entry created 2017-07-05 dataset Swiss-Prot modified 2023-02-22 version 96 accession Q5E5M9 name GLNT2_ALIF1 protein recommendedName fullName evidence 3 Glutamine-transporter-2 gene name evidence 4 type ordered-locus VF_1172 organism name type scientific Aliivibrio-fischeri-(strain-ATCC-700601-/-ES114) name type common Vibrio-fischeri dbReference id 312309 type NCBI-Taxonomy lineage taxon Bacteria taxon Proteobacteria taxon Gammaproteobacteria taxon Vibrionales taxon Vibrionaceae taxon Aliivibrio reference key 1 citation date 2005 first 3004 last 3009 name Proc.-Natl.-Acad.-Sci.-U.S.A. type journal-article volume 102 title Complete-genome-sequence-of-Vibrio-fischeri:-a-symbiotic-bacterium-with-pathogenic-congeners. authorList person name Ruby-E.G. person name Urbanowski-M. person name Campbell-J. person name Dunn-A. person name Faini-M. person name Gunsalus-R. person name Lostroh-P. person name Lupp-C. person name McCann-J. person name Millikan-D. person name Schaefer-A. person name Stabb-E. person name Stevens-A. person name Visick-K. person name Whistler-C. person name Greenberg-E.P. dbReference id 15703294 type PubMed dbReference id 10.1073/pnas.0409900102 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain ATCC-700601-/-ES114 reference key 2 citation date 2017 first 10250 last 10261 name J.-Biol.-Chem. type journal-article volume 292 title Model-enabled-gene-search-(MEGS)-allows-fast-and-direct-discovery-of-enzymatic-and-transport-gene-functions-in-the-marine-bacterium-Vibrio-fischeri. authorList person name Pan-S. person name Nikolakakis-K. person name Adamczyk-P.A. person name Pan-M. person name Ruby-E.G. person name Reed-J.L. dbReference id 28446608 type PubMed dbReference id 10.1074/jbc.m116.763193 type DOI scope FUNCTION source strain ATCC-700601-/-ES114 comment type function text evidence 2 Seems-to-be-involved-in-glutamine-transport.-Complements-an-E.coli-glnP-deletion-mutant. comment type subcellular-location subcellularLocation location evidence 3 Cell-inner-membrane topology evidence 1 Multi-pass-membrane-protein comment type similarity text evidence 3 Belongs-to-the-amino-acid/polyamine-transporter-2-family. dbReference id CP000020 type EMBL property type protein-sequence-ID value AAW85667.1 property type molecule-type value Genomic_DNA dbReference id WP_011261794.1 type RefSeq property type nucleotide-sequence-ID value NC_006840.2 dbReference id YP_204555.1 type RefSeq property type nucleotide-sequence-ID value NC_006840.2 dbReference id Q5E5M9 type AlphaFoldDB dbReference id Q5E5M9 type SMR dbReference id 312309.VF_1172 type STRING dbReference id AAW85667 type EnsemblBacteria property type protein-sequence-ID value AAW85667 property type gene-ID value VF_1172 dbReference id vfi:VF_1172 type KEGG dbReference id fig|312309.11.peg.1179 type PATRIC dbReference id COG0814 type eggNOG property type taxonomic-scope value Bacteria dbReference id CLU_038102_3_0_6 type HOGENOM dbReference id FSAKNEY type OMA dbReference id 18749at2 type OrthoDB dbReference id UP000000537 type Proteomes property type component value Chromosome-I dbReference id GO:0005886 type GO property type term value C:plasma-membrane property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0015173 type GO property type term value F:aromatic-amino-acid-transmembrane-transporter-activity property type evidence value ECO:0007669 property type project value InterPro dbReference id 1.20.1740.10 type Gene3D property type entry-name value Amino-acid/polyamine-transporter-I property type match-status value 1 dbReference id IPR018227 type InterPro property type entry-name value Amino_acid_transport_2 dbReference id IPR013059 type InterPro property type entry-name value Trp_tyr_transpt dbReference id PTHR46997 type PANTHER property type entry-name value LOW-AFFINITY-TRYPTOPHAN-PERMEASE-RELATED property type match-status value 1 dbReference id PTHR46997:SF2 type PANTHER property type entry-name value TYROSINE-SPECIFIC-TRANSPORT-PROTEIN property type match-status value 1 dbReference id PF03222 type Pfam property type entry-name value Trp_Tyr_perm property type match-status value 1 dbReference id PR00166 type PRINTS property type entry-name value AROAAPRMEASE proteinExistence type inferred-from-homology keyword id KW-0029 Amino-acid-transport keyword id KW-0997 Cell-inner-membrane keyword id KW-1003 Cell-membrane keyword id KW-0472 Membrane keyword id KW-1185 Reference-proteome keyword id KW-0812 Transmembrane keyword id KW-1133 Transmembrane-helix keyword id KW-0813 Transport feature description Glutamine-transporter-2 id PRO_0000440878 type chain location begin position 1 end position 388 feature description Helical evidence 1 type transmembrane-region location begin position 5 end position 27 feature description Helical evidence 1 type transmembrane-region location begin position 31 end position 53 feature description Helical evidence 1 type transmembrane-region location begin position 86 end position 106 feature description Helical evidence 1 type transmembrane-region location begin position 121 end position 141 feature description Helical evidence 1 type transmembrane-region location begin position 147 end position 167 feature description Helical evidence 1 type transmembrane-region location begin position 186 end position 206 feature description Helical evidence 1 type transmembrane-region location begin position 218 end position 238 feature description Helical evidence 1 type transmembrane-region location begin position 268 end position 288 feature description Helical evidence 1 type transmembrane-region location begin position 302 end position 322 feature description Helical evidence 1 type transmembrane-region location begin position 326 end position 346 feature description Helical evidence 1 type transmembrane-region location begin position 368 end position 388 evidence key 1 type ECO:0000255 evidence key 2 type ECO:0000269 source dbReference id 28446608 type PubMed evidence key 3 type ECO:0000305 evidence key 4 type ECO:0000312 source dbReference id AAW85667.1 type EMBL sequence checksum 230F2EA5CC4D8741 length 388 mass 42367 modified 2005-03-15 version 1 MNFKLFGSALILSGTALGAGMLAIPMVLAQFGLFYSTLLMLIICAGTTYAALLLTEACSKTELAFGINTVANKTIGKGGQLVTNALFYLLLFCMLIAYILGAADLIKRIFSMMNVEMSIEFAQVAFTLFASAFVVCGTQIIDKLNRLLFFFMISMLVLTLIILIPGMTVENLSQVTNHDKGMLFDTSTILFTSFASMPVIPSLVAYNKEATKQQLRNMVILGSIIPLICYLVWLYAVVGNLTANEITHFSNISDLIQTFSAKNEYIEIILSIFTSLALLTSFLGVAMALYNQNKDMISHNKIVTYVCTFILPLLGAGLAADQFLSVLGYAGVILVFLAIFIPLAMVVTLRKKETEEVHQNLHIYTAEGGKLALGLTLLFGLLLLISQI 
entry created 2017-12-20 dataset Swiss-Prot modified 2023-02-22 version 30 accession I6NXV7 name GREA_SUIGR protein recommendedName fullName Atromentin-synthetase-greA ecNumber 2.3.1.- alternativeName fullName Nonribosomal-peptide-synthase-like-enzyme-greA shortName NRPS-like gene name type primary greA organism name type scientific Suillus-grevillei name type common Larch-bolete name type synonym Boletus-elegans dbReference id 5382 type NCBI-Taxonomy lineage taxon Eukaryota taxon Fungi taxon Dikarya taxon Basidiomycota taxon Agaricomycotina taxon Agaricomycetes taxon Agaricomycetidae taxon Boletales taxon Suillineae taxon Suillaceae taxon Suillus reference key 1 citation date 2012 first 1798 last 1804 name ChemBioChem type journal-article volume 13 title Characterization-of-the-Suillus-grevillei-quinone-synthetase-GreA-supports-a-nonribosomal-code-for-aromatic-alpha-keto-acids. authorList person name Wackler-B. person name Lackner-G. person name Chooi-Y.H. person name Hoffmeister-D. dbReference id 22730234 type PubMed dbReference id 10.1002/cbic.201200187 type DOI scope NUCLEOTIDE-SEQUENCE-[GENOMIC-DNA] scope FUNCTION scope BIOPHYSICOCHEMICAL-PROPERTIES source strain DSM-8404 comment type function text evidence 3 An-L-tyrosine:2-oxoglutarate-aminotransferase-and-atromentin-synthetase-greA-catalyze-consecutive-steps-to-turn-over-L-tyrosine-into-atromentin,-which-represents-the-generic-precursor-molecule-for-the-entire-terphenylquinone-and-pulvinic-acid-family-of-pigments,-which-are-widely-distributed-secondary-metabolites-in-homobasidiomycetes.-The-first-step-catalyzed-by-the-aminotransferase-converts-L-tyrosine-in-to-4-hydroxyphenylpyruvate-(4-HPP).