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Conserved domains on  [gi|335346105|gb|AEH41571|]
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ATP synthase beta subunit, partial [Erwinia typographi]

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 4.30e-164

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: 460.33  E-value: 4.30e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   1 GSSDGLKRSLDVTDLKHPIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLM 80
Cdd:COG0055   61 DSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLL 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  81 CPFAKGGKVGLFGGAGVGKTVNMMELIRNIAAEHSGFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNR 160
Cdd:COG0055  141 APYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGAR 220

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 335346105 161 LRVALTGLTMAEKFR-EEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 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 4.30e-164

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: 460.33  E-value: 4.30e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   1 GSSDGLKRSLDVTDLKHPIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLM 80
Cdd:COG0055   61 DSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLL 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  81 CPFAKGGKVGLFGGAGVGKTVNMMELIRNIAAEHSGFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNR 160
Cdd:COG0055  141 APYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGAR 220

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 335346105 161 LRVALTGLTMAEKFR-EEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 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 1.63e-152

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: 431.07  E-value: 1.63e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105    1 GSSDGLKRSLDVTDLKHPIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLM 80
Cdd:TIGR01039  58 GSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLL 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   81 CPFAKGGKVGLFGGAGVGKTVNMMELIRNIAAEHSGFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNR 160
Cdd:TIGR01039 138 APYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGAR 217

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 335346105  161 LRVALTGLTMAEKFR-EEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 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 1.26e-139

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: 391.20  E-value: 1.26e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  20 EVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGK 99
Cdd:cd01133    1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105 100 TVNMMELIRNIAAEHSGFSVFAGVGERTREGNDFYHEMTDSNVI-----DKVSLVYGQMNEPPGNRLRVALTGLTMAEKF 174
Cdd:cd01133   81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVInldglSKVALVYGQMNEPPGARARVALTGLTMAEYF 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 335346105 175 R-EEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:cd01133  161 RdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPT 201
atpB CHL00060
ATP synthase CF1 beta subunit
 2-214 1.72e-124

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 360.90  E-value: 1.72e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   2 SSDGLKRSLDVTDLKHPIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLMC 81
Cdd:CHL00060  77 ATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLA 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  82 PFAKGGKVGLFGGAGVGKTVNMMELIRNIAAEHSGFSVFAGVGERTREGNDFYHEMTDSNVID-------KVSLVYGQMN 154
Cdd:CHL00060 157 PYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMN 236

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 335346105 155 EPPGNRLRVALTGLTMAEKFREEGR-DVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 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 1.01e-60

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: 188.72  E-value: 1.01e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   73 GIKVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAAehsGFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQ 152
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 335346105  153 MNEPPGNRLRVALTGLTMAEKFREEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:pfam00006  78 SDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPS 139
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 85-205 5.26e-05

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: 41.98  E-value: 5.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105    85 KGGKVGLFGGAGVGKTVNMMELIRNIAAEHSGFSVFAGvgertregndfyhEMTDSNVIDKVSLVYGQMNEPPGNRLRVA 164
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG-------------EDILEEVLDQLLLIIVGGKKASGSGELRL 67

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 335346105   165 LTGLTMAEKFreegRDVLLFIDNIYRYTLAGTEVSALLGRM 205
Cdd:smart00382  68 RLALALARKL----KPDVLILDEITSLLDAEQEALLLLLEE 104
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-214 4.30e-164

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: 460.33  E-value: 4.30e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   1 GSSDGLKRSLDVTDLKHPIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLM 80
Cdd:COG0055   61 DSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLL 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  81 CPFAKGGKVGLFGGAGVGKTVNMMELIRNIAAEHSGFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNR 160
Cdd:COG0055  141 APYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGAR 220

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 335346105 161 LRVALTGLTMAEKFR-EEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 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 1.63e-152

