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LOCUS XP_016993341 464 aa linear INV 09-DEC-2024 takahashii]. ACCESSION XP_016993341 VERSION XP_016993341.2 DBLINK BioProject: PRJNA1194641 DBSOURCE REFSEQ: accession XM_017137852.3 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_016993341.1. ##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..464 /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..464 /product="probable citrate synthase, mitochondrial isoform X2" /calculated_mol_wt=51489 Region 34..461 /region_name="ScCit1-2_like" /note="Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with oxaloacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or...; cd06105" /db_xref="CDD:99858" Site order(72..73,76..82,167,171,174,266,271,274..275,278..279, 282..284,288,295..296,299..301,349,446..454) /site_type="other" /note="dimer interface [polypeptide binding]" /db_xref="CDD:99858" Site order(74,266,270,300..303,305,308,342..349,352,357,398, 401,403,425,429,446,449) /site_type="active" /db_xref="CDD:99858" Site order(74,300..302,305,308,342..349,352,398,401,403,446) /site_type="other" /note="coenzyme A binding site [chemical binding]" /db_xref="CDD:99858" Site order(74,266,270,301..302,342..343,345..349,357,401,429) /site_type="other" /note="citrylCoA binding site [chemical binding]" /db_xref="CDD:99858" Site order(266,270,302..303,348..349,357,403,425,429,449) /site_type="other" /note="oxalacetate/citrate binding site [chemical binding]" /db_xref="CDD:99858" Site order(302,348,403) /site_type="active" /note="catalytic triad [active]" /db_xref="CDD:99858" CDS 1..464 /gene="kdn" /coded_by="XM_017137852.3:201..1595" /db_xref="GeneID:108054783" ORIGIN 1 mslyrisark lteaqklpnv gayvrmisad gkslrdvlta kvpqeqervk nfrkqhgatk 61 mgettidmmy ggmrgikalv tetsvldade girfrglsip ecqkvlpaad ggteplpegl 121 fwllltgevp tksqvqqlsr ewaeraalpq hvvtmlnnmp ttlhpmsqfa aavtalnhds 181 kfakaysdgv hkskyweyvy edsmdliakl pvvaatiycn tyrggkgsrs idssldwsan 241 fvkmlgydna pftelmrlyl tihsdheggn vsahtvhlvg salsdpylsf aaglnglagp 301 lhglanqevl vwlrklqkea gnnpseeqlk eyiwktlksg qvvpgyghav lrktdprytc 361 qrefalkhlp ddetfqlvsk iykvvppilt etgkvknpwp nvdahsgvll qyygmkemny 421 ytvlfgvsra lgvlaslvwd ralglpierp ksfstdllvk mvqk