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Conserved domains on  [gi|490432834|gb|AGL12381|]
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ATP synthase beta subunit, partial [Citrobacter koseri]

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 ...
 1-214 3.58e-166

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: 465.72  E-value: 3.58e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   1 GSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLM 80
Cdd:COG0055   61 DSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLL 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  81 CPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNR 160
Cdd:COG0055  141 APYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGAR 220

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490432834 161 LRVALTGLTMAEKFRD-EGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:COG0055  221 LRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPT 275
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-214 3.58e-166

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: 465.72  E-value: 3.58e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   1 GSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLM 80
Cdd:COG0055   61 DSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLL 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  81 CPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNR 160
Cdd:COG0055  141 APYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGAR 220

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490432834 161 LRVALTGLTMAEKFRD-EGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:COG0055  221 LRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPT 275
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 1-214 1.01e-155

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: 439.15  E-value: 1.01e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834    1 GSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLM 80
Cdd:TIGR01039  58 GSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLL 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   81 CPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNR 160
Cdd:TIGR01039 138 APYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGAR 217

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490432834  161 LRVALTGLTMAEKFRDE-GRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:TIGR01039 218 MRVALTGLTMAEYFRDEqGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPT 272
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 20-214 3.74e-141

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: 395.05  E-value: 3.74e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  20 EVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGK 99
Cdd:cd01133    1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834 100 TVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVI-----DKVSLVYGQMNEPPGNRLRVALTGLTMAEKF 174
Cdd:cd01133   81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVInldglSKVALVYGQMNEPPGARARVALTGLTMAEYF 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 490432834 175 RD-EGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:cd01133  161 RDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPT 201
atpB CHL00060
ATP synthase CF1 beta subunit
 2-214 1.98e-126

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 365.90  E-value: 1.98e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   2 SSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMC 81
Cdd:CHL00060  77 ATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLA 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  82 PFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVID-------KVSLVYGQMN 154
Cdd:CHL00060 157 PYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMN 236

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490432834 155 EPPGNRLRVALTGLTMAEKFRDEGR-DVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:CHL00060 237 EPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPT 297
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 73-214 2.43e-61

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: 190.26  E-value: 2.43e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   73 GIKVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAiehSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQ 152
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQAS---ADVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490432834  153 MNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:pfam00006  78 SDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPS 139
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 85-205 3.22e-04

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: 39.66  E-value: 3.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834    85 KGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGvgertregndfyhEMTDSNVIDKVSLVYGQMNEPPGNRLRVA 164
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG-------------EDILEEVLDQLLLIIVGGKKASGSGELRL 67

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 490432834   165 LTGLTMAEKFRDEgrdvLLFVDNIYRYTLAGTEVSALLGRM 205
Cdd:smart00382  68 RLALALARKLKPD----VLILDEITSLLDAEQEALLLLLEE 104
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-214 3.58e-166

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: 465.72  E-value: 3.58e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   1 GSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLM 80
Cdd:COG0055   61 DSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLL 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  81 CPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNR 160
Cdd:COG0055  141 APYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGAR 220

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490432834 161 LRVALTGLTMAEKFRD-EGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:COG0055  221 LRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPT 275
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 1-214 1.01e-155

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: 439.15  E-value: 1.01e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834    1 GSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLM 80
Cdd:TIGR01039  58 GSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLL 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   81 CPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNR 160
Cdd:TIGR01039 138 APYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGAR 217

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490432834  161 LRVALTGLTMAEKFRDE-GRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:TIGR01039 218 MRVALTGLTMAEYFRDEqGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPT 272
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 20-214 3.74e-141

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: 395.05  E-value: 3.74e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  20 EVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGK 99
Cdd:cd01133    1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834 100 TVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVI-----DKVSLVYGQMNEPPGNRLRVALTGLTMAEKF 174
Cdd:cd01133   81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVInldglSKVALVYGQMNEPPGARARVALTGLTMAEYF 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 490432834 175 RD-EGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:cd01133  161 RDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPT 201
atpB CHL00060
ATP synthase CF1 beta subunit
 2-214 1.98e-126

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 365.90  E-value: 1.98e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   2 SSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMC 81
Cdd:CHL00060  77 ATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLA 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  82 PFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVID-------KVSLVYGQMN 154
Cdd:CHL00060 157 PYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMN 236

