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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
A0A024SMV2 | XDH_TRIR3 | MASGNPYTLKWGIMATGGIAETFCKDLLCNPAIRGADDVRHEIVAVASSSSSKRAEEFLQRIDGAFDAKTYGSYPELVADPNVDIVYVATPHSHHFQNTMLALEAGKNVLCEKAFTVTAAQARKLVETAKAKKLFLMEAVWTRYFPLSIKIRELIAAGEIGTVFRTIADLSINANSEQGQALKFADSHRMVNPDLAGGATLDLGVYPLTWVFQTLYHLQPEEDKEAPTVVASSNKYTTGADENTAIICSFPRHNSIGIASTTMRADTDPEKDTIPAVRIQGSKGEIQVFFPTYRPLKYKVVKTNGEAQTVDCPIPGDPAR... | 1.1.1.179 | null | null | null | D-xylose 1-dehydrogenase (NADP+) activity [GO:0047837]; nucleotide binding [GO:0000166] | PF01408;PF22725; | 3.30.360.10;3.40.50.720; | Gfo/Idh/MocA family | null | null | CATALYTIC ACTIVITY: Reaction=D-xylose + NADP(+) = D-xylono-1,5-lactone + NADPH + H(+); Xref=Rhea:RHEA:22000, ChEBI:CHEBI:15378, ChEBI:CHEBI:15867, ChEBI:CHEBI:53455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.179; Evidence={ECO:0000269|PubMed:18031347}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=250 uM for NADP(+) {ECO:0000269|PubMed:18031347}; KM=43 mM for D-xylose {ECO:0000269|PubMed:18031347}; KM=24 mM for D-glucose {ECO:0000269|PubMed:18031347}; KM=60 mM for L-arabinose {ECO:0000269|PubMed:18031347}; KM=100 mM for D-galactose {ECO:0000269|PubMed:180313... | null | null | null | FUNCTION: NADP-dependent D-xylose dehydrogenase catalyzing the oxydation of D-xylose into D-xylonolactone. Also displays some, albeit lower activity with D-glucose, D-galactose and L-arabinose as substrate. Probably not involved in D-xylose degradation, as it has been shown that H.jecorina assimilates D-xylose via D-xy... | Trichoderma reesei (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / VTT-D-86271 / Rut C-30) (Hypocrea jecorina) | [
7515,
9764,
16354,
19431,
21509,
24471
] | [
"go_mf: nucleotide binding (GO:0000166)",
"interpro: Gfo/Idh/MocA-like oxidoreductase, N-terminal (IPR000683)",
"interpro: NAD(P)-binding domain superfamily (IPR036291)",
"interpro: GFO/IDH/MocA-like oxidoreductase domain (IPR055170)",
"pfam: GFO_IDH_MocA (PF01408)",
"pfam: GFO_IDH_MocA_C3 (PF22725)"
] | [
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"InterPro=match:Pfam"
] | Function: NADP-dependent D-xylose dehydrogenase catalyzing the oxydation of D-xylose into D-xylonolactone. Also displays some, albeit lower activity with D-glucose, D-galactose and L-arabinose as substrate. Probably not involved in D-xylose degradation, as it has been shown that H.jecorina assimilates D-xylose via D-xy... |
A0A024SNB7 | GUN1_TRIR3 | MAPSVTLPLTTAILAIARLVAAQQPGTSTPEVHPKLTTYKCTKSGGCVAQDTSVVLDWNYRWMHDANYNSCTVNGGVNTTLCPDEATCGKNCFIEGVDYAASGVTTSGSSLTMNQYMPSSSGGYSSVSPRLYLLDSDGEYVMLKLNGQELSFDVDLSALPCGENGSLYLSQMDENGGANQYNTAGANYGSGYCDAQCPVQTWRNGTLNTSHQGFCCNEMDILEGNSRANALTPHSCTATACDSAGCGFNPYGSGYKSYYGPGDTVDTSKTFTIITQFNTDNGSPSGNLVSITRKYQQNGVDIPSAQPGGDTISSCPSASA... | 3.2.1.4 | null | carbohydrate metabolic process [GO:0005975] | extracellular region [GO:0005576] | cellulase activity [GO:0008810]; cellulose binding [GO:0030248] | PF00734;PF00840; | 2.70.100.10; | Glycosyl hydrolase 7 (cellulase C) family | PTM: Asn-204 contains mainly a high-mannose-type glycan (Hex(7-9)GlcNAc(2)), with a small fraction (8%) bearing a single GlcNAc at this site. {ECO:0000269|PubMed:12499406}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07981}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000250|UniProtKB:P07981}; | null | null | null | null | FUNCTION: Endoglucanase (EG) that cleaves the internal beta-1,4-glucosidic bonds in cellulose. The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with EGs, which cut internal glycosidic linkages to reduce the polymerization degree of the substrate and creates ne... | Trichoderma reesei (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / VTT-D-86271 / Rut C-30) (Hypocrea jecorina) | [
241,
837,
6485,
8322,
8683,
9557,
10313,
13148,
16198,
16693,
21109,
21177,
24983
] | [
"ec: EC 3.2.1.4",
"go_bp: carbohydrate metabolic process (GO:0005975)",
"go_cc: extracellular region (GO:0005576)",
"go_mf: cellulase activity (GO:0008810)",
"go_mf: cellulose binding (GO:0030248)",
"interpro: Cellulose-binding domain (IPR000254)",
"interpro: Glycoside hydrolase, family 7 (IPR001722)",
... | [
"UniProtKB=ECO:0000250",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000... | Function: Endoglucanase (EG) that cleaves the internal beta-1,4-glucosidic bonds in cellulose. The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with EGs, which cut internal glycosidic linkages to reduce the polymerization degree of the substrate and creates ne... |
A0A026W182 | ORCO_OOCBI | MMKMKQQGLVADLLPNIRVMKTFGHFVFNYYNDNSSKYLHKVYCCVNLFMLLLQFGLCAVNLIVESADVDDLTANTITLLFFTHSIVKICYFAIRSKYFYRTWAIWNNPNSHPLFAESNARYHAIALKKMRLLLFLVGGTTMLAAVAWTVLTFFEHPIRKIVDPVTNETEIIELPQLLIRSFYPFDAGKGITHVLVLVYQFYWVLFMLIDANSLDVLFCSWLLFACEQLQHLKQIMKPLMELSATLDTVVPNSSELFKAGSADHLRDGDNPPPPPPPQSDNMLDLDLRNIYSNRQDFTATFRPTAGMTFNGGVGPNGLTK... | null | null | antennal development [GO:0007469]; detection of chemical stimulus involved in sensory perception of smell [GO:0050911]; detection of pheromone [GO:0043695]; olfactory behavior [GO:0042048]; response to pheromone [GO:0019236]; social behavior [GO:0035176] | plasma membrane [GO:0005886] | odorant binding [GO:0005549]; olfactory receptor activity [GO:0004984] | PF02949; | null | Insect chemoreceptor superfamily, Heteromeric odorant receptor channel (TC 1.A.69) family, Orco subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Odorant coreceptor which complexes with conventional odorant receptors (ORs) to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability (By similarity). Obligate coreceptor of all odorant receptors (By similarity). Orco is a universal and integral part of the f... | Ooceraea biroi (Clonal raider ant) (Cerapachys biroi) | [
1415,
2325,
3195,
3438,
3743,
4519,
6620,
8039,
8181,
11177,
22104,
24856,
25110
] | [
"go_bp: antennal development (GO:0007469)",
"go_bp: response to pheromone (GO:0019236)",
"go_bp: social behavior (GO:0035176)",
"go_bp: olfactory behavior (GO:0042048)",
"go_bp: detection of pheromone (GO:0043695)",
"go_bp: detection of chemical stimulus involved in sensory perception of smell (GO:0050911... | [
"UniProtKB-GO=ECO:0000315",
"UniProtKB-GO=ECO:0000315",
"UniProtKB-GO=ECO:0000315",
"UniProtKB-GO=ECO:0000315",
"UniProtKB-GO=ECO:0000315",
"UniProtKB-GO=ECO:0000315",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000315",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"... | Function: Odorant coreceptor which complexes with conventional odorant receptors (ORs) to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability (By similarity). Obligate coreceptor of all odorant receptors (By similarity). Orco is a universal and integral part of the f... |
A0A031WDE4 | HYPD_CLODI | MARGTFERTKKLREESINAEPHISIERAVLMTEAYKKYEGSVEIPVLRALSFKHYIENRTLSINDGELIVGEKGDSPNGAPTYPEICCHTMEDLEVMHNRDIINFSVSEEARKIHKEEIIPFWKKRQTRDKIINAMTPEWLAAYEAGMFTEFMEQRAPGHTVCGDTIYKKGFLDLKKDIEARLKELDFLNDLDAYNKKADLEAMAIACDAMVILGKRYAEKARQMAEEETDEAKKKDLLLIAETCDVVPAHKPETYHQAIQMYWFVHIGVTTELNIWDAFTPGRLDQHLNPFYERDVENGILDRDRAQELLECLWVKFNN... | 4.2.1.172 | null | L-proline biosynthetic process [GO:0055129] | cytosol [GO:0005829] | carbon-oxygen lyase activity [GO:0016835] | PF01228;PF02901; | 3.20.70.20; | Glycyl radical enzyme (GRE) family, HYPD subfamily | PTM: Requires the activating protein PflE to generate the key active site glycyl radical on Gly-765 that is involved in catalysis. {ECO:0000269|PubMed:28183913}. | null | CATALYTIC ACTIVITY: Reaction=trans-4-hydroxy-L-proline = (S)-1-pyrroline-5-carboxylate + H2O + H(+); Xref=Rhea:RHEA:54644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17388, ChEBI:CHEBI:58375; EC=4.2.1.172; Evidence={ECO:0000269|PubMed:28183913}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 mM for trans-4-hydroxy-L-proline {ECO:0000269|PubMed:28183913}; Note=kcat is 45 sec(-1) for trans-4-hydroxy-L-proline as substrate. {ECO:0000269|PubMed:28183913}; | null | null | null | FUNCTION: Glycine radical enzyme that catalyzes the dehydration of the non-proteinogenic amino acid trans-4-hydroxy-L-proline (Hyp) to produce delta(1)-pyrroline-5-carboxylate (P5C). Is involved in the anaerobic degradation of 4-hydroxyproline. {ECO:0000269|PubMed:28183913}. | Clostridioides difficile (Peptoclostridium difficile) | [
4749,
6588
] | [
"go_bp: L-proline biosynthetic process (GO:0055129)",
"go_cc: cytosol (GO:0005829)"
] | [
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000501"
] | Function: Glycine radical enzyme that catalyzes the dehydration of the non-proteinogenic amino acid trans-4-hydroxy-L-proline (Hyp) to produce delta(1)-pyrroline-5-carboxylate (P5C). Is involved in the anaerobic degradation of 4-hydroxyproline.
Catalytic Activity: trans-4-hydroxy-L-proline = (S)-1-pyrroline-5-carboxyla... |
A0A044RE18 | BLI_ONCVO | MYWQLVRILVLFDCLQKILAIEHDSICIADVDDACPEPSHTVMRLRERNDKKAHLIAKQHGLEIRGQPFLDGKSYFVTHISKQRSRRRKREIISRLQEHPDILSIEEQRPRVRRKRDFLYPDIAHELAGSSTNIRHTGLISNTEPRIDFIQHDAPVLPFPDPLYKEQWYLNNGAQGGFDMNVQAAWLLGYAGRNISVSILDDGIQRDHPDLAANYDPLASTDINGHDDDPTPQDDGDNKHGTRCAGEVASIAGNVYCGVGVAFHAKIGGVRMLDGPVSDSVEAASLSLNRHHIDIYSASWGPEDDGRTFDGPGPLAREAF... | 3.4.21.75 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12855702}; Note=Binds 3 calcium ions per subunit. {ECO:0000250|UniProtKB:P09958}; | cellular response to salt [GO:1902075]; chemosensory behavior [GO:0007635]; collagen and cuticulin-based cuticle development [GO:0040002]; dibasic protein processing [GO:0090472]; positive regulation of synaptic assembly at neuromuscular junction [GO:0045887]; zymogen activation [GO:0031638] | extracellular region [GO:0005576]; Golgi membrane [GO:0000139]; nucleus [GO:0005634]; trans-Golgi network [GO:0005802] | serine-type endopeptidase activity [GO:0004252] | PF01483;PF00082;PF16470; | 2.60.120.260;3.30.70.850;3.40.50.200; | Peptidase S8 family, Furin subfamily | PTM: N-glycosylated. {ECO:0000269|PubMed:12855702}.; PTM: The inhibition peptide, which plays the role of an intramolecular chaperone, is probably autocatalytically removed in the endoplasmic reticulum (ER) and remains non-covalently bound as a potent autoinhibitor. Probably following transport to the trans Golgi, a se... | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:12855702}. | CATALYTIC ACTIVITY: Reaction=Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors.; EC=3.4.21.75; Evidence={ECO:0000269|P... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. Active from pH 7.0 to 8.5. {ECO:0000269|PubMed:12855702}; | null | FUNCTION: Serine endoprotease which cleaves substrates at the RX(K/R)R consensus motif. {ECO:0000269|PubMed:12855702}. | Onchocerca volvulus | [
1484,
2770,
3406,
4024,
5960,
6386,
6485,
6494,
6577,
7773,
9532,
10798,
12445,
13532,
14675,
14911,
14912,
15802,
15997,
16591,
16961,
19935,
20587,
21557,
23990,
24983
] | [
"go_bp: chemosensory behavior (GO:0007635)",
"go_bp: zymogen activation (GO:0031638)",
"go_bp: collagen and cuticulin-based cuticle development (GO:0040002)",
"go_bp: positive regulation of synaptic assembly at neuromuscular junction (GO:0045887)",
"go_bp: cellular response to salt (GO:1902075)",
"go_cc: ... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000314",
"InterPro=match"... | Function: Serine endoprotease which cleaves substrates at the RX(K/R)R consensus motif.
Catalytic Activity: Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand ... |
A0A059J0G5 | MDR1_TRIIM | MASQPPQPPSGQPDTQYEEYQSEVITETTNRPTPAADVYEITPTNDVMDDRYEHEHDDYESGAMYETVRTWSPQSRPELVRIASVFSRIDSHPDVAPTTEDGGQLNRRDTLAGVKIGDPVLDPTKPEFDFYKWARMFTHVMEKEGIKRNRTGVMFRNLTVLGSGSAVQYQDTFLSPFAAPFRPGELCGKGRNPEKVILHDFNGAIREGELLMVLGRPGSGCSTFLKAICGELHGLQKKKESIIHYNGVSQHTFKKELRGEAVYSAEDEHHFPHLTVGQTLEFAAAARTPSKRVLGLSRKDFSTHLARVMMSVFGLSHTYN... | null | null | null | plasma membrane [GO:0005886] | ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887] | PF01061;PF19055;PF00005;PF14510;PF06422; | 3.40.50.300; | ABC transporter superfamily, ABCG family, PDR (TC 3.A.1.205) subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=voriconazole(in) + ATP + H2O = voriconazole(out) + ADP + phosphate + H(+); Xref=Rhea:RHEA:61912, ChEBI:CHEBI:10023, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:F2SHL1}; PhysiologicalDirection=left-to-right; ... | null | null | null | null | FUNCTION: Pleiotropic ABC efflux transporter that may be involved in the modulation susceptibility to a wide range of unrelated cytotoxic compounds, including ethidium bromide, ketoconazole, cycloheximide, fluconazole, griseofulvin, imazalil and itraconazole. {ECO:0000269|PubMed:16519017}. | Trichophyton interdigitale (strain MR816) | [
6620,
8167,
8563,
9349,
10977,
11013,
12661,
13168,
13905,
15266,
15498,
15968,
15969,
17671,
20453,
20454,
20514,
21309,
22826,
23794,
24268,
24856,
25110
] | [
"go_cc: plasma membrane (GO:0005886)",
"go_mf: ATP binding (GO:0005524)",
"go_mf: ATP hydrolysis activity (GO:0016887)",
"go_mf: ABC-type transporter activity (GO:0140359)",
"interpro: ABC transporter-like, ATP-binding domain (IPR003439)",
"interpro: AAA+ ATPase domain (IPR003593)",
"interpro: CDR ABC t... | [
"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: Pleiotropic ABC efflux transporter that may be involved in the modulation susceptibility to a wide range of unrelated cytotoxic compounds, including ethidium bromide, ketoconazole, cycloheximide, fluconazole, griseofulvin, imazalil and itraconazole.
Catalytic Activity: voriconazole(in) + ATP + H2O = voriconaz... |
A0A059J5P2 | DEFTR_TRIIM | MQFTKLATVLIVSLMGSAAIAAPSVDNAPAVAAEEVAAAPAENLEKRGFGCPLNERECHSHCQSIGRKFGYCGGTLRLTCICGKE | null | null | defense response [GO:0006952] | extracellular region [GO:0005576] | null | PF01097; | 3.30.30.10; | Invertebrate defensin family | PTM: Disulfide bonds are essential for antimicrobial activity. {ECO:0000269|PubMed:30102941}. | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Antimicrobial peptide with broad-spectrum activity against Gram-positive bacteria, Gram-negative bacteria, and fungi. Also inhibits clinical isolates, including methicillin-resistant S.aureus (MRSA) (MIC=32 uM), K.pneumoniae, C.albicans and C.parapsilosis. Displays minimal inhibitory concentration (MIC) value... | Trichophyton interdigitale (strain MR816) | [
1190,
6485,
10221,
16484,
21337,
24983
] | [
"go_bp: defense response (GO:0006952)",
"go_cc: extracellular region (GO:0005576)",
"interpro: Defensin, invertebrate/fungal (IPR001542)",
"interpro: Knottin, scorpion toxin-like superfamily (IPR036574)",
"pfam: Defensin_2 (PF01097)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305"
] | Function: Antimicrobial peptide with broad-spectrum activity against Gram-positive bacteria, Gram-negative bacteria, and fungi. Also inhibits clinical isolates, including methicillin-resistant S.aureus (MRSA) (MIC=32 uM), K.pneumoniae, C.albicans and C.parapsilosis. Displays minimal inhibitory concentration (MIC) value... |
A0A059JJ46 | MDR2_TRIIM | MVEVSEKPNTQDDGVSKQENRNPASSSSSTSDKEKVAKKGNSDATKSSTPEDLDAQLAHLPEHEREILKQQLFIPDAKATYGTLFRYATRNDMIFLAIVSLASIAAGAALPLFTVLFGSLAGTFRDIALHRITYDEFNSILTRNSLYFVYLGIAQFILLYVSTVGFIYVGEHITQKIRAKYLHAILRQNIGFFDKLGAGEVTTRITADTNLIQDGISEKVGLTLTALSTFFSAFIIGYVRYWKLALICSSTIVAMILVMGGISRFVVKSGRMTLVSYGEGGTVAEEVISSIRNATAFGTQEKLARQYEVHLKEARKWGRR... | null | null | oligopeptide export from mitochondrion [GO:0090374] | mitochondrial inner membrane [GO:0005743]; plasma membrane [GO:0005886] | ABC-type azole transporter activity [GO:0140394]; ABC-type oligopeptide transporter activity [GO:0015421]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887] | PF00664;PF00005; | 1.20.1560.10;3.40.50.300; | ABC transporter superfamily, ABCB family, Multidrug resistance exporter (TC 3.A.1.201) subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=itraconazole(in) + ATP + H2O = itraconazole(out) + ADP + phosphate + H(+); Xref=Rhea:RHEA:33503, ChEBI:CHEBI:6076, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:F2T1C4}; PhysiologicalDirection=left-to-right; X... | null | null | null | null | FUNCTION: Pleiotropic ABC efflux transporter that may be involved in the modulation susceptibility to a wide range of unrelated cytotoxic compounds, including terbinafine, 4-nitroquinoline N-oxide, and ethidium bromide (PubMed:16849730). May play a role in pathogenicity (PubMed:19141731). {ECO:0000269|PubMed:16849730, ... | Trichophyton interdigitale (strain MR816) | [
6543,
6620,
8167,
8563,
9352,
10977,
11013,
12812,
13905,
15266,
16509,
17097,
20310,
20514,
21060,
24856,
25110
] | [
"go_cc: mitochondrial inner membrane (GO:0005743)",
"go_cc: plasma membrane (GO:0005886)",
"go_mf: ATP binding (GO:0005524)",
"go_mf: ATP hydrolysis activity (GO:0016887)",
"go_mf: ABC-type azole transporter activity (GO:0140394)",
"interpro: ABC transporter-like, ATP-binding domain (IPR003439)",
"inter... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000250",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000250",
... | Function: Pleiotropic ABC efflux transporter that may be involved in the modulation susceptibility to a wide range of unrelated cytotoxic compounds, including terbinafine, 4-nitroquinoline N-oxide, and ethidium bromide. May play a role in pathogenicity.
Catalytic Activity: itraconazole(in) + ATP + H2O = itraconazole(ou... |
A0A059JK44 | MDR4_TRIIM | MAVEEKNSPTGAAMTNTGILVPSSQQSLPEWWTKTQKFFSRENTITPTFGYFRLLFGTQPGKTDIALIVIGTIAGIGAGIPFPLLGILFGELVDDLNSSTCSTTQAPPGGYQAAITTKVLQVIYVSILNFVCMYIHTGCWSMVGERLVRRLRTKYFHSLLRQEIAFTDTLPSGDVTSRLVSDIEVIQAGTSEKVGLFIGTISYFVAAYIVAFLKVATIAAMLMSVVPIYFLMAFGGGHYIKKYSGRISTHINAATSIVSSSLSHMSIVHAFNANARLEALFAQHLVSARMDALKKAITHSIQFGMLYFVAYASNALAFWQ... | null | null | oligopeptide export from mitochondrion [GO:0090374] | mitochondrial inner membrane [GO:0005743]; plasma membrane [GO:0005886] | ABC-type oligopeptide transporter activity [GO:0015421]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887] | PF00664;PF00005; | 1.20.1560.10;3.40.50.300; | ABC transporter superfamily, ABCB family, Multidrug resistance exporter (TC 3.A.1.201) subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Pleiotropic ABC efflux transporter that may be involved in the modulation susceptibility to a wide range of unrelated cytotoxic compounds. {ECO:0000305}. | Trichophyton interdigitale (strain MR816) | [
6543,
6620,
8167,
8563,
10977,
11013,
12812,
13905,
15266,
16509,
17097,
20514,
21060,
24856,
25110
] | [
"go_cc: mitochondrial inner membrane (GO:0005743)",
"go_cc: plasma membrane (GO:0005886)",
"go_mf: ATP binding (GO:0005524)",
"go_mf: ATP hydrolysis activity (GO:0016887)",
"interpro: ABC transporter-like, ATP-binding domain (IPR003439)",
"interpro: AAA+ ATPase domain (IPR003593)",
"interpro: ABC transp... | [
"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:Pfam",
"InterPro=match:Pfam",
"UniPr... | Function: Pleiotropic ABC efflux transporter that may be involved in the modulation susceptibility to a wide range of unrelated cytotoxic compounds.
