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Conserved domains on  [gi|667484560|gb|AIG56878|]
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ATP synthase beta subunit, partial [Streptomyces viridis]

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 ...
 2-165 9.65e-135

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: 383.67  E-value: 9.65e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   2 FDELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIDEMSE 81
Cdd:COG0055  120 FEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKE 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  82 SGVIDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADE 161
Cdd:COG0055  200 SGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATE 279


                 ....
gi 667484560 162 MGLL 165
Cdd:COG0055  280 MGAL 283
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 2-165 9.65e-135

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: 383.67  E-value: 9.65e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   2 FDELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIDEMSE 81
Cdd:COG0055  120 FEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKE 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  82 SGVIDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADE 161
Cdd:COG0055  200 SGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATE 279


                 ....
gi 667484560 162 MGLL 165
Cdd:COG0055  280 MGAL 283
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 2-165 2.46e-119

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: 337.65  E-value: 2.46e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   2 FDELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIDEMSE 81
Cdd:cd01133   41 FVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKE 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  82 SGVI-----DKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:cd01133  121 SGVInldglSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQP 200


                 ....*....
gi 667484560 157 NLADEMGLL 165
Cdd:cd01133  201 TLATEMGSL 209
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 2-165 5.87e-116

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: 335.92  E-value: 5.87e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560    2 FDELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIDEMSE 81
Cdd:TIGR01039 117 FEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKE 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   82 SGVIDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADE 161
Cdd:TIGR01039 197 SGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATE 276


                  ....
gi 667484560  162 MGLL 165
Cdd:TIGR01039 277 MGEL 280
atpB CHL00060
ATP synthase CF1 beta subunit
 2-165 1.44e-109

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 320.83  E-value: 1.44e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   2 FDELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIDEMSE 81
Cdd:CHL00060 135 FIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKE 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  82 SGVID-------KTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGY 154
Cdd:CHL00060 215 SGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGY 294

                        170
                 ....*....|.
gi 667484560 155 QPNLADEMGLL 165
Cdd:CHL00060 295 QPTLSTEMGSL 305
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 15-163 1.18e-66

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: 201.82  E-value: 1.18e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   15 GVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIYRvaNNHDGVSVFAGVGERTREGNDLIDEMSESGVIDKTALVFGQ 94
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAG-MIAR--QASADVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 667484560   95 MDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMG 163
Cdd:pfam00006  78 SDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLA 145
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 27-140 1.11e-04

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 40.43  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560    27 KGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIDEMSESGVIDKTalvfgqmdepPGTRLRVA 106
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS----------GELRLRLA 70

                           90       100       110
                   ....*....|....*....|....*....|....
gi 667484560   107 LAgltMAEYFRdvqkQDVLfFIDNIFRFTQAGSE 140
Cdd:smart00382  71 LA---LARKLK----PDVL-ILDEITSLLDAEQE 96
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 2-165 9.65e-135

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: 383.67  E-value: 9.65e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   2 FDELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIDEMSE 81
Cdd:COG0055  120 FEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKE 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  82 SGVIDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADE 161
Cdd:COG0055  200 SGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATE 279


                 ....
gi 667484560 162 MGLL 165
Cdd:COG0055  280 MGAL 283
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 2-165 2.46e-119

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: 337.65  E-value: 2.46e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   2 FDELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIDEMSE 81
Cdd:cd01133   41 FVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKE 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  82 SGVI-----DKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:cd01133  121 SGVInldglSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQP 200


                 ....*....
gi 667484560 157 NLADEMGLL 165
Cdd:cd01133  201 TLATEMGSL 209
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 2-165 5.87e-116

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: 335.92  E-value: 5.87e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560    2 FDELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIDEMSE 81
Cdd:TIGR01039 117 FEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKE 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   82 SGVIDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADE 161
Cdd:TIGR01039 197 SGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATE 276


                  ....
gi 667484560  162 MGLL 165
Cdd:TIGR01039 277 MGEL 280
atpB CHL00060
ATP synthase CF1 beta subunit
 2-165 1.44e-109

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 320.83  E-value: 1.44e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   2 FDELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIDEMSE 81
Cdd:CHL00060 135 FIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKE 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  82 SGVID-------KTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGY 154
Cdd:CHL00060 215 SGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGY 294

                        170
                 ....*....|.
gi 667484560 155 QPNLADEMGLL 165
Cdd:CHL00060 295 QPTLSTEMGSL 305
alt_F1F0_F1_bet TIGR03305
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ...
 7-165 2.41e-84

