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Conserved domains on  [gi|297528181|gb|ADI46126|]
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ATP synthase beta subunit, partial [Rhizobium sp. CCBAU 05003]

Protein Classification

F0F1 ATP synthase subunit beta( domain architecture ID 1903243)

F0F1 ATP synthase subunit beta is part of the catalytic core of the F-type ATPase that produces ATP from ADP in the presence of a proton gradient across the membrane and is found in bacterial, mitochondrial, and chloroplast membranes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AtpD super family cl43008
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-167 1.22e-119

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


The actual alignment was detected with superfamily member COG0055:

Pssm-ID: 439825 [Multi-domain]  Cd Length: 468  Bit Score: 345.54  E-value: 1.22e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   1 VIGEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA 80
Cdd:COG0055   94 VLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKE 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  81 HGGYSVFAGVGERTREGNDLYHEMIESGVNKhgggegsKAALVYGQMNEPPGARARVALTGLTVAENFRD-QGQDVLFFV 159
Cdd:COG0055  174 HGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFI 246


                 ....*...
gi 297528181 160 DNIFRFTQ 167
Cdd:COG0055  247 DNIFRFTQ 254
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-167 1.22e-119

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: 345.54  E-value: 1.22e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   1 VIGEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA 80
Cdd:COG0055   94 VLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKE 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  81 HGGYSVFAGVGERTREGNDLYHEMIESGVNKhgggegsKAALVYGQMNEPPGARARVALTGLTVAENFRD-QGQDVLFFV 159
Cdd:COG0055  174 HGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFI 246


                 ....*...
gi 297528181 160 DNIFRFTQ 167
Cdd:COG0055  247 DNIFRFTQ 254
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 1-167 1.17e-117

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: 333.80  E-value: 1.17e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   1 VIGEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA 80
Cdd:cd01133   15 VLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNIAKA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  81 HGGYSVFAGVGERTREGNDLYHEMIESGVNKHGGgeGSKAALVYGQMNEPPGARARVALTGLTVAENFRDQ-GQDVLFFV 159
Cdd:cd01133   95 HGGYSVFAGVGERTREGNDLYHEMKESGVINLDG--LSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEeGQDVLLFI 172


                 ....*...
gi 297528181 160 DNIFRFTQ 167
Cdd:cd01133  173 DNIFRFTQ 180
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 1-167 3.91e-103

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: 303.18  E-value: 3.91e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181    1 VIGEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA 80
Cdd:TIGR01039  91 VLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKE 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   81 HGGYSVFAGVGERTREGNDLYHEMIESGVNKhgggegsKAALVYGQMNEPPGARARVALTGLTVAENFRD-QGQDVLFFV 159
Cdd:TIGR01039 171 HGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFI 243


                  ....*...
gi 297528181  160 DNIFRFTQ 167
Cdd:TIGR01039 244 DNIFRFTQ 251
atpB CHL00060
ATP synthase CF1 beta subunit
 1-167 3.27e-102

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 301.96  E-value: 3.27e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   1 VIGEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA 80
Cdd:CHL00060 109 VLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKA 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  81 HGGYSVFAGVGERTREGNDLYHEMIESGV-NKHGGGEgSKAALVYGQMNEPPGARARVALTGLTVAENFRDQG-QDVLFF 158
Cdd:CHL00060 189 HGGVSVFGGVGERTREGNDLYMEMKESGViNEQNIAE-SKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNkQDVLLF 267


                 ....*....
gi 297528181 159 VDNIFRFTQ 167
Cdd:CHL00060 268 IDNIFRFVQ 276
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 40-167 4.41e-49

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: 157.13  E-value: 4.41e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   40 GIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKahgGYSVFAGVGERTREGNDLYHEMIESGVNKhgggegsK 119
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALK-------R 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 297528181  120 AALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVDNIFRFTQ 167
Cdd:pfam00006  71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAE 118
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 52-165 3.20e-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: 44.67  E-value: 3.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181    52 KGGKIGLFGGAGVGKTVLIMELINNVAKAHGGysVFAGVGERTREGNDLYHEMIESGVNKHGGGegskaalvygqmnepP 131
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGG--VIYIDGEDILEEVLDQLLLIIVGGKKASGS---------------G 63

                           90       100       110
                   ....*....|....*....|....*....|....
gi 297528181   132 GARARVALTGLtvaenfRDQGQDVLFFvDNIFRF 165
Cdd:smart00382  64 ELRLRLALALA------RKLKPDVLIL-DEITSL 90
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-167 1.22e-119

