GenomeNet

Database: UniProt
Entry: A0A484BHV1_DRONA
LinkDB: A0A484BHV1_DRONA
Original site: A0A484BHV1_DRONA 
ID   A0A484BHV1_DRONA        Unreviewed;       550 AA.
AC   A0A484BHV1;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=ATP synthase subunit alpha {ECO:0000256|RuleBase:RU003551};
GN   ORFNames=AWZ03_005293 {ECO:0000313|EMBL:TDG48338.1};
OS   Drosophila navojoa (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7232 {ECO:0000313|EMBL:TDG48338.1, ECO:0000313|Proteomes:UP000295192};
RN   [1] {ECO:0000313|EMBL:TDG48338.1, ECO:0000313|Proteomes:UP000295192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Navoj_Jal97 {ECO:0000313|EMBL:TDG48338.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:TDG48338.1};
RX   PubMed=30423125; DOI=.1093/jhered/esy059;
RA   Vanderlinde T., Dupim E.G., Nazario-Yepiz N.O., Carvalho A.B.;
RT   "An Improved Genome Assembly for Drosophila navojoa, the Basal Species in
RT   the mojavensis Cluster.";
RL   J. Hered. 110:118-123(2019).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000256|RuleBase:RU003551}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|RuleBase:RU000339}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TDG48338.1}.
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DR   EMBL; LSRL02000034; TDG48338.1; -; Genomic_DNA.
DR   RefSeq; XP_017961732.1; XM_018106243.1.
DR   AlphaFoldDB; A0A484BHV1; -.
DR   STRING; 7232.A0A484BHV1; -.
DR   GeneID; 108654728; -.
DR   KEGG; dnv:108654728; -.
DR   OMA; INQRDNW; -.
DR   OrthoDB; 1102723at2759; -.
DR   Proteomes; UP000295192; Unassembled WGS sequence.
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   CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR   CDD; cd18116; ATP-synt_F1_alpha_N; 1.
DR   CDD; cd01132; F1-ATPase_alpha_CD; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   Gene3D; 1.20.150.20; ATP synthase alpha/beta chain, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR   InterPro; IPR023366; ATP_synth_asu-like_sf.
DR   InterPro; IPR000793; ATP_synth_asu_C.
DR   InterPro; IPR038376; ATP_synth_asu_C_sf.
DR   InterPro; IPR033732; ATP_synth_F1_a_nt-bd_dom.
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; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00962; atpA; 1.
DR   PANTHER; PTHR48082; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48082:SF2; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
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; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310,
KW   ECO:0000256|RuleBase:RU003551};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003551};
KW   CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|RuleBase:RU003551};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW   ECO:0000256|RuleBase:RU000339};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU000339}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003551};
KW   Reference proteome {ECO:0000313|Proteomes:UP000295192};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000339}.
FT   DOMAIN          66..132
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          189..412
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   DOMAIN          419..544
FT                   /note="ATP synthase alpha subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00306"
SQ   SEQUENCE   550 AA;  59278 MW;  312B08AA98A66409 CRC64;
     MISARLASSV ARNLPKAAAQ VACKAAYPAG TLAARKFHVA STQRSAEISN ILEERILGVA
     PKADLEETGR VLSIGDGIAR VYGLNNIQAD EMVEFSSGLK GMALNLEPDN VGVVVFGNDK
     LIKQGDIVKR TGAIVDVPVG DELLGRVVDA LGNAIDGKGA INTKDRFRVG IKAPGIIPRV
     SVREPMQTGI KAVDSLVPIG RGQRELIIGD RQTGKTALAI DTIINQKRFN DGQDESKKLY
     CIYVAIGQKR STVAQIVKRL TDSGAMGYTI IVSATASDAA PLQYLAPYSG CAMGEFFRDK
     GKHALIIYDD LSKQAVAYRQ MSLLLRRPPG REAYPGDVFY LHSRLLERAA KMSPAMGGGS
     LTALPVIETQ AGDVSAYIPT NVISITDGQI FLETELFYKG IRPAINVGLS VSRVGSAAQT
     KAMKQVAGSM KLELAQYREV AAFAQFGSDL DAATQQLLNR GVRLTELLKQ GQYVPMSIED
     QVAVIYCGVR GHLDKMDPSK ITKFEKEFLQ HIKTSEQGLL DSIAKEGQIS EAADAKLKDI
     VQKFMSTFQG
//
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