ID W9WYB0_9EURO Unreviewed; 422 AA.
AC W9WYB0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN ORFNames=A1O5_07118 {ECO:0000313|EMBL:EXJ70045.1};
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:EXJ70045.1, ECO:0000313|Proteomes:UP000019471};
RN [1] {ECO:0000313|EMBL:EXJ70045.1, ECO:0000313|Proteomes:UP000019471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ70045.1,
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:EXJ70045.1}.
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DR EMBL; AMGX01000010; EXJ70045.1; -; Genomic_DNA.
DR RefSeq; XP_007745897.1; XM_007747707.1.
DR AlphaFoldDB; W9WYB0; -.
DR STRING; 1182543.W9WYB0; -.
DR GeneID; 19191824; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_19_3_1; -.
DR OrthoDB; 2092435at2759; -.
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: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:UP000019471}.
FT DOMAIN 12..179
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 346..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 46625 MW; 93590F22415E77B8 CRC64;
MSPHAVSNPV LDVIIVGAGI AGLAAAHAIH GAGHHVTIVE GASVLREIGA GVLISSNATR
ELIRWDLEDD LKDVIVQSRV SRVLRWDDGK VLSEVKMDPS FALKKYDAPV WMLHRADLHT
VMLKKVQSLG IEIRLGSRVV DADVAKASVS LASGAVLDCD FIVGADGVRS KMRDIISQTP
VPAMPTGDYA FQFALDIEQH KDDLVIAPLV EGHTATAWWG PGRHVIGTLL RGEKLFNCVA
VFPDDGSLGD EHKQLGADVD ELRRNFSDWC PAVRTILFHA DPGSIVKWKL QDLDPLESWH
RGHAGASQAI EDGAVLAQCL AHLPLDRVGP AFQDLRFSRA TQIQQNARRQ KIENHYPDGP
EQQARDERLK DPTQVRAWRW EPVAGKPTKS WSDGLFGYDS RAECDEYFRE HDARRLFVKQ
AV
//
