ID Q3SD88_PARTE Unreviewed; 644 AA.
AC Q3SD88;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Heat shock 70 kDa protein {ECO:0000256|ARBA:ARBA00018181};
GN Name=Hsp70Pt03 {ECO:0000313|EMBL:CAI44477.1};
GN ORFNames=GSPATT00026192001 {ECO:0000313|EMBL:CAK93869.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAI44477.1};
RN [1] {ECO:0000313|EMBL:CAI44477.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=D4-2 {ECO:0000313|EMBL:CAI44477.1};
RA Genoscope;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAI44477.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=D4-2 {ECO:0000313|EMBL:CAI44477.1};
RA Meyer E.;
RT "hsp70 genes in Paramecium.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAK93869.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK93869.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
RN [4] {ECO:0000313|EMBL:CAK93869.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK93869.1};
RG Genoscope;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR EMBL; CR933371; CAI44477.1; -; Genomic_DNA.
DR EMBL; CT868674; CAK93869.1; -; Genomic_DNA.
DR RefSeq; XP_001461242.1; XM_001461205.1.
DR AlphaFoldDB; Q3SD88; -.
DR STRING; 5888.Q3SD88; -.
DR EnsemblProtists; CAK93869; CAK93869; GSPATT00026192001.
DR GeneID; 5047027; -.
DR KEGG; ptm:GSPATT00026192001; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_7_0_1; -.
DR InParanoid; Q3SD88; -.
DR OMA; VNEAESY; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR CDD; cd10233; HSPA1-2_6-8-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.30.30; -; 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:SF395; HEAT SHOCK 70 KDA PROTEIN COGNATE 1-RELATED; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600}.
FT REGION 620..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 644 AA; 71556 MW; EDFD41AD470694D0 CRC64;
MSKSNETAIG IDLGTTYSCV GVFINDKVEI IANDQGNRTT PSYVAFTENE RLIGDAAKNQ
VARNPQNTVF DAKRLIGRKF NDPTVQKDIK LWPFKVEAGA DDKPLIVVKF KGETKKFHPE
EISSMVLTKM KEIAEAYLGK SVKNAVITVP AYFNDSQRQA TKDAGLICGL NVLRIINEPT
AASIAYGLDQ KIKGEKNVLI FDLGGGTFDV SLLTIDEGIF EVKATSGDTH LGGEDFDNRL
VEYCCAEFQK KKGIDMRTNA RALRRLRTQC ERAKRILSSA NQTTIELDAL AENEDFNCSI
TRAKFEELCL DQFKKCIPPV EQVLKDSGMS KSQIHEVVLV GGSTRIPKVQ ELLKDYFNGK
ELNKSINPDE AVAYGAAVQA AILTGTGSQK CENLVLLDVT PLSLGIETAG GVMSVLIPRN
TTIPTKKSQV FTTYADNQPG VLIQVFEGER QMTKDCHKLG QFQLDGIAPA PRGVPQIEVT
FDIDENGIMN ILAEDKASKK NNKITITNDK GRLSKQDIDR LVNEAEKYKA DDEKIRLRIE
AKNNLESTAY HMKNTMNEEQ FKDKFTSDEK RQLSDLVEQT QKWLDSHQNE EADVYKDKLK
ELESKFHPIM QRVYAQTGAG AGASMPNMNR GPGSEFKPTV DQVD
//
