ID   RCA_CUCSA               Reviewed;         413 AA.
AC   Q01587;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Ribulose bisphosphate carboxylase/oxygenase activase, chloroplastic;
DE            Short=RA;
DE            Short=RuBisCO activase;
DE   Flags: Precursor;
OS   Cucumis sativus (Cucumber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cotyledon;
RX   PubMed=1482683; DOI=10.1016/0167-4781(92)90122-g;
RA   Preisig-Mueller R., Kindl H.;
RT   "Sequence analysis of cucumber cotyledon ribulosebisphosphate
RT   carboxylase/oxygenase activase cDNA.";
RL   Biochim. Biophys. Acta 1171:205-206(1992).
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
CC   -!- SIMILARITY: Belongs to the RuBisCO activase family. {ECO:0000305}.
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DR   EMBL; X67674; CAA47906.1; -; mRNA.
DR   PIR; S28172; S28172.
DR   AlphaFoldDB; Q01587; -.
DR   SMR; Q01587; -.
DR   STRING; 3659.XP_004160190.1; -.
DR   PRIDE; Q01587; -.
DR   EnsemblPlants; KGN47126; KGN47126; Csa_6G188680.
DR   Gramene; KGN47126; KGN47126; Csa_6G188680.
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..54
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           55..413
FT                   /note="Ribulose bisphosphate carboxylase/oxygenase
FT                   activase, chloroplastic"
FT                   /id="PRO_0000030230"
FT   BINDING         162..169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   413 AA;  45710 MW;  930EF06AF142A27D CRC64;
     MAATVSTIGA VNRTTLNNSN YGGLVPNSAF LGSRLKVSSR FTTSKMVTGN FKIVAEQDEE
     KQTEKDKWRG LAFDTSDDQQ DITRGKGLAD PLFQAPMGTG THNAVLSSYE YISAGLRDYS
     YDNNVDGFYI APAFMDKLTV HIVKNFLTLP NIKVPLILGV WGGKGQGKSF QCELVFAKMG
     INPIMMSAGE LESGNAGEPA KLIRQRYREA ADIIKKGKMC CLFINDLDAG AGRLGGTTQY
     TVNNQMVNAT LMNIADNPTN VQLPGMYNKE ENPRVPIIVT GNDFSTLYAP LIRDGRMDKF
     YWAPTREDRI GICTGIFRTD GVPFEDIVKL VDTFPGQSID FFGALRARVY DDEVRKWAVG
     VGVERIGRNL VNSKESPPTF DQPKMTIEKL LEYGNMLVME QENVKRVKLV TSI