ID S8ASK7_DACHA Unreviewed; 400 AA.
AC S8ASK7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 03-MAY-2023, entry version 36.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EPS43976.1};
GN ORFNames=H072_2063 {ECO:0000313|EMBL:EPS43976.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS43976.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS43976.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS43976.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317}.
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:EPS43976.1}.
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DR EMBL; AQGS01000063; EPS43976.1; -; Genomic_DNA.
DR RefSeq; XP_011108051.1; XM_011109749.1.
DR AlphaFoldDB; S8ASK7; -.
DR STRING; 1284197.S8ASK7; -.
DR eggNOG; KOG0557; Eukaryota.
DR HOGENOM; CLU_035825_2_0_1; -.
DR OMA; MWEILVA; -.
DR OrthoDB; 52212at2759; -.
DR Proteomes; UP000015100; Unassembled WGS sequence.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF82; PYRUVATE DEHYDROGENASE COMPLEX PROTEIN X COMPONENT, MITOCHONDRIAL; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW Reference proteome {ECO:0000313|Proteomes:UP000015100};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 36..115
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 177..214
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 121..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 400 AA; 42881 MW; FA3149686B9DA73C CRC64;
MSSALRTSTK RLLHPGYTWR AVAARGISSS SRDCKAHNFN MPALSPTMTE GSIASWKISE
GDKFAAGDVI LEVETDKAQM DVEAQDDGIL AKIFVQASKD QIQVGTRIGI LADVDDDIAS
LEIPPEDSPI KTESAEPEKP APQSAPAPSK SKPAPTESSS EDASSSHPHK PRKNPFVASP
GITHLLHMNG LEMSDVKGTG PGGRVLKGDV LAHLGKIDKD KPKSVAGEIA KLAKLDLSNI
KPKPIAPKDT AKKDDIKKPK KVNPLDEIEV SMPISLARVS DGARPVADSI ARAVEYANSG
LPESKIPPTT SELFDEILGI PVTKAEPRYT VKSSDYKPTP TAPVLSDLFD EIIGVATPKP
AAAPSLLLKE FKVKVPAVDK DRAEFFLAKV KFSLEQDERR
//
