NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|936369950|gb|ALH21753|]
View 

ATP synthase beta chain, partial [Burkholderia sp. BL13-R2]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-215 5.95e-156

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: 439.91  E-value: 5.95e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950   1 YDALILE---GSELTLEVQQQLGDGVVRTICLGASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSE 77
Cdd:COG0055   29 YNALEVEnegGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAK 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  78 TTRAIHQKAPAFDQLSPSTELLETGIKVIDLICPFAKGGKVGLFGGAGVGKTVNMMELINNIAKEHGGYSVFAGVGERTR 157
Cdd:COG0055  109 ERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTR 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 936369950 158 EGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEHFRD-EGLDVLFFVD 215
Cdd:COG0055  189 EGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFID 247
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-215 5.95e-156

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: 439.91  E-value: 5.95e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950   1 YDALILE---GSELTLEVQQQLGDGVVRTICLGASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSE 77
Cdd:COG0055   29 YNALEVEnegGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAK 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  78 TTRAIHQKAPAFDQLSPSTELLETGIKVIDLICPFAKGGKVGLFGGAGVGKTVNMMELINNIAKEHGGYSVFAGVGERTR 157
Cdd:COG0055  109 ERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTR 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 936369950 158 EGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEHFRD-EGLDVLFFVD 215
Cdd:COG0055  189 EGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFID 247
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 1-215 2.73e-138

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: 394.86  E-value: 2.73e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950    1 YDALILE---GSELTLEVQQQLGDGVVRTICLGASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSE 77
Cdd:TIGR01039  26 YNALKVQnraESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950   78 TTRAIHQKAPAFDQLSPSTELLETGIKVIDLICPFAKGGKVGLFGGAGVGKTVNMMELINNIAKEHGGYSVFAGVGERTR 157
Cdd:TIGR01039 106 ERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTR 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 936369950  158 EGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEHFRDE-GLDVLFFVD 215
Cdd:TIGR01039 186 EGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEqGQDVLLFID 244
atpB CHL00060
ATP synthase CF1 beta subunit
 1-215 1.23e-120

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 351.27  E-value: 1.23e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950   1 YDALILEGSE-------LTLEVQQQLGDGVVRTICLGASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGP 73
Cdd:CHL00060  40 YNALVVKGRDtagqeinVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGP 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  74 ISSETTRAIHQKAPAFDQLSPSTELLETGIKVIDLICPFAKGGKVGLFGGAGVGKTVNMMELINNIAKEHGGYSVFAGVG 153
Cdd:CHL00060 120 VDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVG 199

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 154 ERTREGNDFYHEMKDSNVLD-------KVALVYGQMNEPPGNRLRVALTGLTMAEHFRDEGL-DVLFFVD 215
Cdd:CHL00060 200 ERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFID 269
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 49-215 6.40e-116

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: 331.49  E-value: 6.40e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  49 SVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIHQKAPAFDQLSPSTELLETGIKVIDLICPFAKGGKVGLFGGAGVGK 128
Cdd:cd01133    1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 129 TVNMMELINNIAKEHGGYSVFAGVGERTREGNDFYHEMKDSNV-----LDKVALVYGQMNEPPGNRLRVALTGLTMAEHF 203
Cdd:cd01133   81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVinldgLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160

                        170
                 ....*....|...
gi 936369950 204 RD-EGLDVLFFVD 215
Cdd:cd01133  161 RDeEGQDVLLFID 173
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 102-215 1.29e-47

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: 155.59  E-value: 1.29e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  102 GIKVIDLICPFAKGGKVGLFGGAGVGKTVNMMELINNIAKehgGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQ 181
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 936369950  182 MNEPPGNRLRVALTGLTMAEHFRDEGLDVLFFVD 215
Cdd:pfam00006  78 SDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMD 111
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 114-173 7.03e-03

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: 35.81  E-value: 7.03e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950   114 KGGKVGLFGGAGVGKTVNMMELINNIAKEHGGYSVFAGVGERTREGNDFYHEMKDSNVLD 173
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS 60
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-215 5.95e-156

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: 439.91  E-value: 5.95e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950   1 YDALILE---GSELTLEVQQQLGDGVVRTICLGASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSE 77
Cdd:COG0055   29 YNALEVEnegGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAK 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  78 TTRAIHQKAPAFDQLSPSTELLETGIKVIDLICPFAKGGKVGLFGGAGVGKTVNMMELINNIAKEHGGYSVFAGVGERTR 157
Cdd:COG0055  109 ERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTR 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 936369950 158 EGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEHFRD-EGLDVLFFVD 215
Cdd:COG0055  189 EGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFID 247
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 1-215 2.73e-138

