ID A0A4Q4UM29_9PEZI Unreviewed; 508 AA.
AC A0A4Q4UM29;
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 ORFNames=DL767_009207 {ECO:0000313|EMBL:RYP21691.1};
OS Monosporascus sp. MG133.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariales incertae sedis; Monosporascus.
OX NCBI_TaxID=2211645 {ECO:0000313|EMBL:RYP21691.1, ECO:0000313|Proteomes:UP000293831};
RN [1] {ECO:0000313|EMBL:RYP21691.1, ECO:0000313|Proteomes:UP000293831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG133 {ECO:0000313|EMBL:RYP21691.1,
RC ECO:0000313|Proteomes:UP000293831};
RA Robinson A.J., Natvig D.O.;
RT "Complete Genomes of Monosporascus.";
RL Submitted (JUN-2018) 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:RYP21691.1}.
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DR EMBL; QJNX01000374; RYP21691.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q4UM29; -.
DR STRING; 2211645.A0A4Q4UM29; -.
DR Proteomes; UP000293831; 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; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 2.
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; 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:UP000293831}.
FT DOMAIN 250..261
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 165..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 508 AA; 56570 MW; 8CE8FA075B5CEAD7 CRC64;
MAAASLVKSN SIPIIGLTTG IDEETGTRPA RRNINELEVE AGPIWDLFIR ALSALEDDSD
SEENSYFGVA ERSTPAPADY KQQILGQKVQ QLANEYSGKD ASAYKAAGQT FRLPYWDWAS
DARIPPSCTR QNITVNAPKG PITIRNPLYS YKWHQYPLDQ GLFPGSESLE NETTRSPNPA
SHFPVEDVNT KLAAQARQIK LKVYYAFAFA DTYEKMASMT GNGNSFESPH NDVHNLVGGS
FATLTVTSFD PLFMLHHCNL DRLAAIWAAI YFENTVQTTP YQSGGLFATA KGEDITADSP
LKPFYQADGK TFHTSRSVRD ITQFGYTYPE LQDLDLDVHQ NALRVTELVN DLYGSLPARR
LSRAHSRGYG AQSLREWVVS VEVERSELEI PCTINIYMGD RYAGRTTLLD MPRNGILFDE
IPFAEAIGAS EFRGMSPDAV EGLLEKELRF EIKKDDGTVL DPTKVPSLRL DVQGFDLQPP
SSLSELPKYS DKYTYSKVFA QYNGTPTL
//
