLELWDLLQIPAGPRSVAISHCSVGQPPEYMLPTLV... | 2.5.1.- | null | alkaloid metabolic process [GO:0009820] | null | transferase activity, transferring alkyl or aryl (other than methyl) groups [GO:0016765] | PF11991; | null | Tryptophan dimethylallyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=preechinulin + dimethylallyl diphosphate = tardioxopiperazine B + diphosphate; Xref=Rhea:RHEA:73775, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:193003, ChEBI:CHEBI:193006; Evidence={ECO:0000269|PubMed:29072465, ECO:0000269|PubMed:33381959}; PhysiologicalDirection=left-to-right; Xref=... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.03 mM for preechinulin {ECO:0000269|PubMed:29072465}; KM=0.1 mM for dimethylallyl diphosphate (DMAPP) {ECO:0000269|PubMed:29072465}; Vmax=356 nmol/min/mg enzyme towards preechinulin {ECO:0000269|PubMed:33381959}; | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:29072465, ECO:0000269|PubMed:33381959}.; PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:29072465, ECO:0000269|PubMed:33381959}. | null | null | FUNCTION: Prenyltransferase; part of the gene cluster that mediates the biosynthesis of echinulin family alkaloid (PubMed:29072465, PubMed:33381959). The pathway begins with the biosynthesis of the cyclic dipeptide cyclo-L-Trp-L-Ala (cyclo-TA) by the NRPS echPS via condensation of L-alanine and L-tryptophan (By similar... | Aspergillus ruber (strain CBS 135680) | [
1741,
8537,
13887,
15962,
23484
] | [
"go_bp: alkaloid metabolic process (GO:0009820)",
"go_mf: transferase activity, transferring alkyl or aryl (other than methyl) groups (GO:0016765)",
"interpro: Aromatic prenyltransferase, NscD-like (IPR017795)",
"interpro: Aromatic prenyltransferase (IPR033964)",
"pfam: Trp_DMAT (PF11991)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam"
] | Function: Prenyltransferase; part of the gene cluster that mediates the biosynthesis of echinulin family alkaloid. The pathway begins with the biosynthesis of the cyclic dipeptide cyclo-L-Trp-L-Ala (cyclo-TA) by the NRPS echPS via condensation of L-alanine and L-tryptophan (By similarity). The prenyltransferase echPT1 ... |
A0A017SQ41 | ECHPS_ASPRC | MGSIESDSVLSFFSQRCCQNPDNTAIDDGPNGKLSYSQLDQQSSALAYCLQQNGITAGQVIPLLTTSRLEMVIAVLGILKAGGVYVPIDVDQWPADRINYVLSRTCSGLVVYTGDNIPSGVSLEEECRTVQVQIWPESALETQYEPNRRPQLMCIIFTSGTTDKPKGVMIPHSSVARFVTSPGFNYDIVPGDRLLLVLSVAFDGMGTLFNTICNGGTVILANRLNFQERSRQCTVLVVTPSILDVLSPPQSPSDYPSLERIFLGGETPSQQLLEAWSAFNDVALWIAYGPTEATCAVLSGRLQASSETGKFHPTRLGHCI... | 6.3.2.- | COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000255|PROSITE-ProRule:PRU00258}; | amino acid activation for nonribosomal peptide biosynthetic process [GO:0043041]; secondary metabolite biosynthetic process [GO:0044550] | cytoplasm [GO:0005737] | catalytic activity [GO:0003824]; phosphopantetheine binding [GO:0031177] | PF00501;PF00668;PF00550; | 3.30.300.30;1.10.1200.10;3.30.559.10;3.40.50.12780;3.30.559.30; | NRP synthetase family | null | null | CATALYTIC ACTIVITY: Reaction=L-tryptophan + L-alanine + 2 ATP = cyclo(L-tryptophyl-L-alanyl) + 2 ADP + 2 phosphate + 2 H(+); Xref=Rhea:RHEA:73763, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57912, ChEBI:CHEBI:57972, ChEBI:CHEBI:193002, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:A0A1E3... | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000250|UniProtKB:A0A1E3B0T2}.; PATHWAY: Alkaloid biosynthesis. {ECO:0000250|UniProtKB:A0A1E3B0T2}. | null | null | FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of echinulin family alkaloid (PubMed:29072465, PubMed:33381959). The pathway begins with the biosynthesis of the cyclic dipeptide cyclo-L-Trp-L-Ala (cyclo-TA) by the NRPS echPS via condensation of L-alanine and L-tryptoph... | Aspergillus ruber (strain CBS 135680) | [
3796,
6538,
7628,
9863,
10062,
11759,
12505,
14513,
14804,
16550,
17485,
18019,
19938,
20939,
20970,
21063
] | [
"go_bp: secondary metabolite biosynthetic process (GO:0044550)",
"go_cc: cytoplasm (GO:0005737)",
"go_mf: catalytic activity (GO:0003824)",
"interpro: AMP-dependent synthetase/ligase domain (IPR000873)",
"interpro: Condensation domain (IPR001242)",
"interpro: Phosphopantetheine attachment site (IPR006162)... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000255",
"InterPro=match:Pfa... | Function: Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of echinulin family alkaloid. The pathway begins with the biosynthesis of the cyclic dipeptide cyclo-L-Trp-L-Ala (cyclo-TA) by the NRPS echPS via condensation of L-alanine and L-tryptophan (By similarity). The prenyltrans... |
A0A017SR40 | EP450_ASPRC | MWDSPIIFTTMRELVQSVSPAALSWAVVAIYLGTFFWLRSRSSKQRLPLPPGPRGLPLIGNSLQTPAVNPWEKYKEWSDEYGPVMTLSLGLTTTIILSSHQVANDLMEKKSTIYSSRPQLVMFNRLSGGMNSSGMEYGKRWRDHRSLQASVLRPWMTQRYTALRDVETKQLLAELLNTDDFSSCFKRMVASLFMTLAYGKRVQYPDDPEIRGMEELVRVKSEAGEASFRATGQLVEYIPLLQYLPSFLTPWKEMCDRICEQFNKTFVDRLRDGINAPAWTWAKEVSKHKVARPMSELEISYTLGTLYEASLTSQQILRII... | 1.-.-.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | null | membrane [GO:0016020] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=preechinulin + reduced [NADPH--hemoprotein reductase] + O2 = neoechinulin A + oxidized [NADPH--hemoprotein reductase] + 2 H2O + H(+); Xref=Rhea:RHEA:73771, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:582... | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:33381959}.; PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:33381959}. | null | null | FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of echinulin family alkaloid (PubMed:29072465, PubMed:33381959). The pathway begins with the biosynthesis of the cyclic dipeptide cyclo-L-Trp-L-Ala (cyclo-TA) by the NRPS echPS via condensation of L-alanine and L-tryptophan... | Aspergillus ruber (strain CBS 135680) | [
6727,
7856,
8157,
8525,
8657,
10002,
10647,
13954,
16401,
19936,
20574,
24930,
25105
] | [
"go_cc: membrane (GO:0016020)",
"go_mf: monooxygenase activity (GO:0004497)",
"go_mf: iron ion binding (GO:0005506)",
"go_mf: oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen (GO:0016705)",
"go_mf: heme binding (GO:0020037)",
