ID   F7WB48_SORMK            Unreviewed;       533 AA.
AC   F7WB48;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=WGS project CABT00000000 data, contig 2.70 {ECO:0000313|EMBL:CCC14340.1};
GN   ORFNames=SMAC_08927 {ECO:0000313|EMBL:CCC14340.1};
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:CCC14340.1, ECO:0000313|Proteomes:UP000001881};
RN   [1] {ECO:0000313|EMBL:CCC14340.1, 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:CCC14340.1};
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:CCC14340.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CABT02000070; CCC14340.1; -; Genomic_DNA.
DR   RefSeq; XP_003353170.1; XM_003353122.1.
DR   AlphaFoldDB; F7WB48; -.
DR   STRING; 771870.F7WB48; -.
DR   GeneID; 10810871; -.
DR   KEGG; smp:SMAC_08927; -.
DR   VEuPathDB; FungiDB:SMAC_08927; -.
DR   eggNOG; ENOG502SJ3M; Eukaryota.
DR   HOGENOM; CLU_018354_0_1_1; -.
DR   InParanoid; F7WB48; -.
DR   OMA; GICECVG; -.
DR   OrthoDB; 1068078at2759; -.
DR   Proteomes; UP000001881; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.20; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
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:SF9; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF08031; BBE; 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};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..533
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003371250"
FT   DOMAIN          99..271
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   533 AA;  58472 MW;  902709E11CFADA30 CRC64;
     MLSSTRSLIW GGLLALASFA TASPVATGPL PIAIRDSSPP SSLENRDYNT SSLLSPVVFI
     PPTIQQDLTS LLSPSALVIL PSSPSFPQYT SRWSLNTRTN SPSYAVIVIP ASERDVSLTI
     QYANAHSIPF LATTGTHGTW HGLSKLQGGM AIWTRNLTKM EFAADGNSAT LGGGLRGNDV
     VPALWARGKQ TTTGSCRCVS LLGPALGGGH GWLQGQYGLG ADQILSARVV LANGTAVKAS
     NTENSDLFWA LRGAGHNFGV VTEVEYKLYD AVRPNWAYQS FTFTQDRLED VYRVHNEVMK
     NQNQYVVYWS LWRLVPEVDA VNPILVSTVY YNGPASEALP YFAPFAALNP LDTTPVQTTD
     YPGLAAAAQF RVTDWACQPK TGATVYGMDV DTYDLPALRQ SYNFLSQMIR TEPALSASMA
     YLEGYSLQAV QAVPYESTAF ALRDRKLLYG FLVTYEGATN KTLDAQAQKW GEKIRNAAYG
     GVSRKYAYVN YAKGSETMQQ MYGYEGWRQE RLKQLKRKYD PRGRFSFYAG IKA
//