-Adenylation-of-two-4-HPP-monomers-by-the-greA-adenylation-(A)-domain,-covalent-tethering-of-the-monomers-as-a-thioester-and-oxoester-onto-the-greA-thiolation-(T)-and-thioesterase-(TE)-domains,-respectively,-and-symmetric-C-C-bond-formation-between-two-monomers-catalyzed-by-the-greA-TE-domain-leads-to-atromentin. comment type biophysicochemical-properties phDependence text evidence 3 Optimum-pH-is-7.5. temperatureDependence text evidence 3 Optimum-temperature-is-23-degrees-Celsius. comment type pathway text evidence 5 Secondary-metabolite-biosynthesis. comment type similarity text evidence 4 Belongs-to-the-ATP-dependent-AMP-binding-enzyme-family. dbReference id 2.3.1.- type EC dbReference id JQ681152 type EMBL property type protein-sequence-ID value AFB76152.1 property type molecule-type value Genomic_DNA dbReference id I6NXV7 type AlphaFoldDB dbReference id I6NXV7 type SMR dbReference id suigr-grea type ESTHER property type family-name value Thioesterase dbReference id MetaCyc:MON-18723 type BioCyc 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 GO:0009058 type GO property type term value P:biosynthetic-process property type evidence value ECO:0007669 property type project value InterPro dbReference id 3.30.300.30 type Gene3D property type match-status value 1 dbReference id 1.10.1200.10 type Gene3D property type entry-name value ACP-like property type match-status value 1 dbReference id 3.40.50.1820 type Gene3D property type entry-name value alpha/beta-hydrolase property type match-status value 1 dbReference id 3.40.50.12780 type Gene3D property type entry-name value N-terminal-domain-of-ligase-like property type match-status value 1 dbReference id IPR029058 type InterPro property type entry-name value AB_hydrolase dbReference id IPR036736 type InterPro property type entry-name value ACP-like_sf dbReference id IPR045851 type InterPro property type entry-name value AMP-bd_C_sf dbReference id IPR020845 type InterPro property type entry-name value AMP-binding_CS dbReference id IPR000873 type InterPro property type entry-name value AMP-dep_Synth/Lig dbReference id IPR042099 type InterPro property type entry-name value ANL_N_sf dbReference id IPR020802 type InterPro property type entry-name value PKS_thioesterase dbReference id IPR009081 type InterPro property type entry-name value PP-bd_ACP dbReference id IPR001031 type InterPro property type entry-name value Thioesterase dbReference id PTHR43767 type PANTHER property type entry-name value LONG-CHAIN-FATTY-ACID--COA-LIGASE property type match-status value 1 dbReference id PTHR43767:SF10 type PANTHER property type entry-name value SURFACTIN-SYNTHASE-SUBUNIT-1 property type match-status value 1 dbReference id PF00501 type Pfam property type entry-name value AMP-binding property type match-status value 1 dbReference id PF00550 type Pfam property type entry-name value PP-binding property type match-status value 1 dbReference id PF00975 type Pfam property type entry-name value Thioesterase property type match-status value 1 dbReference id SM00824 type SMART property type entry-name value PKS_TE property type match-status value 1 dbReference id SSF56801 type SUPFAM property type entry-name value Acetyl-CoA-synthetase-like property type match-status value 1 dbReference id SSF47336 type SUPFAM property type entry-name value ACP-like 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 dbReference id PS00455 type PROSITE property type entry-name value AMP_BINDING property type match-status value 1 dbReference id PS50075 type PROSITE property type entry-name value CARRIER property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0596 Phosphopantetheine keyword id KW-0597 Phosphoprotein keyword id KW-0808 Transferase feature description Atromentin-synthetase-greA id PRO_0000442627 type chain location begin position 1 end position 958 feature description Carrier evidence 2 type domain location begin position 597 end position 675 feature description Adenylation-(A)-domain evidence 1 type region-of-interest location begin position 60 end position 465 feature description Thiolation-and-peptide-carrier-(T)-domain evidence 1 type region-of-interest location begin position 602 end position 672 feature description Thioesterase-(TE)-domain evidence 1 type region-of-interest location begin position 698 end position 946 feature description O-(pantetheine-4'-phosphoryl)serine evidence 2 type modified-residue location position position 634 evidence key 1 type ECO:0000255 evidence key 2 type ECO:0000255 source dbReference id PRU00258 type PROSITE-ProRule evidence key 3 type ECO:0000269 source dbReference id 22730234 type PubMed evidence key 4 type ECO:0000305 evidence key 5 type ECO:0000305 source dbReference id 22730234 type PubMed sequence checksum 71F44FA4E9DDCFC7 length 958 mass 104883 modified 2012-10-03 version 1 MASIAVTTTTTTTTAEFVTSPRTSIVPEQPNTLHDVIAQAVDSYPLHELGFITSSAHDSSIQTKTFSAFNQYVRNLARAMLEWGKPTGSVVVVYLTEHEDNMTAVWACLLAGFVPCLQPALSAQQAHKEGHVAHIKNLFGSATWLTSELGAEQINSISGLEVHLLSELKSSAEKFTVAADWVAYEAKPDDEAILFLTSGSTGFSKAVVHTHRTILAACRAKGQSYGLTSESQVLNWVGFDHVAGSLEMHITPLLYGASQLHVHASAILADPLRLLRLIDEKSIELAFAPNFLLSKLTRDLEKRTDLFGSFDLSSIKRINSGGEAVVSKTAQAFAATMKQLSKNPSAVSFVISAGFGMTETCAGCIYDPVDVLKNKPAHEFLDLGRPINGCEMRIVDPEDGATLRPDGESGELQVRGPMVFVRYYNNAEATSSSFVEGGWYRTGDVGIIENGVMRLSGRIKDTVIVHGVSYGIPELETYLQTVEGVTHSFLAAAPYRAPGQETEGFIIFYSPTFDLNGADASTKLFATHRALRDICVKMITLPPQFVVPIPVNQMEKTTLGKLSRARLISLFKQGQLAQHIARSEELLSEARGATFVAPSTETEKALAKIYAGIFNLAESEMSASDNFFELGGTSIDVIRLKREGEAHFGLPEIPTIQILKHPVVSSLANYVNALLSKDSQTEEYDPIVPLQLTGNKTPIFFVHPGVGEVLIFVNLAKYFQNERPFYALRARGFEPGHPFFTSMDEMVSCYAAAVKRTQATGPYAIAGYSYGGVVAFEVAKRLEAMGDEVKFTGLINIPPHIADRMHEIDWTGGMLNLSYFLGLVSKHDANDLAPALRPMTRNEQLEVVWKLSPPERLVELQLTPGKLDHWVDIAGSLIECGKDYNPSGSVSAVDVFYAIPLRGSKADWLNNQLKPWSGFSRGDASYTDVPGQHYTLMDFDHVPQFQKIFRGRLEARGL 
entry created 2018-07-18 dataset Swiss-Prot modified 2023-02-22 version 19 accession V5XKK6 name AFT8_ALTAL protein recommendedName fullName evidence 1 Putative-epoxide-hydrolase-AFT8 ecNumber evidence 1 3.-.-.- alternativeName fullName evidence 7 AF-toxin-biosynthesis-protein-8 gene name evidence 7 type primary AFT8 organism name type scientific Alternaria-alternata name type common Alternaria-rot-fungus name type synonym Torula-alternata dbReference id 5599 type NCBI-Taxonomy lineage taxon Eukaryota taxon Fungi taxon Dikarya taxon Ascomycota taxon Pezizomycotina taxon Dothideomycetes taxon Pleosporomycetidae taxon Pleosporales taxon Pleosporineae taxon Pleosporaceae taxon Alternaria taxon Alternaria-sect.-Alternaria taxon Alternaria-alternata-complex reference key 1 citation date 2013-11 db EMBL/GenBank/DDBJ-databases type submission title The-gene-cluster-involved-in-AF-toxin-biosynthesis-of-Alternaria-alternata. authorList person name Kondou-H. person name Hara-A. person name Mase-C. person name Harimoto-Y. person name Tsuge-T. scope NUCLEOTIDE-SEQUENCE-[GENOMIC-DNA] source strain NAF8 reference key 2 citation date 2002 first 59 last 70 name Genetics type journal-article volume 161 title A-conditionally-dispensable-chromosome-controls-host-specific-pathogenicity-in-the-fungal-plant-pathogen-Alternaria-alternata. authorList person name Hatta-R. person name Ito-K. person name Hosaki-Y. person name Tanaka-T. person name Tanaka-A. person name Yamamoto-M. person name Akimitsu-K. person name Tsuge-T. dbReference id 12019223 type PubMed dbReference id 10.1093/genetics/161.1.59 type DOI scope FUNCTION source strain NAF8 reference key 3 citation date 2004 first 399 last 411 name Mol.-Microbiol. type journal-article volume 52 title Dissection-of-the-host-range-of-the-fungal-plant-pathogen-Alternaria-alternata-by-modification-of-secondary-metabolism. authorList person name Ito-K. person name Tanaka-T. person name Hatta-R. person name Yamamoto-M. person name Akimitsu-K. person name Tsuge-T. dbReference id 15066029 type PubMed dbReference id 10.1111/j.1365-2958.2004.04004.x type DOI scope FUNCTION source strain NAF8 reference key 4 citation date 2005 first 107 last 116 name J.-Gen.-Plant-Pathol. type journal-article volume 71 title Structural-analysis-of-cosmid-clone-pcAFT-2-carrying-AFT10-1-encoding-an-acyl-CoA-dehydrogenase-involved-in-AF-toxin-production-in-the-strawberry-pathotype-of-Alternaria-alternata. authorList person name Ruswandi-S. person name Kitani-K. person name Akimitsu-K. person name Tsuge-T. person name Shiraishi-T. person name Yamamoto-M. dbReference id 10.1007/s10327-004-0170-3 type DOI scope FUNCTION source strain NAF8 reference key 5 citation date 2008 first 1591 last 1599 name Mol.