GenomeNet

Database: UniProt
Entry: A0A0G2EWS7_9PEZI
LinkDB: A0A0G2EWS7_9PEZI
Original site: A0A0G2EWS7_9PEZI 
ID   A0A0G2EWS7_9PEZI        Unreviewed;       654 AA.
AC   A0A0G2EWS7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE            EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN   ORFNames=UCDDS831_g01201 {ECO:0000313|EMBL:KKY26541.1};
OS   Diplodia seriata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY26541.1, ECO:0000313|Proteomes:UP000034182};
RN   [1] {ECO:0000313|EMBL:KKY26541.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY26541.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY26541.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY26541.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) 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:KKY26541.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LAQI01000031; KKY26541.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2EWS7; -.
DR   Proteomes; UP000034182; 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:SF32; 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   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..654
FT                   /note="tyrosinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002543608"
FT   DOMAIN          138..155
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00497"
FT   DOMAIN          341..352
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
FT   REGION          30..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   654 AA;  72689 MW;  FFDBBB5323AAB6C5 CRC64;
     MREALGRRLL ALAISGSCLL STVAGTPLNP AHQQISREPH GAHSLGSLTK SKRQQTGGES
     LAVTGIDHDE VQPRLEIRDL AKNEFQWNLF LLAMQRFQQT DQDERTSWYS VAGIHGKPYQ
     TWDGVQPQGQ QNSGYCMHSS NLFLPWHRPY LALYEQTLQG LMTEIVDEWS ESPESDNYTE
     AANSFRLPYW DWAVLPPDGE KSVPEFLSSP TINVTRPNGT ETIENPLYSY KYHPLNGDAL
     YDSGTPQFSV YPQTMRYPPT QGADSQSQDD QFVSTMDKNR PQLRDALYDL FTNYHNFTIF
     GNMASYKAGQ FQSVEAVHGW VHIWAGGNYG NMYHVPWSSF DPIFMLHHAN IDRIFAMWQV
     LNPDSYVEPW AQAYSTYMVK NGQVLDAESK LYPFHSNTNG EFWTSAKVRD VKTFSYTYPE
     LADEGAMKTT INRLYGQSTV SHRTKRTDVG DAVDGVAEGV TGIINKLVQP GQIDADAAEK
     DERRYEYTAN IKLSKCALGG PGVIYLFLGN FSDSPADWMT DDHLAGSSPL FVMDDSAMGA
     GESQDIYAAV SLTREIEQRV ASEDLGCMDP SEVVPYLKKN LQWRVAKADG SSVPADQVEG
     LEISIAKAAY RPAASDCEFP SLVGVIETLS DITHGKAGGL SSVGSLLGTK GDEE
//
DBGET integrated database retrieval system