ID   F7WAC2_SORMK            Unreviewed;       515 AA.
AC   F7WAC2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=WGS project CABT00000000 data, contig 2.60 {ECO:0000313|EMBL:CCC14157.1};
GN   ORFNames=SMAC_08600 {ECO:0000313|EMBL:CCC14157.1};
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:CCC14157.1, ECO:0000313|Proteomes:UP000001881};
RN   [1] {ECO:0000313|EMBL:CCC14157.1, 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:CCC14157.1};
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   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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:CCC14157.1}.
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DR   EMBL; CABT02000060; CCC14157.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7WAC2; -.
DR   STRING; 771870.F7WAC2; -.
DR   eggNOG; KOG1231; Eukaryota.
DR   HOGENOM; CLU_018354_1_2_1; -.
DR   InParanoid; F7WAC2; -.
DR   OMA; WGEVYAW; -.
DR   OrthoDB; 879734at2759; -.
DR   Proteomes; UP000001881; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR   PANTHER; PTHR42973:SF34; FAD BINDING DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_3G02770); 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001881}.
FT   DOMAIN          82..254
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   515 AA;  56718 MW;  2A1EF5E513634D12 CRC64;
     MTIHKMSALL KLIRVTRTHL LSTTKHSFFR QNSTMSVPKT DLERAAAARD LLKSIFGQRV
     TTFDDDASGP RLALRAPWST TCHTRSAAYF QPETPAEVST ALSIITKTQS KFAVRATGHN
     PNPGFSSTHE DAVIIDLHRL DTKTFDEETG IASIGAGNTW GEVYTWLEGK GRSVMGGRYQ
     EIGVAGFCLG GGMPGFVNLR GMGCDQVRGF EVVLGDGTPV YCSAHVRSDL YRALKGGGSN
     FGVVTRFELQ TYALLKTQYI VSLYKPNDYA NIIKASVDAH KEMENDPKAA YFTNVHRDFV
     AIGQLYADTP KEEPKVFEPF RKLESMMAPV VPKTDGTLST LAQAIGHRPP KGKRVIFTIS
     TKVDQDLYLA IHKIWQDVTA TLPSSADGTD LHYTIQPVTA SAARAGQDNG TGDNALGLEE
     VSQNWYVFTL EYQWNGDDSV HKPAMDSIYE QVKNAAEESG LLLDFVCPTF ADKRQDVLRG
     FGEENVELIK EVAGKYDGEG VFQKLQYGGF LVRDL
//