ID G0W576_NAUDC Unreviewed; 505 AA.
AC G0W576;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 Name=NDAI0A08100 {ECO:0000313|EMBL:CCD22964.1};
GN OrderedLocusNames=NDAI_0A08100 {ECO:0000313|EMBL:CCD22964.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD22964.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD22964.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE580267; CCD22964.1; -; Genomic_DNA.
DR RefSeq; XP_003668207.1; XM_003668159.1.
DR AlphaFoldDB; G0W576; -.
DR STRING; 1071378.G0W576; -.
DR GeneID; 11494430; -.
DR KEGG; ndi:NDAI_0A08100; -.
DR eggNOG; KOG1351; Eukaryota.
DR HOGENOM; CLU_022916_3_0_1; -.
DR OMA; GFKIKPR; -.
DR OrthoDB; 5473721at2759; -.
DR Proteomes; UP000000689; Chromosome 1.
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:UP000000689};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366021}.
FT DOMAIN 33..97
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 154..380
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 505 AA; 56496 MW; 951D4259E66DA736 CRC64;
MVLSDKELFD INKKAVEQGF KIKPRLNYNT VNGVNGPLVI LEKVKFPRYN EIVNLTLPDG
SIRQGQVLEV RGDRAIVQVF EGTSGIDVKK TTVEFTGENL KIPVSEDTLG RIFDGSGRPI
DNGPKVFAED YLDINGSPIN PYARIYPEEM ISTGISAIDT MNSIARGQKI PIFSASGLPH
NEIAAQICRQ AGLVRPTKDV HDGHEENFSI VFAAMGVNLE TARFFKQDFE ENGSLERTSL
FLNLANDPTI ERIITPRLAL TTAEYLAYQT DRHVLTILTD MSSYADALRE VSAAREEVPG
RRGYPGYMYT DLSTIYERAG RVEGRNGSIT QIPILTMPND DITHPIPDLT GYITEGQISV
DRQLHNKGVY PPINVLPSLS RLMKSAIGEG MTRKDHGDVS NQLYAKYAIG RDAAAMKAVV
GEEALSIEDK LSLEFLEKFE KTFISQGAYE NRTVFESLDQ AWSLLRIYPK EMLNRISPKV
LDEFYDRARD EDEDDEEDPD SRPSK
//
