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LOCUS XP_070075188 517 aa linear INV 09-DEC-2024 takahashii]. ACCESSION XP_070075188 VERSION XP_070075188.1 DBLINK BioProject: PRJNA1194641 DBSOURCE REFSEQ: accession XM_070219087.1 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..517 /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..517 /product="probable citrate synthase, mitochondrial isoform X1" /calculated_mol_wt=57552 Region 87..514 /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(125..126,129..135,220,224,227,319,324,327..328, 331..332,335..337,341,348..349,352..354,402,499..507) /site_type="other" /note="dimer interface [polypeptide binding]" /db_xref="CDD:99858" Site order(127,319,323,353..356,358,361,395..402,405,410,451, 454,456,478,482,499,502) /site_type="active" /db_xref="CDD:99858" Site order(127,353..355,358,361,395..402,405,451,454,456,499) /site_type="other" /note="coenzyme A binding site [chemical binding]" /db_xref="CDD:99858" Site order(127,319,323,354..355,395..396,398..402,410,454,482) /site_type="other" /note="citrylCoA binding site [chemical binding]" /db_xref="CDD:99858" Site order(319,323,355..356,401..402,410,456,478,482,502) /site_type="other" /note="oxalacetate/citrate binding site [chemical binding]" /db_xref="CDD:99858" Site order(355,401,456) /site_type="active" /note="catalytic triad [active]" /db_xref="CDD:99858" CDS 1..517 /gene="kdn" /coded_by="XM_070219087.1:81..1634" /db_xref="GeneID:108054783" ORIGIN 1 mfvlrlvsas srqyfsmqhr slakksiwda kpfgfqrlrs kqeddttgql keqqqpspes 61 lgkvseaqkl pnvgayvrmi sadgkslrdv ltakvpqeqe rvknfrkqhg atkmgettid 121 mmyggmrgik alvtetsvld adegirfrgl sipecqkvlp aadggteplp eglfwllltg 181 evptksqvqq lsrewaeraa lpqhvvtmln nmpttlhpms qfaaavtaln hdskfakays 241 dgvhkskywe yvyedsmdli aklpvvaati ycntyrggkg srsidssldw sanfvkmlgy 301 dnapftelmr lyltihsdhe ggnvsahtvh lvgsalsdpy lsfaaglngl agplhglanq 361 evlvwlrklq keagnnpsee qlkeyiwktl ksgqvvpgyg havlrktdpr ytcqrefalk 421 hlpddetfql vskiykvvpp iltetgkvkn pwpnvdahsg vllqyygmke mnyytvlfgv 481 sralgvlasl vwdralglpi erpksfstdl lvkmvqk