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Database: UniProt
Entry: A0A094DGP1_9PEZI
LinkDB: A0A094DGP1_9PEZI
Original site: A0A094DGP1_9PEZI 
ID   A0A094DGP1_9PEZI        Unreviewed;       712 AA.
AC   A0A094DGP1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=V496_06046 {ECO:0000313|EMBL:KFY58650.1};
OS   Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY58650.1, ECO:0000313|Proteomes:UP000029302};
RN   [1] {ECO:0000313|EMBL:KFY58650.1, ECO:0000313|Proteomes:UP000029302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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:KFY58650.1}.
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DR   EMBL; JPJY01001088; KFY58650.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094DGP1; -.
DR   STRING; 1420909.A0A094DGP1; -.
DR   HOGENOM; CLU_008162_3_1_1; -.
DR   OrthoDB; 5473187at2759; -.
DR   Proteomes; UP000029302; 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:UP000029302};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          123..185
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          201..322
FT                   /note="ATPsynthase alpha/beta subunit N-terminal extension"
FT                   /evidence="ECO:0000259|Pfam:PF16886"
FT   DOMAIN          331..556
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   REGION          58..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   712 AA;  78554 MW;  B3C537AAC4D81EA9 CRC64;
     MHNVGFTPRP RLRGRPSFYD LIKSSAATTP RPDLAVDSLP GVNPRLHREL HDLIASTIPL
     PTSPTHQRHR SLPQSTSSIS EEVAPLNEPI TLPDNDTSMG PKKSEKKTEA ARDVESEEQY
     GSIYSVSGPV VVAENMLGVA MYELVKVGHD NLIGEVIRIE ADRATIQVYE ETAGVTVGDP
     AIRTGKPLSV ELGPGLMETI YDGIQRPLKS IAELSNSIYI PRGISAPALD RKKLWEFKPL
     MKVGDHITGG DIFGTVYENS LLDDHKILLP PRARGTITRI SEAGKYTVDA KILEIEFNGK
     KSEHMMMHTW PVRVARPTTE KLAADKPFVV GQRVLDALFP SVQGGTVAIP GAFGCGKTVI
     SQSVSKFSNS DIIIYVGCGE RGNEMAEVLM DFPELSIDIN GRKEPIMKRT TLIANTSNMP
     VAAREASIYT GITVAEYFRD QGKDVAMMAD STSRWAEALR ELSGRLGEMP ADQGFPAYLG
     AKLASFYERA GKVQALGNPA REGSVSIVGA VSPPGGDFSD PVTSSTLGIV QVFWGLDKKL
     AQRKHFPSIN TSVSYSRYTA VLDKYYEKDF PDFPRLRERI KTLLSDSEEL DQVVQLVGKS
     ALSDPNKITL DVAQLLKEDF LQQNGYSDYD QFCPIWKTEW MMKAMMGFHD EAQKVISQGQ
     SWNKVREATS DLQSQLRSMK FELPSDGEEV IVAKYEKLIS DMNEKFASVV DE
//
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