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: 431.07  E-value: 1.63e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105    1 GSSDGLKRSLDVTDLKHPIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLM 80
Cdd:TIGR01039  58 GSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLL 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   81 CPFAKGGKVGLFGGAGVGKTVNMMELIRNIAAEHSGFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNR 160
Cdd:TIGR01039 138 APYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGAR 217

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 335346105  161 LRVALTGLTMAEKFR-EEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 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 1.26e-139

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: 391.20  E-value: 1.26e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  20 EVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGK 99
Cdd:cd01133    1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105 100 TVNMMELIRNIAAEHSGFSVFAGVGERTREGNDFYHEMTDSNVI-----DKVSLVYGQMNEPPGNRLRVALTGLTMAEKF 174
Cdd:cd01133   81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVInldglSKVALVYGQMNEPPGARARVALTGLTMAEYF 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 335346105 175 R-EEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:cd01133  161 RdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPT 201
atpB CHL00060
ATP synthase CF1 beta subunit
 2-214 1.72e-124

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 360.90  E-value: 1.72e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   2 SSDGLKRSLDVTDLKHPIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLMC 81
Cdd:CHL00060  77 ATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLA 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  82 PFAKGGKVGLFGGAGVGKTVNMMELIRNIAAEHSGFSVFAGVGERTREGNDFYHEMTDSNVID-------KVSLVYGQMN 154
Cdd:CHL00060 157 PYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMN 236

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 335346105 155 EPPGNRLRVALTGLTMAEKFREEGR-DVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:CHL00060 237 EPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPT 297
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 21-214 1.69e-88

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: 261.62  E-value: 1.69e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  21 VPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKT 100
Cdd:cd19476    2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105 101 VNMMELIRNIAAEHSGFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFREEGRD 180
Cdd:cd19476   82 VLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 335346105 181 VLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:cd19476  162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPY 195
alt_F1F0_F1_bet TIGR03305
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ...
 2-214 3.82e-88

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: 266.69  E-value: 3.82e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105    2 SSDGLKRSLDVTDLKHPIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLMC 81
Cdd:TIGR03305  54 PTQGLARGMPVRDSGGPLKAPVGKPTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLV 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   82 PFAKGGKVGLFGGAGVGKTVNMMELIRNIAAEHSGFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRL 161
Cdd:TIGR03305 134 PLERGGKAGLFGGAGVGKTVLLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARF 213

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 335346105  162 RVALTGLTMAEKFR-EEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:TIGR03305 214 RVGHTALTMAEYFRdDEKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPT 267
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 73-214 1.01e-60

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: 188.72  E-value: 1.01e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   73 GIKVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAAehsGFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQ 152
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 335346105  153 MNEPPGNRLRVALTGLTMAEKFREEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:pfam00006  78 SDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPS 139
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 20-214 1.08e-42

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: 144.62  E-value: 1.08e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  20 EVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGK 99
Cdd:cd01136    1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105 100 TVNMMELIRNIAAEhsgFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFREEGR 179
Cdd:cd01136   81 STLLGMIARNTDAD---VNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGK 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 335346105 180 DVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:cd01136  158 KVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPS 192
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 1-214 4.48e-39

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: 139.01  E-value: 4.48e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   1 GSSDGLKRSLDVTDLKHPIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLM 80
Cdd:COG1157   72 GDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGL 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  81 CPFAKGGKVGLFGGAGVGKTVNMMELIRNIAAEhsgFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNR 160
Cdd:COG1157  152 LTVGRGQRIGIFAGSGVGKSTLLGMIARNTEAD---VNVIALIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMR 228

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 335346105 161 LRVALTGLTMAEKFREEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:COG1157  229 LRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPS 282
PRK08149 PRK08149
FliI/YscN family ATPase;
1-211 2.48e-32

