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Conserved domains on  [gi|2471747920|gb|WEY07771|]
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ATP synthase beta subunit, partial [Agrobacterium sp.]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
1-79 3.40e-54

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd01133:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 277  Bit Score: 168.55  E-value: 3.40e-54
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2471747920   1 KTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESNVNKLGGgeGSKAALVYGQMNEPPGARARVALTGLTI 79
Cdd:cd01133    80 KTVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDG--LSKVALVYGQMNEPPGARARVALTGLTM 156
 
Name Accession Description Interval E-value
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
1-79 3.40e-54

F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.


Pssm-ID: 410877 [Multi-domain]  Cd Length: 277  Bit Score: 168.55  E-value: 3.40e-54
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2471747920   1 KTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESNVNKLGGgeGSKAALVYGQMNEPPGARARVALTGLTI 79
Cdd:cd01133    80 KTVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDG--LSKVALVYGQMNEPPGARARVALTGLTM 156
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
1-79 1.18e-52

FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 439825 [Multi-domain]  Cd Length: 468  Bit Score: 169.50  E-value: 1.18e-52
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2471747920   1 KTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESNVNKlgggegsKAALVYGQMNEPPGARARVALTGLTI 79
Cdd:COG0055   159 KTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALTM 230
atpB CHL00060
ATP synthase CF1 beta subunit
1-79 3.19e-46

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 153.27  E-value: 3.19e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2471747920   1 KTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESNVNKLGGGEGSKAALVYGQMNEPPGARARVALTGLTI 79
Cdd:CHL00060  174 KTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTM 252
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
1-79 2.23e-45

ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 211621 [Multi-domain]  Cd Length: 461  Bit Score: 150.64  E-value: 2.23e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2471747920   1 KTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESNVNKlgggegsKAALVYGQMNEPPGARARVALTGLTI 79
Cdd:TIGR01039 156 KTVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTM 227
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
1-79 3.75e-17

ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.


Pssm-ID: 425417 [Multi-domain]  Cd Length: 212  Bit Score: 71.62  E-value: 3.75e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2471747920   1 KTVLIMELINNVAKahgGYSVFAGVGERTREGNDLYHEMIESNVNKlgggegsKAALVYGQMNEPPGARARVALTGLTI 79
Cdd:pfam00006  27 KTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALK-------RTVVVVATSDEPPLARYRAPYTALTI 95
 
Name Accession Description Interval E-value
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
1-79 3.40e-54

F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.


Pssm-ID: 410877 [Multi-domain]  Cd Length: 277  Bit Score: 168.55  E-value: 3.40e-54
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2471747920   1 KTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESNVNKLGGgeGSKAALVYGQMNEPPGARARVALTGLTI 79
Cdd:cd01133    80 KTVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDG--LSKVALVYGQMNEPPGARARVALTGLTM 156
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
1-79 1.18e-52

FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 439825 [Multi-domain]  Cd Length: 468  Bit Score: 169.50  E-value: 1.18e-52
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2471747920   1 KTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESNVNKlgggegsKAALVYGQMNEPPGARARVALTGLTI 79
Cdd:COG0055   159 KTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALTM 230
atpB CHL00060
ATP synthase CF1 beta subunit
1-79 3.19e-46

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 153.27  E-value: 3.19e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2471747920   1 KTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESNVNKLGGGEGSKAALVYGQMNEPPGARARVALTGLTI 79
Cdd:CHL00060  174 KTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTM 252
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
1-79 2.23e-45

ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 211621 [Multi-domain]  Cd Length: 461  Bit Score: 150.64  E-value: 2.23e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2471747920   1 KTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESNVNKlgggegsKAALVYGQMNEPPGARARVALTGLTI 79
Cdd:TIGR01039 156 KTVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTM 227
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
1-79 5.78e-28

RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410884 [Multi-domain]  Cd Length: 270  Bit Score: 100.99  E-value: 5.78e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2471747920   1 KTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESNVNklgggegSKAALVYGQMNEPPGARARVALTGLTI 79
Cdd:cd19476    80 KTVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAM-------ERTVVVANTANDPPGARMRVPYTGLTI 151
alt_F1F0_F1_bet TIGR03305
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ...
1-79 6.75e-24

alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 beta subunit of this apparent second ATP synthase.


Pssm-ID: 132348 [Multi-domain]  Cd Length: 449  Bit Score: 92.58  E-value: 6.75e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2471747920   1 KTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESNVNklgggegSKAALVYGQMNEPPGARARVALTGLTI 79
Cdd:TIGR03305 151 KTVLLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVL-------DNTVMVFGQMNEPPGARFRVGHTALTM 222
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
1-79 3.75e-17

ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.


Pssm-ID: 425417 [Multi-domain]  Cd Length: 212  Bit Score: 71.62  E-value: 3.75e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2471747920   1 KTVLIMELINNVAKahgGYSVFAGVGERTREGNDLYHEMIESNVNKlgggegsKAALVYGQMNEPPGARARVALTGLTI 79
Cdd:pfam00006  27 KTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALK-------RTVVVVATSDEPPLARYRAPYTALTI 95
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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