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Database: UniProt
Entry: G2YPF4_BOTF4
LinkDB: G2YPF4_BOTF4
Original site: G2YPF4_BOTF4 
ID   G2YPF4_BOTF4            Unreviewed;       371 AA.
AC   G2YPF4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   25-APR-2018, entry version 18.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=BofuT4_P135470.1 {ECO:0000313|EMBL:CCD53502.1};
OS   Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD53502.1, ECO:0000313|Proteomes:UP000008177};
RN   [1] {ECO:0000313|Proteomes:UP000008177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P.,
RA   Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S.,
RA   Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M.,
RA   Pradier J.-M., Quevillon E., Sharon A., Simon A., ten Have A.,
RA   Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V.,
RA   Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z.,
RA   Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C.,
RA   Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S.,
RA   Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M.,
RA   Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C.,
RA   Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H.,
RA   Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C.,
RA   Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(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; FQ790347; CCD53502.1; -; Genomic_DNA.
DR   EnsemblFungi; CCD53502; CCD53502; BofuT4_P135470.1.
DR   InParanoid; G2YPF4; -.
DR   OrthoDB; EOG092C0YCY; -.
DR   Proteomes; UP000008177; Unplaced contigs.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0015078; F:proton 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:UP000008177};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU361189};
KW   Ion transport {ECO:0000256|RuleBase:RU361189};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008177};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   COILED      101    128       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   371 AA;  42301 MW;  899DDF03D7CA0D40 CRC64;
     MAPSQDTMFR SADMSLVQLY IANEIGREIV NALGELGQIQ FRDLNSDVTA FQRTFTQEIR
     RLDNVERQLR YFHTQMDKAG IPLRKLDLDI ETLAAPSATE IDELSDRSQS LEQRIASLND
     SYETLKKREV ELTEWRWVLR EAGSFFDRAH GNVDEIRAST DDDDAPLLQD IEQSHQNGDA
     ERSFSGMNIG FVSGVIPRDR IAAFERILWR TLRGNLYMNQ SEISEPIVDP TNNEAIDKNV
     FVIFAHGKEL IAKIRKISES LGADLYSVDE NSDLRRDQIH EVNTRLSDLG SVLRNTKQTL
     DAELTQIARS LAAWMVIIKK EKAVYQTLNL FSYDHARKTL IAEAWCPSNS LPLIKSTLHD
     DKQNSSDLPE D
//
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