entry created 2018-12-05 dataset Swiss-Prot modified 2023-02-22 version 64 accession Q9AXK2 name P102C_LUPLU protein recommendedName fullName evidence 3 Class-10-plant-pathogenesis-related-protein-2C shortName evidence 3 Llpr10.2c shortName evidence 3 Ypr-10.2c ecNumber evidence 1 3.1.27.- allergenName evidence 4 Lup-l-4 gene name evidence 3 type primary PR10.2C organism name type scientific Lupinus-luteus name type common European-yellow-lupine dbReference id 3873 type NCBI-Taxonomy lineage taxon Eukaryota taxon Viridiplantae taxon Streptophyta taxon Embryophyta taxon Tracheophyta taxon Spermatophyta taxon Magnoliopsida taxon eudicotyledons taxon Gunneridae taxon Pentapetalae taxon rosids taxon fabids taxon Fabales taxon Fabaceae taxon Papilionoideae taxon 50-kb-inversion-clade taxon genistoids-sensu-lato taxon core-genistoids taxon Genisteae taxon Lupinus reference key 1 citation date 2000-11 db EMBL/GenBank/DDBJ-databases type submission title Structure-of-Lupinus-luteus-cDNA-encoding-PR10.2C-protein. authorList person name Handschuh-L.A. person name Sikorski-M.M. scope NUCLEOTIDE-SEQUENCE-[MRNA] source strain cv.-Ventus tissue Root comment type function text evidence 1-2 Class-II-ribonuclease-(RNase)-(By-similarity).-Binds-to-cytokinins-(By-similarity).-Interacts-with-melatonin-(By-similarity). comment type subcellular-location subcellularLocation location evidence 2 Cytoplasm location evidence 2 Cytosol comment type allergen text evidence 4 Causes-an-allergic-reaction-in-human. comment type similarity text evidence 4 Belongs-to-the-BetVI-family. dbReference evidence 1 id 3.1.27.- type EC dbReference id AF322225 type EMBL property type protein-sequence-ID value AAK09428.1 property type molecule-type value mRNA dbReference id Q9AXK2 type AlphaFoldDB dbReference id Q9AXK2 type SMR dbReference id 9727 type Allergome property type allergen-name value Lup-l-4 dbReference id GO:0005829 type GO property type term value C:cytosol property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0010427 type GO property type term value F:abscisic-acid-binding property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0005509 type GO property type term value F:calcium-ion-binding property type evidence value ECO:0000250 property type project value UniProtKB dbReference id GO:0044373 type GO property type term value F:cytokinin-binding property type evidence value ECO:0000250 property type project value UniProtKB dbReference id GO:1904408 type GO property type term value F:melatonin-binding property type evidence value ECO:0000250 property type project value UniProtKB dbReference id GO:0004864 type GO property type term value F:protein-phosphatase-inhibitor-activity property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0004540 type GO property type term value F:ribonuclease-activity property type evidence value ECO:0000250 property type project value UniProtKB dbReference id GO:0038023 type GO property type term value F:signaling-receptor-activity property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0009738 type GO property type term value P:abscisic-acid-activated-signaling-pathway property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0006952 type GO property type term value P:defense-response property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0009607 type GO property type term value P:response-to-biotic-stimulus property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0090501 type GO property type term value P:RNA-phosphodiester-bond-hydrolysis property type evidence value ECO:0000250 property type project value UniProtKB dbReference id cd07816 type CDD property type entry-name value Bet_v1-like property type match-status value 1 dbReference id 3.30.530.20 type Gene3D property type match-status value 1 dbReference id IPR000916 type InterPro property type entry-name value Bet_v_I/MLP dbReference id IPR024949 type InterPro property type entry-name value Bet_v_I_allergen dbReference id IPR023393 type InterPro property type entry-name value START-like_dom_sf dbReference id PTHR31213 type PANTHER property type match-status value 1 dbReference id PTHR31213:SF55 type PANTHER property type entry-name value STRESS-INDUCED-PROTEIN-SAM22 property type match-status value 1 dbReference id PF00407 type Pfam property type entry-name value Bet_v_1 property type match-status value 1 dbReference id PR00634 type PRINTS property type entry-name value BETALLERGEN dbReference id SSF55961 type SUPFAM property type entry-name value Bet-v1-like property type match-status value 1 proteinExistence type evidence-at-transcript-level keyword id KW-0020 Allergen keyword id KW-0106 Calcium keyword id KW-0963 Cytoplasm keyword id KW-0378 Hydrolase keyword id KW-0479 Metal-binding keyword id KW-0540 Nuclease keyword id KW-0568 Pathogenesis-related-protein keyword id KW-0611 Plant-defense feature description Class-10-plant-pathogenesis-related-protein-2C id PRO_0000445931 type chain location begin position 1 end position 158 feature evidence 2 type binding-site location position position 8 ligand name trans-zeatin dbReference id CHEBI:16522 type ChEBI label 1 feature evidence 2 type binding-site location position position 32 ligand name Ca(2+) dbReference id CHEBI:29108 type ChEBI feature evidence 2 type binding-site location position position 35 ligand name Ca(2+) dbReference id CHEBI:29108 type ChEBI feature evidence 2 type binding-site location position position 38 ligand name Ca(2+) dbReference id CHEBI:29108 type ChEBI feature evidence 2 type binding-site location position position 60 ligand name trans-zeatin dbReference id CHEBI:16522 type ChEBI label 2 feature evidence 2 type binding-site location position position 69 ligand name trans-zeatin dbReference id CHEBI:16522 type ChEBI label 3 feature evidence 2 type binding-site location position position 81 ligand name trans-zeatin dbReference id CHEBI:16522 type ChEBI label 3 feature evidence 2 type binding-site location position position 83 ligand name trans-zeatin dbReference id CHEBI:16522 type ChEBI label 1 evidence key 1 type ECO:0000250 source dbReference id P52779 type UniProtKB evidence key 2 type ECO:0000250 source dbReference id Q9LLQ2 type UniProtKB evidence key 3 type ECO:0000303 source ref 1 evidence key 4 type ECO:0000305 sequence checksum 2F6A0BE4072439A0 length 158 mass 16812 modified 2001-06-01 version 1 MGVFTFQDESTSTIAPAKLYKALVTDADIIIPKAVETIQSVEIVEGNGGPGTIKKLTFIEGGESKYVLHKIEAIDEANLGYNYSIVGGVGLPDTIEKISFETKLVEGANGGSIGKVTIKIETKGDAQPNEEEGKAAKARGDAFFKAIESYLSAHPDYN 
entry created 2019-01-16 dataset Swiss-Prot modified 2023-02-22 version 37 accession K0KPV8 name EAT1_WICCI protein recommendedName fullName Ethanol-acetyltransferase-1 ecNumber 2.3.1.268 alternativeName fullName Acetyl-CoA-hydrolase ecNumber 3.1.2.1 alternativeName fullName Acetyl-CoA-thioesterase alternativeName fullName Alcohol-acetyltransferase shortName AAT alternativeName fullName Ethyl-acetate-esterase ecNumber 3.1.1.- gene name type primary EAT1 name type ORF BN7_4634 organism name type scientific Wickerhamomyces-ciferrii name type common Yeast name type synonym Pichia-ciferrii dbReference id 1041607 type NCBI-Taxonomy lineage taxon Eukaryota taxon Fungi taxon Dikarya taxon Ascomycota taxon Saccharomycotina taxon Saccharomycetes taxon Saccharomycetales taxon Phaffomycetaceae taxon Wickerhamomyces reference key 1 citation date 2012 first 1582 last 1583 name Eukaryot.-Cell type journal-article volume 11 title Draft-genome-sequence-of-Wickerhamomyces-ciferrii-NRRL-Y-1031-F-60-10. authorList person name Schneider-J. person name Andrea-H. person name Blom-J. person name Jaenicke-S. person name Rueckert-C. person name Schorsch-C. person name Szczepanowski-R. person name Farwick-M. person name Goesmann-A. person name Puehler-A. person name Schaffer-S. person name Tauch-A. person name Koehler-T. person name Brinkrolf-K. dbReference id 23193139 type PubMed dbReference id 10.1128/ec.00258-12 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain ATCC-14091-/-BCRC-22168-/-CBS-111-/-JCM-3599-/-NBRC-0793-/-NRRL-Y-1031-F-60-10 reference key 2 citation date 2017 first 92 last 101 name Metab.-Eng. type journal-article volume 41 title Ethyl-acetate-production-by-the-elusive-alcohol-acetyltransferase-from-yeast. authorList person name Kruis-A.J. person name Levisson-M. person name Mars-A.E. person name van-der-Ploeg-M. person name Garces-Daza-F. person name Ellena-V. person name Kengen-S.W.M. person name van-der-Oost-J. person name Weusthuis-R.A. dbReference id 28356220 type PubMed dbReference id 10.1016/j.ymben.2017.03.004 type DOI scope FUNCTION scope CATALYTIC-ACTIVITY source strain ATCC-14091-/-BCRC-22168-/-CBS-111-/-JCM-3599-/-NBRC-0793-/-NRRL-Y-1031-F-60-10 comment type function text evidence 1-4 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). comment type catalytic-activity reaction evidence 4 text acetyl-CoA-+-ethanol-=-CoA-+-ethyl-acetate dbReference id RHEA:55972 type Rhea dbReference id CHEBI:16236 type ChEBI dbReference id CHEBI:27750 type ChEBI dbReference id CHEBI:57287 type ChEBI dbReference id CHEBI:57288 type ChEBI dbReference id 2.3.1.268 type EC comment type catalytic-activity reaction evidence 1 text acetyl-CoA-+-H2O-=-acetate-+-CoA-+-H(+) dbReference id RHEA:20289 type Rhea dbReference id CHEBI:15377 type ChEBI dbReference id CHEBI:15378 type ChEBI dbReference id CHEBI:30089 type ChEBI dbReference id CHEBI:57287 type ChEBI dbReference id CHEBI:57288 type ChEBI dbReference id 3.1.2.1 type EC comment type catalytic-activity reaction evidence 1 text ethyl-acetate-+-H2O-=-acetate-+-ethanol-+-H(+) dbReference id RHEA:58148 type Rhea dbReference id CHEBI:15377 type ChEBI dbReference id CHEBI:15378 type ChEBI dbReference id CHEBI:16236 type ChEBI dbReference id CHEBI:27750 type ChEBI dbReference id CHEBI:30089 type ChEBI comment type subcellular-location subcellularLocation location evidence 1 Mitochondrion comment type similarity text evidence 5 Belongs-to-the-AB-hydrolase-superfamily. dbReference id 2.3.1.268 type EC dbReference id 3.1.2.1 type EC dbReference id 3.1.1.