ID T0LLL7_COLGC Unreviewed; 695 AA.
AC T0LLL7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Multicopper oxidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CGLO_07772 {ECO:0000313|EMBL:EQB52591.1};
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:EQB52591.1, 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:EQB52591.1}.
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DR EMBL; AMYD01001565; EQB52591.1; -; Genomic_DNA.
DR AlphaFoldDB; T0LLL7; -.
DR STRING; 1237896.T0LLL7; -.
DR HOGENOM; CLU_006504_3_2_1; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd13854; CuRO_1_MaLCC_like; 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 PANTHER; PTHR11709:SF71; LACCASE; 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; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530}.
FT DOMAIN 120..236
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 246..425
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 521..632
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 674..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 695 AA; 77292 MW; D981D0121FBBB010 CRC64;
MLSLRHVWII VTDVANSLFG SPFLGQGFQY PIGAKFGASR PGIEAVKSGG PIFRPPGSNI
DDFWCDYSTT MPGFEHCGTS GDQSCWLRNP TTGEEFNLST DYEDINQTPK GVTRVYYLNV
TDGPINANGL DFRQGKLFNG TFPGPLIEAC WGDTVIIHVR NHLQYNGTSI HWHGLRQWQT
MHMDGVNGLT QCPIAPGSEF MYNWTAMQYG SSWYHSHYSV QYADGLQAPI TIHGPSSYPY
DVAIEPITIT DWANNSAFQN IAPSRGGRAD TMDVLLNGTG DITRFTGGQT MNTDTIPPRF
ELSFDDAAPN PMTGAKRYLL RLINTSFGNS FIFTIDNHNL TVIEADFVPV HNFNTTSILV
AIGQRYNIIV EATPIVNVSN PSANPIPKDG NFWIRTYAPQ NSDVLESYYH VDQNTYMKTG
VLRYDKTSTT DPTTTGWNIS DTDSDKSIND QLKPILQWSV QKPANWDNSP EVFNIVPTKG
EGHYATAFVA FQRNGTTDVN PFQTTYGNPT FLNLDNVGDE WPAGWFVVPE NYTDNDWIFL
VIDKPKLGPH PIHLHGHDFA IVQQSDNSSF DMNNFNQNRP DVNFPRRDVV LVTKTGHAVI
AFKADNPGIW LMHCHIAGHA SGGLSLQIME RQKAANGIWP PGNSDALNEA HKLCASWNSW
SYDCKNLWPG NTGNSQKAEY PSCKDSTNVQ NDSGV
//
