ID S9W0B7_SCHCR Unreviewed; 640 AA.
AC S9W0B7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Heat shock protein S {ECO:0000313|EMBL:EPY51819.1};
GN ORFNames=SPOG_00242 {ECO:0000313|EMBL:EPY51819.1};
OS Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS NBRC 106824 / NRRL Y48691) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY51819.1, ECO:0000313|Proteomes:UP000015464};
RN [1] {ECO:0000313|EMBL:EPY51819.1, ECO:0000313|Proteomes:UP000015464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC {ECO:0000313|Proteomes:UP000015464};
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 -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR EMBL; KE546990; EPY51819.1; -; Genomic_DNA.
DR RefSeq; XP_013023205.1; XM_013167751.1.
DR AlphaFoldDB; S9W0B7; -.
DR STRING; 653667.S9W0B7; -.
DR EnsemblFungi; EPY51819; EPY51819; SPOG_00242.
DR GeneID; 25034574; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_7_0_1; -.
DR OMA; SYAYNIK; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000015464; 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; 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:SF395; HEAT SHOCK 70 KDA PROTEIN COGNATE 1-RELATED; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000015464};
KW Stress response {ECO:0000313|EMBL:EPY51819.1}.
FT REGION 610..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 640 AA; 70084 MW; 8EA11395A2439AD6 CRC64;
MSKSIGIDLG TTYSCVGHFS NNRVEIIAND QGNRTTPSYV AFTDTERLIG DAAKNQVAMN
PHNTVFDAKR LIGRRYNDAE VQSDMKHWPF KVVNKDDRPL IQVEYKGETK TFTPEEISSM
VLLKMREVAE AFMGSKITDA VVTVPAYFND SQRQATKDAG TIAGMNVLRI INEPTAAAIA
YGLDRNTQRE TNVLIFDLGG GTFDVSLLTI EEGIFEVKST AGDTHLGGED FDSRLVNHFI
QEFKRKNKKD ISGNARAVRR LRTACERAKR TLSSSSQASI EIDSMYEGID FYTSITRARF
EELCSDMFRN TMEPVEKVLR DAKVDKSSVH EIVLVGGSTR IPRIQKLVSD YFNGKEPCKS
INPDEAVAYG AAVQAAILTG DTSEKTQDLL LLDVAPLSMG IETAGGVMTP LIKRNTTIPT
KKSEVFSTYS DNQPGVLIQV YEGERARTKD CNLLGKFELS GIPPAPRGVP QIEVTFDVDA
NGILNVSALE KGTGKTQKIT ITNDKGRLSK EDIDRMVAEA EKYKAEDEAE ASRIQAKNHL
ESYAYSLRNS MDDPNLKDKV EASDKEAIDK AVKETIEWLD SNTTAAKDEY ESKQKELEGV
ANPIMAKVYQ AGGAPGGAPP GAAPGAAPGG DQGPEVEEVD
//
