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Database: UniProt
Entry: A0A166U747_9PEZI
LinkDB: A0A166U747_9PEZI
Original site: A0A166U747_9PEZI 
ID   A0A166U747_9PEZI        Unreviewed;       468 AA.
AC   A0A166U747;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=FAD-binding domain protein {ECO:0000313|EMBL:KZL73029.1};
GN   ORFNames=CT0861_06817 {ECO:0000313|EMBL:KZL73029.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL73029.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL73029.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL73029.1,
RC   ECO:0000313|Proteomes:UP000076552};
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 paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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:KZL73029.1}.
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DR   EMBL; LFIV01000049; KZL73029.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166U747; -.
DR   STRING; 708197.A0A166U747; -.
DR   OrthoDB; 2678872at2759; -.
DR   Proteomes; UP000076552; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR13789:SF315; FAD-DEPENDENT MONOOXYGENASE MDPD; 1.
DR   PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076552}.
FT   DOMAIN          24..57
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          127..344
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   468 AA;  51154 MW;  EF89AB94DAC35927 CRC64;
     MTVAQTSTGT VDDVARSSRT GIQVVIVGAG IGGLMTALEC WRKGNDVIIL EKAEKISVIG
     DILAIGPSAW VTLQNYPKMA KDYDKFKLDT TFGFYSQQGE LLRGPQEIEW NGPAVAKHAS
     YPTRIGAVAA RQDIVALLFN QVQRLGIKVE FGTNIIEFSE DANRGTATAR AFDGREFTGD
     LVVAADGLGT KSHTVVLGRP ISAVHSGYAC LRGSFPTEAV QDVPTKTHLI LTLTHQRVYV
     ALTVQDDGTA EESWSKTISG SEIAAQLSSS GEWDKAVIDC FENAPDGCIV SWKLCWRDPQ
     PKWTSKWSRI IQLGDSAHSF LPTSGNGGTM AVEDALSLAE CLRMAGKADV PMASKVHETL
     RYRRVSLIQK TGFVNLREMH QDMKAIISKG STPMLLGKWI WAHDPELYAK DNYEAARAAI
     ETTTSFENSN LPPGHKWEPW TMAEELEKEA SGVFFQDLKT NGDWGVLA
//
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