"interpro: Cytochrome P450 ... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000250",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000255",
"UniPro... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of echinulin family alkaloid. The pathway begins with the biosynthesis of the cyclic dipeptide cyclo-L-Trp-L-Ala (cyclo-TA) by the NRPS echPS via condensation of L-alanine and L-tryptophan (By similarity). The prenyltransfe... |
A0A017TC06 | FDBR_CHOA4 | MIDASSLKALVRRAEGGLVEALGLRPLQLDPEATHAVGTYRGRAVTLETRAYRGQPLHYARFVEITGEGLAIGNMLCTPCVDHPLPILGVDLVMLGDTLMLVADLSPTLPPGKEREAQLAPLDAACAARSSTLPPGGALPAWCTAWFSPFALYTRVAGADLARAASACDDLVRVHVSLCTASAPAPQHRLGTARAVEGYAAAHREHDKGLRMLAKLFGEGWAARYIAETLFPALLTMGEAPEVPVAPEAPTSAPASSAPDPATPLLKSPPQSSPNIARLLGSP | 1.3.7.4 | null | phytochromobilin biosynthetic process [GO:0010024] | null | cobalt ion binding [GO:0050897]; phytochromobilin:ferredoxin oxidoreductase activity [GO:0050619] | PF05996; | 3.40.1500.20; | HY2 family | null | null | CATALYTIC ACTIVITY: Reaction=(3Z)-phytochromobilin + 2 oxidized [2Fe-2S]-[ferredoxin] = biliverdin IXalpha + 2 reduced [2Fe-2S]-[ferredoxin] + 2 H(+); Xref=Rhea:RHEA:16377, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57439, ChEBI:CHEBI:57991; EC=1.3.7... | null | null | null | null | FUNCTION: Enzyme that catalyzes the two-electron reduction of biliverdin IX-alpha into phytobilins; it is not clear if this is the physiological function (PubMed:37071675). Expression in E.coli with M.psychrotolerans heme oxygenase (HO) and C.apiculatus probable acceptor protein CAP_1521 allows chromophorylation of CAP... | Chondromyces apiculatus (strain DSM 436 / NBRC 100084 / Cm a2) | [
9117
] | [
"go_mf: cobalt ion binding (GO:0050897)"
] | [
"UniProtKB-GO=ECO:0000501"
] | Function: Enzyme that catalyzes the two-electron reduction of biliverdin IX-alpha into phytobilins; it is not clear if this is the physiological function. Expression in E.coli with M.psychrotolerans heme oxygenase (HO) and C.apiculatus probable acceptor protein CAP_1521 allows chromophorylation of CAP_1521. Other poten... |
A0A017TC46 | BBAG2_CHOA4 | MLDLADRIEGRAAQLAEEALAEMYRDPFWEARYGERGRRFSHEDGHYHVRYLVEALRSGTPETLCAYARWLQTLLTSRGMCTAHLVENFERIGAKVGSAVEGSEAAVAYLKAAVEALRYPEGAAREVQDAAEAMEAQVRAQVKAQEGAADERQAPEGIAGAGTLLSYLIDAIARDRPELFGDHLLFAADYLGARGAPPALLEGRLDAIEASLALLPEGAPGRALAAEVVDAARGRIRQGAQGAGDARGAHDALEAARAT | null | null | null | null | null | null | 1.10.490.20; | Phycobiliprotein family | PTM: This protein is chromophorylated upon expression in E.coli with heme oxygenase (HO, from M.psychrotolerans) and CAP_1520 (a ferredoxin-dependent bilin reductase) from C.apiculatus; the adduct is probably biliverdin IX-alpha, no other adducts are seen. {ECO:0000269|PubMed:37071675}. | null | null | null | null | null | null | null | Chondromyces apiculatus (strain DSM 436 / NBRC 100084 / Cm a2) | [] | [] | [] | PTM: This protein is chromophorylated upon expression in E.coli with heme oxygenase (HO, from M.psychrotolerans) and CAP_1520 (a ferredoxin-dependent bilin reductase) from C.apiculatus; the adduct is probably biliverdin IX-alpha, no other adducts are seen.
Sequence Mass (Da): 27707
Sequence Length: 259 |
A0A023FBW4 | E1142_AMBCJ | MTSHGAVKIAIFAVIALHSIFECLSKPQILQRTDHSTDSDWDPQMCPETCNPSKNISCSSECLCVTLGGGDETGTCFNMSGVDWLGHAQASDGHNDG | null | null | null | extracellular region [GO:0005576] | C-X-C chemokine binding [GO:0019958] | null | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL4, CXCL5, CXCL6, CXCL7, CXCL10 and CXCL11. {ECO:0000269|PubMed:31167786}. | Amblyomma cajennense (Cayenne tick) (Acarus cajennensis) | [
6485,
8655,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"go_mf: C-X-C chemokine binding (GO:0019958)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000314",
"UniProtKB=ECO:0000305"
] | Function: Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL4, CXCL5, CXCL6, CXCL7, CXCL10 and CXCL11.
Subcellular Location: Secreted
Sequence Mass (Da): 10328
Sequence Length: 97 |
A0A023FBW7 | EV546_AMBCJ | MKVLLYIAASCLMLLALNVSAENTQQEEEDYDYGTDTCPFPVLANKTNKAKFVGCHQKCNGGDQKLTDGTACYVVERKVWDRMTPMLWYSCPLGECKNGVCEDLRKKEECRKGNGEEK | null | null | null | extracellular region [GO:0005576] | C-C chemokine binding [GO:0019957] | PF19429; | 2.30.130.100; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Salivary chemokine-binding protein which binds to host chemokines CCL1, CCL3, CCL5 and CCL22. {ECO:0000269|PubMed:28655871}. | Amblyomma cajennense (Cayenne tick) (Acarus cajennensis) | [
6485,
8654,
18011,
24284,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"go_mf: C-C chemokine binding (GO:0019957)",
"interpro: Evasins Class A (IPR045797)",
"pfam: EVA_Class_A (PF19429)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000314",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305"
] | Function: Salivary chemokine-binding protein which binds to host chemokines CCL1, CCL3, CCL5 and CCL22.
Subcellular Location: Secreted
Sequence Mass (Da): 13310
Sequence Length: 118 |
A0A023FDY8 | EV974_AMBCJ | MKVLLCIAASCLMLLALNVSAENTQQEEQDYDYGTDTCPFPVLANKTNKAKFVGCHQKCNGGDQKLTDGTACYVVERKVWDRMTPMLWYECPLGECKNGVCEDLRKKEDCRKGNGEEK | null | null | null | extracellular region [GO:0005576] | C-C chemokine binding [GO:0019957] | PF19429; | 2.30.130.100; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Salivary chemokine-binding protein which has chemokine-neutralizing activity and binds to host chemokines CCL1, CCL3, CCL4, CCL7, CCL8, CCL11, CCL13, CCL14, CCL16, CCL17, CCL18 and CCL22. {ECO:0000269|PubMed:28655871, ECO:0000269|PubMed:35217625}. | Amblyomma cajennense (Cayenne tick) (Acarus cajennensis) | [
6485,
8654,
18011,
24284,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"go_mf: C-C chemokine binding (GO:0019957)",
"interpro: Evasins Class A (IPR045797)",
"pfam: EVA_Class_A (PF19429)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000314",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305"
] | Function: Salivary chemokine-binding protein which has chemokine-neutralizing activity and binds to host chemokines CCL1, CCL3, CCL4, CCL7, CCL8, CCL11, CCL13, CCL14, CCL16, CCL17, CCL18 and CCL22.