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 120.87  E-value: 2.48e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   1 GSSDGLKRSLDVTDLKHPIEVPVGVATLGRIMNVLG---EPIDMKGDIGEEERW-AIHRAAPSYEDQSNSQELLETGIKV 76
Cdd:PRK08149  62 GNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGkivERFDAPPTVGPISEErVIDVAPPSYAERRPIREPLITGVRA 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  77 ID--LMCpfAKGGKVGLFGGAGVGKTVNMMELIRNIAAEhsgFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMN 154
Cdd:PRK08149 142 IDglLTC--GVGQRMGIFASAGCGKTSLMNMLIEHSEAD---VFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSD 216

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 335346105 155 EPPGNRLRVALTGLTMAEKFREEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGY 211
Cdd:PRK08149 217 FSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGY 273
fliI PRK08472
flagellar protein export ATPase FliI;
15-214 2.82e-32

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 120.95  E-value: 2.82e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  15 LKHPIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLMCPFAKGGKVGLFGG 94
Cdd:PRK08472  86 SKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAG 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  95 AGVGKTVNMMELIRNIAAEhsgFSVFAGVGERTREGNDFYHEMTDSNVIDKVsLVYGQMNEPPGNRLRVALTGLTMAEKF 174
Cdd:PRK08472 166 SGVGKSTLMGMIVKGCLAP---IKVVALIGERGREIPEFIEKNLGGDLENTV-IVVATSDDSPLMRKYGAFCAMSVAEYF 241

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 335346105 175 REEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK08472 242 KNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPS 281
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
2-214 1.64e-30

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 116.07  E-value: 1.64e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   2 SSDGLKRSLDVTDLKHPIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERwAIHRAAPSYEDQSNSQELLETGIKVIDLMC 81
Cdd:PRK06820  80 SSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWR-ELDCPPPSPLTRQPIEQMLTTGIRAIDGIL 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  82 PFAKGGKVGLFGGAGVGKTVNMMELIRNIAAEhsgFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRL 161
Cdd:PRK06820 159 SCGEGQRIGIFAAAGVGKSTLLGMLCADSAAD---VMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERL 235

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 335346105 162 RVALTGLTMAEKFREEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK06820 236 KGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPS 288
fliI PRK06002
flagellar protein export ATPase FliI;
29-214 2.04e-30

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 116.25  E-value: 2.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  29 GRIMNVLGEPIDMKGDIGE-EERWAIHRAAPSYEDQSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKT--VNMMe 105
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKStlLAML- 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105 106 lirniaAEHSGFS--VFAGVGERTREGNDFYHEMTDSNvIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFREEGRDVLL 183
Cdd:PRK06002 186 ------ARADAFDtvVIALVGERGREVREFLEDTLADN-LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLL 258

                        170       180       190
                 ....*....|....*....|....*....|.
gi 335346105 184 FIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK06002 259 IVDSVTRFAHAAREVALAAGEPPVARGYPPS 289
fliI PRK08972
flagellar protein export ATPase FliI;
12-214 5.71e-29

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 112.10  E-value: 5.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  12 VTDLKHPIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERwaIHRAAPSYEDQSNSQ--ELLETGIKVIDLMCPFAKGGKV 89
Cdd:PRK08972  88 VTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQR--ASRHSPPINPLSRRPitEPLDVGVRAINAMLTVGKGQRM 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  90 GLFGGAGVGKTVNMMELIRNIAAEhsgFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLT 169
Cdd:PRK08972 166 GLFAGSGVGKSVLLGMMTRGTTAD---VIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCETATT 242

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 335346105 170 MAEKFREEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK08972 243 IAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPS 287
fliI PRK08927
flagellar protein export ATPase FliI;
1-214 1.68e-28

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 110.84  E-value: 1.68e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   1 GSSDGLKRSLDVTDLKHPIEVPVGVATLGRIMNVLGEPIDMKGDIGE-EERWAIHRAAPSYEDQSNSQELLETGIKVIDL 79
Cdd:PRK08927  72 GPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQgPVPYPLRAPPPPAHSRARVGEPLDLGVRALNT 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  80 MCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAAEhsgFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGN 159
Cdd:PRK08927 152 FLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALM 228