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: 394.86  E-value: 2.73e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950    1 YDALILE---GSELTLEVQQQLGDGVVRTICLGASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSE 77
Cdd:TIGR01039  26 YNALKVQnraESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950   78 TTRAIHQKAPAFDQLSPSTELLETGIKVIDLICPFAKGGKVGLFGGAGVGKTVNMMELINNIAKEHGGYSVFAGVGERTR 157
Cdd:TIGR01039 106 ERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTR 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 936369950  158 EGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEHFRDE-GLDVLFFVD 215
Cdd:TIGR01039 186 EGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEqGQDVLLFID 244
atpB CHL00060
ATP synthase CF1 beta subunit
 1-215 1.23e-120

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 351.27  E-value: 1.23e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950   1 YDALILEGSE-------LTLEVQQQLGDGVVRTICLGASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGP 73
Cdd:CHL00060  40 YNALVVKGRDtagqeinVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGP 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  74 ISSETTRAIHQKAPAFDQLSPSTELLETGIKVIDLICPFAKGGKVGLFGGAGVGKTVNMMELINNIAKEHGGYSVFAGVG 153
Cdd:CHL00060 120 VDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVG 199

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 154 ERTREGNDFYHEMKDSNVLD-------KVALVYGQMNEPPGNRLRVALTGLTMAEHFRDEGL-DVLFFVD 215
Cdd:CHL00060 200 ERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFID 269
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 49-215 6.40e-116

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: 331.49  E-value: 6.40e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  49 SVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIHQKAPAFDQLSPSTELLETGIKVIDLICPFAKGGKVGLFGGAGVGK 128
Cdd:cd01133    1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 129 TVNMMELINNIAKEHGGYSVFAGVGERTREGNDFYHEMKDSNV-----LDKVALVYGQMNEPPGNRLRVALTGLTMAEHF 203
Cdd:cd01133   81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVinldgLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160

                        170
                 ....*....|...
gi 936369950 204 RD-EGLDVLFFVD 215
Cdd:cd01133  161 RDeEGQDVLLFID 173
alt_F1F0_F1_bet TIGR03305
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ...
 9-215 3.18e-87

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: 264.38  E-value: 3.18e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950    9 SELTLEVQQQLGDGVVRTICLGASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIHQKAPA 88
Cdd:TIGR03305  32 GEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKPTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPT 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950   89 FDQLSPSTELLETGIKVIDLICPFAKGGKVGLFGGAGVGKTVNMMELINNIAKEHGGYSVFAGVGERTREGNDFYHEMKD 168
Cdd:TIGR03305 112 LTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKE 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 936369950  169 SNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEHFR-DEGLDVLFFVD 215
Cdd:TIGR03305 192 AGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRdDEKQDVLLLID 239
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 49-215 3.51e-77

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: 232.73  E-value: 3.51e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  49 SVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIHQKAPAFDQLSPSTELLETGIKVIDLICPFAKGGKVGLFGGAGVGK 128
Cdd:cd19476    1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 129 TVNMMELINNIAKEHGGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEHFRDEGL 208
Cdd:cd19476   81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160


                 ....*..
gi 936369950 209 DVLFFVD 215
Cdd:cd19476  161 HVLLIID 167
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 102-215 1.29e-47

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: 155.59  E-value: 1.29e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  102 GIKVIDLICPFAKGGKVGLFGGAGVGKTVNMMELINNIAKehgGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQ 181
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 936369950  182 MNEPPGNRLRVALTGLTMAEHFRDEGLDVLFFVD 215
Cdd:pfam00006  78 SDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMD 111
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 29-215 1.13e-41

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: 145.94  E-value: 1.13e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  29 LGASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIHQKAPAFDQLSPSTELLETGIKVIDL 108
Cdd:COG1157   71 LGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDG 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 109 ICPFAKGGKVGLFGGAGVGKTVnmmeLINNIAKehggYS-----VFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMN 183
Cdd:COG1157  151 LLTVGRGQRIGIFAGSGVGKST----LLGMIAR----NTeadvnVIALIGERGREVREFIEDDLGEEGLARSVVVVATSD 222

                        170       180       190
                 ....*....|....*....|....*....|..
gi 936369950 184 EPPGNRLRVALTGLTMAEHFRDEGLDVLFFVD 215
Cdd:COG1157  223 EPPLMRLRAAYTATAIAEYFRDQGKNVLLLMD 254
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 49-215 1.13e-35