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490432834 155 EPPGNRLRVALTGLTMAEKFRDEGR-DVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:CHL00060 237 EPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPT 297
alt_F1F0_F1_bet TIGR03305
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ...
 2-214 4.55e-90

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: 271.70  E-value: 4.55e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834    2 SSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMC 81
Cdd:TIGR03305  54 PTQGLARGMPVRDSGGPLKAPVGKPTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLV 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   82 PFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRL 161
Cdd:TIGR03305 134 PLERGGKAGLFGGAGVGKTVLLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARF 213

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 490432834  162 RVALTGLTMAEKFR-DEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:TIGR03305 214 RVGHTALTMAEYFRdDEKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPT 267
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 21-214 6.26e-90

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: 265.09  E-value: 6.26e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  21 VPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKT 100
Cdd:cd19476    2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834 101 VNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRD 180
Cdd:cd19476   82 VLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 490432834 181 VLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:cd19476  162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPY 195
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 73-214 2.43e-61

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: 190.26  E-value: 2.43e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   73 GIKVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAiehSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQ 152
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQAS---ADVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490432834  153 MNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:pfam00006  78 SDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPS 139
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 20-214 5.19e-41

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: 140.00  E-value: 5.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  20 EVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGK 99
Cdd:cd01136    1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834 100 TVNMMELIRNIAiehSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGR 179
Cdd:cd01136   81 STLLGMIARNTD---ADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGK 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 490432834 180 DVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:cd01136  158 KVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPS 192
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 1-214 5.21e-40

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: 141.32  E-value: 5.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   1 GSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLM 80
Cdd:COG1157   72 GDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGL 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  81 CPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNR 160
Cdd:COG1157  152 LTVGRGQRIGIFAGSGVGKSTLLGMIARNTEAD---VNVIALIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMR 228

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490432834 161 LRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:COG1157  229 LRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPS 282
PRK08149 PRK08149
FliI/YscN family ATPase;
1-211 4.64e-34

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 125.49  E-value: 4.64e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   1 GSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPV---DMKGEIGEEERW-AIHRAAPSYEELSNSQELLETGIKV 76
Cdd:PRK08149  62 GNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVerfDAPPTVGPISEErVIDVAPPSYAERRPIREPLITGVRA 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  77 ID--LMCpfAKGGKVGLFGGAGVGKTVNMmelirNIAIEHSGYSVF--AGVGERTREGNDFYHEMTDSNVIDKVSLVYGQ 152
Cdd:PRK08149 142 IDglLTC--GVGQRMGIFASAGCGKTSLM-----NMLIEHSEADVFviGLIGERGREVTEFVESLRASSRREKCVLVYAT 214

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490432834 153 MNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGY 211
Cdd:PRK08149 215 SDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGY 273
fliI PRK08472
flagellar protein export ATPase FliI;
4-214 5.32e-32

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 120.18  E-value: 5.32e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   4 DGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPF 83
Cdd:PRK08472  75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTC 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  84 AKGGKVGLFGGAGVGKTVNMMELIRNiaiEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVsLVYGQMNEPPGNRLRV 163
Cdd:PRK08472 155 GKGQKLGIFAGSGVGKSTLMGMIVKG---CLAPIKVVALIGERGREIPEFIEKNLGGDLENTV-IVVATSDDSPLMRKYG 230

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490432834 164 ALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK08472 231 AFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPS 281
fliI PRK08927
flagellar protein export ATPase FliI;
1-214 1.14e-30

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 116.62  E-value: 1.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   1 GSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGE-EERWAIHRAAPSYEELSNSQELLETGIKVIDL 79
Cdd:PRK08927  72 GPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQgPVPYPLRAPPPPAHSRARVGEPLDLGVRALNT 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  80 MCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGN 159
Cdd:PRK08927 152 FLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALM 228

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490432834 160 RLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK08927 229 RRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPT 283
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
2-214 1.23e-30

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 116.45  E-value: 1.23e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   2 SSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERwAIHRAAPSYEELSNSQELLETGIKVIDLMC 81
Cdd:PRK06820  80 SSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWR-ELDCPPPSPLTRQPIEQMLTTGIRAIDGIL 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  82 PFAKGGKVGLFGGAGVGKTVnmmeLIRNIAiEHSGYSV--FAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGN 159
Cdd:PRK06820 159 SCGEGQRIGIFAAAGVGKST----LLGMLC-ADSAADVmvLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALE 233