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 335346105 160 RLRVALTGLTMAEKFREEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK08927 229 RRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPT 283
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 1-214 1.32e-27

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 108.32  E-value: 1.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   1 GSSDGLKRSLDVTDLKHPIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLM 80
Cdd:PRK09099  78 GELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGL 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  81 CPFAKGGKVGLFGGAGVGKTVNMMELIRNIAAEhsgFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNR 160
Cdd:PRK09099 158 MTLGEGQRMGIFAPAGVGKSTLMGMFARGTQCD---VNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIER 234

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 335346105 161 LRVALTGLTMAEKFREEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK09099 235 AKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPS 288
atpA TIGR00962
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ...
 1-206 6.42e-27

proton translocating ATP synthase, F1 alpha 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. The alpha-subunit contains a highly conserved adenine-specific noncatalytic nucleotide-binding domain. The conserved amino acid sequence is Gly-X-X-X-X-Gly-Lys. Proton translocating ATP synthase F1, alpha subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), B subunit. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 273365 [Multi-domain]  Cd Length: 501  Bit Score: 107.09  E-value: 6.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105    1 GSSDGLKRSLDVTDLKHPIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLM 80
Cdd:TIGR00962  76 GDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAM 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   81 CPFAKGGKVGLFGGAGVGKTVNMMELIRNIAAEHSgFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNR 160
Cdd:TIGR00962 156 IPIGRGQRELIIGDRQTGKTAVAIDTIINQKDSDV-YCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQ 234

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 335346105  161 LRVALTGLTMAEKFREEGRDVLLFIDNIYRYTLAGTEVSALLGRMP 206
Cdd:TIGR00962 235 YLAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPP 280
fliI PRK07196
flagellar protein export ATPase FliI;
20-214 4.04e-26

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 104.20  E-value: 4.04e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  20 EVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGK 99
Cdd:PRK07196  89 ELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGK 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105 100 TVNMMELIRNIAAEhsgFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFREEGR 179
Cdd:PRK07196 169 SVLLGMITRYTQAD---VVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGH 245

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 335346105 180 DVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK07196 246 DVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPS 280
fliI PRK07721
flagellar protein export ATPase FliI;
18-214 1.12e-25

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 102.88  E-value: 1.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  18 PIEVPVGVATLGRIMNVLGEPIDM----KGDigeeERWAIHRAAPSYEDQSNSQELLETGIKVIDLMCPFAKGGKVGLFG 93
Cdd:PRK07721  90 PLEVKVGSGLIGQVLDALGEPLDGsalpKGL----APVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFA 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  94 GAGVGKTVNMMELIRNIAAEhsgFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEK 173
Cdd:PRK07721 166 GSGVGKSTLMGMIARNTSAD---LNVIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEY 242

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 335346105 174 FREEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK07721 243 FRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPS 283
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
1-213 6.76e-25

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 100.80  E-value: 6.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   1 GSSDGLKRSLDVTDLKHPIEVPVGVATLGRIMNVLGEPIDMKGDigEEERWAIHRA--APSYEDQSNSQELLeTGIKVID 78
Cdd:PRK07594  71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGREL--PDVCWKDYDAmpPPAMVRQPITQPLM-TGIRAID 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  79 LMCPFAKGGKVGLFGGAGVGKTVNMMELIrniAAEHSGFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPG 158
Cdd:PRK07594 148 SVATCGEGQRVGIFSAPGVGKSTLLAMLC---NAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPAL 224

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 335346105 159 NRLRVALTGLTMAEKFREEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQP 213
Cdd:PRK07594 225 ERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPP 279
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
20-214 8.81e-25

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 100.60  E-value: 8.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  20 EVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGK 99
Cdd:PRK06936  96 QVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGK 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105 100 TVNMMELIRNIAAEhsgFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFREEGR 179
Cdd:PRK06936 176 STLLASLIRSAEVD---VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGK 252