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: 126.52  E-value: 1.13e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  49 SVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIHQKAPAFDQLSPSTELLETGIKVIDLICPFAKGGKVGLFGGAGVGK 128
Cdd:cd01136    1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 129 TVNMMELINNIAKEhggYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEHFRDEGL 208
Cdd:cd01136   81 STLLGMIARNTDAD---VNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGK 157


                 ....*..
gi 936369950 209 DVLFFVD 215
Cdd:cd01136  158 KVLLLMD 164
PRK08149 PRK08149
FliI/YscN family ATPase;
29-215 4.79e-34

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 125.49  E-value: 4.79e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  29 LGASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDE-AGPISSET---TRAIHQKAPAFDQLSPSTELLETGIK 104
Cdd:PRK08149  61 IGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERfDAPPTVGPiseERVIDVAPPSYAERRPIREPLITGVR 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 105 VID--LICpfAKGGKVGLFGGAGVGKTVNMMELInniakEHGGYSVF--AGVGERTREGNDFYHEMKDSNVLDKVALVYG 180
Cdd:PRK08149 141 AIDglLTC--GVGQRMGIFASAGCGKTSLMNMLI-----EHSEADVFviGLIGERGREVTEFVESLRASSRREKCVLVYA 213

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 936369950 181 QMNEPPGNRLRVALTGLTMAEHFRDEGLDVLFFVD 215
Cdd:PRK08149 214 TSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFID 248
atpA TIGR00962
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ...
 24-215 2.60e-31

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: 119.03  E-value: 2.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950   24 VRTICLGASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIHQKAPAFDQLSPSTELLETGI 103
Cdd:TIGR00962  70 VGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGI 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  104 KVIDLICPFAKGGKVGLFGGAGVGKTVNMMELINNiAKEHGGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMN 183
Cdd:TIGR00962 150 KAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTIIN-QKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATAS 228

                         170       180       190
                  ....*....|....*....|....*....|..
gi 936369950  184 EPPGNRLRVALTGLTMAEHFRDEGLDVLFFVD 215
Cdd:TIGR00962 229 DSASLQYLAPYTGCTMGEYFRDNGKHALIIYD 260
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
32-215 4.38e-28

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 109.52  E-value: 4.38e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  32 SDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSEtTRAIHQKAPAFDQLSPSTELLETGIKVIDLICP 111
Cdd:PRK06820  81 SDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQ-WRELDCPPPSPLTRQPIEQMLTTGIRAIDGILS 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 112 FAKGGKVGLFGGAGVGKTVnmmeLINNIAKE-HGGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRL 190
Cdd:PRK06820 160 CGEGQRIGIFAAAGVGKST----LLGMLCADsAADVMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERL 235

                        170       180
                 ....*....|....*....|....*
gi 936369950 191 RVALTGLTMAEHFRDEGLDVLFFVD 215
Cdd:PRK06820 236 KGLSTATTIAEYFRDRGKKVLLMAD 260
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 27-215 6.81e-28

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 109.62  E-value: 6.81e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  27 ICLGASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIHQKAPAFDQLSPSTELLETGIKVI 106
Cdd:PRK13343  74 VLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVV 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 107 DLICPFAKGGKVGLFGGAGVGKTVNMMELINNiAKEHGGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPP 186
Cdd:PRK13343 154 DALIPIGRGQRELIIGDRQTGKTAIAIDAIIN-QKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPP 232

                        170       180
                 ....*....|....*....|....*....
gi 936369950 187 GNRLRVALTGLTMAEHFRDEGLDVLFFVD 215
Cdd:PRK13343 233 GLQYLAPFAGCAIAEYFRDQGQDALIVYD 261
fliI PRK07721
flagellar protein export ATPase FliI;
38-215 1.25e-25

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 102.88  E-value: 1.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  38 GTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIHQKAPAFDQLSPSTELLETGIKVIDLICPFAKGGK 117
Cdd:PRK07721  81 GCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQR 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 118 VGLFGGAGVGKTVnmmeLINNIAKE-HGGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTG 196
Cdd:PRK07721 161 VGIFAGSGVGKST----LMGMIARNtSADLNVIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTA 236

                        170
                 ....*....|....*....
gi 936369950 197 LTMAEHFRDEGLDVLFFVD 215
Cdd:PRK07721 237 TAIAEYFRDQGLNVMLMMD 255
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 30-215 3.89e-25

