ID A0A165R782_9APHY Unreviewed; 628 AA.
AC A0A165R782;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=DAEQUDRAFT_667696 {ECO:0000313|EMBL:KZT70397.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT70397.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT70397.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT70397.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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}.
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DR EMBL; KV429051; KZT70397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165R782; -.
DR STRING; 1314783.A0A165R782; -.
DR OrthoDB; 2785948at2759; -.
DR Proteomes; UP000076727; 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.
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:UP000076727}.
FT DOMAIN 95..112
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT REGION 416..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..461
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 628 AA; 69211 MW; 6F61C8FBEA2AB2C1 CRC64;
MTEQPLRPII TGATGGQALV GSLAPNRLEF RDFVKDKKLL ALYVQALDVI FKEPFDNDFS
WPAISGIHGM PYVRWGDSGP ANSPDGDTFG GYCTHGSVLF PTWHRPYVSL FEQSMQAAAL
NVAEHYTTDK PGWTQAAQNF RVPFWDWARP IPEGQPAVPQ EMRSETITIV TPQGEKAVKN
PIHSFTFLSQ FPYTTFDAPY NGWQTTLRYP TSNDPDAKSQ MDLFNSTYGQ DNSQLRIWTY
QMLTRLVTWD YFSNHTTKQN PPIANSLETI HDQVHNLIGG VDYQGHMSDV PVAGFDAAFF
LHHANVDRLL SLWQAINYDV WVTPGDQPGG TYTIKDDGPI NVQSDLTPFW LTQSSYWKST
EVRDWAGSLN YSYPDFDGLK GASLPEMRKA ILQRVAKLYG PTPLPFNPGG PIIPAGGSGS
IQPGGPIIPA GGSGSTQPGG PKIPLGGGPG PVQPGGPEKP PTTQSNPGDS TTVQFNSATH
EWTVHIRFKK FELGKSYSIQ VFLGETYVGS VSAFTSGSAQ RCENCRNNMN VELEGFVVLN
EAIWAKVHTL APDVVVPFLS EQLHIEVKGR KPDGTPAIIE RDLPSLKVAP FSRHVHQHAP
HEVPRLGDVT YHHDILAGKS GHTPADRW
//
