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LOCUS XP_016993366 437 aa linear INV 09-DEC-2024 isoform X1 [Drosophila takahashii]. ACCESSION XP_016993366 VERSION XP_016993366.2 DBLINK BioProject: PRJNA1194641 DBSOURCE REFSEQ: accession XM_017137877.3 KEYWORDS RefSeq. SOURCE Drosophila takahashii ORGANISM Drosophila takahashii Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora. COMMENT MODEL REFSEQ: This record is predicted by automated computational analysis. This record is derived from a genomic sequence (NC_091683) annotated using gene prediction method: Gnomon. Also see: Documentation of NCBI's Annotation Process On Oct 18, 2021 this sequence version replaced XP_016993366.1. ##Genome-Annotation-Data-START## Annotation Provider :: NCBI RefSeq Annotation Status :: Full annotation Annotation Name :: GCF_030179915.1-RS_2024_12 Annotation Pipeline :: NCBI eukaryotic genome annotation pipeline Annotation Software Version :: 10.3 Annotation Method :: Gnomon; cmsearch; tRNAscan-SE Features Annotated :: Gene; mRNA; CDS; ncRNA Annotation Date :: 12/07/2024 ##Genome-Annotation-Data-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..437 /organism="Drosophila takahashii" /strain="IR98-3 E-12201" /db_xref="taxon:29030" /chromosome="X" /sex="female" /tissue_type="Whole fly" /dev_stage="Adult fly" /collected_by="Originally obtained from EHIME-Fly" Protein 1..437 /product="pyruvate dehydrogenase E1 component subunit alpha, mitochondrial isoform X1" /calculated_mol_wt=48163 Region 72..420 /region_name="TPP_enzymes" /note="Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and...; cl01629" /db_xref="CDD:470272" Site order(130,182,207..208,239,241..244,247,251,255,270..273, 287,337,341) /site_type="other" /note="tetramer interface [polypeptide binding]" /db_xref="CDD:238958" Site order(160..161,207,209,237..240,267,269,333) /site_type="other" /note="TPP-binding site [chemical binding]" /db_xref="CDD:238958" Site order(202,204,206,211,214..215,218..219,221..222,225, 244..245,251..252,255) /site_type="other" /note="heterodimer interface [polypeptide binding]" /db_xref="CDD:238958" Site order(328..334,336..346,355..357) /site_type="phosphorylation" /note="phosphorylation loop region [posttranslational modification]" /db_xref="CDD:238958" CDS 1..437 /gene="Pdha" /coded_by="XM_017137877.3:232..1545" /db_xref="GeneID:108054803" ORIGIN 1 mlrtlsrvse lpiivkqlqk rchnnnnnsg wriysnnnnn neiigngrys ssffglfqna 61 aqagvsktnn yateatiqvn rpfklhrlde gpatevkltk dqalkyytqm qtirrletaa 121 gnlykekiir gfchlysgqe acavgmkaam rdvdniisay rvhgwtylmg vspsgvlael 181 tgvqggcarg kggsmhmyap nfyggngivg aqvplgagvg lackykgngg mclalygdga 241 anqgqvfeay nmaylwklpv ifvcennnyg mgtsserasc ntdyytrgda lpgiwvdgmd 301 vlavrsatef ainyvnthgp lvletntyry sghsmsdpgt syrtreeiqe vrqkrdpits 361 fkelcielgl ittdevkaid lkvrkevdea tafaksdael gvshlwtdvy snnlepklrg 421 tiaydidhiq erkgvnh