ID   RCA_MAIZE               Reviewed;         433 AA.
AC   Q9ZT00;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2003, sequence version 3.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Ribulose bisphosphate carboxylase/oxygenase activase, chloroplastic;
DE            Short=RA;
DE            Short=RuBisCO activase;
DE   Flags: Precursor;
GN   Name=RCA1; Synonyms=RCA;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Chalqueno; TISSUE=Leaf;
RA   Ayala-Ochoa A., Loza-Tavera H., Sanchez de Jimenez E.;
RT   "A cDNA from maize (Zea mays L) encoding ribulose-1,5-bisphosphate
RT   carboxylase/oxygenase activase.";
RL   (er) Plant Gene Register PGR98-207(1998).
RN   [2]
RP   SEQUENCE REVISION TO 57-68; 160; 219 AND 347.
RA   Ayala-Ochoa A., Loza-Tavera H., Sanchez de Jimenez E.;
RL   Submitted (APR-2002) 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; AF084478; AAC97932.3; -; mRNA.
DR   RefSeq; NP_001104921.1; NM_001111451.2.
DR   AlphaFoldDB; Q9ZT00; -.
DR   SMR; Q9ZT00; -.
DR   STRING; 4577.GRMZM2G162200_P01; -.
DR   PaxDb; Q9ZT00; -.
DR   PRIDE; Q9ZT00; -.
DR   EnsemblPlants; Zm00001eb164390_T001; Zm00001eb164390_P001; Zm00001eb164390.
DR   EnsemblPlants; Zm00001eb164390_T002; Zm00001eb164390_P002; Zm00001eb164390.
DR   GeneID; 541712; -.
DR   Gramene; Zm00001eb164390_T001; Zm00001eb164390_P001; Zm00001eb164390.
DR   Gramene; Zm00001eb164390_T002; Zm00001eb164390_P002; Zm00001eb164390.
DR   KEGG; zma:541712; -.
DR   MaizeGDB; 114858; -.
DR   eggNOG; KOG0651; Eukaryota.
DR   HOGENOM; CLU_038420_0_0_1; -.
DR   OMA; RFAQNNK; -.
DR   OrthoDB; 655049at2759; -.
DR   Proteomes; UP000007305; Chromosome 4.
DR   ExpressionAtlas; Q9ZT00; baseline and differential.
DR   Genevisible; Q9ZT00; ZM.
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   GO; GO:0046863; F:ribulose-1,5-bisphosphate carboxylase/oxygenase activator activity; IBA:GO_Central.
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..53
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           54..433
FT                   /note="Ribulose bisphosphate carboxylase/oxygenase
FT                   activase, chloroplastic"
FT                   /id="PRO_0000030236"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         161..168
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   433 AA;  47938 MW;  5730A336E6D378D2 CRC64;
     MAAAFSSTVG APASTPTRSS FLGKKLNKPQ VSAAVTYHGK SSSSNSRFKA MAAKEVDETK
     QTDEDRWKGL AYDISDDQQD ITRGKGLVDN LFQAPMGDGT HVAVLSSYDY ISQGQKSYNF
     DNMMDGFYIA KGFMDKLVVH LSKNFMTLPN IKVPLILGIW GGKGQGKSFQ CELVFAKMGI
     TPIMMSAGEL ESGNAGEPAK LIRQRYREAS DLIKKGKMSC LFINDLDAGA GRMGGTTQYT
     VNNQMVNATL MNIADNPTNV QLPGMYNKED NPRVPIIVTG NDFSTLYAPL IRDGRMEKFY
     WAPTREDRIG VCKGIFRTDG VDEEHVVQLV DTFPGQSIDF FGALRARVYD DEVRRWVSET
     GVENIARKLV NSKEGPPTFE QPKITIEKLL EYGHMLVAEQ ENVKRVQLAD KYLNEAALGE
     ANEDAMKTGS FFK