ID   B5VT57_YEAS6            Unreviewed;       693 AA.
AC   B5VT57;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   22-FEB-2023, entry version 47.
DE   SubName: Full=YPL106Cp-like protein {ECO:0000313|EMBL:EDZ68886.1};
GN   ORFNames=AWRI1631_161560 {ECO:0000313|EMBL:EDZ68886.1};
OS   Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=545124 {ECO:0000313|EMBL:EDZ68886.1, ECO:0000313|Proteomes:UP000008988};
RN   [1] {ECO:0000313|EMBL:EDZ68886.1, ECO:0000313|Proteomes:UP000008988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1631 {ECO:0000313|EMBL:EDZ68886.1,
RC   ECO:0000313|Proteomes:UP000008988};
RX   PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA   Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT   "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL   FEMS Yeast Res. 8:1185-1195(2008).
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:EDZ68886.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ABSV01002336; EDZ68886.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5VT57; -.
DR   Proteomes; UP000008988; 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; cd11732; HSP105-110_like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
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   PANTHER; PTHR45639:SF4; HSC70CB, ISOFORM G; 1.
DR   PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   REGION          653..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..693
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   693 AA;  77308 MW;  6558274111B0BC38 CRC64;
     MSTPFGLDLG NNNSVLAVAR NRGIDIVVNE VSNRSTPSVV GFGPKNRYLG ETGKNKQTSN
     IKNTVANLKR IIGLDYHHPD FEQESKHFTS KLVELDDKKT GAEVRFAGEK HVFSATQLAA
     MFIDKVKDTV KQDTKANITD VCIAVPPWYT EEQRYNIADA ARIAGLNPVR IVNDVTAAGV
     SYGIFKTDLP EGEEKPRIVA FVDIGHSSYT CSIMAFKKGQ LKVLGTACDK HFGGRDFDLA
     ITEHFADEFK TKYKIDIREN PKAYNRILTA AEKLKKVLSA NTNAPFSVES VMNDVDVSSQ
     LSREELEELV KPLLERVTEP VTKALAQAKL SAEEVDFVEI IGGTTRIPTL KQSISEAFGK
     PLSTTLNQDE AIAKGAAFIC AIHSPTLRVR PFKFEDIHPY SVSYSWDKQV EDEDHMEVFP
     AGSSFPSTKL ITLNRTGDFS MAASYTDITQ LPPNTPEQIA NWEITGVQLP EGQDSVPVKL
     KLRCDPSGLH TIEEAYTIED IEVEEPIPLP EDAPEDAEQE FKKVTKTVKK DDLTIVAHTF
     GLDAKKLNEL IEKENEMLAQ DKLVAETEDR KNTLEEYIYT LRGKLEEEYA PFASDAEKTK
     LQGMLNKAEE WLYDEGFDSI KAKYIAKYEE LASLGNIIRG RYLAKEEEKK QAIRSKQEAS
     QMAAMAEKLA AQRKAEAEKK EEKKDTEGDV GMD
//