Subcellular Location: Secreted
Sequence Mass (Da): 13277
Sequence Length: 118 |
A0A023FF81 | E1126_AMBCJ | MTSHSAVRIAIFAVIALHSIFECLSKPQILQRTDKSTDSEWDPQTCPETCIPSKNITCSDGCVCVKLGEEEEGTCFNMTGVDWLGSPSDD | null | null | null | extracellular region [GO:0005576] | C-X-C chemokine binding [GO:0019958] | null | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL4, CXCL5, CXCL6, CXCL7, CXCL10 and CXCL11. {ECO:0000269|PubMed:31167786}. | Amblyomma cajennense (Cayenne tick) (Acarus cajennensis) | [
6485,
8655,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"go_mf: C-X-C chemokine binding (GO:0019958)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000314",
"UniProtKB=ECO:0000305"
] | Function: Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL4, CXCL5, CXCL6, CXCL7, CXCL10 and CXCL11.
Subcellular Location: Secreted
Sequence Mass (Da): 9826
Sequence Length: 90 |
A0A023FFB5 | EV983_AMBCJ | MKASFCVIASCLVVFALKGTAEDTGTEDDFDYGNTGCPFPVLGNYKSNMTKPVGCKNKCGSGYEVLNDTTPCYVIDQKVFNNMVPLRQYSKCPLGFCENGECKPNDQAEDCYKGREEQK | null | null | null | extracellular region [GO:0005576] | C-C chemokine binding [GO:0019957] | PF19429; | 2.30.130.100; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Salivary chemokine-binding protein which binds to host chemokines CCL2, CCL3 and CCL8. {ECO:0000269|PubMed:28655871}. | Amblyomma cajennense (Cayenne tick) (Acarus cajennensis) | [
6485,
8654,
18011,
24284,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"go_mf: C-C chemokine binding (GO:0019957)",
"interpro: Evasins Class A (IPR045797)",
"pfam: EVA_Class_A (PF19429)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000314",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305"
] | Function: Salivary chemokine-binding protein which binds to host chemokines CCL2, CCL3 and CCL8.
Subcellular Location: Secreted
Sequence Mass (Da): 13124
Sequence Length: 119 |
A0A023FFD0 | EV991_AMBCJ | MHSTIVYACLLALAVFVALHGTPLAALAENGEGTTQPDYDNSTDYYNYEDFKCTCPAPHLNNTNGTVMKPIGCYYTCNVTRCTAPDTYPCYNLTEHQAKNLTTSPTTLCAVGNCDHGICVPNGTKELCFKAPNLEE | null | null | negative regulation of chemokine activity [GO:1900137] | extracellular region [GO:0005576] | C-C chemokine binding [GO:0019957] | PF19429; | 2.30.130.100; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Salivary chemokine-binding protein which has chemokine-neutralizing activity and binds to host chemokines CCL2, CCL3, CCL3L1, CCL4, CCL4L1, CCL5, CCL6, CCL7, CCL8, CCL9, CCL11, CCL12, CCL13, CCL14, CCL16, CCL17, CCL18, CCL19, CCL22, CCL23, CCL24 and CCL27. {ECO:0000269|PubMed:28655871, ECO:0000269|PubMed:3872... | Amblyomma cajennense (Cayenne tick) (Acarus cajennensis) | [
6485,
8654,
18011,
24284,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"go_mf: C-C chemokine binding (GO:0019957)",
"interpro: Evasins Class A (IPR045797)",
"pfam: EVA_Class_A (PF19429)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000314",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305"
] | Function: Salivary chemokine-binding protein which has chemokine-neutralizing activity and binds to host chemokines CCL2, CCL3, CCL3L1, CCL4, CCL4L1, CCL5, CCL6, CCL7, CCL8, CCL9, CCL11, CCL12, CCL13, CCL14, CCL16, CCL17, CCL18, CCL19, CCL22, CCL23, CCL24 and CCL27.
Subcellular Location: Secreted
Sequence Mass (Da): 14... |
A0A023FT45 | EV985_AMBPA | MHSTIAYVSLLPLALFVAMHGASTDEESEELGASTDVDYEELDANCTCPAPALTSTRNNKHYPLGCIYNCSSYNCTIPDGTPCYVLTLGEVKEHLQIGSTVPNCTCGLCRNGTCVSNGTVEECFAVEEIEET | null | null | null | extracellular region [GO:0005576] | C-C chemokine binding [GO:0019957] | PF19429; | 2.30.130.100; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Salivary chemokine-binding protein which binds to host chemokine CCL5. {ECO:0000269|PubMed:28655871}. | Amblyomma parvum (South American tick) | [
6485,
8654,
18011,
24284,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"go_mf: C-C chemokine binding (GO:0019957)",
"interpro: Evasins Class A (IPR045797)",
"pfam: EVA_Class_A (PF19429)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000314",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305"
] | Function: Salivary chemokine-binding protein which binds to host chemokine CCL5.
Subcellular Location: Secreted
Sequence Mass (Da): 14165
Sequence Length: 132 |
A0A023G6B6 | E1180_AMBTT | MARNWSFRVIFVSAMWCALLKFATLEEPKDGYDYTEGCPFVVLGNGTHAKPAGCSHLCNGAPETLDDNMECYNVTEEVAKRMTPDIPYTCWLGWCSKGECKRDNRTEVCYRGSERE | null | null | null | extracellular region [GO:0005576] | C-C chemokine binding [GO:0019957] | PF19429; | 2.30.130.100; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Salivary chemokine-binding protein which binds to host chemokines CCL2, CCL3, CCL4, CCL8 and CCL18. {ECO:0000269|PubMed:28655871}. | Amblyomma triste (Neotropical tick) | [
6485,
8654,
18011,
24284,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"go_mf: C-C chemokine binding (GO:0019957)",
"interpro: Evasins Class A (IPR045797)",
"pfam: EVA_Class_A (PF19429)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000314",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305"
] | Function: Salivary chemokine-binding protein which binds to host chemokines CCL2, CCL3, CCL4, CCL8 and CCL18.
Subcellular Location: Secreted
Sequence Mass (Da): 13174
Sequence Length: 116 |
A0A023G9N9 | E1183_AMBTT | MTRNWSFRVIFVSAMWCALLKFATLEAPKDDFEYDGGCPFVVLDNGTHVKPAGCSHLCNGAPETLDNIECYNVTEEVAKRMTPGIPYACWLGWCSKGECKRDNRTEVCYRGSEEE | null | null | null | extracellular region [GO:0005576] | C-C chemokine binding [GO:0019957] | PF19429; | 2.30.130.100; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Salivary chemokine-binding protein which binds to host chemokine CCL2. {ECO:0000269|PubMed:28655871}. | Amblyomma triste (Neotropical tick) | [
6485,
8654,
18011,
24284,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"go_mf: C-C chemokine binding (GO:0019957)",
"interpro: Evasins Class A (IPR045797)",
"pfam: EVA_Class_A (PF19429)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000314",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305"
] | Function: Salivary chemokine-binding protein which binds to host chemokine CCL2.
Subcellular Location: Secreted
Sequence Mass (Da): 12982
Sequence Length: 115 |
A0A023GPI8 | LECA_CANBL | ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVGKRLSAVVSYPNGDSATVSYDVDLDNVLPEWVRVGLSATTGLYKETNTILSWSFTSKLKSNSTHETNALHFMFNQFSKDQKDLILQGDATTGRDGNLELTRVSSNGSPQGSSVGRALFYAPVHIWESSAVVASFDATFTFLIKSSDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN | null | null | null | null | carbohydrate binding [GO:0030246] | PF00139; | 2.60.120.200; | Leguminous lectin family | null | null | null | null | null | null | null | FUNCTION: D-mannose/D-glucose-binding lectin (PubMed:24865454). Has anti-inflammatory activity in animal models when applied intravenously (PubMed:24865454). Has antinociceptive activity in mice when applied intravenously (PubMed:19705102). {ECO:0000269|PubMed:19705102, ECO:0000269|PubMed:24865454}. | Canavalia boliviana | [
8681,
9924,
10049,
13148,
14366,
18521,
20641
] | [
"go_mf: carbohydrate binding (GO:0030246)",
"interpro: Legume lectin, alpha chain, conserved site (IPR000985)",
"interpro: Legume lectin domain (IPR001220)",
"interpro: Concanavalin A-like lectin/glucanase domain superfamily (IPR013320)",
"interpro: Legume lectin, beta chain, Mn/Ca-binding site (IPR019825)"... | [
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam"
] | Function: D-mannose/D-glucose-binding lectin. Has anti-inflammatory activity in animal models when applied intravenously. Has antinociceptive activity in mice when applied intravenously.