- type EC dbReference id CAIF01000179 type EMBL property type protein-sequence-ID value CCH45056.1 property type molecule-type value Genomic_DNA dbReference id K0KPV8 type AlphaFoldDB dbReference id K0KPV8 type SMR dbReference id 1206466.K0KPV8 type STRING dbReference id wiccf-k0kpv8 type ESTHER property type family-name value ABHD11-Acetyl_transferase dbReference id KOG2382 type eggNOG property type taxonomic-scope value Eukaryota dbReference id CLU_020336_53_0_1 type HOGENOM dbReference id K0KPV8 type InParanoid dbReference id UP000009328 type Proteomes property type component value Unassembled-WGS-sequence dbReference id GO:0005739 type GO property type term value C:mitochondrion property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0003986 type GO property type term value F:acetyl-CoA-hydrolase-activity property type evidence value ECO:0007669 property type project value UniProtKB-EC dbReference id GO:0016740 type GO property type term value F:transferase-activity property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id 3.40.50.1820 type Gene3D property type entry-name value alpha/beta-hydrolase property type match-status value 1 dbReference id IPR029058 type InterPro property type entry-name value AB_hydrolase dbReference id IPR000073 type InterPro property type entry-name value AB_hydrolase_1 dbReference id PTHR46118 type PANTHER property type entry-name value PROTEIN-ABHD11 property type match-status value 1 dbReference id PTHR46118:SF4 type PANTHER property type entry-name value PROTEIN-ABHD11 property type match-status value 1 dbReference id PF00561 type Pfam property type entry-name value Abhydrolase_1 property type match-status value 1 dbReference id SSF53474 type SUPFAM property type entry-name value alpha/beta-Hydrolases property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0378 Hydrolase keyword id KW-0496 Mitochondrion keyword id KW-1185 Reference-proteome keyword id KW-0808 Transferase keyword id KW-0809 Transit-peptide feature description Mitochondrion evidence 2 type transit-peptide location begin position 1 end position 25 feature description Ethanol-acetyltransferase-1 id PRO_0000446184 type chain location begin position 26 end position 393 feature description AB-hydrolase-1 evidence 2 type domain location begin position 49 end position 151 feature description Disordered evidence 3 type region-of-interest location begin position 343 end position 393 feature description Polar-residues evidence 3 type compositionally-biased-region location begin position 352 end position 377 feature description Basic-and-acidic-residues evidence 3 type compositionally-biased-region location begin position 378 end position 393 feature description Charge-relay-system evidence 1 type active-site location position position 122 feature description Charge-relay-system evidence 1 type active-site location position position 146 feature description Charge-relay-system evidence 1 type active-site location position position 296 evidence key 1 type ECO:0000250 source dbReference id A0A1E3P8S6 type UniProtKB evidence key 2 type ECO:0000255 evidence key 3 type ECO:0000256 source dbReference id MobiDB-lite type SAM evidence key 4 type ECO:0000269 source dbReference id 28356220 type PubMed evidence key 5 type ECO:0000305 sequence checksum F9C3DD9FA054D17E length 393 mass 44775 modified 2012-11-28 precursor true version 1 MHFTRTLFNQVASKASRQLPVQKRVQMAYDLHIPNKTVNPNLNIRSHEPIVFVHGIFGSKKNYRFDCQKIANVTHTPVYTVDLRNHGQSIHALPFDYETLAQDVADFCEDHGLKKVNLIGYSLGAKICMLTMLQNPDLIRSGVIIDNSPIEQPHIEIFLQMFVKSMIHVLNSTKIEANDSDWKRKADDAMKRYIPDGGIRKYLLANLINKVPKGYKSPVIDYDDGFIHFQNPVKHMTEVAVKNVSAWPTEKVAGKTFEGPIRFIKGTKSAFIDDAGKKAIAGYFPNHSISEINATHFILNERPLEYVRVICDFIKTERFRSLQEHLRNVEHFSPSEIEAKQAAKHAQQIEELRKVTSTSESSIPHSTQSSEQAFTENIDLARQEREHQKSVSA 
entry created 2019-12-11 dataset Swiss-Prot modified 2023-02-22 version 87 accession Q0UK52 name STHC_PHANO protein recommendedName fullName evidence 5 Short-chain-dehydrogenase/reductase-sthC ecNumber evidence 7 1.1.1.- alternativeName fullName evidence 5 Stemphyloxin-II-biosynthesis-cluster-protein-C gene name evidence 5 type primary sthC name type ORF SNOG_07862 organism name type scientific Phaeosphaeria-nodorum-(strain-SN15-/-ATCC-MYA-4574-/-FGSC-10173) name type common Glume-blotch-fungus name type synonym Parastagonospora-nodorum dbReference id 321614 type NCBI-Taxonomy lineage taxon Eukaryota taxon Fungi taxon Dikarya taxon Ascomycota taxon Pezizomycotina taxon Dothideomycetes taxon Pleosporomycetidae taxon Pleosporales taxon Pleosporineae taxon Phaeosphaeriaceae taxon Parastagonospora reference key 1 citation date 2007 first 3347 last 3368 name Plant-Cell type journal-article volume 19 title Dothideomycete-plant-interactions-illuminated-by-genome-sequencing-and-EST-analysis-of-the-wheat-pathogen-Stagonospora-nodorum. authorList person name Hane-J.K. person name Lowe-R.G.T. person name Solomon-P.S. person name Tan-K.-C. person name Schoch-C.L. person name Spatafora-J.W. person name Crous-P.W. person name Kodira-C.D. person name Birren-B.W. person name Galagan-J.E. person name Torriani-S.F.F. person name McDonald-B.A. person name Oliver-R.P. dbReference id 18024570 type PubMed dbReference id 10.1105/tpc.107.052829 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain SN15-/-ATCC-MYA-4574-/-FGSC-10173 reference key 2 citation date 2019 first 15062 last 15066 name Chemistry type journal-article volume 25 title Biosynthesis-of-a-Tricyclo[6.2.2.02,7]dodecane-System-by-a-Berberine-Bridge-Enzyme-like-Intramolecular-Aldolase. authorList person name Li-H. person name Hu-J. person name Wei-H. person name Solomon-P.S. person name Stubbs-K.A. person name Chooi-Y.H. dbReference id 31553484 type PubMed dbReference id 10.1002/chem.201904360 type DOI scope FUNCTION scope CATALYTIC-ACTIVITY scope PATHWAY comment type function text evidence 4 Short-chain-dehydrogenase/reductase;-part-of-the-gene-cluster-that-mediates-the-biosynthesis-of-the-phytotoxin-stemphyloxin-II-(PubMed:31553484).-The-first-step-of-the-pathway-is-the-synthesis-of-dehydroprobetaenone-I-by-the-polyketide-synthase-sthA-and-the-enoyl-reductase-sthE-via-condensation-of-one-acetyl-CoA-starter-unit-with-7-malonyl-CoA-units-and-5-methylations-(PubMed:31553484).-The-C-terminal-reductase-(R)-domain-of-sthA-catalyzes-the-reductive-release-of-the-polyketide-chain-(PubMed:31553484).-Because-sthA-lacks-a-designated-enoylreductase-(ER)-domain,-the-required-activity-is-provided-the-enoyl-reductase-sthE-(PubMed:31553484).-The-short-chain-dehydrogenase/reductase-sthC-then-catalyzes-reduction-of-dehydroprobetaenone-I-to-probetaenone-I-(PubMed:31553484).-The-cytochrome-P450-monooxygenase-sthF-catalyzes-successive-epoxidation,-oxidation-(resulting-from-epoxide-opening)-and-hydroxylation-to-install-a-tertiary-alcohol-in-the-decaline-ring-to-yield-betaenone-C-from-dehydroprobetaenone-I-and-betaenone-B-from-probetaenone-I-(PubMed:31553484).-The-FAD-linked-oxidoreductase-sthB-is-responsible-for-the-conversion-of-betaenone-C-to-betaenone-A-via-an-intramolecular-aldol-reaction-between-C-1-and-C-17-to-form-the-bridged-tricyclic-system-in-betaenone-A-(PubMed:31553484).-Finally,-the-cytochrome-P450-monooxygenase-sthD-catalyzes-the-hydroxylation-of-C-15-to-afford-the-final-metabolite-stemphyloxin-II-(PubMed:31553484). comment type catalytic-activity reaction evidence 4 text AH2-+-dehydroprobetaenone-I-=-A-+-probetaenone-I dbReference id RHEA:61864 type Rhea dbReference id CHEBI:13193 type ChEBI dbReference id CHEBI:17499 type ChEBI dbReference id CHEBI:145061 type ChEBI dbReference id CHEBI:145062 type ChEBI physiologicalReaction direction left-to-right evidence 4 dbReference id RHEA:61865 type Rhea comment type catalytic-activity reaction evidence 4 text AH2-+-betaenone-C-=-A-+-betaenone-B dbReference id RHEA:61900 type Rhea dbReference id CHEBI:13193 type ChEBI dbReference id CHEBI:17499 type ChEBI dbReference id CHEBI:145053 type ChEBI dbReference id CHEBI:145054 type ChEBI physiologicalReaction direction left-to-right evidence 4 dbReference id RHEA:61901 type Rhea comment type pathway text evidence 4 Mycotoxin-biosynthesis. comment type similarity text evidence 6 Belongs-to-the-short-chain-dehydrogenases/reductases-(SDR)-family. dbReference evidence 7 id 1.1.1.