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Database: UniProt
Entry: T0KVS5_COLGC
LinkDB: T0KVS5_COLGC
Original site: T0KVS5_COLGC 
ID   T0KVS5_COLGC            Unreviewed;       584 AA.
AC   T0KVS5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=FAD binding domain-containing protein {ECO:0000313|EMBL:EQB56219.1};
GN   ORFNames=CGLO_03785 {ECO:0000313|EMBL:EQB56219.1};
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:EQB56219.1, 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 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:EQB56219.1}.
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DR   EMBL; AMYD01000776; EQB56219.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0KVS5; -.
DR   STRING; 1237896.T0KVS5; -.
DR   HOGENOM; CLU_018354_4_4_1; -.
DR   OMA; TSWYPFY; -.
DR   OrthoDB; 1641938at2759; -.
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; -; 2.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR13878:SF91; FAD BINDING DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_6G12070)-RELATED; 1.
DR   PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 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..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..584
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004566435"
FT   DOMAIN          129..312
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   584 AA;  64147 MW;  1E09049230480F3E CRC64;
     MRISSLVLLY SLLASSTSQI TATNDHQSKL TEGISTLNDT LGGRVHHAEP FALACFTSFE
     GTAISRNESL CAERQENYHS PVYRSNVAAA YMYEQSTICA SDPLSQDQCI LNTADPLNPD
     AWDDVNCRLG NLPSWWLEVR EAQDVVEAFD WARKTGGKLS IKNSGHSFVL DSSMKDSLLL
     WTRNLRQVRH EPIFIPEGCP DEQSFDVITT GAGVSSAEVY EFADTVGRTI LGGYSPTVGI
     SGGWVQGAGH SVLSNVYGLG VDRVIQFTVV TPDGSTRVAN RCQNIELFWA LRGGGGGTFG
     VVLESSHVVE PVVPMAVADI GIPPDDKEAY SGWMDLLVDT AVALAEDGWG GHIYGNSLVH
     VSPLMTTFED AEASLSKLIA FADAHGGHVN ITIAPNWLSF FTDHVLADSV AVGNLRLINT
     RLVPVAVFTN DTLRAGLKGF LREIIGLDGS PYIPVDSPYI FRPDALNPSA VHPGWYDSLW
     IVGQPSIWEW NSTLEERVDI VRQMQANTER QREITPGGFS YMNEANPFMS EWEEVMFGEN
     YERLLEVKRM VDPDGLLSCW RCVGWTDEEA RASCYGAFND VRTT
//
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