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LOCUS XP_017002264 573 aa linear INV 09-DEC-2024 ACCESSION XP_017002264 VERSION XP_017002264.1 DBLINK BioProject: PRJNA1194641 DBSOURCE REFSEQ: accession XM_017146775.3 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 ##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..573 /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..573 /product="heat shock protein 60A" /calculated_mol_wt=60727 Region 24..544 /region_name="GroEL" /note="GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. The symmetry of type I is seven-fold and they are found...; cd03344" /db_xref="CDD:239460" Site order(24,28,45,56..59,61,66..67,69,79,81,89,93,96,217,249, 277,405,407,480,534,537..543) /site_type="other" /note="ring oligomerisation interface [polypeptide binding]" /db_xref="CDD:239460" Site order(51..53,107,111,170,419,436,475,514,516) /site_type="other" /note="ATP/Mg binding site [chemical binding]" /db_xref="CDD:239460" Site order(129,455,473,482,484..485,488) /site_type="active" /note="stacking interactions [active]" /db_xref="CDD:239460" Site order(161,206,213,396,430..431) /site_type="other" /note="hinge regions" /db_xref="CDD:239460" CDS 1..573 /gene="Hsp60A" /coded_by="XM_017146775.3:161..1882" /db_xref="GeneID:108060867" ORIGIN 1 mfrlpvslar tsisrqlamr gyakdvrfgp evralmlqgv dvladavavt mgpkgrnvii 61 eqswgspkit kdgvtvaksi elkdkfqnig aklvqdvann tneeagdgtt tatvlaraia 121 kegfekiskg anpveirrgv mlavetvkdn lktmsrpvkt peeiaqvati sangdqaign 181 liseamkkvg rdgvitvkdg ktlndelevi egmkfdrgyi spyfinsskg akvefqdall 241 llsekkissv qsiipalela naqrkplvii aedidgeals tlvvnrlkig lqvaavkapg 301 fgdnrkstlt dmaiasggiv fgddadlvkl edvkvsdlgq vgevvitkdd tlllkgkgkk 361 edvlrranqi keqiedttse yekeklqerl arlasgvall rvggssevev nekkdrvhda 421 lnatraavee givpgggtal lrciekldav ktnnedqnlg veivrralrm pcmtiaknag 481 vdgamvvakv etqagdygyd alkgeygnli ekgiidptkv vrtaitdasg vasllttaea 541 vvteipkedg apgmpgmggm ggmggmggmg gmm