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Database: UniProt
Entry: A7F2P8_SCLS1
LinkDB: A7F2P8_SCLS1
Original site: A7F2P8_SCLS1 
ID   A7F2P8_SCLS1            Unreviewed;       854 AA.
AC   A7F2P8;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   22-NOV-2017, entry version 50.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=SS1G_12196 {ECO:0000313|EMBL:EDN95990.1};
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White
OS   mold) (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN95990.1, ECO:0000313|Proteomes:UP000001312};
RN   [1] {ECO:0000313|Proteomes:UP000001312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
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; CH476639; EDN95990.1; -; Genomic_DNA.
DR   RefSeq; XP_001587166.1; XM_001587116.1.
DR   STRING; 5180.EDN95990; -.
DR   EnsemblFungi; APA09398; APA09398; sscle_05g041680.
DR   EnsemblFungi; EDN95990; EDN95990; SS1G_12196.
DR   GeneID; 5483169; -.
DR   KEGG; ssl:SS1G_12196; -.
DR   EuPathDB; FungiDB:SS1G_12196; -.
DR   InParanoid; A7F2P8; -.
DR   KO; K02154; -.
DR   OMA; WTAYDAH; -.
DR   OrthoDB; EOG092C0YCY; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
DR   GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR   GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IBA:GO_Central.
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:UP000001312};
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:UP000001312};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    422    447       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    467    484       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    545    563       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    575    598       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    637    657       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    781    806       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   COILED      101    128       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   854 AA;  97395 MW;  4D8FF4453E38672E CRC64;
     MAPSQDTMFR SADMSMVQLY IANEIGREIV NALGELGQIQ FRDLNSDVTA FQRTFTQEIR
     RLDNVERQLR YFHSQMDKAG IPLRKLDLDV ETVAAPSATE IDELSDRSQS LEQRIASLND
     SYETLKKREV ELTEWRWVLR EAGSFFDRAH GNVDEIRAST DNDDAPLLQD VEQSHHNGDA
     ERSFSGMNIG FVSGVIPRDR IAAFERILWR TLRGNLYMNQ SEIAEPIIDP TNNEAINKNV
     FVIFAHGKEL IAKIRKISES LGADLYTVDE NSDLRRDQIH EVNTRLSDLG SVLRNTKQTL
     DAELTQIARS LAAWMVIIKK EKAVYQTLNL FSYDHARKTL IAEAWCPSNS LPLIKSTLHD
     VNNRAGLSVP SIINEIRTNK TPPTYQKTNR FTEGFQTIIN AYGTAKYQEV NPGLPTIVTF
     PFLFAVMFGD FGHGVIMVCA AAAMIYWEKS LKKVRDELFS MAFYGRYIML MMGIFSMYTG
     LIYNDVFSKS FSFFPSAWAW SEHYPDSIEA HLKEPNGYRY PFGLDWMWHD TENDLLFTNS
     YKMKLSILMG WCHMTYSLCL SYINARHFKT PIDIWGVFVP GMIFFQAIFG YLVFAIIYKW
     SIDWQGIGES PPGLLNMLIY MFLSPGTIDE QLYPGQGFVQ ICLVIIAVIQ VPIMLLLKPF
     YLRWEHNKAR GRGYRGIGET SRVSALDGDD DDDHTLDGRI SMNSDGEGVA MITQDIGDEE
     HEEFEFSEVM IHQVIHTIEF CLNCVSHTAS YLRLWALSLA HQQLSVVLWD MTLSIGLHMT
     GVAGVFMVVV TFFAWFFLTI AVLVIMEGTS AMLHSLRLHW VEAMSKHFMG DGIPFEPFSF
     KQMLEDDASA ADIS
//
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