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: 254.75  E-value: 2.41e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560    7 SKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIDEMSESGVID 86
Cdd:TIGR03305 117 SKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLD 196

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 667484560   87 KTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLL 165
Cdd:TIGR03305 197 NTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAEL 275
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 1-165 7.41e-71

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: 214.63  E-value: 7.41e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   1 NFDELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIDEMS 80
Cdd:cd19476   40 NPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFT 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  81 ESGVIDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLAD 160
Cdd:cd19476  120 KSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRD-NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFT 198


                 ....*
gi 667484560 161 EMGLL 165
Cdd:cd19476  199 KLATL 203
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 15-163 1.18e-66

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: 201.82  E-value: 1.18e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   15 GVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIYRvaNNHDGVSVFAGVGERTREGNDLIDEMSESGVIDKTALVFGQ 94
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAG-MIAR--QASADVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 667484560   95 MDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMG 163
Cdd:pfam00006  78 SDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLA 145
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 9-156 2.38e-33

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: 118.43  E-value: 2.38e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   9 TEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIqEMIyrvANNHDG-VSVFAGVGERTREGNDLIDEMSESGVIDK 87
Cdd:cd01136   48 EQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLL-GMI---ARNTDAdVNVIALIGERGREVREFIEKDLGEEGLKR 123

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 667484560  88 TALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:cd01136  124 SVLVVATSDESPLLRVRAAYTATAIAEYFRD-QGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPP 191
fliI PRK06002
flagellar protein export ATPase FliI;
12-156 2.38e-29

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 111.24  E-value: 2.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  12 FETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIYRvANNHDGVsVFAGVGERTREGNDLIDE-MSESgvIDKTAL 90
Cdd:PRK06002 149 LRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLA-MLAR-ADAFDTV-VIALVGERGREVREFLEDtLADN--LKKAVA 223

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 667484560  91 VFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:PRK06002 224 VVATSDESPMMRRLAPLTATAIAEYFRD-RGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPP 288
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 9-156 6.78e-29

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: 109.74  E-value: 6.78e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   9 TEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIYRVANNhDgVSVFAGVGERTREGNDLIDE------MSES 82
Cdd:COG1157  138 TEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLG-MIARNTEA-D-VNVIALIGERGREVREFIEDdlgeegLARS 214

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 667484560  83 GVIDKTAlvfgqmDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:COG1157  215 VVVVATS------DEPPLMRLRAAYTATAIAEYFRD-QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPP 281
PRK08149 PRK08149
FliI/YscN family ATPase;
9-154 2.56e-25

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 100.07  E-value: 2.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   9 TEMFETGVKVID-LLTPYVkGGKIGLFGGAGVGKTVLIQEMIyrvanNHDGVSVF--AGVGERTREGNDLIDEMSESGVI 85
Cdd:PRK08149 132 REPLITGVRAIDgLLTCGV-GQRMGIFASAGCGKTSLMNMLI-----EHSEADVFviGLIGERGREVTEFVESLRASSRR 205

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 667484560  86 DKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGY 154
Cdd:PRK08149 206 EKCVLVYATSDFSSVDRCNAALVATTVAEYFRD-QGKRVVLFIDSMTRYARALRDVALAAGELPARRGY 273
fliI PRK08472
flagellar protein export ATPase FliI;
10-156 7.76e-24

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 95.91  E-value: 7.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  10 EMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIyrVANNHDGVSVFAGVGERTREGNDLIdEMSESGVIDKTA 89
Cdd:PRK08472 139 EVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMG-MI--VKGCLAPIKVVALIGERGREIPEFI-EKNLGGDLENTV 214

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 667484560  90 LVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:PRK08472 215 IVVATSDDSPLMRKYGAFCAMSVAEYFKN-QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPP 280
fliI PRK08927
flagellar protein export ATPase FliI;
13-156 2.36e-23

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 94.66  E-value: 2.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  13 ETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIYRVANNHdgVSVFAGVGERTREGNDLI-DEMSESGvIDKTALV 91
Cdd:PRK08927 143 DLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLS-MLARNADAD--VSVIGLIGERGREVQEFLqDDLGPEG-LARSVVV 218

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 667484560  92 FGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:PRK08927 219 VATSDEPALMRRQAAYLTLAIAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTP 282
fliI PRK07721
flagellar protein export ATPase FliI;
10-156 3.84e-23

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 94.02  E-value: 3.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  10 EMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIYRvaNNHDGVSVFAGVGERTREGNDLID-EMSESGvIDKT 88
Cdd:PRK07721 140 EPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMG-MIAR--NTSADLNVIALIGERGREVREFIErDLGPEG-LKRS 215

