ID A7TK36_VANPO Unreviewed; 405 AA.
AC A7TK36;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 03-MAY-2023, entry version 74.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDO17382.1};
GN ORFNames=Kpol_1060p38 {ECO:0000313|EMBL:EDO17382.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO17382.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317}.
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DR EMBL; DS480405; EDO17382.1; -; Genomic_DNA.
DR RefSeq; XP_001645240.1; XM_001645190.1.
DR AlphaFoldDB; A7TK36; -.
DR STRING; 436907.A7TK36; -.
DR GeneID; 5545599; -.
DR KEGG; vpo:Kpol_1060p38; -.
DR eggNOG; KOG0557; Eukaryota.
DR HOGENOM; CLU_035825_2_1_1; -.
DR InParanoid; A7TK36; -.
DR OMA; NRFEVYD; -.
DR OrthoDB; 52212at2759; -.
DR PhylomeDB; A7TK36; -.
DR Proteomes; UP000000267; 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 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:UP000000267};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 29..105
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 167..208
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 123..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 405 AA; 44795 MW; 7D09FC1D0E8E9FA1 CRC64;
MLRFGASRNI LLRRLSFRKF GTSLRLFDAN AFAMPAMSPT MEKGGIVQWK FKVGEPFSAG
DVLLEVETDK AQIDVEAQDD GKIAKIIIGD GAKDVPVGDT IAFLAEVDDD LSTLKIPDVT
AAPKKDAAPK TEPLSKPISK PVENPTEVRS NETVSSAATK SADMKQVLLP SVAIELSLNG
IKKEDALKNI KATGTKGRLL KGDVLAYVGK INKDSPSKIA SYIEKGEKLD LSNIELREPA
VQETKESTSK ESTKMVKEPI ILNEYIALRA KPGASLEKLE LALGQYLDSM FQKAHNDTLV
DTRSQFYDPI FEDLLSIESN KPRFTLSYEL IELENEDIPS RRSRASEADI FDLLSNETPA
SQVNEKSNNN ATEFVVSLRV EVNDKYPDSM ERAQKFVSYM KQLQL
//