- type EC dbReference id CH445335 type EMBL property type protein-sequence-ID value EAT85328.2 property type molecule-type value Genomic_DNA dbReference id XP_001798189.1 type RefSeq property type nucleotide-sequence-ID value XM_001798137.1 dbReference id Q0UK52 type AlphaFoldDB dbReference id Q0UK52 type SMR dbReference id 13684.SNOT_07862 type STRING dbReference id SNOT_07862 type EnsemblFungi property type protein-sequence-ID value SNOT_07862 property type gene-ID value SNOG_07862 dbReference id 5975082 type GeneID dbReference id pno:SNOG_07862 type KEGG dbReference id KOG1208 type eggNOG property type taxonomic-scope value Eukaryota dbReference id CLU_010194_44_6_1 type HOGENOM dbReference id Q0UK52 type InParanoid dbReference id 2718479at2759 type OrthoDB dbReference id UP000001055 type Proteomes property type component value Unassembled-WGS-sequence dbReference id GO:0016491 type GO property type term value F:oxidoreductase-activity property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id 3.40.50.720 type Gene3D property type entry-name value NAD(P)-binding-Rossmann-like-Domain property type match-status value 1 dbReference id IPR036291 type InterPro property type entry-name value NAD(P)-bd_dom_sf dbReference id IPR002347 type InterPro property type entry-name value SDR_fam dbReference id PTHR24320 type PANTHER property type entry-name value RETINOL-DEHYDROGENASE property type match-status value 1 dbReference id PTHR24320:SF236 type PANTHER property type entry-name value SHORT-CHAIN-DEHYDROGENASE/REDUCTASE-PKFC property type match-status value 1 dbReference id PF00106 type Pfam property type entry-name value adh_short property type match-status value 1 dbReference id PR00081 type PRINTS property type entry-name value GDHRDH dbReference id SSF51735 type SUPFAM property type entry-name value NAD(P)-binding-Rossmann-fold-domains property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0520 NAD keyword id KW-0521 NADP keyword id KW-0560 Oxidoreductase keyword id KW-1185 Reference-proteome feature description Short-chain-dehydrogenase/reductase-sthC id PRO_0000448655 type chain location begin position 1 end position 314 feature description Disordered evidence 3 type region-of-interest location begin position 1 end position 27 feature description Polar-residues evidence 3 type compositionally-biased-region location begin position 11 end position 27 feature description Proton-acceptor evidence 2 type active-site location position position 222 feature evidence 1 type binding-site location begin position 48 end position 56 ligand name NAD(+) dbReference id CHEBI:57540 type ChEBI feature evidence 1 type binding-site location begin position 75 end position 76 ligand name NAD(+) dbReference id CHEBI:57540 type ChEBI feature evidence 1 type binding-site location begin position 111 end position 113 ligand name NAD(+) dbReference id CHEBI:57540 type ChEBI feature evidence 1 type binding-site location begin position 222 end position 226 ligand name NAD(+) dbReference id CHEBI:57540 type ChEBI feature evidence 1 type binding-site location begin position 255 end position 257 ligand name NAD(+) dbReference id CHEBI:57540 type ChEBI evidence key 1 type ECO:0000250 source dbReference id Q92506 type UniProtKB evidence key 2 type ECO:0000255 source dbReference id PRU10001 type PROSITE-ProRule evidence key 3 type ECO:0000256 source dbReference id MobiDB-lite type SAM evidence key 4 type ECO:0000269 source dbReference id 31553484 type PubMed evidence key 5 type ECO:0000303 source dbReference id 31553484 type PubMed evidence key 6 type ECO:0000305 evidence key 7 type ECO:0000305 source dbReference id 31553484 type PubMed sequence checksum 008CEAD9347C4FDF length 314 mass 34055 modified 2008-02-05 version 2 MAPAETTGNVQRPEAGKQSMGSFWTQMFPPKPTYTEEQVPDLTGKIFIVTGSSSGVGKEAARMLYAKNAKVYMAARPGPKLPAAINSVQEAVPKSGGALIPLELDLADLAVVKKAVEKFTSLETKLHGLINNAAVQALKDTDGDARTAQGHEIHMGVNVLAPFLFTRLLTGVLTATARQEPPGTVRVVWVSSMGTETIGEKRRGLSPDYVDYWPLMSPLERYGLSKAGNWLHGVEFARRYAADGIASFPINPGHLKSDLYREGGALFKFALKPVLYPPTYGAYVELFAALSPTLTLKDSGAWSKYVEMVYFPDC 
entry created 2020-02-26 dataset Swiss-Prot modified 2023-02-22 version 96 accession Q9X1I0 name GLK_THEMA protein recommendedName fullName evidence 3 Glucokinase ecNumber evidence 1 2.7.1.2 alternativeName fullName evidence 2 ATP-dependent-glucokinase shortName evidence 2 ATP-GLK alternativeName fullName evidence 3 Glucose-kinase gene name evidence 2 type primary glk name evidence 4 type ordered-locus TM_1469 organism name type scientific Thermotoga-maritima-(strain-ATCC-43589-/-DSM-3109-/-JCM-10099-/-NBRC-100826-/-MSB8) dbReference id 243274 type NCBI-Taxonomy lineage taxon Bacteria taxon Thermotogae taxon Thermotogales taxon Thermotogaceae taxon Thermotoga reference key 1 citation date 1999 first 323 last 329 name Nature type journal-article volume 399 title Evidence-for-lateral-gene-transfer-between-Archaea-and-Bacteria-from-genome-sequence-of-Thermotoga-maritima. authorList person name Nelson-K.E. person name Clayton-R.A. person name Gill-S.R. person name Gwinn-M.L. person name Dodson-R.J. person name Haft-D.H. person name Hickey-E.K. person name Peterson-J.D. person name Nelson-W.C. person name Ketchum-K.A. person name McDonald-L.A. person name Utterback-T.R. person name Malek-J.A. person name Linher-K.D. person name Garrett-M.M. person name Stewart-A.M. person name Cotton-M.D. person name Pratt-M.S. person name Phillips-C.A. person name Richardson-D.L. person name Heidelberg-J.F. person name Sutton-G.G. person name Fleischmann-R.D. person name Eisen-J.A. person name White-O. person name Salzberg-S.L. person name Smith-H.O. person name Venter-J.C. person name Fraser-C.M. dbReference id 10360571 type PubMed dbReference id 10.1038/20601 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain ATCC-43589-/-DSM-3109-/-JCM-10099-/-NBRC-100826-/-MSB8 reference key 2 citation date 2003 first 405 last 411 name FEMS-Microbiol.-Lett. type journal-article volume 226 title ATP-dependent-glucokinase-from-the-hyperthermophilic-bacterium-Thermotoga-maritima-represents-an-extremely-thermophilic-ROK-glucokinase-with-high-substrate-specificity. authorList person name Hansen-T. person name Schoenheit-P. dbReference id 14553940 type PubMed dbReference id 10.1016/s0378-1097(03)00642-6 type DOI scope FUNCTION scope CATALYTIC-ACTIVITY scope COFACTOR scope BIOPHYSICOCHEMICAL-PROPERTIES scope SUBUNIT comment type function text evidence 1 Catalyzes-the-phosphorylation-of-D-glucose-to-D-glucose-6-phosphate-using-ATP-as-the-phosphate-donor.-Can-also-phosphorylate-2-deoxyglucose,-with-lower-efficiency.-ITP-can-also-serve-as-a-phosphoryl-donor. comment type catalytic-activity reaction evidence 1 text ATP-+-D-glucose-=-ADP-+-D-glucose-6-phosphate-+-H(+) dbReference id RHEA:17825 type Rhea dbReference id CHEBI:4167 type ChEBI dbReference id CHEBI:15378 type ChEBI dbReference id CHEBI:30616 type ChEBI dbReference id CHEBI:61548 type ChEBI dbReference id CHEBI:456216 type ChEBI dbReference id 2.7.1.2 type EC comment type cofactor cofactor evidence 1 name a-divalent-metal-cation dbReference id CHEBI:60240 type ChEBI text evidence 1 Mg(2+)-is-the-most-effective-ion.-It-can-be-efficiently-replaced-with-Mn(2+)-or-Co(2+)-and-to-some-extent-with-Ni(2+). comment type biophysicochemical-properties kinetics KM evidence 1 1-mM-for-glucose KM evidence 1 1.1-mM-for-2-deoxyglucose KM evidence 1 0.36-mM-for-ATP phDependence text evidence 1 Optimum-pH-is-7.3. temperatureDependence text evidence 1 Optimum-temperature-is-93-degrees-Celsius. comment type subunit text evidence 1 Homodimer. comment type similarity text evidence 3 Belongs-to-the-ROK-(NagC/XylR)-family. dbReference evidence 1 id 2.7.1.2 type EC dbReference id AE000512 type EMBL property type protein-sequence-ID value AAD36537.1 property type molecule-type value Genomic_DNA dbReference id F72246 type PIR property type entry-name value F72246 dbReference id NP_229269.1 type RefSeq property type nucleotide-sequence-ID value NC_000853.1 dbReference id Q9X1I0 type AlphaFoldDB dbReference id Q9X1I0 type SMR dbReference id 243274.THEMA_06955 type STRING dbReference id AAD36537 type EnsemblBacteria property type protein-sequence-ID value AAD36537 property type gene-ID value TM_1469 dbReference id tma:TM1469 type KEGG dbReference id fig|243274.5.peg.1485 type PATRIC dbReference id Q9X1I0 type InParanoid dbReference id DHLVMIT type OMA dbReference id 9810372at2 type OrthoDB dbReference id MetaCyc:MON-6111 type BioCyc dbReference id UP000008183 type Proteomes property type component value Chromosome dbReference id GO:0005737 type GO property type term value C:cytoplasm property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0005524 type GO property type term value F:ATP-binding property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0004340 type GO property type term value F:glucokinase-activity property type evidence value ECO:0007669 property type project value UniProtKB-EC dbReference id GO:0006006 type GO property type term value P:glucose-metabolic-process property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0006096 type GO property type term value P:glycolytic-process property type evidence value ECO:0007669 property type project value InterPro dbReference id cd00012 type CDD property type entry-name value NBD_sugar-kinase_HSP70_actin property type match-status value 1 dbReference id 3.30.420.40 type Gene3D property type match-status value 2 