ID S9W844_SCHCR Unreviewed; 803 AA.
AC S9W844;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Hsp78-like protein {ECO:0000313|EMBL:EPY53900.1};
GN ORFNames=SPOG_02875 {ECO:0000313|EMBL:EPY53900.1};
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:EPY53900.1, ECO:0000313|Proteomes:UP000015464};
RN [1] {ECO:0000313|EMBL:EPY53900.1, 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 ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; KE546988; EPY53900.1; -; Genomic_DNA.
DR RefSeq; XP_013020990.1; XM_013165536.1.
DR AlphaFoldDB; S9W844; -.
DR STRING; 653667.S9W844; -.
DR EnsemblFungi; EPY53900; EPY53900; SPOG_02875.
DR GeneID; 25037196; -.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_005070_4_0_1; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000015464; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0051787; F:misfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0034605; P:cellular response to heat; IEA:EnsemblFungi.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
DR GO; GO:0042026; P:protein refolding; IEA:EnsemblFungi.
DR GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
DR GO; GO:0043335; P:protein unfolding; IEA:EnsemblFungi.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF176; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000015464}.
FT DOMAIN 132..278
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 532..675
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 701..790
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT COILED 346..426
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 803 AA; 90061 MW; C65E3CB649CF5A53 CRC64;
MYAVQKGIVN RIINVRQYHG SLKKLPRHLI SRNLSQKPAI VQSTGSVNAS SRLSLAVKSN
WRNLRWNQRR FYAANPNGGT FRMNLGGTPK PGAALEEFGT DLTALAKQGK LDPVIGREEE
IQRTIQILSR RTKNNPALVG PAGVGKTAIM EGLATRIVRG EVPESMKEKT VIVLDLGALI
SGAKFRGDFE ERLKSVLSDL ETAEGKVILF VDEMHLLLGF GKAEGSIDAS NLLKPALARG
KLQCCGATTL EEYRKYIEKD AALARRFQAV MITEPSISDS ISILRGLKER YEVHHGVRIT
DDSLVTAVTY SARYITDRFL PDKAIDLVDE ACSSLRLQQE SKPDELRRLD RQIMTIQIEL
ESLRKETDTT SIERREKLES KLAELRVDQE KLSAVWEEER GALNNIKAAK SELEKARIEL
ERTQREGDYT RASELQYAII PELKRKLPEE EENLHNKKPS LVHDSVTSDD IAIVVSRATG
IPTTNLMRGE RDRLLHMERT IGKTIIGQDE ALHAIADAVR LSRAGLQNSN RPLASFLFLG
PTGVGKTALT KALAEFLFDS EKAMIRFDMS EFQEKHTVSR LVGSPPGYVG YEESGELTEA
VRRKPYAVLL FDELEKAHND VTNLLLQVLD EGFLTDAQGR KVDFRSTLIV MTSNLGSEIL
VNDPSSSVTP ESRTKVLEMV QSYYPPEFIN RIDDQIVFNK LSEKNLEGIV NVRLAEVQER
LNDRRITLNV SDAAKKWLAE KGYSPSYGAR PLNRLIQKKI LNTMAMKIIQ GEIKSDENVM
IDVLDGDLEF KISRLESKNS QEN
//