Subcellular Location: Cell membrane
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 149560
Sequence Length: 1379 |
A0A059Q4T4 | CS_ERYCB | MEMSKKKLEIILRKTIKPSSSTPQHLQTFELSFWDEPLPPDYGTIIFFYQTNGSKNDDDEALSIFFQRSSSLQNSLSKTLIHYYPLAGRLKDDGTAVDCNDEGAYFVEARIDCQLSTLLNHPDADFLSHYFCPALDSNNLPSGCMLAIQLTLFNCGGIAISVSPSHKIADASSACTFVQSWASMTTIGEVAPKPIFLEPSSSPPRSLRNAPMLTEIPGEFVKRRFVFPASKIAQLRTKTTGPSSPTGKQHMSDADLVMALFMKCAILASRSLSKSSSGPYVLFQVVDLRKRVRPPLPANTIGNVVLYYTTQIEENQIELN... | 2.3.1.334 | null | cocaine biosynthetic process [GO:0050799]; tropane alkaloid biosynthetic process [GO:0009710] | null | acyltransferase activity [GO:0016746] | PF02458; | 3.30.559.10; | Plant acyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=ecgonine methyl ester + benzoyl-CoA = cocaine + CoA; Xref=Rhea:RHEA:81559, ChEBI:CHEBI:57287, ChEBI:CHEBI:57369, ChEBI:CHEBI:59908, ChEBI:CHEBI:60056; EC=2.3.1.334; Evidence={ECO:0000269|PubMed:25406120}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:81560; Evidence={ECO:0000269|PubM... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=370 uM for ecgonine methyl ester (in the presence of benzoyl-CoA as acyl donor) {ECO:0000269|PubMed:25406120}; KM=62 uM for ecgonine methyl ester (in the presence of cinnamoyl-CoA as acyl donor) {ECO:0000269|PubMed:25406120}; KM=93 uM for benzoyl-CoA (in the presen... | PATHWAY: Alkaloid biosynthesis; tropane alkaloid biosynthesis. {ECO:0000269|PubMed:25406120}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.4 with ecgonine methyl ester as substrate and benzoyl-CoA as acyl donor. {ECO:0000269|PubMed:25406120}; | null | FUNCTION: Acyltransferase involved in the biosynthesis of tropane (e.g. cocaine) alkaloids natural products, acting as toxic repellents against herbivorous predators and exhibiting antispasmodic, stimulant, anticholinergic and psychoactive effects in medical use (PubMed:25406120). Catalyzes the formation of cocaine fro... | Erythroxylum coca (Coca plant) | [
1698,
8531,
14804
] | [
"go_bp: tropane alkaloid biosynthetic process (GO:0009710)",
"go_mf: acyltransferase activity (GO:0016746)",
"interpro: Chloramphenicol acetyltransferase-like domain superfamily (IPR023213)"
] | [
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000314",
"InterPro=match"
] | Function: Acyltransferase involved in the biosynthesis of tropane (e.g. cocaine) alkaloids natural products, acting as toxic repellents against herbivorous predators and exhibiting antispasmodic, stimulant, anticholinergic and psychoactive effects in medical use. Catalyzes the formation of cocaine from ecgonine methyl ... |
A0A059T2H4 | TX2A_CHEPU | MKFSLFFGVLFLAILHSCLSESEKDLTDEDHFRSSDSFLSEIQEESRGKKCIERNKECTNDRHGCCRGKIFKDKCECVGSGGKERCVCKQKKWAKIIESYIGDIPTLPKPEDDKCVPKHEDCSERKNDCCKSGLFTLKCKCYDMQDDEDGKKTELCGCVQPFEHKAIEQALRFGKWMVG | null | null | null | extracellular region [GO:0005576] | toxin activity [GO:0090729] | PF10530; | null | Spider toxin CSTX family, Double-CSTX subfamily | PTM: Cleavage of the propeptide depends on the processing quadruplet motif (XXXR, with at least one of X being E). {ECO:0000303|PubMed:24717175}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24717175}. | null | null | null | null | null | FUNCTION: Spider venom toxin that exhibits cytolytic activity by forming an alpha-helix across the membrane (By similarity). Lethal to insect larvae (PubMed:24717175). {ECO:0000250|UniProtKB:C0HKG7, ECO:0000269|PubMed:24717175}. | Cheiracanthium punctorium (Yellow sac spider) (Aranea punctoria) | [
6485,
9266,
12752,
14292,
23399,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"go_mf: toxin activity (GO:0090729)",
"interpro: Spider toxin CSTX, Knottin scaffold conserved site (IPR011142)",
"interpro: Spider toxin CSTX, Knottin scaffold (IPR019553)",
"pfam: Toxin_35 (PF10530)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000269",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000269"
] | Function: Spider venom toxin that exhibits cytolytic activity by forming an alpha-helix across the membrane (By similarity). Lethal to insect larvae.
Subcellular Location: Secreted
Domain: The presence of 'disulfide through disulfide knots' structurally defines this protein as a knottin. This toxin contains 2 'disulfid... |
A0A059TC02 | CCR1_PETHY | MRSVSGQVVCVTGAGGFIASWLVKILLEKGYTVRGTVRNPDDPKNGHLRELEGAKERLTLCKADLLDYQSLREAINGCDGVFHTASPVTDDPEQMVEPAVIGTKNVINAAAEANVRRVVFTSSIGAVYMDPNRDPETVVDETCWSDPDFCKNTKNWYCYGKMVAEQAAWEEAKEKGVDLVVINPVLVQGPLLQTTVNASVLHILKYLTGSAKTYANSVQAYVDVKDVALAHILLYETPEASGRYLCAESVLHRGDVVEILSKFFPEYPIPTKCSDVTKPRVKPYKFSNQKLKDLGLEFTPVKQCLYETVKSLQEKGHLPI... | 1.2.1.44 | null | circadian rhythm [GO:0007623]; green leaf volatile biosynthetic process [GO:0010597]; lignin biosynthetic process [GO:0009809]; phenylpropanoid biosynthetic process [GO:0009699] | cytoplasm [GO:0005737] | cinnamoyl-CoA reductase activity [GO:0016621]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616] | PF01370; | 3.40.50.720; | NAD(P)-dependent epimerase/dehydratase family, Dihydroflavonol-4-reductase subfamily | PTM: The formation of a reversible disulfide bond reduces activity by perturbing the positioning of nearby catalytic residues. {ECO:0000269|PubMed:25217505}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24985707}. | CATALYTIC ACTIVITY: Reaction=(E)-coniferaldehyde + NADP(+) + CoA = (E)-feruloyl-CoA + NADPH + H(+); Xref=Rhea:RHEA:64648, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:87305; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}; Ph... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=208.6 uM for p-coumaroyl-CoA {ECO:0000269|PubMed:25217505}; KM=307.6 uM for feruloyl-CoA {ECO:0000269|PubMed:25217505}; KM=270.3 uM for sinapoyl-CoA {ECO:0000269|PubMed:25217505}; Vmax=1235.7 nmol/sec/mg enzyme with p-coumaroyl-CoA as substrate {ECO:0000269|PubMed:... | PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:25217505}; | null | FUNCTION: Involved in the latter stages of lignin biosynthesis (PubMed:24985707). Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (PubMed:24985707, PubMed:25217505). Mediates the conversion of feruloyl CoA to coniferylaldehyde (PubMed... | Petunia hybrida (Petunia) | [
1476,
1696,
1737,
1966,
6538,
8516,
10208,
16354,
18618,
21487,
24883
] | [
"go_bp: circadian rhythm (GO:0007623)",
"go_bp: phenylpropanoid biosynthetic process (GO:0009699)",
"go_bp: lignin biosynthetic process (GO:0009809)",
"go_bp: green leaf volatile biosynthetic process (GO:0010597)",
"go_cc: cytoplasm (GO:0005737)",
"go_mf: oxidoreductase activity, acting on the CH-OH group... | [
"UniProtKB-GO=ECO:0000270",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000315",
"UniProtKB-GO=ECO:0000315",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000269"
] | Function: Involved in the latter stages of lignin biosynthesis. Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes. Mediates the conversion of feruloyl CoA to coniferylaldehyde. Also active toward p-coumaroyl-CoA and sinapoyl-CoA. Involv... |
A0A059U8Y9 | NDBM_MESGB | MQLKKQLIVIFFTYFIVVNESEAFFGALFKLATKIIPSLFRKRKGREVMMKRDLEQLFDPYQRNLELDRLLKQLPNY | null | null | null | extracellular region [GO:0005576] | null | null | null | Non-disulfide-bridged peptide (NDBP) superfamily, Medium-length antimicrobial peptide (group 3) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29896190}. Target cell membrane {ECO:0000305}. | null | null | null | null | null | FUNCTION: Antimicrobial peptide with potent activity against bacteria. Acts by fastly disrupting the bacterial membrane. Shows activity against Gram-positive bacteria S.aureus (MIC=1.5-3.0 uM) and S.epidermidis (MIC=1.5 uM), M.luteus (MIC>48.3 uM), B.thuringiensis (MIC=1.5 uM), B.subtilis (MIC=3 uM) and Gram-negative b... | Mesobuthus gibbosus (Mediterranean checkered scorpion) (Buthus gibbosus) | [
6485,
24983,
25059
] | [
"go_cc: extracellular region (GO:0005576)",
"subcellular_location: Secreted (SL-0243)",
"subcellular_location: Target cell membrane (SL-0451)"
] | [
"UniProtKB-GO=ECO:0000269",
"UniProtKB=ECO:0000269",
"UniProtKB=ECO:0000305"
] | Function: Antimicrobial peptide with potent activity against bacteria. Acts by fastly disrupting the bacterial membrane. Shows activity against Gram-positive bacteria S.aureus (MIC=1.5-3.0 uM) and S.epidermidis (MIC=1.5 uM), M.luteus (MIC>48.3 uM), B.thuringiensis (MIC=1.5 uM), B.subtilis (MIC=3 uM) and Gram-negative b... |
A0A059U906 | KA145_MESGB | MKIFFAILLILAVCSMAIWTVNGTPFAIRCKTDSDCSYKCPGNPPCRNGFCKCT | null | null | null | extracellular region [GO:0005576] | null | null | null | Short scorpion toxin superfamily, Potassium channel inhibitor family, Alpha-KTx 14 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q95NK7}. | null | null | null | null | null | FUNCTION: Inhibits potassium channels. May be active towards small conductance calcium-activated potassium channels (KCNN, SK), and less active towards voltage-gated potassium channels (Kv/KCN). {ECO:0000250|UniProtKB:Q95NK7}. | Mesobuthus gibbosus (Mediterranean checkered scorpion) (Buthus gibbosus) | [
6485,
16484,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"interpro: Knottin, scorpion toxin-like superfamily (IPR036574)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000250",
"InterPro=match",
"UniProtKB=ECO:0000250"
] | Function: Inhibits potassium channels. May be active towards small conductance calcium-activated potassium channels (KCNN, SK), and less active towards voltage-gated potassium channels (Kv/KCN).
Subcellular Location: Secreted
Domain: Has the structural arrangement of an alpha-helix connected to a beta-sheet by disulfid... |
A0A059UEE4 | KA274_MESGB | MKFLFLTLVLLYFTAILVFIVFPSYAQIQTNASCTTSTHCVEPCRKRCLLIHKCINDKCTCYPRINICEKKNN | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200] | PF00451; | 3.30.30.10; | Short scorpion toxin superfamily, Potassium channel inhibitor family, Alpha-KTx 27 subfamily | PTM: Contains 4 disulfide bonds. {ECO:0000305}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | null | Mesobuthus gibbosus (Mediterranean checkered scorpion) (Buthus gibbosus) | [
6485,
8231,
10439,
16484,
20900,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"go_mf: ion channel inhibitor activity (GO:0008200)",
"interpro: Scorpion short chain toxin, potassium channel inhibitor (IPR001947)",
"interpro: Knottin, scorpion toxin-like superfamily (IPR036574)",
"pfam: Toxin_2 (PF00451)",
"subcellular_location: Secreted (S... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000250"
] | Subcellular Location: Secreted
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
PTM: Contains 4 disulfide bonds.
Sequence Mass (Da): 8479
Sequence Length: 73 |
A0A059UI21 | KA263_MESGB | MSGLSVFILIALVLSVIIDVLNNSKVEAACKENCRQYCQAKGARNGKCINSNCKCYY | null | null | null | extracellular region [GO:0005576] | null | null | null | Short scorpion toxin superfamily, Potassium channel inhibitor family, Alpha-KTx 26 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Recombinant toxin that reversibly inhibits the potassium current of mKv1.3/KCNA3 channel stably expressed in COS7 cells (IC(50)=150 nM). {ECO:0000250|UniProtKB:A7KJJ7}. | Mesobuthus gibbosus (Mediterranean checkered scorpion) (Buthus gibbosus) | [
6485,
16484,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"interpro: Knottin, scorpion toxin-like superfamily (IPR036574)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"UniProtKB=ECO:0000250"
] | Function: Recombinant toxin that reversibly inhibits the potassium current of mKv1.3/KCNA3 channel stably expressed in COS7 cells (IC(50)=150 nM).
Subcellular Location: Secreted
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Sequence Ma... |
A0A059UI30 | KBX1_MESGB | MQRNLVVLLFLGMVALSSCGLREKHFQKLVKYAVPEGTLRTIIQTAVHKLGKTQFGCPAYQGYCDDHCQDIKKQEGFCHGFKCKCGIPMGF | null | null | null | extracellular region [GO:0005576] | null | PF14866; | null | Long chain scorpion toxin family, Class 1 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24746279}. | null | null | null | null | null | FUNCTION: Inhibits voltage-gated potassium channel. {ECO:0000250|UniProtKB:P69940}. | Mesobuthus gibbosus (Mediterranean checkered scorpion) (Buthus gibbosus) | [
6485,
15464,
23865,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"interpro: Long chain scorpion toxin, cysteine-stabilized alpha/beta domain (IPR029237)",
"pfam: Scorpion_toxin_alpha-beta (PF14866)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305"
] | Function: Inhibits voltage-gated potassium channel.
Subcellular Location: Secreted
Sequence Mass (Da): 10211
Sequence Length: 91 |
A0A059WGE7 | RPH_STRSQ | MSGRLVVDLQDVDAAGLAEVGGKGAHLGELSRIDGVRVPSGFCVTTHAFRRIMAEAPESGELLDRLSRVDEGDQEAVRSLAARLRQVVGATPLPDEVAAAVTGALARHGERSAYAVRSSATAEDLPTASFAGQQDTYLNVVGTEEILRHVSRCWASLFTERAVTYRGRQGVDHRTVHMGVVVQRMVVPRASGILFTADPVTGDRRTATVDAGFGLGEALVSGLVDPDVLTVRHGEVVARTIAAKRRALHAVQGGGTRETPIEERRQREPVLTDDQAVELVALGRRIEAHFGSPQDIEWCLDDDGFHIVQSRPITTLFPVP... | 2.7.9.6 | null | null | null | ATP binding [GO:0005524]; kinase activity [GO:0016301] | PF00391;PF01326;PF27448; | 3.30.1490.20;3.30.470.20;3.50.30.10; | Rifampicin phosphotransferase family | null | null | CATALYTIC ACTIVITY: Reaction=rifampicin + ATP + H2O = 21-phosphorifampicin + AMP + phosphate + 2 H(+); Xref=Rhea:RHEA:56304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:71365, ChEBI:CHEBI:140195, ChEBI:CHEBI:456215; EC=2.7.9.6; Evidence={ECO:0000269|PubMed:24778229}; Physiolo... | null | null | null | null | FUNCTION: Catalyzes the phosphorylation of rifampicin, also known as rifampin (RIF), leading to its inactivation (PubMed:24778229). Confers high level resistance to a variety of clinically used rifamycin antibiotics (PubMed:24778229). {ECO:0000269|PubMed:24778229}. | Streptomyces sp | [
8167,
8496,
10565,
12309,
13273,
16506,
20854,
21473
] | [
"go_mf: ATP binding (GO:0005524)",
"go_mf: kinase activity (GO:0016301)",
"interpro: Pyruvate phosphate dikinase, AMP/ATP-binding (IPR002192)",
"interpro: PEP-utilising enzyme, mobile domain (IPR008279)",
"interpro: ATP-grasp fold, subdomain 1 (IPR013815)",
"interpro: Phosphohistidine domain superfamily (... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"InterPro=match:Pfam"
] | Function: Catalyzes the phosphorylation of rifampicin, also known as rifampin (RIF), leading to its inactivation. Confers high level resistance to a variety of clinically used rifamycin antibiotics.
Catalytic Activity: rifampicin + ATP + H2O = 21-phosphorifampicin + AMP + phosphate + 2 H(+)
Domain: Contains three domai... |
A0A059WI14 | ARSI_BACX0 | MKYAHVGLNVTNLEKSIEFYSKLFGAEPVKVKPDYAKFLLESPGLNFTLNLRDEVNGNQVGHFGIQVESTEEVVAHKNRLAENGILSQYDEINTTCCYALQDKFWIHDPDGNEWEFFYTKTTVEENSTHPPTCCVNEPNVEKAECCSPTASSNKDTSNCCS | 1.13.11.- | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:24821808, ECO:0000269|PubMed:28936873}; | response to cadmium ion [GO:0046686] | null | null | PF00903; | 3.10.180.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=methylarsonous acid + AH2 + O2 = arsenite + methanol + A + H(+); Xref=Rhea:RHEA:82323, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:17790, ChEBI:CHEBI:17826, ChEBI:CHEBI:29242; Evidence={ECO:0000269|PubMed:24821808, ECO:0000269|PubMed:28936873}; Ph... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.9 uM for methylarsonous acid {ECO:0000269|PubMed:24821808}; KM=6.4 uM for roxarsone (III) {ECO:0000269|PubMed:24821808}; Note=kcat is 0.25 min(-1) with methylarsonous acid as substrate. kcat is 0.22 min(-1) with roxarsone (III) as substrate. {ECO:0000269|PubMed:2... | null | null | null | FUNCTION: Nonheme iron-dependent dioxygenase that can break carbon-arsenic bonds, playing a role in the detoxification of environmental organoarsenical compounds. Catalyzes the oxygen-dependent demethylation of highly toxic methylarsonous acid (MAs(III)) to arsenite, which can then be exported out of the cell. Can also... | Bacillus sp. (strain MD1) | [
4138,
11258,
15450,
16803,
19928,
21216
] | [
"go_bp: response to cadmium ion (GO:0046686)",
"interpro: Glyoxalase/fosfomycin resistance/dioxygenase domain (IPR004360)",
"interpro: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (IPR029068)",
"interpro: Vicinal oxygen chelate (VOC), core domain (IPR037523)",
"cofactor: Fe(2+) (CHE... | [
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000269",
"InterPro=match:Pfam"
] | Function: Nonheme iron-dependent dioxygenase that can break carbon-arsenic bonds, playing a role in the detoxification of environmental organoarsenical compounds. Catalyzes the oxygen-dependent demethylation of highly toxic methylarsonous acid (MAs(III)) to arsenite, which can then be exported out of the cell. Can also... |
A0A059WLZ7 | CNDA_RHIWD | MFLQNAWYAVAWCDEVTDGIVTRKVLGRELALFRDGEGQPRAILNRCPHRFAPLSLGKRIGDAIQCPYHGLHFGPDGRCVHNPHGDGVVPDVATPTFPARERHKLIWAWMGDPALATDDIAGGEYGYLDDVELDLLPRGHLHLDCDYRLVIDNLMDPAHVAVLHDSALASEALIRAVPRVWREEDVIRVESWAPDSKPSFLFGAWLGNHDDPVDHWVASRWQAAGLLSVEGGVVAVGGDREDGLRVRGAHMITPETETSAHYFWAVVRNFREDDAEQSEQIRATTAAIFTGEDKWMLEAIERSMDGEEFWSLRPAILGTD... | 1.14.15.23 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250|UniProtKB:Q5S3I3}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250|UniProtKB:Q5S3I3}; | null | null | 2 iron, 2 sulfur cluster binding [GO:0051537]; oxidoreductase activity [GO:0016491] | PF00355;PF19112; | 3.90.380.10;2.102.10.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=butachlor + 2 reduced [2Fe-2S]-[ferredoxin] + O2 + 2 H(+) = butyl formate + N-(2,6-diethylphenyl)-2-chloroacetamide + 2 oxidized [2Fe-2S]-[ferredoxin] + H2O; Xref=Rhea:RHEA:52204, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:3230, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:24928877}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:24928877}; | FUNCTION: Component of the chloroacetanilide N-alkylformylase multicomponent enzyme system involved in the degradation of chloroacetanilide herbicides (N-alkoxyalkyl-N-chloroacetyl-substituted aniline derivatives). In vitro, catalyzes the N-dealkylation of butachlor, alachlor and acetochlor to yield 2-chloro-N-(2,6-die... | Rhizorhabdus wittichii (strain DC-6 / KACC 16600) (Sphingomonas wittichii) | [
8506,
9138,
13934,
16645,
18709,
19956,
20825
] | [
"go_mf: oxidoreductase activity (GO:0016491)",
"go_mf: 2 iron, 2 sulfur cluster binding (GO:0051537)",
"interpro: Rieske [2Fe-2S] iron-sulphur domain (IPR017941)",
"interpro: Rieske [2Fe-2S] iron-sulphur domain superfamily (IPR036922)",
"interpro: Cholesterol 7-desaturase (IPR050584)",
"cofactor: [2Fe-2S]... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000250",
"InterPro=match:Pfam"
] | Function: Component of the chloroacetanilide N-alkylformylase multicomponent enzyme system involved in the degradation of chloroacetanilide herbicides (N-alkoxyalkyl-N-chloroacetyl-substituted aniline derivatives). In vitro, catalyzes the N-dealkylation of butachlor, alachlor and acetochlor to yield 2-chloro-N-(2,6-die... |
A0A059WYP6 | TET50_UNKP | MTKHIKILVIGVGVAGPAVAYWLKRFGFSPVLIEKSAAVRKGGQALDIRGIATHIAKEMGIYDQICNMRTQIKCGRYVDVKGNVLHEEQGETFGFRQDDEVEILRGDLVEILMKAIADIPCEFKQSVIKIEQNEDSVTVTYKDGRVENYDLVIAADGIHSATRGMVFSKNEYQLINLGSYVSAFTIPNYLGLDHMELLCESNHKLVTLQSDSQADKAMAGFMFRSKHVLEDIRDEQEQKHFLHASFQNFGWETQNILNRMPESDDFYFDAITQIKMKSWTKGRIALIGDAAYCPSPLSGQGNNLAFVGAYILAGELKKAD... | 1.14.13.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:28481346}; Note=Binds 1 FAD per subunit; it is seen bound in two conformations. {ECO:0000269|PubMed:28481346}; | null | null | FAD binding [GO:0071949] | PF01494; | 3.30.9.10;3.50.50.60; | Aromatic-ring hydroxylase family | null | null | CATALYTIC ACTIVITY: Reaction=a tetracycline + NADPH + O2 + H(+) = a (1S,10aS)-3-(CONH2)-1-(Me2N)-3,3a,4,6-(HO)4-2,5-dioxo-1H,10aH,11H,11aH-cyclopenta[b]anthracene + CO + NADP(+) + H2O; Xref=Rhea:RHEA:61564, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=17 uM for tetracycline {ECO:0000269|PubMed:28481346}; KM=6.3 uM for chlortetracycline {ECO:0000269|PubMed:28481346}; Note=kcat for tetracycline is 4.3 min(-1), kcat for chlortetracycline is 3.5 min(-1). {ECO:0000269|PubMed:28481346}; | null | null | null | FUNCTION: An FAD-requiring monooxygenase active on tetracycline antibiotic and some of its derivatives, which leads to their inactivation (PubMed:26097034). Expression in E.coli confers high resistance to tetracycline and oxytetracycline, does not confer resistance to minocycline or tigecycline. Degrades tetracycline a... | Unknown prokaryotic organism | [
9248,
10825,
16307,
19943,
21565
] | [
"go_mf: FAD binding (GO:0071949)",
"interpro: FAD-binding domain (IPR002938)",
"interpro: FAD/NAD(P)-binding domain superfamily (IPR036188)",
"cofactor: FAD (CHEBI:57692)",
"pfam: FAD_binding_3 (PF01494)"
] | [
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000269",
"InterPro=match:Pfam"
] | Function: An FAD-requiring monooxygenase active on tetracycline antibiotic and some of its derivatives, which leads to their inactivation. Expression in E.coli confers high resistance to tetracycline and oxytetracycline, does not confer resistance to minocycline or tigecycline. Degrades tetracycline and oxytetracycline... |
A0A059XKS9 | CRT_TOXGO | MPPAHHGSGGRRRPGRGNKGKRDTEAGMTASPDPGYMRPETHAAPSQQTDVRSPASAREHRNADVGVAAPDALTPNAGEQKEVEGVAKVNVAVSSDQPPDWAPSQSDLPPSLSPTTASRPATSSRSPRARSRHSPVASSSAFSSPAPSASALTSASGVPEAPLAAPELKHTLAADEGNPEPRLEGPVERLHARQENPLTDSSDGSYILLEEGESQRACLDRKNRHLRQTTPPGVWTTADLASQNSHSASFASGFRRALLPSGGSGDHDEQASDCRASLRGMQRPCFGSPSTDTRMGAAEGLPLASRRRRQHWRRELRAFG... | null | null | null | vacuolar membrane [GO:0005774] | null | PF08627; | null | CRT-like transporter family | null | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:24859994}; Multi-pass membrane protein {ECO:0000255}. Note=In intracellular parasites, localizes to a population of multiple dynamic vesicles originated from the vacuole compartment (PubMed:24859994). In extracellular parasites, also localizes to the vacuole st... | null | null | null | null | null | FUNCTION: Nutrient transporter (By similarity). Involved in maintaining the osmotic homeostasis of the digestive vacuole (PubMed:31170269, PubMed:31387907). Required for the proper organization of the endolysosomal system and, in turn, indirectly for microneme secretion and parasite invasion (PubMed:31170269). Required... | Toxoplasma gondii | [
6557,
16741,
25001,
25110
] | [
"go_cc: vacuolar membrane (GO:0005774)",
"interpro: Multidrug transporter EmrE superfamily (IPR037185)",
"subcellular_location: Vacuole membrane (SL-0271)",
"membrane_topology: Multi-pass membrane protein (SL-9909)"
] | [
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"UniProtKB=ECO:0000269",
"UniProtKB=ECO:0000255"
] | Function: Nutrient transporter (By similarity). Involved in maintaining the osmotic homeostasis of the digestive vacuole. Required for the proper organization of the endolysosomal system and, in turn, indirectly for microneme secretion and parasite invasion. Required for bradyzoite viability and cyst development.