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 335346105 180 DVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK06936 253 RVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPS 287
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 1-206 6.12e-24

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 98.45  E-value: 6.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   1 GSSDGLKRSLDVTDLKHPIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLM 80
Cdd:PRK13343  77 DDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDAL 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  81 CPFAKGGKVGLFGGAGVGKTVNMMELIrnIAAEHSG-FSVFAGVGERTRegndfyhemTDSNVIDKV---------SLVY 150
Cdd:PRK13343 157 IPIGRGQRELIIGDRQTGKTAIAIDAI--INQKDSDvICVYVAIGQKAS---------AVARVIETLrehgaleytTVVV 225

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 335346105 151 GQMNEPPGNRLRVALTGLTMAEKFREEGRDVLLFIDNIYRYTLAGTEVSALLGRMP 206
Cdd:PRK13343 226 AEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPP 281
fliI PRK05688
flagellar protein export ATPase FliI;
1-214 5.85e-23

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 95.57  E-value: 5.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   1 GSSDGLKRSLDVTDLKHPIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLM 80
Cdd:PRK05688  83 GSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGL 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  81 CPFAKGGKVGLFGGAGVGKTVNMMELIRNIAAEhsgFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNR 160
Cdd:PRK05688 163 LTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEAD---IIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMR 239

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 335346105 161 LRVALTGLTMAEKFREEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK05688 240 LRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPS 293
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 19-206 2.47e-22

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: 91.47  E-value: 2.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  19 IEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVG 98
Cdd:cd01132    2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  99 KTVNMMELIRNIAAEHSgFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFREEG 178
Cdd:cd01132   82 KTAIAIDTIINQKGKKV-YCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160

                        170       180
                 ....*....|....*....|....*...
gi 335346105 179 RDVLLFIDNIYRYTLAGTEVSALLGRMP 206
Cdd:cd01132  161 KHALIIYDDLSKQAVAYRQMSLLLRRPP 188
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 18-211 2.76e-22

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: 91.51  E-value: 2.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  18 PIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGV 97
Cdd:cd01135    1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  98 GKTVNMMELIRN--IAAEHSGFS-VFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKF 174
Cdd:cd01135   81 PHNELAAQIARQagVVGSEENFAiVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYL 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 335346105 175 R-EEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGY 211
Cdd:cd01135  161 AyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGY 198
PRK05922 PRK05922
type III secretion system ATPase; Validated
 11-211 1.57e-21

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 91.50  E-value: 1.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  11 DVTDLKHPIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLMCPFAKGGKVG 90
Cdd:PRK05922  82 EVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIG 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  91 LFGGAGVGKTvnmmELIRNIA-AEHSGFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLT 169
Cdd:PRK05922 162 VFSEPGSGKS----SLLSTIAkGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMT 237

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 335346105 170 MAEKFREEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGY 211
Cdd:PRK05922 238 IAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHY 279
fliI PRK06793
flagellar protein export ATPase FliI;
12-206 1.08e-20

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 88.88  E-value: 1.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  12 VTDLKHPIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLMCPFAKGGKVGL 91
Cdd:PRK06793  82 VTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGI 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  92 FGGAGVGKTVNMMELIRNIAAEhsgFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMA 171
Cdd:PRK06793 162 FAGSGVGKSTLLGMIAKNAKAD---INVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIA 238

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 335346105 172 EKFREEGRDVLLFIDNIYRYTLAGTEVSALLGRMP 206
Cdd:PRK06793 239 EYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP 273
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
 4-211 1.48e-18