Sequence Mass (Da): 25571
Sequence Length: 237 |
A0A023GPJ0 | CDII_ENTCC | MFGIFSKGEPVSMEGELVQPSSIVINDYEEELHLPLSYWDIKDYKNSWLKSLGEGLSNKTHSALAVSMYEPEKTNFIFTWVLYFEDEKVYVQNNVIFLEECHGFSPENINKFIESRTTHDGDGMKISEWHTDLNSVLDFYHSLNN | null | null | null | null | null | PF18228; | 3.30.2450.20; | null | null | null | null | null | null | null | null | FUNCTION: Immunity protein component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion. Protects cells against th... | Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCTC 10005 / WDCM 00083 / NCDC 279-56) | [] | [] | [] | Function: Immunity protein component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion. Protects cells against th... |
A0A023GS28 | DIOX1_RUTGR | MAPTKDFSTTTTNGAESWDDVADFVTKKGHGVKGLSERGIKTLPKPFHQPLEERFSEKKILERASIPLIDMSQWDSPEVVKSICDAAENWGFFQIVNHGVPLETLERVKEATHRFFGLPAEEKNNYSKENSPINNVRFGSSFVPHVEKALEWKDFLSMFYVSEEETNTYWPPICRDEMLEYMRSSEVLIQRLMEVLVVKGLKVKQIDEIREPMLVGSRRINLNYYPKCPNPELTLGVGRHSDISTFTILLQDQIGGLHVRKLDDTGNTWVHVTPIAGSLIINIGDALQIMSNGRYKSIEHMVVANGTQDRISVPLFVNPK... | 1.14.11.61; 1.14.11.62 | COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:Q9C899}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805}; | coumarin biosynthetic process [GO:0009805]; phenylpropanoid biosynthetic process [GO:0009699]; response to UV-B [GO:0010224] | null | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; 4-coumaroyl 2'-hydroxylase activity [GO:0102312] | PF03171;PF14226; | 2.60.120.330; | Iron/ascorbate-dependent oxidoreductase family | null | null | CATALYTIC ACTIVITY: Reaction=(E)-4-coumaroyl-CoA + 2-oxoglutarate + O2 = (E)-2,4-dihydroxycinnamoyl-CoA + succinate + CO2; Xref=Rhea:RHEA:57868, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:85008, ChEBI:CHEBI:142398; EC=1.14.11.62; Evidence={ECO:0000250|UniProtKB:W5QJZ5}; CATA... | null | PATHWAY: Phenylpropanoid metabolism. {ECO:0000250|UniProtKB:W5QJZ5}. | null | null | FUNCTION: 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD) involved in scopoletin and umbelliferone biosynthesis (By similarity). Converts feruloyl CoA into 6'-hydroxyferuloyl CoA, and p-coumaroyl CoA into 2,4-dihydroxycinnamoyl-CoA (By similarity). {ECO:0000250|UniProtKB:W5QJZ5}. | Ruta graveolens (Common rue) | [
1696,
1734,
1880,
8526,
11444,
15198,
15274,
17797,
19928,
19937,
22188,
23766
] | [
"go_bp: phenylpropanoid biosynthetic process (GO:0009699)",
"go_bp: coumarin biosynthetic process (GO:0009805)",
"go_bp: response to UV-B (GO:0010224)",
"go_mf: 2-oxoglutarate-dependent dioxygenase activity (GO:0016706)",
"interpro: Oxoglutarate/iron-dependent dioxygenase domain (IPR005123)",
"interpro: N... | [
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000250",
"InterPro=match:Pfam",
"InterPro=match:Pfam"
] | Function: 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD) involved in scopoletin and umbelliferone biosynthesis (By similarity). Converts feruloyl CoA into 6'-hydroxyferuloyl CoA, and p-coumaroyl CoA into 2,4-dihydroxycinnamoyl-CoA (By similarity).
Catalytic Activity: (E)-4-coumaroyl-CoA + 2-oxoglutarate +... |
A0A023GS29 | DIOX2_RUTGR | MAPTKDFSTATNGADSWDDVADFVTKKGHGVKGLSERGIKTLPKPFHQPLEERFSEKKILERASIPLIDMSEWDSPEVVKSICDAAENWGFFQIVNHGVPLETLERVKEATHRFFGLPAEEKNKYSKENSPINNVRFGSSFVPHVEKALEWKDFLSMFYVSXEETNTYWPPICXDQMLEYMRSSEVLIKRLMEVLVVKGLKVKQIDEIREPMLVGSRRVNLNYYPKCPNRELTLGVGRHSDISTFTILLQDQIEVLHVRKLDDTGNTWVHVTPIAGSLIINIGDALQIMSNGRYKSIEHMVVANGTQDRISVPLFVNPKP... | 1.14.11.61; 1.14.11.62 | COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:Q9C899}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805}; | coumarin biosynthetic process [GO:0009805]; phenylpropanoid biosynthetic process [GO:0009699]; response to UV-B [GO:0010224] | null | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; 4-coumaroyl 2'-hydroxylase activity [GO:0102312] | PF03171;PF14226; | 2.60.120.330; | Iron/ascorbate-dependent oxidoreductase family | null | null | CATALYTIC ACTIVITY: Reaction=(E)-4-coumaroyl-CoA + 2-oxoglutarate + O2 = (E)-2,4-dihydroxycinnamoyl-CoA + succinate + CO2; Xref=Rhea:RHEA:57868, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:85008, ChEBI:CHEBI:142398; EC=1.14.11.62; Evidence={ECO:0000250|UniProtKB:W5QJZ5}; CATA... | null | PATHWAY: Phenylpropanoid metabolism. {ECO:0000250|UniProtKB:W5QJZ5}. | null | null | FUNCTION: 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD) involved in scopoletin and umbelliferone biosynthesis (By similarity). Converts feruloyl CoA into 6'-hydroxyferuloyl CoA, and p-coumaroyl CoA into 2,4-dihydroxycinnamoyl-CoA (By similarity). {ECO:0000250|UniProtKB:W5QJZ5}. | Ruta graveolens (Common rue) | [
1696,
1734,
1880,
8526,
11444,
15198,
15274,
17797,
19928,
19937,
22188,
23766
] | [
"go_bp: phenylpropanoid biosynthetic process (GO:0009699)",
"go_bp: coumarin biosynthetic process (GO:0009805)",
"go_bp: response to UV-B (GO:0010224)",
"go_mf: 2-oxoglutarate-dependent dioxygenase activity (GO:0016706)",
"interpro: Oxoglutarate/iron-dependent dioxygenase domain (IPR005123)",
"interpro: N... | [
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000250",
"InterPro=match:Pfam",
"InterPro=match:Pfam"
] | Function: 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD) involved in scopoletin and umbelliferone biosynthesis (By similarity). Converts feruloyl CoA into 6'-hydroxyferuloyl CoA, and p-coumaroyl CoA into 2,4-dihydroxycinnamoyl-CoA (By similarity).
