ID A0A0W0GA47_9AGAR Unreviewed; 677 AA.
AC A0A0W0GA47;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=FAS1 domain-containing protein {ECO:0000259|PROSITE:PS50213};
GN ORFNames=WG66_2083 {ECO:0000313|EMBL:KTB45400.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB45400.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB45400.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB45400.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-2015) 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:KTB45400.1}.
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DR EMBL; LATX01000716; KTB45400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0GA47; -.
DR eggNOG; KOG2614; Eukaryota.
DR Proteomes; UP000054988; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 2.30.180.10; FAS1 domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR036378; FAS1_dom_sf.
DR InterPro; IPR000782; FAS1_domain.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR PANTHER; PTHR13789:SF147; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G01950)-RELATED; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF02469; Fasciclin; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SMART; SM00554; FAS1; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF82153; FAS1 domain; 1.
DR PROSITE; PS50213; FAS1; 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:UP000054988}.
FT DOMAIN 519..672
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
SQ SEQUENCE 677 AA; 75738 MW; B42E41DBE035C0D3 CRC64;
MFEGRKAVVQ LHIVIVGAGI GGLSAAYCLV QAGHRITVVE RAKELKEIGA GIQLTPNSTR
LLMRWGLGRK LEEIAGSDRC EATLIFRCKS FVMFGQPYGK AFERQCGGAS MYQMHRADLQ
KMLYELASPH MTLRLGSEVA FIDSSAPSVT LKSGEILSGD LVVGADGIHS IVRRVLGSPQ
EPEPTHDSTY RYLIPADEML ADPELRPLIE TSSLASWLGP EKHVVGYGIR GKSLYNMAVH
VPEPEFQVPG VYTTKGNPNH MRAAYDKEGE NWDPRVRKLL SLAKSDHVLK FKSLHCKPLD
TWVHPAGRVT LLGDACHSFP SHYAQGSALA IEDAAVLGNL FSRLTDHSQI KSLLEAYEAI
RRPRASATWL DTMERQVWLH YRDGSNQEAR DAGIKDTKIF KHRREHEATI PILCANPYGY
DADEVVDIWW KQNCGNREGP GRRWRCPLSK YCLPISRYDI VILHCYDHMR LQHLALFFIP
LVTAKFHPGH RGDERSPLRN QQIPMVFDEP EYTPQVKTQP TLADLLTIEA SSSIFYSYAR
ELELSKLLND ESARLTLLVP TNKAVVALPR KPHQDPETKD DAVISEEEFD KLSKRNVERW
VSAHIIPESL NALEHKSYST LLDGKLVTFS ASGKGSDTNA PSWQNTVVED GVRIMDTKEA
SNGVIYILDG TISVETS
//