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: 81.47  E-value: 1.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   4 DGLKRSLDVTDLKHPIEVPVGVATlgrimnvlgepidmkgdigeeERWAIHRAAPSYEDQSnSQELLETGIKVIDLMCPF 83
Cdd:cd01134   16 DGIQRPLEVIAETGSIFIPRGVNV---------------------QRWPVRQPRPVKEKLP-PNVPLLTGQRVLDTLFPV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  84 AKGGKVGLFGGAGVGKTVNMMELIRNIAAEhsgFSVFAGVGER----TREGNDFYH---EMTDSNVIDKVSLVYGQMNEP 156
Cdd:cd01134   74 AKGGTAAIPGPFGCGKTVISQSLSKWSNSD---VVIYVGCGERgnemAEVLEEFPElkdPITGESLMERTVLIANTSNMP 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 335346105 157 PGNRLRVALTGLTMAEKFREEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGY 211
Cdd:cd01134  151 VAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGY 205
fliI PRK07960
flagellum-specific ATP synthase FliI;
20-214 3.78e-18

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 81.75  E-value: 3.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  20 EVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGK 99
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105 100 TVNMMELIRNIAAEhsgFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFREEGR 179
Cdd:PRK07960 189 SVLLGMMARYTQAD---VIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQ 265

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 335346105 180 DVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT 214
Cdd:PRK07960 266 HVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPS 300
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
 17-211 4.12e-17

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 78.71  E-value: 4.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  17 HPIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAA--PSYEDQsnSQELLETGIKVIDLMCPFAKGGKVGLFGG 94
Cdd:PRK04196  74 EPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPVAREY--PEEFIQTGISAIDGLNTLVRGQKLPIFSG 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  95 AGVGKTVNMMELIRN--IAAEHSGFS-VFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRL---RVAltgL 168
Cdd:PRK04196 152 SGLPHNELAAQIARQakVLGEEENFAvVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERIltpRMA---L 228

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 335346105 169 TMAE--KFrEEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGY 211
Cdd:PRK04196 229 TAAEylAF-EKGMHVLVILTDMTNYCEALREISAAREEVPGRRGY 272
AtpA COG0056
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ...
 1-206 4.28e-17

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


Pssm-ID: 439826 [Multi-domain]  Cd Length: 504  Bit Score: 78.93  E-value: 4.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   1 GSSDGLKRSLDVTDLKHPIEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLM 80
Cdd:COG0056   77 GDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAM 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  81 CPFAKGGKVGLFGGAGVGKTVNMMELIrnIAAEHSG-FSVFAGVGERtregndfyhEMTDSNVIDKVSlVYGQM------ 153
Cdd:COG0056  157 IPIGRGQRELIIGDRQTGKTAIAIDTI--INQKGKDvICIYVAIGQK---------ASTVAQVVETLE-EHGAMeytivv 224

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 335346105 154 ----NEPPGNRLRVALTGLTMAEKFREEGRDVLLFIDNI------YRytlagtEVSALLGRMP 206
Cdd:COG0056  225 aataSDPAPLQYIAPYAGCAMGEYFMDQGKDVLIVYDDLskhavaYR------ELSLLLRRPP 281
PRK09281 PRK09281
F0F1 ATP synthase subunit alpha; Validated
 19-206 3.36e-16

F0F1 ATP synthase subunit alpha; Validated


Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 76.26  E-value: 3.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  19 IEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVG 98
Cdd:PRK09281  95 LEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTG 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  99 KTVNMMELIrnIAAEHSG-FSVFAGVGERtregndfyhEMTDSNVIDKVSlVYGQM----------NEPPGNRLRVALTG 167
Cdd:PRK09281 175 KTAIAIDTI--INQKGKDvICIYVAIGQK---------ASTVAQVVRKLE-EHGAMeytivvaataSDPAPLQYLAPYAG 242

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 335346105 168 LTMAEKFREEGRDVLLFIDNI------YRytlagtEVSALLGRMP 206
Cdd:PRK09281 243 CAMGEYFMDNGKDALIVYDDLskqavaYR------QLSLLLRRPP 281
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
 16-211 1.34e-14

