ID   VATA_TRYCO              Reviewed;         610 AA.
AC   Q26975;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=V-type proton ATPase catalytic subunit A;
DE            Short=V-ATPase subunit A;
DE            EC=7.1.2.2;
DE   AltName: Full=V-ATPase 69 kDa subunit;
DE   AltName: Full=Vacuolar proton pump subunit alpha;
OS   Trypanosoma congolense.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX   NCBI_TaxID=5692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=IL3000;
RA   Fish W.R., Muriuki C.W., Macklin M.D., Young J.R., Murphy N.B.;
RL   Submitted (SEP-1993) 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   -!- 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   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC       catalytic V1 complex (main components: subunits A, B, C, D, E, and F)
CC       attached to an integral membrane V0 proton pore complex (main
CC       component: the proteolipid protein).
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; Z25814; CAA81062.1; -; mRNA.
DR   PIR; S37049; S37049.
DR   AlphaFoldDB; Q26975; -.
DR   SMR; Q26975; -.
DR   VEuPathDB; TriTrypDB:TcIL3000.A.H_000359700; -.
DR   VEuPathDB; TriTrypDB:TcIL3000_4_700; -.
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: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   Gene3D; 1.10.1140.10; -; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 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   PANTHER; PTHR43607; PTHR43607; 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; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01042; V-ATPase_V1_A; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Hydrogen ion transport; Ion transport; Nucleotide-binding;
KW   Translocase; Transport.
FT   CHAIN           1..610
FT                   /note="V-type proton ATPase catalytic subunit A"
FT                   /id="PRO_0000144571"
FT   BINDING         245..252
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   610 AA;  67638 MW;  9BB4560C71D8B017 CRC64;
     MTSDKNPYKT EQRMGAVKAV SGPVVIAENM GGSAMYELVQ VGSFRLVGEI IRLEGDTATI
     QVYEETGGLT VGDPVYCTGK PLSLELGPGI MSEIFDGIQR PLDTIYRMVE NVFIPRGVQV
     KSLNDQKQWD FKPCLKVGDL VSGGDIIGSV VENSLMYNHS IMIPPNVRGR VTSIVPSGNY
     TLQDDIIELE YNGTVKSLKL MHRWPVRTPR PVASKESGNH PLLTGQRVLD ALFPSVQGGT
     CAIPGAFGCG KTVISQALSK FSNSDAVIYV GCGERGNEMA EVLMDFPTLT TVIDGREESI
     MKRTCLVANT SNMPVAAREA SIYTGITLAE YYRDMGKHIA MMADSTSRWA EALREISGRL
     AEMPADGGYP AYLSARLASF YERAGRVTCI GGPKREGSVT IVGAVSPPGG DFSDPVTSAT
     LGIVQVFWGL EKRLAQRKHF PSVNWLISYS KYLNALEPFF NTLDPDYMRL RSVAAEILQR
     EEELQEIVQL VGKDSLSESD KIILETAKVI REEFLQQNAF TPYDKYCPPY KTCWMLRNIV
     AFYEESQRVV AESAGELKIT WNYIREMIPH IYTGLTEMKF RDPQEGEEAN VEFYRKQNEE
     IVSAFASLLQ