(data stored in ACNUC8465 zone)

SWISSPROT: Q6FJ33_CANGA

ID   Q6FJ33_CANGA            Unreviewed;       543 AA.
AC   Q6FJ33;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 100.
DE   RecName: Full=ATP synthase subunit alpha {ECO:0000256|RuleBase:RU003551};
GN   Name=ATP1 {ECO:0000313|CGD:CAL0137183};
GN   OrderedLocusNames=CAGL0M09581g {ECO:0000313|CGD:CAL0137183,
GN   ECO:0000313|EMBL:CAG62739.1};
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593 {ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG62739.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
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: Produces ATP from ADP in the presence of a proton
CC       gradient across the membrane. {ECO:0000256|RuleBase:RU003551}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|RuleBase:RU000339}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CR380959; CAG62739.1; -; Genomic_DNA.
DR   RefSeq; XP_449761.1; XM_449761.1.
DR   ProteinModelPortal; Q6FJ33; -.
DR   STRING; 284593.XP_449761.1; -.
DR   PRIDE; Q6FJ33; -.
DR   EnsemblFungi; CAG62739; CAG62739; CAGL0M09581g.
DR   KEGG; cgr:CAGL0M09581g; -.
DR   CGD; CAL0137183; ATP1.
DR   EuPathDB; FungiDB:CAGL0M09581g; -.
DR   eggNOG; KOG1353; Eukaryota.
DR   eggNOG; COG0056; LUCA.
DR   HOGENOM; HOG000130111; -.
DR   InParanoid; Q6FJ33; -.
DR   KO; K02132; -.
DR   OMA; GNAQIKS; -.
DR   OrthoDB; EOG092C1T32; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IEA:EnsemblFungi.
DR   GO; GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:EnsemblFungi.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:EnsemblFungi.
DR   CDD; cd01132; F1_ATPase_alpha; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR   InterPro; IPR023366; ATP_synth_asu-like.
DR   InterPro; IPR000793; ATP_synth_asu_C.
DR   InterPro; IPR033732; ATP_synth_F1_a.
DR   InterPro; IPR005294; ATP_synth_F1_asu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF00306; ATP-synt_ab_C; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00962; atpA; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FJ33.
DR   SWISS-2DPAGE; Q6FJ33.
KW   ATP synthesis {ECO:0000256|RuleBase:RU003551};
KW   ATP-binding {ECO:0000256|RuleBase:RU003551};
KW   CF(1) {ECO:0000256|RuleBase:RU003551};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU000339};
KW   Ion transport {ECO:0000256|RuleBase:RU000339};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003551};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   Transport {ECO:0000256|RuleBase:RU000339}.
FT   DOMAIN       62    127       ATP-synt_ab_N. {ECO:0000259|Pfam:
FT                                PF02874}.
FT   DOMAIN      184    407       ATP-synt_ab. {ECO:0000259|Pfam:PF00006}.
FT   DOMAIN      414    539       ATP-synt_ab_C. {ECO:0000259|Pfam:
FT                                PF00306}.
SQ   SEQUENCE   543 AA;  58521 MW;  74CCA76653419D22 CRC64;
     MLSRVVLARN ALRAVSRASR ASRGSVVRTS ARCYAAKAQP TEVSSILEEK IRGVSDEAQL
     NETGRVLAVG DGIARVFGLN NIQAEELVEF ASGVKGMALN LEPGQVGIVL FGSDRLVKEG
     EIVKRTGKIV DVPVGPGLLG RVVDALGNPI DGKGPIESVG TARAQVKAPG ILPRRSVHEP
     VQTGLKAVDA LVPIGRGQRE LIIGDRQTGK TAVALDTILN QKRWNDGNDE SKKLYCVYVA
     IGQKRSTVAQ LVQTLEQHDA LKYSIIVAAT ASEAAPLQYL APFTAASIGE WFRDNGKHAL
     IVYDDLSKQA VAYRQLSLLL RRPPGREAYP GDVFYLHSRL LERAAKMSDK EGAGSLTALP
     VIETQGGDVS AYIPTNVISI TDGQIFLEAE LFYKGIRPAI NVGLSVSRVG SAAQVKALKQ
     VAGSLKLFLA QYREVAAFAQ FGSDLDASTK QTLVRGERLT QLLKQSQYSP LAAEEQVPLI
     YAGVNGYLDN IDLGRIAEFE SSFLAYLKSN HENILNDIRD KGELTKDLLA TLKSATESFV
     ATF
//

If you have problems or comments...

PBIL Back to PBIL home page