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Database: UniProt
Entry: I3EIJ6_NEMP3
LinkDB: I3EIJ6_NEMP3
Original site: I3EIJ6_NEMP3 
ID   I3EIJ6_NEMP3            Unreviewed;       500 AA.
AC   I3EIJ6;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
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=NEQG_00862 {ECO:0000313|EMBL:EIJ89043.1};
OS   Nematocida parisii (strain ERTm3) (Nematode killer fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nematocida.
OX   NCBI_TaxID=935791 {ECO:0000313|EMBL:EIJ89043.1, ECO:0000313|Proteomes:UP000002872};
RN   [1] {ECO:0000313|EMBL:EIJ89043.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ERTm3 {ECO:0000313|EMBL:EIJ89043.1};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cuomo C., Troemel E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.,
RA   Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Nematocida parisii strain ERTm3.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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; GL870877; EIJ89043.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3EIJ6; -.
DR   STRING; 935791.I3EIJ6; -.
DR   EnsemblFungi; EIJ89043; EIJ89043; NEQG_00862.
DR   VEuPathDB; MicrosporidiaDB:NEQG_00862; -.
DR   HOGENOM; CLU_022916_0_0_1; -.
DR   InParanoid; I3EIJ6; -.
DR   OMA; GFKIKPR; -.
DR   Proteomes; UP000002872; 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:UP000002872};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366021}.
FT   DOMAIN          28..94
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          151..376
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
SQ   SEQUENCE   500 AA;  55765 MW;  4DC4782FB0FEEDD0 CRC64;
     MNNYEVFSEH VRALNDSCIP PTTTYRTVSS VNGPLVIMDN VKSPKYSEIV HLTLPDGSRR
     TGQVLEVCGK KAIIQVFEGT SGIDTKHTCA EFTGETMKMA VSEDLLGRTF NSIGVPIDGG
     PKIVAEDYLD IQGQPINPYA RIYPEEMVQT GISAIDVMNS VARGQKIPIF SGAGLPHNEV
     AAQICRQAGL VNNKSTVDKS KDNFSIVFAA MGVNAETAQF FRNEFEQSGV LDRTILYLNL
     ANDPTIERII TPRFALTAAE YLAYTTGKHV LMIMTDMSSY ADALREVSAA REEVPGRRGY
     PGYMYTDLST IYERAGRIAG IDGSITQIPI LTMPNDDITH PIPDLTGYIT EGQIYIDRSL
     HNRQIYPPIN VLPSLSRLMK SAIGENMTRD DHSDVSSQLY SKYAVGKEAL AMKSVVGEES
     LSTEDKLVIE FVENFEKEFI SQRKDENRTI SESLDLAWRL LRIFPKELLN RIPDNILNKY
     YTIKTTEEDN SHVSNEEKKE
//
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