ID A0A4Z1KK63_9HELO Unreviewed; 575 AA.
AC A0A4Z1KK63;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=BPOR_0481g00070 {ECO:0000313|EMBL:TGO84652.1};
OS Botrytis porri.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=87229 {ECO:0000313|EMBL:TGO84652.1, ECO:0000313|Proteomes:UP000297280};
RN [1] {ECO:0000313|EMBL:TGO84652.1, ECO:0000313|Proteomes:UP000297280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL3349 {ECO:0000313|EMBL:TGO84652.1,
RC ECO:0000313|Proteomes:UP000297280};
RA Valero-Jimenez C.A., Tapia P., Veloso J., Silva-Moreno E., Staats M.,
RA Valdes J.H., Van Kan J.A.L.;
RT "Comparative genomics of Botrytis spp.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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:TGO84652.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PQXO01000480; TGO84652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Z1KK63; -.
DR STRING; 87229.A0A4Z1KK63; -.
DR Proteomes; UP000297280; 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:UP000297280};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..575
FT /note="tyrosinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5021357145"
FT DOMAIN 137..154
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 339..350
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 575 AA; 63376 MW; 11171262D99F1125 CRC64;
MVFFRGASIV SFLTIAGSFL SQTAQAIPRP HDHRPRGYDY GVDIGALLKR DVTPMPTTGV
SFNGSNSSIP VRQEIRDLQK NADLWELYIL GVSMMQTINQ SDIRSWYQIA GIHGRPYLPY
DEVQGTPGNE NNGYCTHVSI LFPTWHRPYL ALYEQVLHSV VEFIAAQFPA GAERDRYTAA
AANFRIPYWD WAVVPPAGES VLPPSVSEPT VTVNGPAGVQ TISNPLFSYH FNPLDPSELP
DAPFSQFPQT LRYPTSNDAS ATSQNNLVAQ QLDNSAASFR NRLYNLFTNY HDYSTFSNEA
WITASSPGDF DSIESLHDQI HGLTGSGGHM SYIDYSSFDP LFFLHHTMID RCFAIWQTLN
PDSYVTPREA SYSTFTMTAG TTQDVSTPLK PFYNADGNDF YTSSDVVSTE SFGYAYPETL
PGGNTTAQAI KAINLLYGTT APAKTVSRGL IPGLTSKLLG REHQLNSTYD LISLALAPNG
QYTEWIANIQ VEKFALSRSF FIHVFLGPFN DDPASWSFEP NLVGTHCVFA KLSSSGTVVA
DPNQLVTGTI PLTSALLDDI SEGHLRSLND VDVEP
//