Subce... |
A0A059ZRB8 | HPHA_ACIBA | MKISQLFLGLVACSTAFAYAGIDGISSNESNIKIGAAANASHPGGVAAVSVQAAGAPYNAFTGFSSLKGLAQAFAAQGTSNTNVTVGSKTFNISHIPVSAMPPSHSALGNFNFGQVGTQEVYFGEWWKAGDTPASASHTVYYAGDNTNTTVPTAGTATYTVAGINGSASNLLSGTFTANYGAGTLEGTLTGTGTAVSSLSLDGVAFNPGTAAFAGLATANGTAGVDNSGVVQGQFFGANASALAGIAQFDNVSYNTAFGGAKN | null | null | null | extracellular region [GO:0005576] | null | PF22829;PF22828; | 2.40.160.90; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34725337}. Note=Secretion through the outer membrane is HsmA-dependent. {ECO:0000269|PubMed:34725337}. | null | null | null | null | null | FUNCTION: Part of a high affinity heme acquisition system (PubMed:34725337). Functions as a hemophore that acquires heme from human hemoglobin and delivers the heme to its cognate receptor, HphR, facilitating transport of heme across the bacterial outer membrane (PubMed:34725337). Apo HphA interacts specifically with h... | Acinetobacter baumannii | [
6485,
12766,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"interpro: Outer membrane protein/outer membrane enzyme PagP-like, beta-barrel superfamily (IPR011250)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000269",
"InterPro=match",
"UniProtKB=ECO:0000269"
] | Function: Part of a high affinity heme acquisition system. Functions as a hemophore that acquires heme from human hemoglobin and delivers the heme to its cognate receptor, HphR, facilitating transport of heme across the bacterial outer membrane. Apo HphA interacts specifically with human hemoglobin and steals heme thro... |
A0A059ZV61 | SUS_ACICK | MIEALRQQLLDDPRSWYAFLRHLVASQRDSWLYTDLQRACADFREQLPEGYAEGIGPLEDFVAHTQEVIFRDPWMVFAWRPRPGRWIYVRIHREQLALEELSTDAYLQAKEGIVGLGAEGEAVLTVDFRDFRPVSRRLRDESTIGDGLTHLNRRLAGRIFSDLAAGRSQILEFLSLHRLDGQNLMLSNGNTDFDSLRQTVQYLGTLPRETPWAEIREDMRRRGFAPGWGNTAGRVRETMRLLMDLLDSPSPAALESFLDRIPMISRILIVSIHGWFAQDKVLGRPDTGGQVVYILDQARALEREMRNRLRQQGVDVEPRI... | 2.4.1.13 | null | sucrose metabolic process [GO:0005985] | null | sucrose synthase activity [GO:0016157] | PF00534;PF00862;PF24862;PF24861; | 1.20.120.1230;3.10.450.330;3.40.50.2000; | Glycosyltransferase 1 family | null | null | CATALYTIC ACTIVITY: Reaction=an NDP-alpha-D-glucose + D-fructose = a ribonucleoside 5'-diphosphate + sucrose + H(+); Xref=Rhea:RHEA:16241, ChEBI:CHEBI:15378, ChEBI:CHEBI:17992, ChEBI:CHEBI:37721, ChEBI:CHEBI:57930, ChEBI:CHEBI:76533; EC=2.4.1.13; Evidence={ECO:0000269|PubMed:25846332}; CATALYTIC ACTIVITY: Reaction=ADP-... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.17 mM for ADP in sucrose breakdown {ECO:0000269|PubMed:25846332}; KM=16.9 mM for CDP in sucrose breakdown {ECO:0000269|PubMed:25846332}; KM=8.5 mM for GDP in sucrose breakdown {ECO:0000269|PubMed:25846332}; KM=7.8 mM for UDP in sucrose breakdown {ECO:0000269|PubM... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:25846332}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. Remains stable after 15 minutes at 60 degrees Celsius. {ECO:0000269|PubMed:25846332}; | FUNCTION: Catalyzes the reversible conversion of sucrose and a nucleotide disphosphate (NDP) into fructose and NDP-glucose; although the reaction is freely reversible in vitro, the physiological reaction seems to be sucrose cleavage. Unlike characterized plant enzymes prefers ADP as a cosubstrate, whereas plants prefer... | Acidithiobacillus caldus (strain ATCC 51756 / DSM 8584 / KU) | [
8479,
9609,
10098,
13010,
19550,
19551,
20958,
21192,
24637,
24638
] | [
"go_mf: sucrose synthase activity (GO:0016157)",
"interpro: Sucrose synthase, first GT-B domain (IPR000368)",
"interpro: Glycosyl transferase, family 1 (IPR001296)",
"interpro: Sucrose synthase, plant/cyanobacteria (IPR012820)",
"interpro: Sucrose synthase, N-terminal (IPR056735)",
"interpro: Sucrose synt... | [
"UniProtKB-GO=ECO:0000269",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"InterPro=match:Pfam",
"InterPro=match:Pfam",
"InterPro=match:Pfam"
] | Function: Catalyzes the reversible conversion of sucrose and a nucleotide disphosphate (NDP) into fructose and NDP-glucose; although the reaction is freely reversible in vitro, the physiological reaction seems to be sucrose cleavage. Unlike characterized plant enzymes prefers ADP as a cosubstrate, whereas plants prefer... |
A0A060A682 | HAP2_TETTH | MKFLAFGLIYFHFCILNRCEYITSSTIQKCYNSSNEPNNCSQKAVIVLSLENGQIANTEQVVATLNQLSDSGVNKQLQNSFIFEVTKSPVTALFPLIYLQDFNSQPLEQVIATTLFSCKDGFYDSSPTCKFQYDSKGQKILDSQGYCCYCSLSDILGMGNDLSRGKVCYALNLGAGSATAHCLKFSPLWYSAFKIQQYQLYFEVNINIYTVDSQNQKNLKQTLKLSTSNPTMKSSDNSTISKIIGTFTPTQPPADLSSYYLVKPSFPATDPRVLQGISSWMFVDKTMFTLDGTQCNKIGVSYSGFRQQSSSCSQPVGSCL... | null | null | fertilization [GO:0009566]; single fertilization [GO:0007338] | anchoring junction [GO:0070161]; cell-cell junction [GO:0005911]; plasma membrane [GO:0005886] | fusogenic activity [GO:0140522] | PF10699; | null | HAP2/GCS1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:25155508, ECO:0000305|PubMed:28238660}; Single-pass type I membrane protein {ECO:0000255}. Cell junction {ECO:0000269|PubMed:25155508, ECO:0000269|PubMed:28238660}. Note=Detected at the mating junction. {ECO:0000269|PubMed:25155508, ECO:0000269|PubMed:28238660}. | null | null | null | null | null | FUNCTION: During fertilization, required for the formation of intercellular membrane pores and subsequent exchange of gametic pronuclei between cells. Probably initiates the formation of intercellular membrane pores by inserting part of its extracellular domain into the cell membrane of the adjoining cell in the mating... | Tetrahymena thermophila | [
1362,
1649,
6620,
6628,
7250,
24855,
24856,
25106
] | [
"go_bp: single fertilization (GO:0007338)",
"go_bp: fertilization (GO:0009566)",
"go_cc: plasma membrane (GO:0005886)",
"go_cc: cell-cell junction (GO:0005911)",
"go_cc: anchoring junction (GO:0070161)",
"subcellular_location: Cell junction (SL-0038)",
"subcellular_location: Cell membrane (SL-0039)",
... | [
"UniProtKB-GO=ECO:0000315",
"UniProtKB-GO=ECO:0000315",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000269",
"UniProtKB=ECO:0000269",
"UniProtKB=ECO:0000305",
"UniProtKB=ECO:0000255"
] | Function: During fertilization, required for the formation of intercellular membrane pores and subsequent exchange of gametic pronuclei between cells. Probably initiates the formation of intercellular membrane pores by inserting part of its extracellular domain into the cell membrane of the adjoining cell in the mating... |
A0A060D764 | GRF1_MAIZE | MAMPYASLSPAGAADHRSSTATASLVPFCRSTPLSAGGGLGEEDAQASARWPAARPVVPFTPAQYQELEQQALIYKYLVAGVPVPPDLVVPIRRGLDSLATRFYGQPTLGYGPYLGRKLDPEPGRCRRTDGKKWRCSKEAAPDSKYCERHMHRGRNRSRKPVETQLAPQSQPPAAAAVSAAPPLAAAAAATTNGSGFQNHSLYPAIAGSTGGGGGVGGSGNISSPFSSSMGGSSQLHMDSAASYSYAALGGGTAKDLRYNAYGIRSLADEHNQLIAEAIDSSIESQWRLPSSSFPLSSYPHLGALGDLGGQNSTVSSLPK... | null | null | DNA-templated transcription [GO:0006351]; leaf development [GO:0048366]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription [GO:0006355] | nucleus [GO:0005634] | ATP binding [GO:0005524] | PF08880;PF08879; | null | GRF family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU01002}. | null | null | null | null | null | FUNCTION: Transcription activator that plays a role in the regulation of cell expansion in developing leaves (PubMed:26036253). Component of a network formed by the microRNA396 (miRNA396), the GRFs and their interacting factors (GIFs) acting in the regulation of meristem function and the transition between cell divisio... | Zea mays (Maize) | [
954,
957,
4026,
4259,
6494,
8167,
13466,
13467,
15595,
23244,
23245,
24954
] | [
"go_bp: DNA-templated transcription (GO:0006351)",
"go_bp: regulation of DNA-templated transcription (GO:0006355)",
"go_bp: positive regulation of DNA-templated transcription (GO:0045893)",
"go_bp: leaf development (GO:0048366)",
"go_cc: nucleus (GO:0005634)",
"go_mf: ATP binding (GO:0005524)",
"interpr... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000318",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000315",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000255"
] | Function: Transcription activator that plays a role in the regulation of cell expansion in developing leaves. Component of a network formed by the microRNA396 (miRNA396), the GRFs and their interacting factors (GIFs) acting in the regulation of meristem function and the transition between cell division and cell expansi... |
A0A060KY90 | MYC1_SOLLC | MTDYRLWSNTNTTNTCDDTMMMDSFLSSDPSSFWPASTPNRPTPVNGVGETMPFFNQESLQQRLQALIDGARESWAYAIFWQSSVVDFASQTVLGWGDGYYKGEEDKNKRRGSSSSAANFVAEQEHRKKVLRELNSLISGVQASAGNGTDDAVDEEVTDTEWFFLISMTQSFVNGNGLPGLAMYSSSPIWVTGTEKLAASQCERARQAQGFGLQTIVCIPSANGVVELGSTELIFQSSDLMNKVKYLFNFNIDMGSVTGSGSGSGSCAVHPEPDPSALWLTDPSSSVVEPKDSLIHSSSRDVQLVYGNENSENQQQHCQG... | null | null | positive regulation of DNA-templated transcription [GO:0045893]; trichome morphogenesis [GO:0010090] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; protein dimerization activity [GO:0046983]; sequence-specific DNA binding [GO:0043565] | PF14215;PF22754;PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. | null | null | null | null | null | FUNCTION: Transcriptional activator that binds to the G-box motif (5'-AACGTG-3') found in a number of promoters of jasmonate-induced genes (PubMed:15231736). Transcription activator involved in the transcriptional regulation of terpene biosynthesis in glandular trichomes (PubMed:24884371, PubMed:30518626). Binds to the... | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) | [
1836,
4026,
6494,
7602,
8963,
9033,
12826,
15074,
16507,
17874,
19395,
20519,
23765,
24473,
24954
] | [
"go_bp: trichome morphogenesis (GO:0010090)",
"go_bp: positive regulation of DNA-templated transcription (GO:0045893)",
"go_cc: nucleus (GO:0005634)",
"go_mf: DNA-binding transcription factor activity (GO:0003700)",
"go_mf: sequence-specific DNA binding (GO:0043565)",
"go_mf: protein dimerization activity... | [
"UniProtKB-GO=ECO:0000315",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"InterPro=m... | Function: Transcriptional activator that binds to the G-box motif (5'-AACGTG-3') found in a number of promoters of jasmonate-induced genes. Transcription activator involved in the transcriptional regulation of terpene biosynthesis in glandular trichomes. Binds to the promoter of the linalool synthase TPS5 and promotes ... |
A0A060L102 | OLEG_PINMS | MQKIHDHTPNPTQILGFITLFVSGAVLLFLTGLTLTGTVVGLVVLTPVLIFFSPILIPLATVLFVAVAGFLSAGGFGLAALSAISWLYNYIKGRHPPGADQIDYARMRIADTATHVKDYAREYGGYLQSKIQDAAPGA | null | null | lipid storage [GO:0019915] | lipid droplet [GO:0005811]; membrane [GO:0016020]; monolayer-surrounded lipid storage body [GO:0012511] | null | PF01277; | null | Oleosin family | null | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:24954070}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Surface of oil bodies. Oleosins exist at a monolayer lipid/water interface. {ECO:0000305}. | null | null | null | null | null | null | Pinus massoniana (Chinese red pine) | [
2382,
6578,
6714,
6727,
9501,
21453,
24924,
24930,
25110
] | [
"go_bp: lipid storage (GO:0019915)",
"go_cc: lipid droplet (GO:0005811)",
"go_cc: monolayer-surrounded lipid storage body (GO:0012511)",
"go_cc: membrane (GO:0016020)",
"interpro: Oleosin (IPR000136)",
"pfam: Oleosin (PF01277)",
"subcellular_location: Lipid droplet (SL-0154)",
"subcellular_location: M... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000269",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000269",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Lipid droplet; Membrane
Location Topology: Multi-pass membrane protein
Domain: The proline-knot motif may be involved in targeting to lipid bodies.
Sequence Mass (Da): 14717
Sequence Length: 138 |
A0A060L4I9 | OLEL_PINMS | MEAAQQKNESVMDYAPDWTQISVLFFVVMGGGVLASLSALALAGTVVLMLILTPVFLLLSPVILPVGAVIALAAAAFMAAVTIGIAGAAALIWVYRYARGQPTVGSEKIDRARVRLFEAAEKLKAQLQYKLFNENSKANFD | null | null | lipid storage [GO:0019915] | lipid droplet [GO:0005811]; membrane [GO:0016020]; monolayer-surrounded lipid storage body [GO:0012511] | null | PF01277; | null | Oleosin family | null | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:24954070}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Surface of oil bodies. Oleosins exist at a monolayer lipid/water interface. {ECO:0000305}. | null | null | null | null | null | null | Pinus massoniana (Chinese red pine) | [
2382,
6578,
6714,
6727,
9501,
21453,
24924,
24930,
25110
] | [
"go_bp: lipid storage (GO:0019915)",
"go_cc: lipid droplet (GO:0005811)",
"go_cc: monolayer-surrounded lipid storage body (GO:0012511)",
"go_cc: membrane (GO:0016020)",
"interpro: Oleosin (IPR000136)",
"pfam: Oleosin (PF01277)",
"subcellular_location: Lipid droplet (SL-0154)",
"subcellular_location: M... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000269",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000269",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Lipid droplet; Membrane
Location Topology: Multi-pass membrane protein
Domain: The proline-knot motif may be involved in targeting to lipid bodies.
Sequence Mass (Da): 15060
Sequence Length: 141 |
A0A060LAL9 | PXG_PINMS | MASNESLQTTAAMAPVTIERRVNPNLDDELPKPFLPRALVAVDTEHPSGTPGHQHGDMSVLQQHVAFSNRNNDGIVYPWETFLGFRAVGFNIIISFFGCLIINIFLSYPTLPGWIPSPFFPIYIDRIHRAKHGSDSEVYDTEGRFVPAKFEEIFTKNAKTHPDKLSFSELWNLTEHNRNALDPLGWIAAKLEWFLLYSLAKDPHGFVPKEAARGVFDGSLFEFCEKSRKVKQATVKSLTFKI | 1.11.2.3 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group. {ECO:0000250|UniProtKB:O81270}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:O22788}; | negative regulation of lipid storage [GO:0010888] | lipid droplet [GO:0005811]; monolayer-surrounded lipid storage body [GO:0012511] | calcium ion binding [GO:0005509]; heme binding [GO:0020037]; monooxygenase activity [GO:0004497]; plant seed peroxygenase activity [GO:1990137]; protein homodimerization activity [GO:0042803] | PF05042; | null | Caleosin family | null | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:24954070}. Microsome membrane {ECO:0000250|UniProtKB:Q9SQ57}. | CATALYTIC ACTIVITY: Reaction=RH + ROOH = ROH + ROH.; EC=1.11.2.3; Evidence={ECO:0000250|UniProtKB:O81270}; | null | null | null | null | FUNCTION: Calcium-binding peroxygenase involved in the degradation of storage lipid in oil bodies. {ECO:0000250|UniProtKB:O81270}. | Pinus massoniana (Chinese red pine) | [
2037,
6578,
6714,
7856,
8159,
8657,
8915,
12192,
19935,
19951,
22653,
24924,
24932
] | [
"go_bp: negative regulation of lipid storage (GO:0010888)",
"go_cc: lipid droplet (GO:0005811)",
"go_cc: monolayer-surrounded lipid storage body (GO:0012511)",
"go_mf: monooxygenase activity (GO:0004497)",
"go_mf: calcium ion binding (GO:0005509)",
"go_mf: heme binding (GO:0020037)",
"go_mf: protein hom... | [
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000269",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"InterPro=match",
"UniProtKB=ECO:0000250",
"UniProtKB=none",
"InterPro=match:Pfam",
"UniProtKB=ECO... | Function: Calcium-binding peroxygenase involved in the degradation of storage lipid in oil bodies.
Catalytic Activity: RH + ROOH = ROH + ROH.
