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Database: UniProt
Entry: S9W844_SCHCR
LinkDB: S9W844_SCHCR
Original site: S9W844_SCHCR 
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
//
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