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Database: UniProt
Entry: M3C9Q8_SPHMS
LinkDB: M3C9Q8_SPHMS
Original site: M3C9Q8_SPHMS 
ID   M3C9Q8_SPHMS            Unreviewed;       642 AA.
AC   M3C9Q8;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE            EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN   ORFNames=SEPMUDRAFT_152200 {ECO:0000313|EMBL:EMF08575.1};
OS   Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS   musiva).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX   NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF08575.1, ECO:0000313|Proteomes:UP000016931};
RN   [1] {ECO:0000313|EMBL:EMF08575.1, ECO:0000313|Proteomes:UP000016931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO2202 {ECO:0000313|EMBL:EMF08575.1,
RC   ECO:0000313|Proteomes:UP000016931};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(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; KB456271; EMF08575.1; -; Genomic_DNA.
DR   RefSeq; XP_016756696.1; XM_016907299.1.
DR   AlphaFoldDB; M3C9Q8; -.
DR   STRING; 692275.M3C9Q8; -.
DR   GeneID; 27904436; -.
DR   eggNOG; ENOG502RF2C; Eukaryota.
DR   HOGENOM; CLU_013691_3_0_1; -.
DR   OMA; VIAYIPI; -.
DR   OrthoDB; 1908494at2759; -.
DR   Proteomes; UP000016931; 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:UP000016931};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..642
FT                   /note="tyrosinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004031727"
FT   DOMAIN          117..134
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00497"
FT   DOMAIN          324..335
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
SQ   SEQUENCE   642 AA;  69447 MW;  43DAB8C1E3954140 CRC64;
     MKFSSLSSLA LACTSIFAHP VEHNEEHSDI KARQQNYVRL EGGKGNAVQP RLEVRQLKNQ
     QPDQWNIFLV ALDYWMTQST GEAGYYGIST IHGVPRQNYA DVAQCSTCAG ADGYCPHDSV
     LFPAWHRAYV ALFEQEFLKV ALDRANQFPA ATRQRYVNAA TNLRFPYFDW AAVPPNNGPA
     LPTLITDSSV TFQGPNGQQT VRNPLYGYVF RNGEQSGLLY ATLNTYTKTL RYPKSNDPNA
     ANNSPQCAAA FAGSRQSLQD QIYQLFTACD NYLYFSNDDS SDSSGRCSNS LEAIHNTVHN
     NAGGLGGNGI SGGHMTYLST ASYDPIFWLH HANVDRLAAM WQTIHSNSYG ASQIAPHNTW
     TVAQGSNQGP TSGLRPFRRP GTSTSFWTTN QVRDWRQFGY TYPEFSNSDG SAGAITGYVN
     ALYGPNPSAT AGSSKREAAA DPSLLGGVSK VLDEPNILSS LGDILADNPL KASNGSLYQY
     VANIKTARYA LGGSYTIFLF NGNPVSEDVK TWPTDPNLYG PMGVLAQEMS GSGMNMSLIT
     SSSIPLTTKL TSLFGSGVLG SLSELVVAPY LKENLQWRIA KDGSSVDPST IPGFVVTVVT
     SSAQPAADAK SFPVYSPFIE LLGITQDMAG GASETQYGPP SY
//
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