Cofactor: heme b; Ca(2+)
Subcellular Location: Lipid droplet; Microsome membrane
Domain: Transmembrane regions are predicted by sequence analysis tools, but these regions probabl... |
A0A060S684 | CHLE_MYCMD | MRLPNLTLLVWAATSVGLVSALPQVSYKADATASAPTVKLHQGTVRGLADDNYGLEQFFGIPYAKPPVGSLRFAKPQPLGPASSHKTVIDATRFGDICMQTVAPSPLYNMSEDCLNLNVVRPKGTTAKDKLPVLVWIYGGAFRQGSTPIYNASELVQKSVEIGKPIVFVAISYRVGPFGFIGGSEIADSDSATSNAGLYDQRLGLKWIRHNIGKFGGDKNRVTLFGQSAGAMSIALQNFAYDGNNHGLWHAAIMNSGGIAPGPLLTPKHPTVEQSFKRLANGVGCTGGSLLRCLRKANASEVQTVASNLTAQAGGTFPIP... | 3.1.1.42 | null | null | extracellular region [GO:0005576] | chlorogenate hydrolase activity [GO:0047745] | PF00135; | 3.40.50.1820; | Type-B carboxylesterase/lipase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}. | CATALYTIC ACTIVITY: Reaction=chlorogenate + H2O = L-quinate + (E)-caffeate + H(+); Xref=Rhea:RHEA:20689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29751, ChEBI:CHEBI:57644, ChEBI:CHEBI:57770; EC=3.1.1.42; Evidence={ECO:0000269|Ref.1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20690; Evidence={ECO:000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=19.6 uM for chlorogenic acid {ECO:0000269|Ref.1}; KM=64.1 uM for methyl p-coumarate {ECO:0000269|Ref.1}; KM=72.5 uM for methyl caffeate {ECO:0000269|Ref.1}; KM=101.8 uM for methyl ferulate {ECO:0000269|Ref.1}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000303|Ref.1}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000303|Ref.1}; | FUNCTION: Extracellular chlorogenic acid esterase that displays a surprisingly broad substrate profile (Ref.1). The enzyme's unique properties may contribute to the specific environmental interaction between the pathogenic fungus and its host, Zea mays (Ref.1). Additionally, the release of caffeic, p-coumaric, and feru... | Mycosarcoma maydis (Corn smut fungus) (Ustilago maydis) | [
6485,
10475,
14367,
15442,
18549,
20638,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"interpro: Carboxylesterase, type B (IPR002018)",
"interpro: Carboxylesterase type B, active site (IPR019826)",
"interpro: Alpha/Beta hydrolase fold (IPR029058)",
"interpro: Type-B Carboxylesterase/Lipase (IPR050309)",
"pfam: COesterase (PF00135)",
"subcellula... | [
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000269"
] | Function: Extracellular chlorogenic acid esterase that displays a surprisingly broad substrate profile. The enzyme's unique properties may contribute to the specific environmental interaction between the pathogenic fungus and its host, Zea mays. Additionally, the release of caffeic, p-coumaric, and ferulic acids from a... |
A0A060SMC0 | LP14A_PYCCI | MLASLPASLALVVALATSASAHAAFWDKSMYGFNVTAQTFSYDNRPQVPLYDMTFDQWWFHGHKDYPPNEGDFFELPAGGEVNAIISCDKGATPFYASSPGGDSGYGSDSPCPGQPTSEYHTTGIDDVKGCCMAIAYKADVNDVQPDDFVVFSCNATCVWTMNTKFEIPKLPACPEGGCHCAWFWIHSYDSGAEQIYMNGFKCQVTGDVGTQPLGKPAVPRRCGADPDHGRPDPVPGNCTIGAKTPMYWYQKEGNNMFEDTYDAPYYNQLYGFADGAQNDIFMDGVIASLASSGASSTLTSSADSLSAVASSTSYPAHPT... | 1.14.99.- | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:A0A2I6QAZ5}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:A0A2I6QAZ5}; | null | extracellular region [GO:0005576] | null | PF22810; | null | Polysaccharide monooxygenase AA14 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A0A2I6QAZ5}. | null | null | null | null | null | FUNCTION: Lytic polysaccharide monooxygenase (LPMO) showing oxidase and peroxidase activities that are common for LPMOs (By similarity). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (By similarity). Shows no activity o... | Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina) | [
6485,
19931,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"cofactor: Cu(2+) (CHEBI:29036)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000250",
"UniProtKB=ECO:0000250",
"UniProtKB=ECO:0000250"
] | Function: Lytic polysaccharide monooxygenase (LPMO) showing oxidase and peroxidase activities that are common for LPMOs (By similarity). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (By similarity). Shows no activity o... |
A0A060SRI5 | LP14B_PYCCI | MIPVFLAAIAVFLPLTSGHIAFWHNSMYGFNVTEQTFPYDNRPVVPLQNMTFKEWWFHNHLDYPPHPGDFFELPAGKPAMAELACNKGATTWFNSSEGGNIQNGDDPCPGSPPSEYHTTGFDDLKGCALAIAYEPDVTKIKPEDFTIFSVNQTCVWYRFTDFQVPERMPSCPPGGCHCAWFWIHSPDSGGEQIYMNGFKCKITGSTSNVPLAKPKVARRCGADPDHGKPDAVPGNCTYGAKQPLYWLQQEGNNEFDDYIAPPFYNDLYNFKDGAQNDIFIDSYPHGIPDPSPEQTIIPTPLDAAVISNATPAPSNGSCSS... | 1.14.99.- | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:A0A2I6QB00}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:A0A2I6QB00}; | null | extracellular region [GO:0005576] | null | PF22810; | 2.70.50.70; | Polysaccharide monooxygenase AA14 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A0A2I6QB00}. | null | null | null | null | null | FUNCTION: Lytic polysaccharide monooxygenase (LPMO) that oxidatively cleaves xylan with both C1 and C4 regioselectivity and that specifically targets the protective shield made by heteroxylans that cover cellulose microfibrils in wood (By similarity). Catalysis by LPMOs requires the reduction of the active-site copper ... | Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina) | [
6485,
19931,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"cofactor: Cu(2+) (CHEBI:29036)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000250",
"UniProtKB=ECO:0000250",
"UniProtKB=ECO:0000250"
] | Function: Lytic polysaccharide monooxygenase (LPMO) that oxidatively cleaves xylan with both C1 and C4 regioselectivity and that specifically targets the protective shield made by heteroxylans that cover cellulose microfibrils in wood (By similarity). Catalysis by LPMOs requires the reduction of the active-site copper ... |
A0A060WQA3 | OTOL1_ONCMY | MPSLRLLAILTTLLAVVLMATQSSATRTTRRPKPQNTKKPPRGGGTGGGGGGGDQPARLGFRQTTTTMSPSSSLGTDETTEDTMTDAYSLSPTDSTTYAGDAYPTEFHTDSMALPGAGMGNYTLDYSHCYLNVCECCPPEKGPVGPPGERGPPGPGAERAPAVPSETLALMLGTDIYTHTFKIPILLSFYLIGDKGDQGDTGMPGAPGILGKEGQKGDLGPKGEKGETGLPGLKGDLGERGKPGWNGTQGEKGDLGKIGPAGPSGLTGPMGQNGQKGEMGECPTGEKGEKGEAGLPGPPGPRGSVGPPGVNGSNGLPGPV... | null | null | otolith mineralization [GO:0045299] | null | calcium ion binding [GO:0005509] | PF00386;PF01391; | 2.60.120.40; | OTOL1 family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q4ZJM7}. Note=Localized in both the surrounding otoconial matrix and otoconia. {ECO:0000250|UniProtKB:Q4ZJM7}. | null | null | null | null | null | FUNCTION: Collagen-like protein, which provides an organic scaffold for otoliths onto the sensory epithelium of the inner ear. Acts as a scaffold for biomineralization by sequestering calcium. {ECO:0000250|UniProtKB:A5PN28}. | Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri) | [
8159,
9973,
12270,
12447,
18604,
20849,
21495,
24899,
24900,
24983
] | [
"go_mf: calcium ion binding (GO:0005509)",
"interpro: C1q domain (IPR001073)",
"interpro: Collagen triple helix repeat (IPR008160)",
"interpro: Tumour necrosis factor-like domain superfamily (IPR008983)",
"interpro: Collagen/C1q domain-containing (IPR050392)",
"pfam: C1q (PF00386)",
"pfam: Collagen (PF0... | [
"UniProtKB-GO=ECO:0000250",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000250",
"UniProtKB=ECO:0000250",
"UniProtKB=ECO:0000250"
] | Function: Collagen-like protein, which provides an organic scaffold for otoliths onto the sensory epithelium of the inner ear. Acts as a scaffold for biomineralization by sequestering calcium.
Subcellular Location: Secreted, Extracellular space, Extracellular matrix
Domain: The C1q domain mediates calcium-binding.
Sequ... |
A0A060X6Z0 | TY3H_ONCMY | MPISSSSSSSTKSMRRAASELERSDSVTSPRFIGRRQSLIEDARKEREAAAAAAEAAEATEQIVFEEEDGKALLNLFFTLRSSKTPALSRSLKVFETFEAKIHHLETRPCRKPRDSLEGLEYFVRCEVHLSDVSTLISSIKRIAEDVKTTKEVKFHWFPKKISELDRCHHLITKFDPDLDQEHPGFTDPVYRQRRKMIGDIAFRYKQGEPIPRVEYTEEEIGTWREVYSTLRDLYTTHACSEHLEAFNLLERHCGYSPENIPQLEDVSRFLRERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDC... | 1.14.16.2 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:P24529}; | dopamine biosynthetic process from tyrosine [GO:0006585] | axon [GO:0030424]; cell body fiber [GO:0070852]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471] | iron ion binding [GO:0005506]; tyrosine 3-monooxygenase activity [GO:0004511] | PF00351;PF21417;PF12549; | 3.30.70.260;1.10.800.10; | Biopterin-dependent aromatic amino acid hydroxylase family | null | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P24529}. Cell projection, axon {ECO:0000250|UniProtKB:P24529}. Note=Expressed in dopaminergic axons and axon terminals. {ECO:0000250|UniProtKB:P24529}. | CATALYTIC ACTIVITY: Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-dopa; Xref=Rhea:RHEA:18201, ChEBI:CHEBI:15379, ChEBI:CHEBI:15642, ChEBI:CHEBI:57504, ChEBI:CHEBI:58315, ChEBI:CHEBI:59560; EC=1.14.16.2; Evidence={ECO:0000269|PubMed:... | null | PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 1/2. {ECO:0000250|UniProtKB:P24529}. | null | null | FUNCTION: Plays an important role in the physiology of adrenergic neurons. {ECO:0000250|UniProtKB:P24529}. | Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri) | [
6823,
7121,
7211,
7267,
8157,
10085,
14129,
14334,
14335,
16369,
16664,
17448,
18028,
19928,
20821,
24883,
24957,
25007,
25008
] | [
"go_cc: axon (GO:0030424)",
"go_cc: perikaryon (GO:0043204)",
"go_cc: perinuclear region of cytoplasm (GO:0048471)",
"go_cc: cell body fiber (GO:0070852)",
"go_mf: iron ion binding (GO:0005506)",
"interpro: Aromatic amino acid hydroxylase (IPR001273)",
"interpro: Aromatic amino acid hydroxylase, iron/co... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniPr... | Function: Plays an important role in the physiology of adrenergic neurons.
Catalytic Activity: (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-dopa
Cofactor: Fe(2+)
Pathway: Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-ty... |
A0A060XQP6 | OMM64_ONCMY | MLSRLLIVPLIFALAGLAISAPVNDGTEADNDERAASLLVHLKGDKDGGGLTGSPDGVSAGTTDGTDSSKELAGGAVDSSPDTTDTPDASSSDIFPDTNNRDTSVETTGNPDDSDAPDAAESAGSQDTTDAADASEAVAETVDTYDIPDTDGADDREKVSTEVSTEDLDSAGVDKSPESDSTESPGSDSAESPGSDSAESPGSDSTESPGSDSTESPRSDSTDEVLTDVQADSADVTSDDMDEATETDKDDDKSDDKSDADAATDKDDSDEDKDTELDGKAHAEDTQTEEAADSDSKQGAADSDSDTDDDRPEKDVKNDS... | null | null | null | null | null | null | null | null | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18410381}. Note=Accumulates in the ring-like structures of otoliths. {ECO:0000269|PubMed:18410381}. | null | null | null | null | null | FUNCTION: Calcium-binding component of otoliths, a calcium carbonate structure of the inner ear involved in hearing and balance sensing (PubMed:18410381). Binds calcium (PubMed:18410381, PubMed:28866388). {ECO:0000269|PubMed:18410381, ECO:0000269|PubMed:28866388}. | Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri) | [
24899,
24900,
24983
] | [
"subcellular_location: Extracellular matrix (SL-0111)",
"subcellular_location: Extracellular space (SL-0112)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB=ECO:0000269",
"UniProtKB=ECO:0000269",
"UniProtKB=ECO:0000269"
] | Function: Calcium-binding component of otoliths, a calcium carbonate structure of the inner ear involved in hearing and balance sensing. Binds calcium.
Subcellular Location: Secreted, Extracellular space, Extracellular matrix
Domain: The Asp/Glu-rich (acidic) region mediates binding to calcium.
Sequence Mass (Da): 6656... |
A0A061ACU2 | PIEZ1_CAEEL | MTVPPLLKSCVVKLLLPAALLAAAIIRPSFLSIGYVLLALVSAVLPPIRKSLALPKLVGTFVIITFLFCLAVALGVGSYQISEQVVHKNDRTYICNRSDTTLFRSIGLVRFHPTGTFESTRAFLPEIIATSAALLTIIIVMFLSHRDEQLDVVGDVVTVRSESGREQRRQRKLAAIMWSAIGNSLRRLTNFVLFLFTAYVGIVKPSLSNSIYFLAFLFISTWWSTYTPLRHGVYNQIKKFLIFYSALHFLVLYTYQIPIVHHSWLPTGSFLPRLFGLTVLMDSSCPEWWKFPFVAPDFNDDDLIMKWPLYANPIVVLVFF... | null | null | cellular response to mechanical stimulus [GO:0071260]; detection of mechanical stimulus [GO:0050982]; flagellated sperm motility [GO:0030317]; monoatomic cation transmembrane transport [GO:0098655]; positive regulation of brood size [GO:0090727]; positive regulation of ovulation [GO:0060279]; regulation of membrane pot... | plasma membrane [GO:0005886] | mechanosensitive monoatomic cation channel activity [GO:0140135] | PF12166;PF24874;PF24871;PF15917;PF23188; | null | PIEZO (TC 1.A.75) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32490809}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Pore-forming subunit of a mechanosensitive non-specific cation channel (By similarity). Generates currents characterized by a linear current-voltage relationship (By similarity). Plays a role in reproduction by positively regulating inter-tissue signaling to promote oocyte maturation, ovulation and fertilizat... | Caenorhabditis elegans | [
1657,
2566,
3507,
4540,
4835,
5210,
5551,
5633,
6620,
24856,
25110
] | [
"go_bp: response to mechanical stimulus (GO:0009612)",
"go_bp: flagellated sperm motility (GO:0030317)",
"go_bp: regulation of membrane potential (GO:0042391)",
"go_bp: detection of mechanical stimulus (GO:0050982)",
"go_bp: positive regulation of ovulation (GO:0060279)",
"go_bp: cellular response to mech... | [
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000315",
"UniProtKB-GO=ECO:0000318",
"UniProtKB-GO=ECO:0000318",
"UniProtKB-GO=ECO:0000315",
"UniProtKB-GO=ECO:0000318",
"UniProtKB-GO=ECO:0000315",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000314",
"UniProtKB=ECO:0000269",
"UniProtKB=ECO:0000... | Function: Pore-forming subunit of a mechanosensitive non-specific cation channel (By similarity). Generates currents characterized by a linear current-voltage relationship (By similarity). Plays a role in reproduction by positively regulating inter-tissue signaling to promote oocyte maturation, ovulation and fertilizat... |
A0A061AE05 | PAPSH_CAEEL | MLTPRDENNEGDAMPMLKKPRYSSLSGQSTNITYQEHTISREERAAAVGRHEGFRGCTIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSKEDRQENIRRVAEVAKLFADSGMICLAAFISPFQEDRLDARKIHESENVKFIEVHVSTTLEVCEQRDPKPSELYKKARAGQILGFTGIDSAYEPPENAEIILDAGKDGVQQCVQKVLDHLESKGLLPEQIPDVPAVRELFVSDDLTVAELLKESQNLPTVELTKVDLQWLQVLAEGWATPLSGFMRERQYLQSMHFGQLLDLKHKVAFVGEKSD... | 2.7.1.25; 2.7.7.4 | null | 3'-phosphoadenosine 5'-phosphosulfate biosynthetic process [GO:0050428]; sulfate assimilation [GO:0000103] | nucleus [GO:0005634] | adenylylsulfate kinase activity [GO:0004020]; ATP binding [GO:0005524]; sulfate adenylyltransferase (ATP) activity [GO:0004781] | PF01583;PF01747;PF14306; | 3.40.50.620;3.40.50.300;3.10.400.10; | APS kinase family; Sulfate adenylyltransferase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16497669}. | CATALYTIC ACTIVITY: Reaction=sulfate + ATP + H(+) = adenosine 5'-phosphosulfate + diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000269|PubMed:16497669}; CATALYTIC ACTIVITY: Reaction=adenosine 5'-phosphosulfate... | null | PATHWAY: Sulfur metabolism; sulfate assimilation. {ECO:0000303|PubMed:16497669}. | null | null | FUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway (PubMed:16497669). The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group fro... | Caenorhabditis elegans | [
158,
412,
6494,
7697,
7982,
8167,
10737,
10803,
13401,
13620,
15042,
15131,
15266,
19730,
20107,
21607,
21671,
23771,
24954
] | [
"ec: EC 2.7.7.4",
"go_bp: sulfate assimilation (GO:0000103)",
"go_cc: nucleus (GO:0005634)",
"go_mf: adenylylsulfate kinase activity (GO:0004020)",
"go_mf: sulfate adenylyltransferase (ATP) activity (GO:0004781)",
"go_mf: ATP binding (GO:0005524)",
"interpro: Sulphate adenylyltransferase (IPR002650)",
... | [
"UniProtKB=ECO:0000269",
"UniProtKB-GO=ECO:0000318",
"UniProtKB-GO=ECO:0000269",
"UniProtKB-GO=ECO:0000269",
"UniProtKB-GO=ECO:0000269",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
... | Function: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yield... |
A0A061AYY2 | EAT2_CYBFA | MRSTSLLMQAKAAIPDIKQLPTKHKVSLAYTIHWPHKTVNPNINIKPREPVIFLHGVFGSKKNYRDYCQTIANQNYTPVYSLDFRNHGESEHAFPLVNYSTLTQDVVDFIHEHKLEKVDIVGYSLGAKVALLTLLKHPELCRSGVIIGNAPIKTPQVKVYLKAFIKALKALGDKRPEIKSNDKAWRAKARDVMRKYIPDGDILHYLLRNIDIRKPKNITEYKPGTINFSMPISHFDNKVVEDIADWPEEEVEGLKFEGPVRVIRGTQSVFINDKGLAAYQKHFPNYTLTNFNSNHLIWAERPLQVTKVVSDFLKKTRLLE... | 2.3.1.- | null | null | mitochondrion [GO:0005739] | carboxylic ester hydrolase activity [GO:0052689] | PF00561; | 3.40.50.1820; | AB hydrolase superfamily | null | null | null | null | null | null | null | FUNCTION: Probable alcohol acetyltransferase that uses acetyl-CoA to synthesize acetate esters from various alcohols (Probable). Not involved in the synthesis of ethyl acetate (PubMed:28356220). {ECO:0000269|PubMed:28356220, ECO:0000305|PubMed:28356220}. | Cyberlindnera fabianii (Yeast) (Hansenula fabianii) | [
6539,
9163,
9476,
15442,
20975
] | [
"go_cc: mitochondrion (GO:0005739)",
"go_mf: carboxylic ester hydrolase activity (GO:0052689)",
"interpro: Alpha/beta hydrolase fold-1 (IPR000073)",
"interpro: Alpha/Beta hydrolase fold (IPR029058)",
"pfam: Abhydrolase_1 (PF00561)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam"
] | Function: Probable alcohol acetyltransferase that uses acetyl-CoA to synthesize acetate esters from various alcohols (Probable). Not involved in the synthesis of ethyl acetate.
EC: 2.3.1.-
Sequence Mass (Da): 42144
Sequence Length: 371 |
A0A061B0Q2 | EAT1_CYBFA | MFKPTRVLKSSQPILNSLPHAETVKMAYDLHLPKKTLHQNMNITSDEPIVFVHGIFGSKKSYATDSKLIANGTHSPVYTIDLRNHGETGHAQPFNYDTLVQDIKEFCSTHNLSNIKLVGYSLGAKVSMLAALRLPELVKSAVIIDNAPIKQPYIESYMKQYIKSMLHVDDAKISTTDKDWKRKASEAMKRYMPNATVRKNLLVNLVNKKPEGFESPAIDFENGNIQFLNPIKHMEEMAVKDVSDWPVESTEGLKFDGPVKFIRGLKSPFISPEGFKKINEHFPKNEFYDVNSAHDILDQRPSEYVKVICDFFNLQRYNSA... | 2.3.1.268; 3.1.1.-; 3.1.2.1 | null | null | mitochondrion [GO:0005739] | acetyl-CoA hydrolase activity [GO:0003986]; acetylesterase activity [GO:0008126]; alcohol O-acetyltransferase activity [GO:0004026] | PF00561; | 3.40.50.1820; | AB hydrolase superfamily | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:A0A1E3P8S6}. | CATALYTIC ACTIVITY: Reaction=ethanol + acetyl-CoA = ethyl acetate + CoA; Xref=Rhea:RHEA:55972, ChEBI:CHEBI:16236, ChEBI:CHEBI:27750, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.268; Evidence={ECO:0000269|PubMed:28356220}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O = acetate + CoA + H(+); Xref=Rhea:RHEA:20289, ChE... | null | null | null | null | FUNCTION: Alcohol acetyltransferase that catalyzes the synthesis of ethyl acetate from ethanol and acetyl-CoA (PubMed:28356220). Can also function as a thioesterase by hydrolyzing acetyl-CoA in the absence of ethanol, as well as esterase hydrolyzing ethyl acetate (By similarity). {ECO:0000250|UniProtKB:A0A1E3P8S6, ECO:... | Cyberlindnera fabianii (Yeast) (Hansenula fabianii) | [
97,
6539,
7683,
8206,
9476,
15442,
20435,
20975,
24939
] | [
"ec: EC 2.3.1.268",
"go_cc: mitochondrion (GO:0005739)",
"go_mf: acetyl-CoA hydrolase activity (GO:0003986)",
"go_mf: acetylesterase activity (GO:0008126)",
"interpro: Alpha/beta hydrolase fold-1 (IPR000073)",
"interpro: Alpha/Beta hydrolase fold (IPR029058)",
"rhea: ethanol + acetyl-CoA = ethyl acetate... | [
"UniProtKB=ECO:0000269,none",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000269",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000250"
] | Function: Alcohol acetyltransferase that catalyzes the synthesis of ethyl acetate from ethanol and acetyl-CoA. Can also function as a thioesterase by hydrolyzing acetyl-CoA in the absence of ethanol, as well as esterase hydrolyzing ethyl acetate (By similarity).
