ID U9T1P6_RHIID Unreviewed; 506 AA.
AC U9T1P6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Vacuolar proton pump subunit B {ECO:0000256|RuleBase:RU366021};
DE Short=V-ATPase subunit B {ECO:0000256|RuleBase:RU366021};
DE AltName: Full=Vacuolar proton pump subunit B {ECO:0000256|RuleBase:RU366021};
GN ORFNames=GLOIN_2v1578130 {ECO:0000313|EMBL:POG74152.1},
GN GLOINDRAFT_334467 {ECO:0000313|EMBL:ERZ97305.1};
OS Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
OS (Arbuscular mycorrhizal fungus) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=747089 {ECO:0000313|EMBL:ERZ97305.1};
RN [1] {ECO:0000313|EMBL:POG74152.1, ECO:0000313|Proteomes:UP000018888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 181602 / DAOM 197198 / MUCL 43194
RC {ECO:0000313|Proteomes:UP000018888}, and DAOM 197198
RC {ECO:0000313|EMBL:POG74152.1};
RX PubMed=24277808; DOI=10.1073/pnas.1313452110;
RA Tisserant E., Malbreil M., Kuo A., Kohler A., Symeonidi A., Balestrini R.,
RA Charron P., Duensing N., Frei Dit Frey N., Gianinazzi-Pearson V.,
RA Gilbert L.B., Handa Y., Herr J.R., Hijri M., Koul R., Kawaguchi M.,
RA Krajinski F., Lammers P.J., Masclaux F.G., Murat C., Morin E.,
RA Ndikumana S., Pagni M., Petitpierre D., Requena N., Rosikiewicz P.,
RA Riley R., Saito K., San Clemente H., Shapiro H., van Tuinen D., Becard G.,
RA Bonfante P., Paszkowski U., Shachar-Hill Y.Y., Tuskan G.A., Young P.W.,
RA Sanders I.R., Henrissat B., Rensing S.A., Grigoriev I.V., Corradi N.,
RA Roux C., Martin F.;
RT "Genome of an arbuscular mycorrhizal fungus provides insight into the
RT oldest plant symbiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20117-20122(2013).
RN [2] {ECO:0000313|EMBL:ERZ97305.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DAOM 197198 {ECO:0000313|EMBL:ERZ97305.1};
RG DOE Joint Genome Institute;
RA Tisserant E., Malbreil M., Kuo A., Kohler A., Symeonidi A., Balestrini R.,
RA Charron P., Duensing N., Frei-dit-Frey N., Gianinazzi-Pearson V.,
RA Gilbert B., Handa Y., Hijri M., Kaul R., Kawaguchi M., Krajinski F.,
RA Lammers P., Lapierre D., Masclaux F.G., Murat C., Morin E., Ndikumana S.,
RA Pagni M., Petitpierre D., Requena N., Rosikiewicz P., Riley R., Saito K.,
RA San Clemente H., Shapiro H., van Tuinen D., Becard G., Bonfante P.,
RA Paszkowski U., Shachar-Hill Y., Young J.P., Sanders I.R., Henrissat B.,
RA Rensing S.A., Grigoriev I.V., Corradi N., Roux C., Martin F.;
RT "The genome of an arbuscular mycorrhizal fungus provides insights into the
RT evolution of the oldest plant symbiosis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:POG74152.1, ECO:0000313|Proteomes:UP000018888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 181602 / DAOM 197198 / MUCL 43194
RC {ECO:0000313|Proteomes:UP000018888}, and DAOM 197198
RC {ECO:0000313|EMBL:POG74152.1};
RX PubMed=29355972;
RA Chen E.C.H., Morin E., Beaudet D., Noel J., Yildirir G., Ndikumana S.,
RA Charron P., St-Onge C., Giorgi J., Kruger M., Marton T., Ropars J.,
RA Grigoriev I.V., Hainaut M., Henrissat B., Roux C., Martin F., Corradi N.;
RT "High intraspecific genome diversity in the model arbuscular mycorrhizal
RT symbiont Rhizophagus irregularis.";
RL New Phytol. 0:0-0(2018).
CC -!- FUNCTION: Non-catalytic subunit of the V1 complex of vacuolar(H+)-
CC ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral
CC complex (V1) that hydrolyzes ATP and a membrane integral complex (V0)
CC that translocates protons. V-ATPase is responsible for acidifying and
CC maintaining the pH of intracellular compartments.
CC {ECO:0000256|RuleBase:RU366021}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex attached to an integral membrane V0 proton pore
CC complex. {ECO:0000256|RuleBase:RU366021}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|RuleBase:RU366021}.
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DR EMBL; KI299727; ERZ97305.1; -; Genomic_DNA.
DR EMBL; AUPC02000074; POG74152.1; -; Genomic_DNA.
DR AlphaFoldDB; U9T1P6; -.
DR STRING; 747089.U9T1P6; -.
DR VEuPathDB; FungiDB:GLOIN_2v1578130; -.
DR eggNOG; KOG1351; Eukaryota.
DR HOGENOM; CLU_022916_3_0_1; -.
DR OrthoDB; 5473721at2759; -.
DR Proteomes; UP000018888; 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:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR CDD; cd18112; ATP-synt_V_A-type_beta_C; 1.
DR CDD; cd18118; ATP-synt_V_A-type_beta_N; 1.
DR CDD; cd01135; V_A-ATPase_B; 1.
DR Gene3D; 3.40.50.12240; -; 1.
DR HAMAP; MF_00310; ATP_synth_B_arch; 1.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR005723; ATPase_V1-cplx_bsu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022879; V-ATPase_su_B/beta.
DR NCBIfam; TIGR01040; V-ATPase_V1_B; 1.
DR PANTHER; PTHR43389; V-TYPE PROTON ATPASE SUBUNIT B; 1.
DR PANTHER; PTHR43389:SF4; V-TYPE PROTON ATPASE SUBUNIT B; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|RuleBase:RU366021};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU366021};
KW Reference proteome {ECO:0000313|Proteomes:UP000018888};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366021}.
FT DOMAIN 29..95
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 152..380
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 506 AA; 56521 MW; 09B9EFA67EF369E8 CRC64;
MDENQAFQIN AAAVTRNYSV TPRIDYRTVA SINGPLVVLD NVKFPKYAEI VNLTLPDGSR
RAGQVLEVQG KRAVVQVFEG TSGVDAKATH VEFTGDTLKI PVSEDMLGRI FNGSGKAIDK
GPKVFAEEFL DINGSPINPF SRIYPEEMIQ TGISAIDTMN SIARGQKIPI FSAAGLPHNE
IAAQICRQAG LVKKIADKGI YDDHEDNFSI VFAAMGVNME TARFFKQDFE ENGSIERVTL
FLNLANDPTI ERIVTPRLAL TTAEYYAYQL EKHVLVILTD MSSYADALRE VSAAREEVPG
RRGYPGYMYT DLSTIYERAG RVEGRNGSIT QIPILTMPND DITHPIPDLT GYITEGQIFV
DRQLHNRQIY PPINVLPSLS RLMKSAIGEG MTRKDHGDVS NQLYAKYAIG RDAAAMKAVV
GEEALNQEDK LSLEFLEKFE KTYISQGAYE SRTIYESLDH AWSILRIFPK EMLNRIPQKV
LQEFYQRDRK AKATQKNKAV VDTTEA
//
