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Database: UniProt
Entry: X6M5R4_RETFI
LinkDB: X6M5R4_RETFI
Original site: X6M5R4_RETFI 
ID   X6M5R4_RETFI            Unreviewed;       622 AA.
AC   X6M5R4;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:ETO08961.1};
DE   Flags: Fragment;
GN   ORFNames=RFI_28426 {ECO:0000313|EMBL:ETO08961.1};
OS   Reticulomyxa filosa.
OC   Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC   Reticulomyxidae; Reticulomyxa.
OX   NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO08961.1, ECO:0000313|Proteomes:UP000023152};
RN   [1] {ECO:0000313|EMBL:ETO08961.1, ECO:0000313|Proteomes:UP000023152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24332546;
RA   Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA   Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA   Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT   "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL   Curr. Biol. 0:0-0(2013).
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETO08961.1}.
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DR   EMBL; ASPP01024507; ETO08961.1; -; Genomic_DNA.
DR   AlphaFoldDB; X6M5R4; -.
DR   EnsemblProtists; ETO08961; ETO08961; RFI_28426.
DR   OMA; LWINEDA; -.
DR   Proteomes; UP000023152; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; IEA:InterPro.
DR   CDD; cd16927; HATPase_Hsp90-like; 1.
DR   Gene3D; 3.30.230.80; -; 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   InterPro; IPR036890; HATPase_C_sf.
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; PF00183; HSP90; 2.
DR   PIRSF; PIRSF002583; Hsp90; 2.
DR   PRINTS; PR00775; HEATSHOCK90.
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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000023152};
KW   Stress response {ECO:0000313|EMBL:ETO08961.1}.
FT   COILED          267..308
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ETO08961.1"
SQ   SEQUENCE   622 AA;  73375 MW;  C70A032ADD51DD47 CRC64;
     TQEEMEANEH WKSSREAETF QFNADIAQLM RVRKKKNKNV CMNNKKKRMY NQKKMIRITK
     KTHTYEIFLR ELISNASDAL DKIRYVSRPN PEVLEKEKKL KNEIIPDPDE KVLIIRNAGI
     GMTKEDLVNN IGTIARSGTK QFIEIISAGA DISTIGQFGV GFYSAYLANE RVVVRSKHNE
     DEQHVWKIIA SGTFRVRDDI DNPYQIKRGT EIYLHLKDDC ANFCKKKNVK KLVKKYSRFV
     AFQISLLTIK EEEKVLYLCF ICFEVNKEEV KVSNDKEKKK IKEKKEKLEL LNKQKQIWTR
     KLEEVSKEEY TAFYKSICND CEEHLAVKHF SADGQLEFSG LLFVPKKALL FEPTKKKKNI
     KLFVQRVFII DGCKDLCTEC LSFIRGVVKS EDLPLKSLQQ NMILKIIQKN IVNKCLELFG
     EIVENKADFK VFYEQFHKNL KLWINEDAKN RNKLADLLKY HSTKSSEELK SLKEYVKGLD
     LPLTEEEKEQ KDEKVILVDN VEKIMVSCRM VESTCPLVTG EYGWSANMER IMKMISFKMK
     MTQKMYQKNK KRTNQTLQQK MLTWKRKKSM QWKKLINLCC RGSKEIVSLC FTNAFFNFYF
     KLDIFEMNTF NHWFAKKTIH FY
//
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