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: 345.54  E-value: 1.22e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   1 VIGEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA 80
Cdd:COG0055   94 VLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKE 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  81 HGGYSVFAGVGERTREGNDLYHEMIESGVNKhgggegsKAALVYGQMNEPPGARARVALTGLTVAENFRD-QGQDVLFFV 159
Cdd:COG0055  174 HGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFI 246


                 ....*...
gi 297528181 160 DNIFRFTQ 167
Cdd:COG0055  247 DNIFRFTQ 254
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 1-167 1.17e-117

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: 333.80  E-value: 1.17e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   1 VIGEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA 80
Cdd:cd01133   15 VLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNIAKA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  81 HGGYSVFAGVGERTREGNDLYHEMIESGVNKHGGgeGSKAALVYGQMNEPPGARARVALTGLTVAENFRDQ-GQDVLFFV 159
Cdd:cd01133   95 HGGYSVFAGVGERTREGNDLYHEMKESGVINLDG--LSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEeGQDVLLFI 172


                 ....*...
gi 297528181 160 DNIFRFTQ 167
Cdd:cd01133  173 DNIFRFTQ 180
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 1-167 3.91e-103

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: 303.18  E-value: 3.91e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181    1 VIGEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA 80
Cdd:TIGR01039  91 VLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKE 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   81 HGGYSVFAGVGERTREGNDLYHEMIESGVNKhgggegsKAALVYGQMNEPPGARARVALTGLTVAENFRD-QGQDVLFFV 159
Cdd:TIGR01039 171 HGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFI 243


                  ....*...
gi 297528181  160 DNIFRFTQ 167
Cdd:TIGR01039 244 DNIFRFTQ 251
atpB CHL00060
ATP synthase CF1 beta subunit
 1-167 3.27e-102

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 301.96  E-value: 3.27e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   1 VIGEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA 80
Cdd:CHL00060 109 VLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKA 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  81 HGGYSVFAGVGERTREGNDLYHEMIESGV-NKHGGGEgSKAALVYGQMNEPPGARARVALTGLTVAENFRDQG-QDVLFF 158
Cdd:CHL00060 189 HGGVSVFGGVGERTREGNDLYMEMKESGViNEQNIAE-SKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNkQDVLLF 267


                 ....*....
gi 297528181 159 VDNIFRFTQ 167
Cdd:CHL00060 268 IDNIFRFVQ 276
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 1-167 8.96e-72

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: 216.94  E-value: 8.96e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   1 VIGEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA 80
Cdd:cd19476   15 GLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  81 HGGYSVFAGVGERTREGNDLYHEMIESGVNkhgggegSKAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVD 160
Cdd:cd19476   95 HAGVVVFAGIGERGREVNDLYEEFTKSGAM-------ERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIID 167


                 ....*..
gi 297528181 161 NIFRFTQ 167
Cdd:cd19476  168 DISRYAE 174
alt_F1F0_F1_bet TIGR03305
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ...
 1-167 6.96e-67

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: 210.07  E-value: 6.96e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181    1 VIGEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA 80
Cdd:TIGR03305  86 VFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNMVGQ 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   81 HGGYSVFAGVGERTREGNDLYHEMIESGVNKHgggegskAALVYGQMNEPPGARARVALTGLTVAENFR-DQGQDVLFFV 159
Cdd:TIGR03305 166 HQGVSIFCGIGERCREGEELYREMKEAGVLDN-------TVMVFGQMNEPPGARFRVGHTALTMAEYFRdDEKQDVLLLI 238


                  ....*...
gi 297528181  160 DNIFRFTQ 167
Cdd:TIGR03305 239 DNIFRFIQ 246
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 40-167 4.41e-49

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: 157.13  E-value: 4.41e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   40 GIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKahgGYSVFAGVGERTREGNDLYHEMIESGVNKhgggegsK 119
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALK-------R 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 297528181  120 AALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVDNIFRFTQ 167
Cdd:pfam00006  71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAE 118
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 3-165 3.80e-34

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: 120.74  E-value: 3.80e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   3 GEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAhg 82
Cdd:cd01136   17 GEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDAD-- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  83 gYSVFAGVGERTREGNdlyhEMIEsgvnKHGGGEG-SKAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVDN 161
Cdd:cd01136   95 -VNVIALIGERGREVR----EFIE----KDLGEEGlKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDS 165


                 ....
gi 297528181 162 IFRF 165
Cdd:cd01136  166 LTRF 169
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 3-165 5.33e-30

