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Database: UniProt
Entry: A0A369GLD6_9HYPO
LinkDB: A0A369GLD6_9HYPO
Original site: A0A369GLD6_9HYPO 
ID   A0A369GLD6_9HYPO        Unreviewed;       762 AA.
AC   A0A369GLD6;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=ATP synthase subunit alpha, mitochondrial {ECO:0000256|ARBA:ARBA00016087};
GN   ORFNames=CP532_5198 {ECO:0000313|EMBL:RDA83783.1};
OS   Ophiocordyceps camponoti-leonardi (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=2039875 {ECO:0000313|EMBL:RDA83783.1, ECO:0000313|Proteomes:UP000252748};
RN   [1] {ECO:0000313|EMBL:RDA83783.1, ECO:0000313|Proteomes:UP000252748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC 80369 {ECO:0000313|EMBL:RDA83783.1,
RC   ECO:0000313|Proteomes:UP000252748};
RA   Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA   Luangsa-Ard J.-J., Giraud T.;
RT   "A genome scan of diversifying selection in the zombie-ant fungus
RT   Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT   coevolution and host-specificity.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:RDA83783.1}.
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DR   EMBL; PDHP01000160; RDA83783.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369GLD6; -.
DR   STRING; 2039875.A0A369GLD6; -.
DR   Proteomes; UP000252748; 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   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   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:UP000252748};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000339}.
FT   DOMAIN          278..344
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          401..624
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   DOMAIN          631..756
FT                   /note="ATP synthase alpha subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00306"
SQ   SEQUENCE   762 AA;  82777 MW;  9DA620C37368B66A CRC64;
     MGSAESKQVE GRLRQVDLSH IDFPERFNIY FESKSRLRLV LGEEKSRPSH IASMPGGFYG
     KLVLYDGPTV EAAPVIVIRS GRKLGYYDDM ELAASQPGAQ HKVEELRCEG KGWSMSYSFV
     TSVGEGGLPE KFEWRSSRGD EVKSLGEHSY GWKLVRLGNQ EEVVAVGADA KISRSLSKVG
     AFGFVGRGAS GELGDRWAVM AVASLIRIIQ RQWQTGITVA ATRAVSAAGR LAVVRNASPA
     VVGFQARSYA ADAKPNPTEV SSILEQRIRG VQEETGLAET GRVLSVGDGI ARVYGLTNVQ
     AEELVEFASG VKGMCMNLEA GQVGVVLFGS DRLVREGETV KRTGEIVDVP VGDALLGRVI
     DALGNPIDGK GPINTKEKRR AMLKAPGILP RKSVNQPVQT GYKSIDAMVP IGRGQRELVI
     GDRQTGKTAV CLDTILNQKR WNNGNEEDKK LYCVYVAVGQ KRSTVAQLVK TLEENDAMKY
     SIVVAATASE AAPLQYIAPF TGAAVGEHFR DSGRHSLVIF DDLSKQAIAY RQMSLLLRRP
     PGREAYPGDV FYLHSRLLER AAKLNKDHGG GSMTALPIIE TQGGDVSAFI PTNVISITDG
     QIFLESELFY KGIRPAINVG LSVSRVGSAA QLKAMKQVAG SLKLFLAQYR EVAAFAQFGS
     DLDAATKQTL ARGERLTELL KQKQYSPMAV NEMVPLIFAG INGYLDSVPV DKILQWESDY
     LAHLKSNESD LLATIDREGS ISKETEGRLK EVTQSFVKSF LG
//
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