(data stored in ACNUC16935 zone)

SWISSPROT: C8VMQ7_EMENI

ID   C8VMQ7_EMENI            Unreviewed;       556 AA.
AC   C8VMQ7;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   05-JUL-2017, entry version 57.
DE   RecName: Full=ATP synthase subunit alpha {ECO:0000256|RuleBase:RU003551};
GN   ORFNames=ANIA_01523 {ECO:0000313|EMBL:CBF85040.1};
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF85040.1, ECO:0000313|Proteomes:UP000000560};
RN   [1] {ECO:0000313|Proteomes:UP000000560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R.,
RA   Batzoglou S., Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M., Hynes M., Paoletti M., Fischer R., Miller B., Dyer P.,
RA   Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2] {ECO:0000313|Proteomes:UP000000560}
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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}.
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DR   EMBL; BN001307; CBF85040.1; -; Genomic_DNA.
DR   STRING; 162425.CADANIAP00008151; -.
DR   EnsemblFungi; CADANIAT00008151; CADANIAP00008151; CADANIAG00008151.
DR   InParanoid; C8VMQ7; -.
DR   OMA; GNAQIKS; -.
DR   OrthoDB; EOG092C1T32; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
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; C8VMQ7.
DR   SWISS-2DPAGE; C8VMQ7.
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:UP000000560};
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:UP000000560};
KW   Transport {ECO:0000256|RuleBase:RU000339}.
FT   DOMAIN       73    138       ATP-synt_ab_N. {ECO:0000259|Pfam:
FT                                PF02874}.
FT   DOMAIN      195    418       ATP-synt_ab. {ECO:0000259|Pfam:PF00006}.
FT   DOMAIN      425    549       ATP-synt_ab_C. {ECO:0000259|Pfam:
FT                                PF00306}.
SQ   SEQUENCE   556 AA;  60067 MW;  8A62F49C49270365 CRC64;
     MFRNALRQSS RTVAAATATG RIASVRAAVP GPLSAASKQV RTYAAEAKAS PTEVSSILEQ
     RIRGVQEESG LAETGRVLSV GDGIARVHGM TNVQAEELVE FASGVKGMCM NLEAGQVGVV
     LFGSDRLVKE GETVKRTGEI VDVPVGPELL GRVVDALGNP IDGKGPINAS TKSRAQLKAP
     GILPRRSVNQ PVQTGLKCVD SMVPIGRGQR ELIIGDRQTG KTAVALDAML NQKRWNNTSD
     ESKKLYCIYV AVGQKRSTVA QLVKTLEEND AMKYSIVVAA TASEAAPLQY LAPFTGCAMG
     EWFRDNGRHA VIVYDDLSKQ AVAYRQMSLL LRRPPGREAY PGDVFYLHSR LLERAAKMND
     KHGGGSLTAL PVIETQGGDV SAYIPTNVIS ITDGQIFLEA ELFYKGIRPA INVGLSVSRV
     GSAAQVKAMK QVAGSLKLFL AQYREVAAFA QFGSDLDAST KQTLNRGQRL TELLKQKQYS
     PMAVSDMVPL IFAGVNGYLD NIPVAKILQW ESDFLAYLKS NHPEVQETIE KEGQVSKELE
     AKLKDIIPSF NKSFNA
//

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