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: 112.82  E-value: 5.33e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   3 GEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKAHg 82
Cdd:COG1157  107 GRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIARN-TEAD- 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  83 gYSVFAGVGERTREGNdlyhEMIEsgvnKHGGGEG-SKAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVDN 161
Cdd:COG1157  185 -VNVIALIGERGREVR----EFIE----DDLGEEGlARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDS 255


                 ....
gi 297528181 162 IFRF 165
Cdd:COG1157  256 LTRF 259
fliI PRK06002
flagellar protein export ATPase FliI;
2-165 1.39e-27

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 106.62  E-value: 1.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   2 IGEPVDEAGPLVTASKR-SIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinnvAKA 80
Cdd:PRK06002 113 LGEPIDGLGPLAPGTRPmSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML----ARA 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  81 HGGYSV-FAGVGERTREgndlYHEMIESGVnkhgGGEGSKAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFV 159
Cdd:PRK06002 189 DAFDTVvIALVGERGRE----VREFLEDTL----ADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIV 260


                 ....*.
gi 297528181 160 DNIFRF 165
Cdd:PRK06002 261 DSVTRF 266
fliI PRK08927
flagellar protein export ATPase FliI;
3-165 2.32e-21

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 89.27  E-value: 2.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   3 GEPVDEAGPLVT-ASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAh 81
Cdd:PRK08927 107 GEPIDGKGPLPQgPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD- 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  82 ggYSVFAGVGERTREgndlYHEMIESGVnkhgGGEG-SKAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVD 160
Cdd:PRK08927 186 --VSVIGLIGERGRE----VQEFLQDDL----GPEGlARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMD 255


                 ....*
gi 297528181 161 NIFRF 165
Cdd:PRK08927 256 SVTRF 260
PRK08149 PRK08149
FliI/YscN family ATPase;
18-165 3.97e-21

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 88.51  E-value: 3.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  18 RSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvakAHGGYSVFAGVGERTREG 97
Cdd:PRK08149 116 RVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGERGREV 192

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297528181  98 NDLYHEMIESGvnkhgggEGSKAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVDNIFRF 165
Cdd:PRK08149 193 TEFVESLRASS-------RREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRY 253
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
2-165 6.02e-21

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 88.27  E-value: 6.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   2 IGEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvakAH 81
Cdd:PRK06936 111 LGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRS---AE 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  82 GGYSVFAGVGERTREgndlYHEMIESGVnkhgGGEG-SKAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVD 160
Cdd:PRK06936 188 VDVTVLALIGERGRE----VREFIESDL----GEEGlRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMD 259


                 ....*
gi 297528181 161 NIFRF 165
Cdd:PRK06936 260 SVTRF 264
fliI PRK08472
flagellar protein export ATPase FliI;
3-165 2.97e-20

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 86.28  E-value: 2.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   3 GEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLiMELINNVAKAHg 82
Cdd:PRK08472 107 GRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTL-MGMIVKGCLAP- 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  83 gYSVFAGVGERTREgndlYHEMIEsgvnKHGGGEGSKAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVDNI 162
Cdd:PRK08472 185 -IKVVALIGERGRE----IPEFIE----KNLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSV 255


                 ...
gi 297528181 163 FRF 165
Cdd:PRK08472 256 TRF 258
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
2-165 1.18e-19

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 84.48  E-value: 1.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   2 IGEPVDeAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinnVAKAH 81
Cdd:PRK06820 113 LGAPID-GGPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGML---CADSA 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  82 GGYSVFAGVGERTREgndlYHEMIESGVNKHGGgegSKAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVDN 161
Cdd:PRK06820 189 ADVMVLALIGERGRE----VREFLEQVLTPEAR---ARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADS 261


                 ....
gi 297528181 162 IFRF 165
Cdd:PRK06820 262 LTRY 265
fliI PRK07721
flagellar protein export ATPase FliI;
2-165 1.08e-18

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 81.69  E-value: 1.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   2 IGEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLiMELINNVAKAH 81
Cdd:PRK07721 107 LGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTL-MGMIARNTSAD 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  82 ggYSVFAGVGERTREgndlYHEMIEsgvnKHGGGEG-SKAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVD 160
Cdd:PRK07721 186 --LNVIALIGERGRE----VREFIE----RDLGPEGlKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMD 255


                 ....*
gi 297528181 161 NIFRF 165
Cdd:PRK07721 256 SVTRV 260
fliI PRK08972
flagellar protein export ATPase FliI;
2-167 7.19e-18