-Plant-Microbe-Interact. type journal-article volume 21 title Functional-analysis-of-a-multicopy-host-selective-ACT-toxin-biosynthesis-gene-in-the-tangerine-pathotype-of-Alternaria-alternata-using-RNA-silencing. authorList person name Miyamoto-Y. person name Masunaka-A. person name Tsuge-T. person name Yamamoto-M. person name Ohtani-K. person name Fukumoto-T. person name Gomi-K. person name Peever-T.L. person name Akimitsu-K. dbReference id 18986255 type PubMed dbReference id 10.1094/mpmi-21-12-1591 type DOI scope FUNCTION source strain NAF8 reference key 6 citation date 2013 first 44 last 66 name FEMS-Microbiol.-Rev. type journal-article volume 37 title Host-selective-toxins-produced-by-the-plant-pathogenic-fungus-Alternaria-alternata. authorList person name Tsuge-T. person name Harimoto-Y. person name Akimitsu-K. person name Ohtani-K. person name Kodama-M. person name Akagi-Y. person name Egusa-M. person name Yamamoto-M. person name Otani-H. dbReference id 22846083 type PubMed dbReference id 10.1111/j.1574-6976.2012.00350.x type DOI scope REVIEW-ON-HOST-SELECTIVE-TOXINS comment type function text evidence 2-3-4-5-6-9 Putative-epoxide-hydrolase;-part-of-the-gene-clusters-that-mediate-the-biosynthesis-of-the-host-selective-toxins-(HSTs)-AF-toxins-responsible-for-Alternaria-black-spot-of-strawberry-disease-by-the-strawberry-pathotype-(Probable).-AF-toxin-I-and-III-are-valine-derivatives-of-2,3-dyhydroxy-isovaleric-acid-and-2-hydroxy-isovaleric-acid-respectively,-while-AF-II-is-an-isoleucine-derivative-of-2-hydroxy-valeric-acid-(PubMed:15066029,-Ref.4,-PubMed:22846083).-These-derivatives-are-bound-to-a-9,10-epoxy-8-hydroxy-9-methyl-decatrienoic-acid-(EDA)-moiety-(PubMed:15066029,-Ref.4,-PubMed:22846083).-On-cellular-level,-AF-toxins-affect-plasma-membrane-of-susceptible-cells-and-cause-a-sudden-increase-in-loss-of-K(+)-after-a-few-minutes-of-toxin-treatment-(PubMed:22846083).-The-aldo-keto-reductase-AFTS1-catalyzes-the-conversion-of-2-keto-isovaleric-acid-(2-KIV)-to-2-hydroxy-isovaleric-acid-(2-HIV)-by-reduction-of-its-ketone-to-an-alcohol-(PubMed:15066029).-The-acyl-CoA-ligase-AFT1,-the-hydrolase-AFT2-and-the-enoyl-CoA-hydratases-AFT3-and-AFT6,-but-also-the-polyketide-synthase-AFT9,-the-acyl-CoA-dehydrogenase-AFT10,-the-cytochrome-P450-monooxygenase-AFT11-and-the-oxidoreductase-AFT12-are-all-involved-in-the-biosynthesis-of-the-AK-,-AF--and-ACT-toxin-common-EDA-structural-moiety-(PubMed:12019223,-Ref.4,-PubMed:18986255).-The-exact-function-of-each-enzyme,-and-of-additional-enzymes-identified-within-the-AF-toxin-clusters-have-still-to-be-determined-(PubMed:12019223,-Ref.4,-PubMed:18986255). comment type pathway text evidence 8 Mycotoxin-biosynthesis. comment type miscellaneous text evidence 2 Gene-clusters-encoding-host-selective-toxins-(HSTs)-are-localized-on-conditionally-dispensable-chromosomes-(CDCs),-also-called-supernumerary-chromosomes,-where-they-are-present-in-multiple-copies-(PubMed:12019223).-The-CDCs-are-not-essential-for-saprophytic-growth-but-controls-host-selective-pathogenicity-(PubMed:12019223). comment type similarity text evidence 8 Belongs-to-the-peptidase-S33-family. dbReference evidence 1 id 3.-.-.- type EC dbReference id AB873047 type EMBL property type protein-sequence-ID value BAO05507.1 property type molecule-type value Genomic_DNA dbReference id V5XKK6 type AlphaFoldDB dbReference id V5XKK6 type SMR dbReference id altal-aft8 type ESTHER property type family-name value Epoxide_hydrolase dbReference id FungiDB:CC77DRAFT_801013 type VEuPathDB dbReference id GO:0016787 type GO property type term value F:hydrolase-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 IPR010497 type InterPro property type entry-name value Epoxide_hydro_N dbReference id PTHR21661 type PANTHER property type entry-name value EPOXIDE-HYDROLASE-1-RELATED property type match-status value 1 dbReference id PTHR21661:SF39 type PANTHER property type entry-name value HYDROLASE,-PUTATIVE-(AFU_ORTHOLOGUE-AFUA_3G08960)-RELATED property type match-status value 1 dbReference id PF06441 type Pfam property type entry-name value EHN 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 inferred-from-homology keyword id KW-0378 Hydrolase keyword id KW-0843 Virulence feature description Putative-epoxide-hydrolase-AFT8 id PRO_0000444844 type chain location begin position 1 end position 402 evidence key 1 type ECO:0000250 source dbReference id M2WIS5 type UniProtKB evidence key 2 type ECO:0000269 source dbReference id 12019223 type PubMed evidence key 3 type ECO:0000269 source dbReference id 15066029 type PubMed evidence key 4 type ECO:0000269 source dbReference id 18986255 type PubMed evidence key 5 type ECO:0000269 source ref 4 evidence key 6 type ECO:0000303 source dbReference id 22846083 type PubMed evidence key 7 type ECO:0000303 source ref 1 evidence key 8 type ECO:0000305 evidence key 9 type ECO:0000305 source ref 1 sequence checksum F71C6EBD956CA692 length 402 mass 44371 modified 2014-02-19 version 1 MASYKNIPSTAKGSPISFDFSFPQPKLDHLRQVLELHPLGREAPSKTLRGSSKPQWFGNAKEIMRRFDWAAEEELLKAFPHYVVGVEDTIGGQMLQVHFVALFSTSPDAIPVLLIHSWFSSYVEYLCLLSVFTERFPQACDLPFHVIVPSLPGYDFSSPLSRETNNAQINEDNARVLNQLMVNLGFGAGSGGIGGYVVHGGVSSLRMCYTLAKEYKDCRALHANLDGAYRHTLTSSGGDEFEAVKSVLAELHPPEDWDSHERDMIRLAISTSPVSLLALIGSQFFGEQEQGAALRMVALIVAHHWMTDTYPDASQESYCIKDMSAEDLSHVLKHTGLEPNKPVGISFFSHGQGSASDIRPIVDGSSWSSRHEGNPFVAVLDQPNQTVGDLLGFVRQVQKQHS 
entry created 2020-04-22 dataset Swiss-Prot modified 2023-02-22 version 12 accession A0A4V1FW34 name PYIG_MAGGR protein recommendedName fullName evidence 5 Pyrichalasin-C-7-hydroxylase ecNumber evidence 7 1.-.-.- alternativeName fullName evidence 5 Cytochrome-P450-monooxygenase-pyiG alternativeName fullName evidence 5 Pyrichalasin-H-biosynthesis-cluster-protein-G gene name evidence 5 type primary pyiG organism name type scientific Magnaporthe-grisea name type common Crabgrass-specific-blast-fungus name type synonym Pyricularia-grisea dbReference id 148305 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 2019 first 4163 last 4167 name Org.-Lett. type journal-article volume 21 title Targeted-gene-inactivations-expose-silent-cytochalasans-in-Magnaporthe-grisea-NI980. authorList person name Wang-C. person name Hantke-V. person name Cox-R.J. person name Skellam-E. dbReference id 31099577 type PubMed dbReference id 10.1021/acs.orglett.9b01344 type DOI scope NUCLEOTIDE-SEQUENCE-[GENOMIC-DNA] scope FUNCTION scope DISRUPTION-PHENOTYPE scope PATHWAY source strain NI980 reference key 2 citation date 2019 first 8756 last 8760 name Org.-Lett. type journal-article volume 21 title Investigating-the-function-of-cryptic-cytochalasan-cytochrome-P450-monooxygenases-using-combinatorial-biosynthesis. authorList person name Wang-C. person name Becker-K. person name Pfuetze-S. person name Kuhnert-E. person name Stadler-M. person name Cox-R.J. person name Skellam-E. dbReference id 31644300 type PubMed dbReference id 10.1021/acs.orglett.9b03372 type DOI scope FUNCTION reference key 3 citation date 2020 first 2925 last 2928 name Chem.-Commun.-(Camb.) type journal-article volume 56 title Evidence-for-enzyme-catalysed-intramolecular-[4+2]-Diels-Alder-cyclization-during-the-biosynthesis-of-pyrichalasin-H. authorList person name Hantke-V. person name Skellam-E.J. person name Cox-R.J. dbReference id 32039410 type PubMed dbReference id 10.1039/c9cc09590j type DOI scope FUNCTION comment type function text evidence 3-4-8 Cytochrome-P450-monooxygenase;-part-of-the-gene-cluster-that-mediates-the-biosynthesis-of-the-mycotoxin-pyrichalasin-H,-a-tyrosine-derived-cytochalasan-that-inhibits-the-growth-of-rice-seedlings,-but-also-inhibits-lymphocyte-capping-and-actin-polymerization-and-alters-cell-morphology-(PubMed:31099577)-(Probable).-Pyrichalasin-H-is-indicated-as-the-responsible-agent-for-the-genus-specific-pathogenicity-of-M.grisea-toward-crabgrass-(PubMed:31099577).-The-first-step-in-the-pathway-is-catalyzed-by-the-O-methyltransferase-pyiA-which-methylates-free-tyrosine-to-generate-the-precursor-O-methyltyrosine-(PubMed:31099577).-The-hybrid-PKS-NRPS-pyiS,-assisted-by-the-enoyl-reductase-pyiC,-are-responsible-for-fusion-of-the-O-methyltyrosine-precursor-and-the-polyketide-backbone-(PubMed:31099577).-The-polyketide-synthase-module-(PKS)-of-pyiS-is-responsible-for-the-synthesis-of-the-polyketide-backbone-and-the-downstream-nonribosomal-peptide-synthetase-(NRPS)-amidates-the-carboxyl-end-of-the-polyketide-with-the-O-methyltyrosine-precursor-(PubMed:31099577).