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Database: UniProt
Entry: A0DZP1_PARTE
LinkDB: A0DZP1_PARTE
Original site: A0DZP1_PARTE 
ID   A0DZP1_PARTE            Unreviewed;       660 AA.
AC   A0DZP1;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   SubName: Full=Chromosome undetermined scaffold_70, whole genome shotgun sequence {ECO:0000313|EMBL:CAK88508.1};
GN   ORFNames=GSPATT00021676001 {ECO:0000313|EMBL:CAK88508.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK88508.1, ECO:0000313|Proteomes:UP000000600};
RN   [1] {ECO:0000313|EMBL:CAK88508.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK88508.1,
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).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved in
CC       various types of cell motility and are ubiquitously expressed in all
CC       eukaryotic cells. {ECO:0000256|ARBA:ARBA00003520}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; CT868650; CAK88508.1; -; Genomic_DNA.
DR   RefSeq; XP_001455905.1; XM_001455868.1.
DR   AlphaFoldDB; A0DZP1; -.
DR   STRING; 5888.A0DZP1; -.
DR   EnsemblProtists; CAK88508; CAK88508; GSPATT00021676001.
DR   GeneID; 5041690; -.
DR   KEGG; ptm:GSPATT00021676001; -.
DR   eggNOG; KOG0102; Eukaryota.
DR   HOGENOM; CLU_005965_2_1_1; -.
DR   InParanoid; A0DZP1; -.
DR   OMA; DKMVLQR; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; 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:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_00332; DnaK; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR012725; Chaperone_DnaK.
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   NCBIfam; TIGR02350; prok_dnaK; 1.
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; 2.
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          622..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        625..660
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   660 AA;  71917 MW;  283E90FC0DBFEC68 CRC64;
     MLSKLFKPTL KVNQHTLNAF SSKVTKGEYV IGIDLGTTNS CVSIMEAGTP KVIENAEGMR
     TTPSVVAFTA DGQRIVGAPA KRQAVTNPEN TVYATKRLIG RRFDDPNVQK DIKHLSYSVV
     RAQNGDAWVS LKSGQTYSPS QIGAFVLMKM KETADAYIGK PQSKAVVTVP AYFNDSQRQA
     TKDAGKIAGL DVLRIINEPT AAALAFGLEK KDNKIIAVYD LGGGTFDISI LEINAGVFEV
     KATNGDTSCG GEDVDSILSN WISSEFKAQS GVDIQKDKMA LLKRLKLNYH PLLKLISTYP
     YLTADASGPK HCNLKLTRAK LESLTEDFLK KTIKPTENCI KDSGIDKSKI DEVILVGGMS
     RMPRVQKLVQ DLFNKPPNKS VNPDEAVSIG AAIQGGVLKG DVKELLLLDV TPLSLGIETL
     GGVFTKMIPR NTTIPTKKSQ TYSTASDNQT VVSIRVFQGE REMAADNKLL GQFDLSGIPP
     APRGVPQIDV TFDIDANGIV HVSAKDKATG KDHSITIQSS GGLSESEIQD MINKAEKYKD
     EDKKRRELVD LKNEADGAIF NTEKSLNEHK SKLQPNEVQE IESAVQNLRV LLTENLTSND
     VQRLKDAVEG VKNAAMKIGQ AMYRNTGGAS EQQQQHSHEQ TGDQQQQQNQ EGGENNNKQN
//
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