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Database: UniProt
Entry: A0A4T0VHK0_9PEZI
LinkDB: A0A4T0VHK0_9PEZI
Original site: A0A4T0VHK0_9PEZI 
ID   A0A4T0VHK0_9PEZI        Unreviewed;       599 AA.
AC   A0A4T0VHK0;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   08-OCT-2025, entry version 22.
DE   RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE            EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN   ORFNames=CH35J_011066 {ECO:0000313|EMBL:TIC91226.1};
OS   Colletotrichum higginsianum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=80884 {ECO:0000313|EMBL:TIC91226.1, ECO:0000313|Proteomes:UP000305883};
RN   [1] {ECO:0000313|EMBL:TIC91226.1, ECO:0000313|Proteomes:UP000305883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF305635-RFP {ECO:0000313|EMBL:TIC91226.1,
RC   ECO:0000313|Proteomes:UP000305883};
RX   PubMed=31028389; DOI=.1093/gbe/evz087;
RA   Tsushima A., Gan P., Kumakura N., Narusaka M., Takano Y., Narusaka Y.,
RA   Shirasu K.;
RT   "Genomic Plasticity Mediated by Transposable Elements in the Plant
RT   Pathogenic Fungus Colletotrichum higginsianum.";
RL   Genome Biol. Evol. 11:1487-1500(2019).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 L-dopa + O2 = 2 L-dopaquinone + 2 H2O; Xref=Rhea:RHEA:34287,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504,
CC         ChEBI:CHEBI:57924; EC=1.14.18.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00048233};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosine + O2 = L-dopaquinone + H2O; Xref=Rhea:RHEA:18117,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57924,
CC         ChEBI:CHEBI:58315; EC=1.14.18.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00048881};
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|ARBA:ARBA00001973};
CC   -!- SIMILARITY: Belongs to the tyrosinase family.
CC       {ECO:0000256|ARBA:ARBA00009928}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TIC91226.1}.
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DR   EMBL; MWPZ01000010; TIC91226.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4T0VHK0; -.
DR   OrthoDB; 1658288at2759; -.
DR   Proteomes; UP000305883; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004503; F:tyrosinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.310.20; -; 1.
DR   Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR   InterPro; IPR008922; Di-copper_centre_dom_sf.
DR   InterPro; IPR050316; Tyrosinase/Hemocyanin.
DR   InterPro; IPR041640; Tyrosinase_C.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   PANTHER; PTHR11474:SF76; SHKT DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   Pfam; PF18132; Tyrosinase_C; 1.
DR   PRINTS; PR00092; TYROSINASE.
DR   SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Melanin biosynthesis {ECO:0000256|ARBA:ARBA00023101};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          102..119
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00497"
FT   DOMAIN          296..307
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
SQ   SEQUENCE   599 AA;  69080 MW;  4F79EC4902C1BD7F CRC64;
     MSSENPQHEF VVIQGIPVPP GGKPGLRKEF TKWATEKPEE NIQVSLFIRA LQLFYNEDYT
     KTLSYFQIAG IHGYPGTVAW DNSAEPTHKS RDDKQHFIYC THNSLTFPTW HRPYMALFEQ
     TIYQFMGKVI EQLHFSSEAE KNVWIEESTQ WRLPYWDWAL NTEVPDLFRP TTVKIRAPFG
     ADGLQPEPEI VPNPLYRYEL RLKDPRNIKD LENLDDPVGE LRKHPVSDLV YRLLSNVKDW
     ASFSSTITAQ KEKPKDWEQW ISLEYIHNNL HGFIGGFGGF NEGIGHMMNV PAAAFDPIFY
     MHHCNIDRLF AIWQVLHENS WFKDVKGPPA TDSLTPFHHN QADYFDSNRA RTWLNLGYQY
     DVLQRDDHET DVKYLERINA YVDKTYRSTG SVLLEDKGDL FQKNQDLAGD EMYDDYMINV
     SYDRYGYKNG APYTIHFLLE ELSTQETAIE SDTSPPRPHR HVGSIFTFSS PVTSGEVHTA
     GHPRCGNCAQ QLEEGVLSRA SIPLTISLYK DATNQKVHGI RDLGPENVEP YLCDRLTWVA
     KSTDGTTIPW SELNRTKVYV FKGKAKHYPK TGRLSVYQDY KPLPRVTHGK DAGASHQEY
//
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