-As-the-NRPS-A-domain-demonstrates-substrate-tolerance,-pyiS-can-also-use-phenylalanine,-tyrosine-and-even-para-chlorophenylalanine-as-amino-acid-precursor,-which-leads-to-the-production-of-novel-cytochalasans,-including-halogenated-cytochalasans-(PubMed:31099577).-Because-pyiS-lacks-a-designated-enoylreductase-(ER)-domain,-the-required-activity-is-provided-the-enoyl-reductase-pyiC-(PubMed:31099577).-Reduction-by-the-hydrolyase-pyiE-leads-to-1,5-dihydropyrrolone,-which-is-substrate-for-dehydration-and-intra-molecular-Diels-Alder-cyclization-by-the-Diels-Alderase-pyiF-to-yield-the-required-isoindolone-fused-macrocycle-(PubMed:32039410).-The-tailoring-cytochrome-P450-monooxygenases-piyD-and-piyG-catalyze-the-hydroxylation-at-C-18-and-C-7,-respectivily,-whereas-the-short-chain-dehydrogenase/reductase-pyiH-reduces-the-carbonyl-at-C-21-in-preparation-for-the-transfer-of-an-acetyl-group-by-the-acetyltransferase-pyiB-(PubMed:31099577).-These-3-reactions-whose-order-is-not-clear-yet,-lead-to-the-production-of-O-methylpyrichalasin-J,-a-deacetylated-pyrichalasin-H-(PubMed:31099577).-Finally,-pyiB-to-converts-O-methylpyrichalasin-J-into-the-final-product-pyrichalasin-H-via-acetylation-of-C-21-(PubMed:31099577). comment type cofactor cofactor evidence 1 name heme dbReference id CHEBI:30413 type ChEBI comment type pathway text evidence 7 Mycotoxin-biosynthesis. comment type disruption-phenotype text evidence 3 Leads-to-the-loss-of-pyrichalasin-H-production,-but-accumulates-novel-cytochalasans,-all-lacking-a-hydroxyl-group-at-C-7. comment type similarity text evidence 6 Belongs-to-the-cytochrome-P450-family. dbReference evidence 7 id 1.-.-.- type EC dbReference id MK801691 type EMBL property type protein-sequence-ID value QCS37514.1 property type molecule-type value Genomic_DNA dbReference id A0A4V1FW34 type AlphaFoldDB dbReference id A0A4V1FW34 type SMR dbReference id UP000515153 type Proteomes property type component value Genome-assembly dbReference id GO:0020037 type GO property type term value F:heme-binding property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0005506 type GO property type term value F:iron-ion-binding property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0004497 type GO property type term value F:monooxygenase-activity property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0016705 type GO property type term value F:oxidoreductase-activity,-acting-on-paired-donors,-with-incorporation-or-reduction-of-molecular-oxygen property type evidence value ECO:0007669 property type project value InterPro dbReference id 1.10.630.10 type Gene3D property type entry-name value Cytochrome-P450 property type match-status value 1 dbReference id IPR001128 type InterPro property type entry-name value Cyt_P450 dbReference id IPR017972 type InterPro property type entry-name value Cyt_P450_CS dbReference id IPR002403 type InterPro property type entry-name value Cyt_P450_E_grp-IV dbReference id IPR036396 type InterPro property type entry-name value Cyt_P450_sf dbReference id PTHR46206 type PANTHER property type entry-name value CYTOCHROME-P450 property type match-status value 1 dbReference id PTHR46206:SF7 type PANTHER property type entry-name value ENT-KAURENE-OXIDASE property type match-status value 1 dbReference id PF00067 type Pfam property type entry-name value p450 property type match-status value 1 dbReference id PR00465 type PRINTS property type entry-name value EP450IV dbReference id SSF48264 type SUPFAM property type entry-name value Cytochrome-P450 property type match-status value 1 dbReference id PS00086 type PROSITE property type entry-name value CYTOCHROME_P450 property type match-status value 1 proteinExistence type inferred-from-homology keyword id KW-0349 Heme keyword id KW-0408 Iron keyword id KW-0479 Metal-binding keyword id KW-0503 Monooxygenase keyword id KW-0560 Oxidoreductase keyword id KW-1185 Reference-proteome keyword id KW-0732 Signal feature evidence 2 type signal-peptide location begin position 1 end position 17 feature description Pyrichalasin-C-7-hydroxylase id PRO_0000449435 type chain location begin position 18 end position 504 feature description axial-binding-residue evidence 1 type binding-site location position position 449 ligand name heme dbReference id CHEBI:30413 type ChEBI ligandPart name Fe dbReference id CHEBI:18248 type ChEBI evidence key 1 type ECO:0000250 source dbReference id P04798 type UniProtKB evidence key 2 type ECO:0000255 evidence key 3 type ECO:0000269 source dbReference id 31099577 type PubMed evidence key 4 type ECO:0000269 source dbReference id 32039410 type PubMed evidence key 5 type ECO:0000303 source dbReference id 31099577 type PubMed evidence key 6 type ECO:0000305 evidence key 7 type ECO:0000305 source dbReference id 31099577 type PubMed evidence key 8 type ECO:0000305 source dbReference id 31644300 type PubMed sequence checksum 647784166A085A71 length 504 mass 57662 modified 2019-07-31 precursor true version 1 MLNSAACIVLAITAVLGRMIYTHFYSNTCAAMKRALAHIPELHFEEDDTPERYRTETRSLVRKGYERYLQYGIPFQMRNPVSELGNQVVLPVKYLEEVKRAPRSLYSFEAFSEKVFLLKYIDAPRQTDALLYAVKLDINKNMDHILNGLWDETQVLLKETVPVTGQITIPGGELACNIIARTMSYVLVGPSLCRNPEWTKIAIEATFALVAGTQGLRDRYSPGWRWLARFQRSSEKLGEVREKAMELIKPLHEERMKALKDDSGQFRNFYDTIFWTMNKRKVDRSLRAIVDQQLFLTLASIHTTAGTLQSILCDWLAHPEYHDEILAEINERLAAFKGAGGKWTQQEVNEMKKLDSFMKESTRVNPVGCMTVQRYAQRTHTFSDGFVLPAGTIFQFPSDAVHHDPKLFPDPEKFDGHRFLRLREKDANAYHYGYVSDTTLNWGAGTHACPGRFLATYVLKFAFIALITQYDLSFPEGTGKPGYFYFDNSVRIDPTAKLDIKKSS 
entry created 2020-06-17 dataset Swiss-Prot modified 2023-02-22 version 66 accession O04925 name OLEH2_SESIN protein recommendedName fullName evidence 7 Oleosin-H2 alternativeName fullName evidence 7-8 Oleosin-15.5-kDa organism evidence 11 name type scientific Sesamum-indicum name type common Oriental-sesame name type synonym Sesamum-orientale dbReference id 4182 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 asterids taxon lamiids taxon Lamiales taxon Pedaliaceae taxon Sesamum reference evidence 11 key 1 citation date 1997 first 819 last 824 name J.-Biochem. type journal-article volume 122 title Cloning,-expression-and-isoform-classification-of-a-minor-oleosin-in-sesame-oil-bodies. authorList person name Chen-J.C. person name Lin-R.H. person name Huang-H.C. person name Tzen-J.T. dbReference id 9399587 type PubMed dbReference id 10.1093/oxfordjournals.jbchem.a021828 type DOI scope NUCLEOTIDE-SEQUENCE-[MRNA] scope SUBCELLULAR-LOCATION scope TISSUE-SPECIFICITY source strain evidence 8 cv.-Tainan-1 tissue evidence 8 Seed reference key 2 citation date 2002 first 2146 last 2153 name Biosci.-Biotechnol.-Biochem. type journal-article volume 66 title Gene-family-of-oleosin-isoforms-and-their-structural-stabilization-in-sesame-seed-oil-bodies. authorList person name Tai-S.S. person name Chen-M.C. person name Peng-C.C. person name Tzen-J.T. dbReference id 12450125 type PubMed dbReference id 10.1271/bbb.66.2146 type DOI scope SUBCELLULAR-LOCATION scope TISSUE-SPECIFICITY scope DEVELOPMENTAL-STAGE comment type function text evidence 9 May-have-a-structural-role-to-stabilize-the-lipid-body-during-desiccation-of-the-seed-by-preventing-coalescence-of-the-oil.-Probably-interacts-with-both-lipid-and-phospholipid-moieties-of-lipid-bodies.-May-also-provide-recognition-signals-for-specific-lipase-anchorage-in-lipolysis-during-seedling-growth. comment type subcellular-location subcellularLocation location evidence 3-5-6 Lipid-droplet subcellularLocation location evidence 3 Membrane topology evidence 3 Multi-pass-membrane-protein text evidence 9 Surface-of-oil-bodies.-Oleosins-exist-at-a-monolayer-lipid/water-interface. comment type tissue-specificity text evidence 5-6 Expressed-in-seeds-(at-protein-level). comment type developmental-stage text evidence 5 Expressed-during-seed-maturation.-Expressed-in-maturing-seeds-about-2-and-half-weeks-after-flowering.