GenomeNet

Database: UniProt
Entry: A0A094CLF5_9PEZI
LinkDB: A0A094CLF5_9PEZI
Original site: A0A094CLF5_9PEZI 
ID   A0A094CLF5_9PEZI        Unreviewed;       516 AA.
AC   A0A094CLF5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=ATP synthase subunit beta {ECO:0000256|RuleBase:RU003553};
DE            EC=7.1.2.2 {ECO:0000256|RuleBase:RU003553};
GN   ORFNames=V497_07462 {ECO:0000313|EMBL:KFY54804.1};
OS   Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY54804.1, ECO:0000313|Proteomes:UP000029268};
RN   [1] {ECO:0000313|EMBL:KFY54804.1, ECO:0000313|Proteomes:UP000029268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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: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:KFY54804.1}.
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; JPJZ01001190; KFY54804.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094CLF5; -.
DR   STRING; 1420910.A0A094CLF5; -.
DR   HOGENOM; CLU_022398_0_2_1; -.
DR   OrthoDB; 3420200at2759; -.
DR   Proteomes; UP000029268; 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: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:UP000029268};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          184..429
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   516 AA;  55486 MW;  6AB00D1C1B0663DF CRC64;
     MFKSGLLKAV RPSVAAASRN ALRPAARTGL KASAARFAST DSATHGKIHQ VIGAVVDVKF
     DTEKLPPILN ALETQNGDQR LVLEVAQHLG ENVVRCIAMD GTEGLVRGHR ATDTGNPIMV
     PVGPETLGRI MNVTGDPIDE RGPIKTAKRA SIHADAPPFT EQSTSAEVLV TGIKVVDLLA
     PYARGGKIGL FGGAGVGKTV FIQELINNIA KAHGGYSVFT GVGERTREGN DLYHEMQETK
     VINLEGESKV ALVFGQMNEP PGARARVALT GLTVAEYFRD VEGQDVLLFI DNIFRFTQAG
     SEVSALLGRI PSAVGYQPTL AVDMGLMQER ITTTTKGSIT SVQAVYVPAD DLTDPAPAST
     FAHLDSTTVL SRGISELGIY PAVDPLDSKS RMLDPRVIGQ DHYDTATKVQ QMLQEYKSLQ
     DIIAILGMDE LSEADKLTVE RARKVQRFLS QPFAVAEVFT GIQGTLVDLP KTIESFKRIM
     AGEGDNLPEN AFYMVGDFES ARAKGEKILA ELEKSE
//
DBGET integrated database retrieval system