ID A0A0F7ZYT2_9HYPO Unreviewed; 627 AA.
AC A0A0F7ZYT2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=HIM_07589 {ECO:0000313|EMBL:KJZ73017.1};
OS Hirsutella minnesotensis 3608.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX NCBI_TaxID=1043627 {ECO:0000313|EMBL:KJZ73017.1, ECO:0000313|Proteomes:UP000054481};
RN [1] {ECO:0000313|EMBL:KJZ73017.1, ECO:0000313|Proteomes:UP000054481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3608 {ECO:0000313|EMBL:KJZ73017.1,
RC ECO:0000313|Proteomes:UP000054481};
RX PubMed=25359922; DOI=10.1093/gbe/evu241;
RA Lai Y., Liu K., Zhang X., Zhang X., Li K., Wang N., Shu C., Wu Y., Wang C.,
RA Bushley K.E., Xiang M., Liu X.;
RT "Comparative genomics and transcriptomics analyses reveal divergent
RT lifestyle features of nematode endoparasitic fungus Hirsutella
RT minnesotensis.";
RL Genome Biol. Evol. 6:3077-3093(2014).
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};
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DR EMBL; KQ030539; KJZ73017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7ZYT2; -.
DR OrthoDB; 1908494at2759; -.
DR Proteomes; UP000054481; 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; 1.
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:UP000054481};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..627
FT /note="tyrosinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002526124"
FT DOMAIN 122..139
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 326..337
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 627 AA; 69429 MW; 565EDFEFF2B56A8A CRC64;
MVLRLLLCTL GASLVLAQAT GYDFGTDISH LSRRQDGTAP IVIGKLPLAP DGSVPKRLEI
RQMKADRYKW DLFILALSLI QFVGQDDPLS WYQIAGIHGV PFKPWNGVLP VQGGGQSGYC
THNSVLFPMW HRPYMALFEQ QVFRMANGIA GMFVNETQRR LYQQAAADFR VPYWDWSRNA
PPGDTHLPGD FWKPVIAQDG PNGVQNINNP LYSYHFHPLD MDALIWDPLK QWNETKRGPD
LGVSLTAPPS DNGKVNEALL TKLPEIQQRL YVLFSNYHDY NSFSNKAWAV SNNLSTLDSI
ESVHDVIHLY GGSKGHLTYV PLSSFDPLFF LHHAMTDRLV AIWQVLNPTA WITPMPAGET
TFTALKGTIQ SSSSPLTPFY ASSDGTFWTS DSARSTEAFG YTYADTDPAL GSSQDIRQAL
IAKINDWYGS ASPMGNLVKA QDMGASDESQ QHPWNGPLKE DGRLGSHVKL KHEQTLQDNR
YTEWIANVHV NAEALNGSFV IHFFIGAPPI NEDDWETAPN LGGSVGIFAM NRTTGSQFKI
SGAVPLTAAL MRSTTGRVLA DLSPEVMVPT LRESLQFRIL GSDGHQVDPS SVRGLYIAVS
SSNVKPPKTL VELPVWGPVE PRLELWA
//