Catalytic Activity: ethanol + acetyl-CoA = ethyl acetate ... |
A0A061DFA8 | MTR1_THECC | MEQILSMNGGSGEQSYANNSIGQSTCLSRSMPVLKQAVLDSCCTNLPETVTMADLGCSSGPNTFYAVSEITSIIYKRCCQLGRSAPEFRVFLNDLPGNDFNTVFQSLPAYQGKLREENGPGFGPLYVAGVPGSFYGRLFPLKTLHFVHSSSSLHWLSQVPPELTDKANPLINKWKIFISKTSPPAVISSYLTQFRKDFSLFLKLRSEEVAPEGRMVLTFRGRTTADPTSDESCLLWDYLGQAFQDLVAEGLVEEERLDTYNTPYYEPHPEEIQAEIEKEGSFTLDRLEVIALPWDSVNGGIKDDRATTAKRMAKAIRAVN... | 2.1.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9FLN8}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9FLN8}; | null | null | methyltransferase activity [GO:0008168] | PF03492; | 1.10.1200.270;3.40.50.150; | Methyltransferase superfamily, Type-7 methyltransferase family | null | null | null | null | null | null | null | null | Theobroma cacao (Cacao) (Cocoa) | [
8215,
11485,
15446,
17478,
19924,
22282
] | [
"go_mf: methyltransferase activity (GO:0008168)",
"interpro: SAM dependent carboxyl methyltransferase (IPR005299)",
"interpro: S-adenosyl-L-methionine-dependent methyltransferase superfamily (IPR029063)",
"interpro: Methyltransferase, alpha-helical capping domain (IPR042086)",
"cofactor: Mg(2+) (CHEBI:18420... | [
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000250",
"InterPro=match:Pfam"
] | Cofactor: Mg(2+)
EC: 2.1.1.-
Sequence Mass (Da): 40659
Sequence Length: 364 |
A0A061DFM8 | MTR2_THECC | MVKASVPCMNSGDKETSYGTCSLPQEIVLPKARPILEDTIKDMFSNVSSTDCIKVADLGCSSGPNTFMAISIVVDTFHEMCQQAQLKTSPEFQVFLNDLPENDFNNIFRSVASFTDRIKKGKGDKFGLCFVTGVPGSFYGRLFPNRSLHLVHSSYSVNWLSKACISFHVPDGIGNNKGSVYMAESSPPNVFKAHSRQFKEDFSTFLKLRSQEMIPGGRMVLTFNGRSNLYPSKQDDDWKLQLAKSLYDLVVEGIVKEADADSFNIPMYAPYKGELCEIIQKEDSFDLDKLEVVQINWGPRDVLTNEDFEFDKYQRGQKTA... | 2.1.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9FLN8}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9FLN8}; | null | null | methyltransferase activity [GO:0008168] | PF03492; | 1.10.1200.270;3.40.50.150; | Methyltransferase superfamily, Type-7 methyltransferase family | null | null | null | null | null | null | null | null | Theobroma cacao (Cacao) (Cocoa) | [
8215,
11485,
15446,
17478,
19924,
22282
] | [
"go_mf: methyltransferase activity (GO:0008168)",
"interpro: SAM dependent carboxyl methyltransferase (IPR005299)",
"interpro: S-adenosyl-L-methionine-dependent methyltransferase superfamily (IPR029063)",
"interpro: Methyltransferase, alpha-helical capping domain (IPR042086)",
"cofactor: Mg(2+) (CHEBI:18420... | [
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000250",
"InterPro=match:Pfam"
] | Cofactor: Mg(2+)
EC: 2.1.1.-
Sequence Mass (Da): 41421
Sequence Length: 369 |
A0A061DM17 | MTR3_THECC | MDVEKVFHMTGGVGKTSYAQNSSLQKKASDMVKHITMETIEELYYSIAPKSLGIADLGCSSGPNSLSLIKDIVEVVEETSHKLFHPLPEFRVYLNDLPTNDFNSVFKSLPDFYRDLKKDRNEGGPAIFIAGYPGSFYGRLFPNNCLHFIYSSYSLHWLSKVPPALYDEHGKSTNKGNVYISESSPPSVSQAYWNQFQEDFSLFLKSRSVEVVTGGRMVLILLGRIGQDHVDRGNSFFWEILSRSLAISVSQGQIDREKLDSYEVHFYAPSTNEIEDEVGREGSFEVDRLEMFEIDREAKDGESYGTAVAMTVRAIQESMI... | 2.1.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9FLN8}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9FLN8}; | null | null | methyltransferase activity [GO:0008168] | PF03492; | 1.10.1200.270;3.40.50.150; | Methyltransferase superfamily, Type-7 methyltransferase family | null | null | null | null | null | null | null | null | Theobroma cacao (Cacao) (Cocoa) | [
8215,
11485,
15446,
17478,
19924,
22282
] | [
"go_mf: methyltransferase activity (GO:0008168)",
"interpro: SAM dependent carboxyl methyltransferase (IPR005299)",
"interpro: S-adenosyl-L-methionine-dependent methyltransferase superfamily (IPR029063)",
"interpro: Methyltransferase, alpha-helical capping domain (IPR042086)",
"cofactor: Mg(2+) (CHEBI:18420... | [
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000250",
"InterPro=match:Pfam"
] | Cofactor: Mg(2+)
EC: 2.1.1.-
Sequence Mass (Da): 39384
Sequence Length: 349 |
A0A061FBW2 | JMT2_THECC | MEVMQVLHMNKGNGETSYAKNSTVQSKIISVGKPIIEEAVHEISCNNLLESMGIADLGCSSGPNTLSVISEIMDMVQTTSRRLGRPVPEFRVYLNDLYSNDFNYIFMSLPAFYHRLKEEKGIGCGSCYISGVAGSFYGRLFPSKSLHFVHSSSSLHWLSQVPPGLESKALAPLNKGKVYISKSSPQSVLNAYSLQFQNDFSMFIESRSQELVPGGRMVLSFMGRRSTDPTTEESCHHWELLAQAIMSLVREGLIEEAKVDSFNAPYYAPCAEEIKVEIQKVGSFVIDRLEGFEIDWDGGAVSDVQTAQGKLLIGQRVAKT... | 2.1.1.141 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9FLN8}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9FLN8}; | oxylipin biosynthetic process [GO:0031408] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | methyl jasmonate methylesterase activity [GO:0030795] | PF03492; | 1.10.1200.270;3.40.50.150; | Methyltransferase superfamily, Type-7 methyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9SBK6}. Nucleus {ECO:0000250|UniProtKB:Q9SBK6}. Note=Predominantly cytoplasmic (By similarity). Partially nuclear (By similarity). {ECO:0000250|UniProtKB:Q9SBK6}. | CATALYTIC ACTIVITY: Reaction=jasmonate + S-adenosyl-L-methionine = methyl (-)-jasmonate + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:13349, ChEBI:CHEBI:15929, ChEBI:CHEBI:57856, ChEBI:CHEBI:58431, ChEBI:CHEBI:59789; EC=2.1.1.141; Evidence={ECO:0000250|UniProtKB:Q9AR07}; | null | PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000250|UniProtKB:Q9AR07}. | null | null | FUNCTION: Catalyzes the methylation of jasmonate into methyljasmonate, a plant volatile that acts as an important cellular regulator mediating diverse developmental processes and defense responses. {ECO:0000250|UniProtKB:Q9AR07}. | Theobroma cacao (Cacao) (Cocoa) | [
2743,
6494,
6538,
11485,
15446,
17478,
19924,
22282,
24883,
24954
] | [
"go_bp: oxylipin biosynthetic process (GO:0031408)",
"go_cc: nucleus (GO:0005634)",
"go_cc: cytoplasm (GO:0005737)",
"interpro: SAM dependent carboxyl methyltransferase (IPR005299)",
"interpro: S-adenosyl-L-methionine-dependent methyltransferase superfamily (IPR029063)",
"interpro: Methyltransferase, alph... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000250",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000250",
"UniProtKB=ECO:0000250"
] | Function: Catalyzes the methylation of jasmonate into methyljasmonate, a plant volatile that acts as an important cellular regulator mediating diverse developmental processes and defense responses.
Catalytic Activity: jasmonate + S-adenosyl-L-methionine = methyl (-)-jasmonate + S-adenosyl-L-homocysteine
Cofactor: Mg(2+... |
A0A061FDP1 | JMT1_THECC | MEVMQVLHMNRGNGENSYAKNSTVQSKIISIGKPIIEEAVHEISCNNVLESMGIADLGCSSGPNTLCVISEIMDMVQATSHRLGHPVPEFRLYLNDLYSNDFNSIFMSLPAFYHRLKEEKGIGCGSCFISGVAGSFYGRLFPSKSLHYVHSSSSLHWLSQVPPGLESNAVTPLNKGKVYISKSSPHSVLHAYSLQFQNDFPMFIESRSQELVSGGRMVLSLFGRRSTDPTTEESCYQWELLAQAIMSLVREGLIEEEKVDSFNTPFYAPCAEEIKVEIQKEGSFIIDRLEGFEIDWDGGAVSDVHTAQGKLLIGQRAAKA... | 2.1.1.141 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9FLN8}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9FLN8}; | oxylipin biosynthetic process [GO:0031408] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | methyl jasmonate methylesterase activity [GO:0030795] | PF03492; | 1.10.1200.270;3.40.50.150; | Methyltransferase superfamily, Type-7 methyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9SBK6}. Nucleus {ECO:0000250|UniProtKB:Q9SBK6}. Note=Predominantly cytoplasmic (By similarity). Partially nuclear (By similarity). {ECO:0000250|UniProtKB:Q9SBK6}. | CATALYTIC ACTIVITY: Reaction=jasmonate + S-adenosyl-L-methionine = methyl (-)-jasmonate + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:13349, ChEBI:CHEBI:15929, ChEBI:CHEBI:57856, ChEBI:CHEBI:58431, ChEBI:CHEBI:59789; EC=2.1.1.141; Evidence={ECO:0000250|UniProtKB:Q9AR07}; | null | PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000250|UniProtKB:Q9AR07}. | null | null | FUNCTION: Catalyzes the methylation of jasmonate into methyljasmonate, a plant volatile that acts as an important cellular regulator mediating diverse developmental processes and defense responses. {ECO:0000250|UniProtKB:Q9AR07}. | Theobroma cacao (Cacao) (Cocoa) | [
2743,
6494,
6538,
11485,
15446,
17478,
19924,
22282,
24883,
24954
] | [
"go_bp: oxylipin biosynthetic process (GO:0031408)",
"go_cc: nucleus (GO:0005634)",
"go_cc: cytoplasm (GO:0005737)",
"interpro: SAM dependent carboxyl methyltransferase (IPR005299)",
"interpro: S-adenosyl-L-methionine-dependent methyltransferase superfamily (IPR029063)",
"interpro: Methyltransferase, alph... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000250",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000250",
"UniProtKB=ECO:0000250"
] | Function: Catalyzes the methylation of jasmonate into methyljasmonate, a plant volatile that acts as an important cellular regulator mediating diverse developmental processes and defense responses.
Catalytic Activity: jasmonate + S-adenosyl-L-methionine = methyl (-)-jasmonate + S-adenosyl-L-homocysteine
Cofactor: Mg(2+... |
A0A061FKL9 | BTS2_THECC | MAMKVKDIVFMNKGDGENSYVKSAGLTLKVIAKTQPIVQKAVQSLFTGTHSTPLQVVNVADLGCALGPQPLESMSIVIESIVEKCGELGCEMPEIQFHLNDLAGNDFNTLFKGLSVVQEKYKNVSWFAMGAPGSFHGRLFPRNSMHLVHSCYSVHWLSKAPKITSEAGLPLNKGKIYMSKTSPPAVREGYLSQFEEDFSSVLRFRSPELAPDGRMVLILNGRQSADPTEKDICYLWDLLAEALSYLVSEGLIDEEKLDSFNVPYYNPSQEEVERVIDKEGSFTTEFSDTVVLEIGGKNAWSDPGLRIKGYRCFSEPILSH... | 2.1.1.159 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9FLN8}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9FLN8}; | null | null | caffeine synthase activity [GO:0102741] | PF03492; | 1.10.1200.270;3.40.50.150; | Methyltransferase superfamily, Type-7 methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=7-methylxanthine + S-adenosyl-L-methionine = theobromine + S-adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:24604, ChEBI:CHEBI:15378, ChEBI:CHEBI:28946, ChEBI:CHEBI:48991, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.159; Evidence={ECO:0000250|UniProtKB:A0A061FMF5}; PhysiologicalDirection... | null | PATHWAY: Alkaloid biosynthesis. {ECO:0000250|UniProtKB:A0A061FMF5}. | null | null | FUNCTION: Involved in the biosynthesis of theobromine. {ECO:0000250|UniProtKB:A0A061FMF5}. | Theobroma cacao (Cacao) (Cocoa) | [
9304,
11485,
15446,
17478,
19924,
20230,
22282
] | [
"go_mf: caffeine synthase activity (GO:0102741)",
"interpro: SAM dependent carboxyl methyltransferase (IPR005299)",
"interpro: S-adenosyl-L-methionine-dependent methyltransferase superfamily (IPR029063)",
"interpro: Methyltransferase, alpha-helical capping domain (IPR042086)",
"cofactor: Mg(2+) (CHEBI:18420... | [
"UniProtKB-GO=ECO:0000250",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000250",
"UniProtKB=ECO:0000250",
"InterPro=match:Pfam"
] | Function: Involved in the biosynthesis of theobromine.
Catalytic Activity: 7-methylxanthine + S-adenosyl-L-methionine = theobromine + S-adenosyl-L-homocysteine + H(+)
Cofactor: Mg(2+)
Pathway: Alkaloid biosynthesis.
EC: 2.1.1.159
Sequence Mass (Da): 40910
Sequence Length: 367 |
A0A061FKM4 | BTS5_THECC | MEAVKDVLCMNNGVGENSYVKAEALTIKVMAITKPIVPKAVQSLFTETDHSIPLQVVNVADLGCAVGPQPLEFMSTVIESILKKCGEMGREMPEIQFFLNDLVGNDFNTLFKGLSVVQEKYKKVSWFAMGAPGSFHGRLFPRNSMHLVYSCYSVHWLSEAPKITNEAGLPLNKGKIYMSKTSPPAVTKAYLSQFQEDFSSLLKFRSQELAPNGRVVLIFNGRQTADPTNKDTCYTWDLLAEALSYLVSQGLVDEGKLDSFNVPYYNPSQEEIKYLVDKEGSLTIEFIDTIELEIGGPNGYWSSPESRIRGHRCFTEPLLS... | 2.1.1.159 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9FLN8}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9FLN8}; | null | null | caffeine synthase activity [GO:0102741] | PF03492; | 1.10.1200.270;3.40.50.150; | Methyltransferase superfamily, Type-7 methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=7-methylxanthine + S-adenosyl-L-methionine = theobromine + S-adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:24604, ChEBI:CHEBI:15378, ChEBI:CHEBI:28946, ChEBI:CHEBI:48991, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.159; Evidence={ECO:0000250|UniProtKB:A0A061FMF5}; PhysiologicalDirection... | null | PATHWAY: Alkaloid biosynthesis. {ECO:0000250|UniProtKB:A0A061FMF5}. | null | null | FUNCTION: Involved in the biosynthesis of theobromine. {ECO:0000250|UniProtKB:A0A061FMF5}. | Theobroma cacao (Cacao) (Cocoa) | [
9304,
11485,
15446,
17478,
19924,
20230,
22282
] | [
"go_mf: caffeine synthase activity (GO:0102741)",
"interpro: SAM dependent carboxyl methyltransferase (IPR005299)",
"interpro: S-adenosyl-L-methionine-dependent methyltransferase superfamily (IPR029063)",
"interpro: Methyltransferase, alpha-helical capping domain (IPR042086)",
"cofactor: Mg(2+) (CHEBI:18420... | [
"UniProtKB-GO=ECO:0000250",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000250",
"UniProtKB=ECO:0000250",
"InterPro=match:Pfam"
] | Function: Involved in the biosynthesis of theobromine.
Catalytic Activity: 7-methylxanthine + S-adenosyl-L-methionine = theobromine + S-adenosyl-L-homocysteine + H(+)
Cofactor: Mg(2+)
Pathway: Alkaloid biosynthesis.
EC: 2.1.1.159
Sequence Mass (Da): 40757
Sequence Length: 364 |
A0A061FLA2 | BTS4_THECC | MEVKDIVFMNKGDGENSYVKSAGLTLKVIAKTQPMVQKAVQSLFKGTHSAPLQVVNVADLGCALAPQPLESMSIVIESIVEKCGELGCEMPEIQFHFNDLAGNDFNTLFKGLSVVQEKYKNVSWFAMGAPGSFHGRLFPRNSMHLVHSCYSVHWLSKAPKITSEEGLPLNKGKIYMSKTSXXXXXXXXXXXFEEDFSSVLRFRSPELAPDGRMVLILNGRQSADPTEKDICYLWDLLAEALSYLVSEGLIDEEKLDSFNVPYYNPSQEEVERVIDKEGSFTTEFSDTVVLEIGGKNAWSDPGLRIKGYRCFSEPVLSHQF... | 2.1.1.159 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9FLN8}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9FLN8}; | null | null | caffeine synthase activity [GO:0102741] | PF03492; | 1.10.1200.270;3.40.50.150; | Methyltransferase superfamily, Type-7 methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=7-methylxanthine + S-adenosyl-L-methionine = theobromine + S-adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:24604, ChEBI:CHEBI:15378, ChEBI:CHEBI:28946, ChEBI:CHEBI:48991, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.159; Evidence={ECO:0000250|UniProtKB:A0A061FMF5}; PhysiologicalDirection... | null | PATHWAY: Alkaloid biosynthesis. {ECO:0000250|UniProtKB:A0A061FMF5}. | null | null | FUNCTION: Involved in the biosynthesis of theobromine. {ECO:0000250|UniProtKB:A0A061FMF5}. | Theobroma cacao (Cacao) (Cocoa) | [
9304,
11485,
15446,
17478,
19924,
20230,
22282
] | [
"go_mf: caffeine synthase activity (GO:0102741)",
"interpro: SAM dependent carboxyl methyltransferase (IPR005299)",
"interpro: S-adenosyl-L-methionine-dependent methyltransferase superfamily (IPR029063)",
"interpro: Methyltransferase, alpha-helical capping domain (IPR042086)",
"cofactor: Mg(2+) (CHEBI:18420... | [
"UniProtKB-GO=ECO:0000250",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000250",
"UniProtKB=ECO:0000250",
"InterPro=match:Pfam"
] | Function: Involved in the biosynthesis of theobromine.
Catalytic Activity: 7-methylxanthine + S-adenosyl-L-methionine = theobromine + S-adenosyl-L-homocysteine + H(+)
Cofactor: Mg(2+)
Pathway: Alkaloid biosynthesis.
EC: 2.1.1.159
Sequence Mass (Da): 40842
Sequence Length: 365 |
A0A061FMF5 | BTS1_THECC | MEVKEMLFMNKGDGENSYVKTSGYTQKVAAVTQPVVYRAAQSLFTGRNSCSYQVLNVADLGCSSGPNTFTVMSTVIESTRDKCTELNWQMPEIQFYLNDLVGNDFNTLFKGLSVIQDKYKNVSCFAMGAPGSFHGRLFPQNSMHLIHSSYGVQWLSKVPKMTSEGGLSPPNKGKIYISKTSPPAVWKAYLSQFQEDFLSFLRCRSPELVPDGRMVLIIHGRKSADPTTRESCYTWEVLADAISYQVSQGLIDEEKLNSFNVPYYIPSQEEVRDLVNKEGSFLTEFVDTIEVELEGIWTGPENGAKNLRSFTEPMISHQFG... | 2.1.1.159 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9FLN8}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9FLN8}; | null | null | caffeine synthase activity [GO:0102741] | PF03492; | 1.10.1200.270;3.40.50.150; | Methyltransferase superfamily, Type-7 methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=7-methylxanthine + S-adenosyl-L-methionine = theobromine + S-adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:24604, ChEBI:CHEBI:15378, ChEBI:CHEBI:28946, ChEBI:CHEBI:48991, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.159; Evidence={ECO:0000269|PubMed:16333668}; PhysiologicalDirection=left... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.4 mM for 7-methylxanthine (in the presence of 50 uM S-adenosyl-L-methionine) {ECO:0000269|PubMed:16333668}; | PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:16333668}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0-9.5. {ECO:0000269|PubMed:16333668}; | null | FUNCTION: Involved in the biosynthesis of theobromine (PubMed:16333668). Catalyzes the conversion of 7-methylxanthine (7mX) to theobromine but not able to convert paraxanthine to caffeine (PubMed:16333668). {ECO:0000269|PubMed:16333668}. | Theobroma cacao (Cacao) (Cocoa) | [
9304,
11485,
15446,
17478,
19924,
20230,
22282
] | [
"go_mf: caffeine synthase activity (GO:0102741)",
"interpro: SAM dependent carboxyl methyltransferase (IPR005299)",
"interpro: S-adenosyl-L-methionine-dependent methyltransferase superfamily (IPR029063)",
"interpro: Methyltransferase, alpha-helical capping domain (IPR042086)",
"cofactor: Mg(2+) (CHEBI:18420... | [
"UniProtKB-GO=ECO:0000269",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000250",
"UniProtKB=ECO:0000269",
"InterPro=match:Pfam"
] | Function: Involved in the biosynthesis of theobromine. Catalyzes the conversion of 7-methylxanthine (7mX) to theobromine but not able to convert paraxanthine to caffeine.
Catalytic Activity: 7-methylxanthine + S-adenosyl-L-methionine = theobromine + S-adenosyl-L-homocysteine + H(+)
Cofactor: Mg(2+)
Pathway: Alkaloid bi... |
A0A061FTC2 | BTS3_THECC | MEVKDIVFMNKGDGENSYVKSAGLTLKVIAKTQPMVQKAVQSLFKGTHSAPLQVVNVADLGCALGPQPLESMSIVIESIVEKCGELGCEMPEIQFHLNDLAGNDFNTLFKGLSVVQEKYKNVSWFAMGAPGSFHGRLFPRNSMHLVHSCYSVHWLSKAPKITSEEGLPLNKGKIYMSKTSPPAVKEAYLSQFEEDFSSVLRFRSPELAPDGRMVLILNGRQSADPTEKDICYLRDLLAEALSYLVSEGLIDEEKLGSFNVPYYNPSQEEVERVIDKEGSFTTEFSDTVVLEIGGKNAWSDPGLRIKGYRCFSEPVLSHQF... | 2.1.1.159 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9FLN8}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9FLN8}; | null | null | caffeine synthase activity [GO:0102741] | PF03492; | 1.10.1200.270;3.40.50.150; | Methyltransferase superfamily, Type-7 methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=7-methylxanthine + S-adenosyl-L-methionine = theobromine + S-adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:24604, ChEBI:CHEBI:15378, ChEBI:CHEBI:28946, ChEBI:CHEBI:48991, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.159; Evidence={ECO:0000250|UniProtKB:A0A061FMF5}; PhysiologicalDirection... | null | PATHWAY: Alkaloid biosynthesis. {ECO:0000250|UniProtKB:A0A061FMF5}. | null | null | FUNCTION: Involved in the biosynthesis of theobromine. {ECO:0000250|UniProtKB:A0A061FMF5}. | Theobroma cacao (Cacao) (Cocoa) | [
9304,
11485,
15446,
17478,
19924,
20230,
22282
] | [
"go_mf: caffeine synthase activity (GO:0102741)",
"interpro: SAM dependent carboxyl methyltransferase (IPR005299)",
"interpro: S-adenosyl-L-methionine-dependent methyltransferase superfamily (IPR029063)",
"interpro: Methyltransferase, alpha-helical capping domain (IPR042086)",
"cofactor: Mg(2+) (CHEBI:18420... | [
"UniProtKB-GO=ECO:0000250",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000250",
"UniProtKB=ECO:0000250",
"InterPro=match:Pfam"
] | Function: Involved in the biosynthesis of theobromine.
Catalytic Activity: 7-methylxanthine + S-adenosyl-L-methionine = theobromine + S-adenosyl-L-homocysteine + H(+)
Cofactor: Mg(2+)
Pathway: Alkaloid biosynthesis.
