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Database: UniProt
Entry: A0A316WCA9_9BASI
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ID   A0A316WCA9_9BASI        Unreviewed;       618 AA.
AC   A0A316WCA9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=V-type proton ATPase catalytic subunit A {ECO:0000256|ARBA:ARBA00018860};
DE            EC=7.1.2.2 {ECO:0000256|ARBA:ARBA00012473};
GN   ORFNames=IE81DRAFT_320274 {ECO:0000313|EMBL:PWN45513.1};
OS   Ceraceosorus guamensis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=1522189 {ECO:0000313|EMBL:PWN45513.1, ECO:0000313|Proteomes:UP000245783};
RN   [1] {ECO:0000313|EMBL:PWN45513.1, ECO:0000313|Proteomes:UP000245783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4658 {ECO:0000313|EMBL:PWN45513.1,
RC   ECO:0000313|Proteomes:UP000245783};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
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   -!- SUBCELLULAR LOCATION: Endomembrane system
CC       {ECO:0000256|ARBA:ARBA00029433}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00029433}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00029433}. Vacuole membrane
CC       {ECO:0000256|ARBA:ARBA00029427}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00029427}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00029427}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936}.
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DR   EMBL; KZ819355; PWN45513.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316WCA9; -.
DR   STRING; 1522189.A0A316WCA9; -.
DR   InParanoid; A0A316WCA9; -.
DR   OrthoDB; 5473187at2759; -.
DR   Proteomes; UP000245783; Unassembled WGS sequence.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
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:UP000245783};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          28..89
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          105..227
FT                   /note="ATPsynthase alpha/beta subunit N-terminal extension"
FT                   /evidence="ECO:0000259|Pfam:PF16886"
FT   DOMAIN          236..461
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
SQ   SEQUENCE   618 AA;  67383 MW;  0F14B3FEB36D37BA CRC64;
     MAGAMENAKK NLPKIRDEER EGRFGSVFGV SGPVVIAENM IGSQMYELVR VGHDELVGEI
     IRIDADKVTI QVYEETSGVS VGDPVLSTGK PLSVELGPGL MENIYDGIQR PLEGIMKKSQ
     GIYIPRGINT QALNRELQWD FKPTNLKVGD HISGGDIFGS VFENTLLTDH KIMLGPRARG
     TITSIAEAGS YNVDDIVLEV DFQGQKSKHS LMQLWPVRAP RPTTEKLVAN QPLLTGQRVL
     DTLFPCIQGG TTAIPGAFGC GKTVISQALS KFSNSDIITY VGCGERGNEM AEVLAEFPEL
     TLTRDGKEQP IMKRTTLVAN TSNMPVAARE ASIYTGITLS EYFRDQGYNV AMMADSTSRW
     AEALREISGR LAEMPADSGY PAYLGAKLAS FYERAGKVTC LGSPERTGSV SIVGAVSPPG
     GDFSDPVTSS TLGIVGAFWG LDKKLAQRKH FPSVNWDASY SNYVQALEGH YEKNSPGFIK
     LRSTAKDLLQ QDTSLAEIVQ LVGKSALGEN DKVTLEVANI VKNDFLAQNG ISAWDQYCPF
     YKSAGMLKNL VDFYDKAQAA INSNPDMTWA KIRDHSGDVI HGLTQMKFLH PGDGEESVQS
     ELDKLNQQIE QNFQTLSD
//
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