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 101.38  E-value: 3.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  30 GASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIHQKAPafDQLspSTELLE----TGIKV 105
Cdd:PRK09099  78 GELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPP--DPM--SRRMVEaplpTGVRI 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 106 IDLICPFAKGGKVGLFGGAGVGKTVNMMELINNIAKEhggYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEP 185
Cdd:PRK09099 154 VDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQCD---VNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRS 230

                        170       180       190
                 ....*....|....*....|....*....|
gi 936369950 186 PGNRLRVALTGLTMAEHFRDEGLDVLFFVD 215
Cdd:PRK09099 231 SIERAKAAYVATAIAEYFRDRGLRVLLMMD 260
fliI PRK08472
flagellar protein export ATPase FliI;
33-215 7.12e-25

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 100.92  E-value: 7.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  33 DGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIhQKAPafdqLSPS-----TELLETGIKVID 107
Cdd:PRK08472  75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPI-MKAP----IAAMkrgliDEVFSVGVKSID 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 108 LICPFAKGGKVGLFGGAGVGKTVNM-MELINNIAKehggYSVFAGVGERTREGNDFYHEMKDSNvLDKVALVYGQMNEPP 186
Cdd:PRK08472 150 GLLTCGKGQKLGIFAGSGVGKSTLMgMIVKGCLAP----IKVVALIGERGREIPEFIEKNLGGD-LENTVIVVATSDDSP 224

                        170       180
                 ....*....|....*....|....*....
gi 936369950 187 GNRLRVALTGLTMAEHFRDEGLDVLFFVD 215
Cdd:PRK08472 225 LMRKYGAFCAMSVAEYFKNQGLDVLFIMD 253
fliI PRK08972
flagellar protein export ATPase FliI;
34-215 1.60e-24

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 99.77  E-value: 1.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  34 GLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIHqkAPAFDQLS--PSTELLETGIKVIDLICP 111
Cdd:PRK08972  81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRH--SPPINPLSrrPITEPLDVGVRAINAMLT 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 112 FAKGGKVGLFGGAGVGKTV--NMM------ELInniakehggysVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMN 183
Cdd:PRK08972 159 VGKGQRMGLFAGSGVGKSVllGMMtrgttaDVI-----------VVGLVGERGREVKEFIEEILGEEGRARSVVVAAPAD 227

                        170       180       190
                 ....*....|....*....|....*....|..
gi 936369950 184 EPPGNRLRVALTGLTMAEHFRDEGLDVLFFVD 215
Cdd:PRK08972 228 TSPLMRLKGCETATTIAEYFRDQGLNVLLLMD 259
fliI PRK06002
flagellar protein export ATPase FliI;
58-215 6.86e-24

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 98.15  E-value: 6.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  58 GRIMDVLGRPIDEAGPI-SSETTRAIHQKAPAFDQLSPSTELLETGIKVIDLICPFAKGGKVGLFGGAGVGKTVnmmeLI 136
Cdd:PRK06002 107 GRVINALGEPIDGLGPLaPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKST----LL 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 137 NNIAKEHGGYSV-FAGVGERTREGNDFYHEMKDSNvLDKVALVYGQMNEPPGNRLRVALTGLTMAEHFRDEGLDVLFFVD 215
Cdd:PRK06002 183 AMLARADAFDTVvIALVGERGREVREFLEDTLADN-LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVD 261
fliI PRK08927
flagellar protein export ATPase FliI;
30-215 8.21e-24

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 97.74  E-value: 8.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  30 GASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPIS-SETTRAIHQKAPAFDQLSPSTELLETGIKVIDL 108
Cdd:PRK08927  72 GPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPqGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNT 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 109 ICPFAKGGKVGLFGGAGVGKTVNMMELINNIAKEhggYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGN 188
Cdd:PRK08927 152 FLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALM 228

                        170       180
                 ....*....|....*....|....*..
gi 936369950 189 RLRVALTGLTMAEHFRDEGLDVLFFVD 215
Cdd:PRK08927 229 RRQAAYLTLAIAEYFRDQGKDVLCLMD 255
AtpA COG0056
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ...
 29-211 1.28e-23

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: 97.80  E-value: 1.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  29 LGASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIHQKAPAFDQLSPSTELLETGIKVIDL 108
Cdd:COG0056   76 LGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDA 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 109 ICPFAKGGKVGLFGGAGVGKT---VNMMelINNiaKEHGGYSVFAGVGErtregndfyhemKDSNVLDKVALV--YGQM- 182
Cdd:COG0056  156 MIPIGRGQRELIIGDRQTGKTaiaIDTI--INQ--KGKDVICIYVAIGQ------------KASTVAQVVETLeeHGAMe 219

