ID   HSP70_MIMIV             Reviewed;         634 AA.
AC   Q5UQ49;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Heat shock 70 kDa protein homolog;
GN   Name=HSP70; OrderedLocusNames=MIMI_L393;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
CC   -!- FUNCTION: In cooperation with other chaperones, Hsp70s stabilize
CC       preexistent proteins against aggregation and mediate the folding of
CC       newly translated polypeptides. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; AY653733; AAV50662.1; -; Genomic_DNA.
DR   RefSeq; YP_003986897.1; NC_014649.1.
DR   SMR; Q5UQ49; -.
DR   GeneID; 9925014; -.
DR   KEGG; vg:9925014; -.
DR   Proteomes; UP000001134; Genome.
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; 2.60.34.10; -; 1.
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; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..634
FT                   /note="Heat shock 70 kDa protein homolog"
FT                   /id="PRO_0000078671"
FT   REGION          611..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   634 AA;  70514 MW;  0294A6E97DFBCAAD CRC64;
     MSDKIAIGID LGTTFSCVGV WQNGKVEIIA NDQGNRTTPS YVSFTETEHL IGDAAKYQAA
     INPTNTIFDA KRLIGRDFND QSVQSDMKYW PFKVINVGNK PYFEVSYQNE SKQYSPEQIS
     SMILSKMKQT ASAYIGKEVT DAVITVPAYF NDSQRQATKD AGRIAGLNVL RIINEPTAAA
     FAYGLDKNQD KEMNVLIFDM GGGTHDVTLL SLEDGLFQVR ATSGNTKLGG EDFDNRLVTW
     CVEDFKRKYK TDLNQSAKAL RRLRTACERA KRALSSSTQT TIEVDSLFEG IDYNVTLTRA
     KFEELCSDLF RAGLEPVEKV LLDSKLDKSQ VHEIVLVGGS SRIPKVRQLL SNFFNGKKLN
     ETVNPDEAVA YGAAIQAAIL VGQTDEKLQN IVLVDVTPLS LGLETAGGIM TNIIDRNTTI
     PCKKSRVFTT YSDNQTVVTI QIFEGERKFT KDNNNLGTFN LEGIPPAQRG VPQIEVTFDL
     DANGILNVTA ADKSTNKSKN ITITNNRGRF SEDQIERMIR EAKEFEEADN KKKAAVDSKN
     ELENYTHSVK QAVTDPSNSN NIEESSRSQI ESKCAEIMKF VDENPNEDQG TYDLRRKELE
     DLWNPIAVTL YAQKNNQSNQ TSTESTGPTV EEVD