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Database: UniProt
Entry: A0A0C9XIR7_9HOMO
LinkDB: A0A0C9XIR7_9HOMO
Original site: A0A0C9XIR7_9HOMO 
ID   A0A0C9XIR7_9HOMO        Unreviewed;       449 AA.
AC   A0A0C9XIR7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   08-JUN-2016, entry version 6.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=PISMIDRAFT_18895 {ECO:0000313|EMBL:KIK12225.1};
OS   Pisolithus microcarpus 441.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Boletales; Sclerodermatineae;
OC   Pisolithaceae; Pisolithus.
OX   NCBI_TaxID=765257 {ECO:0000313|EMBL:KIK12225.1, ECO:0000313|Proteomes:UP000054018};
RN   [1] {ECO:0000313|EMBL:KIK12225.1, ECO:0000313|Proteomes:UP000054018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=441 {ECO:0000313|EMBL:KIK12225.1,
RC   ECO:0000313|Proteomes:UP000054018};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
RA   Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA   Nordberg H.P., Cantor M.N., Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=441 {ECO:0000313|Proteomes:UP000054018};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal
RT   Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN834104; KIK12225.1; -; Genomic_DNA.
DR   EnsemblFungi; KIK12225; KIK12225; PISMIDRAFT_18895.
DR   Proteomes; UP000054018; Unassembled WGS sequence.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR002490; V-ATPase_116kDa_su.
DR   PANTHER; PTHR11629; PTHR11629; 1.
DR   Pfam; PF01496; V_ATPase_I; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054018};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU361189};
KW   Ion transport {ECO:0000256|RuleBase:RU361189};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054018};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   COILED      135    162       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   449 AA;  50324 MW;  8B63FCFE7AC6933F CRC64;
     MGWVQSKKTS SDLCQPGNTM LNPVSLHGVH GIPQVFSLEH DKVYVRDEGG IKTKEESVSE
     TDGVNLKAGM RVLGVSFTRM YSNSCVGDLQ YTREGGSHRI RTLVLSIPLT LGVLVHCSIE
     SAPLITVGPR AARTIDELDE VLGEHEARLL QMNESYKTLS ERTKELVEAR HVLRETAAET
     QQTEVRSSFN DSSTPLLQYD DRKTQHSSSL QFELEFVAGT IERSHIPTLE RVLWRLLRGN
     LYVNHTDIAE PFVDPVTSVE TRKNVFIIFA HGESVLAKIR KVAKSMGATL YPIDANADKC
     ADSLREVTAR LEDVQTVLYH TGLTRRSELM IIGENLSRWQ DVVCKEKAIY EMMNLFNYDV
     RRKTLVAKGW CPTRDLVVIQ AALRRVMEES GTNVVPILHE LPTNKTLPTF LGNGTPLKVR
     GESGRGCEET TPSHTKLQIE VEDAKCIRN
//
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