ID A0A4Z1JEZ4_9HELO Unreviewed; 671 AA.
AC A0A4Z1JEZ4;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 08-OCT-2025, entry version 20.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=BELL_0525g00060 {ECO:0000313|EMBL:TGO71824.1};
OS Botrytis elliptica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=278938 {ECO:0000313|EMBL:TGO71824.1, ECO:0000313|Proteomes:UP000297229};
RN [1] {ECO:0000313|EMBL:TGO71824.1, ECO:0000313|Proteomes:UP000297229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Be9601 {ECO:0000313|EMBL:TGO71824.1,
RC ECO:0000313|Proteomes:UP000297229};
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 L-dopaquinone + 2 H2O; 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:ARBA00048233};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosine + O2 = L-dopaquinone + H2O; 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:ARBA00048881};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
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:TGO71824.1}.
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DR EMBL; PQXM01000523; TGO71824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Z1JEZ4; -.
DR STRING; 278938.A0A4Z1JEZ4; -.
DR OrthoDB; 1658288at2759; -.
DR Proteomes; UP000297229; 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 GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
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; IPR050316; Tyrosinase/Hemocyanin.
DR InterPro; IPR041640; Tyrosinase_C.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF76; SHKT DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR Pfam; PF18132; Tyrosinase_C; 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 Copper {ECO:0000256|ARBA:ARBA00023008};
KW Melanin biosynthesis {ECO:0000256|ARBA:ARBA00023101};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000297229}.
FT DOMAIN 303..314
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 671 AA; 73979 MW; D83B9DD658956484 CRC64;
MATIPVLNYP ITGPPKPSPT PADGSVPLRR EIRDLQRNFP DQWTLYILGL QAFQQLDQKS
DLSWYGIAGI HGRPYRPWGG VQGDNPAGWQ GYCTHSSILF APWHRPYLAL FEQYLYQIIQ
KIAATFPAST KTRYQQAALT FRMPYWDWAA APPAGDKYFP TVVGQPSIQI ITPTSNNKPV
QINNPLYSYK FNPLNPLKGD FPSAPESRWP TTLRYPTNGS ATAKSQEQQV FDAMESQFDS
YQSNVYLIMR DPNYKQFDAF SNHQWASNNA PGTYGSIEDV HNSVHSETGG SGQMGDPDYA
AFDPLFWLHH TNVDRQFAIW QALNPNSYAI NKPSGDGTFS IQSGSQETST TPLTPFNNAT
GKTYWTSDGV RSTATFNYAY PETQQWKYPT VQQYQTSVLA AVQTLYGATS NQFMQLMGVQ
TAAAPEQIST QAEKVVADSS DAAQKPIGDG AASSSHGHDF LSNLLHSSAK AKPKPGDAVR
GGEDFESEIG KASKSPATAG PIKYREYIAN IRAPKHILHQ TYRVRIFLGD FNSDPATWAT
EHSTIGTFSS FGKNPETTGC GKCIKDEARS LMISGTVPLT PILLKLYKNG DLGSLETENV
IPYLRKNLHW RVTLADGTEI DRGNVEGLKI SVVSTEVKCA QGGFPEYSGE YEVHSEVTGG
RPAGLGEGDR I
//
