ID W9S238_9ROSA Unreviewed; 623 AA.
AC W9S238;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=L484_003800 {ECO:0000313|EMBL:EXB82939.1};
OS Morus notabilis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX NCBI_TaxID=981085 {ECO:0000313|EMBL:EXB82939.1, ECO:0000313|Proteomes:UP000030645};
RN [1] {ECO:0000313|Proteomes:UP000030645}
RP NUCLEOTIDE SEQUENCE.
RA He N., Zhao S.;
RT "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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; KE344875; EXB82939.1; -; Genomic_DNA.
DR RefSeq; XP_010100585.1; XM_010102283.1.
DR AlphaFoldDB; W9S238; -.
DR STRING; 981085.W9S238; -.
DR GeneID; 21387324; -.
DR KEGG; mnt:21387324; -.
DR eggNOG; KOG1352; Eukaryota.
DR OrthoDB; 5473187at2759; -.
DR Proteomes; UP000030645; Unassembled 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; IEA:UniProtKB-EC.
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:UP000030645};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 25..85
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 102..223
FT /note="ATPsynthase alpha/beta subunit N-terminal extension"
FT /evidence="ECO:0000259|Pfam:PF16886"
FT DOMAIN 232..458
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 623 AA; 68753 MW; 467F25B5876359E1 CRC64;
MPSVYGARLT TFEDSEKESE YGYVRKVSGP VVVADGMAGA AMYELVRVGH DNLIGEIIRL
EGHSATIQVY EETAGLTVND PVLRTHKPLS VELGPGILGT IFDGIQRPLK TIAKRSGDVY
IPRGVAVPAL DKDTLWEFQP KKIGEGDLLT GGDLYAAVFE NSLMQHHVVL PPDAMGKITY
IAPAGQYSLQ DTVLELEFQG VKKEFTMLQT WPVRTPRPVA SKLAADTPLL TGQRVLDALF
PSVLGGTCAI PGAFGCGKTV ISQALSKYSN SDTVVYVGCG ERGNEMAEVL MDFPQLTMTL
PDGREESVMK RTTLVANTSN MPVAAREASI YTGITIAEYF RDMGYNVSMM ADSTSRWAEA
LREISGRLAE MPADSGYPAY LAARLASFYE RAGKVKCLGG PERTGSVTIV GAVSPPGGDF
SDPVTSATLS IVQVFWGLDK KLAQRKHFPS VNWLISYSKY AGALESFYEQ FDPDFINIRT
KAREILQRED DLNEIVQLVG KDALAETDKI TLETAKLLRE DYLAQNAFSP YDKYCPFYKS
VWMMRNIIHF YNLANQAVEK GAGMDGQKIT YTLIKHRLGD LFYRLVSQKF EDPAEGEPVL
VEKFKKLHED LTNGFHALED ETR
//
