ID A0A072NX41_9EURO Unreviewed; 462 AA.
AC A0A072NX41;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN ORFNames=A1O9_11670 {ECO:0000313|EMBL:KEF52429.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF52429.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF52429.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF52429.1,
RC ECO:0000313|Proteomes:UP000027920};
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 Exophiala aquamarina CBS 119918.";
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:KEF52429.1}.
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DR EMBL; AMGV01000018; KEF52429.1; -; Genomic_DNA.
DR RefSeq; XP_013255019.1; XM_013399565.1.
DR AlphaFoldDB; A0A072NX41; -.
DR STRING; 1182545.A0A072NX41; -.
DR GeneID; 25286567; -.
DR VEuPathDB; FungiDB:A1O9_11670; -.
DR HOGENOM; CLU_009665_19_0_1; -.
DR OrthoDB; 1113861at2759; -.
DR Proteomes; UP000027920; 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:SF314; FAD-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR13789; MONOOXYGENASE; 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:UP000027920}.
FT DOMAIN 74..349
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 462 AA; 51425 MW; 4B3EFE9CC2CA3B14 CRC64;
MAESFRIIIV GGGIGGLSAV RYRATEDTNL LRISQAIALR KDDREITVLE QSSLNREIGA
TISLQPNASK IVERQWGLEA PLHAKGSMID QGFQVYNLDG ELQMRQPLNT TAKYGSERML
YHRVDLHDVM KSRCTDSAYS GRPVTIRVSS KVVSCDVEQG TVVLESGERL TADLIVAADG
IKSTIREAVL GDRVDPMPTG HSAYRIVIPM DEIASSQAFT DVLNPQESFT TMVLGHDKRL
IMGPARNSSI YSIVAMIPDE TMHESSTESS WNTRADLSQM LSTFKDFPAW ARVPLELAKE
AGLWKLRDID PLRTWYRGRA ILIGDAAHAM LPTQGQGASQ TVEDAEALGA FFCGTSGNQT
AIDIEAINKL VFDCRYERAT LIQTFSRQAA RPATDLSDHT IKMNPNEFMH YNFDYTGALD
WIKRHDLPTP RRQESDKAFG SKFTSMDKGD TDFRRLLQVV EP
//
