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Database: UniProt
Entry: B7QCK2_IXOSC
LinkDB: B7QCK2_IXOSC
Original site: B7QCK2_IXOSC 
ID   B7QCK2_IXOSC            Unreviewed;       555 AA.
AC   B7QCK2;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=ATP synthase subunit alpha {ECO:0000256|RuleBase:RU003551};
GN   Name=8039213 {ECO:0000313|EnsemblMetazoa:ISCW011988-PA};
GN   ORFNames=IscW_ISCW011988 {ECO:0000313|EMBL:EEC16574.1};
OS   Ixodes scapularis (Black-legged tick) (Deer tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=6945;
RN   [1] {ECO:0000313|EMBL:EEC16574.1, ECO:0000313|Proteomes:UP000001555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}, and Wikel colony
RC   {ECO:0000313|EMBL:EEC16574.1};
RG   Ixodes scapularis Genome Project Consortium;
RA   Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA   Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA   Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA   Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT   "Annotation of Ixodes scapularis.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ISCW011988-PA}
RP   IDENTIFICATION.
RC   STRAIN=wikel {ECO:0000313|EnsemblMetazoa:ISCW011988-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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}.
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DR   EMBL; ABJB010925079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS908087; EEC16574.1; -; Genomic_DNA.
DR   RefSeq; XP_002413266.1; XM_002413221.1.
DR   AlphaFoldDB; B7QCK2; -.
DR   STRING; 6945.B7QCK2; -.
DR   PaxDb; 6945-B7QCK2; -.
DR   EnsemblMetazoa; ISCW011988-RA; ISCW011988-PA; ISCW011988.
DR   GeneID; 8039213; -.
DR   KEGG; isc:IscW_ISCW011988; -.
DR   VEuPathDB; VectorBase:ISCI011988; -.
DR   VEuPathDB; VectorBase:ISCP_016637; -.
DR   VEuPathDB; VectorBase:ISCW011988; -.
DR   HOGENOM; CLU_010091_2_1_1; -.
DR   InParanoid; B7QCK2; -.
DR   OMA; INQRDNW; -.
DR   OrthoDB; 1102723at2759; -.
DR   Proteomes; UP000001555; Unassembled WGS sequence.
DR   GO; GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; IBA:GO_Central.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR   GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
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   1: Evidence at protein level;
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}; Hydrolase {ECO:0000313|EMBL:EEC16574.1};
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   Proteomics identification {ECO:0007829|PeptideAtlas:B7QCK2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001555};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000339}.
FT   DOMAIN          71..137
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          194..417
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   DOMAIN          424..549
FT                   /note="ATP synthase alpha subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00306"
SQ   SEQUENCE   555 AA;  59844 MW;  9CA3963C402284E6 CRC64;
     MAFVSARITG ALAKQIARTV TKYPTKCIGV SSVAVRALST SNRLYAGAGS AEVSSILEER
     ILGQTTTSNL EETGRVLSIG DGIARVYGLK NIQAEEMVEF SSGLKGMALN LEPDNVGIVV
     FGNDKLIREG DIVKRTGAIV DVPVGPELLG RVVDALGNPI DGKGPVACKG RARVGVKAPG
     IIPRISVKEP MLTGIKAVDS LVPIGRGQRE LIIGDRQTGK TAIAIDTIIN QKHFNDGSDE
     KKKLYCIYVA IGQKRSTVAQ ILKRLTSADA MKYTIIVSAT ASDAAPLQYL APYAGCAMGE
     YFRDNGMHGL IIYDDLSKQA VAYRQMSLLL RRPPGREAYP GDVFYLHSRL LERAAKMNDT
     FGGGSLTALP VIETQAGDVS AYIPTNVISI TDGQIFLETE LFYKGIRPAI NVGLSVSRVG
     SAAQTKAMKQ VAGSMKLELA QYREVAAFAQ FGSDLDAATQ QLLNRGVRLT ELLKQGQYTP
     MAIEEQVAVI YTGVRGYLDK LDPSQINRFE AEFLPHIRST QKELLATIAK EGHISPDTDA
     KLKKIVVDFM ASFQA
//
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