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 667484560  89 ALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:PRK07721 216 IVVVATSDQPALMRIKGAYTATAIAEYFRD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTP 282
fliI PRK06793
flagellar protein export ATPase FliI;
4-149 4.88e-22

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 91.19  E-value: 4.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   4 ELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIYRvaNNHDGVSVFAGVGERTREGNDLI-DEMSES 82
Cdd:PRK06793 132 EREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLG-MIAK--NAKADINVISLVGERGREVKDFIrKELGEE 208

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 667484560  83 GvIDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMP 149
Cdd:PRK06793 209 G-MRKSVVVVATSDESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVKELP 273
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
9-158 2.19e-21

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 89.49  E-value: 2.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   9 TEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIyrVANNHDGVSVFAGVGERTREGNDLIDEMSESGVIDKT 88
Cdd:PRK06820 144 EQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLG-ML--CADSAADVMVLALIGERGREVREFLEQVLTPEARART 220

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  89 ALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNL 158
Cdd:PRK06820 221 VVVVATSDRPALERLKGLSTATTIAEYFRD-RGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSV 289
fliI PRK08972
flagellar protein export ATPase FliI;
9-156 1.05e-20

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 87.45  E-value: 1.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   9 TEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIYR--VANnhdgVSVFAGVGERTREGNDLIDE-MSESGVi 85
Cdd:PRK08972 143 TEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLG-MMTRgtTAD----VIVVGLVGERGREVKEFIEEiLGEEGR- 216

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 667484560  86 DKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:PRK08972 217 ARSVVVAAPADTSPLMRLKGCETATTIAEYFRD-QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPP 286
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
 9-159 4.71e-20

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


Pssm-ID: 410878 [Multi-domain]  Cd Length: 288  Bit Score: 84.16  E-value: 4.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   9 TEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVlIQEMIYRVANNhDGVsVFAGVGERtreGND----------LIDE 78
Cdd:cd01134   57 NVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTV-ISQSLSKWSNS-DVV-IYVGCGER---GNEmaevleefpeLKDP 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  79 MSESGVIDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNL 158
Cdd:cd01134  131 ITGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRD-MGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYL 209


                 .
gi 667484560 159 A 159
Cdd:cd01134  210 G 210
fliI PRK05688
flagellar protein export ATPase FliI;
10-156 2.36e-19

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 83.63  E-value: 2.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  10 EMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMI-YRVANnhdgVSVFAGVGERTREGNDLIDEMSESGVIDKT 88
Cdd:PRK05688 150 EPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTrFTEAD----IIVVGLIGERGREVKEFIEHILGEEGLKRS 225

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 667484560  89 ALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:PRK05688 226 VVVASPADDAPLMRLRAAMYCTRIAEYFRD-KGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPP 292
PRK05922 PRK05922
type III secretion system ATPase; Validated
 10-154 5.15e-19

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 82.64  E-value: 5.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  10 EMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMiyrVANNHDGVSVFAGVGERTREGNDLIDEMSESGVIDKTA 89
Cdd:PRK05922 139 EIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTI---AKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTI 215

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 667484560  90 LVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGY 154
Cdd:PRK05922 216 IIASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHY 279
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
13-156 2.14e-18

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 80.95  E-value: 2.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  13 ETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNhdgVSVFAGVGERTREGNDLID-EMSESGvIDKTALV 91
Cdd:PRK06936 147 SLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVD---VTVLALIGERGREVREFIEsDLGEEG-LRKAVLV 222

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 667484560  92 FGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:PRK06936 223 VATSDRPSMERAKAGFVATSIAEYFRD-QGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPP 286
fliI PRK07196
flagellar protein export ATPase FliI;
12-157 2.35e-18

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 80.71  E-value: 2.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  12 FETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIYRVANNHdgVSVFAGVGERTREGNDLIDEMSESGVIDKTALV 91
Cdd:PRK07196 139 LDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLG-MITRYTQAD--VVVVGLIGERGREVKEFIEHSLQAAGMAKSVVV 215

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 667484560  92 FGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPN 157
Cdd:PRK07196 216 AAPADESPLMRIKATELCHAIATYYRD-KGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPS 280
fliI PRK07960
flagellum-specific ATP synthase FliI;
9-158 3.16e-16

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 74.82  E-value: 3.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   9 TEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMI-YRVANnhdgVSVFAGVGERTREGNDLIDEMSESGVIDK 87
Cdd:PRK07960 156 EHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMArYTQAD----VIVVGLIGERGREVKDFIENILGAEGRAR 231

