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Database: UniProt
Entry: E3QP00_COLGM
LinkDB: E3QP00_COLGM
Original site: E3QP00_COLGM 
ID   E3QP00_COLGM            Unreviewed;       761 AA.
AC   E3QP00;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE            EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN   ORFNames=GLRG_07602 {ECO:0000313|EMBL:EFQ32588.1};
OS   Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS   anthracnose fungus) (Glomerella graminicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN   [1] {ECO:0000313|Proteomes:UP000008782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
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; GG697363; EFQ32588.1; -; Genomic_DNA.
DR   RefSeq; XP_008096608.1; XM_008098417.1.
DR   AlphaFoldDB; E3QP00; -.
DR   STRING; 645133.E3QP00; -.
DR   EnsemblFungi; EFQ32588; EFQ32588; GLRG_07602.
DR   GeneID; 24412967; -.
DR   VEuPathDB; FungiDB:GLRG_07602; -.
DR   eggNOG; ENOG502R1BY; Eukaryota.
DR   HOGENOM; CLU_013691_3_0_1; -.
DR   OrthoDB; 1908494at2759; -.
DR   Proteomes; UP000008782; 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:UP000008782}.
FT   DOMAIN          103..120
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00497"
FT   DOMAIN          325..336
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
SQ   SEQUENCE   761 AA;  84778 MW;  2426777D33DA17A9 CRC64;
     MSVDVNALKS AQARGLTVGV IPKGVGKPLR LEIDDFLQDV ELANLYFLAL EAFMSKKLSE
     SPFSYYEICG IHGQPWRAWD GVKSAEFGFS AGSPDPQSGY CSHGSVIFPT WHRVYVAQFE
     QALYLHAAEI APKLKAQAAL DRFRIPYFDP FLPRQKLVTE DIYTYGIPVI FLLPHIQVRR
     PESPSSWVSM ANPLYQFKFP ADGKGGFDWS MYTQIPAARD LTIRGLNTAT QSADHSYVMR
     AFDNAYNPVS GLSSQTPQSI WHVMFGKQTW VQMSNHYDPR TRDPASVVYN ANSLEGFHDN
     IHNQLATGPQ GSSGHMGSPA FAGFDPSFWL HHCNVDRLLA IWQGIHSLDP ESVAWWTSLE
     VPEGNFVEPG RLAETPRTPL VPFRKGLTAD SKPIWWTSNE CRNHLDLGYD YPQTAAARKS
     GDIVRSLTAW ANTQLGWLAP RSPRPADEGA RAQLKRQINQ PMPFFPLKVL IDGKTPFSNG
     QAFIGSMATT MTARISANNK PLSVSRRLLN RAKTVIKVYS PRRRHRKPTE VTAGSGVTIN
     RSSDSIATPQ QLSQLVLSTA LPSANMDFNR CYGHLGDLIS HHKMTHWNAT FSVDKFSLDG
     SFTIFFFLGD FSPDVESWII DPHLVGSSGI FANSRATITI GACANCAKQE AGGIKYMDTI
     ALTPALLTYW DSQEEHYGCR VGDLSPDYVL PFLTRNLHWR IVNSHGAQVP RETITSLKVM
     VYSEIVTLPH NITDKPQFEG QNVHYEVTNG RPGGIHTGED M
//
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