ID A0DBI1_PARTE Unreviewed; 710 AA.
AC A0DBI1;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE SubName: Full=Chromosome undetermined scaffold_44, whole genome shotgun sequence {ECO:0000313|EMBL:CAK80398.1};
GN ORFNames=GSPATT00015293001 {ECO:0000313|EMBL:CAK80398.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK80398.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK80398.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK80398.1,
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; CT868363; CAK80398.1; -; Genomic_DNA.
DR RefSeq; XP_001447795.1; XM_001447758.1.
DR AlphaFoldDB; A0DBI1; -.
DR STRING; 5888.A0DBI1; -.
DR EnsemblProtists; CAK80398; CAK80398; GSPATT00015293001.
DR GeneID; 5033580; -.
DR KEGG; ptm:GSPATT00015293001; -.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; A0DBI1; -.
DR OMA; MRRMKEM; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF34; HEAT SHOCK PROTEIN 83; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600}.
FT DOMAIN 31..189
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 220..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 710 AA; 81698 MW; 50F038E9385AE87F CRC64;
MSTTQNKEEQ FHFNADIQQL MGLIINTFYS NKEIFLRELI SNASDALDKI RYKSITDPDS
AGLNVEPNFK IKIIPDKNNN TLTIQDTGIG MTRDELINNL GTIAKSGTKA FMEALNSGAD
ISMIGQFGVG FYSAYLVADK VVVLSKAVGQ QQYKWESQAG GTFFIYDDSE NPNQLTRGSA
VILHLKQDNL EFLEEKRLKD LVKKHSEFIG FPIELQVEKT HEKEVSDDEE DNKEKKTEEG
EVQEEKNKDE KKKKKKIKEV TTEFEQVNKN KPLWMKKPEE VTKEEYANFY KSLTNDWEDH
LSVKQFSVEG GLEFKAVLFI PKRAPFDLFE TKKKKNNIKL YVRRVFIMDD CEELIPEYLG
FIKGVVDSED LPLNISREFL QHNKILKVIK KNITKKCIEM FQELSENTED YKKFYEQFSK
NLKLGIHEDS ANRTKLAEFL RFHTSKSGEE QISLKDYISK MKEGQKDIYF ITGESKASVA
ASPFVESLKK KDYEVIYMVD PIDEYVIQQL KEFDGKKLKN CSKEGLELDQ TEDEKKKFEE
LKSQFEGLCK LIKDILGDKI EKVQLGQRLE QSPCVLVTGE YGWSANMERI MKAQALRDPS
MSSYMMSKKT LEINASHPIM TELKKKADKD KSDKTVKDLI WLLYETALLT SGFSLDDPAH
FASRIHKMIK LGLSIDDAAI EEEDEKLPSL EKKSETANTE ATKSKMEEVD
//
