ID V9DIC1_9EURO Unreviewed; 410 AA.
AC V9DIC1;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN ORFNames=G647_10376 {ECO:0000313|EMBL:ETI26615.1};
OS Cladophialophora carrionii CBS 160.54.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1279043 {ECO:0000313|EMBL:ETI26615.1, ECO:0000313|Proteomes:UP000030678};
RN [1] {ECO:0000313|EMBL:ETI26615.1, ECO:0000313|Proteomes:UP000030678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 160.54 {ECO:0000313|EMBL:ETI26615.1,
RC ECO:0000313|Proteomes:UP000030678};
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 carrionii CBS 160.54.";
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}.
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DR EMBL; KB822702; ETI26615.1; -; Genomic_DNA.
DR RefSeq; XP_008724589.1; XM_008726367.1.
DR AlphaFoldDB; V9DIC1; -.
DR GeneID; 19988869; -.
DR VEuPathDB; FungiDB:G647_10376; -.
DR HOGENOM; CLU_009665_19_5_1; -.
DR OrthoDB; 5491711at2759; -.
DR Proteomes; UP000030678; 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:SF309; PUTATIVE (AFU_ORTHOLOGUE AFUA_6G14510)-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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..410
FT /note="FAD-binding domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004773419"
FT DOMAIN 2..362
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 410 AA; 45431 MW; 442E318A873A018F CRC64;
MKITVIGAGI SGLSVALALT KWLPEKPDIT IIELRPEPST IGGAVGLTPN ALRCLHHLGV
LSRIHENSLG ATIDKIELFT IHTGARLGEI GFTGAQGEGV GQPPFKGLRI MRADLVQSLT
ECVRNLNNVR FAYGRRPTQI IESDAQITVH TDDGDTMTSD LLLGCDGIHS FVRTNLVDPE
RTPLYTGIAA VFGFAGLDDE AQVPWKDTGL CQAKRGSLMT SYYEPQRKRQ FVAAIMETED
VISKEGWLAR GSEQDKIRQN VKGRFGNSAI GFLNSLIDAT DHWTLYPVFS LAPRGKWCTT
RAMLLGDAAH AMPPQGESTG YALEDAILFA RAMAVKLDKG LDVTFATYQK VRRERINKAY
DEAAFGWETQ KDCGWFTFLL RTWLTTAFLW WTAAARQRRY SEDVTKMDLE
//
