ID A0A4U6XEV8_9PEZI Unreviewed; 707 AA.
AC A0A4U6XEV8;
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=tyr1 {ECO:0000313|EMBL:TKW53732.1};
GN ORFNames=CTA1_1002 {ECO:0000313|EMBL:TKW53732.1};
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:TKW53732.1, ECO:0000313|Proteomes:UP000310108};
RN [1] {ECO:0000313|EMBL:TKW53732.1, ECO:0000313|Proteomes:UP000310108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRIP57314 {ECO:0000313|EMBL:TKW53732.1};
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 -!- 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:TKW53732.1}.
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DR EMBL; PJEX01000170; TKW53732.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U6XEV8; -.
DR STRING; 1306861.A0A4U6XEV8; -.
DR Proteomes; UP000310108; 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; PS00497; TYROSINASE_1; 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:UP000310108};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..707
FT /note="tyrosinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5020747359"
FT DOMAIN 225..242
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 416..427
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 21..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..71
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 707 AA; 75826 MW; D5EF90BF852C22AF CRC64;
MVLLSKSAST VAVCILAALA VAQPGGPPRP PGRGPPGPPA RGPPARDPPP PPGPPDRGGP
APAPAPAPNP VSSQAPASQR SSSRLSSPTA QPSLQPASTS APQRPATTTS SSLRPSVAAV
SSSSTSSRQA QTSPSPSGPY AITGLKTGID STSGQRPLRQ NINDLQASGA QWDLYILGLA
AMQSDGSEND QLSYFQISGI HGRPFIPWNG VQAVPRGSGG GYCPHGNVQF PMWHRPYVAL
FEQVLGGHIQ AIAANYTGSQ AQEYRTAADN WRAPYWDWAA DGGAQLPPAT TQATVTVNGP
GGQVRLPNPL LGYKWQRFPL NTASNYFPTS GDRNCWAWPQ TKRWPDANGN NRPSLANQEL
SQDDLKSTTY NVFTTATDFE TMASTGSTGN SFEAVHNSVH AAIYAVMAYI EYAAFDPLFM
LHHANVDRLI AMWQAIHYND RTQTQTLPSN ALFATAANTP ITADSPLKPF YRDASGNFHT
GRTASDIKTF GYSYPEIADW NQSPDALARQ VTVSVNRLYG PAGASAKRRA RHDRRQPGSY
AAHKEYTALV DLERSELPLP CSVSVYVDGE FAGKISVMSM PASGMMHSTV PLNKALEKLG
KSMDVPESQD NNYGSSATNG TAAQQPALSS EDEEIILQKQ LTVEIKSCRM IINPMGILTW
VGEKYNEVAN PENQTKPFWI EASRLSSSTL SRHQDGRLSG RATWCST
//
