ID   RCA_CHLRE               Reviewed;         408 AA.
AC   P23489;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Ribulose bisphosphate carboxylase/oxygenase activase, chloroplastic;
DE            Short=RA;
DE            Short=RuBisCO activase;
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].
RC   STRAIN=137c / CC-125;
RX   PubMed=16667924; DOI=10.1104/pp.94.4.1837;
RA   Roesler K.R., Ogren W.L.;
RT   "Primary structure of Chlamydomonas reinhardtii ribulose 1,5-bisphosphate
RT   carboxylase/oxygenase activase and evidence for a single polypeptide.";
RL   Plant Physiol. 94:1837-1841(1990).
CC   -!- FUNCTION: Activation of RuBisCO (ribulose-1,5-bisphosphate
CC       carboxylase/oxygenase; EC 4.1.1.39) involves the ATP-dependent
CC       carboxylation of the epsilon-amino group of lysine leading to a
CC       carbamate structure.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
CC   -!- SIMILARITY: Belongs to the RuBisCO activase family. {ECO:0000305}.
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DR   EMBL; M62962; AAA33091.1; -; mRNA.
DR   PIR; A45507; A45507.
DR   AlphaFoldDB; P23489; -.
DR   SMR; P23489; -.
DR   STRING; 3055.EDP04194; -.
DR   ProMEX; P23489; -.
DR   eggNOG; KOG0651; Eukaryota.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR044960; RCA-like.
DR   PANTHER; PTHR32429; PTHR32429; 1.
DR   Pfam; PF00004; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chloroplast; Nucleotide-binding; Plastid; Transit peptide.
FT   TRANSIT         1..32
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..408
FT                   /note="Ribulose bisphosphate carboxylase/oxygenase
FT                   activase, chloroplastic"
FT                   /id="PRO_0000030229"
FT   BINDING         138..145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   408 AA;  45039 MW;  A623408C5FCC1CD5 CRC64;
     MQVTMKSSAV SGQRVGGARV ATRSVRRAQL QVVAPSRKQM GRWRSIDAGV DASDDQQDIT
     RGREMVDDLF QGGFGAGGTH NAVLSSQEYL SQSRASFNNI EDGFYISPAF LDKMTIHIAK
     NFMDLPKIKV PLILGIWGGK GQGKTFQCAL AYKKLGIAPI VMSAGELESG NAGEPAKLIR
     TRYREASDII KKGRMCSLFI NDLDAGAGRM GDTTQYTVNN QMVNATLMNI ADNPTNVQLP
     GVYKNEEIPR VPIVCTGNDF STLYAPLIRD GRMEKYYWNP TREDRIGVCM GIFQEDNVQR
     REVENLVDTF PGQSIDFFGA LRARVYDDMV RQWITDTGVD KIGQQLVNAR QKVAMPKVSM
     DLNVLIKYGK SLVDEQENVK RVQLADAYLS GAELAGHGGS SLPEAYSR