RCA_ARAHY
ID RCA_ARAHY Reviewed; 140 AA.
AC P85086;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Ribulose bisphosphate carboxylase/oxygenase activase, chloroplastic;
DE Short=RA;
DE Short=RuBisCO activase;
DE Flags: Fragments;
GN Name=RCA {ECO:0000250|UniProtKB:O98997};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, AND INDUCTION.
RC STRAIN=cv. ICGS-76 {ECO:0000269|Ref.1}; TISSUE=Leaf {ECO:0000269|Ref.1};
RA Katam R., Vasanthaiah H.K.N., Basha S.M., McClung S.;
RT "Water stress responsive differential expression of leaf polypeptides in
RT Peanut.";
RL Submitted (JAN-2007) to UniProtKB.
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
CC -!- INDUCTION: By water stress. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the RuBisCO activase family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P85086; -.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR InterPro; IPR044960; RCA-like.
DR PANTHER; PTHR32429; PTHR32429; 4.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Direct protein sequencing; Nucleotide-binding;
KW Plastid; Stress response.
FT CHAIN <1..>140
FT /note="Ribulose bisphosphate carboxylase/oxygenase
FT activase, chloroplastic"
FT /id="PRO_0000280229"
FT BINDING 55..?
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT NON_CONS 15..16
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 46..47
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 57..58
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 80..81
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 95..96
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 114..115
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 123..124
FT /evidence="ECO:0000303|Ref.1"
FT NON_TER 1
FT /evidence="ECO:0000303|Ref.1"
FT NON_TER 140
FT /evidence="ECO:0000303|Ref.1"
SQ SEQUENCE 140 AA; 15046 MW; B01425BECB370ABE CRC64;
GLAYDISDDQ QDITRGMVDS LFQAPMNDGT HYAVMSSYEY ISQGLRVPLI LGIWGGKMGI
NPIMMSAGEL ESGNAGEPAK MCCLFINDLD AGAGRVPIIV TGNDFSTLYA PLIRIGVCTG
IFRLVDTFPG QSIDFFGALR