ID B2WC39_PYRTR Unreviewed; 690 AA.
AC B2WC39;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=ATP synthase subunit alpha, mitochondrial {ECO:0000256|ARBA:ARBA00016087};
GN ORFNames=PTRG_07548 {ECO:0000313|EMBL:EDU50467.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU50467.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|RuleBase:RU000339}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS231622; EDU50467.1; -; Genomic_DNA.
DR RefSeq; XP_001937880.1; XM_001937845.1.
DR AlphaFoldDB; B2WC39; -.
DR STRING; 426418.B2WC39; -.
DR EnsemblFungi; EDU50467; EDU50467; PTRG_07548.
DR GeneID; 6345820; -.
DR eggNOG; KOG1353; Eukaryota.
DR HOGENOM; CLU_010091_2_0_1; -.
DR InParanoid; B2WC39; -.
DR OMA; INQRDNW; -.
DR OrthoDB; 1102723at2759; -.
DR Proteomes; UP000001471; 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; 2.
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 PANTHER; PTHR48082; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48082:SF2; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 2.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 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; 2.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196};
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 Reference proteome {ECO:0000313|Proteomes:UP000001471};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000339}.
FT DOMAIN 94..160
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 217..319
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT DOMAIN 430..552
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT DOMAIN 559..684
FT /note="ATP synthase alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00306"
SQ SEQUENCE 690 AA; 75690 MW; DB131688BDC7E4E4 CRC64;
MFSRAIRQSS RRVAAISATS RIASLRGLRW GREQQRAPLH YEAVLTALAR LQTRAPTFTS
AIRSYASDAK ATPTEVSSIL EQRIRGVQEE TSLSETGRVL SVGDGIARVH GMNNVQAEEL
VEFASGVKGM CMNLEAGQVG VVLFGSDRLV KEGETVKRTG EIVDVPVGEA LLGRVVDALG
NPIDGKGPLK TTERRRAQLK APGILPRQSV KEPVQTGLKS VDAMVPIGRG QRELIIGDRQ
TGKTAVALDA MLNQNRWNRG TDEKKKLYCI YVAVGQKRST VAQLVKTLEE NDAMKYTIIV
AATASEAAPL QYIAPFTGCY SDLTNIEDVD LEHYNLDGAY DGYPSKSDLE DYKLHYNADY
VYDSLSDTDS DIADFEHVCF EHGLLKPAST HITTAYTLTL LPYAPGSDFN LTNIDDVGIQ
EVVNPSYPSI IEEFRDNGKH ALIIYDDLTK QAVAYRQMSL LLRRPPGREA YPGDVFYLHS
RLLERAAKMN DKLGGGSLTA LPVIETQGGD VSAYIPTNVI SITGKFDGQI FLEAELFYKG
IRPAINVGLS VSRVGSAAQV KAMKQVAGSL KLFLAQYREV AAFAQFGSDL DAATKQTLSR
GERLTELLKQ KQYSPMAVNE MVPLIYAGIN GLLDNVPVNK ILQWEADFLA HLKANESDML
NKIDREGALS KELEAQLREV AQSFTKSFIA
//
