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Database: UniProt
Entry: A0A0N5D235_THECL
LinkDB: A0A0N5D235_THECL
Original site: A0A0N5D235_THECL 
ID   A0A0N5D235_THECL        Unreviewed;       413 AA.
AC   A0A0N5D235;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   08-MAY-2019, entry version 16.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
OS   Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX   NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000692901-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000692901-mRNA-1}
RP   NUCLEOTIDE SEQUENCE.
RG   Helminth Genomes Consortium;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:TCLT_0000692901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003423}.
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DR   WBParaSite; TCLT_0000692901-mRNA-1; TCLT_0000692901-mRNA-1; TCLT_0000692901.
DR   OMA; VPNIKNC; -.
DR   Proteomes; UP000046394; Genome Assembly.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000046394};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    413       Dihydrolipoamide acetyltransferase
FT                                component of pyruvate dehydrogenase
FT                                complex. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5005896346.
FT   DOMAIN       16     91       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      128    165       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   COILED      301    321       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   413 AA;  46348 MW;  9796B4F71B33C049 CRC64;
     LLTNLFSCIL ARWLPIVQFR LSDIGEGIAQ VQIKEWHVKE GDHVAQFDNI CEVQSDKASA
     TITSRYDGII KKLHYNIEDI AKVGTTLVDI EVVDEHGNVH SDVQEEILED VKENVACTKG
     AQESGKILAT PAVRHFAELK GVNLRDVSGT GSDGRILKDD IIQFYESQKG RFNSCFGVLE
     DDKIVPIRGY TRTMIKSMTE ALKIPHFSLY EEINFDQLIA MKEELKKFEG MYSARMTFMP
     IIIKAVSLAL NKFPKLNAVT DEYLENIIYK AFKNISIAMD TPEGLVVPNI KNCERRTIWD
     IAQELDRLKK ASSQMKIASE DLKDGTFTLS NVGMIGGTYL NAIIMPPQLA IGAIGQISKL
     PRFDKDGKVY AANVAYFSWA ADHRVVDGAT LARFSSQVKQ YLENPYSMLA DYE
//
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