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Conserved domains on  [gi|343796692|gb|AEM63728|]
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ATP synthase beta subunit, partial [Rhizobium sp. FB1202]

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 ...
 1-137 2.76e-92

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: 267.93  E-value: 2.76e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNVAK 80
Cdd:cd01133   14 NVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNIAK 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 343796692  81 AHGGYSVFAGVGERTREGNDLYHEMIESNVNKHGGgeGSKAALVYGQMNEPPGARAR 137
Cdd:cd01133   94 AHGGYSVFAGVGERTREGNDLYHEMKESGVINLDG--LSKVALVYGQMNEPPGARAR 148
 
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 ...
 1-137 2.76e-92

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: 267.93  E-value: 2.76e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNVAK 80
Cdd:cd01133   14 NVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNIAK 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 343796692  81 AHGGYSVFAGVGERTREGNDLYHEMIESNVNKHGGgeGSKAALVYGQMNEPPGARAR 137
Cdd:cd01133   94 AHGGYSVFAGVGERTREGNDLYHEMKESGVINLDG--LSKVALVYGQMNEPPGARAR 148
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-137 6.68e-92

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: 273.50  E-value: 6.68e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNVAK 80
Cdd:COG0055   93 NVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAK 172

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 343796692  81 AHGGYSVFAGVGERTREGNDLYHEMIESNVNKhgggegsKAALVYGQMNEPPGARAR 137
Cdd:COG0055  173 EHGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLR 222
atpB CHL00060
ATP synthase CF1 beta subunit
 1-137 8.32e-82

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 248.42  E-value: 8.32e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNVAK 80
Cdd:CHL00060 108 NVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAK 187

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 343796692  81 AHGGYSVFAGVGERTREGNDLYHEMIESNV-NKHGGGEgSKAALVYGQMNEPPGARAR 137
Cdd:CHL00060 188 AHGGVSVFGGVGERTREGNDLYMEMKESGViNEQNIAE-SKVALVYGQMNEPPGARMR 244
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 1-137 4.18e-80

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: 243.09  E-value: 4.18e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692    1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNVAK 80
Cdd:TIGR01039  90 NVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAK 169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 343796692   81 AHGGYSVFAGVGERTREGNDLYHEMIESNVNKhgggegsKAALVYGQMNEPPGARAR 137
Cdd:TIGR01039 170 EHGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMR 219
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 41-137 2.21e-29

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: 105.90  E-value: 2.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   41 GIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNVAKahgGYSVFAGVGERTREGNDLYHEMIESNVNKhgggegsK 120
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALK-------R 70

                          90
                  ....*....|....*..
gi 343796692  121 AALVYGQMNEPPGARAR 137
Cdd:pfam00006  71 TVVVVATSDEPPLARYR 87
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 53-124 2.77e-06

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 43.90  E-value: 2.77e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343796692    53 RGGKIGLFGGAGVGKTVLIMELINNVAKAHGGysVFAGVGERTREGNDLYHEMIESNVNKHGGGEGSKAALV 124
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGG--VIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLA 70
 
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 ...
 1-137 2.76e-92

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: 267.93  E-value: 2.76e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNVAK 80
Cdd:cd01133   14 NVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNIAK 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 343796692  81 AHGGYSVFAGVGERTREGNDLYHEMIESNVNKHGGgeGSKAALVYGQMNEPPGARAR 137
Cdd:cd01133   94 AHGGYSVFAGVGERTREGNDLYHEMKESGVINLDG--LSKVALVYGQMNEPPGARAR 148
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-137 6.68e-92

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: 273.50  E-value: 6.68e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNVAK 80
Cdd:COG0055   93 NVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAK 172

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 343796692  81 AHGGYSVFAGVGERTREGNDLYHEMIESNVNKhgggegsKAALVYGQMNEPPGARAR 137
Cdd:COG0055  173 EHGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLR 222
atpB CHL00060
ATP synthase CF1 beta subunit
 1-137 8.32e-82

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 248.42  E-value: 8.32e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNVAK 80
Cdd:CHL00060 108 NVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAK 187

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 343796692  81 AHGGYSVFAGVGERTREGNDLYHEMIESNV-NKHGGGEgSKAALVYGQMNEPPGARAR 137
Cdd:CHL00060 188 AHGGVSVFGGVGERTREGNDLYMEMKESGViNEQNIAE-SKVALVYGQMNEPPGARMR 244
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 1-137 4.18e-80