Catalytic Activity: (E)-4-coumaroyl-CoA + 2-oxoglutarate +... |
A0A023I4C8 | PRX4_PENRO | MIPRWQPASIPLLLHLDTLRCHHVSVQPPRATMTSLNIKEEDIPRLDGKVVVISGGASGIGLAAANIFARAGAKIFLFDCNPPDSGEAPENSTFIKADITSWAELKAAFAQAGHVDIAVANAGVSEEQPYFEDTFDEQGELKEPGFAVVDVNFKGTVMFTKLAVSYMRKQGKGGSVVITASATGYAPEQNLPVYSAIKSGLVGLVRSLRSTLPRFDISINAVAPAATITKLLPMDIAGPLMAAGLPVSSAHMVGLAVVYSAVARQPRMVETYGKENVLDLESKWNGRTILTLGEHYTELEEKLADLRPVWFGWRNTDLTK... | 1.1.99.- | null | null | membrane [GO:0016020] | null | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | PATHWAY: Sesquiterpene biosynthesis. {ECO:0000269|PubMed:24239699, ECO:0000305|PubMed:27921136}. | null | null | FUNCTION: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of PR-toxin, a bicyclic sesquiterpene belonging to the eremophilane class and acting as a mycotoxin (PubMed:24239699, PubMed:27921136). The first step of the pathway is catalyzed by the aristolochene synthase which pe... | Penicillium roqueforti | [
6727,
10628,
16354,
20610,
24930,
25105
] | [
"go_cc: membrane (GO:0016020)",
"interpro: Short-chain dehydrogenase/reductase SDR (IPR002347)",
"interpro: NAD(P)-binding domain superfamily (IPR036291)",
"pfam: adh_short (PF00106)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Single-pass membrane protein (SL-9904)"
] | [
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Function: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of PR-toxin, a bicyclic sesquiterpene belonging to the eremophilane class and acting as a mycotoxin. The first step of the pathway is catalyzed by the aristolochene synthase which performs the cyclization of trans,tra... |
A0A023I4D6 | PRX3_PENRO | MLSLKAFLALSLSIHLSQGLVASVSHRRANACTELSRSYPDSTIHPGSSVFAEDVIEPWSQTCQTTPTCVFAPASAEEVAGGLAILRKADQTFAVRTQGHMPIPGAADISNGVLMVTTSLNSVQYADDSKSVVQIGAGNRWLDVYKVLAKDNLAVVGGRFGQVGVSGLLLGGGISYFNSDHGWGANSVVNYEVVLANGTVCAANAQQNSDLYWALKGGSFNFGIVTRFDLATFSVPYMWGGSAFYDASALDPLVNAYASYAVASGGSSDPAAHSDPSILYNVTTGEVSGYGIYMHRGDDPAPAALKNFTDIPSTFQDFRV... | 1.-.-.- | null | null | null | FAD binding [GO:0071949] | PF01565; | 3.30.465.10; | Oxygen-dependent FAD-linked oxidoreductase family | null | null | null | null | PATHWAY: Sesquiterpene biosynthesis. {ECO:0000269|PubMed:24239699, ECO:0000305|PubMed:27921136}. | null | null | FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of PR-toxin, a bicyclic sesquiterpene belonging to the eremophilane class and acting as a mycotoxin (PubMed:24239699, PubMed:27921136). The first step of the pathway is catalyzed by the aristolochene synthase which performs t... | Penicillium roqueforti | [
9248,
11713,
13688,
13690,
16364,
18616,
21598
] | [
"go_mf: FAD binding (GO:0071949)",
"interpro: FAD linked oxidase, N-terminal (IPR006094)",
"interpro: FAD-binding domain, PCMH-type (IPR016166)",
"interpro: FAD-binding, type PCMH, subdomain 2 (IPR016169)",
"interpro: FAD-binding, type PCMH-like superfamily (IPR036318)",
"interpro: FAD-linked Oxidoreducta... | [
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam"
] | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of PR-toxin, a bicyclic sesquiterpene belonging to the eremophilane class and acting as a mycotoxin. The first step of the pathway is catalyzed by the aristolochene synthase which performs the cyclization of trans,trans-farne... |
A0A023I4F1 | PRX1_PENRO | MANPLISNHIGKHGKYTQAFLEQNGPGDARPTALDILKDNDRIDNMKDKVFLLTGSSGGIGIETGRALAATGGKVYLGVRDLEKGKQALAEILEPGRVELLELDVGSMESVRTAAKTFLSKSTQLNVLVNNAGIMACPEAKTVDGFESQLAINYLGHFLLYKLLEQTLLSSSTPEFQSRVVNVSSAGHHMSSVVLDNINLEGEYEPWKAYGNAKTACIWMTNEIEHRYGSKGLHGLSLMPGGIATSLQRHVDPETLKEWGSSEFAQKYAKSSAQGAATTITAALGKEWEGKGGVYLEDCQEAGPVPEGGTLAVGVAPHAF... | 1.1.99.- | null | null | null | null | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | null | null | PATHWAY: Sesquiterpene biosynthesis. {ECO:0000269|PubMed:24239699, ECO:0000305|PubMed:27921136}. | null | null | FUNCTION: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of PR-toxin, a bicyclic sesquiterpene belonging to the eremophilane class and acting as a mycotoxin (PubMed:24239699, PubMed:27921136). The first step of the pathway is catalyzed by the aristolochene synthase which pe... | Penicillium roqueforti | [
10628,
16354,
20610
] | [
"interpro: Short-chain dehydrogenase/reductase SDR (IPR002347)",
"interpro: NAD(P)-binding domain superfamily (IPR036291)",
"pfam: adh_short (PF00106)"
] | [
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam"
] | Function: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of PR-toxin, a bicyclic sesquiterpene belonging to the eremophilane class and acting as a mycotoxin. The first step of the pathway is catalyzed by the aristolochene synthase which performs the cyclization of trans,tra... |
A0A023I7E1 | ENG1_RHIMI | MRFQVIVAAATITMITSYIPGVASQSTSDGDDLFVPVSNFDPKSIFPEIKHPFEPMYANTENGKIVPTNSWISNLFYPSADNLAPTTPDPYTLRLLDGYGGNPGLTIRQPSAKVLGSYPPTNDVPYTDAGYMINSVVVDLRLTSSEWSDVVPDRQVTDWDHLSANLRLSTPQDSNSYIDFPIVRGMAYITANYNNLTPQFLSQHAIISVEADEKKSDDNTSTFSGRKFKITMNDDPTSTFIIYSLGDKPLELRKQDNSNLVASKPYTGVIRVAKLPAPEFETLLDASRAVWPTGGDISARSDDNNGASYTIKWKTNSNEA... | 3.2.1.39 | null | polysaccharide catabolic process [GO:0000272] | null | glucan endo-1,3-beta-D-glucosidase activity [GO:0042973] | PF17652;PF03639; | 1.10.287.1170;2.70.98.30;1.20.5.420; | Glycosyl hydrolase 81 family | null | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250|UniProtKB:P53753}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.; EC=3.2.1.39; Evidence={ECO:0000269|PubMed:34801773}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:34801773}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:34801773}; | FUNCTION: Cleaves internal linkages in 1,3-beta-glucan. {ECO:0000269|PubMed:34801773}. | Rhizomucor miehei | [
253,
433,
8925,
11473,
17249,
17280,
22314,
24107,
24858,
24983
] | [
"ec: EC 3.2.1.39",
"go_bp: polysaccharide catabolic process (GO:0000272)",
"go_mf: glucan endo-1,3-beta-D-glucosidase activity (GO:0042973)",
"interpro: Endo-1,3(4)-beta-glucanase (IPR005200)",
"interpro: Glycosyl hydrolase family 81, N-terminal (IPR040451)",
"interpro: Glycosyl hydrolase family 81, C-ter... | [
"UniProtKB=ECO:0000269",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000314",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000250",
"UniProtKB=ECO:0000250"
] | Function: Cleaves internal linkages in 1,3-beta-glucan.
Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Subcellular Location: Secreted, Cell wall
EC: 3.2.1.39
Sequence Mass (Da): 89495
Sequence Length: 796 |
A0A023IWD9 | MSD4_AMAEX | MSDINATRLPVWIGYSPCVGDDCIALLTRGEGLC | null | null | null | null | null | null | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic heptapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By s... | null | null | null | null | null | null | FUNCTION: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths (PubMed:24050899, PubMed:24613547). {ECO:0000305|PubMed:24050899, ECO:0000305|PubMed:24613547}. | Amanita exitialis (Guangzhou destroying angel) | [] | [] | [] | Function: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic heptapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Confo... |
A0A023IWE0 | MSD1_AMAFL | MSDINATCLPAWLALCPCVGDDVNPTLTRGGT | null | null | null | null | null | null | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic heptapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By s... | null | null | null | null | null | null | FUNCTION: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita fuligineoides | [] | [] | [] | Function: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic heptapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Confo... |
A0A023IWE1 | MSD4_AMAPH | MSDINGTRLPWLATCPCVGEDVNPTLSRGER | null | null | null | null | null | null | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic hexapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By si... | null | null | null | null | null | null | FUNCTION: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita phalloides (Death cap) | [] | [] | [] | Function: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic hexapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Confor... |
A0A023IWE2 | BAMAT_AMAPL | MSDINATRLPIWGIGCDPCVGDDVTAVLTRGEA | null | null | null | null | null | PF24112; | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide (PubMed:24613547). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By ... | null | null | null | null | null | null | FUNCTION: Toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita pallidorosea | [] | [] | [] | Function: Toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide. POPB first removes 10 residu... |
A0A023IWE3 | AAMA1_AMAFL | MSDINATRLPIWGIGCNPCVGDEVTALLTRGEA | null | null | null | null | null | PF24112; | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide (PubMed:24613547). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By ... | null | null | null | null | null | null | FUNCTION: Major toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita fuligineoides | [] | [] | [] | Function: Major toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide. POPB first removes 10 ... |
A0A023IWG1 | MSD3_AMAFL | MSDINATRLPVWIGYSPCVGDDAVALLNRGEG | null | null | null | null | null | null | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic heptapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By s... | null | null | null | null | null | null | FUNCTION: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita fuligineoides | [] | [] | [] | Function: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic heptapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Confo... |
A0A023IWG2 | MSD6_AMAPH | MSDINATRLPLILLAALGIPSDDADSTLTRGER | null | null | null | null | null | null | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By si... | null | null | null | null | null | null | FUNCTION: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita phalloides (Death cap) | [] | [] | [] | Function: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Confor... |
A0A023IWG3 | BAMAT_AMAFL | MSDINATRLPIWGIGCDPCVGDEVTALLTRGEA | null | null | null | null | null | PF24112; | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide (PubMed:24613547). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By ... | null | null | null | null | null | null | FUNCTION: Toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita fuligineoides | [] | [] | [] | Function: Toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide. POPB first removes 10 residu... |
A0A023IWG4 | AAMAT_AMAFU | MSDINATRLPIWGIGCNPSVGDEVTALLTSGEA | null | null | null | null | null | PF24112; | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide (PubMed:24613547). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By ... | null | null | null | null | null | null | FUNCTION: Major toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita fuliginea (East Asian brown death cap) | [] | [] | [] | Function: Major toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide. POPB first removes 10 ... |
A0A023IWI4 | MSD2_AMAFL | MSDINATRLPHLVRYPPYVGDGTDLTLNRGEK | null | null | null | null | null | null | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic heptapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By s... | null | null | null | null | null | null | FUNCTION: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita fuligineoides | [] | [] | [] | Function: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic heptapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Confo... |
A0A023IWI5 | MSD5_AMAPH | MSDINATRLPIFWFIYFPCVGDNVDNTLTRGER | null | null | null | null | null | null | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic octapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By si... | null | null | null | null | null | null | FUNCTION: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita phalloides (Death cap) | [] | [] | [] | Function: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic octapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Confor... |
A0A023IWI6 | BAMAT_AMAFU | MSDINATRLPIWGIGCDPCVGDEVTALLTRGEA | null | null | null | null | null | PF24112; | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide (PubMed:24613547). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By ... | null | null | null | null | null | null | FUNCTION: Toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita fuliginea (East Asian brown death cap) | [] | [] | [] | Function: Toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide. POPB first removes 10 residu... |
A0A023IWI8 | PHAT_AMAPL | MSDINATRLPAWLVDCPCVGDDINRLLTRGEK | null | null | null | null | null | null | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic heptapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By s... | null | null | null | null | null | null | FUNCTION: Major toxin that belongs to the bicyclic heptapeptides called phallotoxins (PubMed:24613547). Although structurally related to amatoxins, phallotoxins have a different mode of action, which is the stabilization of F-actin (PubMed:24613547). Phallotoxins are poisonous when administered parenterally, but not or... | Amanita pallidorosea | [] | [] | [] | Function: Major toxin that belongs to the bicyclic heptapeptides called phallotoxins. Although structurally related to amatoxins, phallotoxins have a different mode of action, which is the stabilization of F-actin. Phallotoxins are poisonous when administered parenterally, but not orally because of poor absorption.
