ID Q4UJ82_PARTE Unreviewed; 618 AA.
AC Q4UJ82;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 108.
DE RecName: Full=H(+)-transporting two-sector ATPase {ECO:0000256|ARBA:ARBA00012473};
DE EC=7.1.2.2 {ECO:0000256|ARBA:ARBA00012473};
GN Name=vhaA1 {ECO:0000313|EMBL:CAH39848.1};
GN Synonyms=vhaA2 {ECO:0000313|EMBL:CAH39847.1};
GN ORFNames=GSPATT00014758001 {ECO:0000313|EMBL:CAK79826.1},
GN GSPATT00039196001 {ECO:0000313|EMBL:CAK77062.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAH39848.1};
RN [1] {ECO:0000313|EMBL:CAH39848.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=D4-2 {ECO:0000313|EMBL:CAH39848.1};
RA Genoscope;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAH39848.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=D4-2 {ECO:0000313|EMBL:CAH39848.1};
RA Wassmer T., Froissard M., Plattner H., Kissmehl R., Cohen J.;
RT "The vacuolar proton-ATPase plays a major role in several membrane-bounded
RT organelles in Paramecium.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAK77062.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK77062.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
RN [4] {ECO:0000313|EMBL:CAK77062.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK77062.1};
RG Genoscope;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001741};
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936}.
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DR EMBL; CR764096; CAH39847.1; -; Genomic_DNA.
DR EMBL; CR764097; CAH39848.1; -; Genomic_DNA.
DR EMBL; CT868262; CAK77062.1; -; Genomic_DNA.
DR EMBL; CT868341; CAK79826.1; -; Genomic_DNA.
DR RefSeq; XP_001444459.1; XM_001444422.1.
DR RefSeq; XP_001447223.1; XM_001447186.1.
DR AlphaFoldDB; Q4UJ82; -.
DR STRING; 5888.Q4UJ82; -.
DR TCDB; 3.A.2.2.8; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR EnsemblProtists; CAK77062; CAK77062; GSPATT00039196001.
DR EnsemblProtists; CAK79826; CAK79826; GSPATT00014758001.
DR GeneID; 5030242; -.
DR GeneID; 5033008; -.
DR KEGG; ptm:GSPATT00014758001; -.
DR KEGG; ptm:GSPATT00039196001; -.
DR eggNOG; KOG1352; Eukaryota.
DR HOGENOM; CLU_008162_3_1_1; -.
DR InParanoid; Q4UJ82; -.
DR OMA; RIVKTFW; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR CDD; cd18111; ATP-synt_V_A-type_alpha_C; 1.
DR CDD; cd18119; ATP-synt_V_A-type_alpha_N; 1.
DR CDD; cd01134; V_A-ATPase_A; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00309; ATP_synth_A_arch; 1.
DR InterPro; IPR031686; ATP-synth_a_Xtn.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
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; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR005725; ATPase_V1-cplx_asu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022878; V-ATPase_asu.
DR NCBIfam; TIGR01042; V-ATPase_V1_A; 1.
DR PANTHER; PTHR43607; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1.
DR PANTHER; PTHR43607:SF1; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF16886; ATP-synt_ab_Xtn; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 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.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 22..83
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 100..223
FT /note="ATPsynthase alpha/beta subunit N-terminal extension"
FT /evidence="ECO:0000259|Pfam:PF16886"
FT DOMAIN 232..457
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 618 AA; 69298 MW; 704F090A7D459E33 CRC64;
MNKQRKTQLE ELQEKESSFG RVFKVAGPLV VAEKMAGAKM FELVKVGWDK LVGEIIKLEG
DNASIQCYED TSGLTVGDPV MRTKSPLSVE LGPGILTQIF DGIQRPLQVI AEQSSSIFVP
RGVDIPALDQ DRIWEFKPSS LVKVGSMISG GDIYGSVFEN NLFDEHKILT APRVQGRVTY
IAPEGNYTLK DKVLEVELDG KKHQYGMSHF WPVRQPRPII EKLQGNTPLL TGQRVLDALY
PSVLGGTCCI PGAFGCGKTC ISQALSKYSN SECIIYVGCG ERGNEMAEVL SEFPELTIQM
KGKEENIMQR TCLVANTSNM PVAAREASIY TGITLAEYFR DMGFNVSMMA DSTSRWAEAL
REISGRLAEM PADQGYPAYL ASKLAQFYER AGRVRCRGSP DREGSITIVG AVSPPGGDFT
DPVTTATLTI VQVFWGLDKK LAQRKHFPSV NWTISNSNYE KILEPYFNAF DPEFSHLRVM
FKQILHEESE LNEIVQLVGR DSLSEDQKLS LEIAKIIRED FLQQDAFSKY DYNCPLYKTI
GMMRCIVSFF ECGKKAILES SGDAKITWNI ILNQTKPQFV KLSQMKFEDP KQPKQELMNY
FTKFVDEIKS AFRNLTDK
//
