ID   A5E677_LODEL            Unreviewed;       713 AA.
AC   A5E677;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=ATP-dependent molecular chaperone HSC82 {ECO:0000313|EMBL:EDK46935.1};
GN   ORFNames=LELG_05116 {ECO:0000313|EMBL:EDK46935.1};
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK46935.1, ECO:0000313|Proteomes:UP000001996};
RN   [1] {ECO:0000313|EMBL:EDK46935.1, ECO:0000313|Proteomes:UP000001996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC   NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH981531; EDK46935.1; -; Genomic_DNA.
DR   RefSeq; XP_001523700.1; XM_001523650.1.
DR   AlphaFoldDB; A5E677; -.
DR   STRING; 379508.A5E677; -.
DR   GeneID; 5230892; -.
DR   KEGG; lel:LELG_05116; -.
DR   VEuPathDB; FungiDB:LELG_05116; -.
DR   eggNOG; KOG0019; Eukaryota.
DR   HOGENOM; CLU_006684_1_3_1; -.
DR   InParanoid; A5E677; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 547579at2759; -.
DR   Proteomes; UP000001996; 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:UP000001996}.
FT   DOMAIN          29..167
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          219..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          680..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   713 AA;  81682 MW;  41B8F229C5C18260 CRC64;
     MSDPKSETHE FTAEISQLMS LIINTVYSNK EIFLRELISN ASDALDKIRY QALSDPSLLE
     SEPKLFIRII PQKDQKVLEI RDSGIGMTKA DLVNNLGTIA KSGTKSFMEA LSAGADVSMI
     GQFGVGFYSL FLVADHVQVI SKHNDDEQYI WESNAGGKFT VTLDETNERL GRGTMLRLFL
     KEDQLEYLEE KRIKEVVKKH SEFVAYPIEL VVTKEVEKEI PEDESLTKDE EEQTEGDDEK
     KPKLEEVDDE DGKKEKKTKK VKEEVTETEE LNKVKPLWTR NPQDITQDEY NAFYKSISND
     WEDPLAVKHF SVEGQLEFRA ILFVPKRAPF DAFESKKKKN NIKLYVRRVF ITDDAEELIP
     EWLSFIRGVV DSEDLPLNLS REMLQQNKIL KVIRKNIVKK MIETFQEISE DQEQFEKFYS
     AFSKNIKLGI HEDTQNRQAL AKLLRYNSTK STEETTSLTD YVTRMQPHQK NIYYITGESL
     KAVEKSPFLD ALKAKNFEVL FMVDPIDEYA MTQLKEFDDK KLVDITKDFD LEETEEEKAQ
     REKETKDFEP LTKAVKDILG DQVEKVIISD KLVDAPAAIR TGQFGWSANM ERIMKAQALR
     DTTMSSYMSS KKTFELSPRS PIIQTLRKKV EEDGAEDKTV KDLTTLLFDT ALLTSGFTLE
     EPSSFAQRIN RLIALGLNID DDEPETQTES TDAKADTAAT EEPAVESAME EVD
//