PTM... |
A0A023IWK3 | MSD2_AMAFU | MSDINATRLPVWIGCSPCVGDDCIALLTRGEG | null | null | null | null | null | null | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic heptapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By s... | null | null | null | null | null | null | FUNCTION: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita fuliginea (East Asian brown death cap) | [] | [] | [] | Function: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic heptapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Confo... |
A0A023IWK4 | MSD3_AMAPH | MSDINATRLPSFFFPIPCISDDIEMVLTRGER | null | null | null | null | null | null | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic heptapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By s... | null | null | null | null | null | null | FUNCTION: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita phalloides (Death cap) | [] | [] | [] | Function: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic heptapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Confo... |
A0A023IWK5 | MSD2_AMARI | MSDINATRVPAWLAECPCVGDDISHLLTRGEK | null | null | null | null | null | null | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic heptapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By s... | null | null | null | null | null | null | FUNCTION: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita rimosa | [] | [] | [] | Function: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic heptapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Confo... |
A0A023IWK6 | BAMA1_AMAPH | MSDINATRLPIWGIGCDPCVGDEVTALLTRGEA | null | null | null | null | null | PF24112; | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide (PubMed:24613547). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By ... | null | null | null | null | null | null | FUNCTION: Toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita phalloides (Death cap) | [] | [] | [] | Function: Toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide. POPB first removes 10 residu... |
A0A023IWK7 | AAMAT_AMAPL | MSDINATRLPIWGIGCNPCVGDEVTALITRGEA | null | null | null | null | null | PF24112; | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide (PubMed:24613547). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By ... | null | null | null | null | null | null | FUNCTION: Major toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita pallidorosea | [] | [] | [] | Function: Major toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide. POPB first removes 10 ... |
A0A023IWM4 | MSD1_AMAFU | MSDINATRLPIIWAPVVPCISDDNDSTLTRGQR | null | null | null | null | null | null | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic octapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By si... | null | null | null | null | null | null | FUNCTION: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita fuliginea (East Asian brown death cap) | [] | [] | [] | Function: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic octapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Confor... |
A0A023IWM5 | MSD2_AMAPH | MSDINATRLPIILAPIIPCINDDVNSTLTSGER | null | null | null | null | null | null | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic octapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By si... | null | null | null | null | null | null | FUNCTION: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita phalloides (Death cap) | [] | [] | [] | Function: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic octapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Confor... |
A0A023IWM6 | MSD1_AMARI | MSDINATRLPIIIVLGLIIPLCVSDIEMILTRGER | null | null | null | null | null | null | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By si... | null | null | null | null | null | null | FUNCTION: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita rimosa | [] | [] | [] | Function: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Confor... |
A0A023IWM7 | BAMAT_AMARI | MSDINATRLPIWGIGCDPCVGDDVAALTTRGEA | null | null | null | null | null | PF24112; | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide (PubMed:24613547). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By ... | null | null | null | null | null | null | FUNCTION: Toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita rimosa | [] | [] | [] | Function: Toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide. POPB first removes 10 residu... |
A0A023IWM8 | AAMA1_AMARI | MSDINATRLPIWGIGCNPSVGDEVTALLASGEA | null | null | null | null | null | PF24112; | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide (PubMed:24613547). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By ... | null | null | null | null | null | null | FUNCTION: Major toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita rimosa | [] | [] | [] | Function: Major toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide. POPB first removes 10 ... |
A0A023PMT2 | CECB1_AEDAE | MNFSKVFALVLLIGLVLLTGHTEAGGLKKLGKKLEGVGKRVFKASEKALPVVTGYKAIGK | null | null | antibacterial humoral response [GO:0019731]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830] | extracellular region [GO:0005576] | null | PF00272; | null | Cecropin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Putative antimicrobial peptide (By similarity). Partially neutralizes lipopolysaccharides (LPS) (PubMed:30107813). Exhibits anti-inflammatory properties: inhibits LPS-induced iNOS/NOS2 transcription, nitric oxide (NO) and pro-inflammatory cytokine production in mouse macrophages and human peripheral blood mon... | Aedes aegypti (Yellowfever mosquito) (Culex aegypti) | [
2368,
4488,
4489,
6485,
24983
] | [
"go_bp: antibacterial humoral response (GO:0019731)",
"go_bp: defense response to Gram-negative bacterium (GO:0050829)",
"go_bp: defense response to Gram-positive bacterium (GO:0050830)",
"go_cc: extracellular region (GO:0005576)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000305"
] | Function: Putative antimicrobial peptide (By similarity). Partially neutralizes lipopolysaccharides (LPS). Exhibits anti-inflammatory properties: inhibits LPS-induced iNOS/NOS2 transcription, nitric oxide (NO) and pro-inflammatory cytokine production in mouse macrophages and human peripheral blood mononuclear cells (PB... |
A0A023PXA5 | YA19A_YEAST | MLLSELVATASSLPYTAISIHNNCRVPAARHIHHGCRYFHGPPVMHLPQCLRTIQFSPSVISTSYQIPVICQHHAVVPTARYLPDYCSIISWHRPLWGIHILIVPQSQLPLPIRPKRIHTTHRYKPVIAFNDHIPSLALWICLHYQGSNGCVTPVAAKFFIIFHFVGLKEIMSPSRNATRNLNQYWRVL | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 21605
Sequence Length: 189 |
A0A023PXB0 | YA019_YEAST | MFINGFVNYPVRTPPNDLLQVVLHGFLRCPLDGSQVDSIGIGHTVHGIVLPGKWVVLMCVLSFLEPPSRRYTFCEADLPYTKITARKAERPSQGGKDYNGTAKSAQSTTV | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 12092
Sequence Length: 110 |
A0A023PXB5 | IRC2_YEAST | MFALIISSKGKTSGFFFNSSFSSSALVGIAPLTAYSALVTPVFKSFLVILPAGLKSKSFAVNTPFKSCWCVIVMCSYFFCVYHLQKQHYCGAPSLYSYLLCL | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25110
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Multi-pass membrane protein (SL-9909)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11193
Sequence Length: 102 |
A0A023PXB9 | YD99W_YEAST | MEYVLIYNIWFFSFLQDKPCFCFVDYACSIFLLSSYCGNCLTAVATKPNEMATTPKSIPLLTLVLLPSTTPSSSVLINVSSVSFFSSLESFCFTLALLSLLIPPLKLLCVKTKFFPLSSSI | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25110
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Multi-pass membrane protein (SL-9909)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13391
Sequence Length: 121 |
A0A023PXC2 | YE53A_YEAST | MLPLCLTFLSFFLSLGGSFKAVMTKEEADGTTEAAACLFWIFNWTVTLIPLNSLVALAISSPTFFGDRPKGPIFGAKAAEAPTSPPTALRYKYLTSLGSNFGGIFVYPLFLLSTF | null | null | null | membrane [GO:0016020] | null | PF29870; | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25110
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Multi-pass membrane protein (SL-9909)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12414
Sequence Length: 115 |
A0A023PXC7 | YE068_YEAST | MAPPTLITANCCCETEVKYFKYCSTSLFVLILFNSWITVDLVAEKPLVDETYLFEYPTFFLVNATDGGALKGTDANPAMVDLFNEDTNFWNLEALSLFVETSKLADGIMMQTYFSLQISLSFAFSGICVKYITGLKNNIQKCS | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25110
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Multi-pass membrane protein (SL-9909)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15999
Sequence Length: 143 |
