ID T0KIM9_COLGC Unreviewed; 628 AA.
AC T0KIM9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Multicopper oxidase {ECO:0000313|EMBL:EQB52044.1};
GN ORFNames=CGLO_08352 {ECO:0000313|EMBL:EQB52044.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB52044.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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:EQB52044.1}.
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DR EMBL; AMYD01001681; EQB52044.1; -; Genomic_DNA.
DR AlphaFoldDB; T0KIM9; -.
DR STRING; 1237896.T0KIM9; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_7_3_1; -.
DR OMA; RGYEQCE; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:InterPro.
DR CDD; cd13851; CuRO_1_Fet3p; 1.
DR CDD; cd13877; CuRO_2_Fet3p_like; 1.
DR CDD; cd13899; CuRO_3_Fet3p; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR001117; Cu-oxidase_2nd.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR044130; CuRO_2_Fet3-like.
DR PANTHER; PTHR11709:SF361; IRON TRANSPORT MULTICOPPER OXIDASE FET3; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; Cupredoxins; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..628
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004579056"
FT TRANSMEM 556..578
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..148
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 157..304
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 365..499
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 586..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 628 AA; 67870 MW; 99534A33EEAE8961 CRC64;
MDFTARACRF GLLAALLLQP ASAATVSHDF NIGWVTANPD GAFARPVIGI NGQWPIPRID
ANVGDTILIN VQNNLGNQST SLHFHGLFMN GTTHMDGPSQ VSQCAIPPGS SFTYNFTIQQ
PGTYWYHSHT QSQYPDGLRG PVVIHDPDSP FKGQYDEEVV VTLSDWYHDQ MADLIPPFMS
KGNPTGAEPV PQAALMNDTQ NLTVTVQPGK TYLFRMVNMA AFAGQYVWIE GHNISIVEVD
GVYTEPADAS MIYLAAAQRC SFLVKTLNDT GSNFAIVGSM DTSLFDTLPP DLNYNVTGWL
VYDSSKPMNQ AATLDNFAPF DDMTLIPYDK QPLLTSPSQT VELDVIMDNL GDGANYAFFN
DITYKAPKVP TLYTALSAGG NATNPQVYGT YTHSFVLERD EVVQIIVNNL DPGRHPFHLH
GHNFQALYRA PEEGGTFENA NVSEADFPKT PMRRDTLVVW PNGNIVLRFK ANNPGVWLFH
CHIEWHVTSG LMATFVEAPL DLQKSLTIPQ NHKDACAAGN VPITGNAAAN TLDYLDLSGQ
NTPPARLPDG FTARGIVALV FSCITGILGV LVVAWYGLAK TNDGPSGAGY AAPTTGTASG
AGHVSKDQHQ KEPIIVGAGS GSSATART
//
