ID   RCA_VIGRR               Reviewed;         439 AA.
AC   O98997;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Ribulose bisphosphate carboxylase/oxygenase activase, chloroplastic;
DE            Short=RA;
DE            Short=RuBisCO activase;
DE   Flags: Precursor;
GN   Name=RCA;
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. 2937;
RA   Yang M.T., Chen Y.M.;
RT   "Cloning and sequencing of a Vigna radiata cDNA.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
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; AF126870; AAD20019.2; -; mRNA.
DR   RefSeq; NP_001304204.1; NM_001317275.1.
DR   AlphaFoldDB; O98997; -.
DR   SMR; O98997; -.
DR   STRING; 3916.O98997; -.
DR   PRIDE; O98997; -.
DR   GeneID; 106757684; -.
DR   KEGG; vra:106757684; -.
DR   Proteomes; UP000087766; Chromosome 3.
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; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..439
FT                   /note="Ribulose bisphosphate carboxylase/oxygenase
FT                   activase, chloroplastic"
FT                   /id="PRO_0000030239"
FT   BINDING         167..174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   439 AA;  47902 MW;  8C0F19682068878D CRC64;
     MAASVSTVGA VNRAILNLNG SGAGASAPTS AFFGTSLKKA VASRVPNSKV TNGSFKIVAA
     EKEIEESQQT NKDRWKGLAY DISDDQQDIT RGKGMVDPLF QAPMDAGTHY AVMSSYEYLS
     TGLRQLDNIK DGFYIAPAFL DKLVVHITKN FMTLPNIKVP LILGIWGGKG QGKSFQCELV
     FAKMGINPIM MSAGELESGN AGEPAKLIRQ RYREAADLIA KGKMCALFIN DLDAGAGRLG
     GTTQYTVNNQ MVNATLMNIA DNPTNVQLPG MYNKEENARV PIIVTGNDFS TLYAPLIRDG
     RMEKFYWAPT RDDRVGVCKG IFRTDGVPEE DITKLVDTFP GQSIDFFGAL RARVYDDEVR
     KWISGVGVDA TGKKLVNSKE GPPTFDQPKM SLDKLLQYGN MLVQEQENVK RVQLADKYLN
     EAALGNANED AIKSGSFFK