ID   CBBX_GUITH              Reviewed;         371 AA.
AC   Q9SCC7;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Protein cbbX homolog, chloroplastic;
DE   Flags: Precursor;
GN   Name=cbbX;
OS   Guillardia theta (Cryptophyte) (Cryptomonas phi).
OG   Nucleomorph.
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX   NCBI_TaxID=55529;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10742049; DOI=10.1093/oxfordjournals.molbev.a026337;
RA   Maier U.-G., Fraunholz M., Zauner S., Penny S., Douglas S.;
RT   "A nucleomorph-encoded CbbX and the phylogeny of RuBisCO regulators.";
RL   Mol. Biol. Evol. 17:576-583(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11323671; DOI=10.1038/35074092;
RA   Douglas S.E., Zauner S., Fraunholz M., Beaton M., Penny S.L., Deng L.-T.,
RA   Wu X., Reith M.E., Cavalier-Smith T., Maier U.-G.;
RT   "The highly reduced genome of an enslaved algal nucleus.";
RL   Nature 410:1091-1096(2001).
CC   -!- FUNCTION: Seems to be necessary for the expression of RuBisCO.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the CbxX/CfxQ family. {ECO:0000305}.
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DR   EMBL; AJ251479; CAB65663.1; -; Genomic_DNA.
DR   EMBL; AJ010592; CAC27030.1; -; Genomic_DNA.
DR   PIR; A90109; A90109.
DR   RefSeq; XP_001713246.1; XM_001713194.1.
DR   AlphaFoldDB; Q9SCC7; -.
DR   SMR; Q9SCC7; -.
DR   GeneID; 857449; -.
DR   GO; GO:0009507; C:chloroplast; 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; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041627; AAA_lid_6.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR000470; CbxX/CfqX_mono.
DR   InterPro; IPR000641; CbxX/CfxQ.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17866; AAA_lid_6; 1.
DR   PRINTS; PR00819; CBXCFQXSUPER.
DR   PRINTS; PR00820; CBXXCFQX.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chloroplast; Nucleotide-binding; Plastid; Transit peptide.
FT   TRANSIT         1..54
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           55..371
FT                   /note="Protein cbbX homolog, chloroplastic"
FT                   /id="PRO_0000004776"
FT   BINDING         137..144
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   371 AA;  42330 MW;  00683E645C860886 CRC64;
     MIAFISNYIT FKTNRTYKNN ICQLHCQSLN DNDIEARKIK EEAERRKQQA ERNRMQKQMK
     IDRLNAIPED AEAGTVEEFM YKDGVKEILE KLDNDLVGLV PVKSRVREIA ALLVVDKLRR
     NLGLDTSVPS LHMCFTGAPG TGKTTVAMRM GQILQRMGYC RSGHLVVATR DDLVGQYVGH
     TAPKTKEVIK KAMGGVLLID EAYYLYNASN DRDYGQESIE ILLNVMEENR EDLVVVLAGY
     KDRMDKFFSF IPGMSSRVGN HIEFPNYEAE ELLSIAKVMC RDLEYEMSKD AEPIFFEYIK
     KRMTMPYFSN ARTVRNAVDR ARMRAAIRLF NQATSGNSNG LVSKKQLMTL EKEDFVSVEE
     LIARGDNAIV E