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Database: UniProt
Entry: A0A066XPH4_COLSU
LinkDB: A0A066XPH4_COLSU
Original site: A0A066XPH4_COLSU 
ID   A0A066XPH4_COLSU        Unreviewed;       503 AA.
AC   A0A066XPH4;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN   ORFNames=CSUB01_08708 {ECO:0000313|EMBL:KDN70777.1};
OS   Colletotrichum sublineola (Sorghum anthracnose fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN70777.1, ECO:0000313|Proteomes:UP000027238};
RN   [1] {ECO:0000313|Proteomes:UP000027238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX   PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA   Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT   "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT   of cultivated sorghum.";
RL   Genome Announc. 2:E0054014-E0054014(2014).
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:KDN70777.1}.
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DR   EMBL; JMSE01000293; KDN70777.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A066XPH4; -.
DR   STRING; 1173701.A0A066XPH4; -.
DR   eggNOG; KOG2614; Eukaryota.
DR   HOGENOM; CLU_009665_12_2_1; -.
DR   OMA; SIGLWPN; -.
DR   OrthoDB; 2332834at2759; -.
DR   Proteomes; UP000027238; 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; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR47356:SF2; FAD-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR47356; FAD-DEPENDENT MONOOXYGENASE ASQG-RELATED; 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:UP000027238}.
FT   DOMAIN          9..345
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   503 AA;  55185 MW;  B6EA78FB61E7A575 CRC64;
     MAANEAKRHQ VVIVGGGITG LTLALMLQNL DVDYVLLEAY GTVTPNVGAS IGLYANGLRI
     LDQLGCYQDI LTKSQPTEET ICRNAASGKR IMTRHAKDAV IRRHGYATIF MERHDLLCVL
     YEHLRDKDRI ILNKKVQRVE TREGSAVVYT ADGSIFEGQI VVGADGVRST IRKEMWRNAD
     DNGDSAAIPA RDRGAIPCEH ACVFGTAKPT PGIKPGDVIS ASGDGTVVGC MGGADGRVFV
     FWFWTLPASQ RSCPIDDIPR FDDEDKRREL ARGADAIIAD NGLRFRAVVD NLKFSGVTAL
     PHFVMRRWHY GRIIILGDAA HKFNPLVGQG GNSCIESCAS LVNALRDRGL AAGGGASWAL
     AQVTEAFTVV ERQRIDRVDK MVEESQDAMR ASAWDTLKGR LMFKYIMPLM PMSLWLNFYS
     EHISGGLSLT GVGSLMRAHE WPYSDEKGAE EKGSVLTRST VVTTLPIAAL TAFFLARVLQ
     KGDVLGGSFV FSRVMEQVSW FRR
//
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