ID   A0A2K6T6U1_SAIBB        Unreviewed;       503 AA.
AC   A0A2K6T6U1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Stress-70 protein, mitochondrial {ECO:0000256|ARBA:ARBA00019355};
DE   AltName: Full=75 kDa glucose-regulated protein {ECO:0000256|ARBA:ARBA00031419};
DE   AltName: Full=Heat shock 70 kDa protein 9 {ECO:0000256|ARBA:ARBA00030055};
OS   Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Saimiriinae; Saimiri.
OX   NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000015352.1, ECO:0000313|Proteomes:UP000233220};
RN   [1] {ECO:0000313|Ensembl:ENSSBOP00000015352.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR   AlphaFoldDB; A0A2K6T6U1; -.
DR   STRING; 39432.ENSSBOP00000015352; -.
DR   Ensembl; ENSSBOT00000032152.1; ENSSBOP00000015352.1; ENSSBOG00000024405.1.
DR   GeneTree; ENSGT00920000149123; -.
DR   Proteomes; UP000233220; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233220}.
FT   REGION          478..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..503
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   503 AA;  54800 MW;  3DB212FBA6FA058D CRC64;
     MISASRTVAA RLVGAAATRG PAAARHQDSW NGLSQEALRI VSRRDYPTAA ALAYGLDKSE
     DKVIAVYDLG GGTFDISILE IQKGVFEVKS TNGDTFLGGE DFDQALLRHI VKEFKRETGV
     DLTKDNMALQ RVREAAEKAK CELSSSVQTD INLPYLTMDS SGPKHLNMKL TRAQFEGIVT
     DLIRRTIAPC QKAMQDAEVS KSDIGEVILV CGMTRMPKVQ QTVQDLFGRA PSKTVNPDEA
     VAIGAAIQGG VLAGDVTDVL LLDVTPLSLG IETLGGVFTK LINRNTTIPT KKSQVFSTAA
     NGQTQVEIKV CQGEREMAGD NKLLGQFTLI GIPPAPRGVP QIEVTFDIDA NGIVHVSAKD
     KGTGREQQIV IQSSGGLSKD DIENTVKNAE KYAEEDRRKK ERVEAINMAE GIIHDTETKM
     EEFKDQLPAD ECNKLKEEIS KMRELQARKD SETGENIRQA ASPLQQASLK LFEMAYKKMA
     SEREGSGSSG TGEQKEDQKE EKQ
//