ID   RCA_MALDO               Reviewed;         437 AA.
AC   Q40281;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Ribulose bisphosphate carboxylase/oxygenase activase, chloroplastic;
DE            Short=RA;
DE            Short=RuBisCO activase;
DE   Flags: Precursor;
GN   Name=RCA;
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8219085; DOI=10.1007/bf00019298;
RA   Watillon B., Kettmann R., Boxus P., Burny A.;
RT   "Developmental and circadian pattern of rubisco activase mRNA accumulation
RT   in apple plants.";
RL   Plant Mol. Biol. 23:501-509(1993).
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; Z21794; CAA79857.1; -; mRNA.
DR   PIR; S39551; S39551.
DR   RefSeq; NP_001280819.1; NM_001293890.1.
DR   AlphaFoldDB; Q40281; -.
DR   SMR; Q40281; -.
DR   STRING; 3750.XP_008393915.1; -.
DR   PRIDE; Q40281; -.
DR   GeneID; 103456062; -.
DR   KEGG; mdm:103456062; -.
DR   OrthoDB; 655049at2759; -.
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..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..437
FT                   /note="Ribulose bisphosphate carboxylase/oxygenase
FT                   activase, chloroplastic"
FT                   /id="PRO_0000030237"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         165..172
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   437 AA;  48077 MW;  62465BE200C896C3 CRC64;
     MATAVSTIGS VNRAPPNLNG SSSSASVPSS TFLGSSLKKV NSRFTNSKVS SGSLRIVASV
     DEDKQTDKDR WKGLAFDTSD DQQDITRGKG KVDSLFQAPQ GSGTHFAIMS SYEYISTGLR
     QYNFDNNMDG YYIAPAFMDK LVVHITKNFM TLPNMKVPLI LGIWGGKGQG KSFQCELVFA
     KMRISPIMMS AGELESGNAG EPAKLIRQRY REAADIIRKG KMCALFINDL DAGAGRLGGT
     TQYTVNNQMV NATLMNIADN PTNVQLPGMY NKEENPRVPI IVTGNDFSTL YAPLIRDGRM
     EKFYWAPTRE DRIGVCIGIF RSDNVAKEDI VKLVDTFPGQ SIDFFGALRA RVYDDEVRKW
     ITGVGVDSIG KKLVNSKEGP PTFEQPKMTI EKLLEYGNML VQEQENVKRV QLADKYLSEA
     ALGDANSDAM NTGTFYG