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LOCUS XP_022226639 464 aa linear INV 14-MAY-2021 obscura]. ACCESSION XP_022226639 VERSION XP_022226639.1 DBLINK BioProject: PRJNA728747 DBSOURCE REFSEQ: accession XM_022370947.2 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 ##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..464 /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..464 /product="probable citrate synthase, mitochondrial isoform X2" /calculated_mol_wt=51502 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="LOC111076900" /coded_by="XM_022370947.2:148..1542" /db_xref="GeneID:111076900" ORIGIN 1 mslyrisark lveaqklpnv gsyvrlisad grslrdvlna kvpeeqervk nfrkqhgatk 61 lgettidmmy ggmrgikalv tetsvldade girfrglsip ecqkvlpaap ggteplpegl 121 fwllltgevp sqaqvqqlsr ewaeraalpq hvvtmlnnmp tslhpmsqla aavtalnhds 181 kfakaysegv hkskyweyvy edsmdliakl pvvaatiycn tyrggkgsrs idssldwsan 241 fvkmlgydna qftelmrlyl tihsdheggn vsahtvhlvg salsdpylsf aagmnglagp 301 lhglanqevl vwlrklqkea gnnpseeqlk eyiwktlksg qvvpgyghav lrktdprytc 361 qrefalkhlp edelfqlvsk iykvvppilt etgkvknpwp nvdahsgvll qyfgmkemny 421 ytvlfgvsra lgvlaslvwd ralglpierp ksystdllvk mvqk