dbReference id IPR043129 type InterPro property type entry-name value ATPase_NBD dbReference id IPR000600 type InterPro property type entry-name value ROK dbReference id IPR004654 type InterPro property type entry-name value ROK_glcA dbReference id PTHR18964:SF149 type PANTHER property type entry-name value BIFUNCTIONAL-UDP-N-ACETYLGLUCOSAMINE-2-EPIMERASE/N-ACETYLMANNOSAMINE-KINASE property type match-status value 1 dbReference id PTHR18964 type PANTHER property type entry-name value ROK-(REPRESSOR,-ORF,-KINASE)-FAMILY property type match-status value 1 dbReference id PF00480 type Pfam property type entry-name value ROK property type match-status value 1 dbReference id SSF53067 type SUPFAM property type entry-name value Actin-like-ATPase-domain property type match-status value 1 dbReference id TIGR00744 type TIGRFAMs property type entry-name value ROK_glcA_fam property type match-status value 1 dbReference id PS01125 type PROSITE property type entry-name value ROK property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0067 ATP-binding keyword id KW-0119 Carbohydrate-metabolism keyword id KW-0313 Glucose-metabolism keyword id KW-0418 Kinase keyword id KW-0460 Magnesium keyword id KW-0547 Nucleotide-binding keyword id KW-1185 Reference-proteome keyword id KW-0808 Transferase feature description Glucokinase id PRO_0000448972 type chain location begin position 1 end position 317 evidence key 1 type ECO:0000269 source dbReference id 14553940 type PubMed evidence key 2 type ECO:0000303 source dbReference id 14553940 type PubMed evidence key 3 type ECO:0000305 evidence key 4 type ECO:0000312 source dbReference id AAD36537.1 type EMBL sequence checksum 30B1DE9D69FFFA3F length 317 mass 33891 modified 1999-11-01 version 1 MPKLKLIGVDLGGTTFSVGLVSEDGKILKKVTRDTLVENGKEDVIRRIAETILEVSDGEEAPYVGIGSPGSIDRENGIVRFSPNFPDWHNVPLTDELAKRTGKKVFLENDANAFVLGEKWFGAGRGHDHIVALTLGTGIGGGVVTHGYLLTGRDGIGAELGHVVVEPNGPMCNCGTRGCLEAVASATAIRRFLREGYKKYHSSLVYKLAGSPEKADAKHLFDAARQGDRFALMIRDRVVDALARAVAGYIHIFNPEIVIIGGGISRAGEILFGPLREKVVDYIMPSFVGTYEVVASPLVEDAGILGAASIIKERIGG 
entry created 2020-10-07 dataset Swiss-Prot modified 2023-02-22 version 10 accession P9WEU6 name NIT_TRAVS protein recommendedName fullName evidence 3 Arylacetonitrilase ecNumber evidence 2 3.5.5.1 alternativeName fullName evidence 3 NitTv1 gene name type primary nit name type ORF TRAVEDRAFT_139011 organism name type scientific Trametes-versicolor-(strain-FP-101664) name type common White-rot-fungus name type synonym Coriolus-versicolor dbReference id 717944 type NCBI-Taxonomy lineage taxon Eukaryota taxon Fungi taxon Dikarya taxon Basidiomycota taxon Agaricomycotina taxon Agaricomycetes taxon Polyporales taxon Polyporaceae taxon Trametes reference key 1 citation date 2012 first 1715 last 1719 name Science type journal-article volume 336 title The-Paleozoic-origin-of-enzymatic-lignin-decomposition-reconstructed-from-31-fungal-genomes. authorList person name Floudas-D. person name Binder-M. person name Riley-R. person name Barry-K. person name Blanchette-R.A. person name Henrissat-B. person name Martinez-A.T. person name Otillar-R. person name Spatafora-J.W. person name Yadav-J.S. person name Aerts-A. person name Benoit-I. person name Boyd-A. person name Carlson-A. person name Copeland-A. person name Coutinho-P.M. person name de-Vries-R.P. person name Ferreira-P. person name Findley-K. person name Foster-B. person name Gaskell-J. person name Glotzer-D. person name Gorecki-P. person name Heitman-J. person name Hesse-C. person name Hori-C. person name Igarashi-K. person name Jurgens-J.A. person name Kallen-N. person name Kersten-P. person name Kohler-A. person name Kuees-U. person name Kumar-T.K.A. person name Kuo-A. person name LaButti-K. person name Larrondo-L.F. person name Lindquist-E. person name Ling-A. person name Lombard-V. person name Lucas-S. person name Lundell-T. person name Martin-R. person name McLaughlin-D.J. person name Morgenstern-I. person name Morin-E. person name Murat-C. person name Nagy-L.G. person name Nolan-M. person name Ohm-R.A. person name Patyshakuliyeva-A. person name Rokas-A. person name Ruiz-Duenas-F.J. person name Sabat-G. person name Salamov-A. person name Samejima-M. person name Schmutz-J. person name Slot-J.C. person name St-John-F. person name Stenlid-J. person name Sun-H. person name Sun-S. person name Syed-K. person name Tsang-A. person name Wiebenga-A. person name Young-D. person name Pisabarro-A. person name Eastwood-D.C. person name Martin-F. person name Cullen-D. person name Grigoriev-I.V. person name Hibbett-D.S. dbReference id 22745431 type PubMed dbReference id 10.1126/science.1221748 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain FP-101664 reference key 2 citation date 2019 first 0 last 0 name Int.-J.-Mol.-Sci. type journal-article volume 20 title Genetic-and-functional-diversity-of-nitrilases-in-Agaricomycotina. authorList person name Rucka-L. person name Chmatal-M. person name Kulik-N. person name Petraskova-L. person name Pelantova-H. person name Novotny-P. person name Prihodova-R. person name Patek-M. person name Martinkova-L. dbReference id 31795104 type PubMed dbReference id 10.3390/ijms20235990 type DOI scope FUNCTION scope CATALYTIC-ACTIVITY comment type function text evidence 2 Nitrilase-that-hydrolyzes-preferentially-fumaronitrile,-while-3-phenylpropionitrile,-beta-cyano-L-alanine-and-4-cyanopyridine-are-transformed-at-much-lower-rates. comment type catalytic-activity reaction evidence 2 text a-nitrile-+-2-H2O-=-a-carboxylate-+-NH4(+) dbReference id RHEA:21724 type Rhea dbReference id CHEBI:15377 type ChEBI dbReference id CHEBI:18379 type ChEBI dbReference id CHEBI:28938 type ChEBI dbReference id CHEBI:29067 type ChEBI dbReference id 3.5.5.1 type EC comment type similarity text evidence 4 Belongs-to-the-carbon-nitrogen-hydrolase-superfamily.-Nitrilase-family. dbReference evidence 2 id 3.5.5.1 type EC dbReference id JH711783 type EMBL property type protein-sequence-ID value EIW64330.1 property type molecule-type value Genomic_DNA dbReference id XP_008032838.1 type RefSeq property type nucleotide-sequence-ID value XM_008034647.1 dbReference id P9WEU6 type AlphaFoldDB dbReference id P9WEU6 type SMR dbReference id 19409089 type GeneID dbReference id tvs:TRAVEDRAFT_139011 type KEGG dbReference id IYADVDF type OMA dbReference id 1361256at2759 type OrthoDB dbReference id UP000054317 type Proteomes property type component value Unassembled-WGS-sequence dbReference id GO:0080061 type GO property type term value F:indole-3-acetonitrile-nitrilase-activity property type evidence value ECO:0007669 property type project value UniProtKB-EC dbReference id GO:0006807 type GO property type term value P:nitrogen-compound-metabolic-process property type evidence value ECO:0007669 property type project value InterPro dbReference id cd07564 type CDD property type entry-name value nitrilases_CHs property type match-status value 1 dbReference id 3.60.110.10 type Gene3D property type entry-name value Carbon-nitrogen-hydrolase property type match-status value 1 dbReference id IPR003010 type InterPro property type entry-name value C-N_Hydrolase dbReference id IPR036526 type InterPro property type entry-name value C-N_Hydrolase_sf dbReference id IPR044149 type InterPro property type entry-name value Nitrilases_CHs dbReference id PTHR46044:SF1 type PANTHER property type entry-name value CN-HYDROLASE-DOMAIN-CONTAINING-PROTEIN property type match-status value 1 dbReference id PTHR46044 type PANTHER property type entry-name value NITRILASE property type match-status value 1 dbReference id PF00795 type Pfam property type entry-name value CN_hydrolase property type match-status value 1 dbReference id SSF56317 type SUPFAM property type entry-name value Carbon-nitrogen-hydrolase property type match-status value 1 dbReference id PS50263 type PROSITE property type entry-name value CN_HYDROLASE property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0378 Hydrolase keyword id KW-1185 Reference-proteome feature description Arylacetonitrilase id PRO_0000451139 type chain location begin position 1 end position 320 feature description CN-hydrolase evidence 1 type domain location begin position 5 end position 286 feature description Proton-acceptor evidence 1 type active-site location position position 46 feature evidence 1 type active-site location position position 133 feature description Nucleophile evidence 1 type active-site location position position 178 evidence key 1 type ECO:0000255 source dbReference id PRU00054 type PROSITE-ProRule evidence key 2 type ECO:0000269 source dbReference id 31795104 type PubMed evidence key 3 type ECO:0000303 source dbReference id 31795104 type PubMed evidence key 4 type ECO:0000305 sequence checksum CACC4932ED2228FE length 320 mass 34911 modified 2020-10-07 version 1 MANTIKASVVQASTAAYSLPDTLDKLEKLTRLAKERDGAQLAVFPEAFIGGYPKMSTFGLVVGDRQPEGRDEFVRYAKAAIEIPSPAITRIEQISRETNVFIVVGVIERDAGTLYCTAVFVDPEKGYVDKHRKLVPTAMERVIWGQGDGSTLPVLDKSFESASAPGSTVNTKLSATICWENYMPLLRTYYYSQGTQIYCAPTVDARPAWQHTMTHIALEGRCFVLSACQFAQEKDYPPDHAVANASARDPNNVMIAGGSVIISPLGKVLAGPLLDAEGVISAELDLDDVLRGKFDLDVTGHYARNDVFEFKLREPPATSS 