A0A023PXD3 | YE88A_YEAST | MTRLPPIPRMTVTLTTRPAVPTCNEGSSILHYIYIPIYEPNEQKEKRRRKTPPEPRAYTTTTTIATNSRISGCSLTLEDGIHLRGKRAETARLPAATPQKRTGPARG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 11926
Sequence Length: 107 |
A0A023PXD5 | YE147_YEAST | MMTAAKRLGLYSALRACSATVFRSNLHPKVTVATMFCSVGTIPDVAEVSFSDSGAALFMSSSLWKVVAGFVPSRFWFSHTCLVFGSNTILFASLNSFKRSSSAIIKKVSLDTPVYVGLEKKNKMQPLLPCFFRRAV | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25105
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Single-pass membrane protein (SL-9904)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14885
Sequence Length: 136 |
A0A023PXD9 | YF015_YEAST | MIKKSRTYYPSFGAYFHLLPAHPNAHSVTLLFGIFRSSPFLLLFLLIHRKVGEGRGSQRMKKKRGRANPSENLRERADPTNGPAENGKKGSVMCGCQLAVAMTTC | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25105
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Single-pass membrane protein (SL-9904)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 11665
Sequence Length: 105 |
A0A023PXE5 | YH006_YEAST | MDLYPPASWAALVPFCKALTFKVPVVLGNRNPSPPSPLPPMALSLSLLIPLSRLSLSGSSDTADGSLLISCISRGSCGIFRMGCEAVKGRSLGCLLPRSNCTYGCMSLRKYVSVCSM | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 12357
Sequence Length: 117 |
A0A023PXE8 | YH028_YEAST | MSLSNKCFFFVSKSSSGMRSTSSSPPSMSNLAYWYVAKILSERILRISALLMYTLMEAFLIRNSPSISFNTASGGIEGEKFGREHIIVINIYIYIYIYTSTLQLCV | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 11958
Sequence Length: 106 |
A0A023PXF2 | YH071_YEAST | MVGRLRLAEGLNIPSFLGLAHQFSVSKDVDLSLVDRLCQNKILSSVLYFLCGRRLLVRLLGTAVHYWRGLCSMALLKAEGMYYIFFFLRKCISVNNRYKNFSPKRL | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 12235
Sequence Length: 106 |
A0A023PXF5 | YH218_YEAST | MQVLIGTKLVTEGIDIKQLMMVIMLDNRLNIIELIQGVGRLRDGGLCYLLSRKNSWAARNRKGELPPIKEGCITEQVREFYGLESKKGKKGPACWMLWLQDRPVC | null | null | null | null | null | PF00271; | 3.40.50.300; | Helicase family, Yeast subtelomeric Y' repeat subfamily | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
10276,
15266,
20756
] | [
"interpro: Helicase, C-terminal domain-like (IPR001650)",
"interpro: P-loop containing nucleoside triphosphate hydrolase (IPR027417)",
"pfam: Helicase_C (PF00271)"
] | [
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam"
] | Sequence Mass (Da): 11974
Sequence Length: 105 |
A0A023PXF8 | YI066_YEAST | MRIQKQQYTISSNSRINLLGILVLNVVCGKSSIFFSHPQRLGKLGGSSLGSTGPFQTLSINFCIGCFLFNSNHFDLLFSLPSSSSILSMSVLEKFCSCIDSVTRCCPSQSLETPGSVASHVVLALSSKCTPIQFNAKWSISHKSNTG | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25105
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Single-pass membrane protein (SL-9904)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15856
Sequence Length: 147 |
A0A023PXG3 | YI56A_YEAST | MATENNKNPAIRFLLSVVGSGNSLSILNGLFLSFKTILASSSATLLLNLALVENECSKEPRTSTALAAEGVTFGNPLVTSLNIMYSLFYLLLLCRGLVRRERSNCFKTGIKMTRRRFLSLHNDQNKNKQNAKR | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25110
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Multi-pass membrane protein (SL-9909)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14768
Sequence Length: 133 |
A0A023PXG7 | YL230_YEAST | MTRVSIDRNLLDRPYQTNLTYMVHHQSSQSPHSYRTLLEHSRLEIDSLYRRLEGTFSQQHHHRQQHTLAFAFCGRANTFISCFISFASLIRLLTYLLRKIE | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25105
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Single-pass membrane protein (SL-9904)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12051
Sequence Length: 101 |
End of preview. Expand in Data Studio
Swiss-Prot 2026_03
Every reviewed UniProtKB entry of release 2026_03, 575,748 proteins, with UniProt's annotation columns, the Annotation
Vocabulary tokens of its terms, a readable form of each token, and a natural-language description. It replaces the July 2024
release of this repository and the former Synthyra/SwissProtNLP and Synthyra/SwissProt-AV.
| Proteins (rows) | 575,748 |
| With at least one vocabulary token | 557,864 |
| With a description beyond mass and length | 534,454 |
| Tokens | 6,025,408 |
| Vocabulary terms used | 24,970 of 25,119 |
Homology leakage
None is controlled: this is a corpus, one train split of every entry, with no clustering and no held-out split. Do not
report a score measured on it as held-out performance; the vocabulary's own release, Synthyra/annotation_experimental_v2,
holds the split by 0.5 identity for that.
How it was built
- Downloaded the Swiss-Prot XML and
subcell.txtof UniProt release 2026_03 from the UniProt FTP, and UniProt's TSV export of the 2024 release's 20 fields from its REST service, checking that both served 2026_03 before and after. - Read each entry's terms from the XML: EC numbers, Rhea reactions, ChEBI cofactors, subcellular locations, membrane topology and orientation from its comments, and GO terms, InterPro entries and Pfam families from its database references, with every evidence code. Isoform-scoped comments are left out.
- Turned each term into the token the vocabulary of
Synthyra/annotation_experimental_v2gives it; a term the vocabulary lacks gets no token and is counted. - Wrote the description from the entry's function, catalytic activity, cofactor, pathway, location, domain and PTM comments, its EC numbers, mass and length, with citations removed.
- Joined the XML's rows to the TSV's by accession, refusing the build unless both name the same 575,748 entries with the same sequences.
Tokens by aspect:
| Aspect | Tokens |
|---|---|
| interpro | 1,894,901 |
| go_bp | 925,050 |
| go_mf | 867,517 |
| go_cc | 806,802 |
| pfam | 592,072 |
| subcellular_location | 512,621 |
| cofactor | 143,041 |
| membrane_topology | 112,653 |
| rhea | 87,067 |
| ec | 70,873 |
| membrane_orientation | 12,811 |
Columns
| Column | Meaning |
|---|---|
Entry ... Organism |
The 20 columns of the 2024 release, as UniProt's TSV export of the same fields writes them; an empty field is null. |
av_tokens |
Annotation Vocabulary tokens of every term the entry is annotated with, ascending, from the vocabulary of Synthyra/annotation_experimental_v2; vocabulary.parquet maps a token to its term. |
av_text |
For each token, in the same order, <aspect>: <label> (<accession>). |
av_provenance |
For each token, in the same order, the sources and evidence codes that assert it, such as UniProtKB-GO=ECO:0000314;UniProtKB=ECO:0000269 or InterPro=match:Pfam; none names an assertion without an evidence tag. |
nl_text |
A natural-language description of the entry built from its comments, one Section: text line each, in the style of SwissProtNLP. |
Example rows
| Entry | Sequence | av_tokens | av_text | nl_text |
|---|---|---|---|---|
| A0A009IHW8 | MSLEQKKGADIISKILQIQNSIGKTTSPSTLKTKLSEISRKEQENARIQSKLSDLQK... | [259, 1285, 2363, 7667, ...] | [ec: EC 3.2.2.6, go_bp: signal transduction (GO:0007165),... | Function: NAD(+) hydrolase (NADase) that catalyzes cleava... |
| A0A011QK89 | MESIEAVVIGAGVVGLACARELARRGFETVILERHGAFGTETSARNSEVIHAGLYYP... | [9050, 11702, 16307, 19943, ...] | [go_mf: (S)-2-hydroxyglutarate dehydrogenase activity (GO... | Function: Catalyzes the dehydrogenation of L-2-hydroxyglu... |
| A0A017SE81 | MSTKFALVTGCGQGGIGEALITEYARRGIHAIATVLPAEPSDHLARAGITFFPLDVT... | [1075, 2346, 3796, 6563, ...] | [go_bp: phosphatidic acid biosynthetic process (GO:000665... | Function: Short-chain dehydrogenase; part of the gene clu... |
What a model trained on it may say
The rows are what UniProt's curators and automatic annotation assert for each reviewed protein, with InterPro and Pfam matches
computed. A token's evidence may be experimental, inferred by similarity or electronic; filter av_provenance on experimental
codes (such as ECO:0000269, ECO:0000314) for the experimental subset. Absence of a token is not evidence that the protein
lacks the term, and the corpus has no held-out split, so it supports pretraining, retrieval indexes and description generation,
not a held-out claim.
Sources and licence
UniProtKB/Swiss-Prot 2026_03 (CC BY 4.0), with Gene Ontology terms (CC BY 4.0) and InterPro and Pfam references (CC0) as
UniProt carries them; the vocabulary is that of Synthyra/annotation_experimental_v2. Released under CC BY 4.0; cite UniProt.
Files
| File | Holds |
|---|---|
data/train-00000-of-00002.parquet |
the train split |
data/train-00001-of-00002.parquet |
the train split |
vocabulary.parquet |
each token's term: token, term_id, aspect, source_database, accession, label |
receipts/build.json |
the sources and their digests, the counts and the build's timings |
- Downloads last month
- 198