ID F7W8Y0_SORMK Unreviewed; 494 AA.
AC F7W8Y0;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=WGS project CABT00000000 data, contig 2.47 {ECO:0000313|EMBL:CCC05103.1};
GN ORFNames=SMAC_07760 {ECO:0000313|EMBL:CCC05103.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC05103.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC05103.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC05103.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:CCC05103.1}.
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DR EMBL; CABT02000047; CCC05103.1; -; Genomic_DNA.
DR RefSeq; XP_003346104.1; XM_003346056.1.
DR AlphaFoldDB; F7W8Y0; -.
DR STRING; 771870.F7W8Y0; -.
DR GeneID; 10803491; -.
DR KEGG; smp:SMAC_07760; -.
DR VEuPathDB; FungiDB:SMAC_07760; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_19_1_1; -.
DR InParanoid; F7W8Y0; -.
DR OMA; ETFKHSG; -.
DR OrthoDB; 2678872at2759; -.
DR Proteomes; UP000001881; 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; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789:SF315; FAD-DEPENDENT MONOOXYGENASE MDPD; 1.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR Pfam; PF00890; FAD_binding_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000001881}.
FT DOMAIN 21..96
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 132..366
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 494 AA; 55970 MW; C4AB146082659D12 CRC64;
MPYITEGEPK PIGSYPDSGI DVLIVGTGLA GLTAAIECRR KGHKVRILEK CPDINTQGDM
YFMGLSATKF FKHWPEMAKE FDEISLHNAW IETYKHEGEL VIPPIKVSVR LREAGLDPNT
PPGLFQMRPL VYRMYIRQVE RLGIPITFNK KVVDYWEDIQ SGKGGVTTED GDRYEADVVI
AADGVGSKAQ KLVGGQVRAM KSGRAMWRAA FDIKYLDKNP EIKEFFSMHT PKEGGKPEPI
VRTWLGPGTY AMSLTRPDTI IWIMNHDVTG SEKESWTHTV EADDVLRNMD NKVPKPWDPK
LKELVKLTPP KTIINFELFW RNPQPKWASQ GARVINIGDA AHSFLPASGN GATQAIEDAV
SLAACLQIGG RENVPMSVRA HVRMRFIRNA CAQKLGFSNA ELLQDTDWKN ARMDPRKAQP
KMPKWVWQHD PEKYAYEVYD HVVDSMKRGI PFDQDFDMPP NYPPGYKYEP WKIEDIRDAM
RAGRKVELGA GDWS
//