entry created 2020-10-07 dataset Swiss-Prot modified 2023-02-22 version 20 accession A0A251PW43 accession A0A251PUT9 accession M5X7Z4 name DRO1_PRUPE protein recommendedName fullName evidence 3 Protein-DEEPER-ROOTING-1 shortName evidence 3 PpeDRO1 gene name evidence 3 type primary DRO1 name evidence 5 type ORF PRUPE_3G038300 organism name type scientific Prunus-persica name type common Peach name type synonym Amygdalus-persica dbReference id 3760 type NCBI-Taxonomy lineage taxon Eukaryota taxon Viridiplantae taxon Streptophyta taxon Embryophyta taxon Tracheophyta taxon Spermatophyta taxon Magnoliopsida taxon eudicotyledons taxon Gunneridae taxon Pentapetalae taxon rosids taxon fabids taxon Rosales taxon Rosaceae taxon Amygdaloideae taxon Amygdaleae taxon Prunus reference key 1 citation date 2013 first 487 last 494 name Nat.-Genet. type journal-article volume 45 title The-high-quality-draft-genome-of-peach-(Prunus-persica)-identifies-unique-patterns-of-genetic-diversity,-domestication-and-genome-evolution. authorList consortium name International-Peach-Genome-Initiative person name Verde-I. person name Abbott-A.G. person name Scalabrin-S. person name Jung-S. person name Shu-S. person name Marroni-F. person name Zhebentyayeva-T. person name Dettori-M.T. person name Grimwood-J. person name Cattonaro-F. person name Zuccolo-A. person name Rossini-L. person name Jenkins-J. person name Vendramin-E. person name Meisel-L.A. person name Decroocq-V. person name Sosinski-B. person name Prochnik-S. person name Mitros-T. person name Policriti-A. person name Cipriani-G. person name Dondini-L. person name Ficklin-S. person name Goodstein-D.M. person name Xuan-P. person name Del-Fabbro-C.D. person name Aramini-V. person name Copetti-D. person name Gonzalez-S. person name Horner-D.S. person name Falchi-R. person name Lucas-S. person name Mica-E. person name Maldonado-J. person name Lazzari-B. person name Bielenberg-D. person name Pirona-R. person name Miculan-M. person name Barakat-A. person name Testolin-R. person name Stella-A. person name Tartarini-S. person name Tonutti-P. person name Arus-P. person name Orellana-A. person name Wells-C. person name Main-D. person name Vizzotto-G. person name Silva-H. person name Salamini-F. person name Schmutz-J. person name Morgante-M. person name Rokhsar-D.S. dbReference id 23525075 type PubMed dbReference id 10.1038/ng.2586 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain cv.-Nemared reference key 2 citation date 2017 first 1093 last 1105 name Plant-J. type journal-article volume 89 title DRO1-influences-root-system-architecture-in-Arabidopsis-and-Prunus-species. authorList person name Guseman-J.M. person name Webb-K. person name Srinivasan-C. person name Dardick-C. dbReference id 28029738 type PubMed dbReference id 10.1111/tpj.13470 type DOI scope FUNCTION scope TISSUE-SPECIFICITY comment type function text evidence 2 Involved-in-the-development-of-the-root-system-architecture-by-influencing-lateral-root-angles-and-primary-root-length. comment type tissue-specificity text evidence 2 Expressed-in-roots. comment type miscellaneous text evidence 2 Plants-overexpressing-DRO1-exhibit-increased-length-and-density-of-roots,-and-increased-biomass-of-shoots. comment type similarity text evidence 4 Belongs-to-the-LAZY-family. comment evidence 4 type sequence-caution conflict type erroneous-gene-model-prediction sequence id EMJ17638 resource EMBL-CDS version 1 comment evidence 4 type sequence-caution conflict type erroneous-gene-model-prediction sequence id ONI15341 resource EMBL-CDS version 1 dbReference id KB639030 type EMBL property type protein-sequence-ID value EMJ17638.1 property type status value ALT_SEQ property type molecule-type value Genomic_DNA dbReference id CM007653 type EMBL property type protein-sequence-ID value ONI15340.1 property type molecule-type value Genomic_DNA dbReference id CM007653 type EMBL property type protein-sequence-ID value ONI15341.1 property type status value ALT_SEQ property type molecule-type value Genomic_DNA dbReference id A0A251PW43 type AlphaFoldDB dbReference id A0A251PW43 type SMR dbReference id ONI15340 type EnsemblPlants property type protein-sequence-ID value ONI15340 property type gene-ID value PRUPE_3G038300 dbReference id ONI15341 type EnsemblPlants property type protein-sequence-ID value ONI15341 property type gene-ID value PRUPE_3G038300 dbReference id ONI15340 type Gramene property type protein-sequence-ID value ONI15340 property type gene-ID value PRUPE_3G038300 dbReference id ONI15341 type Gramene property type protein-sequence-ID value ONI15341 property type gene-ID value PRUPE_3G038300 dbReference id ENOG502QSTE type eggNOG property type taxonomic-scope value Eukaryota dbReference id CLU_068790_0_0_1 type HOGENOM dbReference id 344914at2759 type OrthoDB dbReference id UP000006882 type Proteomes property type component value Chromosome-g3 dbReference id GO:0009958 type GO property type term value P:positive-gravitropism property type evidence value ECO:0000315 property type project value UniProtKB dbReference id GO:0040008 type GO property type term value P:regulation-of-growth property type evidence value ECO:0007669 property type project value InterPro dbReference id IPR044683 type InterPro property type entry-name value LAZY dbReference id PTHR34045 type PANTHER property type entry-name value OS03G0406300-PROTEIN property type match-status value 1 dbReference id PTHR34045:SF3 type PANTHER property type entry-name value PROTEIN-LAZY-2 property type match-status value 1 proteinExistence type evidence-at-transcript-level keyword id KW-0341 Growth-regulation keyword id KW-1185 Reference-proteome feature description Protein-DEEPER-ROOTING-1 id PRO_0000451023 type chain location begin position 1 end position 268 feature description Disordered evidence 1 type region-of-interest location begin position 11 end position 39 feature description Disordered evidence 1 type region-of-interest location begin position 220 end position 246 feature description IGT-motif evidence 4 type short-sequence-motif location begin position 44 end position 50 feature description Polar-residues evidence 1 type compositionally-biased-region location begin position 11 end position 28 feature description Basic-and-acidic-residues evidence 1 type compositionally-biased-region location begin position 225 end position 246 feature description In-Ref.-1;-ONI15341. evidence 4 ref 1 type sequence-conflict original L variation V location position position 204 evidence key 1 type ECO:0000256 source dbReference id MobiDB-lite type SAM evidence key 2 type ECO:0000269 source dbReference id 28029738 type PubMed evidence key 3 type ECO:0000303 source dbReference id 28029738 type PubMed evidence key 4 type ECO:0000305 evidence key 5 type ECO:0000312 source dbReference id ONI15340.1 type EMBL sequence checksum F08D13A533C413E0 length 268 mass 30460 modified 2017-11-22 version 1 MKLFGWMQNKLNGKQGNKKPNTVPITTHPAKQEPREEFSDWPHGLLAIGTFGNNDLKENAAESQDIQEDPTSSEEILDNFTPEEVGKLHKELTKLLTRKPNIEKEIADLPLDRFLNCPSSLEVDRRNSNALCSDSADDHKDEDIEKTISVILGRCKEICGDKNKKAIGKKSISFLLKKMFVCRSGFAPQPSLRDTLQESRMEKLLRVMLNKKIINPQGSSRAASMKKYLEDRQIPTKKESNTEDDTKEKINNGCKWVKTDSEYIVLEI 
entry created 2021-06-02 dataset Swiss-Prot modified 2023-02-22 version 76 accession Q3S406 name GSK1_MAGOR protein recommendedName fullName evidence 4 Glycogen-synthase-kinase-1 ecNumber evidence 3 2.7.11.1 gene name evidence 4 type primary GSK1 organism name type scientific Magnaporthe-oryzae name type common Rice-blast-fungus name type synonym Pyricularia-oryzae dbReference id 318829 type NCBI-Taxonomy lineage taxon Eukaryota taxon Fungi taxon Dikarya taxon Ascomycota taxon Pezizomycotina taxon Sordariomycetes taxon Sordariomycetidae taxon Magnaporthales taxon Pyriculariaceae taxon Pyricularia reference key 1 citation date 2017 first 945 last 945 name Sci.-Rep. type journal-article volume 7 title The-glycogen-synthase-kinase-MoGsk1,-regulated-by-Mps1-MAP-kinase,-is-required-for-fungal-development-and-pathogenicity-in-Magnaporthe-oryzae. authorList person name Zhou-T. person name Dagdas-Y.F. person name Zhu-X. person name Zheng-S. person name Chen-L. person name Cartwright-Z. person name Talbot-N.J. person name Wang-Z. dbReference id 28424497 type PubMed dbReference id 10.1038/s41598-017-01006-w type DOI scope NUCLEOTIDE-SEQUENCE-[GENOMIC-DNA] scope INDUCTION scope FUNCTION scope DISRUPTION-PHENOTYPE scope SUBCELLULAR-LOCATION source strain Guyane-11 reference key 2 citation date 2019 first 1234 last 1257 name Autophagy type journal-article volume 15 title Histone-acetyltransferase-MoHat1-acetylates-autophagy-related-proteins-MoAtg3-and-MoAtg9-to-orchestrate-functional-appressorium-formation-and-pathogenicity-in-Magnaporthe-oryzae. authorList person name Yin-Z. person name Chen-C. person name Yang-J. person name Feng-W. person name Liu-X. person name Zuo-R. person name Wang-J. person name Yang-L. person name Zhong-K. person name Gao-C. person name Zhang-H. person name Zheng-X. person name Wang-P. person name Zhang-Z. dbReference id 30776962 type PubMed dbReference id 10.1080/15548627.2019.1580104 type DOI scope FUNCTION scope CATALYTIC-ACTIVITY comment type function text evidence 2-3 Protein-kinase-that-acts-downstream-of-the-MPS1-MAPK-cascade-as-a-highly-conservative-signal-modulator-that-dictates-growth,-conidiation-and-pathogenicity-(PubMed:28424497).