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Database: UniProt
Entry: A0A166RW27_9PEZI
LinkDB: A0A166RW27_9PEZI
Original site: A0A166RW27_9PEZI 
ID   A0A166RW27_9PEZI        Unreviewed;       464 AA.
AC   A0A166RW27;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:KZL69832.1};
GN   ORFNames=CT0861_01054 {ECO:0000313|EMBL:KZL69832.1};
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:KZL69832.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL69832.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL69832.1,
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 beta-cyclopiazonate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00043981}.
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:KZL69832.1}.
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DR   EMBL; LFIV01000100; KZL69832.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166RW27; -.
DR   STRING; 708197.A0A166RW27; -.
DR   OrthoDB; 1771364at2759; -.
DR   Proteomes; UP000076552; Unassembled WGS sequence.
DR   Gene3D; 1.10.405.20; -; 1.
DR   Gene3D; 3.30.70.1990; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR42923:SF26; FMN REDUCTASE LOT6, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G06600)-RELATED; 1.
DR   PANTHER; PTHR42923; PROTOPORPHYRINOGEN OXIDASE; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..464
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007879245"
SQ   SEQUENCE   464 AA;  50182 MW;  A96BAC8F78877563 CRC64;
     MRSQLLSLCA LGASLINASP VGLGCYDESA FKPEDIIQRD VLIVGGGATG AYAAVRLRDQ
     NKTVAVVERA DKLGGHVNTF RDPASGAPID YGVQAYIQND QTTQFFERFG VQLNASALSP
     FPSRVVDFKT GFVIPNATAV DPNTLVGPLA NYLFATLNFD FLAQGAYDIP ENVPEDLLLP
     FGQFVEKYNL TDVVQVVWIF AHGVGNLLET PTLYVLQNFG QPHLLGLSAG YLYAPGGNQQ
     VFDKAGAFLG SDVLYSSVVV TSKRTDNGVT AVVATANGRK LIKAKKLLLT IPPTVENLAP
     FDLDDSEISV FEQWQDVPYY VGVVSQSGLP DLTNFLNVDI TAPDALPQTP FVWRLETVGV
     PGYQTVKVVG EPDSSKAQGL VSDAIRKVGA STNATFTTGG DFSAWEQHAN LQLHVSPEAV
     KAGFYRDLYA LQGKRSTYYT GNAWCSDYSP LLWAFTETRI LPSL
//
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