ID A0A066Y1V3_COLSU Unreviewed; 555 AA.
AC A0A066Y1V3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=CSUB01_02387 {ECO:0000313|EMBL:KDN72041.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN72041.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(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 -!- 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:KDN72041.1}.
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DR EMBL; JMSE01000064; KDN72041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066Y1V3; -.
DR STRING; 1173701.A0A066Y1V3; -.
DR eggNOG; ENOG502R1BY; Eukaryota.
DR HOGENOM; CLU_013691_2_0_1; -.
DR OMA; FENATMH; -.
DR OrthoDB; 1908494at2759; -.
DR Proteomes; UP000027238; 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 SUPFAM; SSF48056; Di-copper centre-containing domain; 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:UP000027238};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..555
FT /note="tyrosinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001631036"
FT DOMAIN 78..314
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|Pfam:PF00264"
SQ SEQUENCE 555 AA; 61759 MW; FAA2967D799EBCAE CRC64;
MLSPQFIPVF SVLAIVRLTA AAQEIPVVGV RSGINTRTGE VPIRRNINSI YNERGPHWDL
YVGALTAMQD TNETDPISYF QLAGIHGQPY MAWSGGGPQT GIDTGYCPHN TFTNFASRRW
GLTPLQQVLV HQAKRIALSY PEPHRKRYVE AAERLRIAYW DWAADYHVPP ATVMPTVVIN
KPAAGTMQPT VVRNPLYRFK YPKSVLNGQF GSFNGGKYTN RCAKDGESYP ATANKMLAYY
SLKEKVYNVF VRAISFDEMV SAQNQGANFE GPHGEVHIAA ACGQDLAFLS ISAFEPLFWL
HHANVDRLIA YWQALHFENA TMHFSYASDA MFATPAGTIV TPQYPIWPFM SSGGEPLTSE
SVTHIRDWGY TYAPMRFWDQ APGETKMAVI RTVNTLYGTL EQQQWQRQHL VRGLRRRKGM
PKREYFAKVE VERSELELPC QVQLFLKGRL AGSFTLLGMP KQGRSYDEIP LSRGVEAVGI
SGLSMKSAVG VIGDGLKIVI NNLDGTTQSL AHVPSLKIEV EGVDVVPPNS LNELPTLGAA
LTRIVLARPY AIGKY
//