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 667484560  88 TALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNL 158
Cdd:PRK07960 232 SVVIAAPADVSPLLRMQGAAYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSV 301
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 14-162 4.79e-16

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 74.03  E-value: 4.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  14 TGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIYRVANNHdgVSVFAGVGERTREGNDLIDEMSESGVIDKTALVFG 93
Cdd:PRK09099 149 TGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMG-MFARGTQCD--VNVIALIGERGREVREFIELILGEDGMARSVVVCA 225

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 667484560  94 QMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEM 162
Cdd:PRK09099 226 TSDRSSIERAKAAYVATAIAEYFRD-RGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAEL 293
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 10-154 1.00e-15

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: 72.25  E-value: 1.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  10 EMFETGVKVIDLLTPYVKGGKIGLFGGAGV-GKTVLIQemIYR----VANNHDGVSVFAGVGERTREGNDLIDEMSESGV 84
Cdd:cd01135   51 EMIQTGISAIDVMNTLVRGQKLPIFSGSGLpHNELAAQ--IARqagvVGSEENFAIVFAAMGVTMEEARFFKDDFEETGA 128

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  85 IDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGY 154
Cdd:cd01135  129 LERVVLFLNLANDPTIERIITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGY 198
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
14-156 2.68e-15

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 71.91  E-value: 2.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  14 TGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMiyrvANNHDG-VSVFAGVGERTREGNDLIDEMSESGVIDKTALVF 92
Cdd:PRK07594 141 TGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAML----CNAPDAdSNVLVLIGERGREVREFIDFTLSEETRKRCVIVV 216

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 667484560  93 GQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:PRK07594 217 ATSDRPALERVRALFVATTIAEFFRD-NGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPP 279
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 9-149 2.46e-13

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 66.48  E-value: 2.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   9 TEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLiqeMIYRVANNHDG--VSVFAGVGERTREGNDLIDEMSESGVID 86
Cdd:PRK13343 143 TEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAI---AIDAIINQKDSdvICVYVAIGQKASAVARVIETLREHGALE 219

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 667484560  87 KTALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMP 149
Cdd:PRK13343 220 YTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPP 281
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
 9-159 5.59e-12

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 62.49  E-value: 5.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   9 TEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEmiyrVANNHDG-VSVFAGVGERTREGNDLIDEMSE-----S 82
Cdd:PRK04192 208 VEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQ----LAKWADAdIVIYVGCGERGNEMTEVLEEFPElidpkT 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  83 G--VIDKTALVFGQMDEPpgtrlrVAlA-------GLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVG 153
Cdd:PRK04192 284 GrpLMERTVLIANTSNMP------VA-AreasiytGITIAEYYRD-MGYDVLLMADSTSRWAEALREISGRLEEMPGEEG 355


                 ....*.
gi 667484560 154 YQPNLA 159
Cdd:PRK04192 356 YPAYLA 361
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
 10-154 2.12e-10

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 58.12  E-value: 2.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  10 EMFETGVKVIDLLTPYVKGGKIGLFGGAGVGktvlIQEMIYRVANNHDG-VSVFAGVGERTREGNDLIDEMSESGVIDKT 88
Cdd:PRK02118 122 EMIRTGIPMIDVFNTLVESQKIPIFSVSGEP----YNALLARIALQAEAdIIILGGMGLTFDDYLFFKDTFENAGALDRT 197

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 667484560  89 ALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGY 154
Cdd:PRK02118 198 VMFIHTASDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGY 263
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 6-149 4.58e-10

F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.


Pssm-ID: 410876 [Multi-domain]  Cd Length: 274  Bit Score: 56.41  E-value: 4.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   6 ESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKT-VLIQEMIYRVANNHdgVSVFAGVGERTREGNDLIDEMSESGV 84
Cdd:cd01132   47 QSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTaIAIDTIINQKGKKV--YCIYVAIGQKRSTVAQIVKTLEEHGA 124

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 667484560  85 IDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMP 149
Cdd:cd01132  125 MEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPP 188
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 59-163 3.14e-09

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 54.64  E-value: 3.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   59 VSVFAGVGERTREGNDLIDEMSE-------SGVIDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVqKQDVLFFIDNI 131
Cdd:PRK14698  684 VVIYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYDVALMADST 762

                          90       100       110
                  ....*....|....*....|....*....|..
gi 667484560  132 FRFTQAGSEVSTLLGRMPSAVGYQPNLADEMG 163
Cdd:PRK14698  763 SRWAEALREISGRLEEMPGEEGYPAYLASKLA 794
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
 10-154 4.17e-09