-Phosphorylates-HAT1-at-'Ser-8'-to-block-its-translocation-from-the-nucleus-to-the-cytoplasm-where-HAT1-positively-regulates-appressorium-development-and-pathogenicity-(PubMed:30776962). comment type catalytic-activity reaction evidence 3 text ATP-+-L-seryl-[protein]-=-ADP-+-H(+)-+-O-phospho-L-seryl-[protein] dbReference id RHEA:17989 type Rhea dbReference id RHEA-COMP:9863 type Rhea dbReference id RHEA-COMP:11604 type Rhea dbReference id CHEBI:15378 type ChEBI dbReference id CHEBI:29999 type ChEBI dbReference id CHEBI:30616 type ChEBI dbReference id CHEBI:83421 type ChEBI dbReference id CHEBI:456216 type ChEBI dbReference id 2.7.11.1 type EC comment type subcellular-location subcellularLocation location evidence 2 Cytoplasm text evidence 2 Mainly-localizes-to-the-cytoplasm-at-the-conidial-stage. comment type induction text evidence 2 Expression-is-regulated-by-MPS1-MAP-kinase,-particularly-under-stress-conditions. comment type disruption-phenotype text evidence 2 Leads-to-significant-delay-in-mycelial-growth,-complete-loss-of-conidiation-and-inability-to-penetrate-the-host-surface-by-mycelia-formed-appressorium-like-structures,-consequently-resulting-in-loss-of-pathogenicity. comment type similarity text evidence 5 Belongs-to-the-protein-kinase-superfamily.-CMGC-Ser/Thr-protein-kinase-family.-GSK-3-subfamily. dbReference evidence 3 id 2.7.11.1 type EC dbReference id DQ168585 type EMBL property type protein-sequence-ID value ABA02071.1 property type molecule-type value Genomic_DNA dbReference id Q3S406 type AlphaFoldDB dbReference id Q3S406 type SMR dbReference id GO:0005737 type GO property type term value C:cytoplasm property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0005524 type GO property type term value F:ATP-binding property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0004674 type GO property type term value F:protein-serine/threonine-kinase-activity property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0051094 type GO property type term value P:positive-regulation-of-developmental-process property type evidence value ECO:0007669 property type project value UniProt dbReference id GO:0006468 type GO property type term value P:protein-phosphorylation property type evidence value ECO:0007669 property type project value InterPro dbReference id cd14137 type CDD property type entry-name value STKc_GSK3 property type match-status value 1 dbReference id 1.10.510.10 type Gene3D property type entry-name value Transferase(Phosphotransferase)-domain-1 property type match-status value 1 dbReference id IPR011009 type InterPro property type entry-name value Kinase-like_dom_sf dbReference id IPR000719 type InterPro property type entry-name value Prot_kinase_dom dbReference id IPR017441 type InterPro property type entry-name value Protein_kinase_ATP_BS dbReference id IPR008271 type InterPro property type entry-name value Ser/Thr_kinase_AS dbReference id IPR039192 type InterPro property type entry-name value STKc_GSK3 dbReference id PTHR24057 type PANTHER property type entry-name value GLYCOGEN-SYNTHASE-KINASE-3-ALPHA property type match-status value 1 dbReference id PTHR24057:SF0 type PANTHER property type entry-name value PROTEIN-KINASE-SHAGGY-RELATED property type match-status value 1 dbReference id PF00069 type Pfam property type entry-name value Pkinase property type match-status value 1 dbReference id SM00220 type SMART property type entry-name value S_TKc property type match-status value 1 dbReference id SSF56112 type SUPFAM property type entry-name value Protein-kinase-like-(PK-like) property type match-status value 1 dbReference id PS00107 type PROSITE property type entry-name value PROTEIN_KINASE_ATP property type match-status value 1 dbReference id PS50011 type PROSITE property type entry-name value PROTEIN_KINASE_DOM property type match-status value 1 dbReference id PS00108 type PROSITE property type entry-name value PROTEIN_KINASE_ST property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0067 ATP-binding keyword id KW-0963 Cytoplasm keyword id KW-0309 Germination keyword id KW-0418 Kinase keyword id KW-0547 Nucleotide-binding keyword id KW-0723 Serine/threonine-protein-kinase keyword id KW-0346 Stress-response keyword id KW-0808 Transferase keyword id KW-0843 Virulence feature description Glycogen-synthase-kinase-1 id PRO_0000453108 type chain location begin position 1 end position 394 feature description Protein-kinase evidence 1 type domain location begin position 35 end position 318 feature evidence 1 type binding-site location begin position 41 end position 49 ligand name ATP dbReference id CHEBI:30616 type ChEBI feature evidence 1 type binding-site location position position 64 ligand name ATP dbReference id CHEBI:30616 type ChEBI evidence key 1 type ECO:0000255 source dbReference id PRU00159 type PROSITE-ProRule evidence key 2 type ECO:0000269 source dbReference id 28424497 type PubMed evidence key 3 type ECO:0000269 source dbReference id 30776962 type PubMed evidence key 4 type ECO:0000303 source dbReference id 28424497 type PubMed evidence key 5 type ECO:0000305 sequence checksum E1DB6459F2E6678B length 394 mass 45383 modified 2005-10-11 version 1 MSQNRPAAFNTLRMGEVIREKVQDGITGETRDLQYTQCKIVGNGSFGVVFQTKLSPSNEDAAIKRVLQDKRFKNRELQIMRIVRHPNIVQLKAFYYSNGERRDEVYLNLVQEFVPETVYRASRFFNKMKTTMPILEVKLYIYQLFRALAYIHSQGICHRDIKPQNLLLDPTTGILKLCDFGSAKILVENEPNVSYICSRYYRAPELIFGATNYTTKIDVWSTGCVMAELMLGQPLFPGESGIDQLVEIIKVLGTPTREQIRTMNPNYMEHKFPQIKPHPFNRVLRKADNNAIDLIARLLEYTPTERLGAIDAMVHPFFDDLRNPSTKLPDSRHQTGQVRDLPPLFDFNRHELSIAPQLNHQLVPPHVRPTLAAQGLDIDHFTPMRKEDMLARLD 
entry created 2021-09-29 dataset Swiss-Prot modified 2023-02-22 version 6 accession C0HLU7 name HCY_SCYOL protein recommendedName fullName evidence 5 Hemocyanin-subunit organism evidence 5 name type scientific Scylla-olivacea name type common Orange-mud-crab name type synonym Cancer-olivacea dbReference id 85551 type NCBI-Taxonomy lineage taxon Eukaryota taxon Metazoa taxon Ecdysozoa taxon Arthropoda taxon Crustacea taxon Multicrustacea taxon Malacostraca taxon Eumalacostraca taxon Eucarida taxon Decapoda taxon Pleocyemata taxon Brachyura taxon Eubrachyura taxon Portunoidea taxon Portunidae taxon Portuninae taxon Scylla reference evidence 6 key 1 citation date 2020-12 db UniProtKB type submission title Characterization-and-molecular-interactions-of-hemolymph-proteins-from-two-mud-crab-species-Scylla-serrata-(Forskal,-1775)-and-Scylla-olivacea-(Herbst,-1796)-from-Visakhapatnam-coast,-Andhra-Pradesh,-India. authorList person name Prasanthi-C. person name Ramesh-B.K. scope PROTEIN-SEQUENCE scope IDENTIFICATION-BY-MASS-SPECTROMETRY scope SUBCELLULAR-LOCATION scope TISSUE-SPECIFICITY source tissue evidence 4 Hemolymph comment type function text evidence 1 Hemocyanins-are-copper-containing-oxygen-carriers-occurring-freely-dissolved-in-the-hemolymph-of-many-mollusks-and-arthropods. comment type subunit text evidence 1 Hexamer-of-a-number-of-different-chains. comment type subcellular-location subcellularLocation location evidence 4 Secreted location evidence 4 Extracellular-space comment type tissue-specificity text evidence 4 Hemolymph. comment type similarity text evidence 6 Belongs-to-the-tyrosinase-family.-Hemocyanin-subfamily. dbReference id C0HLU7 type AlphaFoldDB dbReference id C0HLU7 type SMR dbReference id GO:0005615 type GO property type term value C:extracellular-space property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0046872 type GO property type term value F:metal-ion-binding property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0016491 type GO property type term value F:oxidoreductase-activity property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0005344 type GO property type term value F:oxygen-carrier-activity property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id 1.10.1280.10 type Gene3D property type entry-name value Di-copper-center-containing-domain-from-catechol-oxidase property type match-status value 1 dbReference id 2.60.40.1520 type Gene3D property type entry-name value Hemocyanin,-C-terminal-domain property type match-status value 1 dbReference id 1.20.1370.10 type Gene3D property type entry-name value Hemocyanin,-N-terminal-domain property type match-status value 1 dbReference id IPR008922 type InterPro property type entry-name value Di-copper_centre_dom_sf dbReference id IPR013788 type InterPro property type entry-name value Hemocyanin/hexamerin dbReference id IPR000896 type InterPro property type entry-name value Hemocyanin/hexamerin_mid_dom dbReference id IPR005203 type InterPro property type entry-name value Hemocyanin_C dbReference id IPR037020 type InterPro property type entry-name value Hemocyanin_C_sf dbReference id IPR005204 type InterPro property type entry-name value Hemocyanin_N dbReference id IPR036697 type InterPro property type entry-name value Hemocyanin_N_sf dbReference id IPR014756 type InterPro property type entry-name value Ig_E-set dbReference id IPR002227 type InterPro property type entry-name value Tyrosinase_Cu-bd dbReference id PTHR11511:SF25 type PANTHER property type entry-name value LARVAL-SERUM-PROTEIN-2 property type match-status value 1 dbReference id PTHR11511 type PANTHER property type entry-name value LARVAL-STORAGE-PROTEIN/PHENOLOXIDASE