ID A0A4U0U5W6_9PEZI Unreviewed; 625 AA.
AC A0A4U0U5W6;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=B0A50_02554 {ECO:0000313|EMBL:TKA30327.1};
OS Salinomyces thailandica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Salinomyces.
OX NCBI_TaxID=706561 {ECO:0000313|EMBL:TKA30327.1, ECO:0000313|Proteomes:UP000308549};
RN [1] {ECO:0000313|EMBL:TKA30327.1, ECO:0000313|Proteomes:UP000308549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 6315 {ECO:0000313|EMBL:TKA30327.1,
RC ECO:0000313|Proteomes:UP000308549};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone; 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:ARBA00000426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosine + O2 = H2O + L-dopaquinone; 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:ARBA00001038};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
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:TKA30327.1}.
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DR EMBL; NAJL01000011; TKA30327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U0U5W6; -.
DR Proteomes; UP000308549; 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 Gene3D; 2.60.310.20; -; 1.
DR Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 2.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR041640; Tyrosinase_C.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF32; TYROSINASE; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR Pfam; PF18132; Tyosinase_C; 1.
DR Pfam; PF00264; Tyrosinase; 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 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000308549};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..625
FT /note="tyrosinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5020260516"
FT DOMAIN 130..147
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 306..317
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 625 AA; 69106 MW; 11087219F9050E57 CRC64;
MAAPSFMRRV LLAIALLHAV LLTSCSPLLS HQVEELAAPE APTLQRRQSS LTLVTGITAF
GVQPRLEIRE LQQNADQWNI YLLGLVRWQA VNETEKLSYY QIAGIHGRPY AAWDGVPAEE
NITRPGYCMH VSNVFLPWHR PYLALYEQTL YQHMVDAVNA FPAGATRQRY AAAALSWRMP
YWDWAATPAD GESVYPSAVT TSTVTVTMPN GTNTIPNPLY TYHFHPVKQA DFYFNPFSSW
NVTIRAPTNW TSNAISQNGK VGSDLDNSRV SFQDRVYNLL TFYSNFTQFG NEAWIDPGVS
NADTYDPLFW LHHAMVDRIF ALWQALYNDS YVEPMAAVEQ SFTVAINDHV DENTPLKPFH
ANANGDMWTA ATVRSPQTLG YTYSDLGNGS ISAVKAAVNR LYGRSAGSGG ISKRSGDARV
NVQRELPEAA VENASVTAPE DIIDGRNRQY LANILSQKFA LNGSYGIYLF MGDFDDDPAS
WPQSPNLVGT HAVFAALSTA DAASNPQART KRDGSLIHVT GAMPLTSMLL AKVDAGDISC
MNPETVIPYL TDNLHWRVGM FDGSQIEPQD VADLTITVIS AEVEPASRDD QFPQWSNFEV
LTSITQGKPG GALFLGHERR PIAHK
//