ID A0A1B7N8S0_9AGAM Unreviewed; 545 AA.
AC A0A1B7N8S0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 13-SEP-2023, entry version 23.
DE RecName: Full=ATP synthase subunit alpha {ECO:0000256|RuleBase:RU003551};
GN ORFNames=K503DRAFT_712982 {ECO:0000313|EMBL:OAX41235.1};
OS Rhizopogon vinicolor AM-OR11-026.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=1314800 {ECO:0000313|EMBL:OAX41235.1, ECO:0000313|Proteomes:UP000092154};
RN [1] {ECO:0000313|EMBL:OAX41235.1, ECO:0000313|Proteomes:UP000092154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-026 {ECO:0000313|EMBL:OAX41235.1,
RC ECO:0000313|Proteomes:UP000092154};
RG DOE Joint Genome Institute;
RA Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA Barry K., Grigoriev I.V., Spatafora J.W.;
RT "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT divergence of the mating type B locus.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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; KV448186; OAX41235.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7N8S0; -.
DR STRING; 1314800.A0A1B7N8S0; -.
DR InParanoid; A0A1B7N8S0; -.
DR OrthoDB; 1102723at2759; -.
DR Proteomes; UP000092154; 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:UP000092154};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000339}.
FT DOMAIN 60..127
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 184..407
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT DOMAIN 414..537
FT /note="ATP synthase alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00306"
SQ SEQUENCE 545 AA; 58718 MW; 3B10B215B4D61229 CRC64;
MHRIALQNSA RRAAFAAAPK SNATVGALAS RSYATAKPAA SEVSSILESR IAGTAISGNV
EETGRVLSVG DGIGRVWGLK NVQAEEMVEF SSGVRGMCLN LEADNVGVSI FGNDRLIKEG
DTVKRTGQIV DVPVGPGLLG RVVDALGNPI DGKGPIEAAE RRRASLKAPG ILPRRSVNQP
MMTGLKPIDA MVPIGRGQRE LIIGDRQTGK TAVAIDTILN QKRWNDGKDE DKKLYCVYVA
VGQKRSTVAQ LVKTLEENDA MKYSIIVAAT ASEAAPLQYL APFSGCAMGE WFRDNGKHAL
IIYDDLSKQA VAYRQMSLLL RRPPGREAYP GDVFYLHSRL LERAAKMSDK FGGGSLTALP
IIETQGGDVS AYIPTNVISI TDGQIFLEAE LFFRGVRPAI NVGLSVSRVG SAAQTKIMKK
FAGSLKLYLA QYREVAAFAQ FGSDLDASTR FLLSRGARLT ELLKQGQYQP LPTEIQVPII
YAGVNGLLDS IPVDKITAWE AEFRSHLTAT QGPLLAEIET GNVTPEMEAK IKKVVEDHVS
SFTSS
//
