ID A0A2V0PJ24_9CHLO Unreviewed; 446 AA.
AC A0A2V0PJ24;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Ribulose bisphosphate carboxylase/oxygenase activase, chloroplastic {ECO:0000256|RuleBase:RU369045};
DE Short=RA {ECO:0000256|RuleBase:RU369045};
DE Short=RuBisCO activase {ECO:0000256|RuleBase:RU369045};
GN ORFNames=Rsub_12365 {ECO:0000313|EMBL:GBF99559.1};
OS Raphidocelis subcapitata.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF99559.1, ECO:0000313|Proteomes:UP000247498};
RN [1] {ECO:0000313|EMBL:GBF99559.1, ECO:0000313|Proteomes:UP000247498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-35 {ECO:0000313|EMBL:GBF99559.1,
RC ECO:0000313|Proteomes:UP000247498};
RX PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT insight into genome evolution and environmental adaptations in the
RT Sphaeropleales.";
RL Sci. Rep. 8:8058-8058(2018).
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:0000256|ARBA:ARBA00025556,
CC ECO:0000256|RuleBase:RU369045}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000256|ARBA:ARBA00004470, ECO:0000256|RuleBase:RU369045}.
CC -!- SIMILARITY: Belongs to the RuBisCO activase family.
CC {ECO:0000256|ARBA:ARBA00025781, ECO:0000256|RuleBase:RU369045}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBF99559.1}.
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DR EMBL; BDRX01000162; GBF99559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V0PJ24; -.
DR STRING; 307507.A0A2V0PJ24; -.
DR InParanoid; A0A2V0PJ24; -.
DR Proteomes; UP000247498; Unassembled WGS sequence.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046863; F:ribulose-1,5-bisphosphate carboxylase/oxygenase activator activity; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.8.1070; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR044960; RCA-like.
DR PANTHER; PTHR32429; -; 1.
DR PANTHER; PTHR32429:SF11; OS04G0658300 PROTEIN; 1.
DR Pfam; PF00004; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU369045};
KW Chloroplast {ECO:0000256|RuleBase:RU369045};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU369045};
KW Plastid {ECO:0000256|RuleBase:RU369045};
KW Reference proteome {ECO:0000313|Proteomes:UP000247498}.
FT DOMAIN 197..342
FT /note="ATPase AAA-type core"
FT /evidence="ECO:0000259|Pfam:PF00004"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 446 AA; 48016 MW; DF8482EECCD57A0E CRC64;
MTPLAPAHGR APALARPSRP AAAPRPPRRA RLGVAAAAQQ QAGDGAAAAA AASADPQQQQ
QQQQQQQAGA QAPGPEGEKG ARSRSSSWGA VESGGGRGGG ADYLYELGKS DYNTNVDAGQ
NVAHIDYLFT GNTLGHKTDI ADGSLRGYEF RTFENIQGDY FIAPRFLEKV AVHVVKTYLV
DSGALDPAVR VPLILGIWGP KGCGKTFQLE LAFKKLGVEA VVMSAGELES DIAGKPGRLI
RERYRKASNM GKVRGRLTAL VINDIDAGLG HFANTQITVN NQIVVGTLMN ICDTPTQVSI
SQDWREGDFI NRVPIIVTGN DFSTLFAPLV RDGRMDKFFW CPAFEDKVEI VHQMYRDDGL
PRDDVVDRTT FDSDKADFSD LHRRLVKGAD LPQFEPVTAT LAALVAEGER LVAEQDAVNA
NKLSEEYLKH LAAAKKRRGV GIGLSG
//
