ID B6K3P7_SCHJY Unreviewed; 613 AA.
AC B6K3P7;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=non-chaperonin molecular chaperone ATPase {ECO:0000256|ARBA:ARBA00012554};
DE EC=3.6.4.10 {ECO:0000256|ARBA:ARBA00012554};
GN Name=sks2 {ECO:0000313|JaponicusDB:SJAG_03237};
GN ORFNames=SJAG_03237 {ECO:0000313|EMBL:EEB08104.1};
OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB08104.1, ECO:0000313|Proteomes:UP000001744};
RN [1] {ECO:0000313|EMBL:EEB08104.1, ECO:0000313|Proteomes:UP000001744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
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DR EMBL; KE651167; EEB08104.1; -; Genomic_DNA.
DR RefSeq; XP_002174397.1; XM_002174361.2.
DR AlphaFoldDB; B6K3P7; -.
DR STRING; 402676.B6K3P7; -.
DR EnsemblFungi; EEB08104; EEB08104; SJAG_03237.
DR GeneID; 7049145; -.
DR JaponicusDB; SJAG_03237; sks2.
DR VEuPathDB; FungiDB:SJAG_03237; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_2_1_1; -.
DR OMA; HQTTVQF; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000001744; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR CDD; cd10233; HSPA1-2_6-8-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; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF467; RIBOSOME-ASSOCIATED MOLECULAR CHAPERONE SSB1-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; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000001744};
KW Stress response {ECO:0000313|EMBL:EEB08104.1}.
SQ SEQUENCE 613 AA; 67077 MW; 20043ABCEE07A80B CRC64;
MSEVYEGAIG IDLGTTYSCV AVWETANVEI IPNDQGARTT PSFVAFTDSE RLVGDAAKNQ
AAMNPRNTVF DAKRLIGRRF DDAETQKDIK HWPFKVLDNN GVPTIEVEYL GEKKQFTPQE
ISAMVLTKMK EIAEAKLNKK VEKAVITVPA YFSDSQRAAT KDAGAISGLN VLRIINEPTA
AAIAYGLDAK TEEAKNVLIF DLGGGTFDVS LLKIQGGVFE VLATAGDTHL GGEDFDAALV
EHFIQEFKRK NKLDISEDPR ALRRLRSACE RAKRALSSVT QTTIEVDSLF NGVDFSSSIT
RARFEDINAA TFKKTIDPVA KVLKDAKVTK ANVHDIVLVG GSTRIPKVQK LVSDFFDGRA
LNKSINPDEA VAYGAAVQAA VLTNKADSDK TADLLLLDVV PLSLGVAMEG NVFGVVCPRN
TPIPTIKKRT FTTVADNQTT VTFPVYQGER VNCAENEPLG EFQLTGIPPM PRGQAELEAT
FEIDVNGILK VTAMEKTTGR SAHIEITNSV GHLSSTKIQE MIENAEKNKQ QDKEFAKKLE
AKSQLEAYIS NIEQTISEPN VMMKLKRGDK AKIESQLAEC MSQLELDDAN TDALRKAELR
LKRSVQKAFA SLR
//
