ID A0A4U6XW32_9PEZI Unreviewed; 496 AA.
AC A0A4U6XW32;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN Name=T {ECO:0000313|EMBL:TKW60178.1};
GN ORFNames=CTA1_4875 {ECO:0000313|EMBL:TKW60178.1};
OS Colletotrichum tanaceti.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=1306861 {ECO:0000313|EMBL:TKW60178.1, ECO:0000313|Proteomes:UP000310108};
RN [1] {ECO:0000313|EMBL:TKW60178.1, ECO:0000313|Proteomes:UP000310108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRIP57314 {ECO:0000313|EMBL:TKW60178.1};
RX PubMed=31150449; DOI=10.1371/journal.pone.0212248;
RA Lelwala R.V., Korhonen P.K., Young N.D., Scott J.B., Ades P.A.,
RA Gasser R.B., Taylor P.W.J.;
RT "Comparative genome analysis indicates high evolutionary potential of
RT pathogenicity genes in Colletotrichum tanaceti.";
RL PLoS ONE 14:e0212248-e0212248(2019).
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:TKW60178.1}.
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DR EMBL; PJEX01000001; TKW60178.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U6XW32; -.
DR STRING; 1306861.A0A4U6XW32; -.
DR Proteomes; UP000310108; 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; PS00498; TYROSINASE_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000310108};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..496
FT /note="tyrosinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5020849751"
FT DOMAIN 190..201
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 292..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 496 AA; 55905 MW; A64D333781B22DDB CRC64;
MKTLTLWQQV LYRLVQLIAS WFPDPTERSF YQDAAIDFRI PYWDWATPPP PGEMVYLSEF
AEPGIQVYGP RGWQFIANPL HSYKFRPLDP EVFSEGDHKF PRWTETMRAP FETSDNQSIA
HAIEHARPAL QQRLYTLLSN YKDYGPFSNK YWGIATNQSQ YDSIESLHDA MHVLVGNRGH
LFYIQYSAFD PVFFLHHTMA DRIVAMWQVL YPMSWVSAQV AMEHSFTMPP GYAQDAFTEL
KPFYADVNGT FWNSAMARDT SAFGYSYAET SSSPGSNLAE NQARLIATIN RLYGPSGSSN
PARKRRRTEA GRDPGARSQV RKGPISSKKV VDFSHDVDFV SKLITDATVY TEWVANVHVQ
NGALNGSFTV HFFLGEVPED TTTWLAAPNL VGSMPVFAMK NMGSGNHVSG TVPLTSALMH
LVLAEVISGL DPKETEPYLE ENLRARVVGE SGAEIPVDTI DSLHIQVASS QVRAARNEWE
LPTWGTVVER FVMRHG
//