EC: 2.1.1.159
Sequence Mass (Da): 40665
Sequence Length: 365 |
A0A061I403 | FICD_CRIGR | MPMASVIAVAEPKWISVWGRFLWLTLLSMALGSLLALLLPLGAVEEQCLAVLRSFHLLRSKLDRTQHVVTKCTSPSTELSVTSGDVGLLTVKTKTSPAGKLEAKAALNQALEMKRQGKREKAHKLFLHALKMDPGFVDALNEFGIFSEEEKDIIQADYLYTRALTISPFHEKALVNRDRTLPLVEEIDQRYFSIIDSKVKKVMSIPKGSSALRRVMEETYYHHIYHTVAIEGNTLTLSEIRHILETRYAVPGKSLEEQNEVIGMHAAMKYINTTLVSRIGSVTIDDMLEIHRRVLGYVDPVEAGRFRRTQVLVGHHIPPH... | 2.7.7.108; 3.1.4.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; Note=Divalent metal cation. Prefers Mn(2+) over Mg(2+). {ECO:0000250|UniProtKB:Q9BVA6}; | protein adenylylation [GO:0018117]; protein deadenylylation [GO:0044602]; regulation of IRE1-mediated unfolded protein response [GO:1903894]; response to endoplasmic reticulum stress [GO:0034976] | endoplasmic reticulum membrane [GO:0005789] | AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]; protein-folding chaperone binding [GO:0051087] | PF02661; | 1.10.3290.10;1.25.40.10; | Fic family | PTM: Auto-AMPylated in vitro. {ECO:0000250|UniProtKB:Q9BVA6}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BVA6}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9BVA6}. | CATALYTIC ACTIVITY: Reaction=L-tyrosyl-[protein] + ATP = O-(5'-adenylyl)-L-tyrosyl-[protein] + diphosphate; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIV... | null | null | null | null | FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (PubMed:27918543). The side chain of Glu-231 determines which of the two ... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) | [
172,
2296,
3141,
6567,
8167,
8706,
8915,
9126,
9228,
11074,
12894,
16491,
19924,
19930,
20428,
20429,
21966,
24894,
25107
] | [
"ec: EC 2.7.7.108",
"go_bp: protein adenylylation (GO:0018117)",
"go_bp: response to endoplasmic reticulum stress (GO:0034976)",
"go_cc: endoplasmic reticulum membrane (GO:0005789)",
"go_mf: ATP binding (GO:0005524)",
"go_mf: Hsp70 protein binding (GO:0030544)",
"go_mf: protein homodimerization activity... | [
"UniProtKB=ECO:0000250,ECO:0000269",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000353",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000314",
"InterPro=match",
"InterPro=match",... | Function: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context. The side chain of Glu-231 determines which of the two opposing activitie... |
A0A061IR73 | PEX6_CRIGR | MALAVLRVLDPFPAETPPLAVLLPPGGPWPATGLGLVLALRPASESPAGPALLVAALEGPGSQNGQRGPGPPQLLVSRALLRLLALGPGARVRARPVRRPPALGWALLGSAPGPGPGPRVGPLLVRRGESLPVPGSRVLETRPALQGLLGPGTRLAVTELRGRAKLGPESTQHSRLPPPPVASSFAVSHAVRQLKGVLGGTGDALGVTRSCLRGLGLFQGEWVWVARVGEFPNTSQPHLAKVQLLEPRWDLSERLGPSSGQLGEPLADGLVFVPATLAFNLGCDPLEVGELRIQRYLEGSIIPEDRGSCSLMSGPPFARE... | 3.6.4.- | null | protein import into peroxisome matrix [GO:0016558]; protein import into peroxisome matrix, receptor recycling [GO:0016562]; protein import into peroxisome matrix, translocation [GO:0016561]; protein stabilization [GO:0050821]; protein targeting to peroxisome [GO:0006625]; protein unfolding [GO:0043335] | ATPase complex [GO:1904949]; cytosol [GO:0005829]; peroxisomal membrane [GO:0005778]; photoreceptor outer segment [GO:0001750] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; membrane protein dislocase activity [GO:0140567]; protein-containing complex binding [GO:0044877]; ubiquitin-modified protein reader activity [GO:0140036] | PF00004;PF25395;PF25394; | 1.10.8.60;3.40.50.300; | AAA ATPase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q13608}. Peroxisome membrane {ECO:0000250|UniProtKB:Q13608}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q13608}. Note=Associated with peroxisomal membranes; anchored by PEX26 to peroxisome membranes. Localized at the base o... | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13608}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:Q136... | null | null | null | null | FUNCTION: Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling (PubMed:23929341, PubMed:9539740). Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls i... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) | [
1062,
2264,
2267,
3682,
4486,
6474,
6561,
6588,
7464,
8167,
8563,
8980,
9335,
9361,
11013,
11116,
11117,
15266,
18210,
18471,
20013,
20513,
24873,
24883,
24888,
24960,
25008,
25063
] | [
"go_bp: protein targeting to peroxisome (GO:0006625)",
"go_bp: protein import into peroxisome matrix (GO:0016558)",
"go_bp: protein import into peroxisome matrix, receptor recycling (GO:0016562)",
"go_bp: protein unfolding (GO:0043335)",
"go_bp: protein stabilization (GO:0050821)",
"go_cc: photoreceptor o... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000315",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=EC... | Function: Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen thro... |
A0A063C1W0 | USTZ_USTVR | MASHHQLLCLNILGFRKPGISTEDYRNYMVNVHAPLVAGLMEKYGFLHFTMSHASEQSPQLMDQLYDAQFANTASYDCCVQIVFPSIECFVNMKADPYFKQTVGPDHEKFADTKRSQMMIGWFSPLLINGQQTDSLSAAE | 1.-.-.- | null | null | null | oxidoreductase activity [GO:0016491] | PF07110; | 3.30.70.100; | TpcK family | null | null | CATALYTIC ACTIVITY: Reaction=naphtopyrone YWA1 = norrubrofusarin + H2O + H(+); Xref=Rhea:RHEA:62680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:133763, ChEBI:CHEBI:145839; Evidence={ECO:0000305|PubMed:31050129}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62681; Evidence={ECO:0000305|PubMed:31050129}; | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:31050129}. | null | null | FUNCTION: Dehydratase; part of the gene cluster that mediates the biosynthesis of ustilaginoidins, dimeric gamma-naphthopyrones isolated from different fungal species (PubMed:31050129). The first step in the biosynthesis of ustilaginoidins is the production of gamma-naphthopyrone precursor YWA1 by the non-reducing poly... | Ustilaginoidea virens (Rice false smut fungus) (Villosiclava virens) | [
8506,
12688
] | [
"go_mf: oxidoreductase activity (GO:0016491)",
"interpro: Dimeric alpha-beta barrel (IPR011008)"
] | [
"UniProtKB-GO=ECO:0000501",
"InterPro=match"
] | Function: Dehydratase; part of the gene cluster that mediates the biosynthesis of ustilaginoidins, dimeric gamma-naphthopyrones isolated from different fungal species. The first step in the biosynthesis of ustilaginoidins is the production of gamma-naphthopyrone precursor YWA1 by the non-reducing polyketide synthase us... |
A0A063CBJ7 | SCRE2_USTVR | MLINAARLLLPAAALVHLSLAWATSDRCNGYSSTLIQIKHAGDIYKQPSVPGLPPPGVNPYSLIDTLLKNGEDWCKHCASPRVSVDAGRYKAQMDKLLSYAHPYSASSWDSVQSLGDALEHLCKASRKEN | null | null | null | extracellular region [GO:0005576]; host cell [GO:0043657]; host cell periplasmic space [GO:0044229] | null | null | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31105658}. Host cell {ECO:0000269|PubMed:31105658}. Host periplasm {ECO:0000269|PubMed:31105658}. Note=Localizes in periplasmic spaces and perhaps in multiple subcellular compartments of plant cells. {ECO:0000269|PubMed:31105658}. | null | null | null | null | null | FUNCTION: Secreted effector required for full virulence of U.virens (PubMed:31105658). Inhibits host pathogen-associated molecular pattern-triggered immunity including flg22- and chitin-induced defense gene expression and oxidative burst (PubMed:31105658). {ECO:0000269|PubMed:31105658}. | Ustilaginoidea virens (Rice false smut fungus) (Villosiclava virens) | [
6485,
7141,
24983,
25057
] | [
"go_cc: extracellular region (GO:0005576)",
"go_cc: host cell (GO:0043657)",
"subcellular_location: Secreted (SL-0243)",
"subcellular_location: Host cell (SL-0427)"
] | [
"UniProtKB-GO=ECO:0000269",
"UniProtKB-GO=ECO:0000269",
"UniProtKB=ECO:0000269",
"UniProtKB=ECO:0000269"
] | Function: Secreted effector required for full virulence of U.virens. Inhibits host pathogen-associated molecular pattern-triggered immunity including flg22- and chitin-induced defense gene expression and oxidative burst.
Subcellular Location: Secreted; Host cell; Host periplasm
Domain: The Plant immunity suppression do... |
A0A067CMC7 | HTP3_SAPPC | MLEVPVWIPILAFAVGLGLGLLIPHLQKPFQRFSTVNDIPKEFFEHERTLRGKVVSVTDGDTIRVRHVPWLANGDGDFKGKLTETTLQLRVAGVDCPETAKFGRTGQPFGEEAKAWLKGELQDQVVSFKLLMKDQYSRAVCLVYYGSWAAPMNVSEELLRHGYANIYRQSGAVYGGLLETFEALEAEAREKRVNIWSLDKRETPAQYKARK | 3.1.31.- | null | null | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; host cell cytosol [GO:0044164] | null | PF00565; | 2.40.50.90; | RxLR effector family; LCL3 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29904064}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:29904064}. Note=Uptake into host cells is more efficient at a lower pH of 5.5. S.parasitica acidifies the pH of its environment, which likely leads to the exposure of a gp96 protein to the host cell surface. T... | null | null | null | null | null | FUNCTION: Effector involved in the disease saprolegniosis in salmonids and other freshwater fish, resulting in considerable economic losses in aquaculture (PubMed:29904064). Within the host fish cells, Htp3 is released from vesicles into host cytosol where it degrades nucleic acids (PubMed:29904064). {ECO:0000269|PubMe... | Saprolegnia parasitica (strain CBS 223.65) | [
6485,
6538,
7144,
13646,
16107,
20979,
24983,
25044,
25047
] | [
"go_cc: extracellular region (GO:0005576)",
"go_cc: cytoplasm (GO:0005737)",
"go_cc: host cell cytosol (GO:0044164)",
"interpro: Staphylococcal nuclease (SNase-like), OB-fold (IPR016071)",
"interpro: SNase-like, OB-fold superfamily (IPR035437)",
"pfam: SNase (PF00565)",
"subcellular_location: Secreted (... | [
"UniProtKB-GO=ECO:0000269",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000269",
"UniProtKB=ECO:0000269",
"UniProtKB=ECO:0000269"
] | Function: Effector involved in the disease saprolegniosis in salmonids and other freshwater fish, resulting in considerable economic losses in aquaculture. Within the host fish cells, Htp3 is released from vesicles into host cytosol where it degrades nucleic acids.
Subcellular Location: Secreted; Host cytoplasm, Host c... |
A0A067DDU9 | OSC3_CITSI | MWRLKIGDYGTKNDPYIFSTNNFAGRQIWEFDPDAGSVEELAEVEEARLNYLKNRFNVKNSSDLLWQIQILREKKFKQTIPQVKIGDRGEEITPEIATTALRRAVNIFSALQSSHGHWPADNSGPLFFNTPMNEDGGWGLHVEGHSTMFGTVFNYICMRLLGEGPDGGENSGCTRARKWILDRGGATGIPSWGKTWLSILGVYNWSGCNPMPPEFWKLPYFLPISPGKLLCYCRLTYMPMSYFYGKRFVGPITPLVLQLREEIYIQPYDEINWSKLRHLCAKEDLFFPHTTVQNLLWDALHNLVEPVLNRWPLNKLREKS... | 5.4.99.41 | null | triterpenoid biosynthetic process [GO:0016104] | lipid droplet [GO:0005811] | beta-amyrin synthase activity [GO:0042300]; lupeol synthase activity [GO:0042299] | PF13243;PF13249; | 1.50.10.20; | Terpene cyclase/mutase family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-2,3-epoxysqualene = lupeol; Xref=Rhea:RHEA:31383, ChEBI:CHEBI:6570, ChEBI:CHEBI:15441; EC=5.4.99.41; Evidence={ECO:0000269|PubMed:31371503}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31384; Evidence={ECO:0000269|PubMed:31371503}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:31371503}. | null | null | FUNCTION: Oxidosqualene cyclase catalyzing the conversion of 2,3-oxidosqualene (2,3-epoxysqualene) to lupeol, a pentacyclic triterpenoid with anti-inflammatory properties. {ECO:0000269|PubMed:31371503}. | Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis) | [
2205,
6578,
8898,
10633,
12422,
14138,
15793,
15794,
20285,
23644,
23646
] | [
"go_bp: triterpenoid biosynthetic process (GO:0016104)",
"go_cc: lipid droplet (GO:0005811)",
"go_mf: beta-amyrin synthase activity (GO:0042300)",
"interpro: Terpene synthase, conserved site (IPR002365)",
"interpro: Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid (IPR008930)",
"interpro: S... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000269",
"InterPro=match:Pfam",
"InterPro=match:Pfam"
] | Function: Oxidosqualene cyclase catalyzing the conversion of 2,3-oxidosqualene (2,3-epoxysqualene) to lupeol, a pentacyclic triterpenoid with anti-inflammatory properties.
Catalytic Activity: (S)-2,3-epoxysqualene = lupeol
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 5.4.99.41
Sequence Mass (... |
A0A067DE75 | C6AD2_CITSI | MELLLLLLSTLLILTLCCHFFYLFIRTNKQNGSEKLPLPPGHVSWPFKYFETLDYLKKARTNTIHKFIAERVQKYKTKCFKTCHIGQNMVFLTSAEGNKFLFSNDYKLVRSWWPVTFLKVFENAGEEITVEEVIRARKQFLSFFNEPDALARHVAITDQVVQDHFKCYWDGSKQVGVYPLARKLTFDVSCRLLADIQDREILDESLPLMGNVVRAFFAFPINFPGTILNRAIKSSRRLRKIFVDIIKERRGDLLEKKNLDQRNDVLSRLLVENYKEGRDIDDVFLAKNLVSLLSAAYDNPSVTITSIVKNLAERPEIYEK... | 1.14.14.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | saponin biosynthetic process [GO:0016135]; terpenoid biosynthetic process [GO:0016114] | 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=(1R,2R,3S,8R,10R,11R,15S,16S)-3-(acetyloxy)-15-[(4R)-4-[(2S)-3,3-dimethyloxiran-2-yl]-1,4-dihydroxybutan-2-yl]-2,7,7,11,16-pentamethyl-5-oxo-6-oxatetracyclo[9.7.0.0(2,8).0(12,16)]octadec-12-en-10-yl acetate + reduced [NADPH--hemoprotein reductase] + O2 = (1R,2R,3S,8R,10R,11R,15S,16S)-3-(ace... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:36701471}. | null | null | FUNCTION: Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus (PubMed:36701471). Catalyzes the formation of (1R,2R,3S,8R,10R,11R,15S,16S)-3-(acetyloxy)-15-(1-hydroxy-4-oxobutan-2-yl)-2,7,7,1... | Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis) | [
2207,
2217,
6727,
7856,
8157,
8525,
8657,
10002,
10647,
13954,
16401,
19936,
20574,
24930,
25105
] | [
"go_bp: terpenoid biosynthetic process (GO:0016114)",
"go_bp: saponin biosynthetic process (GO:0016135)",
"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 re... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000318",
"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",
... | Function: Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus. Catalyzes the formation of (1R,2R,3S,8R,10R,11R,15S,16S)-3-(acetyloxy)-15-(1-hydroxy-4-oxobutan-2-yl)-2,7,7,11,16-pentamethyl-5... |
A0A067DFU5 | MOI1_CITSI | MSHSSGTDMALNFSTASLHAWNGVSLLLIIFVTWIISGMSQAKSKIERLLICWWALTGLIHVFQEGYYVFTPDLFNDNSPNFMAEIWKEYSKGDSRYATRHTSVLGIESVASIVLGPLSLLAAYAVAKQKSYRYIFQFAISIAQLYGTIQYFLTAFLEGDNFASSRYYYYSYYVGQSSIWVIVPMLIATRYWIKIHAICKRLQDKKVTKVG | 5.3.3.- | null | sterol biosynthetic process [GO:0016126]; terpenoid biosynthetic process [GO:0016114] | endoplasmic reticulum [GO:0005783]; membrane [GO:0016020] | cholestenol delta-isomerase activity [GO:0047750]; steroid Delta-isomerase activity [GO:0004769] | PF05241; | null | EBP family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=7,8-epoxymelianol = protoglabretal; Xref=Rhea:RHEA:80299, ChEBI:CHEBI:231452, ChEBI:CHEBI:231454; Evidence={ECO:0000269|PubMed:36701471}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:80300; Evidence={ECO:0000269|PubMed:36701471}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:36701471}. | null | null | FUNCTION: Isomerase involved in the biosynthesis of glabretanes triterpene natural products such as glabretal, a component with in vitro antiproliferative properties on lymphocytes (PubMed:36701471). Catalyzes the conversion of 7,8-epoxymelianol to protoglabretal via skeletal rearrangements (PubMed:36701471). {ECO:0000... | Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis) | [
2207,
2213,
6563,
6727,
15825,
22688,
24930,
25110
] | [
"go_bp: terpenoid biosynthetic process (GO:0016114)",
"go_bp: sterol biosynthetic process (GO:0016126)",
"go_cc: endoplasmic reticulum (GO:0005783)",
"go_cc: membrane (GO:0016020)",
"interpro: EXPERA domain (IPR033118)",
"pfam: EBP (PF05241)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topo... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000318",
"UniProtKB-GO=ECO:0000318",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Function: Isomerase involved in the biosynthesis of glabretanes triterpene natural products such as glabretal, a component with in vitro antiproliferative properties on lymphocytes. Catalyzes the conversion of 7,8-epoxymelianol to protoglabretal via skeletal rearrangements.
Catalytic Activity: 7,8-epoxymelianol = proto... |
A0A067DKP1 | L1AT_CITSI | MEINNVSSEIIKPSSPTPQHLKTHKLSVLDQVAGDSLFPIILFYPQTCSNNTSLNKTSDLLKRSLSQTLTLYHPFAGRLKDEFSIDCDDTGATFIEARAAASDMSEIVKQPTVDMLEQLMPYKLNEKPSVAVNLAAKVTYFEHCGGMALCVCFSHVIADITTAANFIKTWVTFASGSDTSSEDDDVIKHAVFGCSSIFPPQKFSSFSRNVISENHSNSAEILTKRFIFDGDKIAALKEKMGSESSSGYHPTRVEAVSAIILGGIMSVEKQADDFNHSHLVASIAVNLRNRVNPPIPEQSIGNIVQAGIAKLPIEKKTIDY... | 2.1.1.- | null | terpenoid biosynthetic process [GO:0016114] | null | acyltransferase activity [GO:0016746] | PF02458; | 3.30.559.10; | Plant acyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=(1S)-1-hydroxy-luvungin A + acetyl-CoA = (1S)-1-acetoxy-luvungin A + CoA; Xref=Rhea:RHEA:80323, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:231477, ChEBI:CHEBI:231478; Evidence={ECO:0000269|PubMed:36701471}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:80324; Evidence={ECO:000... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:36701471}. | null | null | FUNCTION: Acetyltransferase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus (PubMed:36701471). Catalyzes the formation of (1S)-1-acetoxy-luvungin A from (1S)-1-hydroxy-luvungin A (PubMed:36701471). {E... | Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis) | [
2207,
8531,
14804
] | [
"go_bp: terpenoid biosynthetic process (GO:0016114)",
"go_mf: acyltransferase activity (GO:0016746)",
"interpro: Chloramphenicol acetyltransferase-like domain superfamily (IPR023213)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000318",
"InterPro=match"
] | Function: Acetyltransferase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus. Catalyzes the formation of (1S)-1-acetoxy-luvungin A from (1S)-1-hydroxy-luvungin A.
Catalytic Activity: (1S)-1-hydroxy-luv... |
A0A067DT54 | C8A37_CITSI | MELYFSWLILALAIFIGTYAFVFGVLRRVNEWYHCGKLGEMKHSLPPGDMGWPLVGNMLSHQKAFKSSEPQSFIYNLFERYGRKGIYRNHIFGSPCVIVVAPEACKQVFLDDENFKMGYPTSTNKLTFRGSFITASKEGQKRIRKLATSPLKGHKAIVVYIDNIEEIVIKSLKGWASLDTPIEFLTEMRKATFKIIANIFLGSSSDSVIGSVEKHYIDYAHGLISPFPINLPGFSFHKAMKARDMLGEILQPVLNERRAMKSDEQKGRKGLIDLLMEVEDENGTKLDDLDIIDMLISFLSAGHESSAHIATWALIHLHKH... | 1.14.14.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | pollen tube development [GO:0048868]; terpenoid biosynthetic process [GO:0016114] | 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=luvungin A + reduced [NADPH--hemoprotein reductase] + O2 = (1S)-1-hydroxy-luvungin A + oxidized [NADPH--hemoprotein reductase] + H2O + H(+); Xref=Rhea:RHEA:80319, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CH... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:36701471}. | null | null | FUNCTION: Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus (PubMed:36701471). Catalyzes the conversion of luvungin A to (1S)-1-hydroxy-luvungin A (PubMed:36701471). {ECO:0000269|PubMed:36... | Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis) | [
2207,
4413,
6727,
7856,
8157,
8525,
8657,
10002,
10647,
13954,
16401,
19936,
20574,
24930,
25105
] | [
"go_bp: terpenoid biosynthetic process (GO:0016114)",
"go_bp: pollen tube development (GO:0048868)",
"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 reducti... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000318",
"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",
... | Function: Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus. Catalyzes the conversion of luvungin A to (1S)-1-hydroxy-luvungin A.
Catalytic Activity: luvungin A + reduced [NADPH--hemoprote... |
A0A067E1K2 | C8A51_CITSI | MDSNFLWPMLAMFLGSLVVMFGFLKKINEWYYVGRLGEKKNSLPPGEMGWPLLGNMLSLIKAFRSSDPDSFIHCLVDRYGRTGVYKSHLFWSPSIVVCTPETCKHVLMDNEKFGRGNPESTKELLGKQTVSLSTEEHKRLRKLTTNPFRGDKALTMYVGYIEDIVIDMLDELGSINKPVVFLFEMRKLAFKVIGHIVFGTTSDHLLELMEKYYTDLLLGLRSPAINIPGFAFHGALKARKLLVKLLEEVLEERKKRSGIEQKKGQKGMIDLLLEAEDENGKKLEDVHIIDLLIINLLAGHESSAHASMWAVLYLNQHPEM... | 1.14.14.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | pollen tube development [GO:0048868]; terpenoid biosynthetic process [GO:0016114] | 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=melianol + reduced [NADPH--hemoprotein reductase] + O2 = 7,8-epoxymelianol + oxidized [NADPH--hemoprotein reductase] + H2O + H(+); Xref=Rhea:RHEA:80291, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:36701471}. | null | null | FUNCTION: Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus (PubMed:36701471). Catalyzes the epoxidation of melianol to produce 7,8-epoxymelianol (PubMed:36701471). {ECO:0000269|PubMed:367... | Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis) | [
2207,
4413,
6727,
7856,
8157,
8525,
8657,
10002,
10647,
16401,
19936,
20574,
24930,
25105
] | [
"go_bp: terpenoid biosynthetic process (GO:0016114)",
"go_bp: pollen tube development (GO:0048868)",
"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 reducti... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000318",
"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:Pfa... | Function: Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus. Catalyzes the epoxidation of melianol to produce 7,8-epoxymelianol.
Catalytic Activity: melianol + reduced [NADPH--hemoprotein ... |
A0A067E3D8 | MOI2_CITSI | MSHPYSPSDLILPDFTPNLRSTSEVHAWNGIASFLVMFIIWRISGRSPRKLSKTDRWLMIWWAVSGLIHIIHEGYWFFSPEFYKDKSGNYFAEVWKEYSKGDSRYASRHVAVLAIEGIAVIFVGPASLLAMYAIAKGKSYSYILQFALSLVQFYGSSLYFITAFLEGNKFACTRYFYYSYFIAQGGTWLLFPALIMIRCWKRICAACLLLDHKTKVY | 5.3.3.- | null | sterol biosynthetic process [GO:0016126]; terpenoid biosynthetic process [GO:0016114] | endoplasmic reticulum [GO:0005783]; membrane [GO:0016020] | cholestenol delta-isomerase activity [GO:0047750]; steroid Delta-isomerase activity [GO:0004769] | PF05241; | null | EBP family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=7,8-epoxymelianol = isomeliandiol; Xref=Rhea:RHEA:80295, ChEBI:CHEBI:231452, ChEBI:CHEBI:231453; Evidence={ECO:0000269|PubMed:36701471}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:80296; Evidence={ECO:0000269|PubMed:36701471}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:36701471}. | null | null | FUNCTION: Isomerase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus (PubMed:36701471). Catalyzes the conversion of 7,8-epoxymelianol to isomeliandiol via skeletal rearrangements (PubMed:36701471). {EC... | Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis) | [
2207,
2213,
6563,
6727,
15825,
22688,
24930,
25110
] | [
"go_bp: terpenoid biosynthetic process (GO:0016114)",
"go_bp: sterol biosynthetic process (GO:0016126)",
"go_cc: endoplasmic reticulum (GO:0005783)",
"go_cc: membrane (GO:0016020)",
"interpro: EXPERA domain (IPR033118)",
"pfam: EBP (PF05241)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topo... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000318",
"UniProtKB-GO=ECO:0000318",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Function: Isomerase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus. Catalyzes the conversion of 7,8-epoxymelianol to isomeliandiol via skeletal rearrangements.
