GenomeNet

Database: UniProt
Entry: A0A0C4F2P1_PUCT1
LinkDB: A0A0C4F2P1_PUCT1
Original site: A0A0C4F2P1_PUCT1 
ID   A0A0C4F2P1_PUCT1        Unreviewed;       514 AA.
AC   A0A0C4F2P1;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
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=PTTG_07362 {ECO:0000313|EMBL:OAW00033.1};
OS   Puccinia triticina (isolate 1-1 / race 1 (BBBD)) (Brown leaf rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=630390 {ECO:0000313|EnsemblFungi:PTTG_07362P0, ECO:0000313|Proteomes:UP000005240};
RN   [1] {ECO:0000313|Proteomes:UP000005240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 1-1 / race 1 (BBBD)
RC   {ECO:0000313|Proteomes:UP000005240};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Fellers J., Bakkeren G., Szabo L., Young S., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OAW00033.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAW00033.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA   Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblFungi:PTTG_07362P0}
RP   IDENTIFICATION.
RC   STRAIN=isolate 1-1 / race 1 (BBBD)
RC   {ECO:0000313|EnsemblFungi:PTTG_07362P0};
RG   EnsemblFungi;
RL   Submitted (JUN-2015) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:OAW00033.1, ECO:0000313|Proteomes:UP000005240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAW00033.1}, and Isolate 1-1
RC   / race 1 (BBBD) {ECO:0000313|Proteomes:UP000005240};
RA   Cuomo C.A., Bakkeren G., Szabo L., Khalil H., Joly D., Goldberg J.,
RA   Young S., Zeng Q., Fellers J.;
RT   "Comparative analysis highlights variable genome content of wheat rusts and
RT   divergence of the mating loci.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EnsemblFungi:PTTG_07362P0}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=isolate 1-1 / race 1 (BBBD)
RC   {ECO:0000313|EnsemblFungi:PTTG_07362P0};
RX   PubMed=27913634; DOI=10.1534/g3.116.032797;
RA   Cuomo C.A., Bakkeren G., Khalil H.B., Panwar V., Joly D., Linning R.,
RA   Sakthikumar S., Song X., Adiconis X., Fan L., Goldberg J.M., Levin J.Z.,
RA   Young S., Zeng Q., Anikster Y., Bruce M., Wang M., Yin C., McCallum B.,
RA   Szabo L.J., Hulbert S., Chen X., Fellers J.P.;
RT   "Comparative analysis highlights variable genome content of wheat rusts and
RT   divergence of the mating loci.";
RL   G3 (Bethesda) 7:361-376(2017).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ADAS01008790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADAS02000001; OAW00033.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C4F2P1; -.
DR   STRING; 630390.A0A0C4F2P1; -.
DR   EnsemblFungi; PTTG_07362T0; PTTG_07362P0; PTTG_07362.
DR   VEuPathDB; FungiDB:PTTG_07362; -.
DR   OMA; GFKIKPR; -.
DR   OrthoDB; 5473721at2759; -.
DR   Proteomes; UP000005240; 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:UP000005240};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366021}.
FT   DOMAIN          33..99
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          156..392
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
SQ   SEQUENCE   514 AA;  57110 MW;  C6AB608B13A6C83D CRC64;
     MANDPRISQT EAFKINQAAV TRNFKPRIDY RTVSAVNGPL VVLDNVHFPS YNEIVNLTLP
     DGTQRGGQVL EVSGKKAIVQ VFEGTSGIDV RATHVEFSGS SMKLPVSEDM LGRIFNGSGQ
     PIDKGPKVFA EDYLDINGSP INPYSRIYPE EMIQTGISTI DAMNSIARGQ KIPIFSAAGL
     PHNEIAAQIC RQAGLVKKGG VSPGQGKPTK SVHDDHEDNF SIVFAAMGVN METARFFRQD
     FEENGSLDRV TLFLNLANDP TIERIITPRL ALTTAEYFAY QVEKHVLVIL TDMSSYADAL
     REVSAAREEV PGRRGYPGYM YTDLSTIYER AGRVEGRNGS ITQIPILTMP NDDITHPIPD
     LTGYITEGQI FVDRLLYNKQ IYPPINVLPS LSRLMKSAVG EGLTRKDHSD VSNQLYAKYA
     IGKDAAAMKA VVGEEALSSE EKLALEFLDK FESTFVTQGN NENRTIFDSL DLAWSLLRIF
     PREQLNRIPK KILDEWYSRR PANNTNQKNN DPKP
//
DBGET integrated database retrieval system