ID A0A2P7ZDQ2_9PEZI Unreviewed; 642 AA.
AC A0A2P7ZDQ2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=B9Z65_5298 {ECO:0000313|EMBL:PSK46330.1};
OS Elsinoe australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX NCBI_TaxID=40998 {ECO:0000313|EMBL:PSK46330.1, ECO:0000313|Proteomes:UP000243723};
RN [1] {ECO:0000313|EMBL:PSK46330.1, ECO:0000313|Proteomes:UP000243723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL1 {ECO:0000313|EMBL:PSK46330.1,
RC ECO:0000313|Proteomes:UP000243723};
RA Cheng Q.;
RT "Draft genome sequence of Elsinoe australis.";
RL Submitted (MAY-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 -!- 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:PSK46330.1}.
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DR EMBL; NHZQ01000236; PSK46330.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7ZDQ2; -.
DR STRING; 40998.A0A2P7ZDQ2; -.
DR Proteomes; UP000243723; 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:SF76; 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 3: Inferred from homology;
KW Melanin biosynthesis {ECO:0000256|ARBA:ARBA00023101};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000243723};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..642
FT /note="tyrosinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015161171"
FT DOMAIN 125..142
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 328..339
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 642 AA; 71557 MW; C07E56E2013BEDA5 CRC64;
MKFSSVFSGA LVAAASIVPA TAAPSVPLEA RQNGAVVVTG VTNNGVQTRL ELRTMQREQP
DMFNLYLIGL RRMMAVPQQN ALSYYQIAGI HGRPYIQWDG EAPERRQSDN AQAPADGWGG
GYCTHVSNIF LTWHRPYLAL YEQILYGHVQ DAANSFPDDG RRARYQAAAR NFRIPYWDWA
AQPCAECLPY PKLVSQMYLD IDTPNGRQTL MNPLFRYNFT NGAPSELAYN PFATWQWTRR
YPSSWDVNNA WSQNDLIAPQ IANNQASFRD RLYNLLTGPS NFNMFSNSAW FASSNTANPD
SLESVHDAIH SITGSNGHMT YLDFSAFDPI FFLHHAMVDR VWALWTATHG GANGGDTSSY
VQQAASTGSS FYYAQGTNIN ADFPLSPFHR DANRNLWTSN QVKQTSTFGY VYPETPQNVN
PADVTRRIAQ LYGQSTTGNR KRDLVNLSKR DDGHHYHYIT NIASQKFQMN GSYAVYVFLG
EPPANPAEWS TSDKLVGTHG IFSNMPDKNS VGMSQMDVLV TGTIPLTSTL LNKCKTGEVK
DLDPSNVEPY LQQNLNWRVG MFDGTAVDAG DVPGLSVTVV TSDVTPPSSD DQMPVWGHFA
SLPNITVDKI GGHIDKLWAF SEKWSFGELI NEGMKSKKFS LW
//