Catalytic Activity: 7,8-epoxymelianol =... |
A0A067ECN5 | OSC1_CITSI | MWRLKVAEGDKNSPYMFTTNNFVGRQIWEFDPKAGSPEELAEVEEARQKFYKNRHNVKPAGDLLWRLQFLREKNFKQRIPQVKVKDGDAITYETATTAMKRAAHYFSAIQASDGHWPAENAGPMYFLPPFVFCLYITGHLNTVFTVEHRREILRYLYNHQHEDGGWGVHVEAPSSMFGTVFSYLCMRLLGLGPNDGENNACARARKWIRDHGGVTYIPSWGKNWLSILGIFEWSGTNPMPPEFWILPSFVPLHPSKMWCYCRLVYMPVSYLYGKRFVGPITPLIQQLREELHTQPYNEINWRKVRHLCSKEDLYYPHPFV... | 5.4.99.56 | null | triterpenoid biosynthetic process [GO:0016104] | lipid droplet [GO:0005811] | beta-amyrin synthase activity [GO:0042300] | PF13243;PF13249; | 1.50.10.20; | Terpene cyclase/mutase family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-2,3-epoxysqualene = tirucalla-7,24-dien-3beta-ol; Xref=Rhea:RHEA:31887, ChEBI:CHEBI:15441, ChEBI:CHEBI:63468; EC=5.4.99.56; Evidence={ECO:0000269|PubMed:31371503}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31888; Evidence={ECO:0000269|PubMed:31371503}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:31371503}. | null | null | FUNCTION: Oxidosqualene cyclase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus (PubMed:31371503). Converts 2,3-oxidosqualene (2,3-epoxysqualene) into tirucalladienol, generating rings and asymmetric ... | Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis) | [
2205,
6578,
8898,
10633,
12422,
14138,
15793,
15794,
23644,
23646
] | [
"go_bp: triterpenoid biosynthetic process (GO:0016104)",
"go_cc: lipid droplet (GO:0005811)",
"go_mf: beta-amyrin synthase activity (GO:0042300)",
"interpro: Terpene synthase, conserved site (IPR002365)",
"interpro: Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid (IPR008930)",
"interpro: S... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"InterPro=match:Pfam"
] | Function: Oxidosqualene cyclase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus. Converts 2,3-oxidosqualene (2,3-epoxysqualene) into tirucalladienol, generating rings and asymmetric centers in a singl... |
A0A067EES0 | L21AT_CITSI | MDLQITCTEIIKPSSPTPQHQSTYKLSIIDQLTPNVYFSIILLYSNAGESTAKTSDHLKKSLSNTLTHYYPLAGQLKYDQLIVDCNDQGVPFIEAHVANDMRQLLKIPNIDVLEQLLPFKPHEGFDSDRSNLTLQVNYFGCGGMAIGLCFRHKVIDATTAAFFVKNWGVIARGAGEIKDLIIDHASLFPARDLSCLAKSVDEEFLKPESETKRFVFDGPTIASFQETFTSFERRPTRFEVVSAVILGALITATRESDDESNVPERLDTIISVNLRQRMNPPFPEHCMGNIISGGLVYWPLEKKVDYGCLAKEIHESIKKV... | 2.1.1.- | null | terpenoid biosynthetic process [GO:0016114] | null | acyltransferase activity [GO:0016746] | PF02458; | 3.30.559.10; | Plant acyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=isomeliandiol + acetyl-CoA = 21-O-acetyl-isomeliandiol + CoA; Xref=Rhea:RHEA:80303, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:231453, ChEBI:CHEBI:231455; Evidence={ECO:0000269|PubMed:36701471}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:80304; Evidence={ECO:0000269|PubMed:... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:36701471}. | null | null | FUNCTION: Acetyltransferase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus (PubMed:36701471). Catalyzes the formation of 21-O-acetyl-isomeliandiol from isomeliandiol (PubMed:36701471). {ECO:0000269|P... | Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis) | [
2207,
8531,
14804
] | [
"go_bp: terpenoid biosynthetic process (GO:0016114)",
"go_mf: acyltransferase activity (GO:0016746)",
"interpro: Chloramphenicol acetyltransferase-like domain superfamily (IPR023213)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000318",
"InterPro=match"
] | Function: Acetyltransferase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus. Catalyzes the formation of 21-O-acetyl-isomeliandiol from isomeliandiol.
Catalytic Activity: isomeliandiol + acetyl-CoA = 2... |
A0A067ELB0 | C71C1_CITSI | MEFIILSLLLLSLALYSLYYVIIKPKPTTQNLPPGRKGWPFIGETLEYHALSKKGCIEKFMSQRMQKYSSKIFKTSYLGADMVFLCSAEGNKLLFSNEHKLFKPWLPRIIENSFKSSPNITLQDEFNSLRRVIGSFTEPNALRRYVGMMDANAKRHLRKYWDGNDVVKVHDLSRKFIFALCSELMYNIHDTRTADELENLAHCIMTEFFIIPVNIPGTKFGRAVRAGREFHQRFRNMIKQRRLEIEEKREPEHKDILSLLLLEKNKDGEDLTESEIALKMQAVLIGAYDNPSIAISTIIKFLAELPEIYEQVLREQMEIA... | 1.14.14.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | saponin biosynthetic process [GO:0016135]; terpenoid biosynthetic process [GO:0016114] | 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=(21S)-21-acetoxyl-apo-melianone + reduced [NADPH--hemoprotein reductase] + O2 = luvungin A + oxidized [NADPH--hemoprotein reductase] + H2O + H(+); Xref=Rhea:RHEA:80311, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, Ch... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:36701471}. | null | null | FUNCTION: Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus (PubMed:36701471). Catalyzes the conversion of (21S)-21-acetoxyl-apo-melianone to luvungin A (PubMed:36701471). {ECO:0000269|Pub... | Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis) | [
2207,
2217,
6727,
7856,
8157,
8525,
8657,
10002,
10647,
13954,
16401,
19936,
20574,
24930,
25105
] | [
"go_bp: terpenoid biosynthetic process (GO:0016114)",
"go_bp: saponin biosynthetic process (GO:0016135)",
"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 re... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000318",
"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",
... | Function: Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus. Catalyzes the conversion of (21S)-21-acetoxyl-apo-melianone to luvungin A.
Catalytic Activity: (21S)-21-acetoxyl-apo-melianone ... |
A0A067ETA8 | L7AT_CITSI | MEPEILSIELIKPSSPTPRHLKTHKLCFLDQYRNHAYFPMVFFYSVTHDTNLNLSNETDIAQIVSVRLQLLKQSLPETLSLFYPFAGKIKDNLSIDCSDEGIYFTEARFKSPLKEFFNQQNFSCLTYKFVPFDAKELEGSISGLHVAKIQVTSFACGGIVICACLSHLFADGATLCSFLKCWVATACKNNEQRISPNNDASWLFPQNEAYPKEGTWLAMCPRFFGHGRFVTRRFVFDAKAIATIKAKASSSTRVQNPTPTRVEAVSALFSKCVMAAFKAKHGSHKTTLLTHSVNLRNKAKSILSEYSMGNIVWNANALCT... | 2.1.1.- | null | terpenoid biosynthetic process [GO:0016114] | null | acyltransferase activity [GO:0016746] | PF02458; | 3.30.559.10; | Plant acyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=(1S)-1-acetoxy-luvungin A + acetyl-CoA = (1S)-1,7-diacetoxy-luvungin A + CoA; Xref=Rhea:RHEA:80331, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:231478, ChEBI:CHEBI:231479; Evidence={ECO:0000269|PubMed:36701471}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:80332; Evidence={ECO... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:36701471}. | null | null | FUNCTION: Acetyltransferase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus (PubMed:36701471). Catalyzes the formation of (1S)-1,7-diacetoxy-luvungin A from (1S)-1-acetoxy-luvungin A (PubMed:36701471)... | Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis) | [
2207,
8531,
14804
] | [
"go_bp: terpenoid biosynthetic process (GO:0016114)",
"go_mf: acyltransferase activity (GO:0016746)",
"interpro: Chloramphenicol acetyltransferase-like domain superfamily (IPR023213)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000318",
"InterPro=match"
] | Function: Acetyltransferase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus. Catalyzes the formation of (1S)-1,7-diacetoxy-luvungin A from (1S)-1-acetoxy-luvungin A.
Catalytic Activity: (1S)-1-acetoxy... |
A0A067F4I6 | C1BQ4_CITSI | MDTTTTATQMLHLPSLPVLLSFLLFLLMLIRYWKNSNGQGKQPPGPKPLPILGNLHQLADGQPHHVMTKLCRKYGPVMKLKLGQLDAVIISSPEAAKEVLKTNEIKFAQRPEVYAVEIMSYDHSSIVFAPYGDYWREMRKISVLELLSNKRVQSFRSIREDEVWGLVEFISSNQGRPINLSEKIFTMTNDIIARAAFGRKNSDQHNFTVLLEEIMKIGAGFAIADLYPSLTFLRPLTGVKPALMRIQKKMDKILEDIVAEHKLKRKAAANNNVKLEEEDLVDTLLNYAEATNKNEFHLTIDQVKAVTLDIFSAGSETSAT... | 1.14.14.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | terpenoid biosynthetic process [GO:0016114] | 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=dihydroniloticin + 2 reduced [NADPH--hemoprotein reductase] + 2 O2 = melianol + 2 oxidized [NADPH--hemoprotein reductase] + 3 H2O + 2 H(+); Xref=Rhea:RHEA:80283, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHE... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:31371503}. | null | null | FUNCTION: Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus (PubMed:31371503). Catalyzes the conversion of dihydroniloticin to the protolimonoid melianol (PubMed:31371503). {ECO:0000269|Pu... | Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis) | [
2207,
6727,
7856,
8157,
8525,
8657,
10002,
10647,
13954,
16401,
19936,
20574,
24930,
25105
] | [
"go_bp: terpenoid biosynthetic process (GO:0016114)",
"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: h... | [
"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",
"UniProtKB=ECO:0000250",
"InterPro=match:Pfam",
"Uni... | Function: Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus. Catalyzes the conversion of dihydroniloticin to the protolimonoid melianol.
Catalytic Activity: dihydroniloticin + 2 reduced [N... |
A0A067FI21 | OSC2_CITSI | MWKLKVGEGNGEKDAYIYSTNNYAGRQIWQFDPEAGSDEERAQVEAARLHFYNNRDHLKPSADLLWRMQFLKEKKFKQTIPQVKIKVDGDEEEITYETAATTALRRGVRFFSALQASDGHWPAENAGPLFFLPPLVMCLYITGHLNTVFPAESEHRKEILRYIHYHQNEDGGWGLHIEGHSTMFCTALNYICLRILGQPPHHIACATARNWILDRGGVTLIPSWGKTWLSILGVFDWSGCNPMPPEFWILPSFLPMHPGKMWCYCRMVYMPMSYLYGKRFVGAITPLVVELRQELYPEAEPYHKVNWGKARHLCAKEDAY... | 5.4.99.39 | null | triterpenoid biosynthetic process [GO:0016104] | lipid droplet [GO:0005811] | beta-amyrin synthase activity [GO:0042300] | PF13243;PF13249; | 1.50.10.20; | Terpene cyclase/mutase family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-2,3-epoxysqualene = beta-amyrin; Xref=Rhea:RHEA:31007, ChEBI:CHEBI:10352, ChEBI:CHEBI:15441; EC=5.4.99.39; Evidence={ECO:0000269|PubMed:31371503}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31008; Evidence={ECO:0000269|PubMed:31371503}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:31371503}. | null | null | FUNCTION: Oxidosqualene cyclase catalyzing the conversion of 2,3-oxidosqualene (2,3-epoxysqualene) to beta-amyrin, a pentacyclic triterpenoid with anti-inflammatory properties. {ECO:0000269|PubMed:31371503}. | Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis) | [
367,
2205,
6578,
8898,
10633,
12422,
14138,
15793,
15794,
20284,
23644,
23646
] | [
"ec: EC 5.4.99.39",
"go_bp: triterpenoid biosynthetic process (GO:0016104)",
"go_cc: lipid droplet (GO:0005811)",
"go_mf: beta-amyrin synthase activity (GO:0042300)",
"interpro: Terpene synthase, conserved site (IPR002365)",
"interpro: Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid (IPR00... | [
"UniProtKB=ECO:0000269",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000269",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000269",
"InterPro=match:Pfam",
"InterPro=match:Pfam"
] | Function: Oxidosqualene cyclase catalyzing the conversion of 2,3-oxidosqualene (2,3-epoxysqualene) to beta-amyrin, a pentacyclic triterpenoid with anti-inflammatory properties.
Catalytic Activity: (S)-2,3-epoxysqualene = beta-amyrin
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 5.4.99.39
Seque... |
A0A067FT93 | SDR_CITSI | MNGPSSAAPFKRLEGKVAIITGGASGIGAMAVELFHENGAKVVIADVQDKLGEDLADKLGQDVCYIHCDISNEDEVINLVDTAVSKFGKLDIMYNNAGILDRSFGSILDTPKSDLERLINVNTIGGFLGAKHAARVMVPQQKGCILFTASACTEIAGLGSPAYTISKYGILGLVKCLAAELGQYGIRVNCVSPYGLATGMSMKGGVDPALIESSMSQMGNLKGEFLKTDGIANAALYLASDESSYVSGQNLVVDGGFSVVNPTVMRAYGLIK | 1.1.1.- | null | terpenoid biosynthetic process [GO:0016114] | null | oxidoreductase activity [GO:0016491] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=21-O-acetyl-isomeliandiol + A = (21S)-21-acetoxyl-apo-melianone + AH2; Xref=Rhea:RHEA:80307, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:231455, ChEBI:CHEBI:231456; Evidence={ECO:0000269|PubMed:36701471}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:80308; Evidence={ECO:000026... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:36701471}. | null | null | FUNCTION: Oxidoreductase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus (PubMed:36701471). Catalyzes the oxidation of 21-O-acetyl-isomeliandiol to (21S)-21-acetoxyl-apo-melianone (PubMed:36701471). {... | Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis) | [
2207,
8506,
10628,
14539,
16354,
23685
] | [
"go_bp: terpenoid biosynthetic process (GO:0016114)",
"go_mf: oxidoreductase activity (GO:0016491)",
"interpro: Short-chain dehydrogenase/reductase SDR (IPR002347)",
"interpro: Short-chain dehydrogenase/reductase, conserved site (IPR020904)",
"interpro: NAD(P)-binding domain superfamily (IPR036291)",
"pfa... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000318",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam"
] | Function: Oxidoreductase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus. Catalyzes the oxidation of 21-O-acetyl-isomeliandiol to (21S)-21-acetoxyl-apo-melianone.
Catalytic Activity: 21-O-acetyl-isome... |
A0A067GFT7 | C1CD1_CITSI | MEQQFDYFTVTSLLVFLTFLLRLVWGWKKSSDKIKIRLPPGPSKLPIIGSLHHLIGLDVDLPYYALTDLANKYGPLMHLQLGKMSLVVASSAKMFKELMKENDLAISQRPVPYVARVLEDAGRDIAFVPYGDYWRQIRKISRMELFSVKKVQSLHYIREDQSSKLVESIRGHAGTVMNLSKAVSDYTSTVVARAAFGSGCKDQDKFIRLSLEMVAAAGAVSTLPDMFPALGFIPILSGKKAFLKSIQTEADKILDVIIDEHIQKTKSNEYDGKESDKEDIVDVLLRLEKSGELEIPITTQDIKAVIWSVFAGGTDTSSTT... | 1.14.14.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | terpenoid biosynthetic process [GO:0016114] | 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=tirucalla-7,24-dien-3beta-ol + 2 reduced [NADPH--hemoprotein reductase] + 2 O2 = dihydroniloticin + 2 oxidized [NADPH--hemoprotein reductase] + 2 H2O + 2 H(+); Xref=Rhea:RHEA:80279, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CH... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:31371503}. | null | null | FUNCTION: Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus (PubMed:31371503). Catalyzes the conversion of tirucalladienol to dihydroniloticin (PubMed:31371503). {ECO:0000269|PubMed:313715... | Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis) | [
2207,
6727,
7856,
8157,
8525,
8657,
10002,
10647,
13954,
16401,
19936,
20574,
24930,
25105
] | [
"go_bp: terpenoid biosynthetic process (GO:0016114)",
"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: h... | [
"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",
"UniProtKB=ECO:0000250",
"InterPro=match:Pfam",
"Uni... | Function: Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus. Catalyzes the conversion of tirucalladienol to dihydroniloticin.
