ID   C7GTW9_YEAS2            Unreviewed;       538 AA.
AC   C7GTW9;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Ssz1p {ECO:0000313|EMBL:EEU05751.1};
GN   Name=SSZ1 {ECO:0000313|EMBL:EEU05751.1};
GN   ORFNames=C1Q_03880 {ECO:0000313|EMBL:EEU05751.1};
OS   Saccharomyces cerevisiae (strain JAY291) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=574961 {ECO:0000313|EMBL:EEU05751.1, ECO:0000313|Proteomes:UP000008073};
RN   [1] {ECO:0000313|EMBL:EEU05751.1, ECO:0000313|Proteomes:UP000008073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAY291 {ECO:0000313|EMBL:EEU05751.1,
RC   ECO:0000313|Proteomes:UP000008073};
RX   PubMed=19812109; DOI=10.1101/gr.091777.109;
RA   Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M., Netto O.V.,
RA   Missawa S.K., Galzerani F., Costa G.G., Vidal R.O., Noronha M.F.,
RA   Dominska M., Andrietta M.G., Andrietta S.R., Cunha A.F., Gomes L.H.,
RA   Tavares F.C., Alcarde A.R., Dietrich F.S., McCusker J.H., Petes T.D.,
RA   Pereira G.A.;
RT   "Genome structure of a Saccharomyces cerevisiae strain widely used in
RT   bioethanol production.";
RL   Genome Res. 19:2258-2270(2009).
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|RuleBase:RU003322}.
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:EEU05751.1}.
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DR   EMBL; ACFL01000280; EEU05751.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7GTW9; -.
DR   Proteomes; UP000008073; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd10232; ScSsz1p_like_NBD; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF537; RIBOSOME-ASSOCIATED COMPLEX SUBUNIT SSZ1; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322}.
FT   REGION          457..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..482
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   538 AA;  58214 MW;  15AD56E7B44FA041 CRC64;
     MSSPVIGITF GNTSSSIAYI NPKNDVDVIA NPDGERAIPS ALSYIGEDEY HGGQALQQLI
     RNPKNTIINF RDFIGLPFDK CDVSKCANGA PAVEVDGKVG FVISRGEGKE EKLTVDEVVS
     RHLNRLKLAA EDYIGSAVKE AVLTVPTNFS EEQKTALKAS AAKIGLQIVQ FINEPSAALL
     AHAEQFPFEK DVNVVVADFG GIRSDAAVIA VRNGIFTILA TAHDLSLGGD NLDTELVEYF
     ASEFQKKYQA NPRKNARSLA KLKANSSITK KTLSNATSAT ISIDSLADGF DYHASINRMR
     YELVANKVFA QFSSFVDSVI AKAELDPLDI DAVLLTGGVS FTPKLTTNLE YTLPESVEIL
     GPQNKNASNN PNELAASGAA LQARLISDYD ADELAEALQP VIVNTPHLKK AIGLIGAKGE
     FHPVLLAETS FPVQKKLTLK QAKGDFLIGV YEGDHHIEEK TLEPTPKEEN AEEDDESEWS
     DDEPEVVREK LYTLGTKLME LGIKNANGVE IIFNINKDGA LRVTARDLKT GNAVKGEL
//