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490432834 160 RLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK06820 234 RLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPS 288
fliI PRK06002
flagellar protein export ATPase FliI;
29-214 4.07e-29

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 112.40  E-value: 4.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  29 GRIMNVLGEPVDMKGEIGE-EERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELI 107
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLA 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834 108 RNIAIEHSgysVFAGVGERTREGNDFYHEMTDSNvIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDN 187
Cdd:PRK06002 187 RADAFDTV---VIALVGERGREVREFLEDTLADN-LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVDS 262

                        170       180
                 ....*....|....*....|....*..
gi 490432834 188 IYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK06002 263 VTRFAHAAREVALAAGEPPVARGYPPS 289
fliI PRK08972
flagellar protein export ATPase FliI;
5-214 9.09e-29

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 111.33  E-value: 9.09e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   5 GLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERwaIHRAAPSYEELSNSQ--ELLETGIKVIDLMCP 82
Cdd:PRK08972  81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQR--ASRHSPPINPLSRRPitEPLDVGVRAINAMLT 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  83 FAKGGKVGLFGGAGVGKTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLR 162
Cdd:PRK08972 159 VGKGQRMGLFAGSGVGKSVLLGMMTRGTTAD---VIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLK 235

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490432834 163 VALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK08972 236 GCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPS 287
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 1-214 6.58e-28

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 109.09  E-value: 6.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   1 GSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLM 80
Cdd:PRK09099  78 GELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGL 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  81 CPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNR 160
Cdd:PRK09099 158 MTLGEGQRMGIFAPAGVGKSTLMGMFARGTQCD---VNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIER 234

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490432834 161 LRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK09099 235 AKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPS 288
fliI PRK07196
flagellar protein export ATPase FliI;
5-214 7.98e-27

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 106.13  E-value: 7.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   5 GLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFA 84
Cdd:PRK07196  74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIG 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  85 KGGKVGLFGGAGVGKTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVA 164
Cdd:PRK07196 154 KGQRVGLMAGSGVGKSVLLGMITRYTQAD---VVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKAT 230

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 490432834 165 LTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK07196 231 ELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPS 280
fliI PRK07721
flagellar protein export ATPase FliI;
18-214 3.85e-25

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 101.34  E-value: 3.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  18 PIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGV 97
Cdd:PRK07721  90 PLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGV 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  98 GKTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDE 177
Cdd:PRK07721 170 GKSTLMGMIARNTSAD---LNVIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQ 246

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 490432834 178 GRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK07721 247 GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPS 283
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 1-206 3.91e-25

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 101.92  E-value: 3.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   1 GSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLM 80
Cdd:PRK13343  77 DDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDAL 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  81 CPFAKGGKVGLFGGAGVGKTVNMMELIrnIAIEHSG-YSVFAGVGERTRegndfyhemTDSNVIDKV---------SLVY 150
Cdd:PRK13343 157 IPIGRGQRELIIGDRQTGKTAIAIDAI--INQKDSDvICVYVAIGQKAS---------AVARVIETLrehgaleytTVVV 225

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490432834 151 GQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMP 206
Cdd:PRK13343 226 AEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPP 281
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
1-213 6.37e-25

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 100.80  E-value: 6.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   1 GSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDmkGEIGEEERWAIHRAAPSYEELSN--SQELLeTGIKVID 78
Cdd:PRK07594  71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLD--GRELPDVCWKDYDAMPPPAMVRQpiTQPLM-TGIRAID 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  79 LMCPFAKGGKVGLFGGAGVGKTVNMMELIrniAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPG 158
Cdd:PRK07594 148 SVATCGEGQRVGIFSAPGVGKSTLLAMLC---NAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPAL 224

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490432834 159 NRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQP 213
Cdd:PRK07594 225 ERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPP 279
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
20-214 1.28e-24

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 100.21  E-value: 1.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  20 EVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGK 99
Cdd:PRK06936  96 QVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGK 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834 100 TVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGR 179
Cdd:PRK06936 176 STLLASLIRSAEVD---VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGK 252

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 490432834 180 DVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK06936 253 RVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPS 287
fliI PRK05688
flagellar protein export ATPase FliI;
1-214 6.00e-24

