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Database: UniProt
Entry: A0A0A1T3I6_9HYPO
LinkDB: A0A0A1T3I6_9HYPO
Original site: A0A0A1T3I6_9HYPO 
ID   A0A0A1T3I6_9HYPO        Unreviewed;       552 AA.
AC   A0A0A1T3I6;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE            EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN   ORFNames=VHEMI07414 {ECO:0000313|EMBL:CEJ91721.1};
OS   [Torrubiella] hemipterigena.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX   NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ91721.1, ECO:0000313|Proteomes:UP000039046};
RN   [1] {ECO:0000313|EMBL:CEJ91721.1, ECO:0000313|Proteomes:UP000039046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA   Hertweck C., Linde J.;
RT   "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT   Verticillium hemipterigenum.";
RL   Genome Announc. 3:e01439-e01414(2015).
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   -!- SIMILARITY: Belongs to the tyrosinase family.
CC       {ECO:0000256|ARBA:ARBA00009928}.
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DR   EMBL; CDHN01000004; CEJ91721.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1T3I6; -.
DR   STRING; 1531966.A0A0A1T3I6; -.
DR   HOGENOM; CLU_013691_2_0_1; -.
DR   OrthoDB; 1908494at2759; -.
DR   Proteomes; UP000039046; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR002227; Tyrosinase_Cu-bd.
DR   PANTHER; PTHR11474:SF76; TYROSINASE; 1.
DR   PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   PRINTS; PR00092; TYROSINASE.
DR   SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   3: Inferred from homology;
KW   Melanin biosynthesis {ECO:0000256|ARBA:ARBA00023101};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000039046};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..552
FT                   /note="tyrosinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001978835"
FT   DOMAIN          292..303
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
SQ   SEQUENCE   552 AA;  61518 MW;  5D9229634A797C98 CRC64;
     MLPKTVLISV FFALTSALDQ KVATIGAWPA SQDGAVPIRQ NINKLHADGG PQWDLYIQAL
     RMMQDANEDD PFSYFQLAGI HGLPFIEWGN TGGRNNATGW GGYCPHGEAM FLPWHRPYIV
     LYEQIVVNNA RAIAETYPEA QREIYRNAAD QLRVPFWDWG VDGKVPDAVV PEMITIKASR
     DGTVKDVTIP NPLATFVYPK SYGAGKYGPP PIETERVLRC QAPYSFPATA NANLQRRNYR
     QRVYDVFSRA ETFDSFGTVG NKGISLESLH NNIHWDAACD HALVAPSTSG FDPIFFLHHA
     NVDRLWAYWG AMKGDEGSLI QPYVGGPRWS TPNGTTINPD TTLQPFFDQN NQWYTIKSVA
     DVDAFGYTYE GLEFWRKSDE QMKEDATTII NTLYGPRTPK VRRGGSLIPR ASDNTRLFAE
     ISVEASELKD RPCEIEITVK GYKANSIVVL AHPVSGPVYG GFSLDEDESA NTFSAQSVEE
     TVSSLDDNMQ IAIIKPDGTR LDASQILSLQ VDIEEVDVTP RQKDTEMPVV SLPRVHEAVR
     AGKKLPNKRR NL
//
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