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Database: UniProt
Entry: I2JZW5_DEKBR
LinkDB: I2JZW5_DEKBR
Original site: I2JZW5_DEKBR 
ID   I2JZW5_DEKBR            Unreviewed;       849 AA.
AC   I2JZW5;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 2.
DT   05-JUL-2017, entry version 15.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=AWRI1499_1559 {ECO:0000313|EMBL:EIF48517.1};
OS   Brettanomyces bruxellensis AWRI1499.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Pichiaceae; Brettanomyces.
OX   NCBI_TaxID=1124627 {ECO:0000313|EMBL:EIF48517.1, ECO:0000313|Proteomes:UP000004997};
RN   [1] {ECO:0000313|EMBL:EIF48517.1, ECO:0000313|Proteomes:UP000004997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1499 {ECO:0000313|EMBL:EIF48517.1,
RC   ECO:0000313|Proteomes:UP000004997};
RX   PubMed=22470482; DOI=10.1371/journal.pone.0033840;
RA   Curtin C.D., Borneman A.R., Chambers P.J., Pretorius I.S.;
RT   "De-Novo Assembly and Analysis of the Heterozygous Triploid Genome of
RT   the Wine Spoilage Yeast Dekkera bruxellensis AWRI1499.";
RL   PLoS ONE 7:E33840-E33840(2012).
CC   -!- FUNCTION: Essential component of the vacuolar proton pump (V-
CC       ATPase), a multimeric enzyme that catalyzes the translocation of
CC       protons across the membranes. Required for assembly and activity
CC       of the V-ATPase. {ECO:0000256|RuleBase:RU361189}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000256|RuleBase:RU361189}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EIF48517.1}.
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DR   EMBL; AHIQ01000086; EIF48517.1; -; Genomic_DNA.
DR   EnsemblFungi; EIF48517; EIF48517; AWRI1499_1559.
DR   Proteomes; UP000004997; Unassembled WGS sequence.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:EnsemblFungi.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:EnsemblFungi.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:EnsemblFungi.
DR   GO; GO:0016049; P:cell growth; IEA:EnsemblFungi.
DR   GO; GO:0043623; P:cellular protein complex assembly; IEA:EnsemblFungi.
DR   GO; GO:0006797; P:polyphosphate metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0007035; P:vacuolar acidification; IEA:EnsemblFungi.
DR   InterPro; IPR002490; V-ATPase_116kDa_su.
DR   InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR   PANTHER; PTHR11629; PTHR11629; 1.
DR   Pfam; PF01496; V_ATPase_I; 1.
DR   PIRSF; PIRSF001293; ATP6V0A1; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000004997};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU361189};
KW   Ion transport {ECO:0000256|RuleBase:RU361189};
KW   Membrane {ECO:0000256|RuleBase:RU361189};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004997};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    435    458       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    478    497       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    557    579       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    591    612       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    653    673       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    754    777       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    783    806       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   COILED      114    142       {ECO:0000256|SAM:Coils}.
FT   UNSURE      715    715       I or L. {ECO:0000313|EMBL:EIF48517.1}.
SQ   SEQUENCE   849 AA;  96402 MW;  EAB9F62F540DD9BF CRC64;
     MAAKKEEAMF RSAEMSMVQL YIPAEIGRET LFSLGRLGLV EFRDLNKKVN EFQRSFVDEI
     RRLDNVERQY RFLXSAMDKR GIIVPEILVE DYDVKHREIM STSQLDEACS NAXLLEDRIT
     ELSEASEDML KKQTDLKQYQ QVLNRTDAYF DRSYSADLMG LSGNDXNLVD GDVIGESQLH
     SVSNFVTGVI SRAKIPILEK ILWRVLRGNL FMKSSEIDQK IFDXGSKAFI DKNCFVIFSH
     GEXVLSRIRK ICESLGADLY FVDPDHKKRQ DQKVDIRHKL XDVTTVLEGT DRTLETELRV
     VAPELDSWWK QIKLEKSVYK AMNDCYYDLN RKCLIAEGWV PNAEISVIQR SLDAISARYS
     XNNSLRRTAS QSAGQADSDN SIPIIMNTIE TNRKPPTYFK TNKFTEAFQA LCDSYGTATY
     REVNAGLPTI ATFPFIFAIM FGDLGHGFLM FLAALVLVLK EKEISRIKRD EIFDMAYYGR
     YMVLMMGLCS MYTGFIYNDA FSMSLSIFKS GWSWPSSWKL GESIVGHQTG VYPIGFDPIW
     HGAENSLLFA NSYKMKLSIL MGFIHMSYSY VFSLVNAIYF KRPIDIIGKF IPGFIFMHGI
     FGYLCVCIVY KWSVDWIGIX KPAPSLLNML INMFLSPGTI DDQLYPGQAS VQVTLLLLAL
     ICVPCLLLIK PLWYKXVQDR KLSAYHSISS SSEAAEGTPN TSSTQNENLL ANLNLDDDEP
     VEXEAFGDVM INQVIYTIEF CLNCVSHTAS YLRLWALSLA HSQLSSVLWS MTIGASFKFS
     GLFGAIFIFI MFALWFILTV CILVVMEGTS AMLHALRLHW VEAMSKYFEG EGVPYKPFSF
     ISVLTPDQA
//
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