ID   RUBA_CHLRE              Reviewed;         580 AA.
AC   Q42694;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=RuBisCO large subunit-binding protein subunit alpha, chloroplastic;
DE   AltName: Full=60 kDa chaperonin subunit alpha;
DE   AltName: Full=CPN-60 alpha;
DE   Flags: Precursor;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7766872; DOI=10.1007/bf00037029;
RA   Thompson M.D., Paavola C.D., Lenvik T.R., Gantt J.S.;
RT   "Chlamydomonas transcripts encoding three divergent plastid chaperonins are
RT   heat-inducible.";
RL   Plant Mol. Biol. 27:1031-1035(1995).
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   -!- INDUCTION: By heat shock.
CC   -!- MISCELLANEOUS: This protein shows ATPase activity.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR   EMBL; L27472; AAA98642.1; -; mRNA.
DR   PIR; S56645; S56645.
DR   PDB; 5CDJ; X-ray; 1.75 A; A/B=224-408.
DR   PDBsum; 5CDJ; -.
DR   AlphaFoldDB; Q42694; -.
DR   SMR; Q42694; -.
DR   STRING; 3055.EDO96383; -.
DR   PRIDE; Q42694; -.
DR   ProMEX; Q42694; -.
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   HAMAP; MF_00600; CH60; 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; 1.
DR   TIGRFAMs; TIGR02348; GroEL; 1.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Chaperone; Chloroplast; Nucleotide-binding;
KW   Plastid; Stress response; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..580
FT                   /note="RuBisCO large subunit-binding protein subunit alpha,
FT                   chloroplastic"
FT                   /id="PRO_0000005019"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          226..229
FT                   /evidence="ECO:0007829|PDB:5CDJ"
FT   HELIX           235..237
FT                   /evidence="ECO:0007829|PDB:5CDJ"
FT   TURN            241..244
FT                   /evidence="ECO:0007829|PDB:5CDJ"
FT   STRAND          245..260
FT                   /evidence="ECO:0007829|PDB:5CDJ"
FT   HELIX           263..274
FT                   /evidence="ECO:0007829|PDB:5CDJ"
FT   TURN            275..277
FT                   /evidence="ECO:0007829|PDB:5CDJ"
FT   STRAND          280..287
FT                   /evidence="ECO:0007829|PDB:5CDJ"
FT   HELIX           289..300
FT                   /evidence="ECO:0007829|PDB:5CDJ"
FT   STRAND          306..310
FT                   /evidence="ECO:0007829|PDB:5CDJ"
FT   STRAND          312..314
FT                   /evidence="ECO:0007829|PDB:5CDJ"
FT   HELIX           315..329
FT                   /evidence="ECO:0007829|PDB:5CDJ"
FT   HELIX           336..338
FT                   /evidence="ECO:0007829|PDB:5CDJ"
FT   HELIX           342..344
FT                   /evidence="ECO:0007829|PDB:5CDJ"
FT   HELIX           347..349
FT                   /evidence="ECO:0007829|PDB:5CDJ"
FT   STRAND          351..358
FT                   /evidence="ECO:0007829|PDB:5CDJ"
FT   STRAND          363..366
FT                   /evidence="ECO:0007829|PDB:5CDJ"
FT   HELIX           372..388
FT                   /evidence="ECO:0007829|PDB:5CDJ"
FT   HELIX           392..405
FT                   /evidence="ECO:0007829|PDB:5CDJ"
SQ   SEQUENCE   580 AA;  61863 MW;  16FD34B115E706F7 CRC64;
     MAQSQLAKGS RQTTGRPFQN KPARAARRLV IRAADAKEIV FDQESRRRLQ AGINKVADAV
     GVTLGPRGRN VVLEQKFGVP QVINDGVSIR RAIELKDPVE NAGAQLIKEV AGRTNDAAGD
     GTTTASVLAR EMIHYGLQSV TAGANPIAVK RGLDKTAEYL VAKLKEHAKP VKGRDDIKNV
     ASISAGNDNA IGEMIADALD KVGSNGVLSI ETSNSTETVV EVQEGMEIDR GYISPQFVTN
     QERLLVEYDN CRVLVTDQKI DAIRDIIPIL EQVTRLNAPL LIIAEDVSGE ALATLVVNKL
     RGVLNVCAIK APGFGERRKS LLQDIAIVTG AEFIAKDLGM KVEQAVVEQL GVARKVTVAN
     NTTTLIADAA SKDEIEMRIA QLKKELAETD SVYDTEKLSE RIAKLSGGVA VIKVGAATEA
     ELEDRKLRIE DAKNATFAAV EEGIVPGGGA ALLHLSELVP AFKETLTDAE EKLGADIVMK
     SLRAPCRLIA DNAGVEGEVI VQRLLGKPFE VGYNAMIDKV ENLLDAGVID PAKVTRNGLL
     NSVSIAGIML TTQAVMVEKH KPSEIPGGMT ASGMPSGMTI