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 98.26  E-value: 6.00e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   1 GSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERwaIHRAAPSYEELSNS--QELLETGIKVID 78
Cdd:PRK05688  83 GSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDW--VPMDGPTINPLNRHpiSEPLDVGIRSIN 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  79 LMCPFAKGGKVGLFGGAGVGKTV--NMMELIRNIAIehsgySVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEP 156
Cdd:PRK05688 161 GLLTVGRGQRLGLFAGTGVGKSVllGMMTRFTEADI-----IVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDA 235

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490432834 157 PGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK05688 236 PLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPS 293
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 19-206 1.68e-23

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: 94.55  E-value: 1.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  19 IEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVG 98
Cdd:cd01132    2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  99 KTVNMMELIrniaIEHSG---YSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFR 175
Cdd:cd01132   82 KTAIAIDTI----INQKGkkvYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFR 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 490432834 176 DEGRDVLLFVDNIYRYTLAGTEVSALLGRMP 206
Cdd:cd01132  158 DNGKHALIIYDDLSKQAVAYRQMSLLLRRPP 188
fliI PRK06793
flagellar protein export ATPase FliI;
19-206 2.35e-21

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 90.81  E-value: 2.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  19 IEVPVGKATLGRIMNVLGEPVDMKGEIGEEERwaIHRAAPSYEELSNSQ--ELLETGIKVIDLMCPFAKGGKVGLFGGAG 96
Cdd:PRK06793  89 VVIPRGNHLLGKVLSANGEVLNEEAENIPLQK--IKLDAPPIHAFEREEitDVFETGIKSIDSMLTIGIGQKIGIFAGSG 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  97 VGKTVNMMELIRNiaiEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD 176
Cdd:PRK06793 167 VGKSTLLGMIAKN---AKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRD 243

                        170       180       190
                 ....*....|....*....|....*....|
gi 490432834 177 EGRDVLLFVDNIYRYTLAGTEVSALLGRMP 206
Cdd:PRK06793 244 QGNNVLLMMDSVTRFADARRSVDIAVKELP 273
PRK05922 PRK05922
type III secretion system ATPase; Validated
 9-211 7.15e-21

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 89.58  E-value: 7.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   9 GLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGK 88
Cdd:PRK05922  80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQR 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  89 VGLFGGAGVGKTvnmmELIRNIAI-EHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTG 167
Cdd:PRK05922 160 IGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAA 235

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 490432834 168 LTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGY 211
Cdd:PRK05922 236 MTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHY 279
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 18-211 1.11e-20

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: 87.28  E-value: 1.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  18 PIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIH--------RAAPsyeelsnsQELLETGIKVIDLMCPFAKGGKV 89
Cdd:cd01135    1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINgppinpvaRIYP--------EEMIQTGISAIDVMNTLVRGQKL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  90 GLFGGAGVGKTVNMMELIRNIAIEHSGYS---VFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALT 166
Cdd:cd01135   73 PIFSGSGLPHNELAAQIARQAGVVGSEENfaiVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRM 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 490432834 167 GLTMAEKFR-DEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGY 211
Cdd:cd01135  153 ALTTAEYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGY 198
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
 50-211 2.22e-20

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: 86.47  E-value: 2.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  50 RWAIHRAAPSYEELSnSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVnmmelirniaIEH--SGYS-----VFAG 122
Cdd:cd01134   41 RWPVRQPRPVKEKLP-PNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTV----------ISQslSKWSnsdvvIYVG 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834 123 VGER----TREGNDFYH---EMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAG 195
Cdd:cd01134  110 CGERgnemAEVLEEFPElkdPITGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEAL 189

                        170
                 ....*....|....*.
gi 490432834 196 TEVSALLGRMPSAVGY 211
Cdd:cd01134  190 REISGRLEEMPAEEGY 205
PRK09281 PRK09281
F0F1 ATP synthase subunit alpha; Validated
 1-206 4.88e-19

F0F1 ATP synthase subunit alpha; Validated


Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 84.35  E-value: 4.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   1 GSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLM 80
Cdd:PRK09281  77 GDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAM 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  81 CPFAKGGKVGLFGGAGVGKTVnmmelirnIAIE------HSG-YSVFAGVGERtregndfyhEMTDSNVIDKVSlVYGQM 153
Cdd:PRK09281 157 IPIGRGQRELIIGDRQTGKTA--------IAIDtiinqkGKDvICIYVAIGQK---------ASTVAQVVRKLE-EHGAM 218