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 71.74  E-value: 1.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  16 KHPIEVPVGVAtlGRIMNVLG-------EPI---DMKGDIGEE----ERWAIHRAAPsYEDQSNSQELLETGIKVIDLMC 81
Cdd:PRK04192 146 EHKIMVPPGVS--GTVKEIVSegdytvdDTIavlEDEDGEGVEltmmQKWPVRRPRP-YKEKLPPVEPLITGQRVIDTFF 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  82 PFAKGGKVGLFGGAGVGKTVNMMELIRNIAAEhsgFSVFAGVGERtreGNdfyhEMTDsnVIdkvslvygqmNEPP---- 157
Cdd:PRK04192 223 PVAKGGTAAIPGPFGSGKTVTQHQLAKWADAD---IVIYVGCGER---GN----EMTE--VL----------EEFPelid 280

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 335346105 158 ---GNRL--R-----------VA------LTGLTMAEKFREEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGY 211
Cdd:PRK04192 281 pktGRPLmeRtvliantsnmpVAareasiYTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGY 356
atpA CHL00059
ATP synthase CF1 alpha subunit
 20-206 1.42e-13

ATP synthase CF1 alpha subunit


Pssm-ID: 176999 [Multi-domain]  Cd Length: 485  Bit Score: 68.84  E-value: 1.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  20 EVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGK 99
Cdd:CHL00059  75 QIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGK 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105 100 TVNMMELIRNIAAEhSGFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFREEGR 179
Cdd:CHL00059 155 TAVATDTILNQKGQ-NVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGR 233

                        170       180
                 ....*....|....*....|....*..
gi 335346105 180 DVLLFIDNIYRYTLAGTEVSALLGRMP 206
Cdd:CHL00059 234 HTLIIYDDLSKQAQAYRQMSLLLRRPP 260
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
 1-211 1.74e-13

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 68.52  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   1 GSSDGLKRSLDVTDLKHPIEVPVGVATLGRIMNVLGEPIDmKGDIGEEERWAIhrAAPSYEDQSNSQ--ELLETGIKVID 78
Cdd:PRK02118  56 GGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPID-GGPELEGEPIEI--GGPSVNPVKRIVprEMIRTGIPMID 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  79 LMCPFAKGGKVGLFGGAgvGKTVNmmELIRNIAAE-HSGFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPP 157
Cdd:PRK02118 133 VFNTLVESQKIPIFSVS--GEPYN--ALLARIALQaEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPP 208

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 335346105 158 GNRLRVALTGLTMAEKFR-EEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGY 211
Cdd:PRK02118 209 VECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGY 263
PTZ00185 PTZ00185
ATPase alpha subunit; Provisional
 19-211 9.12e-12

ATPase alpha subunit; Provisional


Pssm-ID: 140212 [Multi-domain]  Cd Length: 574  Bit Score: 63.52  E-value: 9.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  19 IEVPVGVATLGRIMNVLGEPIDMkGDIGEEERW--------AIHRAAPSYEDQSNSQELLETGIKVIDLMCPFAKGGKVG 90
Cdd:PTZ00185 115 LYIPVGAGVLGKVVNPLGHEVPV-GLLTRSRALleseqtlgKVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQREL 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  91 LFGGAGVGKT-------VNMMELIRNIAAEHSGFSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRV 163
Cdd:PTZ00185 194 IVGDRQTGKTsiavstiINQVRINQQILSKNAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLA 273

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 335346105 164 ALTGLTMAEKFREEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGY 211
Cdd:PTZ00185 274 PYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAY 321
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
 19-211 9.88e-10

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: 57.42  E-value: 9.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   19 IEVPVGVATLGRIMNVLGEPIDMKGDIGEEERWAIHRAAPSYEDQSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGV- 97
Cdd:TIGR01040  74 LRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLp 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   98 -----GKTVNMMELIRNIAAE-HSG----FS-VFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALT 166
Cdd:TIGR01040 154 hneiaAQICRQAGLVKLPTKDvHDGhednFAiVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRL 233