-Expression-continues-steadily-thereafter-until-it-decreases-in-the-seed-drying-stage,-reaching-undetectable-levels-in-mature-seeds. comment type domain text evidence 9 The-proline-knot-motif-may-be-involved-in-the-targeting-to-oil-bodies. comment type similarity text evidence 3 Belongs-to-the-oleosin-family. dbReference id U97700 type EMBL property type protein-sequence-ID value AAB58402.1 property type molecule-type value mRNA dbReference id JC5703 type PIR property type entry-name value JC5703 dbReference id O04925 type AlphaFoldDB dbReference id UP000504604 type Proteomes property type component value Genome-assembly dbReference id GO:0016020 type GO property type term value C:membrane property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0012511 type GO property type term value C:monolayer-surrounded-lipid-storage-body property type evidence value ECO:0000314 property type project value UniProtKB dbReference id GO:0034389 type GO property type term value P:lipid-droplet-organization property type evidence value ECO:0000305 property type project value UniProtKB dbReference id GO:0019915 type GO property type term value P:lipid-storage property type evidence value ECO:0000305 property type project value UniProtKB dbReference id GO:0010431 type GO property type term value P:seed-maturation property type evidence value ECO:0000270 property type project value UniProtKB dbReference id IPR000136 type InterPro property type entry-name value Oleosin dbReference id PTHR33203 type PANTHER property type entry-name value OLEOSIN property type match-status value 1 dbReference id PTHR33203:SF44 type PANTHER property type entry-name value OLEOSIN-20.3-KDA property type match-status value 1 dbReference id PF01277 type Pfam property type entry-name value Oleosin property type match-status value 1 dbReference id PS00811 type PROSITE property type entry-name value OLEOSINS property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0007 Acetylation keyword id KW-0551 Lipid-droplet keyword id KW-0472 Membrane keyword id KW-1185 Reference-proteome keyword id KW-0812 Transmembrane keyword id KW-1133 Transmembrane-helix feature description Removed evidence 1 type initiator-methionine location position position 1 feature description Oleosin-H2 id PRO_0000449964 type chain location begin position 2 end position 144 feature description Helical evidence 2 type transmembrane-region location begin position 28 end position 48 feature description Helical evidence 2 type transmembrane-region location begin position 53 end position 73 feature description Helical evidence 2 type transmembrane-region location begin position 75 end position 95 feature description Disordered evidence 4 type region-of-interest location begin position 124 end position 144 feature description Proline-knot evidence 10 type short-sequence-motif location begin position 61 end position 72 feature description N-acetylalanine evidence 1 type modified-residue location position position 2 evidence key 1 type ECO:0000250 source dbReference id C3S7F0 type UniProtKB evidence key 2 type ECO:0000255 evidence key 3 type ECO:0000255 source dbReference id RU000540 type RuleBase evidence key 4 type ECO:0000256 source dbReference id MobiDB-lite type SAM evidence key 5 type ECO:0000269 source dbReference id 12450125 type PubMed evidence key 6 type ECO:0000269 source dbReference id 9399587 type PubMed evidence key 7 type ECO:0000303 source dbReference id 12450125 type PubMed evidence key 8 type ECO:0000303 source dbReference id 9399587 type PubMed evidence key 9 type ECO:0000305 evidence key 10 type ECO:0000305 source dbReference id 12450125 type PubMed evidence key 11 type ECO:0000312 source dbReference id AAB58402.1 type EMBL sequence checksum 43E6C011C29B7CF7 length 144 mass 15446 modified 1997-07-01 version 1 MADEPHDQRPTDVIKSYLPEKGPSTSQVLAVVTLFPLGAVLLCLAGLILTGTIIGLAVATPLFVIFSPILVPAALTIALAVTGFLTSGAFGITALSSISWLLNYVRRMRGSLPEQLDHARRRVQETVGQKTREAGQRSQDVIRP 
entry created 2020-08-12 dataset Swiss-Prot modified 2023-02-22 version 14 accession A0A2H5AIZ6 name NOMT_NARPS protein recommendedName fullName evidence 4 Norbelladine-4'-O-methyltransferase ecNumber evidence 1 2.1.1.336 gene name evidence 4 type primary N4OMT organism name type scientific Narcissus-pseudonarcissus name type common Daffodil dbReference id 39639 type NCBI-Taxonomy lineage taxon Eukaryota taxon Viridiplantae taxon Streptophyta taxon Embryophyta taxon Tracheophyta taxon Spermatophyta taxon Magnoliopsida taxon Liliopsida taxon Asparagales taxon Amaryllidaceae taxon Amaryllidoideae taxon Narcissus reference key 1 citation date 2017 first 17356 last 17356 name Sci.-Rep. type journal-article volume 7 title Transcriptome-and-metabolome-profiling-of-Narcissus-pseudonarcissus-'King-Alfred'-reveal-components-of-Amaryllidaceae-alkaloid-metabolism. authorList person name Singh-A. person name Desgagne-Penix-I. dbReference id 29229969 type PubMed dbReference id 10.1038/s41598-017-17724-0 type DOI scope NUCLEOTIDE-SEQUENCE-[MRNA] scope FUNCTION scope REVIEW-ON-THE-AMARYLLIDACEAE-ALKALOID-METABOLISM scope PATHWAY scope TISSUE-SPECIFICITY scope GENE-FAMILY scope NOMENCLATURE source strain cv.-King-Alfred tissue Bulb comment type function text evidence 1-4 4'-O-methyltransferase-converting-norbelladine-to-4'-O-methylnorbelladine-(By-similarity).-4'-O-methylnorbelladine-is-a-precursor-to-all-Amaryllidaceae-alkaloids-such-as-galanthamine,-lycorine-and-haemanthamine,-and-including-haemanthamine--and-crinamine-type-alkaloids,-promising-anticancer-agents-(PubMed:29229969). comment type catalytic-activity reaction evidence 1 text norbelladine-+-S-adenosyl-L-methionine-=-4'-O-methylnorbelladine-+-H(+)-+-S-adenosyl-L-homocysteine dbReference id RHEA:51268 type Rhea dbReference id CHEBI:15378 type ChEBI dbReference id CHEBI:57856 type ChEBI dbReference id CHEBI:59789 type ChEBI dbReference id CHEBI:133993 type ChEBI dbReference id CHEBI:134001 type ChEBI dbReference id 2.1.1.336 type EC comment type cofactor cofactor evidence 1 name Mg(2+) dbReference id CHEBI:18420 type ChEBI comment type pathway text evidence 4 Alkaloid-biosynthesis. comment type tissue-specificity text evidence 3 Mostly-expressed-in-bulbs,-and,-to-a-lower-extent,-in-stems-and-roots. comment type similarity text evidence 5 Belongs-to-the-class-I-like-SAM-binding-methyltransferase-superfamily.-Cation-dependent-O-methyltransferase-family. dbReference evidence 1 id 2.1.1.336 type EC dbReference id MF416096 type EMBL property type protein-sequence-ID value AUG71941.1 property type molecule-type value mRNA dbReference id A0A2H5AIZ6 type AlphaFoldDB dbReference id A0A2H5AIZ6 type SMR 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:0008171 type GO property type term value F:O-methyltransferase-activity property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0009820 type GO property type term value P:alkaloid-metabolic-process property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0032259 type GO property type term value P:methylation property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id 3.40.50.150 type Gene3D property type entry-name value Vaccinia-Virus-protein-VP39 property type match-status value 1 dbReference id IPR029063 type InterPro property type entry-name value SAM-dependent_MTases_sf dbReference id IPR002935 type InterPro property type entry-name value SAM_O-MeTrfase dbReference id PTHR10509 type PANTHER property type entry-name value O-METHYLTRANSFERASE-RELATED property type match-status value 1 dbReference id PTHR10509:SF34 type PANTHER property type entry-name value TAPETUM-SPECIFIC-METHYLTRANSFERASE-1 property type match-status value 1 dbReference id PF01596 type Pfam property type entry-name value Methyltransf_3 property type match-status value 1 dbReference id SSF53335 type SUPFAM property type entry-name value S-adenosyl-L-methionine-dependent-methyltransferases property type match-status value 1 dbReference id PS51682 type PROSITE property type entry-name value SAM_OMT_I property type match-status value 1 proteinExistence type evidence-at-transcript-level keyword id KW-0017 Alkaloid-metabolism keyword id KW-0479 Metal-binding keyword id KW-0489 Methyltransferase keyword id KW-0949 S-adenosyl-L-methionine keyword id KW-0808 Transferase feature description Norbelladine-4'-O-methyltransferase id PRO_0000450641 type chain location begin position 1 end position 239 feature evidence 2 type binding-site location position position 55 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 2 type binding-site location position position 77 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 2 type binding-site location begin position 79 end position 80 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 2 type binding-site location position position 85 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 2 type binding-site location position position 103 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 2 type binding-site location position position 132 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 2 type binding-site location position position 155 ligand name a-divalent-metal-cation dbReference id CHEBI:60240 type ChEBI feature evidence 2 type binding-site location position position 157 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 2 type binding-site location position position 181 ligand name a-divalent-metal-cation dbReference id CHEBI:60240 type ChEBI feature evidence 2 type binding-site location position position 182 ligand name a-divalent-metal-cation dbReference id CHEBI:60240 type ChEBI evidence key 1 type ECO:0000250 source dbReference id A0A077EWA5 type UniProtKB evidence key 2 type ECO:0000255 source dbReference id PRU01019 type PROSITE-ProRule evidence key 3 type ECO:0000269 source dbReference id 29229969 type PubMed evidence key 4 type ECO:0000303 source dbReference id 29229969 type PubMed evidence key 5 type ECO:0000305 sequence checksum 9E516ADDDF3CA928 length 239 mass 27194 modified 2018-02-28 version 1 MGASQDDYSLVHKNILHSEDLLKYILETSAYPREHEQLKGLREVTEKHEWSSALVPADEGLFLSMLLKLMNAKRTIEIGVYTGYSLLTTALALPEDGKITAIDVNKSFFEIGLPFIQKAGVEHKINFIESEALPVLDQMLQEMKEEDLYDYAFVDADKSNYANYHERLVKLVRIGGAILYDNTLWYGSVAYPEYPGLYPEDEVDRLSFRNLNTFLAADPRVEISQVSIGDGVTICRRLY 