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490432834 154 ----------NEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNI------YRytlagtEVSALLGRMP 206
Cdd:PRK09281 219 eytivvaataSDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLskqavaYR------QLSLLLRRPP 281
fliI PRK07960
flagellum-specific ATP synthase FliI;
20-214 1.07e-18

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 83.29  E-value: 1.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  20 EVPVGKATLGRIMNVLGEPVDmkGEIGEEERWAIHRAAPSYEELSNS--QELLETGIKVIDLMCPFAKGGKVGLFGGAGV 97
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLD--GLPAPDTGETGALITPPFNPLQRTpiEHVLDTGVRAINALLTVGRGQRMGLFAGSGV 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  98 GKTVNMMELIRniaIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDE 177
Cdd:PRK07960 187 GKSVLLGMMAR---YTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDR 263

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 490432834 178 GRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK07960 264 GQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPS 300
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
 8-211 2.23e-17

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 79.48  E-value: 2.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   8 RGLDVKD-----LEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAA--PSYEELsnSQELLETGIKVIDLM 80
Cdd:PRK04196  60 TGLDLKDtkvrfTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPVAREY--PEEFIQTGISAIDGL 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  81 CPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYS---VFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPP 157
Cdd:PRK04196 138 NTLVRGQKLPIFSGSGLPHNELAAQIARQAKVLGEEENfavVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPA 217

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490432834 158 GNRL---RVAltgLTMAE--KFrDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGY 211
Cdd:PRK04196 218 IERIltpRMA---LTAAEylAF-EKGMHVLVILTDMTNYCEALREISAAREEVPGRRGY 272
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
 16-211 3.40e-15

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 73.28  E-value: 3.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  16 EHPIEVPVGKAtlGRIMNVLGE---PVD-----MKGEIGEEE------RWAIHRAAPSYEELsNSQELLETGIKVIDLMC 81
Cdd:PRK04192 146 EHKIMVPPGVS--GTVKEIVSEgdyTVDdtiavLEDEDGEGVeltmmqKWPVRRPRPYKEKL-PPVEPLITGQRVIDTFF 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  82 PFAKGGKVGLFGGAGVGKTVnmmeLIRNIAiehsGYS-----VFAGVGERtreGNdfyhEMTDsnVIdkvslvygqmNEP 156
Cdd:PRK04192 223 PVAKGGTAAIPGPFGSGKTV----TQHQLA----KWAdadivIYVGCGER---GN----EMTE--VL----------EEF 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834 157 P-------GNRL--R-----------VA------LTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVG 210
Cdd:PRK04192 276 PelidpktGRPLmeRtvliantsnmpVAareasiYTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEG 355


                 .
gi 490432834 211 Y 211
Cdd:PRK04192 356 Y 356
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
 1-211 8.58e-14

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 69.29  E-value: 8.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   1 GSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEErwaIHRAAPSYEELSNSQ--ELLETGIKVID 78
Cdd:PRK02118  56 GGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGEP---IEIGGPSVNPVKRIVprEMIRTGIPMID 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  79 LMCPFAKGGKVGLFGGAgvGKTVNmmELIRNIAIE-HSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPP 157
Cdd:PRK02118 133 VFNTLVESQKIPIFSVS--GEPYN--ALLARIALQaEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPP 208

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490432834 158 GNRLRVALTGLTMAEKFR-DEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGY 211
Cdd:PRK02118 209 VECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGY 263
atpA CHL00059
ATP synthase CF1 alpha subunit
 4-206 2.08e-13

ATP synthase CF1 alpha subunit


Pssm-ID: 176999 [Multi-domain]  Cd Length: 485  Bit Score: 68.07  E-value: 2.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   4 DGLR--RGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMC 81
Cdd:CHL00059  57 DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMI 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  82 PFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEhSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRL 161
Cdd:CHL00059 137 PIGRGQRELIIGDRQTGKTAVATDTILNQKGQ-NVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQY 215

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 490432834 162 RVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMP 206
Cdd:CHL00059 216 LAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPP 260
PTZ00185 PTZ00185
ATPase alpha subunit; Provisional
 19-211 3.55e-11

ATPase alpha subunit; Provisional


Pssm-ID: 140212 [Multi-domain]  Cd Length: 574  Bit Score: 61.59  E-value: 3.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  19 IEVPVGKATLGRIMNVLGEPVDMkGEIGEEERW--------AIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVG 90
Cdd:PTZ00185 115 LYIPVGAGVLGKVVNPLGHEVPV-GLLTRSRALleseqtlgKVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQREL 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  91 LFGGAGVGKT-------VNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRV 163
Cdd:PTZ00185 194 IVGDRQTGKTsiavstiINQVRINQQILSKNAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLA 273

