ID   RUBA_RICCO              Reviewed;         495 AA.
AC   P08824;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=RuBisCO large subunit-binding protein subunit alpha;
DE   AltName: Full=60 kDa chaperonin subunit alpha;
DE   AltName: Full=CPN-60 alpha;
DE   Flags: Fragment;
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seed;
RX   PubMed=2897629; DOI=10.1038/333330a0;
RA   Hemmingsen S.M., Woolford C., van der Vies S.M., Tilly K., Dennis D.T.,
RA   Georgopoulos C., Hendrix R.W., Ellis R.J.;
RT   "Homologous plant and bacterial proteins chaperone oligomeric protein
RT   assembly.";
RL   Nature 333:330-334(1988).
CC   -!- FUNCTION: This protein binds RuBisCO small and large subunits and is
CC       implicated in the assembly of the enzyme oligomer.
CC   -!- SUBUNIT: Oligomer of probably six alpha and six beta subunits.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- MISCELLANEOUS: This protein shows ATPase activity.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR   EMBL; X07852; CAB51619.1; ALT_SEQ; mRNA.
DR   PIR; S02199; HHCSBA.
DR   AlphaFoldDB; P08824; -.
DR   SMR; P08824; -.
DR   STRING; 3988.XP_002534347.1; -.
DR   PRIDE; P08824; -.
DR   eggNOG; KOG0356; Eukaryota.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR   CDD; cd03344; GroEL; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR   InterPro; IPR001844; Cpn60/GroEL.
DR   InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR   InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR   InterPro; IPR027413; GROEL-like_equatorial_sf.
DR   InterPro; IPR027410; TCP-1-like_intermed_sf.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00298; CHAPERONIN60.
DR   SUPFAM; SSF48592; SSF48592; 1.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   SUPFAM; SSF54849; SSF54849; 2.
DR   TIGRFAMs; TIGR02348; GroEL; 1.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Chloroplast; Nucleotide-binding; Plastid.
FT   CHAIN           <1..>495
FT                   /note="RuBisCO large subunit-binding protein subunit alpha"
FT                   /id="PRO_0000063630"
FT   NON_TER         1
FT   NON_TER         495
SQ   SEQUENCE   495 AA;  52379 MW;  CF6DF44E5E8FE37A CRC64;
     RTALQSGIDK LADAVGLTLG PRGRNVVLDE FGSPKVVNEG VTIARAIELP DPMENAGAAL
     IREVASKTND SAGDGTTTAS VLAREIIKLG LLSVTSGANP VSIKRGIDKT VQGLIEELEK
     KARPVKGRDD IKAVASISAG NDELIGTMIA DAIDKVGPDG VLSIESSSSF ETTVEVEEGM
     EIDRGYISPQ FVTNPEKLIC EFENARVLVT DQKITAIKDI IPLLEKTTQL RAPLLIIAED
     VTGEALATLV VNKMRGILNV AAIKAPGFGE RRKALLQDIA ILTGAEFQAS DLGLLVENTS
     VEQLGIARKV TITKDSTTLI ADAASKDELQ ARIAQLKREL AETDSVYDSE KLAERIAKLS
     GGVAVIKVGA ATETELEDRK LRIEDAKNAT FAAIEEGIVP GGGAALVHLS TVVPAINGED
     KDADERLGAD ILQKALVAPA SLIAQNAGIE GEVVVEKVKA REWEIGYNAM TDKYENLVEA
     GVIDPAKVTR CALQN