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Database: UniProt
Entry: G4ZFV9_PHYSP
LinkDB: G4ZFV9_PHYSP
Original site: G4ZFV9_PHYSP 
ID   G4ZFV9_PHYSP            Unreviewed;       605 AA.
AC   G4ZFV9;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=H(+)-transporting two-sector ATPase {ECO:0000256|ARBA:ARBA00012473};
DE            EC=7.1.2.2 {ECO:0000256|ARBA:ARBA00012473};
GN   ORFNames=PHYSODRAFT_300022 {ECO:0000313|EMBL:EGZ16643.1};
OS   Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS   (Phytophthora megasperma f. sp. glycines).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ16643.1, ECO:0000313|Proteomes:UP000002640};
RN   [1] {ECO:0000313|EMBL:EGZ16643.1, ECO:0000313|Proteomes:UP000002640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P6497 {ECO:0000313|EMBL:EGZ16643.1,
RC   ECO:0000313|Proteomes:UP000002640};
RX   PubMed=16946064; DOI=10.1126/science.1128796;
RA   Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA   Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA   Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA   Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA   Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA   McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA   Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA   Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA   Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA   Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT   "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT   of pathogenesis.";
RL   Science 313:1261-1266(2006).
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936}.
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DR   EMBL; JH159154; EGZ16643.1; -; Genomic_DNA.
DR   RefSeq; XP_009525701.1; XM_009527406.1.
DR   AlphaFoldDB; G4ZFV9; -.
DR   STRING; 1094619.G4ZFV9; -.
DR   EnsemblProtists; EGZ16643; EGZ16643; PHYSODRAFT_300022.
DR   GeneID; 20641810; -.
DR   KEGG; psoj:PHYSODRAFT_300022; -.
DR   InParanoid; G4ZFV9; -.
DR   OMA; RIVKTFW; -.
DR   Proteomes; UP000002640; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002640};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          11..64
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          82..211
FT                   /note="ATPsynthase alpha/beta subunit N-terminal extension"
FT                   /evidence="ECO:0000259|Pfam:PF16886"
FT   DOMAIN          220..444
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
SQ   SEQUENCE   605 AA;  66581 MW;  B1CB3D94D6CCE125 CRC64;
     MELIALNCPA VVIAENMHGA AMYELVRVGH DKLVGEIIKL ENTNASIQVY EDTSGLTVGD
     PVERRKQPLS VELGPGIVDN IFDGIQRPLH AISDLAKDVY IPRGVDVASL NADKKWRYKP
     VNFREGDPIS GGDIFGLVHE NDILHSHKIM CPPNVFGTVV KIYGAGTDNN ESFTLRDTVL
     EVRDDTTGVT HKLGLSHMWP VRKPRPVAEK LAGNVALTTG QRIIDALFPS VLGGTCAVPG
     AFGCGKTVIS QALSKHSNSD AIVYVGCGER GNEMAEVLND FPELTMTIND REVPIMKRTT
     LVANTSNMPV AAREASIYTG ITLAEYFRDQ GMNVSMMADS TSRWAEALRE ISGRLGEMPA
     DSGYPAYLGA RLAAFYERAG RVACLGSPKR EGSVTVVGAV SPPGGDFSDP VTAATLSIVQ
     VFWGLDKKLA QRKHFPSVNW LISYTKYMRV LEPFFNKIDP EYSTLRTKCQ EILQKEDNLT
     EIVQLVGKES LSEDQKVIME VAKIIREDFL QQNAFSDYDF TCPLVKSVGM LRSIILFYNL
     SQKAIADSPP DAKVTWAQIK TSMNPVLQKI IQTKFQLPKQ PEAELKAFFS GLDEEVEQAF
     QTLSD
//
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