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 490432834 164 ALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGY 211
Cdd:PTZ00185 274 PYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAY 321
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 102-211 1.16e-09

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 57.34  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  102 NMMELIRNIAIEH-------SGYSVFAGVGERTREGNDFYHEM-------TDSNVIDKVSLVYGQMNEPPGNRLRVALTG 167
Cdd:PRK14698  662 NMPTLLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEFpklkdpkTGKPLMERTVLIANTSNMPVAAREASIYTG 741

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 490432834  168 LTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGY 211
Cdd:PRK14698  742 ITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGY 785
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
 19-211 3.54e-09

V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273410 [Multi-domain]  Cd Length: 466  Bit Score: 55.88  E-value: 3.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   19 IEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVG 98
Cdd:TIGR01040  74 LRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLP 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   99 KTVNMMELIRNIAI-------EHSGYS-----VFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALT 166
Cdd:TIGR01040 154 HNEIAAQICRQAGLvklptkdVHDGHEdnfaiVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRL 233

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 490432834  167 GLTMAEKFRDE-GRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGY 211
Cdd:TIGR01040 234 ALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGF 279
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 24-137 4.72e-05

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 43.86  E-value: 4.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   24 GKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLeTGIKVIDLMCPFAKGGKVGLFGGAGVGKTVNM 103
Cdd:PRK14698  166 GEYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLI-TGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDG 244

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 490432834  104 MELIRN-----IAIEHSgYSVFAGVGERTREGNDFYHEM 137
Cdd:PRK14698  245 DTLILTkefglIKIKDL-YEILDGKGKKTVEGNEEWTEL 282
rho TIGR00767
transcription termination factor Rho; This RNA helicase, the transcription termination factor ...
 65-207 7.13e-05

transcription termination factor Rho; This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding. [Transcription, Transcription factors]


Pssm-ID: 162030 [Multi-domain]  Cd Length: 415  Bit Score: 42.75  E-value: 7.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   65 NSQELLETG-----IKVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSG-YSVFAGVGERTREgndfyheMT 138
Cdd:TIGR00767 142 NERLRLETStedlsTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEvELIVLLIDERPEE-------VT 214

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490432834  139 DSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPS 207
Cdd:TIGR00767 215 DMQRSVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKVLS 283
PRK12608 PRK12608
transcription termination factor Rho; Provisional
 5-204 1.10e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237150 [Multi-domain]  Cd Length: 380  Bit Score: 42.38  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834   5 GLRRGLDVKDLEHPIEvpvGKATLGRIMNVLGEPvdmkgeigeEERWAihrAAPSYEELS--NSQE--LLETG-----IK 75
Cdd:PRK12608  58 NLRTGDVVEGVARPRE---RYRVLVRVDSVNGTD---------PEKLA---RRPHFDDLTplHPRErlRLETGsddlsMR 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  76 VIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAG-VGERTREGNDFYHEMTdsnvidkvSLVYGQMN 154
Cdd:PRK12608 123 VVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDMRRSVK--------GEVYASTF 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490432834 155 -EPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGR 204
Cdd:PRK12608 195 dRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAYNNEVESSGR 245
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 85-205 3.22e-04

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: 39.66  E-value: 3.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834    85 KGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGvgertregndfyhEMTDSNVIDKVSLVYGQMNEPPGNRLRVA 164
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG-------------EDILEEVLDQLLLIIVGGKKASGSGELRL 67

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 490432834   165 LTGLTMAEKFRDEgrdvLLFVDNIYRYTLAGTEVSALLGRM 205
Cdd:smart00382  68 RLALALARKLKPD----VLILDEITSLLDAEQEALLLLLEE 104
rho_factor_C cd01128
C-terminal ATP binding domain of transcription termination factor rho; Transcription ...
 75-190 3.89e-03

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: 37.18  E-value: 3.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490432834  75 KVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAG-VGERTREgndfyheMTDSNVIDKVSLVYGQM 153
Cdd:cd01128    5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEE-------VTDMRRSVKGEVVASTF 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 490432834 154 NEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYR 190
Cdd:cd01128   78 DEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITR 114
 
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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