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Database: UniProt
Entry: G8JNM1_ERECY
LinkDB: G8JNM1_ERECY
Original site: G8JNM1_ERECY 
ID   G8JNM1_ERECY            Unreviewed;       836 AA.
AC   G8JNM1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   05-JUL-2017, entry version 25.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   OrderedLocusNames=Ecym_2355 {ECO:0000313|EMBL:AET38089.1};
OS   Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166
OS   / NRRL Y-17582) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=931890 {ECO:0000313|EMBL:AET38089.1, ECO:0000313|Proteomes:UP000006790};
RN   [1] {ECO:0000313|Proteomes:UP000006790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582
RC   {ECO:0000313|Proteomes:UP000006790};
RX   DOI=10.1534/g3.111.001032;
RA   Wendland J., Walther A.;
RT   "Genome evolution in the Eremothecium clade of the Saccharomyces
RT   complex revealed by comparative genomics.";
RL   G3 (Bethesda) 1:539-548(2011).
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}.
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DR   EMBL; CP002498; AET38089.1; -; Genomic_DNA.
DR   RefSeq; XP_003644906.1; XM_003644858.1.
DR   STRING; 931890.XP_003644906.1; -.
DR   EnsemblFungi; AET38089; AET38089; Ecym_2355.
DR   GeneID; 11470629; -.
DR   KEGG; erc:Ecym_2355; -.
DR   eggNOG; KOG2189; Eukaryota.
DR   eggNOG; COG1269; LUCA.
DR   InParanoid; G8JNM1; -.
DR   KO; K02154; -.
DR   OrthoDB; EOG092C0YCY; -.
DR   Proteomes; UP000006790; Chromosome 2.
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   Complete proteome {ECO:0000313|Proteomes:UP000006790};
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:UP000006790};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    428    452       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    473    490       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    550    572       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    579    605       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    646    669       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    742    761       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    773    796       Helical. {ECO:0000256|RuleBase:RU361189}.
SQ   SEQUENCE   836 AA;  95777 MW;  901CA0C14F097F86 CRC64;
     MTEKQEGVFR SVDMVLTEMF IPQEIARDAV YTLGDTGLVQ FRDLNRSVQK FQRTFVTELQ
     RLDNVERQYR YFNSLLEKYK IPIYVENLDE EEEYETLVCE NGGLTPLSRF SMPPSTSVID
     DHVENANLLE ERFVQLVEAS EQLESQKTNM EEFRYLLIAV ERFFMSDGSD FHNFGDIENE
     INEDELESGT LAPSVSYLTG VISHEKIITL EKILWRVLRG NLFFKHIELP DPLYDPKLKE
     KVQKDAFIVF THGDLILERV KKIAESLDAN LYQVEHSSEP RSKQLSEVNG RLNDLYKVLE
     TTAVTLEAGL YSISKELEGW NKQICKEKMV YQTLNLFAYD SNRKTLTAEG WIPKDELETL
     QIELKTLTST LGSDAPAIVN VLHTNKTPPT FHRTNKFTKA FQDLCDCYAI PSFQEVNPGL
     ATIVTFPFMF AIMFGDLGHG MLMVMVALVF VYKEAAIGKM KRDEILDMAY SGRYVLLLMG
     SFSIYTGLLY NDMFSISLTV FKSGWKWPAS WEVGETIEAT QVGVYSMGID SAWHGAENAL
     LFSNSLKMKL SIIIGFSHML YSYGFALINA LYFNDMVEIF CNFIPGLLFM CSIFGYLVVC
     IIYKWSIDWV KNSKPAPGLL NMLINMFLAP GNIQEQLYVG QAQFQVFLLL VALVCIPWLL
     LAKPLYFYYN QKKHLHQPLP SSDYDLADVT VEEHLPEDYD LSTDDQNPEG SHGENLGDVI
     IHQVIHTIEW CLNCVSHTAS YLRLWALSLA HAQLSTVLWS MTLQRGFEMD GPFGIFMIVF
     LFAMWFVLTC AILVIMEGTS AMLHSLRLHW VESMSKFFKG EGTLYEPFVF SYNGFE
//
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