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 54.06  E-value: 4.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  10 EMFETGVKVIDLLTPYVKGGKIGLFGGAGVgKTVLIQEMIYRVANNHDGVS----VFAGVGERTREGNDLIDEMSESGVI 85
Cdd:PRK04196 125 EFIQTGISAIDGLNTLVRGQKLPIFSGSGL-PHNELAAQIARQAKVLGEEEnfavVFAAMGITFEEANFFMEDFEETGAL 203

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 667484560  86 DKTALVFGQMDEPPGTRL---RVAlagLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGY 154
Cdd:PRK04196 204 ERSVVFLNLADDPAIERIltpRMA---LTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGY 272
PRK12608 PRK12608
transcription termination factor Rho; Provisional
 16-137 1.25e-06

transcription termination factor Rho; Provisional


Pssm-ID: 237150 [Multi-domain]  Cd Length: 380  Bit Score: 47.00  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  16 VKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAgvgertregnDLIDEMSESgVIDKTALVFGQM 95
Cdd:PRK12608 121 MRVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMV----------LLIDERPEE-VTDMRRSVKGEV 189

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 667484560  96 -----DEPPgtRLRVALAGLTMAEYFRDV-QKQDVLFFIDNIFRFTQA 137
Cdd:PRK12608 190 yastfDRPP--DEHIRVAELVLERAKRLVeQGKDVVILLDSLTRLARA 235
rho TIGR00767
transcription termination factor Rho; This RNA helicase, the transcription termination factor ...
 5-150 1.79e-06

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: 46.60  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560    5 LESKTEMFETgvKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAgvgertregnDLIDEMSESgV 84
Cdd:TIGR00767 147 LETSTEDLST--RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEVELIV----------LLIDERPEE-V 213

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 667484560   85 IDKTALVFGQM-----DEPPGTRLRVALAGLTMAEyfRDV-QKQDVLFFIDNIFRFTQAGSEVSTLLGRMPS 150
Cdd:TIGR00767 214 TDMQRSVKGEVvastfDEPASRHVQVAEMVIEKAK--RLVeHKKDVVILLDSITRLARAYNTVTPASGKVLS 283
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
 10-154 1.89e-06

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: 46.64  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560   10 EMFETGVKVIDLLTPYVKGGKIGLFGGAG----------VGKTVLIQEMIYRVANNHDG--VSVFAGVGERTREGNDLID 77
Cdd:TIGR01040 123 EMIQTGISAIDVMNSIARGQKIPIFSAAGlphneiaaqiCRQAGLVKLPTKDVHDGHEDnfAIVFAAMGVNMETARFFKQ 202

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 667484560   78 EMSESGVIDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGY 154
Cdd:TIGR01040 203 DFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGF 279
rho_factor_C cd01128
C-terminal ATP binding domain of transcription termination factor rho; Transcription ...
 17-150 1.12e-05

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: 43.73  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  17 KVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAG-VGERTREgndlIDEMSESG---VIDKTalvf 92
Cdd:cd01128    5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEE----VTDMRRSVkgeVVAST---- 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 667484560  93 gqMDEPPGTRLRVALAGLTMAEyfRDV-QKQDVLFFIDNIFRFTQAGSEVSTLLGRMPS 150
Cdd:cd01128   77 --FDEPPERHVQVAEMVIEKAK--RLVeHGKDVVILLDSITRLARAYNTVVPSSGKTLS 131
PTZ00185 PTZ00185
ATPase alpha subunit; Provisional
 14-154 1.36e-05

ATPase alpha subunit; Provisional


Pssm-ID: 140212 [Multi-domain]  Cd Length: 574  Bit Score: 44.26  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560  14 TGVKVIDLLTPYVKGGKIGLFGGAGVGKT-VLIQEMIYRVANNHD------GVSVFAGVGERTREGNDLIDEMSESGVID 86
Cdd:PTZ00185 175 TGFKAVDTMIPIGRGQRELIVGDRQTGKTsIAVSTIINQVRINQQilsknaVISIYVSIGQRCSNVARIHRLLRSYGALR 254

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 667484560  87 KTALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGY 154
Cdd:PTZ00185 255 YTTVMAATAAEPAGLQYLAPYSGVTMGEYFMN-RGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAY 321
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 27-140 1.11e-04

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 40.43  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667484560    27 KGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIDEMSESGVIDKTalvfgqmdepPGTRLRVA 106
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS----------GELRLRLA 70

                           90       100       110
                   ....*....|....*....|....*....|....
gi 667484560   107 LAgltMAEYFRdvqkQDVLfFIDNIFRFTQAGSE 140
Cdd:smart00382  71 LA---LARKLK----PDVL-ILDEITSLLDAEQE 96
 
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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