ID A0A167BS04_9PEZI Unreviewed; 500 AA.
AC A0A167BS04;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Fad binding domain-containing protein {ECO:0000313|EMBL:KZL81663.1};
GN ORFNames=CI238_07806 {ECO:0000313|EMBL:KZL81663.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL81663.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL81663.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL81663.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KZL81663.1}.
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DR EMBL; LFIW01001609; KZL81663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167BS04; -.
DR STRING; 1573173.A0A167BS04; -.
DR Proteomes; UP000076584; 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 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; 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:UP000076584};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..500
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007884362"
FT DOMAIN 68..240
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 500 AA; 53505 MW; AD7544C61F02B1DF CRC64;
MRFNSILSLA VTALPLTAAK PLPADAQNSK AGNSSNTIQA CLNAANAPIT TSSSSDWPED
IRPYNARVQF TPALVVTATD AIHVQAAVKC ASQYGKSVTA RGGGHSYSSS GLGGENGHVV
VRLDEMFSVR LNADNTATVQ AGARLGHVAT TLFNQRGRAI SHGSCPGVGA SGHSIHGGFG
FSSHLYGLAT DWIIEATVVT ADGKIVKASA SQNADLFWAI RGAGSSFGIV TEFKFNTFAA
PSVVTWYKVP FTLKKDKLIA ALVALQKYAQ GDMPAELNMR AVITPDSTAF DGLYFGTEAQ
TRSVLKKFLS PLGIDIGGAT ITQTDWIGQL QHYAGQELDQ TGPQSATDTF YASSLMTKEV
SQEGFKAFAN FYQNTAKSTY TGWFVLIDVH GGKNSKTAQV ANSATAYAHR DKVLLWQFYD
SSSGSAYPSS GYSFLGNWMS SVTSTMAKSD WGRYVNYADS QLSKADAQDQ YYRDNLPRLR
TIKAKYDAKG LFTYPQGVGS
//