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 936369950 183 ---------NEPPGNRLRVALTGLTMAEHFRDEGLDVL 211
Cdd:COG0056  220 ytivvaataSDPAPLQYIAPYAGCAMGEYFMDQGKDVL 257
PRK09281 PRK09281
F0F1 ATP synthase subunit alpha; Validated
 22-211 1.50e-23

F0F1 ATP synthase subunit alpha; Validated


Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 97.44  E-value: 1.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  22 GVVrtiCLGASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIHQKAPAFDQLSPSTELLET 101
Cdd:PRK09281  72 GAV---ILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQT 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 102 GIKVIDLICPFAKGGKVGLFGGAGVGKT-VNMMELINNiaKEHGGYSVFAGVGErtregndfyhemKDSNvldkVALV-- 178
Cdd:PRK09281 149 GIKAIDAMIPIGRGQRELIIGDRQTGKTaIAIDTIINQ--KGKDVICIYVAIGQ------------KAST----VAQVvr 210

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 936369950 179 ----YGQM----------NEPPGNRLRVALTGLTMAEHFRDEGLDVL 211
Cdd:PRK09281 211 kleeHGAMeytivvaataSDPAPLQYLAPYAGCAMGEYFMDNGKDAL 257
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
29-215 2.28e-23

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 96.75  E-value: 2.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  29 LGASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIHQKAPAFDQLSPSTELLETGIKVIDL 108
Cdd:PRK06936  76 LGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDG 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 109 ICPFAKGGKVGLFGGAGVGKTVNMMELINNIAKEhggYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGN 188
Cdd:PRK06936 156 LLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVD---VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSME 232

                        170       180
                 ....*....|....*....|....*..
gi 936369950 189 RLRVALTGLTMAEHFRDEGLDVLFFVD 215
Cdd:PRK06936 233 RAKAGFVATSIAEYFRDQGKRVLLLMD 259
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 48-215 3.35e-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: 93.78  E-value: 3.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  48 ISVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIHQKAPAFDQLSPSTELLETGIKVIDLICPFAKGGKVGLFGGAGVG 127
Cdd:cd01132    2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 128 KTVNMMELINNiAKEHGGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEHFRDEG 207
Cdd:cd01132   82 KTAIAIDTIIN-QKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160


                 ....*...
gi 936369950 208 LDVLFFVD 215
Cdd:cd01132  161 KHALIIYD 168
PRK05922 PRK05922
type III secretion system ATPase; Validated
 47-215 2.14e-20

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 88.42  E-value: 2.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  47 PISVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIHQKAPAFDQLSPSTELLETGIKVIDLICPFAKGGKVGLFGGAGV 126
Cdd:PRK05922  89 PPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGS 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 127 GKTvnmmELINNIAK-EHGGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEHFRD 205
Cdd:PRK05922 169 GKS----SLLSTIAKgSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRD 244

                        170
                 ....*....|
gi 936369950 206 EGLDVLFFVD 215
Cdd:PRK05922 245 QGHRVLFIMD 254
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
5-215 4.42e-20

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 87.32  E-value: 4.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950   5 ILEGSELTlEVQQQLGDGVVRTIcLGASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAgPISSETTRAIHQ 84
Cdd:PRK07594  48 IKPGEELA-EVVGINGSKALLSP-FTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDA 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  85 KAPAFDQLSPSTELLETGIKVIDLICPFAKGGKVGLFGGAGVGKTVNMMELINNIAKEhggYSVFAGVGERTREGNDFYH 164
Cdd:PRK07594 125 MPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDAD---SNVLVLIGERGREVREFID 201

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 936369950 165 EMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEHFRDEGLDVLFFVD 215
Cdd:PRK07594 202 FTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLAD 252
fliI PRK06793
flagellar protein export ATPase FliI;
32-215 2.88e-19

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 85.03  E-value: 2.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  32 SDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEagPISSETTRAIHQKAP---AFDQlSPSTELLETGIKVIDL 108
Cdd:PRK06793  73 TEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPpihAFER-EEITDVFETGIKSIDS 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 109 ICPFAKGGKVGLFGGAGVGKTVnmmeLINNIAKE-HGGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPG 187
Cdd:PRK06793 150 MLTIGIGQKIGIFAGSGVGKST----LLGMIAKNaKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHL 225