property type match-status value 1 dbReference id PF03723 type Pfam property type entry-name value Hemocyanin_C property type match-status value 1 dbReference id PF00372 type Pfam property type entry-name value Hemocyanin_M property type match-status value 1 dbReference id PF03722 type Pfam property type entry-name value Hemocyanin_N property type match-status value 1 dbReference id PR00187 type PRINTS property type entry-name value HAEMOCYANIN dbReference id SSF48056 type SUPFAM property type entry-name value Di-copper-centre-containing-domain property type match-status value 1 dbReference id SSF81296 type SUPFAM property type entry-name value E-set-domains property type match-status value 1 dbReference id SSF48050 type SUPFAM property type entry-name value Hemocyanin,-N-terminal-domain property type match-status value 1 dbReference id PS00209 type PROSITE property type entry-name value HEMOCYANIN_1 property type match-status value 1 dbReference id PS00210 type PROSITE property type entry-name value HEMOCYANIN_2 property type match-status value 1 dbReference id PS00498 type PROSITE property type entry-name value TYROSINASE_2 property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0186 Copper keyword id KW-0903 Direct-protein-sequencing keyword id KW-1015 Disulfide-bond keyword id KW-0325 Glycoprotein keyword id KW-0479 Metal-binding keyword id KW-0561 Oxygen-transport keyword id KW-0964 Secreted keyword id KW-0813 Transport feature description Hemocyanin-subunit id PRO_0000453528 type chain location begin position 1 end position 661 feature evidence 1 type binding-site location position position 200 ligand name Cu-cation dbReference id CHEBI:23378 type ChEBI label A feature evidence 1 type binding-site location position position 204 ligand name Cu-cation dbReference id CHEBI:23378 type ChEBI label A feature evidence 1 type binding-site location position position 230 ligand name Cu-cation dbReference id CHEBI:23378 type ChEBI label A feature evidence 1 type binding-site location position position 350 ligand name Cu-cation dbReference id CHEBI:23378 type ChEBI label B feature evidence 1 type binding-site location position position 354 ligand name Cu-cation dbReference id CHEBI:23378 type ChEBI label B feature evidence 1 type binding-site location position position 390 ligand name Cu-cation dbReference id CHEBI:23378 type ChEBI label B feature description N-linked-(GlcNAc...)-asparagine evidence 3 type glycosylation-site location position position 476 feature evidence 2 type disulfide-bond location begin position 3 end position 557 evidence key 1 type ECO:0000250 source dbReference id P04254 type UniProtKB evidence key 2 type ECO:0000250 source dbReference id P80096 type UniProtKB evidence key 3 type ECO:0000255 source dbReference id PRU00498 type PROSITE-ProRule evidence key 4 type ECO:0000269 source ref 1 evidence key 5 type ECO:0000303 source ref 1 evidence key 6 type ECO:0000305 sequence checksum F31F4338168B4069 length 661 mass 75874 modified 2021-09-29 version 1 ADCQAGDSADKLLAQKQHDVNYLVYKLYGDIRDDHLKELGETFNPQGDLLLYHDNGASVNTLMADFKDGRLLQKKHWFSLFNTRQREEALMMHRVLMNCKNWHAFVSNAAYFRTNMNEGEYLYALYVSLIHSGLGEGVVLPPLYEVTPHMFTNSEVIHEAYKAQMTNTPSKFESHFTGSKKNPEQHVAYFGEDVGMNTHHVLWHMEFPFWWEDSSGRHLDRKGESFFWVHHQLTVRYDAERLSNHLDPVEELSWNKAIDEGFAPHTAYKYGGYFPSRPDNVHFSDVDGVARVRDMSMTEDRIRDAIAHGYIDALDGSHIDIMNSHGIEFLGDIIESSGYSANPGFYGSLHNTAHIMLGRQGDPTGKFDLPPGVLEHFETSTRDPSFFRLHKYMDNIFREHKDSLTPYTRDELEFNGVSIDSIAIEGTLETFFENFEYSLLNAVDDTVDIADVEILTYIERLNHKKFSFLILVTNNNNTEVLATVRIFAWPLRDNNGIEYSFNEGRWRALELDRFWVKVKHGHHQITRQSTESSVTVPDVPSLQTLIDRADAAISSGCALHLEDYESALGLPNRFLLPKGQAQGMEFNLVVAVTDGRTDAALDDLHENTKFIHYGYDRQYPDKRPHGYPLDRRVDDERIFEALPNFKQRTVKLYSHEGVDGG 
entry created 2022-05-25 dataset Swiss-Prot modified 2023-02-22 version 14 accession A0A384E0Y8 name DEF3_MESMA protein recommendedName fullName evidence 4-5 Defensin-BmKDfsin3 organism name type scientific Mesobuthus-martensii name type common Manchurian-scorpion name type synonym Buthus-martensii dbReference id 34649 type NCBI-Taxonomy lineage taxon Eukaryota taxon Metazoa taxon Ecdysozoa taxon Arthropoda taxon Chelicerata taxon Arachnida taxon Scorpiones taxon Buthida taxon Buthoidea taxon Buthidae taxon Mesobuthus reference key 1 citation date 2013 first 2602 last 2602 name Nat.-Commun. type journal-article volume 4 title The-genome-of-Mesobuthus-martensii-reveals-a-unique-adaptation-model-of-arthropods. authorList person name Cao-Z. person name Yu-Y. person name Wu-Y. person name Hao-P. person name Di-Z. person name He-Y. person name Chen-Z. person name Yang-W. person name Shen-Z. person name He-X. person name Sheng-J. person name Xu-X. person name Pan-B. person name Feng-J. person name Yang-X. person name Hong-W. person name Zhao-W. person name Li-Z. person name Huang-K. person name Li-T. person name Kong-Y. person name Liu-H. person name Jiang-D. person name Zhang-B. person name Hu-J. person name Hu-Y. person name Wang-B. person name Dai-J. person name Yuan-B. person name Feng-Y. person name Huang-W. person name Xing-X. person name Zhao-G. person name Li-X. person name Li-Y. person name Li-W. dbReference id 24129506 type PubMed dbReference id 10.1038/ncomms3602 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source tissue Muscle reference evidence 8 key 2 citation date 2020 first 351 last 363 name Int.-J.-Biol.-Macromol. type journal-article volume 148 title Ion-channel-modulation-by-scorpion-hemolymph-and-its-defensin-ingredients-highlights-origin-of-neurotoxins-in-telson-formed-in-Paleozoic-scorpions. authorList person name Meng-L. person name Zhao-Y. person name Qu-D. person name Xie-Z. person name Guo-X. person name Zhu-Z. person name Chen-Z. person name Zhang-L. person name Li-W. person name Cao-Z. person name Tian-C. person name Wu-Y. dbReference id 31954123 type PubMed dbReference id 10.1016/j.ijbiomac.2020.01.133 type DOI scope STRUCTURE-BY-NMR scope FUNCTION scope SYNTHESIS-OF-25-62 scope DISULFIDE-BONDS scope TISSUE-SPECIFICITY source tissue Hemolymph tissue Venom-gland comment type function text evidence 3 Antibacterial-peptide-active-against-Gram-positive-bacteria-(including-S.aureus-ATCC25923-(MIC=2.5-uM),-M.luteus-AB93113-(MIC=2.5-uM),-and-the-antibiotic-resistant-S.epidermidis-PRSE-P1389-(MIC=1.25-uM)),-but-not-against-Gram-negative-bacteria-(including-E.coli-and-P.aeruginosa)-(PubMed:31954123).-Also-blocks-the-currents-of-Kv1.1/KCNA1-(57%-inhibition),-Kv1.2/KCNA2-(27.5%-inhibition),-Kv1.3/KCNA3-(IC(50)=23.4-nM,-84.3%-inhibition),-KCa3.1/KCNN4/IK-(15%-inhibition),-KCa2.3/KCNN3/SK3-(87.5%-inhibition)-and-Kv11.1/KCNH2/ERG1-(30.4%-inhibition)-channels-(tested-at-1-uM)-(PubMed:31954123).-It-inhibits-potassium-channel-current-by-interacting-with-the-pore-region-(PubMed:31954123). comment type subcellular-location subcellularLocation location evidence 7 Secreted comment type tissue-specificity text evidence 3 Low-expression-in-both-venom-and-non-venom-glands-(hemolymph). comment type similarity text evidence 2 Belongs-to-the-invertebrate-defensin-family.-Type-2-subfamily. dbReference id 5XA6 type PDB property type method value NMR property type chains value A=25-62 dbReference id 5XA6 type PDBsum dbReference id A0A384E0Y8 type AlphaFoldDB dbReference id A0A384E0Y8 type SMR dbReference id GO:0005576 type GO property type term value C:extracellular-region property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0015459 type GO property type term value F:potassium-channel-regulator-activity property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0090729 type GO property type term value F:toxin-activity property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0042742 type GO property type term value P:defense-response-to-bacterium property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0045087 type GO property type term value P:innate-immune-response property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id 3.30.30.10 type Gene3D property type entry-name value Knottin,-scorpion-toxin-like property type match-status value 1 dbReference id IPR001542 type InterPro property type entry-name value Defensin_invertebrate/fungal dbReference id IPR036574 type InterPro property type entry-name value Scorpion_toxin-like_sf dbReference id PF01097 type Pfam property type entry-name value Defensin_2 property type match-status value 1 dbReference id SSF57095 type SUPFAM property type entry-name value Scorpion-toxin-like property type match-status value 1 dbReference id PS51378 type PROSITE property type entry-name value INVERT_DEFENSINS property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0002 3D-structure keyword id KW-0044 Antibiotic keyword id KW-0929 Antimicrobial keyword id KW-1221 Calcium-activated-potassium-channel-impairing-toxin keyword id KW-0211 Defensin keyword id KW-1015 Disulfide-bond keyword id KW-0391 Immunity keyword id KW-0399 Innate-immunity keyword id KW-0872 Ion-channel-impairing-toxin keyword id KW-0632 Potassium-channel-impairing-toxin keyword id KW-0964 Secreted keyword id KW-0732 Signal keyword id KW-0800 Toxin keyword id KW-1220 Voltage-gated-potassium-channel-impairing-toxin feature evidence 1 type signal-peptide location begin position 1 end position 24 feature description Defensin-BmKDfsin3 evidence 6 id PRO_0000455527 type chain location begin position 25 end position 62 feature evidence 3-9 type disulfide-bond location begin position 28 end position 49 feature evidence 3-9 type disulfide-bond location begin position 35 end position 57 feature evidence 3-9 type disulfide-bond location begin position 39 end position 59 feature evidence 10 type helix location begin position 32 end position 40 feature evidence 10 type turn location begin position 41 end position 43 feature evidence 10 type strand location begin position 52 end position 54 evidence key 1 type ECO:0000255 evidence key 2 type ECO:0000255 source dbReference id PRU00710 type PROSITE-ProRule evidence key 3 type ECO:0000269 source dbReference id 31954123 type PubMed evidence key 4 type ECO:0000303 source dbReference id 24129506 type PubMed evidence key 5 type ECO:0000303 source dbReference id 31954123 type PubMed evidence key 6 type ECO:0000305 source dbReference id 24129506 type PubMed evidence key 7 type ECO:0000305 source dbReference id 31954123 type PubMed evidence key 8 type ECO:0000312 source dbReference id 5XA6 type PDB evidence key 9 type ECO:0007744 source dbReference id 5XA6 type PDB evidence key 10 type ECO:0007829 source dbReference id 5XA6 type PDB sequence checksum A9E6178EBE7E6D44 length 62 mass 7149 modified 2022-05-25 precursor true version 2 MKTIVILFVLALVFCTLEMGMVEAGFGCPFNQGKCHRHCRSIRRRGGYCDGFLKQRCVCYRK 