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 335346105  167 GLTMAEKFR-EEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGY 211
Cdd:TIGR01040 234 ALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGF 279
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 102-211 3.75e-09

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 55.80  E-value: 3.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  102 NMMELIRNIAAEH-------SGFSVFAGVGERTREGNDFYHEM-------TDSNVIDKVSLVYGQMNEPPGNRLRVALTG 167
Cdd:PRK14698  662 NMPTLLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEFpklkdpkTGKPLMERTVLIANTSNMPVAAREASIYTG 741

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 335346105  168 LTMAEKFREEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGY 211
Cdd:PRK14698  742 ITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGY 785
PRK12608 PRK12608
transcription termination factor Rho; Provisional
 70-204 2.44e-06

transcription termination factor Rho; Provisional


Pssm-ID: 237150 [Multi-domain]  Cd Length: 380  Bit Score: 47.00  E-value: 2.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  70 LETG-----IKVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAAEHSGFSVFAG-VGERTREGNDFYHEMTdsnvi 143
Cdd:PRK12608 112 LETGsddlsMRVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDMRRSVK----- 186

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 335346105 144 dkvSLVYGQMN-EPPGNRLRVALTGLTMAEKFREEGRDVLLFIDNIYRYTLAGTEVSALLGR 204
Cdd:PRK12608 187 ---GEVYASTFdRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAYNNEVESSGR 245
rho TIGR00767
transcription termination factor Rho; This RNA helicase, the transcription termination factor ...
 65-207 1.08e-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: 45.45  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   65 NSQELLETG-----IKVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAAEHSG-FSVFAGVGERTREgndfyheMT 138
Cdd:TIGR00767 142 NERLRLETStedlsTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEvELIVLLIDERPEE-------VT 214

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 335346105  139 DSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFREEGRDVLLFIDNIYRYTLAGTEVSALLGRMPS 207
Cdd:TIGR00767 215 DMQRSVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKVLS 283
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 85-205 5.26e-05

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: 41.98  E-value: 5.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105    85 KGGKVGLFGGAGVGKTVNMMELIRNIAAEHSGFSVFAGvgertregndfyhEMTDSNVIDKVSLVYGQMNEPPGNRLRVA 164
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG-------------EDILEEVLDQLLLIIVGGKKASGSGELRL 67

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 335346105   165 LTGLTMAEKFreegRDVLLFIDNIYRYTLAGTEVSALLGRM 205
Cdd:smart00382  68 RLALALARKL----KPDVLILDEITSLLDAEQEALLLLLEE 104
rho_factor_C cd01128
C-terminal ATP binding domain of transcription termination factor rho; Transcription ...
 75-190 1.19e-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: 41.81  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105  75 KVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAAEHSGFSVFAG-VGERTREgndfyheMTDSNVIDKVSLVYGQM 153
Cdd:cd01128    5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEE-------VTDMRRSVKGEVVASTF 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 335346105 154 NEPPGNRLRVALTGLTMAEKFREEGRDVLLFIDNIYR 190
Cdd:cd01128   78 DEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITR 114
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 17-137 1.45e-03

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 39.23  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335346105   17 HPIEVPVGV-------ATLGR--IMNVLGEPIDMKGDIGE---EERWAIHRAAPsYEDQSNSQELLETGIKVIDLMCPFA 84
Cdd:PRK14698  147 HKIMVPPGIegeiveiADEGEytIEEVIAKVKTPSGEIKElkmYQRWPVRVKRP-YKEKLPPEVPLITGQRVIDTFFPQA 225

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 335346105   85 KGGKVGLFGGAGVGKTVNMMELIRN----IAAEHSGFSVFAGVGERTREGNDFYHEM 137
Cdd:PRK14698  226 KGGTAAIPGPFGSGKCVDGDTLILTkefgLIKIKDLYEILDGKGKKTVEGNEEWTEL 282
 
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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