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: 243.09  E-value: 4.18e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692    1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNVAK 80
Cdd:TIGR01039  90 NVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAK 169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 343796692   81 AHGGYSVFAGVGERTREGNDLYHEMIESNVNKhgggegsKAALVYGQMNEPPGARAR 137
Cdd:TIGR01039 170 EHGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMR 219
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 1-137 1.35e-53

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: 169.56  E-value: 1.35e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNVAK 80
Cdd:cd19476   14 DGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAK 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 343796692  81 AHGGYSVFAGVGERTREGNDLYHEMIESNVNkhgggegSKAALVYGQMNEPPGARAR 137
Cdd:cd19476   94 AHAGVVVFAGIGERGREVNDLYEEFTKSGAM-------ERTVVVANTANDPPGARMR 143
alt_F1F0_F1_bet TIGR03305
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ...
 1-137 4.89e-50

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: 165.00  E-value: 4.89e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692    1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNVAK 80
Cdd:TIGR03305  85 DVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNMVG 164

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 343796692   81 AHGGYSVFAGVGERTREGNDLYHEMIESNVNKHgggegskAALVYGQMNEPPGARAR 137
Cdd:TIGR03305 165 QHQGVSIFCGIGERCREGEELYREMKEAGVLDN-------TVMVFGQMNEPPGARFR 214
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 41-137 2.21e-29

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: 105.90  E-value: 2.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   41 GIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNVAKahgGYSVFAGVGERTREGNDLYHEMIESNVNKhgggegsK 120
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALK-------R 70

                          90
                  ....*....|....*..
gi 343796692  121 AALVYGQMNEPPGARAR 137
Cdd:pfam00006  71 TVVVVATSDEPPLARYR 87
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 1-137 9.57e-20

Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.


Pssm-ID: 410880 [Multi-domain]  Cd Length: 265  Bit Score: 81.84  E-value: 9.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNVAK 80
Cdd:cd01136   14 DALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDA 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 343796692  81 AhggYSVFAGVGERTREGNdlyhEMIEsnvnKHGGGEG-SKAALVYGQMNEPPGARAR 137
Cdd:cd01136   94 D---VNVIALIGERGREVR----EFIE----KDLGEEGlKRSVLVVATSDESPLLRVR 140
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 4-97 1.73e-16

Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440771 [Multi-domain]  Cd Length: 433  Bit Score: 74.30  E-value: 1.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   4 GEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNvAKAHg 83
Cdd:COG1157  107 GRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIARN-TEAD- 184

                         90
                 ....*....|....
gi 343796692  84 gYSVFAGVGERTRE 97
Cdd:COG1157  185 -VNVIALIGERGRE 197
fliI PRK06002
flagellar protein export ATPase FliI;
1-107 2.55e-14

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 68.10  E-value: 2.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   1 NVIGEPVDEAGPLVTA-HKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELinnvA 79
Cdd:PRK06002 111 NALGEPIDGLGPLAPGtRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML----A 186

                         90       100
                 ....*....|....*....|....*....
gi 343796692  80 KAHGGYSV-FAGVGERTREgndlYHEMIE 107
Cdd:PRK06002 187 RADAFDTVvIALVGERGRE----VREFLE 211
fliI PRK08927
flagellar protein export ATPase FliI;
1-135 1.69e-11

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 59.99  E-value: 1.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   1 NVIGEPVDEAGPLVT-AHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNVA 79
Cdd:PRK08927 104 NALGEPIDGKGPLPQgPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNAD 183

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 343796692  80 KAhggYSVFAGVGERTREgndlYHEMIESNVnkhgGGEG-SKAALVYGQMNEPPGAR 135
Cdd:PRK08927 184 AD---VSVIGLIGERGRE----VQEFLQDDL----GPEGlARSVVVVATSDEPALMR 229
fliI PRK08472
flagellar protein export ATPase FliI;
1-111 5.09e-11

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 58.93  E-value: 5.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLiMELINNVAK 80
Cdd:PRK08472 104 DPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTL-MGMIVKGCL 182

                         90       100       110
                 ....*....|....*....|....*....|.
gi 343796692  81 AHggYSVFAGVGERTREgndlYHEMIESNVN 111
Cdd:PRK08472 183 AP--IKVVALIGERGRE----IPEFIEKNLG 207
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
3-137 3.21e-10

EscN/YscN/HrcN family type III secretion system ATPase;


