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LOCUS XP_017013821 500 aa linear INV 09-DEC-2024 mitochondrial [Drosophila takahashii]. ACCESSION XP_017013821 VERSION XP_017013821.2 DBLINK BioProject: PRJNA1194641 DBSOURCE REFSEQ: accession XM_017158332.3 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_017013821.1. ##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..500 /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..500 /product="probable pyruvate dehydrogenase E1 component subunit alpha, mitochondrial" /calculated_mol_wt=55360 Region 36..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(89,141,166..167,198,200..203,206,210,214,229..232, 246,249,296,300) /site_type="other" /note="tetramer interface [polypeptide binding]" /db_xref="CDD:238958" Site order(119..120,166,168,196..199,226,228,292) /site_type="other" /note="TPP-binding site [chemical binding]" /db_xref="CDD:238958" Site order(161,163,165,170,173..174,177..178,180..181,184, 203..204,210..211,214) /site_type="other" /note="heterodimer interface [polypeptide binding]" /db_xref="CDD:238958" Site order(287..293,295..305,314..316) /site_type="phosphorylation" /note="phosphorylation loop region [posttranslational modification]" /db_xref="CDD:238958" CDS 1..500 /gene="LOC108068641" /coded_by="XM_017158332.3:123..1625" /db_xref="GeneID:108068641" ORIGIN 1 mkpnrirlvv grsgarsllh rnilssiigr hkcscltlen tfkcydletg ptmdvelsre 61 dalsmytrml elrrfetvag nsykqrlirg fchlytgqea vavgmkerlr rcdsvitayr 121 chawtylmgv slyeimaell glrtgcsrgk ggsmhmygen fyggngivga qvpvgtgigl 181 ahsyrkdngv cvilygdgaa nqgqvfesfn maklwclpci fvcennhygm gthekrasam 241 tefymrgqyi pglwvdgnqv lavrsatqfa vdyalkegpi vlemstyryv ghsmsdpgts 301 yrsrkevqav resrdpitsf rsqiltlcla deeelkalee rtkkqvdaec kraakdkeve 361 lqelhtdiya knvdgkirgv srfdlehirl sevcfgkprk tpaseikdvp vgaavdaaka 421 kerkaaqeak eakegqkkkk edskdlknsk epkdpkpvdp kpptaaaapp aktppskapp 481 skappakktp ptkaptdpkk