                        170       180
                 ....*....|....*....|....*...
gi 936369950 188 NRLRVALTGLTMAEHFRDEGLDVLFFVD 215
Cdd:PRK06793 226 MQLRAAKLATSIAEYFRDQGNNVLLMMD 253
fliI PRK05688
flagellar protein export ATPase FliI;
29-215 4.54e-19

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 84.40  E-value: 4.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  29 LGASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSETTraIHQKAPAFDQLS--PSTELLETGIKVI 106
Cdd:PRK05688  82 VGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDW--VPMDGPTINPLNrhPISEPLDVGIRSI 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 107 DLICPFAKGGKVGLFGGAGVGKTV--NMMELINNiakehGGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNE 184
Cdd:PRK05688 160 NGLLTVGRGQRLGLFAGTGVGKSVllGMMTRFTE-----ADIIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADD 234

                        170       180       190
                 ....*....|....*....|....*....|.
gi 936369950 185 PPGNRLRVALTGLTMAEHFRDEGLDVLFFVD 215
Cdd:PRK05688 235 APLMRLRAAMYCTRIAEYFRDKGKNVLLLMD 265
fliI PRK07196
flagellar protein export ATPase FliI;
52-215 3.83e-18

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 81.86  E-value: 3.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  52 VGKPTLGRIMDVLGRPIDEAGPISSETTRAIHQKAPAFDQLSPSTELLETGIKVIDLICPFAKGGKVGLFGGAGVGKTVn 131
Cdd:PRK07196  92 IGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSV- 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 132 mmeLINNIAKEHGGYSVFAG-VGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEHFRDEGLDV 210
Cdd:PRK07196 171 ---LLGMITRYTQADVVVVGlIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDV 247


                 ....*
gi 936369950 211 LFFVD 215
Cdd:PRK07196 248 LLLVD 252
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
 47-215 1.51e-17

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: 78.77  E-value: 1.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  47 PISVPVGKPTLGRIMDVLGRP---IDEAGPISSETTRAIH-----QKAPAFDQLSPSTELLeTGIKVIDLICPFAKGGKV 118
Cdd:cd01134    1 PLSVELGPGLLGSIFDGIQRPlevIAETGSIFIPRGVNVQrwpvrQPRPVKEKLPPNVPLL-TGQRVLDTLFPVAKGGTA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 119 GLFGGAGVGKTVnmmeLINNIAKehggYS-----VFAGVGER----TREGNDFYH---EMKDSNVLDKVALVYGQMNEPP 186
Cdd:cd01134   80 AIPGPFGCGKTV----ISQSLSK----WSnsdvvIYVGCGERgnemAEVLEEFPElkdPITGESLMERTVLIANTSNMPV 151

                        170       180
                 ....*....|....*....|....*....
gi 936369950 187 GNRLRVALTGLTMAEHFRDEGLDVLFFVD 215
Cdd:cd01134  152 AAREASIYTGITIAEYFRDMGYNVSLMAD 180
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
 29-211 2.03e-17

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 79.87  E-value: 2.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  29 LGASDGL-RRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIHQKA--PAfDQLSPStELLETGIKV 105
Cdd:PRK04196  56 FEGTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPV-AREYPE-EFIQTGISA 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 106 IDLICPFAKGGKVGLFGGAGVgkTVNMMEL-INNIAKEHGGYS----VFAGVGERTREGNDFYHEMKDSNVLDKVALVYG 180
Cdd:PRK04196 134 IDGLNTLVRGQKLPIFSGSGL--PHNELAAqIARQAKVLGEEEnfavVFAAMGITFEEANFFMEDFEETGALERSVVFLN 211

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 936369950 181 QMNEPPGNRL---RVAltgLTMAEHFR-DEGLDVL 211
Cdd:PRK04196 212 LADDPAIERIltpRMA---LTAAEYLAfEKGMHVL 243
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 47-211 3.01e-16

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: 75.34  E-value: 3.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  47 PISVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIHqkAPAFDQLS---PStELLETGIKVIDLICPFAKGGKVGLFGG 123
Cdd:cd01135    1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDIN--GPPINPVAriyPE-EMIQTGISAIDVMNTLVRGQKLPIFSG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 124 AGvgktVNMMELINNIAKEHGGYS-------VFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTG 196
Cdd:cd01135   78 SG----LPHNELAAQIARQAGVVGseenfaiVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMA 153

                        170
                 ....*....|....*.
gi 936369950 197 LTMAEHFR-DEGLDVL 211
Cdd:cd01135  154 LTTAEYLAyEKGKHVL 169
ATP-synt_F1_beta_N cd18115
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ...
 1-48 1.59e-15

F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of FoF1-ATP synthase, N-terminal domain. The F-ATP synthase (also called FoF1-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 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.