Catalytic Activity: tirucalla-7,24-dien-3beta-ol + 2 reduced [... |
A0A067MTM1 | TAS1_BOTB1 | MALFHNLEPKRSIDFMSGARTSSGSPSVSYSNSLPSPHTALVAPLSKMQRALWFDYISAPESTMYNLTLKFKLDQESEEYDGSISAILRAIDFLTKRHGMLRSTFHNSSNPSQPPYFAEIDSRHAHPTTHIVSSSEQLKRAALRGFDLSVDGPIRWIVFTNVKSNELYAVAHHIAVDGSSMSQLSKEIITLLTHYKHQSAEMLAPTTTSNYGLYCLAQDSYTHQESYKKALHFWSSQIAGTLPMEWNSSMLRTNPARLTQTTSQLDHRVCSTWLSLTPQELKAWGNLYKTSWFRVATALIGLLCAKHSKHKFRTDQSLLV... | 6.3.2.50 | 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]; fatty acid biosynthetic process [GO:0006633]; secondary metabolite biosynthetic process [GO:0044550] | cytoplasm [GO:0005737] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; phosphopantetheine binding [GO:0031177] | PF00501;PF00668;PF00109;PF02801;PF00550; | 3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.50.12780;3.30.559.30; | NRP synthetase family | null | null | CATALYTIC ACTIVITY: Reaction=acetoacetyl-CoA + L-isoleucine + ATP = tenuazonic acid + AMP + diphosphate + CoA + 2 H(+); Xref=Rhea:RHEA:52800, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:58045, ChEBI:CHEBI:136842, ChEBI:CHEBI:456215; EC=6.3.2.50; Evidence={E... | null | null | null | null | FUNCTION: Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal ... | Botryobasidium botryosum (strain FD-172 SS1) | [
1065,
3796,
6538,
7782,
9863,
10062,
12505,
12563,
13346,
13347,
13632,
14070,
14491,
14511,
14513,
14804,
16550,
17485,
18019,
19938,
20613,
20939,
20970,
21063,
22030
] | [
"go_bp: fatty acid biosynthetic process (GO:0006633)",
"go_bp: secondary metabolite biosynthetic process (GO:0044550)",
"go_cc: cytoplasm (GO:0005737)",
"go_mf: 3-oxoacyl-[acyl-carrier-protein] synthase activity (GO:0004315)",
"interpro: AMP-dependent synthetase/ligase domain (IPR000873)",
"interpro: Cond... | [
"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: Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal ... |
A0A067N4H9 | VMH2_PLEO1 | MFSRVMFCTFLILPLLAAATAIPRTDTPSCSTGSLQCCSSVQKASDPLVGIIVALLGIVLGPLDLNVGLTCSPITVIGVGGTSCTQQTVCCTGNNFDGLIVAGCSPINIGL | null | null | null | extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12147487}. Secreted, cell wall {ECO:0000269|PubMed:12147487}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6485,
6677,
8086,
10123,
21392,
24858,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"pfam: Hydrophobin (PF01185)",
"subcellular_location: Cell wall (SL-0041)",
"subcellular_location: Secreted (SL... | [
"UniProtKB-GO=ECO:0000269",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000269",
"UniProtKB=ECO:0000269"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067N4P3 | HYD12_PLEO1 | MFSKATLFFTAAVVIVAAGATPTTSQCNTGPVQCCDHTQQASGPTTLTGIGEVDLGDTSTLIAYGNCSPVLPVLGGPKCQGQTVCCDNTEFEGLVNVGCTNVAV | null | null | null | fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33636611}. Secreted, cell wall {ECO:0000305|PubMed:33636611}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6677,
8086,
10123,
21392,
24858,
24983
] | [
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"pfam: Hydrophobin (PF01185)",
"subcellular_location: Cell wall (SL-0041)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305",
"UniProtKB=ECO:0000305"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067N4P7 | HYD9_PLEO1 | MFFFNTKPIVFLVVLSVVATFAAATPAMLARGGGSSCAPSTSLKCCDHVGTFSEVSPYINPLELVGVIAALLGLVGGLFTSVTLALTCSGIDIGGSCNSQTVCCENVVFNGLVNVGCTAIDIL | null | null | null | fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33636611}. Secreted, cell wall {ECO:0000305|PubMed:33636611}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6677,
8086,
10123,
21392,
24858,
24983
] | [
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"pfam: Hydrophobin (PF01185)",
"subcellular_location: Cell wall (SL-0041)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305",
"UniProtKB=ECO:0000305"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067N582 | HYD5_PLEO1 | MFNKQTNAIVLLFTFALFATLAVATPTIVARTGGSGSSCPTTDIKCCSHVGTFSEVQGYIDDDTKVKLIPALLGLLGATIDVVLGVVLGVTCSSISVGSSCSATTVCCENVVFNGLINVGCTAIDIL | null | null | null | fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33636611}. Secreted, cell wall {ECO:0000305|PubMed:33636611}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6677,
8086,
10123,
14338,
21392,
24858,
24983
] | [
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"interpro: Class I Hydrophobin, conserved site (IPR019778)",
"pfam: Hydrophobin (PF01185)",
"subcellular_location: Cell wall (SL-0041)",
"subcellular_locat... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305",
"UniProtKB=ECO:0000305"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067N648 | VMH3_PLEO1 | MFFQTTIVAALASLAVATPLALRTDSRCNTESVKCCNKSEDAETFKKSASAALIPIKIGDITGEVYSECSPIVGLIGGSSCSAQTVCCDNAKFNGLVNIGCTPINVAL | null | null | null | extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:35452811}. Secreted, cell wall {ECO:0000269|PubMed:35452811}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6485,
6677,
8086,
10123,
14338,
21392,
24858,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"interpro: Class I Hydrophobin, conserved site (IPR019778)",
"pfam: Hydrophobin (PF01185)",
"subcellular_locati... | [
"UniProtKB-GO=ECO:0000269",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000269",
"UniProtKB=ECO:0000269"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067N7P3 | HYD20_PLEO1 | MLSHPMKLLFFVFALSALLAAATPVVEVRDYQQFSRVSLINFISFNKARGGDLCANGKKTMCCGELKTFDKNILGLLDGLLTTVVGLAGEILKPTGLVGLECVPITLLGNGGLSDVCKANGVCCKDLTLRAAINVGCVPINIL | null | null | null | fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33636611}. Secreted, cell wall {ECO:0000305|PubMed:33636611}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6677,
8086,
10123,
21392,
24858,
24983
] | [
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"pfam: Hydrophobin (PF01185)",
"subcellular_location: Cell wall (SL-0041)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305",
"UniProtKB=ECO:0000305"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067NEJ5 | HYD18_PLEO1 | MFTEQVLNVIILLQTATVTATAIPASGCNAGDVQCCKSVQKADSAGGAALLGLVGIVLSNLDVFIGGDCSPITAIGVGGTSCSSQAVCCENNSFNGLIALGCVPINLSL | null | null | null | fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33636611}. Secreted, cell wall {ECO:0000305|PubMed:33636611}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6677,
8086,
10123,
21392,
24858,
24983
] | [
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"pfam: Hydrophobin (PF01185)",
"subcellular_location: Cell wall (SL-0041)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305",
"UniProtKB=ECO:0000305"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067NFU6 | HYD8_PLEO1 | MMFSKPVVLATTALATFAAATPLVARTEPTCSSTEIKCCENVGTAAVVSSVLTPILVSIPLVGPLLSLLGLNAVVALLFGTVDVVLGLTCSGIDVGGSCNAQTVCCENVQFNGLINVGCVAIDIL | null | null | null | fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33636611}. Secreted, cell wall {ECO:0000305|PubMed:33636611}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6677,
8086,
10123,
21392,
24858,
24983
] | [
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"pfam: Hydrophobin (PF01185)",
"subcellular_location: Cell wall (SL-0041)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305",
"UniProtKB=ECO:0000305"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067NGV3 | FBH1_PLEO1 | MFSIRIATVVLAASALLAAASPITNTETPVNQCGSGSIQCCESVQSASAAQAAGILGPLDILTNLQGLVASHCSPLAAVGVSGTSCSSQTVCCKDVSKSGLVNLGCSPINLNL | null | null | null | fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33636611}. Secreted, cell wall {ECO:0000305|PubMed:33636611}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6677,
8086,
10123,
21392,
24858,
24983
] | [
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"pfam: Hydrophobin (PF01185)",
"subcellular_location: Cell wall (SL-0041)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305",
"UniProtKB=ECO:0000305"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067NHE1 | HYD17_PLEO1 | MYSQSMVLLAAAFASFVAASPMALHGANSCSTGPVHCCNSVEHHTQPHANSLARGSGLVGLDIETLVGNIGLDCSPIGLSSTDCTAQTVCCDDVTFDGKVAVGCTPVNLSVL | null | null | null | fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33636611}. Secreted, cell wall {ECO:0000305|PubMed:33636611}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6677,
8086,
10123,
21392,
24858,
24983
] | [
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"pfam: Hydrophobin (PF01185)",
"subcellular_location: Cell wall (SL-0041)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305",
"UniProtKB=ECO:0000305"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067NHW8 | HYD15_PLEO1 | MFAKSATIAIVLAALAGFSAAVPTADCRTSKTCSSGKVALVAPAAPVGSCSTGKVQCCNSVEHSTQPHVNNLLLGLEHFGLVKGLIGGLTGNVGIQCSPLLLSGNSCTAQTACCENVHFNGLIAVGCSPVNLSLL | null | null | null | fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33636611}. Secreted, cell wall {ECO:0000305|PubMed:33636611}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6677,
8086,
10123,
14338,
21392,
24858,
24983
] | [
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"interpro: Class I Hydrophobin, conserved site (IPR019778)",
"pfam: Hydrophobin (PF01185)",
"subcellular_location: Cell wall (SL-0041)",
"subcellular_locat... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305",
"UniProtKB=ECO:0000305"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067NMT6 | HYD21_PLEO1 | MFAAPATMLVLAALAALSSAIPAAQTASKCSTGPVQCCDSVEHHTQPHVNNLLLGLEHFGLVKGLVGGLTGNVGIKCNPILLSSNDCTAQSVCCEHVHFKGNIAVGCTPANIDIL | null | null | null | fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33636611}. Secreted, cell wall {ECO:0000305|PubMed:33636611}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6677,
8086,
10123,
21392,
24858,
24983
] | [
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"pfam: Hydrophobin (PF01185)",
"subcellular_location: Cell wall (SL-0041)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305",
"UniProtKB=ECO:0000305"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067NN74 | HYD10_PLEO1 | MLFNTFVVTALASLAAATPTRRNEPAAGSCSTGELQCCKSVQSADSKSLTSLFGLLGLVVGDITGLVGVTCSPVTVVGAGGAQCNAQAVCCNDNSFNGLIALGCTPINLNL | null | null | null | fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33636611}. Secreted, cell wall {ECO:0000305|PubMed:33636611}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6677,
8086,
10123,
21392,
24858,
24983
] | [
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"pfam: Hydrophobin (PF01185)",
"subcellular_location: Cell wall (SL-0041)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305",
"UniProtKB=ECO:0000305"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067NRJ8 | HYD19_PLEO1 | MILLAFSGELFKRINTSPIVHVERRTNPTTTVTVTTKPSPTPISPNQCNTNKIQCCNSVQSSDAPLLTGLLGLLGIVLQGVIPIGVTCSPISVIGIGGNSCSAQTVCCENNTFNGVIAIGCTPINIDL | null | null | null | fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33636611}. Secreted, cell wall {ECO:0000305|PubMed:33636611}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6677,
8086,
10123,
14338,
21392,
24858,
24983
] | [
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"interpro: Class I Hydrophobin, conserved site (IPR019778)",
"pfam: Hydrophobin (PF01185)",
"subcellular_location: Cell wall (SL-0041)",
"subcellular_locat... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305",
"UniProtKB=ECO:0000305"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067NRQ5 | HYD14_PLEO1 | MFSNAAAFSTVALATYAAATPAVVARTEPHPSSSNCGTTTIECCKDVGTATSLESPLKSAFIQHGLVSSLLVALGVVKVVDVVLGVVVDPNVVLGLTCSTVAVGGSCNAQQVCCENVAFNGLVNVGCTAIDIL | null | null | null | fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33636611}. Secreted, cell wall {ECO:0000305|PubMed:33636611}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6677,
8086,
10123,
21392,
24858,
24983
] | [
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"pfam: Hydrophobin (PF01185)",
"subcellular_location: Cell wall (SL-0041)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305",
"UniProtKB=ECO:0000305"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067P0I9 | HYD11_PLEO1 | MRLTPLLAALALPLLTVLATPLTPVGEAEVVEVDVAPRQISLNPASSCPKGQLWCCVSLDLVSNSLIAGLLVTLGILDPTGINTAGVQCTPLSWPFQMSCGNKDLCCDPDLPVVGLLLKLNCRSVNPLL | null | null | null | fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33636611}. Secreted, cell wall {ECO:0000305|PubMed:33636611}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6677,
8086,
10123,
21392,
24858,
24983
] | [
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"pfam: Hydrophobin (PF01185)",
"subcellular_location: Cell wall (SL-0041)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305",
"UniProtKB=ECO:0000305"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067P1E6 | HYD7_PLEO1 | MFAQSFIITALAALAVASPLQVRTSDKCNTGTVHCCNSMKKSDSADISKIASLLQLDVKGVVGDVGLQCSPLVSLVGGGSKCSGQTVCCDQTKFNGLVNIGCSPINVGL | null | null | null | fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33636611}. Secreted, cell wall {ECO:0000305|PubMed:33636611}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6677,
8086,
10123,
14338,
21392,
24858,
24983
] | [
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"interpro: Class I Hydrophobin, conserved site (IPR019778)",
"pfam: Hydrophobin (PF01185)",
"subcellular_location: Cell wall (SL-0041)",
"subcellular_locat... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305",
"UniProtKB=ECO:0000305"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067P1K6 | VMH1_PLEO1 | MLFKQAILVATTLTTLAVATPVVDVRRRTDPASSCSTGTLNCCNSSGTVEDKTIAGLLGILNIVVSDITALVGITCTPITVVGAGGTSCTSQTLCCDNNNFSGLITLGCIPININL | null | null | null | extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12147487}. Secreted, cell wall {ECO:0000269|PubMed:12147487}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6485,
6677,
8086,
10123,
21392,
24858,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"pfam: Hydrophobin (PF01185)",
"subcellular_location: Cell wall (SL-0041)",
"subcellular_location: Secreted (SL... | [
"UniProtKB-GO=ECO:0000269",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000269",
"UniProtKB=ECO:0000269"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067P494 | HYD13_PLEO1 | PTKMTRRTEPASSCSTGSLDCCNSSGDATDTSITTLLAGIGLPIGSVTGLVGVTCSPITGIGLGGSGCSSEALCCSNNSFKGLVALGCVPVDLSL | null | null | null | fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33636611}. Secreted, cell wall {ECO:0000305|PubMed:33636611}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6677,
8086,
10123,
21392,
24858,
24983
] | [
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"pfam: Hydrophobin (PF01185)",
"subcellular_location: Cell wall (SL-0041)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305",
"UniProtKB=ECO:0000305"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067P943 | HYD16_PLEO1 | MKFTSVIALVATAATLVGAVPFETNAERLARGLPPLPPARRASGVEAAKPKPSPSHGCSTGPVQCCNDLVDRSNHTVGILIGLLGIVLGPVTGLFGLGCSPLLGGGAKCQSQTVCCSDNKFSGIINIGCSPINIGL | null | null | null | fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33636611}. Secreted, cell wall {ECO:0000305|PubMed:33636611}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6677,
8086,
10123,
21392,
24858,
24983
] | [
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"pfam: Hydrophobin (PF01185)",
"subcellular_location: Cell wall (SL-0041)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305",
"UniProtKB=ECO:0000305"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067PCX8 | HYD6_PLEO1 | MLFKQLILVATALTTLAVATPAVMRRTEPASSCSTGPVNCCNSSGTAKDGNIAKELALLGIVVPDINALIGVSCSPITVIGAGGASCSSQTLCCEDNKYNGIVALGCIPVDISL | null | null | null | fungal-type cell wall [GO:0009277] | structural constituent of cell wall [GO:0005199] | PF01185; | null | Fungal hydrophobin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33636611}. Secreted, cell wall {ECO:0000305|PubMed:33636611}. | null | null | null | null | null | FUNCTION: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... | Pleurotus ostreatus (strain PC15) (Oyster mushroom) | [
6677,
8086,
10123,
14338,
21392,
24858,
24983
] | [
"go_cc: fungal-type cell wall (GO:0009277)",
"go_mf: structural constituent of cell wall (GO:0005199)",
"interpro: Class I Hydrophobin (IPR001338)",
"interpro: Class I Hydrophobin, conserved site (IPR019778)",
"pfam: Hydrophobin (PF01185)",
"subcellular_location: Cell wall (SL-0041)",
"subcellular_locat... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305",
"UniProtKB=ECO:0000305"
] | Function: Aerial growth, conidiation, and dispersal of filamentous fungi in the environment depend on their ability to secrete small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellula... |
A0A067SEC9 | TERS_GALM3 | MNTTTRTFYLPRLEDTFSVFPDNGLNPHYAECRIQSQAWIDKYYKIVCGPKMRAYMDHCKFELITAYTYPYASSDGLRKTMDLANILWLYDEFTDTLSGKDATNAAAIVIRTLRERDFDDGSWICHMMRDFYAAHIEKFGPNVSRRFIDHFCQYVEGTGTEAKHREKDHVLDINAYIIMRRAASAVLTAFDLAEYCLGIDLPQYVHDDPAFISGYNAGLDLVFLDNDLFSYDMEQAKGHCTTNIITVVMKSKRIDLQSAFDFTAGYCESLTQQLIAAQISLASRTDPVFSNNAVKCLEAIANWVKGSDGWSFATERYFGK... | 4.2.3.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:32233445}; | null | null | terpene synthase activity [GO:0010333] | PF19086; | 1.10.600.10; | Terpene synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = beta-gurjunene + diphosphate; Xref=Rhea:RHEA:83287, ChEBI:CHEBI:33019, ChEBI:CHEBI:80940, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:32233445}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83288; Evidence={ECO:0000305|PubMed:32233445}; | null | null | null | null | FUNCTION: Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to beta-gurjunene. {ECO:0000269|PubMed:32233445}. | Galerina marginata (strain CBS 339.88) | [
8365,
12429,
16042,
19924
] | [
"go_mf: terpene synthase activity (GO:0010333)",
"interpro: Isoprenoid synthase domain superfamily (IPR008949)",
"interpro: Terpene cyclase-like 2 (IPR034686)",
"cofactor: Mg(2+) (CHEBI:18420)"
] | [
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000269"
] | Function: Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to beta-gurjunene.
Catalytic Activity: (2E,6E)-farnesyl diphosphate = beta-gurjunene + diphosphate
Cofactor: Mg(2+)
Domain: The DDXXD motif is important for the catalytic activity, presumably through binding to Mg(2+).
EC: 4.2.3.-
Se... |
A0A067SLB9 | AAMA1_GALM3 | MFDTNATRLPIWGIGCNPWTAEHVDQTLASGNDIC | null | null | null | null | null | PF24112; | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic bicyclic octapeptide (PubMed:29051530). POPB first removes 10 residues from the N-terminus (PubMed:29051530). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization ... | 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:22202811, PubMed:7642577, PubMed:8702941). {ECO:0000269|PubMed:7642577, ECO:0000269|PubMed:8702941, ECO:00003... | Galerina marginata (strain CBS 339.88) | [] | [] | [] | 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 bicyclic octapeptide. POPB first removes 1... |
A0A067XG71 | LECA_CANGR | ADTIVAVELDTYPNTDIGDPNYPHIGIDIKSIRSKKIAKWNMQDGKVATAHIIYNSVGKRLSAVVSYPNADSATVSYDVDLDNVLPEWVRVGLSATTGLYKETNTILSWSFTSKLKSNSTAETNALHFTFNQFTKDQKDLILQGDATTDSDGNLQLTRVSSDGTPQGNSVGRALFYAPVHIWESSAVVASFDATFTFLIKSPDSDPADGITFFISNMDSTIPSGSGGRLLGLFPDAN | null | null | null | null | carbohydrate binding [GO:0030246] | PF00139; | 2.60.120.200; | Leguminous lectin family | PTM: Concanavalin A-like lectins of the Diocleinae subtribe undergo proteolytic processing referred to as circular permutation. The propeptide is split into an N-terminal and a C-terminal part, the gamma and beta chain, respectively. These are then religated in beta-gamma order to form the mature alpha chain. The beta ... | null | null | null | null | null | null | FUNCTION: Lectin (PubMed:24361256). Induces paw edema in mice (PubMed:22368061). Has a weak vasorelaxant effect on rat aorta (PubMed:24361256). Has anti-inflammatory and anti-nociceptive effects (PubMed:19153712). {ECO:0000269|PubMed:19153712, ECO:0000269|PubMed:22368061, ECO:0000269|PubMed:24361256}. | Canavalia grandiflora (Jackbean) | [
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: Lectin. Induces paw edema in mice. Has a weak vasorelaxant effect on rat aorta. Has anti-inflammatory and anti-nociceptive effects.
PTM: Concanavalin A-like lectins of the Diocleinae subtribe undergo proteolytic processing referred to as circular permutation. The propeptide is split into an N-terminal and a C... |
A0A067XGX8 | AROG2_PETHY | MALTATATTRGGSALPNSCLQTPKFQSLQKPTFISSFPTNKKTKPRTKHISAVQSPPSTTKWNLESWKTKPAFQLPDYPDKVELESVLKTLSTYPPIVFAGEARNLEEKLGEAALGNAFLLQGGDCAESFKEFSANNIRDTFRVMLQMGVVLMFGGQMPVIKVGRMAGQFAKPRSDPFEEKDGVKLPSYRGDNVNGDAFDEKSRIPDPHRMVRAYTQSVATLNLLRAFASGGYAAMQRVNQWNLDFTDQSEQGDRYRELAHRVDEAMGFMTAAGLTVDHTIMTTTDFWTSHECLLLPYEQALTREDSTSGLYYDCSAHMI... | 2.5.1.54 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O53512}; Note=Binds 1 divalent metal cation per subunit that could be manganese. {ECO:0000250|UniProtKB:O53512}; | aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423] | chloroplast [GO:0009507] | 3-deoxy-7-phosphoheptulonate synthase activity [GO:0003849] | PF01474; | 3.20.20.70; | Class-II DAHP synthase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:24815009}. | CATALYTIC ACTIVITY: Reaction=D-erythrose 4-phosphate + phosphoenolpyruvate + H2O = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate; Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54; Evidence={ECO:0000250|UniProtKB:O53512}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7. {ECO:0000250|UniProtKB:O53512}. | null | null | FUNCTION: Involved in the production of volatile organic compounds (VOCs) (PubMed:24815009). Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate (By similarity). {ECO:000... | Petunia hybrida (Petunia) | [
1575,
1634,
6685,
7637,
13257,
19930,
24864,
24966
] | [
"go_bp: aromatic amino acid biosynthetic process (GO:0009073)",
"go_bp: chorismate biosynthetic process (GO:0009423)",
"go_cc: chloroplast (GO:0009507)",
"go_mf: 3-deoxy-7-phosphoheptulonate synthase activity (GO:0003849)",
"interpro: Aldolase-type TIM barrel (IPR013785)",
"cofactor: Mn(2+) (CHEBI:29035)"... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000250",
"InterPro=match",
"UniProtKB=ECO:0000250",
"UniProtKB=ECO:0000269",
"UniProtKB=ECO:0000269"
] | Function: Involved in the production of volatile organic compounds (VOCs). Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate (By similarity).
Catalytic Activity: D-eryt... |
A0A067XH53 | AROG1_PETHY | MALSTNSTTSSLLPKTPLVQQPLLKNASLPTTTKAIRFIQPISAIHSSDSSKNTPIVSAKPSSPPAATSTAAATAVTKQEWSIDSWKTKKALQLPEYPNQEELKNVLKTIEDFPPIVFAGEARHLEEKLGEAAMGRAFLLQGGDCAESFKEFNANNIRDTFRILLQMGAVLMFGGQMPVIKVGRMAGQFAKPRSDNFEEKNGVKLPSYRGDNVNGDAFDLKSRTPDPQRLIRAYCQSAATLNLLRAFATGGYAAMQRVTQWNLDFTEHSEQGDRYRELANRVDEALGFMNAAGLTTDHPIMTTTEFWTSHECLLLPYEQS... | 2.5.1.54 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O53512}; Note=Binds 1 divalent metal cation per subunit that could be manganese. {ECO:0000250|UniProtKB:O53512}; | aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; green leaf volatile biosynthetic process [GO:0010597] | chloroplast [GO:0009507] | 3-deoxy-7-phosphoheptulonate synthase activity [GO:0003849] | PF01474; | 3.20.20.70; | Class-II DAHP synthase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:24815009}. | CATALYTIC ACTIVITY: Reaction=D-erythrose 4-phosphate + phosphoenolpyruvate + H2O = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate; Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54; Evidence={ECO:0000250|UniProtKB:O53512}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7. {ECO:0000250|UniProtKB:O53512}. | null | null | FUNCTION: Involved in the production of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26), scent attracting pollinators (e.g. the night-active hawkmoth pollinator Manduca sexta) (PubMed:24815009). Catalyz... | Petunia hybrida (Petunia) | [
1575,
1634,
1966,
6685,
7637,
13257,
19930,
24864,
24966
] | [
"go_bp: aromatic amino acid biosynthetic process (GO:0009073)",
"go_bp: chorismate biosynthetic process (GO:0009423)",
"go_bp: green leaf volatile biosynthetic process (GO:0010597)",
"go_cc: chloroplast (GO:0009507)",
"go_mf: 3-deoxy-7-phosphoheptulonate synthase activity (GO:0003849)",
"interpro: Aldolas... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000315",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000250",
"InterPro=match",
"UniProtKB=ECO:0000250",
"UniProtKB=ECO:0000269",
"UniProtKB=ECO:0000269"
] | Function: Involved in the production of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26), scent attracting pollinators (e.g. the night-active hawkmoth pollinator Manduca sexta). Catalyzes an aldol-like c... |
A0A067XMK8 | PTAJ_PESFW | MAASTAAQVQLSEEALGLARIFENPKGSLEAASKLLQKNHDEFHVFWRDVGGHNHIPHSVLSILALGGGPAELQRAWDDGVAIQRPTPPLDEDVVKKLENPAEFRARIGSIPNYTNFLHFFRNQMDKKGWQAVVSEYAFSRTPLAETIFAQLFEGAYHPFIHIGFGIEFNLPSIIAEGLAQAATHDSAGIEGFFLEAERQAAQSKGPGKSLVQLLDEVRTTEKIKTAARLPDGPVRVRDGVIGRAGAEIAALASQFRVPADQLSRGAAESINISAYTAGAAQRAGKARKIDFFHMHNTTSSLFLTVFLNQPWISTEDKVR... | 1.-.-.- | COFACTOR: Name=NADPH; Xref=ChEBI:CHEBI:57783; Evidence={ECO:0000250|UniProtKB:Q0CCX5}; | null | null | oxidoreductase activity [GO:0016491] | PF14027; | null | Questin oxidase family | null | null | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:24302702}. | null | null | FUNCTION: Baeyer-Villiger oxidase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes (PubMed:24302702). The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS... | Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) | [
8506,
19944
] | [
"go_mf: oxidoreductase activity (GO:0016491)",
"cofactor: NADPH (CHEBI:57783)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000250"
] | Function: Baeyer-Villiger oxidase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes. The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA. As the ptaA... |
A0A067XML2 | PTAD_PESFW | MAEMSKNPASTLKPSRYLCLTICGYRKPGMSEEDYRYHMTQVSAPMTKDLMAKYGVKRWTMNYMIRRWPSCPTLTASAKLCLRTLEDYKRMKQDPWYKEHLIGDHEKFADTKRSKMTIGWIEEWISDGKPVDGLEFKS | 1.-.-.- | null | null | null | oxidoreductase activity [GO:0016491] | PF07110; | 3.30.70.100; | TpcK family | null | null | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:24302702}. | null | null | FUNCTION: Probable decarboxylase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes (PubMed:24302702). The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ... | Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) | [
8506,
12688
] | [
"go_mf: oxidoreductase activity (GO:0016491)",
"interpro: Dimeric alpha-beta barrel (IPR011008)"
] | [
"UniProtKB-GO=ECO:0000501",
"InterPro=match"
] | Function: Probable decarboxylase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes. The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA. As the ptaA ... |
A0A067XMN9 | PTAR2_PESFW | MEAADPNNNLTITSPSTLLSNPTQPPAQPLKLRDSCHACASSKVKCHKEKPTCSRCRKRGITCEYFAHRRPGRKQENRAKDTTNHVERQENTTAVEMLDLNWPAPDFSTQTSIANDNLDVFHDIFVPPDQLNNGLTDFTIDFDDFDIQSDPAEIASLPDTSSLESMFVTSPTAPTDTITPNVITPNVGLSVLEGLPDTTHHTQAINLASYIQTPPTEKTPDSRIKHLEENKDPCMTRALSFLTQLSESTSRICKTSETGCSGTNKKSLPESLDGIIAENRRLLEAMSNILQCRCSEDDDLLCIQAIVASKILNLYASAIE... | null | null | aflatoxin biosynthetic process [GO:0045122] | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; zinc ion binding [GO:0008270] | PF08493;PF00172; | 4.10.240.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}. | null | null | null | null | null | FUNCTION: Transcription factor that, with ptaR1 and ptaR3, coregulates the expression of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes (PubMed:24302702). {ECO:0000305|PubMed:24302702}. | Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) | [
3851,
6494,
7541,
7591,
8242,
10010,
16601,
20671,
24954
] | [
"go_bp: aflatoxin biosynthetic process (GO:0045122)",
"go_cc: nucleus (GO:0005634)",
"go_mf: DNA-binding transcription factor activity, RNA polymerase II-specific (GO:0000981)",
"go_mf: DNA binding (GO:0003677)",
"go_mf: zinc ion binding (GO:0008270)",
"interpro: Zn(2)Cys(6) fungal-type DNA-binding domain... | [
"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:Pfam",
"UniProtKB=ECO:0000255"
] | Function: Transcription factor that, with ptaR1 and ptaR3, coregulates the expression of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes.
Subcellular Location: Nucleus
Sequence Mass (Da): 48761
Sequence Length: 444 |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.