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Database: UniProt
Entry: A0A175VRU2_9PEZI
LinkDB: A0A175VRU2_9PEZI
Original site: A0A175VRU2_9PEZI 
ID   A0A175VRU2_9PEZI        Unreviewed;       552 AA.
AC   A0A175VRU2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=ATP synthase subunit alpha {ECO:0000256|RuleBase:RU003551};
GN   ORFNames=MMYC01_208904 {ECO:0000313|EMBL:KXX74093.1};
OS   Madurella mycetomatis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX   NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX74093.1, ECO:0000313|Proteomes:UP000078237};
RN   [1] {ECO:0000313|Proteomes:UP000078237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA   van de Sande W.W.J.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KXX74093.1, ECO:0000313|Proteomes:UP000078237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA   Van De Sande W.;
RT   "Madurella mycetomatis genome sequencing.";
RL   Submitted (JAN-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}.
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:KXX74093.1}.
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DR   EMBL; LCTW02000386; KXX74093.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A175VRU2; -.
DR   STRING; 100816.A0A175VRU2; -.
DR   VEuPathDB; FungiDB:MMYC01_208904; -.
DR   OrthoDB; 1102723at2759; -.
DR   Proteomes; UP000078237; 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:UP000078237};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000339}.
FT   DOMAIN          68..134
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          191..414
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   DOMAIN          421..546
FT                   /note="ATP synthase alpha subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00306"
SQ   SEQUENCE   552 AA;  59570 MW;  1F4C71CE1D17D3B8 CRC64;
     MFRNAIRQST RAVGALSASS RVAARNAAPA VSALQARTYA ADAKASPTEV SSILEQRIRG
     VQEEAGLAET GRVLSVGDGI ARVHGMANVQ AEELVEFASG VKGMCMNLEA GQVGVVLFGS
     DRLVKEGETV KRTGEIVDVP VGPELLGRVV DALGNPIDGK GPINTKEKRR AQLKAPGILP
     RRSVNQPVQT GLKSVDAMVP IGRGQRELII GDRQTGKTAV GLDTILNQKR WNNGTDETKK
     LYCIYVAVGQ KRSTVAQLVK TLEENDAMKY SIVVAATASE AAPLQYIAPF TGASIGEWFR
     DNGKHSLVIY DDLSKQAVAY RQMSLLLRRP PGREAYPGDV FYLHSRLLER AAKMNDKHGG
     GSMTALPVIE TQGGDVSAYI PTNVISITDG QIFLESELFY KGVRPAINVG LSVSRVGSAA
     QLKAMKQVAG SLKLFLAQYR EVAAFAQFGS DLDAATKQTL ARGERLTELL KQKQYSPMAV
     NEMVPLIFAG VNGYLDTVPV NKILQWEADF LAHLKTNEAD LMATIDKEGA ISKDLEARLR
     DVTQTFTKGF LA
//
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