ID F7VLC7_SORMK Unreviewed; 500 AA.
AC F7VLC7;
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 2.1 {ECO:0000313|EMBL:CCC06304.1};
GN ORFNames=SMAC_00521 {ECO:0000313|EMBL:CCC06304.1};
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:CCC06304.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC06304.1, 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:CCC06304.1};
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:CCC06304.1}.
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DR EMBL; CABT02000001; CCC06304.1; -; Genomic_DNA.
DR RefSeq; XP_003351972.1; XM_003351924.1.
DR AlphaFoldDB; F7VLC7; -.
DR STRING; 771870.F7VLC7; -.
DR GeneID; 10809557; -.
DR KEGG; smp:SMAC_00521; -.
DR VEuPathDB; FungiDB:SMAC_00521; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_018354_0_0_1; -.
DR InParanoid; F7VLC7; -.
DR OMA; KEVCANS; -.
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 InterPro; IPR012951; BBE.
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:SF32; FAD-LINKED OXIDOREDUCTASE AFOF; 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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..500
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003370412"
FT DOMAIN 69..241
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 500 AA; 55129 MW; DEE470ECB4D5D40B CRC64;
MHLTSSLLFT SALLAGGINA SPATNAYRRQ NANMRTIIGD TTPVLSNSTM IRYPDSDGFF
GVTERWDVYR PPSYQAAISP TTEADIVSLV KMAKQHNIPF LATGGRHGYG TTLGNCKEGL
AIDLSHFKDV KLDKKKQTVT IGPGVVFADV FPVVHDAGFQ IQTGTCSCVG MIGATIGAGI
GRLDGVHGLV IDALESVRMV TANGEIVEAS KTKNPELFWG IRGAGANFGI ITQATYKMHK
NMGDIISFDL IYEPEKNVTL FNTIANMYLP PGLTVETIMS YNQTTEKPTL IISSTYAGGS
EAEARRWMQP LLRLNPWYTD IKPIPWKRMS TDTTLGLDKE VCANSQIYDV YGVNLRRHDA
NTWVKTFNKL AKFWNQQPAA QSSVVVLETW PNQAVVAVPD SQTAYPWRDA TTYVMIQMRW
DAPGNPVEAA ADAMGRELRD DYAKTSGYNG LTVYVNYAHG DETPEQIYGR NKLPRLAKLK
KQYDPSSVFG FHNPLPTSYP
//
