ID M3C4F8_SPHMS Unreviewed; 392 AA.
AC M3C4F8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Di-copper centre-containing protein {ECO:0000313|EMBL:EMF15171.1};
GN ORFNames=SEPMUDRAFT_147120 {ECO:0000313|EMBL:EMF15171.1};
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:EMF15171.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF15171.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF15171.1,
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).
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DR EMBL; KB456261; EMF15171.1; -; Genomic_DNA.
DR RefSeq; XP_016763292.1; XM_016904094.1.
DR AlphaFoldDB; M3C4F8; -.
DR STRING; 692275.M3C4F8; -.
DR GeneID; 27901231; -.
DR eggNOG; ENOG502QRET; Eukaryota.
DR HOGENOM; CLU_035914_0_0_1; -.
DR OMA; FNFLAWH; -.
DR OrthoDB; 4070889at2759; -.
DR Proteomes; UP000016931; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF141; N-ACETYL-6-HYDROXYTRYPTOPHAN OXIDASE IVOB-RELATED; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 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:UP000016931};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..392
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004032529"
FT DOMAIN 314..325
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 392 AA; 43817 MW; EFFACE16B2116192 CRC64;
MRFATTVACV ATAGLVAAQA PSISDYSAQQ IASGEAWRNI STIADESMQS NIGSRSNAQC
TYENAAVRQE WRTLSPETRK SFTDAVTCLQ NHAPTRMTAA EAPTYPGVKS RYDEYVATHI
NYTLNIHDTA DFFAWHRAFI HFMEQDLINL CGYTGVMPYW NWAEDAAAPQ DSALFSGDAY
SMGSNGRYIA GRSDTWLAQQ DVTYSPGTGG GCVESGPFSE YTVNLGPLGL PNYDNVDTPF
QYNPHCLERD INPWFSTRYN TYERLTSVVL DYIYIEDFQC QSQGMCGDNK FGVHGGGHWQ
TGGSMMDFYS SPADPLFYVH HAQVDKMWVI WQNLDIYRRQ NIIKGTGTLG CSSPDCPEMT
LNDRLPFGLV ADDQTFSTLM DNFAGPFCYR YD
//