entry created 2022-05-25 dataset Swiss-Prot modified 2023-02-22 version 16 accession V5NBV4 accession D3XNR9 name TPM_MACRS protein recommendedName fullName evidence 11 Tropomyosin-Mac-r-1.0101 alternativeName fullName evidence 11 Major-allergen-Mac-r-1.0101 allergenName evidence 11 Mac-r-1.0101 organism evidence 14 name type scientific Macrobrachium-rosenbergii name type common Giant-fresh-water-prawn dbReference id 79674 type NCBI-Taxonomy lineage taxon Eukaryota taxon Metazoa taxon Ecdysozoa taxon Arthropoda taxon Crustacea taxon Multicrustacea taxon Malacostraca taxon Eumalacostraca taxon Eucarida taxon Decapoda taxon Pleocyemata taxon Caridea taxon Palaemonoidea taxon Palaemonidae taxon Macrobrachium reference evidence 14 key 1 citation date 2016 first 229 last 235 name Asian-Pac.-J.-Allergy-Immunol. type journal-article volume 34 title Cloning-and-characterization-of-recombinant-tropomyosin-of-giant-freshwater-shrimp-M.-rosenbergii-to-determine-major-allergens-causing-allergic-reactions-among-shrimp-allergic-children. authorList person name Kumjim-S. person name Jirapongsananuruk-O. person name Piboonpocanun-S. dbReference id 27001653 type PubMed dbReference id 10.12932/ap0698 type DOI scope NUCLEOTIDE-SEQUENCE-[MRNA] scope TISSUE-SPECIFICITY scope ALLERGEN scope CIRCULAR-DICHROISM-ANALYSIS source tissue evidence 11-14 Muscle reference evidence 13 key 2 citation date 2011-06 db EMBL/GenBank/DDBJ-databases type submission title Molecular-cloning-and-sequencing-of-tropomyosin-from-Macrobrachium-rosenbergii. authorList person name Phiriyangkul-P. person name Phiphobmongkol-C. person name Punyarit-P. scope NUCLEOTIDE-SEQUENCE-[MRNA] scope VARIANT-44-PHE-SER-45 reference key 3 citation date 2021 first 8247 last 8256 name J.-Agric.-Food-Chem. type journal-article volume 69 title Molecular-Characterization-and-Cross-Allergenicity-of-Tropomyosin-from-Freshwater-Crustaceans. authorList person name Laurchan-P. person name E-Kobon-T. person name Srisapoome-P. person name Unajak-S. person name Sinthuvanich-C. dbReference id 34255496 type PubMed dbReference id 10.1021/acs.jafc.1c00934 type DOI scope PROTEIN-SEQUENCE-OF-22-35-AND-113-125 scope TISSUE-SPECIFICITY scope IDENTIFICATION-BY-MASS-SPECTROMETRY scope ALLERGEN scope PHYLOGENETIC-ANALYSIS reference key 4 citation date 2012 first 50 last 54 name Asian-Pac.-J.-Trop.-Biomed. type journal-article volume 2 title Identification-of-the-major-allergen-of-Macrobrachium-rosenbergii-(giant-freshwater-prawn). authorList person name Yadzir-Z.H. person name Misnan-R. person name Abdullah-N. person name Bakhtiar-F. person name Arip-M. person name Murad-S. dbReference id 23569834 type PubMed dbReference id 10.1016/s2221-1691(11)60189-5 type DOI scope IDENTIFICATION-BY-MASS-SPECTROMETRY scope ALLERGEN comment type function text evidence 3 Tropomyosin,-in-association-with-the-troponin-complex,-plays-a-central-role-in-the-calcium-dependent-regulation-of-muscle-contraction. comment type subunit text evidence 2 Homodimer. comment type tissue-specificity text evidence 8-9 Expressed-in-muscle-(at-protein-level)-(PubMed:34255496).-Expressed-in-abdominal-muscle-(PubMed:27001653). comment type domain text evidence 12 The-molecule-is-in-a-coiled-coil-structure-that-is-formed-by-2-polypeptide-chains.-The-sequence-exhibits-a-prominent-seven-residues-periodicity. comment type allergen text evidence 7-8-9 Causes-an-allergic-reaction-in-human.-Natural-protein-binds-to-IgE-in-patients-allergic-to-giant-fresh-water-prawn-(M.rosenbergii)-(PubMed:27001653,-PubMed:23569834,-PubMed:34255496).-Recombinant-protein-binds-to-IgE-in-77%-of-the-13-Thai-children-tested-allergic-to-both-seawater-prawn-P.monodon-and-freshwater-prawn-M.rosenbergii.-Cross-reacts-with-P.monodon-tropomyosin-allergen-Pen-m-1-(PubMed:27001653).-Cross-reacts-with-tropomyosins-of-freshwater-crustaceans-M.lanchesteri,-C.quadricarinatus-and-P.clarkii-(PubMed:34255496). comment type similarity text evidence 5 Belongs-to-the-tropomyosin-family. dbReference id KF571722 type EMBL property type protein-sequence-ID value AHA85706.1 property type molecule-type value mRNA dbReference id GU369816 type EMBL property type protein-sequence-ID value ADC55380.1 property type molecule-type value mRNA dbReference id V5NBV4 type AlphaFoldDB dbReference id 8806 type Allergome property type allergen-name value Mac-r-1 dbReference id 8807 type Allergome property type allergen-name value Mac-r-1.0101 dbReference id GO:0042803 type GO property type term value F:protein-homodimerization-activity property type evidence value ECO:0000250 property type project value UniProtKB dbReference id GO:0040011 type GO property type term value P:locomotion property type evidence value ECO:0000250 property type project value UniProtKB dbReference id GO:0003012 type GO property type term value P:muscle-system-process property type evidence value ECO:0000270 property type project value UniProtKB dbReference id GO:0006937 type GO property type term value P:regulation-of-muscle-contraction property type evidence value ECO:0000250 property type project value UniProtKB dbReference id 1.20.5.170 type Gene3D property type match-status value 2 dbReference id 1.20.5.340 type Gene3D property type match-status value 1 dbReference id IPR000533 type InterPro property type entry-name value Tropomyosin dbReference id PTHR19269 type PANTHER property type entry-name value TROPOMYOSIN property type match-status value 1 dbReference id PTHR19269:SF45 type PANTHER property type entry-name value TROPOMYOSIN-1,-ISOFORMS-33/34 property type match-status value 1 dbReference id PF00261 type Pfam property type entry-name value Tropomyosin property type match-status value 1 dbReference id PR00194 type PRINTS property type entry-name value TROPOMYOSIN dbReference id SSF57997 type SUPFAM property type entry-name value Tropomyosin property type match-status value 1 dbReference id PS00326 type PROSITE property type entry-name value TROPOMYOSIN property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0007 Acetylation keyword id KW-0020 Allergen keyword id KW-0175 Coiled-coil keyword id KW-0903 Direct-protein-sequencing keyword id KW-0514 Muscle-protein keyword id KW-0677 Repeat feature description Tropomyosin-Mac-r-1.0101 id PRO_0000455697 type chain location begin position 1 end position 284 feature description Disordered evidence 6 type region-of-interest location begin position 1 end position 42 feature evidence 4 type coiled-coil-region location begin position 1 end position 273 feature description N-acetylmethionine evidence 1 type modified-residue location position position 1 feature evidence 10 type sequence-variant original FS variation HN location begin position 44 end position 45 evidence key 1 type ECO:0000250 source dbReference id A1KYZ2 type UniProtKB evidence key 2 type ECO:0000250 source dbReference id A2V735 type UniProtKB evidence key 3 type ECO:0000250 source dbReference id Q22866 type UniProtKB evidence key 4 type ECO:0000255 evidence key 5 type ECO:0000255 source dbReference id RU004515 type RuleBase evidence key 6 type ECO:0000256 source dbReference id MobiDB-lite type SAM evidence key 7 type ECO:0000269 source dbReference id 23569834 type PubMed evidence key 8 type ECO:0000269 source dbReference id 27001653 type PubMed evidence key 9 type ECO:0000269 source dbReference id 34255496 type PubMed evidence key 10 type ECO:0000269 source ref 2 evidence key 11 type ECO:0000303 source dbReference id 27001653 type PubMed evidence key 12 type ECO:0000305 evidence key 13 type ECO:0000312 source dbReference id ADC55380.1 type EMBL evidence key 14 type ECO:0000312 source dbReference id AHA85706.1 type EMBL sequence checksum 8ACA4C565D73B144 length 284 mass 32829 modified 2014-02-19 version 1 MDAIKKKMQAMKLEKDNAMDRADTLEQQNKEANNRAEKSEEEVFSLQKRMQQLENDLDSVQEALLKANQHLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSELSGY 