Pssm-ID: 349739 [Multi-domain]  Cd Length: 76  Bit Score: 68.70  E-value: 1.59e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 936369950   1 YDALIL---EGSELTLEVQQQLGDGVVRTICLGASDGLRRGTIVKNTGNPI 48
Cdd:cd18115   26 YNALEVkgdDGKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
atpA CHL00059
ATP synthase CF1 alpha subunit
 33-215 2.26e-15

ATP synthase CF1 alpha subunit


Pssm-ID: 176999 [Multi-domain]  Cd Length: 485  Bit Score: 73.84  E-value: 2.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  33 DGLR--RGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIHQKAPAFDQLSPSTELLETGIKVIDLIC 110
Cdd:CHL00059  57 DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMI 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 111 PFAKGGKVGLFGGAGVGKTVNMMELINNiAKEHGGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRL 190
Cdd:CHL00059 137 PIGRGQRELIIGDRQTGKTAVATDTILN-QKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQY 215

                        170       180
                 ....*....|....*....|....*
gi 936369950 191 RVALTGLTMAEHFRDEGLDVLFFVD 215
Cdd:CHL00059 216 LAPYTGAALAEYFMYRGRHTLIIYD 240
fliI PRK07960
flagellum-specific ATP synthase FliI;
50-215 3.16e-15

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 73.66  E-value: 3.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  50 VPVGKPTLGRIMDVLGRPIDeaGPISSETTRAIHQKAPAFD--QLSPSTELLETGIKVIDLICPFAKGGKVGLFGGAGVG 127
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLD--GLPAPDTGETGALITPPFNplQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVG 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950 128 KTVnmmeLINNIAKEHGGYSVFAG-VGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEHFRDE 206
Cdd:PRK07960 188 KSV----LLGMMARYTQADVIVVGlIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDR 263


                 ....*....
gi 936369950 207 GLDVLFFVD 215
Cdd:PRK07960 264 GQHVLLIMD 272
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
 94-211 5.74e-11

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 60.95  E-value: 5.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  94 PSTELLETGIKVIDLICPFAKGGKVGLFGGAGVGKTVnmmeLINNIAKehggYS-----VFAGVGERtreGNdfyhEMKD 168
Cdd:PRK04192 206 PPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTV----TQHQLAK----WAdadivIYVGCGER---GN----EMTE 270

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 936369950 169 snVLdkvalvygqmNEPP-------GNRL--R-----------VA------LTGLTMAEHFRDEGLDVL 211
Cdd:PRK04192 271 --VL----------EEFPelidpktGRPLmeRtvliantsnmpVAareasiYTGITIAEYYRDMGYDVL 327
PTZ00185 PTZ00185
ATPase alpha subunit; Provisional
 21-215 1.66e-09

ATPase alpha subunit; Provisional


Pssm-ID: 140212 [Multi-domain]  Cd Length: 574  Bit Score: 56.97  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  21 DGVVRTICLGASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPI-------DEAGPISSETTRAIHQKAPAFDQLS 93
Cdd:PTZ00185  88 DGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVpvglltrSRALLESEQTLGKVDAGAPNIVSRS 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  94 PSTELLETGIKVIDLICPFAKGGKVGLFGGAGVGKT-------VNMMELINNIAKEHGGYSVFAGVGERTREGNDFYHEM 166
Cdd:PTZ00185 168 PVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTsiavstiINQVRINQQILSKNAVISIYVSIGQRCSNVARIHRLL 247

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 936369950 167 KDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEHFRDEGLDVLFFVD 215
Cdd:PTZ00185 248 RSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYD 296
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
 37-203 1.69e-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: 56.65  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950   37 RGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDEAGPISSETTRAIH-QKAPAFDQLSPStELLETGIKVIDLICPFAKG 115
Cdd:TIGR01040  63 KKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINgQPINPYARIYPE-EMIQTGISAIDVMNSIARG 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  116 GKVGLFGGAGV------GKTVNMMELINNIAKE-HGGYS-----VFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMN 183
Cdd:TIGR01040 142 QKIPIFSAAGLphneiaAQICRQAGLVKLPTKDvHDGHEdnfaiVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLAN 221

