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heat shock protein 60A [Drosophila takahashii].


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