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LOCUS XP_016993368 399 aa linear INV 09-DEC-2024 isoform X2 [Drosophila takahashii]. ACCESSION XP_016993368 VERSION XP_016993368.1 DBLINK BioProject: PRJNA1194641 DBSOURCE REFSEQ: accession XM_017137879.3 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 ##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..399 /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..399 /product="pyruvate dehydrogenase E1 component subunit alpha, mitochondrial isoform X2" /calculated_mol_wt=43757 Region 34..382 /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(92,144,169..170,201,203..206,209,213,217,232..235, 249,299,303) /site_type="other" /note="tetramer interface [polypeptide binding]" /db_xref="CDD:238958" Site order(122..123,169,171,199..202,229,231,295) /site_type="other" /note="TPP-binding site [chemical binding]" /db_xref="CDD:238958" Site order(164,166,168,173,176..177,180..181,183..184,187, 206..207,213..214,217) /site_type="other" /note="heterodimer interface [polypeptide binding]" /db_xref="CDD:238958" Site order(290..296,298..308,317..319) /site_type="phosphorylation" /note="phosphorylation loop region [posttranslational modification]" /db_xref="CDD:238958" CDS 1..399 /gene="Pdha" /coded_by="XM_017137879.3:229..1428" /db_xref="GeneID:108054803" ORIGIN 1 mlrtlsrvse lpiivkqlqk naaqagvskt nnyateatiq vnrpfklhrl degpatevkl 61 tkdqalkyyt qmqtirrlet aagnlykeki irgfchlysg qeacavgmka amrdvdniis 121 ayrvhgwtyl mgvspsgvla eltgvqggca rgkggsmhmy apnfyggngi vgaqvplgag 181 vglackykgn ggmclalygd gaanqgqvfe aynmaylwkl pvifvcennn ygmgtssera 241 scntdyytrg dalpgiwvdg mdvlavrsat efainyvnth gplvletnty rysghsmsdp 301 gtsyrtreei qevrqkrdpi tsfkelciel glittdevka idlkvrkevd eatafaksda 361 elgvshlwtd vysnnlepkl rgtiaydidh iqerkgvnh