ID   HSP7F_CANGA             Reviewed;         694 AA.
AC   Q6FJI3;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Heat shock protein homolog SSE1;
GN   Name=SSE1; OrderedLocusNames=CAGL0M06083g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; CR380959; CAG62587.1; -; Genomic_DNA.
DR   RefSeq; XP_449611.1; XM_449611.1.
DR   AlphaFoldDB; Q6FJI3; -.
DR   SMR; Q6FJI3; -.
DR   STRING; 5478.XP_449611.1; -.
DR   EnsemblFungi; CAG62587; CAG62587; CAGL0M06083g.
DR   GeneID; 2891659; -.
DR   KEGG; cgr:CAGL0M06083g; -.
DR   CGD; CAL0136515; SSE1.
DR   VEuPathDB; FungiDB:CAGL0M06083g; -.
DR   eggNOG; KOG0103; Eukaryota.
DR   HOGENOM; CLU_005965_5_1_1; -.
DR   InParanoid; Q6FJI3; -.
DR   OMA; AYDRHFG; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005829; C:cytosol; IDA:CGD.
DR   GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR   GO; GO:0005844; C:polysome; IEA:EnsemblFungi.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0042277; F:peptide binding; IEA:EnsemblFungi.
DR   GO; GO:0006914; P:autophagy; IEA:EnsemblFungi.
DR   GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0042026; P:protein refolding; IEA:EnsemblFungi.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
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   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS00329; HSP70_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..694
FT                   /note="Heat shock protein homolog SSE1"
FT                   /id="PRO_0000078393"
FT   REGION          671..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        673..688
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   694 AA;  77366 MW;  9868B6F66F9E3049 CRC64;
     MSTPFGLDFG NDNSVLAVAR NRGIDIVVNE VSNRSTPSMV GFGQKNRFLG ESAKTKQTSN
     IKNTVGNLKR ILGLDYDHPD FQEESKFFTS KLVKLEDGKI GTQVRFAGES TTFSATQLNA
     MFINKVKQTV ETETKANITD VCIAVPTWYT EEQRYAAADA ARIAGLNPVR IVNDITAAGV
     SYGVFKTDLP EGEEKPRIVA FIDIGHSSYT CSIMAFKKGE LKVLGTAWDK NFGGRNFDRA
     ITEHFADEFK TKYKIDIREN PKAYNRVMTS AERLKKVLSA NTAAPFSVEN VMNDVDASSQ
     LSREELEELV KPMLERVTEP VTKALAQAGL TKDDVDFVEI IGGTTRIPTL KNSISEAFGK
     PLSTTLNQDE AIAKGAAFIC AIHSPTLRVR PFKFEDIHQF SVSYKWDKQV EDEDHLEVFP
     ANSNFPSTKL ITLHRSGDFS MEANYTNKEE LPPHLDANIA KWDITGVQIP EGETSVPVKL
     KLRCDPSGLH IIEEAYSLED IVVKEEVPLP EDAPEDAVPE VKEVTKTVKK DTLEITAHTF
     TLADDKLNTL IEKENDMTAQ DRLVAETEDR KNNLEEYIYT LRGKLDEEYS DFASDAEKTK
     LKDMLAKAEE WLYEDGFDTI KAKYIAKYEE LAAIGNVIRG RYLAKEEEKK QALRAKQEAA
     NLAALSEKLA AQRSADSEAK KDATPEGDAQ MDLD