(data stored in SCRATCH zone)

SWISSPROT: Q6BMG5_DEBHA

ID   Q6BMG5_DEBHA            Unreviewed;       352 AA.
AC   Q6BMG5;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 74.
DE   RecName: Full=V-type proton ATPase subunit {ECO:0000256|PIRNR:PIRNR018497};
GN   OrderedLocusNames=DEHA2F05632g {ECO:0000313|EMBL:CAG88931.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88931.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88931.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Vacuolar ATPase is responsible for acidifying a variety
CC       of intracellular compartments in eukaryotic cells. The active
CC       enzyme consists of a catalytic V1 domain attached to an integral
CC       membrane V0 proton pore complex. This subunit is a non-integral
CC       membrane component of the membrane pore domain and is required for
CC       proper assembly of the V0 sector. Might be involved in the
CC       regulated assembly of V1 subunits onto the membrane sector or
CC       alternatively may prevent the passage of protons through V0 pores.
CC       {ECO:0000256|PIRNR:PIRNR018497}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a
CC       peripheral catalytic V1 complex (components A to H) attached to an
CC       integral membrane V0 proton pore complex.
CC       {ECO:0000256|PIRNR:PIRNR018497}.
CC   -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.
CC       {ECO:0000256|PIRNR:PIRNR018497}.
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DR   EMBL; CR382138; CAG88931.1; -; Genomic_DNA.
DR   RefSeq; XP_460606.1; XM_460606.1.
DR   STRING; 4959.XP_460606.1; -.
DR   EnsemblFungi; CAG88931; CAG88931; DEHA2F05632g.
DR   GeneID; 2903379; -.
DR   KEGG; dha:DEHA2F05632g; -.
DR   HOGENOM; HOG000199065; -.
DR   InParanoid; Q6BMG5; -.
DR   KO; K02146; -.
DR   OMA; FMDFITY; -.
DR   OrthoDB; 910004at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:EnsemblFungi.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0007034; P:vacuolar transport; IEA:EnsemblFungi.
DR   Gene3D; 1.20.1690.10; -; 2.
DR   InterPro; IPR036079; ATPase_su_C-like.
DR   InterPro; IPR002843; ATPase_V0-cplx_csu/dsu.
DR   InterPro; IPR016727; ATPase_V0-cplx_dsu.
DR   InterPro; IPR035067; V-type_ATPase_suC.
DR   PANTHER; PTHR11028; PTHR11028; 1.
DR   Pfam; PF01992; vATP-synt_AC39; 1.
DR   PIRSF; PIRSF018497; V-ATP_synth_D; 1.
DR   SUPFAM; SSF103486; SSF103486; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BMG5.
DR   SWISS-2DPAGE; Q6BMG5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Hydrogen ion transport {ECO:0000256|PIRNR:PIRNR018497};
KW   Ion transport {ECO:0000256|PIRNR:PIRNR018497};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Transport {ECO:0000256|PIRNR:PIRNR018497}.
SQ   SEQUENCE   352 AA;  40537 MW;  784C895A30C98740 CRC64;
     MEGIFFNVDY GYVEGVVRGY RSGLLGNNQY VNLTQCDNLE DLKLQLSATD YGNFLASHSG
     PLSTSIMQDN LSKKLFQQFQ YLKSQASGKL IRFLDFISYG YMIDNVSLMI TGTLHERDRS
     EILSKCHPLG WFDTLPTLSI ATDIESLYNT VLIDTPLAPF FKDCLTADDL DDLNIEIIRN
     RLYKNYLEAF VNFIEDEFTS PDKEIMTNLL NFEADKRVIN ISLNSLNNPD LTAENKLSLF
     PSYGRLYPTY HSKLSEIDDV EQLKAIVDSI GEYKDLFSEA PDSNSGGSKN LEDWFYLLEM
     QYCKNAFTQQ FTLSTIWAWL RSKEQEIRNI TWIAECIAQN QKNRIDNYIS VY
//

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