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 56.30  E-value: 3.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   3 IGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNvakAH 82
Cdd:PRK06936 111 LGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRS---AE 187

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 343796692  83 GGYSVFAGVGERTREgndlYHEMIESNVnkhgGGEG-SKAALVYGQMNEPPGARAR 137
Cdd:PRK06936 188 VDVTVLALIGERGRE----VREFIESDL----GEEGlRKAVLVVATSDRPSMERAK 235
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 3-97 9.55e-10

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 55.16  E-value: 9.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   3 IGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNvakAH 82
Cdd:PRK09099 112 LGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARG---TQ 188

                         90
                 ....*....|....*
gi 343796692  83 GGYSVFAGVGERTRE 97
Cdd:PRK09099 189 CDVNVIALIGERGRE 203
PRK08149 PRK08149
FliI/YscN family ATPase;
19-125 1.20e-09

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 55.00  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692  19 RAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNvakAHGGYSVFAGVGERTREG 98
Cdd:PRK08149 116 RVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGERGREV 192

                         90       100
                 ....*....|....*....|....*..
gi 343796692  99 NDLYHEMIESnvnkhggGEGSKAALVY 125
Cdd:PRK08149 193 TEFVESLRAS-------SRREKCVLVY 212
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
3-110 2.12e-09

EscN/YscN/HrcN family type III secretion system ATPase;


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 54.05  E-value: 2.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   3 IGEPVDeAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELinnVAKAH 82
Cdd:PRK06820 113 LGAPID-GGPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGML---CADSA 188

                         90       100
                 ....*....|....*....|....*...
gi 343796692  83 GGYSVFAGVGERTREgndlYHEMIESNV 110
Cdd:PRK06820 189 ADVMVLALIGERGRE----VREFLEQVL 212
PRK05922 PRK05922
type III secretion system ATPase; Validated
 4-116 8.77e-09

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 52.21  E-value: 8.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   4 GEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTvlimELINNVAK-AH 82
Cdd:PRK05922 107 GNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSK 182

                         90       100       110
                 ....*....|....*....|....*....|....
gi 343796692  83 GGYSVFAGVGERTREgndlyhemIESNVNKHGGG 116
Cdd:PRK05922 183 STINVIALIGERGRE--------VREYIEQHKEG 208
fliI PRK06793
flagellar protein export ATPase FliI;
4-124 1.09e-08

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 52.29  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   4 GEPVDEAGPLVTAHKraIHQDAPSY--VEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNvAKA 81
Cdd:PRK06793 106 GEVLNEEAENIPLQK--IKLDAPPIhaFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKA 182

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 343796692  82 HggYSVFAGVGERTREGNDLyhemiesnVNKHGGGEGSKAALV 124
Cdd:PRK06793 183 D--INVISLVGERGREVKDF--------IRKELGEEGMRKSVV 215
fliI PRK07721
flagellar protein export ATPase FliI;
1-124 2.59e-08

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 50.88  E-value: 2.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLiMELINNVAK 80
Cdd:PRK07721 105 DALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTL-MGMIARNTS 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 343796692  81 AHggYSVFAGVGERTREgndlYHEMIESNVnkhgGGEGSKAALV 124
Cdd:PRK07721 184 AD--LNVIALIGERGRE----VREFIERDL----GPEGLKRSIV 217
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 1-95 3.22e-08

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 50.68  E-value: 3.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNvAK 80
Cdd:PRK13343 109 DPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN-QK 187

                         90
                 ....*....|....*
gi 343796692  81 AHGGYSVFAGVGERT 95
Cdd:PRK13343 188 DSDVICVYVAIGQKA 202
fliI PRK08972
flagellar protein export ATPase FliI;
3-124 4.11e-08

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 50.47  E-value: 4.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   3 IGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLI-MELINNVAKA 81
Cdd:PRK08972 111 VGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLgMMTRGTTADV 190

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 343796692  82 hggySVFAGVGERTREGNDLYHEMIesnvnkhgGGEGSKAALV 124
Cdd:PRK08972 191 ----IVVGLVGERGREVKEFIEEIL--------GEEGRARSVV 221
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 1-94 6.11e-07

F1 ATP synthase alpha 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 alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-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: 410876 [Multi-domain]  Cd Length: 274  Bit Score: 46.78  E-value: 6.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNvAK 80
Cdd:cd01132   16 DALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTAIAIDTIIN-QK 94

