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Database: UniProt
Entry: B8XSK8_CHLRE
LinkDB: B8XSK8_CHLRE
Original site: B8XSK8_CHLRE 
ID   B8XSK8_CHLRE            Unreviewed;       272 AA.
AC   B8XSK8;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=ATP synthase CF1 alpha subunit {ECO:0000313|EMBL:ACK37276.1};
DE   Flags: Fragment;
GN   Name=atpA {ECO:0000313|EMBL:ACK37276.1};
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:ACK37276.1}.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055 {ECO:0000313|EMBL:ACK37276.1};
RN   [1] {ECO:0000313|EMBL:ACK37276.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CC-2290 S1 D2 mt- {ECO:0000313|EMBL:ACK37276.1}, and CC-503
RC   cw92 mt+ {ECO:0000313|EMBL:ACK37277.1};
RX   PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA   Smith D.R., Lee R.W.;
RT   "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT   addressing the mutational-hazard hypothesis.";
RL   BMC Evol. Biol. 9:120-120(2009).
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936}.
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DR   EMBL; FJ436944; ACK37276.1; -; Genomic_DNA.
DR   EMBL; FJ436945; ACK37277.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8XSK8; -.
DR   ExpressionAtlas; B8XSK8; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   CDD; cd18116; ATP-synt_F1_alpha_N; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR023366; ATP_synth_asu-like_sf.
DR   InterPro; IPR005294; ATP_synth_F1_asu.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR48082:SF12; ATP SYNTHASE SUBUNIT ALPHA, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR48082; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chloroplast {ECO:0000313|EMBL:ACK37276.1};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Plastid {ECO:0000313|EMBL:ACK37276.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          30..93
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          150..272
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   NON_TER         272
FT                   /evidence="ECO:0000313|EMBL:ACK37276.1"
SQ   SEQUENCE   272 AA;  29113 MW;  43FA277745388FC7 CRC64;
     MAMRTPEELS NLIKDLIEQY TPEVKMVDFG IVFQVGDGIA RIYGLEKAMS GELLEFEDGT
     LGIALNLEAN NVGAVLLGDG LKITEGSRVR CTGKIAEIPV GEAYLGRVVD GLARPVDGKG
     AVQTKDSRAI ESPAPGIVAR RSVYEPLATG LVAVDAMIPV GRGQRELIIG DRQTGKTAIA
     VDTILNQKGK GVICVYVAIG QKASSVAQVL NTLKERGALD YTIIVMANAN EPATLQYLAP
     YTGATLAEYF MYTGRPTLTI YDDLSKQAQA YR
//
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