                         170       180
                  ....*....|....*....|
gi 936369950  184 EPPGNRLRVALTGLTMAEHF 203
Cdd:TIGR01040 222 DPTIERIITPRLALTTAEYL 241
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
 6-207 1.23e-08

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 54.27  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950   6 LEGSELTLEVqqqlgdgvvrticLGASDGLRRGTIVKNTGNPISVPVGKPTLGRIMDVLGRPIDeAGPISSEttRAIHQK 85
Cdd:PRK02118  45 LDGDKVTLQV-------------FGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPID-GGPELEG--EPIEIG 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  86 APAFD---QLSPStELLETGIKVIDLICPFAKGGKVGLFGGAgvGKTVNmmELINNIA-KEHGGYSVFAGVGERTREGND 161
Cdd:PRK02118 109 GPSVNpvkRIVPR-EMIRTGIPMIDVFNTLVESQKIPIFSVS--GEPYN--ALLARIAlQAEADIIILGGMGLTFDDYLF 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 936369950 162 FYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEHFRDEG 207
Cdd:PRK02118 184 FKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEG 229
ATP-synt_ab_N pfam02874
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ...
 5-45 7.83e-07

ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.


Pssm-ID: 427029 [Multi-domain]  Cd Length: 69  Bit Score: 45.23  E-value: 7.83e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 936369950    5 ILEGSELTLEVQQQLGDGVVRTICLGASDGLRRGTIVKNTG 45
Cdd:pfam02874  29 LVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 131-215 3.20e-06

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 47.32  E-value: 3.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  131 NMMELINNIAKEH-------GGYSVFAGVGERTREGNDFYHE---MKDSN----VLDKVALVYGQMNEPPGNRLRVALTG 196
Cdd:PRK14698  662 NMPTLLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEfpkLKDPKtgkpLMERTVLIANTSNMPVAAREASIYTG 741

                          90
                  ....*....|....*....
gi 936369950  197 LTMAEHFRDEGLDVLFFVD 215
Cdd:PRK14698  742 ITIAEYFRDMGYDVALMAD 760
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 53-168 2.34e-05

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 44.63  E-value: 2.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950   53 GKPTLGRIMDVLGRPIDEAGPISSETTRAIHQKAPAFDQLSPSTELLeTGIKVIDLICPFAKGGKVGLFGGAGVGKTVNM 132
Cdd:PRK14698  166 GEYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLI-TGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDG 244

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 936369950  133 MELInnIAKEHG------GYSVFAGVGERTREGNDFYHEMKD 168
Cdd:PRK14698  245 DTLI--LTKEFGlikikdLYEILDGKGKKTVEGNEEWTELEE 284
rho TIGR00767
transcription termination factor Rho; This RNA helicase, the transcription termination factor ...
 84-215 6.42e-03

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: 36.97  E-value: 6.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950   84 QKAPAFDQLSP-----------STELLETgiKVIDLICPFAKGGKVGLFGGAGVGKTVNMMELINNIAKEHGG-YSVFAG 151
Cdd:TIGR00767 128 KNRVLFENLTPlypnerlrletSTEDLST--RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEvELIVLL 205

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 936369950  152 VGERTREgndfyhemkdsnVLDKVALVYGQM-----NEPPGNRLRVALTGLTMAEHFRDEGLDVLFFVD 215
Cdd:TIGR00767 206 IDERPEE------------VTDMQRSVKGEVvastfDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLD 262
PRK07165 PRK07165
ATP F0F1 synthase subunit alpha;
58-174 6.72e-03

ATP F0F1 synthase subunit alpha;


Pssm-ID: 235951 [Multi-domain]  Cd Length: 507  Bit Score: 36.87  E-value: 6.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950  58 GRIMDVLGRPIDeagPISSETT--RAIHQKAPAFDQLS------PSTELLETGIKVIDLICPFAKGGKVGLFGGAGVGKT 129
Cdd:PRK07165  81 GKIIDIDGNIIY---PEAQNPLskKFLPNTSSIFNLAHglmtvkTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKT 157

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 936369950 130 ---VNMMelINNiaKEHGGYSVFAGVGERTREGNDFYHEMKDSNVLDK 174
Cdd:PRK07165 158 hiaLNTI--INQ--KNTNVKCIYVAIGQKRENLSRIYETLKEHDALKN 201
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 114-173 7.03e-03

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: 35.81  E-value: 7.03e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 936369950   114 KGGKVGLFGGAGVGKTVNMMELINNIAKEHGGYSVFAGVGERTREGNDFYHEMKDSNVLD 173
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS 60
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH