ID W9WYG1_9EURO Unreviewed; 398 AA.
AC W9WYG1;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN ORFNames=A1O5_03012 {ECO:0000313|EMBL:EXJ73252.1};
OS Cladophialophora psammophila CBS 110553.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ73252.1, ECO:0000313|Proteomes:UP000019471};
RN [1] {ECO:0000313|EMBL:EXJ73252.1, ECO:0000313|Proteomes:UP000019471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ73252.1,
RC ECO:0000313|Proteomes:UP000019471};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:EXJ73252.1}.
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DR EMBL; AMGX01000004; EXJ73252.1; -; Genomic_DNA.
DR RefSeq; XP_007741815.1; XM_007743625.1.
DR AlphaFoldDB; W9WYG1; -.
DR GeneID; 19187742; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_19_1_1; -.
DR OrthoDB; 1422702at2759; -.
DR Proteomes; UP000019471; 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; PTHR13789; MONOOXYGENASE; 1.
DR PANTHER; PTHR13789:SF236; MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G12060)-RELATED; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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:UP000019471}.
FT DOMAIN 2..304
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 398 AA; 45101 MW; 4F5C9B6F5DD743C7 CRC64;
MHHAGFEVVM FEKVREFQRL GDSLGLGENA FKLLDRWSPF LRDHLIEIGN KSEFMQIRRW
HDGKLLAQQP LMDMAGYIGH RGDYHRGFLE AVAEKGIPLH MGSEVVEYDD LTPSVTLKDG
ERHFADVIIA VDGIKSRARE LVLGFDDKPK SSGYACFRAF FKGDKLKGDP LTAEFVENEC
VNIWIGKDMH VVQNTLRGGD EFNWIITHKD TADIQESWSQ PGDMDEVRRL VATLDPRIAA
AIRKTDECLD WKICYRDPIP TWVSKNHKVA LVGDCCHPHL PTSAQGASQA TESAAVLAQC
LLLAGRDNIP LATRVYEKIR FPRVRRSQTN GEDLRDRWHT ALDRMADGGD GEIDRDSLLI
KNNVLYDYDA EADTRKRWAE MAALVGEELR TGRITPLC
//
