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LOCUS XP_022226637 517 aa linear INV 14-MAY-2021 obscura]. ACCESSION XP_022226637 VERSION XP_022226637.2 DBLINK BioProject: PRJNA728747 DBSOURCE REFSEQ: accession XM_022370945.2 KEYWORDS RefSeq. SOURCE Drosophila obscura ORGANISM Drosophila obscura 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 (NW_024542752.1) annotated using gene prediction method: Gnomon. Also see: Documentation of NCBI's Annotation Process On May 14, 2021 this sequence version replaced XP_022226637.1. ##Genome-Annotation-Data-START## Annotation Provider :: NCBI Annotation Status :: Full annotation Annotation Name :: Drosophila obscura Annotation Release 101 Annotation Version :: 101 Annotation Pipeline :: NCBI eukaryotic genome annotation pipeline Annotation Software Version :: 8.6 Annotation Method :: Best-placed RefSeq; Gnomon Features Annotated :: Gene; mRNA; CDS; ncRNA ##Genome-Annotation-Data-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..517 /organism="Drosophila obscura" /isolate="BZ-5 IFL" /db_xref="taxon:7282" /chromosome="Unknown" /sex="male" /tissue_type="whole fly" /dev_stage="Adult fly" /geo_loc_name="Serbia: Babin Zub" /collection_date="2017" Protein 1..517 /product="probable citrate synthase, mitochondrial isoform X1" /calculated_mol_wt=57369 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="LOC111076900" /coded_by="XM_022370945.2:16..1569" /db_xref="GeneID:111076900" ORIGIN 1 myfsrcltpd vvlhlqcrtl akksvrdakn llreilrapl eeevqektvv qavakpqaar 61 dggpdslqkl pnvgsyvrli sadgrslrdv lnakvpeeqe rvknfrkqhg atklgettid 121 mmyggmrgik alvtetsvld adegirfrgl sipecqkvlp aapggteplp eglfwllltg 181 evpsqaqvqq lsrewaeraa lpqhvvtmln nmptslhpms qlaaavtaln hdskfakays 241 egvhkskywe yvyedsmdli aklpvvaati ycntyrggkg srsidssldw sanfvkmlgy 301 dnaqftelmr lyltihsdhe ggnvsahtvh lvgsalsdpy lsfaagmngl agplhglanq 361 evlvwlrklq keagnnpsee qlkeyiwktl ksgqvvpgyg havlrktdpr ytcqrefalk 421 hlpedelfql vskiykvvpp iltetgkvkn pwpnvdahsg vllqyfgmke mnyytvlfgv 481 sralgvlasl vwdralglpi erpksystdl lvkmvqk