entry created 2020-08-12 dataset Swiss-Prot modified 2023-02-22 version 15 accession A0A077ES70 name NOMT4_NARAP protein recommendedName fullName evidence 4 Norbelladine-4'-O-methyltransferase-4 shortName evidence 4 NpN4OMT4 ecNumber evidence 1 2.1.1.336 gene name evidence 4 type primary N4OMT4 organism name type scientific Narcissus-aff.-pseudonarcissus-MK-2014 name type common Daffodil dbReference id 1540222 type NCBI-Taxonomy lineage taxon Eukaryota taxon Viridiplantae taxon Streptophyta taxon Embryophyta taxon Tracheophyta taxon Spermatophyta taxon Magnoliopsida taxon Liliopsida taxon Asparagales taxon Amaryllidaceae taxon Amaryllidoideae taxon Narcissus reference key 1 citation date 2014 first E103223 last E103223 name PLoS-ONE type journal-article volume 9 title Cloning-and-characterization-of-a-norbelladine-4'-O-methyltransferase-involved-in-the-biosynthesis-of-the-Alzheimer's-drug-galanthamine-in-Narcissus-sp.-aff.-pseudonarcissus. authorList person name Kilgore-M.B. person name Augustin-M.M. person name Starks-C.M. person name O'Neil-Johnson-M. person name May-G.D. person name Crow-J.A. person name Kutchan-T.M. dbReference id 25061748 type PubMed dbReference id 10.1371/journal.pone.0103223 type DOI scope NUCLEOTIDE-SEQUENCE-[MRNA] source strain cv.-Carlton tissue Bulb comment type function text evidence 1-2 4'-O-methyltransferase-converting-norbelladine-to-4'-O-methylnorbelladine-(By-similarity).-4'-O-methylnorbelladine-is-a-precursor-to-all-Amaryllidaceae-alkaloids-such-as-galanthamine,-lycorine-and-haemanthamine,-and-including-haemanthamine--and-crinamine-type-alkaloids,-promising-anticancer-agents-(By-similarity). comment type catalytic-activity reaction evidence 1 text norbelladine-+-S-adenosyl-L-methionine-=-4'-O-methylnorbelladine-+-H(+)-+-S-adenosyl-L-homocysteine dbReference id RHEA:51268 type Rhea dbReference id CHEBI:15378 type ChEBI dbReference id CHEBI:57856 type ChEBI dbReference id CHEBI:59789 type ChEBI dbReference id CHEBI:133993 type ChEBI dbReference id CHEBI:134001 type ChEBI dbReference id 2.1.1.336 type EC comment type cofactor cofactor evidence 1 name Mg(2+) dbReference id CHEBI:18420 type ChEBI comment type pathway text evidence 1 Alkaloid-biosynthesis. comment type similarity text evidence 5 Belongs-to-the-class-I-like-SAM-binding-methyltransferase-superfamily.-Cation-dependent-O-methyltransferase-family. dbReference evidence 1 id 2.1.1.336 type EC dbReference id KJ584564 type EMBL property type protein-sequence-ID value AIL54544.1 property type molecule-type value mRNA dbReference id A0A077ES70 type AlphaFoldDB dbReference id A0A077ES70 type SMR 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:0008171 type GO property type term value F:O-methyltransferase-activity property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0009820 type GO property type term value P:alkaloid-metabolic-process property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0032259 type GO property type term value P:methylation property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id 3.40.50.150 type Gene3D property type entry-name value Vaccinia-Virus-protein-VP39 property type match-status value 1 dbReference id IPR029063 type InterPro property type entry-name value SAM-dependent_MTases_sf dbReference id IPR002935 type InterPro property type entry-name value SAM_O-MeTrfase dbReference id PTHR10509 type PANTHER property type entry-name value O-METHYLTRANSFERASE-RELATED property type match-status value 1 dbReference id PTHR10509:SF34 type PANTHER property type entry-name value TAPETUM-SPECIFIC-METHYLTRANSFERASE-1 property type match-status value 1 dbReference id PF01596 type Pfam property type entry-name value Methyltransf_3 property type match-status value 1 dbReference id SSF53335 type SUPFAM property type entry-name value S-adenosyl-L-methionine-dependent-methyltransferases property type match-status value 1 dbReference id PS51682 type PROSITE property type entry-name value SAM_OMT_I property type match-status value 1 proteinExistence type evidence-at-transcript-level keyword id KW-0017 Alkaloid-metabolism keyword id KW-0479 Metal-binding keyword id KW-0489 Methyltransferase keyword id KW-0949 S-adenosyl-L-methionine keyword id KW-0808 Transferase feature description Norbelladine-4'-O-methyltransferase-4 id PRO_0000450644 type chain location begin position 1 end position 239 feature evidence 3 type binding-site location position position 55 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location position position 77 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location begin position 79 end position 80 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location position position 85 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location position position 103 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location position position 132 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location position position 155 ligand name a-divalent-metal-cation dbReference id CHEBI:60240 type ChEBI feature evidence 3 type binding-site location position position 157 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location position position 181 ligand name a-divalent-metal-cation dbReference id CHEBI:60240 type ChEBI feature evidence 3 type binding-site location position position 182 ligand name a-divalent-metal-cation dbReference id CHEBI:60240 type ChEBI evidence key 1 type ECO:0000250 source dbReference id A0A077EWA5 type UniProtKB evidence key 2 type ECO:0000250 source dbReference id A0A2H5AIZ6 type UniProtKB evidence key 3 type ECO:0000255 source dbReference id PRU01019 type PROSITE-ProRule evidence key 4 type ECO:0000303 source dbReference id 25061748 type PubMed evidence key 5 type ECO:0000305 sequence checksum B522D5166DB862E8 length 239 mass 27137 modified 2014-10-29 version 1 MGASIDDYCLIHKKILHSEDLLKYILETSAYPREHEQLKGLREVTEKHEWSSALVPADEGLFLSMLIKLMNAKRTIEIGVYTGYSLLTTALALPEDGKITAIDVNKSFFEIGLPFIQKAGVEHKINFIESEALPVLDQMLQETKEEDLYDYAFVDADKSNYANYHERLVKLVRIGGAILYDNTLWYGSVAYPEYPGLHPEEEVARLSFRNLNTFLAADPRVEISQVSIGDGVTICRRLY 
