ID A0A1J9RHE1_9PEZI Unreviewed; 718 AA.
AC A0A1J9RHE1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 08-OCT-2025, entry version 30.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=BKCO1_200014 {ECO:0000313|EMBL:OJD40032.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD40032.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD40032.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD40032.1,
RC ECO:0000313|Proteomes:UP000183809};
RA Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA Esteves A.C.;
RT "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT hemibiotrophic lifestyle of Diplodia corticola.";
RL Submitted (OCT-2016) 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:OJD40032.1}.
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DR EMBL; MNUE01000002; OJD40032.1; -; Genomic_DNA.
DR RefSeq; XP_020135019.1; XM_020272330.1.
DR AlphaFoldDB; A0A1J9RHE1; -.
DR STRING; 236234.A0A1J9RHE1; -.
DR GeneID; 31012589; -.
DR OrthoDB; 6132182at2759; -.
DR Proteomes; UP000183809; 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:UP000183809}.
FT DOMAIN 340..351
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 245..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 77361 MW; 5980A5AEA5218CF2 CRC64;
MGSLAQAQAD GVVIGLKGLS GIHPRREIDD LVVNEPDMFN LFILALESLQ KDEGAHQNKM
GYFQIAGIHG LPKRDWDGVQ GEKPGQGGYC THNSILFPTW HRPYLAIQTP SNNPKNKQQT
IYATMEHIAS QFTDPKYRDA ARRFRLPYWD YLHARAARTT TFPGVFAGRK TSFGYDFGLP
LALREAKLMV HRPAGVDAAS EARLVAIDNP LRSFAFPQTN GVAADEWQVL EQQVQAEGGG
FYLSQRRTAR HPRSGPTGGD DDFADLDAAL NKDREPEVQT LLDLIELAPY ADFGNFATAV
PSGKGGAGAP NGSLESFHGA YHVLIGGAGH MSRVPIAAFD PIFWFHHCNI DRILAVWQSL
HDDFTPSSGT PNASSNLYPF RKDSSGSSFW TSTDSRDVTT FGYTYADIAG ATDRQAVLAR
FDACYRWSLQ RQSRQGGAQN PAPPAEMQPV DVRGAQCFRY TAAATVGAAV QAPMQALSLV
QQKVLEVKDQ AVNAISGAAR PAAAATASAG QEAGTEGGAV QVQPSFRRGD EILAEEPAGS
RLVLQWYIDS EVNKDALDGA FTLYFFIGPT AAADTSEAGD GPATWQAEPT LAGMTHVFAA
PRAACDNCAL QSDEGLRVTG TTAVTPILLD YVEDGRAGLG SLAPDDVVPF LRRALVWRVA
DVNQRVTNPA ELAGGLTISV SATISVLRPD QPIPEFREPL FFPEVMDGRP ATGDPVAA
//
