ID T0LQD0_COLGC Unreviewed; 474 AA.
AC T0LQD0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=FAD binding domain-containing protein {ECO:0000313|EMBL:EQB53891.1};
GN ORFNames=CGLO_06336 {ECO:0000313|EMBL:EQB53891.1};
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:EQB53891.1, 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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:EQB53891.1}.
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DR EMBL; AMYD01001283; EQB53891.1; -; Genomic_DNA.
DR AlphaFoldDB; T0LQD0; -.
DR STRING; 1237896.T0LQD0; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_018354_0_2_1; -.
DR OMA; TYINFAH; -.
DR OrthoDB; 1068078at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..474
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004580228"
FT DOMAIN 50..223
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 474 AA; 50194 MW; C15276A4BC19E405 CRC64;
MRLLLVGVQF LTMVASAAVD VSARSVADDL LSLVSTSSVG VQVRARWSDF DLPTPSVIVN
ATSEKDLSAV VKYCAKNNIP FLPQNGGNGW ATGQFNLGST GVLINLAGLN QVNISSDKKT
ATIGGGALIG DVITAADAAG VLVQTGNCNC VGALGAALGG GYGNIMGEHG FAVDNILSMR
VITASGEALT ASSTSNPDLY WALRGAGPNF GIVTSATVNA FPTTNRTSWI MSLTFDPANI
ADVAQTIQDL PLLPQQVVYL VLTNSGDASN SPMVLVTGFL REGTEEQGLK AFAPLYNLGP
STNSSAVTPY TSWNAANDNF CARGGRKPAF STTINNMKAE TWPEIWSLYT GFQNQSTAQN
SAVLIERYNL TTAKSKPAGS AAMQDELRQE AFAQAIVIPW YEDATLDSVA ETFGSKVRDI
WSFSSSAVVN PTYINFAHGD EELEAIYGSS LDRLKTLKTK YDPSGVFGQW FKIQ
//