entry created 2020-08-12 dataset Swiss-Prot modified 2023-02-22 version 15 accession A0A077ESS0 name NOMT5_NARAP protein recommendedName fullName evidence 4 Norbelladine-4'-O-methyltransferase-5 shortName evidence 4 NpN4OMT5 ecNumber evidence 1 2.1.1.336 gene name evidence 4 type primary N4OMT5 organism name type scientific Narcissus-aff.-pseudonarcissus-MK-2014 name type common Daffodil dbReference id 1540222 type NCBI-Taxonomy lineage taxon Eukaryota taxon Viridiplantae taxon Streptophyta taxon Embryophyta taxon Tracheophyta taxon Spermatophyta taxon Magnoliopsida taxon Liliopsida taxon Asparagales taxon Amaryllidaceae taxon Amaryllidoideae taxon Narcissus reference key 1 citation date 2014 first E103223 last E103223 name PLoS-ONE type journal-article volume 9 title Cloning-and-characterization-of-a-norbelladine-4'-O-methyltransferase-involved-in-the-biosynthesis-of-the-Alzheimer's-drug-galanthamine-in-Narcissus-sp.-aff.-pseudonarcissus. authorList person name Kilgore-M.B. person name Augustin-M.M. person name Starks-C.M. person name O'Neil-Johnson-M. person name May-G.D. person name Crow-J.A. person name Kutchan-T.M. dbReference id 25061748 type PubMed dbReference id 10.1371/journal.pone.0103223 type DOI scope NUCLEOTIDE-SEQUENCE-[MRNA] source strain cv.-Carlton tissue Bulb comment type function text evidence 1-2 4'-O-methyltransferase-converting-norbelladine-to-4'-O-methylnorbelladine-(By-similarity).-4'-O-methylnorbelladine-is-a-precursor-to-all-Amaryllidaceae-alkaloids-such-as-galanthamine,-lycorine-and-haemanthamine,-and-including-haemanthamine--and-crinamine-type-alkaloids,-promising-anticancer-agents-(By-similarity). comment type catalytic-activity reaction evidence 1 text norbelladine-+-S-adenosyl-L-methionine-=-4'-O-methylnorbelladine-+-H(+)-+-S-adenosyl-L-homocysteine dbReference id RHEA:51268 type Rhea dbReference id CHEBI:15378 type ChEBI dbReference id CHEBI:57856 type ChEBI dbReference id CHEBI:59789 type ChEBI dbReference id CHEBI:133993 type ChEBI dbReference id CHEBI:134001 type ChEBI dbReference id 2.1.1.336 type EC comment type cofactor cofactor evidence 1 name Mg(2+) dbReference id CHEBI:18420 type ChEBI comment type pathway text evidence 1 Alkaloid-biosynthesis. comment type similarity text evidence 5 Belongs-to-the-class-I-like-SAM-binding-methyltransferase-superfamily.-Cation-dependent-O-methyltransferase-family. dbReference evidence 1 id 2.1.1.336 type EC dbReference id KJ584565 type EMBL property type protein-sequence-ID value AIL54545.1 property type molecule-type value mRNA dbReference id A0A077ESS0 type AlphaFoldDB dbReference id A0A077ESS0 type SMR 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:0008171 type GO property type term value F:O-methyltransferase-activity property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0009820 type GO property type term value P:alkaloid-metabolic-process property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0032259 type GO property type term value P:methylation property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id 3.40.50.150 type Gene3D property type entry-name value Vaccinia-Virus-protein-VP39 property type match-status value 1 dbReference id IPR029063 type InterPro property type entry-name value SAM-dependent_MTases_sf dbReference id IPR002935 type InterPro property type entry-name value SAM_O-MeTrfase dbReference id PTHR10509 type PANTHER property type entry-name value O-METHYLTRANSFERASE-RELATED property type match-status value 1 dbReference id PTHR10509:SF34 type PANTHER property type entry-name value TAPETUM-SPECIFIC-METHYLTRANSFERASE-1 property type match-status value 1 dbReference id PF01596 type Pfam property type entry-name value Methyltransf_3 property type match-status value 1 dbReference id SSF53335 type SUPFAM property type entry-name value S-adenosyl-L-methionine-dependent-methyltransferases property type match-status value 1 dbReference id PS51682 type PROSITE property type entry-name value SAM_OMT_I property type match-status value 1 proteinExistence type evidence-at-transcript-level keyword id KW-0017 Alkaloid-metabolism keyword id KW-0479 Metal-binding keyword id KW-0489 Methyltransferase keyword id KW-0949 S-adenosyl-L-methionine keyword id KW-0808 Transferase feature description Norbelladine-4'-O-methyltransferase-5 id PRO_0000450645 type chain location begin position 1 end position 239 feature evidence 3 type binding-site location position position 55 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location position position 77 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location begin position 79 end position 80 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location position position 85 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location position position 103 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location position position 132 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location position position 155 ligand name a-divalent-metal-cation dbReference id CHEBI:60240 type ChEBI feature evidence 3 type binding-site location position position 157 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location position position 181 ligand name a-divalent-metal-cation dbReference id CHEBI:60240 type ChEBI feature evidence 3 type binding-site location position position 182 ligand name a-divalent-metal-cation dbReference id CHEBI:60240 type ChEBI evidence key 1 type ECO:0000250 source dbReference id A0A077EWA5 type UniProtKB evidence key 2 type ECO:0000250 source dbReference id A0A2H5AIZ6 type UniProtKB evidence key 3 type ECO:0000255 source dbReference id PRU01019 type PROSITE-ProRule evidence key 4 type ECO:0000303 source dbReference id 25061748 type PubMed evidence key 5 type ECO:0000305 sequence checksum 36FF63CBD9AC3160 length 239 mass 27137 modified 2014-10-29 version 1 MGASIDDYCLIHKKILHSEDLLKYILETSAYPREHEQLKGLREVTEKHEWSSALVPADEGLFLSMLLKLMNAKRTIEIGVYTGYSLLTTALALPEDGKITAIDVNKSFFEIGLPFIQKAGVEHKINFIESEALPVLDQMLQETKEEDLYDYAFVDADKSNYANYHERLVKLVRIGGAILYDNTLWYGSVAYPEYPGLHPEEEVARLSFRNLNTFLAADPRVEISQVSIGDGVTICRRLY 
entry created 2020-08-12 dataset Swiss-Prot modified 2023-02-22 version 15 accession A0A077EW86 name NOMT2_NARAP protein recommendedName fullName evidence 4 Norbelladine-4'-O-methyltransferase-2 shortName evidence 4 NpN4OMT2 ecNumber evidence 1 2.1.1.336 gene name evidence 4 type primary N4OMT2 organism name type scientific Narcissus-aff.-pseudonarcissus-MK-2014 name type common Daffodil dbReference id 1540222 type NCBI-Taxonomy lineage taxon Eukaryota taxon Viridiplantae taxon Streptophyta taxon Embryophyta taxon Tracheophyta taxon Spermatophyta taxon Magnoliopsida taxon Liliopsida taxon Asparagales taxon Amaryllidaceae taxon Amaryllidoideae taxon Narcissus reference key 1 citation date 2014 first E103223 last E103223 name PLoS-ONE type journal-article volume 9 title Cloning-and-characterization-of-a-norbelladine-4'-O-methyltransferase-involved-in-the-biosynthesis-of-the-Alzheimer's-drug-galanthamine-in-Narcissus-sp.-aff.-pseudonarcissus. authorList person name Kilgore-M.B. person name Augustin-M.M. person name Starks-C.M. person name O'Neil-Johnson-M. person name May-G.D. person name Crow-J.A. person name Kutchan-T.M. dbReference id 25061748 type PubMed dbReference id 10.1371/journal.pone.0103223 type DOI scope NUCLEOTIDE-SEQUENCE-[MRNA] source strain cv.-Carlton tissue Bulb comment type function text evidence 1-2 4'-O-methyltransferase-converting-norbelladine-to-4'-O-methylnorbelladine-(By-similarity).-4'-O-methylnorbelladine-is-a-precursor-to-all-Amaryllidaceae-alkaloids-such-as-galanthamine,-lycorine-and-haemanthamine,-and-including-haemanthamine--and-crinamine-type-alkaloids,-promising-anticancer-agents-(By-similarity). comment type catalytic-activity reaction evidence 1 text norbelladine-+-S-adenosyl-L-methionine-=-4'-O-methylnorbelladine-+-H(+)-+-S-adenosyl-L-homocysteine dbReference id RHEA:51268 type Rhea dbReference id CHEBI:15378 type ChEBI dbReference id CHEBI:57856 type ChEBI dbReference id CHEBI:59789 type ChEBI dbReference id CHEBI:133993 type ChEBI dbReference id CHEBI:134001 type ChEBI dbReference id 2.1.1.336 type EC comment type cofactor cofactor evidence 1 name Mg(2+) dbReference id CHEBI:18420 type ChEBI comment type pathway text evidence 1 Alkaloid-biosynthesis. comment type similarity text evidence 5 Belongs-to-the-class-I-like-SAM-binding-methyltransferase-superfamily.