ID A0A2S7Q4F8_9HELO Unreviewed; 669 AA.
AC A0A2S7Q4F8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=CJF30_00008247 {ECO:0000313|EMBL:PQE21375.1};
OS Rutstroemia sp. NJR-2017a BBW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Rutstroemiaceae; Rutstroemia.
OX NCBI_TaxID=2070414 {ECO:0000313|EMBL:PQE21375.1, ECO:0000313|Proteomes:UP000238072};
RN [1] {ECO:0000313|EMBL:PQE21375.1, ECO:0000313|Proteomes:UP000238072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJR-2017a BBW {ECO:0000313|EMBL:PQE21375.1,
RC ECO:0000313|Proteomes:UP000238072};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-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 -!- 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:PQE21375.1}.
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DR EMBL; NJPT01000028; PQE21375.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7Q4F8; -.
DR STRING; 2070414.A0A2S7Q4F8; -.
DR Proteomes; UP000238072; 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; 2.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR041640; Tyrosinase_C.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF132; 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 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000238072}.
FT DOMAIN 324..335
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 669 AA; 73297 MW; E13AF4B790535C9A CRC64;
MAAVNYPVTG PPKLSPAPAD GSVPLRLEIR DLQRNHPDQW TLYILGIQAF QQLDEKTDLS
YYGIAGMLPL LLAGPYLLCK VFMDVLTDLG VASRAIILEA GKDIALTVPF SLHHGIVHTW
HCSSNPANRR QQALYAIVQK IASSFPAATK ARYQDAALTF RIPYWDWAAD PPSGDKYFPT
VVGQPSISIV TPTSDGKPVL IANPLYSFKF NPLNPLKGDF PSAPKQENRW PTTLRYPTSG
SASAKSQEQQ VFDAMASQFD SYQNNIYLIM RDPNYKRFDA FSNHQWAPNN APGTYGSIED
VHNSIHSETG GGGQMGDPDY AAFDPLFWLH HVNVDRQFAI WQALNPTSYA IDKPSGDGTF
SIQSGTQETS KTPLAPFNDA TGKTFWNSDG ARYTTTFNYA YPETQQWKFP TQQQYQNSVL
AAVQKLYGAT SNQFMSLMGV NTTALAAAPQ AQLQGLVAGQ KPLQQAAQPA ELSRGGEDFE
AQIGKADPSS KNISAPIKYR EYIANIRAPK HILHQTYRVR IFLGDFNSDP TTWATEQATV
GTFSSFGKDP QTTGCGKCIK DEARELMISG TIPLTPILLK LYKAGDLGSL EKENVIPYLT
KNLHWRVTLA DGTEIDRGNV RGLKVSVVST VVECGGQAHG GLPSYSGVYE VHTEVTGGRP
AGLADEDDV
//