ID D8R3X7_SELML Unreviewed; 591 AA.
AC D8R3X7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=V-type proton ATPase catalytic subunit A {ECO:0000256|ARBA:ARBA00018860};
DE EC=7.1.2.2 {ECO:0000256|ARBA:ARBA00012473};
DE AltName: Full=V-ATPase 69 kDa subunit {ECO:0000256|ARBA:ARBA00032088};
DE AltName: Full=Vacuolar proton pump subunit alpha {ECO:0000256|ARBA:ARBA00030856};
GN ORFNames=SELMODRAFT_167777 {ECO:0000313|EMBL:EFJ33015.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ33015.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
CC -!- FUNCTION: Catalytic subunit of the peripheral V1 complex of vacuolar
CC ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a
CC variety of intracellular compartments in eukaryotic cells.
CC {ECO:0000256|ARBA:ARBA00003685}.
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; GL377571; EFJ33015.1; -; Genomic_DNA.
DR RefSeq; XP_002965595.1; XM_002965549.1.
DR AlphaFoldDB; D8R3X7; -.
DR STRING; 88036.D8R3X7; -.
DR EnsemblPlants; EFJ33015; EFJ33015; SELMODRAFT_167777.
DR Gramene; EFJ33015; EFJ33015; SELMODRAFT_167777.
DR KEGG; smo:SELMODRAFT_167777; -.
DR eggNOG; KOG1352; Eukaryota.
DR HOGENOM; CLU_008162_3_1_1; -.
DR InParanoid; D8R3X7; -.
DR OMA; SDARKYP; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0000325; C:plant-type vacuole; IBA:GO_Central.
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; 2.30.30.650; -; 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; 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:UP000001514};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 4..49
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 66..187
FT /note="ATPsynthase alpha/beta subunit N-terminal extension"
FT /evidence="ECO:0000259|Pfam:PF16886"
FT DOMAIN 196..424
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 591 AA; 65026 MW; A6FB0F7AB64A1C08 CRC64;
MAGAAMYELV RVGNDKLMGE IIRLEGDSAT IQVYEETAGL TVNDPVLRTH NPLSVELGPG
ILSNIFDGIQ RPLKSIAIKS GDVYIPRGVA VPALDKDKLW EFSPKKIGVG SAITGGDLYA
IVHENSLMEH HIALPADAMG KITYIAPHGQ YSLQDKVLEL EFQGTKKQFT MLQMWPVRTP
RPVASKLPAD TPLLTGQRIL DALFPSVLGG TCAIPGAFGC GKTVISQALS KFSNSDAVIY
VGCGERGNEM AEVLKDFPQL TITLPDGREE SVMKRTTLVA NTSNMPVAAR EASIYTGITL
AEYFRDMGYN VSMMADSTSR WAEALREISG RLAEMPADSG YPAYLGARLA TFYERAGKVK
CLGSPDRTGS VSIVGAVSPP GGDFSDPVTA ATLNIVQASV FWGLDKKLAQ RKHFPAVNWL
ISYSKYTQAL EGFYEHYDPN FISIRTKARE VLQREDDLNE IVQLVGKDAL AEGDKIILET
AKLLREDYLA QNAFSVYDKF CPFYKSVWMM RNIVHFCDLS TQAVEKAAGS KGQKITFNII
RQRLGDIIYR LVSQKFEDPA EGESALCSTY QKLYDDLTTA FHNLEDEYRA A
//