-Cation-dependent-O-methyltransferase-family. dbReference evidence 1 id 2.1.1.336 type EC dbReference id KJ584562 type EMBL property type protein-sequence-ID value AIL54542.1 property type molecule-type value mRNA dbReference id A0A077EW86 type AlphaFoldDB dbReference id A0A077EW86 type SMR 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:0008171 type GO property type term value F:O-methyltransferase-activity property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0009820 type GO property type term value P:alkaloid-metabolic-process property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0032259 type GO property type term value P:methylation property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id 3.40.50.150 type Gene3D property type entry-name value Vaccinia-Virus-protein-VP39 property type match-status value 1 dbReference id IPR029063 type InterPro property type entry-name value SAM-dependent_MTases_sf dbReference id IPR002935 type InterPro property type entry-name value SAM_O-MeTrfase dbReference id PTHR10509 type PANTHER property type entry-name value O-METHYLTRANSFERASE-RELATED property type match-status value 1 dbReference id PTHR10509:SF34 type PANTHER property type entry-name value TAPETUM-SPECIFIC-METHYLTRANSFERASE-1 property type match-status value 1 dbReference id PF01596 type Pfam property type entry-name value Methyltransf_3 property type match-status value 1 dbReference id SSF53335 type SUPFAM property type entry-name value S-adenosyl-L-methionine-dependent-methyltransferases property type match-status value 1 dbReference id PS51682 type PROSITE property type entry-name value SAM_OMT_I property type match-status value 1 proteinExistence type evidence-at-transcript-level keyword id KW-0017 Alkaloid-metabolism keyword id KW-0479 Metal-binding keyword id KW-0489 Methyltransferase keyword id KW-0949 S-adenosyl-L-methionine keyword id KW-0808 Transferase feature description Norbelladine-4'-O-methyltransferase-2 id PRO_0000450642 type chain location begin position 1 end position 239 feature evidence 3 type binding-site location position position 55 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location position position 77 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location begin position 79 end position 80 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location position position 85 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location position position 103 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location position position 132 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location position position 155 ligand name a-divalent-metal-cation dbReference id CHEBI:60240 type ChEBI feature evidence 3 type binding-site location position position 157 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI feature evidence 3 type binding-site location position position 181 ligand name a-divalent-metal-cation dbReference id CHEBI:60240 type ChEBI feature evidence 3 type binding-site location position position 182 ligand name a-divalent-metal-cation dbReference id CHEBI:60240 type ChEBI evidence key 1 type ECO:0000250 source dbReference id A0A077EWA5 type UniProtKB evidence key 2 type ECO:0000250 source dbReference id A0A2H5AIZ6 type UniProtKB evidence key 3 type ECO:0000255 source dbReference id PRU01019 type PROSITE-ProRule evidence key 4 type ECO:0000303 source dbReference id 25061748 type PubMed evidence key 5 type ECO:0000305 sequence checksum 7BDF63BBDA18B658 length 239 mass 27093 modified 2014-10-29 version 1 MGASIDDYSLVHKNILHSEDLLKYILETSAYPREHEQLKGLREVTEKHEWSSALVPADEGLFLSMLLKLMNAKRTIEIGVYTGYSLLTTALALPEDGKITAIDVNKSFFEIGLPFIQKAGVEHKINFIESEALPVLDQMLQETKEEDLYDYAFVDADKSNYANYHERLVKLVRIGGAILYDNTLWYGSVAYPEYPGLHPEEEVARLSFRNLNTFLAADPRVEISQVSIGDGVTICRRLY 
entry created 2020-10-07 dataset Swiss-Prot modified 2023-02-22 version 12 accession A0A4Y5X186 name CESS2_CONMO protein recommendedName fullName evidence 5 Conopressin/conophysin,-isoform-2 component recommendedName fullName evidence 5 Conopressin-R component recommendedName fullName evidence 5 Conophysin organism name type scientific Conus-monile name type common Necklace-cone dbReference id 351660 type NCBI-Taxonomy lineage taxon Eukaryota taxon Metazoa taxon Spiralia taxon Lophotrochozoa taxon Mollusca taxon Gastropoda taxon Caenogastropoda taxon Neogastropoda taxon Conoidea taxon Conidae taxon Conus taxon Strategoconus reference key 1 citation date 2020 first 140391 last 140391 name Biochim.-Biophys.-Acta type journal-article volume 1868 title Cone-snail-analogs-of-the-pituitary-hormones-oxytocin/vasopressin-and-their-carrier-protein-neurophysin.-Proteomic-and-transcriptomic-identification-of-conopressins-and-conophysins. authorList person name Kumar-S. person name Vijayasarathy-M. person name Venkatesha-M.A. person name Sunita-P. person name Balaram-P. dbReference id 32058072 type PubMed dbReference id 10.1016/j.bbapap.2020.140391 type DOI scope NUCLEOTIDE-SEQUENCE-[MRNA] scope NOMENCLATURE source tissue Venom-duct comment type function text evidence 3 Targets-vasopressin-oxytocin-related-receptors. comment type subcellular-location subcellularLocation location evidence 7 Secreted comment type tissue-specificity text evidence 7 Expressed-by-the-venom-gland. comment type domain text evidence 6 The-cysteine-framework-of-the-conopressin-is-C-C. comment type miscellaneous text evidence 7 The-letter-'R'-in-the-name-'Conopressin-R'-proposed-by-Kumar-and-colleagues-stands-for-the-eighth-residue,-which-differs-between-conopressins. comment type similarity text evidence 6 Belongs-to-the-vasopressin/oxytocin-family. dbReference id MK263339 type EMBL property type protein-sequence-ID value QDE14047.1 property type molecule-type value mRNA dbReference id A0A4Y5X186 type AlphaFoldDB dbReference id A0A4Y5X186 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:0005185 type GO property type term value F:neurohypophyseal-hormone-activity property type evidence value ECO:0007669 property type project value InterPro 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 2.60.9.10 type Gene3D property type entry-name value Neurohypophysial-hormone-domain property type match-status value 1 dbReference id IPR000981 type InterPro property type entry-name value Neurhyp_horm dbReference id IPR036387 type InterPro property type entry-name value Neurhyp_horm_dom_sf dbReference id IPR022423 type InterPro property type entry-name value Neurohypophysial_hormone_CS dbReference id PTHR11681 type PANTHER property type entry-name value NEUROPHYSIN property type match-status value 1 dbReference id PTHR11681:SF5 type PANTHER property type entry-name value OXYTOCIN property type match-status value 1 dbReference id PF00184 type Pfam property type entry-name value Hormone_5 property type match-status value 1 dbReference id PIRSF001815 type PIRSF property type entry-name value Nonapeptide_hormone_precursor property type match-status value 1 dbReference id PR00831 type PRINTS property type entry-name value NEUROPHYSIN dbReference id SM00003 type SMART property type entry-name value NH property type match-status value 1 dbReference id SSF49606 type SUPFAM property type entry-name value Neurophysin-II property type match-status value 1 dbReference id PS00264 type PROSITE property type entry-name value NEUROHYPOPHYS_HORM property type match-status value 1 proteinExistence type evidence-at-transcript-level keyword id KW-0027 Amidation keyword id KW-1015 Disulfide-bond keyword id KW-1213 G-protein-coupled-receptor-impairing-toxin keyword id KW-0964 Secreted keyword id KW-0732 Signal keyword id KW-0800 Toxin feature evidence 4 type signal-peptide location begin position 1 end position 30 feature description Conopressin-R evidence 1 id PRO_0000450738 type peptide location begin position 31 end position 39 feature evidence 3 id PRO_0000450739 type propeptide location begin position 40 end position 47 feature description Conophysin id PRO_5021467512 type chain location begin position 48 end position 160 feature description Glycine-amide evidence 1 type modified-residue location position position 39 feature evidence 3 type disulfide-bond location begin position 31 end position 36 feature evidence 2 type disulfide-bond location begin position 53 end position 97 feature evidence 2 type disulfide-bond location begin position 56 end position 70 feature evidence 2 type disulfide-bond location begin position 64 end position 87 feature evidence 2 type disulfide-bond location begin position 71 end position 77 feature evidence 2 type disulfide-bond location begin position 104 end position 118 feature evidence 2 type disulfide-bond location begin position 112 end position 130 feature evidence 2 type disulfide-bond location begin position 119 end position 124 feature evidence 8 type non-terminal-residue location position position 160 evidence key 1 type ECO:0000250 source dbReference id A0A291NVT7 type UniProtKB evidence key 2 type ECO:0000250 source dbReference id P01175 type UniProtKB evidence key 3 type ECO:0000250 source dbReference id P05486 type UniProtKB evidence key 4 type ECO:0000255 evidence key 5 type ECO:0000303 source dbReference id 32058072 type PubMed evidence key 6 type ECO:0000305 evidence key 7 type ECO:0000305 source dbReference id 32058072 type PubMed evidence key 8 type ECO:0000312 source dbReference id QDE14047.1 type EMBL sequence checksum B72D8A7CCA0CAA50 fragment single length 160 mass 17194 modified 2019-09-18 precursor true version 1 MKCSVLQMSRLSWAMCLMLLMLLLLGTAQGCFIRNCPRGGKRAVDALQPTRQCMSCGPDGVGQCVGPSVCCGLGLGCLMGTPETEVCQKENESSVPCAISGRHCGMDNTGNCVADGICCVEDACSFNSLCRVDTDQEDSVSARQELLTLIRRLLVNRQYD 
