HSP7F_NAUCC
ID HSP7F_NAUCC Reviewed; 685 AA.
AC Q875V0; G0VCG7;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Heat shock protein homolog SSE1;
GN Name=SSE1; OrderedLocusNames=NCAS_0C01870;
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630;
RX PubMed=12594514; DOI=10.1038/nature01419;
RA Langkjaer R.B., Cliften P.F., Johnston M., Piskur J.;
RT "Yeast genome duplication was followed by asynchronous differentiation of
RT duplicated genes.";
RL Nature 421:848-852(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCC69177.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY144969; AAO32532.1; -; Genomic_DNA.
DR EMBL; HE576754; CCC69177.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; XP_003675543.1; XM_003675495.1.
DR AlphaFoldDB; Q875V0; -.
DR SMR; Q875V0; -.
DR STRING; 1064592.Q875V0; -.
DR EnsemblFungi; CCC69177; CCC69177; NCAS_0C01870.
DR GeneID; 11526433; -.
DR KEGG; ncs:NCAS_0C01870; -.
DR eggNOG; KOG0103; Eukaryota.
DR HOGENOM; CLU_005965_0_1_1; -.
DR InParanoid; Q875V0; -.
DR OrthoDB; 406172at2759; -.
DR Proteomes; UP000001640; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
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..685
FT /note="Heat shock protein homolog SSE1"
FT /id="PRO_0000078394"
FT REGION 651..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 685 AA; 75873 MW; 69308B05204ED598 CRC64;
MSTPFGLDLG NNNSVLAVAR NRGIDIVVNE VSNRSTPSLV GFGQKNRFLG EAGKTKETSN
IKNTVGNLKR IVGLDYTHPD FSTESQFFSS KLVELDDKKV GTQVRLAGES KTFSATQLAA
MFIGKVKNTV QQETKSNIND ICIAVPAWYS EEQRYSIADA AKVAGLNPVR IVNDVTAAAV
SYGVFKTDLP EGDAKPRIVA FVDIGHSSYT CSIMAFKKGE LKVLGTAYDK HFGGRDFDRA
ITEHFADEFK SKYKIDIRTN AKAYNRILTA AEKLKKVLSA NTQAPFSAES VMDDVDVSSS
MTREELEELV KPLLTRVTEP VTKALAQANL TVEDIDFVEI IGGTTRIPTL KNSISEAFNK
PLSTTLNQDE AIAKGAAFIC AIHSPTLRVR PFKFEDIHPY SVSYSWDKQV EEEESMEVFP
AGSTFPSTKL ITLQRTGDFQ MSAYYTTPEQ LPKGTKADIA KWEITGLQVP EGAESVPVKV
VLRCDPSGLH TIEEAYTVED IKVQEVVPLP EDAPEDAEPE FREVTKTVKK DALTIVAHTF
ALEGKPLNDL IEKENAMFAQ DKLVAETEDR KNALEEYIYT LRGKLEEEYA PFASEAEKTK
LTGMLAKAEE WLYDEGYDSI KAKYIAKYEE LASLGNMIRG RYLAKEEEKR QALRSNQEAS
KMADLSAKLA AQRKAEAEAK ENAKE