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 79.36  E-value: 7.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   2 IGEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLI-MELINNVAKA 80
Cdd:PRK08972 111 VGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLgMMTRGTTADV 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  81 hggySVFAGVGERTREGNDLYHEMIesgvnkhgGGEG-SKAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFV 159
Cdd:PRK08972 191 ----IVVGLVGERGREVKEFIEEIL--------GEEGrARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLM 258


                 ....*...
gi 297528181 160 DNIFRFTQ 167
Cdd:PRK08972 259 DSLTRYAQ 266
fliI PRK06793
flagellar protein export ATPase FliI;
3-165 3.44e-17

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 77.71  E-value: 3.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   3 GEPVDEAGPLVTASKrsIHQDAPSY--VEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKA 80
Cdd:PRK06793 106 GEVLNEEAENIPLQK--IKLDAPPIhaFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKA 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  81 HggYSVFAGVGERTREGNDLyhemiesgVNKHGGGEG-SKAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFV 159
Cdd:PRK06793 183 D--INVISLVGERGREVKDF--------IRKELGEEGmRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMM 252


                 ....*.
gi 297528181 160 DNIFRF 165
Cdd:PRK06793 253 DSVTRF 258
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 2-165 6.10e-17

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 76.73  E-value: 6.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   2 IGEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvakAH 81
Cdd:PRK09099 112 LGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARG---TQ 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  82 GGYSVFAGVGERTREgndlYHEMIESGVnkhgGGEG-SKAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVD 160
Cdd:PRK09099 189 CDVNVIALIGERGRE----VREFIELIL----GEDGmARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMD 260


                 ....*
gi 297528181 161 NIFRF 165
Cdd:PRK09099 261 SLTRF 265
PRK05922 PRK05922
type III secretion system ATPase; Validated
 3-165 1.58e-16

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 75.71  E-value: 1.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   3 GEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTvlimELINNVAK-AH 81
Cdd:PRK05922 107 GNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSK 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  82 GGYSVFAGVGERTREGNDLyhemiesgVNKHGGG-EGSKAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVD 160
Cdd:PRK05922 183 STINVIALIGERGREVREY--------IEQHKEGlAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMD 254


                 ....*
gi 297528181 161 NIFRF 165
Cdd:PRK05922 255 SLSRW 259
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
2-167 1.04e-14

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 70.37  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   2 IGEPVDEAgPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINnvaKAH 81
Cdd:PRK07594 105 FGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN---APD 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  82 GGYSVFAGVGERTREgndlYHEMIESGVNKHGggeGSKAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVDN 161
Cdd:PRK07594 181 ADSNVLVLIGERGRE----VREFIDFTLSEET---RKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADS 253


                 ....*.
gi 297528181 162 IFRFTQ 167
Cdd:PRK07594 254 LTRYAR 259
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
 37-167 5.48e-14

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: 67.60  E-value: 5.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  37 LVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinnvAKahggYS-----VFAGVGERTREGNDLYHEMIESGVNK 111
Cdd:cd01134   60 LLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSL----SK----WSnsdvvIYVGCGERGNEMAEVLEEFPELKDPI 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 297528181 112 HGGGEGSKAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVDNIFRFTQ 167
Cdd:cd01134  132 TGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAE 187
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 2-160 1.17e-13

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 67.63  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   2 IGEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKAH 81
Cdd:PRK13343 111 LGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN-QKDS 189

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297528181  82 GGYSVFAGVGERTREGNdlyhEMIESgVNKHGGGEGSkaALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVD 160
Cdd:PRK13343 190 DVICVYVAIGQKASAVA----RVIET-LREHGALEYT--TVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYD 261
fliI PRK05688
flagellar protein export ATPase FliI;
2-167 3.46e-13

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 65.91  E-value: 3.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   2 IGEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLiMELINNVAKAH 81
Cdd:PRK05688 117 AGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVL-LGMMTRFTEAD 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  82 ggYSVFAGVGERTREgndlYHEMIESGVnkhgGGEG-SKAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVD 160
Cdd:PRK05688 196 --IIVVGLIGERGRE----VKEFIEHIL----GEEGlKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMD 265


                 ....*..
gi 297528181 161 NIFRFTQ 167
Cdd:PRK05688 266 SLTRFAQ 272
fliI PRK07196
flagellar protein export ATPase FliI;
2-165 1.17e-12

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 64.53  E-value: 1.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   2 IGEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLiMELINNVAKAH 81
Cdd:PRK07196 104 LGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVL-LGMITRYTQAD 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  82 ggYSVFAGVGERTREgndlYHEMIESGVnkhgGGEG-SKAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVD 160
Cdd:PRK07196 183 --VVVVGLIGERGRE----VKEFIEHSL----QAAGmAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVD 252


