ID W9XAE4_9EURO Unreviewed; 528 AA.
AC W9XAE4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-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=A1O3_09668 {ECO:0000313|EMBL:EXJ77442.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ77442.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ77442.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ77442.1,
RC ECO:0000313|Proteomes:UP000019478};
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 Capronia epimyces CBS 606.96.";
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:EXJ77442.1}.
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DR EMBL; AMGY01000010; EXJ77442.1; -; Genomic_DNA.
DR RefSeq; XP_007737952.1; XM_007739762.1.
DR AlphaFoldDB; W9XAE4; -.
DR STRING; 1182542.W9XAE4; -.
DR GeneID; 19173752; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_6_4_1; -.
DR OrthoDB; 5491711at2759; -.
DR Proteomes; UP000019478; 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; 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:UP000019478}.
FT DOMAIN 3..345
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 360..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 56308 MW; 010352625EBAAB8B CRC64;
MAEVKVLIAG AGIAGLATAI ALRRLDSAEL RLDIQLYEKA RELKEIGASI ALSPNGLRTL
ERLGVANALD DAVGFRGPSG LPMIYRHWKT NEVVSVDEFV DVPDRRHQTA RFHRAHLHEA
LLEYVDRRTI HLNKAVRSAE VEGEADGDGV RLFFDDGTSV RGDILIGADG LRSKVRAAFR
PQHSLHWTGR TLFRSTFDAE LVEGGLIPDL PPDSTHWWGP KHTFFASRLG KNLYTTVGNF
DPAAARAIGQ SQPQTQQIQW DQEGDVAVFR ELYKGWNPVV KALTEATPYV RLYPNLAGAP
LDTWVFGSRV TLVGDAAHTH GGAHAAGGSL ALDDAWALYL AFRHVFAALG LVPGSAGAGA
DSTGADSAGA DNAGAGASAT NNPTTQPTAS IPVPVPLQVQ DIHRALSLYD RTRRPHTERL
VKSVLGAGGA GAGAGTGAAA AAAAVTPVSE SDEDEDEALR LKMKNRPSTT WLAEHDVEAA
FAEVLDQDKH NHSHGHKGNT QGRGFGIGVR VGVGGLPTPA HGRDQSRL
//