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Database: UniProt
Entry: T0KKV2_COLGC
LinkDB: T0KKV2_COLGC
Original site: T0KKV2_COLGC 
ID   T0KKV2_COLGC            Unreviewed;       498 AA.
AC   T0KKV2;
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:EQB56232.1};
GN   ORFNames=CGLO_03769 {ECO:0000313|EMBL:EQB56232.1};
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:EQB56232.1, 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:EQB56232.1}.
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DR   EMBL; AMYD01000773; EQB56232.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0KKV2; -.
DR   STRING; 1237896.T0KKV2; -.
DR   eggNOG; KOG1231; Eukaryota.
DR   HOGENOM; CLU_018354_1_1_1; -.
DR   OMA; QLWGGFT; -.
DR   OrthoDB; 879734at2759; -.
DR   Proteomes; UP000015530; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
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; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR   PANTHER; PTHR42973:SF27; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 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..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..498
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004579122"
FT   DOMAIN          61..234
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   498 AA;  54232 MW;  E58D55624E22A9FA CRC64;
     MKFSTSGLAL LALAGSALSA KSRGPQCSCC TALASDENLK GKVFGKDSAV YDARLKSYYS
     ANAAQEAWCM VLPEGTQDVS AIAKIISKHE CPFGIRSGAH SAWKGSNGVK SGVTIDFGYM
     NATTYDADSK VASICPGSNW GEVYKALDPY GVTAVGGRAS VVGVGGFVTG GGYSFHTNSR
     GFSCDQVTNF EIVLADGTIV NANEHENADL WKAQKGGSGN FGFVTRIDQR VVESTQMWGG
     FFTYNQTKRD AVFDAYMNFA NHMDEDLASQ NIVALYYDKT GYTLRSILSN VDANPEAPAF
     SEYFAIPNIS TTASVGAVSD LVPQFTGPTP LGLYANWFVG QTAHDVRMLK FIDDKLKEYS
     PKMKAAAPDS DFNTLIQFQP VTQSIVQHSA QSGGNVLGLE DVVADGPTLM WLIALTVDTE
     ANQEILLPYI FKFRMEIDNY AKDLGLYKDW KYTNYAWGDQ DPLATHGYKN FDFMSEVAEQ
     YDPEGVFQNL RRTGFKLA
//
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