ID A0A109FKA3_9BASI Unreviewed; 715 AA.
AC A0A109FKA3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:KWU46110.1};
GN ORFNames=RHOSPDRAFT_32104 {ECO:0000313|EMBL:KWU46110.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU46110.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU46110.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU46110.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ954468; KWU46110.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A109FKA3; -.
DR STRING; 1305733.A0A109FKA3; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000062823; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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:UP000062823};
KW Stress response {ECO:0000313|EMBL:KWU46110.1}.
FT DOMAIN 34..189
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 220..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 715 AA; 81055 MW; 15AE93C95A9F0F32 CRC64;
MASTSTTANS GETFSFQAEI TQLLDLIINT FYSNKEIFLR ELISNSSDAL DKIRYAALTD
PTQLDSEKEL FIRITPDKAN KTLTIRDSGI GMTKADLVNN LGTIAKSGTK AFMEALSSGA
DISMIGQFGV GFYSAYLVAD KVTVITKHND DEQYIWESSA GGTFTITQDT VNPPIGRGTV
MILHMKEDQL EYLEEKRIKD IVKKHSEFIS YPIQLVTTKE VEKEVEEEEE ETAEDADKPK
IEEVEDEDSK KEKKKKTVKE NVTEQVELNK TKPLWTRNPQ DITPEEYGAF YKSLTNDWED
HLAVKHFSVE GQLEFKAILF IPKRAPFDLF ESKKKRNNIK LYVRRVFIMD DCEDLIPEYL
NFIKGIVDSE DLPLNISRET LQQNKILKVI RKNLVKKSLE MIQDIAEDKD NFAKFYEAFG
KNLKLGIHED AQNRSKLAEF LRFYSTKSGD EMTSLKDYIT RTPEHQKNIY YLTGESLSQV
RDSPFLEIFK KKGFEVLLMV DPIDEYATTQ LKEFEDKKLV CVSKEGLELE ETDEEKAARE
EESKQFEDLT RTMKEILGDR VEKVAVSNRI ADSPCVLVTG QFGWSANMER IMKAQALRDS
SMSSYMQSKK TLEINPSNPI IRELKNKVQA DAADKAVRDL VVLLFETALL TSGFSLESPQ
TYCQRIYSMI ALGLSIDQDE LPQSSSATEP AATESSGDAP PPLESAGASA MEELD
//