                 ....*
gi 297528181 161 NIFRF 165
Cdd:PRK07196 253 SLTRY 257
fliI PRK07960
flagellum-specific ATP synthase FliI;
35-165 3.44e-10

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 57.49  E-value: 3.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  35 QILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVlimeLINNVAKAHGGYSVFAG-VGERTREGNDLYHEMIesgvnkhg 113
Cdd:PRK07960 157 HVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSV----LLGMMARYTQADVIVVGlIGERGREVKDFIENIL-------- 224

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 297528181 114 GGEG-SKAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVDNIFRF 165
Cdd:PRK07960 225 GAEGrARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRY 277
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 3-160 7.54e-10

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: 56.03  E-value: 7.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   3 GEPVDEAGPLVTASKRSIHQDAPSYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKAHG 82
Cdd:cd01132   19 GNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTAIAIDTIIN-QKGKK 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297528181  83 GYSVFAGVGERTREGNDLYHEMIESGVNKHgggegskAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVD 160
Cdd:cd01132   98 VYCIYVAIGQKRSTVAQIVKTLEEHGAMEY-------TIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGKHALIIYD 168
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
 37-156 2.77e-07

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 49.01  E-value: 2.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  37 LVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinnvAKahggYS-----VFAGVGERTREGNDLYHEMIESGVNK 111
Cdd:PRK04192 211 LITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQL----AK----WAdadivIYVGCGERGNEMTEVLEEFPELIDPK 282

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 297528181 112 HGGGEGSKAALVYGQMNEPPGAR-ARVaLTGLTVAENFRDQGQDVL 156
Cdd:PRK04192 283 TGRPLMERTVLIANTSNMPVAAReASI-YTGITIAEYYRDMGYDVL 327
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 86-167 1.64e-06

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 46.94  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   86 VFAGVGERTREGNDLYHEMIESGVNKHGGGEGSKAALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVDNIFRF 165
Cdd:PRK14698  686 IYIGCGERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRW 765


                  ..
gi 297528181  166 TQ 167
Cdd:PRK14698  766 AE 767
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 52-165 3.20e-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: 44.67  E-value: 3.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181    52 KGGKIGLFGGAGVGKTVLIMELINNVAKAHGGysVFAGVGERTREGNDLYHEMIESGVNKHGGGegskaalvygqmnepP 131
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGG--VIYIDGEDILEEVLDQLLLIIVGGKKASGS---------------G 63

                           90       100       110
                   ....*....|....*....|....*....|....
gi 297528181   132 GARARVALTGLtvaenfRDQGQDVLFFvDNIFRF 165
Cdd:smart00382  64 ELRLRLALALA------RKLKPDVLIL-DEITSL 90
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 37-124 1.61e-04

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 41.16  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181   37 LVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTV----LIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMiESGVNKH 112
Cdd:PRK14698  211 LITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVdgdtLILTKEFGLIKIKDLYEILDGKGKKTVEGNEEWTEL-EEPITLY 289

                          90
                  ....*....|....*.
gi 297528181  113 GGGEGS----KAALVY 124
Cdd:PRK14698  290 GYKDGKiveiKATHVY 305
PRK12608 PRK12608
transcription termination factor Rho; Provisional
 42-166 3.69e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237150 [Multi-domain]  Cd Length: 380  Bit Score: 39.68  E-value: 3.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  42 KVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAG-VGERTREGNDLyhemiesgvnkhgggEGSKA 120
Cdd:PRK12608 122 RVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDM---------------RRSVK 186

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 297528181 121 ALVYGQMN-EPPGARARVALTGLTVAENFRDQGQDVLFFVDNIFRFT 166
Cdd:PRK12608 187 GEVYASTFdRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLA 233
rho_factor_C cd01128
C-terminal ATP binding domain of transcription termination factor rho; Transcription ...
 42-165 8.35e-04

C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.


Pssm-ID: 410872 [Multi-domain]  Cd Length: 249  Bit Score: 38.34  E-value: 8.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297528181  42 KVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAG-VGERTREGNDlyheMIESGvnkhgggegsKA 120
Cdd:cd01128    5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRSV----------KG 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 297528181 121 ALVYGQMNEPPGARARVALTGLTVAENFRDQGQDVLFFVDNIFRF 165
Cdd:cd01128   71 EVVASTFDEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRL 115
 
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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