                         90
                 ....*....|....
gi 343796692  81 AHGGYSVFAGVGER 94
Cdd:cd01132   95 GKKVYCIYVAIGQK 108
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
26-97 7.99e-07

EscN/YscN/HrcN family type III secretion system ATPase;


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 46.87  E-value: 7.99e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343796692  26 PSYVEQSTeSQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINnvaKAHGGYSVFAGVGERTRE 97
Cdd:PRK07594 128 PAMVRQPI-TQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGRE 195
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 53-124 2.77e-06

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 43.90  E-value: 2.77e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343796692    53 RGGKIGLFGGAGVGKTVLIMELINNVAKAHGGysVFAGVGERTREGNDLYHEMIESNVNKHGGGEGSKAALV 124
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGG--VIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLA 70
fliI PRK07196
flagellar protein export ATPase FliI;
1-135 6.10e-06

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 44.11  E-value: 6.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLiMELINNVAK 80
Cdd:PRK07196 102 NGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVL-LGMITRYTQ 180

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 343796692  81 AHggYSVFAGVGERTREgndlYHEMIESNVNKHGggeGSKAALVYGQMNEPPGAR 135
Cdd:PRK07196 181 AD--VVVVGLIGERGRE----VKEFIEHSLQAAG---MAKSVVVAAPADESPLMR 226
PRK09281 PRK09281
F0F1 ATP synthase subunit alpha; Validated
 1-54 9.94e-06

F0F1 ATP synthase subunit alpha; Validated


Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 43.52  E-value: 9.94e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 343796692   1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARG 54
Cdd:PRK09281 109 NPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRG 162
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
 14-107 1.44e-05

V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.


Pssm-ID: 410878 [Multi-domain]  Cd Length: 288  Bit Score: 42.95  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692  14 VTAHKRAIHQDAPsYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELinnvAKahggYS-----VF 88
Cdd:cd01134   37 VNVQRWPVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSL----SK----WSnsdvvIY 107

                         90
                 ....*....|....*....
gi 343796692  89 AGVGERtreGNdlyhEMIE 107
Cdd:cd01134  108 VGCGER---GN----EMAE 119
fliI PRK05688
flagellar protein export ATPase FliI;
1-124 1.69e-05

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 42.80  E-value: 1.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLiMELINNVAK 80
Cdd:PRK05688 115 DGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVL-LGMMTRFTE 193

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 343796692  81 AHggYSVFAGVGERTREgndlYHEMIESNVnkhgGGEGSKAALV 124
Cdd:PRK05688 194 AD--IIVVGLIGERGRE----VKEFIEHIL----GEEGLKRSVV 227
fliI PRK07960
flagellum-specific ATP synthase FliI;
4-100 7.88e-05

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 40.92  E-value: 7.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   4 GEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVlimeLINNVAKAHG 83
Cdd:PRK07960 125 GKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSV----LLGMMARYTQ 200

                         90
                 ....*....|....*...
gi 343796692  84 GYSVFAG-VGERTREGND 100
Cdd:PRK07960 201 ADVIVVGlIGERGREVKD 218
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 28-125 2.30e-04

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 39.62  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   28 YVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTV----LIMELINNVAKAHGGYSVFAGVGERTREGNDLYH 103
Cdd:PRK14698  201 YKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVdgdtLILTKEFGLIKIKDLYEILDGKGKKTVEGNEEWT 280

                          90       100
                  ....*....|....*....|....*.
gi 343796692  104 EMiESNVNKHGGGEGS----KAALVY 125
Cdd:PRK14698  281 EL-EEPITLYGYKDGKiveiKATHVY 305
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 1-64 2.01e-03

V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.


Pssm-ID: 410879 [Multi-domain]  Cd Length: 282  Bit Score: 36.82  E-value: 2.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343796692   1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAG 64
Cdd:cd01135   16 NGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSG 79
atpA CHL00059
ATP synthase CF1 alpha subunit
 1-94 3.96e-03

ATP synthase CF1 alpha subunit


Pssm-ID: 176999 [Multi-domain]  Cd Length: 485  Bit Score: 36.09  E-value: 3.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343796692   1 NVIGEPVDEAGPLVTAHKRAIHQDAPSYVEQSTESQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNvAK 80
Cdd:CHL00059  88 NALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN-QK 166

                         90
                 ....*....|....
gi 343796692  81 AHGGYSVFAGVGER 94
Cdd:CHL00059 167 GQNVICVYVAIGQK 180
 
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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