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Database: UniProt
Entry: A0A286UVA7_9AGAM
LinkDB: A0A286UVA7_9AGAM
Original site: A0A286UVA7_9AGAM 
ID   A0A286UVA7_9AGAM        Unreviewed;       540 AA.
AC   A0A286UVA7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=ATP synthase subunit beta {ECO:0000256|RuleBase:RU003553};
DE            EC=7.1.2.2 {ECO:0000256|RuleBase:RU003553};
GN   ORFNames=PNOK_0058500 {ECO:0000313|EMBL:PAV23517.1};
OS   Pyrrhoderma noxium.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Hymenochaetales; Hymenochaetaceae; Pyrrhoderma.
OX   NCBI_TaxID=2282107 {ECO:0000313|EMBL:PAV23517.1, ECO:0000313|Proteomes:UP000217199};
RN   [1] {ECO:0000313|Proteomes:UP000217199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FFPRI411160 {ECO:0000313|Proteomes:UP000217199};
RA   Chung C.-L., Lee J.T., Akiba M., Lee H.-H., Kuo T.-H., Liu D., Ke H.-M.,
RA   Yokoi T., Roa M.B., Lu M.J., Chang Y.-Y., Ann P.-J., Tsai J.-N.,
RA   Chen C.-Y., Tzean S.-S., Ota Y., Hattori T., Sahashi N., Liou R.-F.,
RA   Kikuchi T., Tsai I.J.;
RT   "The Genomic Landscape Of Tree Rot In Phellinus noxius And Its
RT   Hymenochaetales Members.";
RL   bioRxiv 0:0-0(2017).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000256|RuleBase:RU003553}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC         Evidence={ECO:0000256|RuleBase:RU003553};
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC       subunits: a, b and c. {ECO:0000256|RuleBase:RU003553}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936}.
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:PAV23517.1}.
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DR   EMBL; NBII01000001; PAV23517.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286UVA7; -.
DR   STRING; 2282107.A0A286UVA7; -.
DR   InParanoid; A0A286UVA7; -.
DR   OrthoDB; 3420200at2759; -.
DR   Proteomes; UP000217199; Chromosome 1.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   CDD; cd18110; ATP-synt_F1_beta_C; 1.
DR   CDD; cd18115; ATP-synt_F1_beta_N; 1.
DR   CDD; cd01133; F1-ATPase_beta_CD; 1.
DR   Gene3D; 2.40.10.170; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR005722; ATP_synth_F1_bsu.
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; IPR024034; ATPase_F1/V1_b/a_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR01039; atpD; 1.
DR   PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR   PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   PIRSF; PIRSF039072; ATPase_subunit_beta; 1.
DR   SMART; SM00382; AAA; 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:RU003553};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003553};
KW   CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|RuleBase:RU003553};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217199};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          210..393
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   540 AA;  58230 MW;  36F2C2442F126CF8 CRC64;
     MLTTRGVTRI SRRALNAKKT NAFFSTAAPA LARASLPRFS QPQRPVASRR FAPSSSNAAR
     TYATEAKGQV GSVKQVIGAV VDVQFDTENL PPILNALEVQ DFHGGRLVLE VASHLGENSV
     RTIAMDGTEG LVRGQRVVDT GAPIRIPVGK DTLGRIMNVI GEPIDERGPI KGVKLLPIHA
     DPPAFVDQST TAEVLETGIK VVDLLAPYAR GGKIGLFGGA GVGKTVLIQE LINNVAKAHG
     GFSIFCGVGE RTREGNDLYH EMIETGVINL EGDSKVALVF GQMNEPPGAR ARVALTGLTI
     AEYFRDEEGQ DVLLFIDNIF RFTQAGSEVS ALLGRIPSAV GYQPTLSTDM GGMQERITTT
     KKGSITSVQA VYVPADDLTD PAPATTFAHL DATTVLSRGI AELGIYPAVD PLDSKSRMLD
     PRIVGKEHYE VATAVQKILQ DYKSLQDIIA ILGMDELSEE DKLTVERARK IQRFMSQPFQ
     VAQVFTGYEG KLVPLKDTVR SFKEIISGQH DSLPESAFYM AGTIEDVKSK AEQLAKEMGN
//
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