ID Q3SE31_PARTE Unreviewed; 651 AA.
AC Q3SE31;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=ER-type hsp70 {ECO:0000313|EMBL:CAI39094.1};
GN Name=Hsp70Pt07 {ECO:0000313|EMBL:CAI39094.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAI39094.1};
RN [1] {ECO:0000313|EMBL:CAI39094.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=D4-2 {ECO:0000313|EMBL:CAI39094.1};
RA Genoscope;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAI39094.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=D4-2 {ECO:0000313|EMBL:CAI39094.1};
RA Meyer E.;
RT "hsp70 genes in Paramecium.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR932268; CAI39094.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3SE31; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd10241; HSPA5-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR042050; BIP_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:SF144; ENDOPLASMIC RETICULUM CHAPERONE BIP; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..651
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012497606"
FT REGION 632..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 267..301
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 592..624
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 651 AA; 72292 MW; 64CCA102BB48EBBB CRC64;
MKPIILVVLL LGAWAQEKTN KVECPVIGID LGTTYSCVGI YKNGNVEIIP NEQGNRITPS
VVAFTDEERL IGEAAKNQAA INPTRTLYDV KRLIGRKFTD STVQYDRKFM PYDIVDKDTK
PYIKVTNIKG HQSKIFAPEE ISAMVLTKMK EISETYLGKK VINAVVTVPA YFNDAQRQAT
KDAGTISGLN VVRILNEPTA AAIAYGLDKK DGEKNILVFD LGGGTFDVSI LTIDNGVFEV
VATLGDTHLG GEDFDQRIID HFIKVIKKKH NKDISADKRA IQKLKREVEK SKRALSATHE
TKIEIEDLVD GLDFNEVLTR AKFEELNNDL FKKTTGPMQT ALEDSKFKKT EIHEIVLVGG
SSRIPKVRQI VKDFFNGKEA NTGINPDEAV CYGAAIQGGI ICGEESNETK GLIVIDATPL
SLGIETVGGV MTKIIPKGSY IPTKKSQVFT TYQDQQQTVT ISVFEGERPL VKDNHKLGTF
DLTGIPPAPR GTPQIEVTFE IDANGILQVG AQDKGTGVKN QIVITNDSGR LSKEEIDKML
REAEEFADQD KAAKERIDAK NSLESYIYSM KNQIEDPEKL ANKLSDDDKD TIKDALKDSQ
DWLDKNQNAE KEDYEEELKE LEKICNPIIS RVYQQSGKQQ QASDDDYDSD L
//
