ID   RCA1_LARTR              Reviewed;         476 AA.
AC   Q7X9A0;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Ribulose bisphosphate carboxylase/oxygenase activase 1, chloroplastic;
DE            Short=RA 1;
DE            Short=RuBisCO activase 1;
DE   AltName: Full=RuBisCO activase alpha form;
DE   Flags: Precursor;
GN   Name=RCA1;
OS   Larrea tridentata (Creosote bush) (Zygophyllum tridentatum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Zygophyllales; Zygophyllaceae; Larreoideae; Larrea.
OX   NCBI_TaxID=66636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15084731; DOI=10.1104/pp.103.038323;
RA   Salvucci M.E., Crafts-Brandner S.J.;
RT   "Relationship between the heat tolerance of photosynthesis and the thermal
RT   stability of rubisco activase in plants from contrasting thermal
RT   environments.";
RL   Plant Physiol. 134:1460-1470(2004).
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RuBisCO activase family. {ECO:0000305}.
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DR   EMBL; AY312575; AAP83929.1; -; mRNA.
DR   PDB; 3THG; X-ray; 1.88 A; A=308-409.
DR   PDBsum; 3THG; -.
DR   AlphaFoldDB; Q7X9A0; -.
DR   SMR; Q7X9A0; -.
DR   PRIDE; Q7X9A0; -.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Chloroplast; Nucleotide-binding; Plastid;
KW   Transit peptide.
FT   TRANSIT         1..56
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           57..476
FT                   /note="Ribulose bisphosphate carboxylase/oxygenase activase
FT                   1, chloroplastic"
FT                   /id="PRO_0000030233"
FT   BINDING         165..172
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   HELIX           309..319
FT                   /evidence="ECO:0007829|PDB:3THG"
FT   TURN            320..324
FT                   /evidence="ECO:0007829|PDB:3THG"
FT   HELIX           327..336
FT                   /evidence="ECO:0007829|PDB:3THG"
FT   HELIX           342..373
FT                   /evidence="ECO:0007829|PDB:3THG"
FT   HELIX           390..401
FT                   /evidence="ECO:0007829|PDB:3THG"
SQ   SEQUENCE   476 AA;  52141 MW;  EEDE546300D6D14C CRC64;
     MAAAYSTVGA VNRAPLSLNG SGARASLVPS TAFFGSSLKK SAAKFPKASS GNFKIVAQEI
     SEDQQTDKDK WKGLAYDISD DQQDITRGKG MVDTLFQAPM QSGTHYAVMS SYDYISQGLR
     QYNLDNNMDG FYIAPAFMDK LVVHITKNFL SLPNIKIPLI LGIWGGKGQG KSFQCELVFA
     KMGINPIMMS AGELESGNAG EPAKLIRQRY REAADIIKKG KMCCLFINDL DAGAGRMGGT
     TQYTVNNQMV NATLMNIADN PTNVQLPGMY NKEENPRVPI IVTGNDFSTL YAPLIRDGRM
     EKFYWAPTRE DRIGVCKGIF RTDNVADDDI VKLVDTFPGQ SIDFFGALRA RVYHDEVRKW
     VSEVGVDTIG KKLVNSKEGP PSFEQPKMTI DKLLGYGGML VQEQENVKRV QLADKYMSEA
     ALGDANNDAI KRGTFYGGQA AQQVGNVPVP EGCTDPQATN YDPTARSDDG SCVYKF