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Database: UniProt
Entry: A0A074RXQ6_9AGAM
LinkDB: A0A074RXQ6_9AGAM
Original site: A0A074RXQ6_9AGAM 
ID   A0A074RXQ6_9AGAM        Unreviewed;       617 AA.
AC   A0A074RXQ6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=V565_054030 {ECO:0000313|EMBL:KEP51876.1};
OS   Rhizoctonia solani 123E.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX   NCBI_TaxID=1423351 {ECO:0000313|EMBL:KEP51876.1, ECO:0000313|Proteomes:UP000027456};
RN   [1] {ECO:0000313|EMBL:KEP51876.1, ECO:0000313|Proteomes:UP000027456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=123E {ECO:0000313|EMBL:KEP51876.1,
RC   ECO:0000313|Proteomes:UP000027456};
RA   Cubeta M., Pakala S., Fedorova N., Thomas E., Dean R., Jabaji S., Neate S.,
RA   Toda T., Tavantzis S., Vilgalys R., Bharathan N., Pakala S., Losada L.S.,
RA   Zafar N., Nierman W.;
RL   Submitted (DEC-2013) 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   -!- 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEP51876.1}.
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DR   EMBL; AZST01000137; KEP51876.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074RXQ6; -.
DR   STRING; 1423351.A0A074RXQ6; -.
DR   HOGENOM; CLU_008162_3_1_1; -.
DR   OrthoDB; 5473187at2759; -.
DR   Proteomes; UP000027456; 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:UP000027456};
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          106..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   617 AA;  67744 MW;  6520CD0199146CC3 CRC64;
     MAGALQNAKR DLPKIRDEDR ESRYGQVFGV SGPVVIAENM AGSAMYELVR VGHDELVGEV
     IRIDADKTTI QVYEETSGVT VGDPVLRTGK PLSVELGPGL MENIVDGIQR PLRAIQESSK
     SIYIPRGINT DALDRNIKWD FTPGQFKVGD HISGGDIFGS VYENSLVDNH KIMLSPRALG
     TITSIAEKGS YTVEDTVLEV EFDGKKTQHN MMQLWPVRAP RPTAAKLTAD YPLFTGQRVL
     DSLFPCVQGG TTAIPGAFGA GKTVISQALS KFSNSNIIVY VGCGERGNEM AEVLMEFPEL
     TLDVGDRQEP IMKRTTLVAN TSNMPVAARE ASIYTGITLA EYWRDQGSNV AMMADSTSRW
     AEALREISGR LAEMPADSGY PAYLSTKLAS FYERAGKVTC LGNPQREGTV SIVGAVSPPG
     GDFSDPVTAA TLSIVQVFWG LDKKLAQRKH FPSVNWNVSY SKYIQVLEPH YQSTDPGFVS
     SRNKTKEILQ KEDDLAEIVQ LVGKSALGEA DKVTLEVARM LKDDFLQQNG MSEYDRYCPF
     YKTSLMLKNF VAFHDSAVAA VTKGELTFNK VKEATSDIIF KLSQMKFESP SQGQESVTKK
     LEALNTEIIE KFRSIGE
//
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