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Conserved domains on  [gi|299737694|gb|ADJ37170|]
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ATP synthase beta subunit, partial [Bradyrhizobium sp. CCBAU 051011]

Protein Classification

F0F1 ATP synthase subunit beta( domain architecture ID 1903243)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AtpD super family cl43008
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-155 1.89e-111

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: 323.97  E-value: 1.89e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694   1 RAIHQEAPSYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREG 80
Cdd:COG0055  111 RPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREG 190

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 299737694  81 NDLYHEFIESKVNadphnpdpnvkSKCALVFGQMNEPPGARARVGLTGLTVAEHFRD-QGQDVLFFVDNIFRFTQA 155
Cdd:COG0055  191 NDLYREMKESGVL-----------DKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQA 255
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-155 1.89e-111

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: 323.97  E-value: 1.89e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694   1 RAIHQEAPSYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREG 80
Cdd:COG0055  111 RPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREG 190

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 299737694  81 NDLYHEFIESKVNadphnpdpnvkSKCALVFGQMNEPPGARARVGLTGLTVAEHFRD-QGQDVLFFVDNIFRFTQA 155
Cdd:COG0055  191 NDLYREMKESGVL-----------DKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQA 255
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 1-155 3.62e-110

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: 314.16  E-value: 3.62e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694   1 RAIHQEAPSYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREG 80
Cdd:cd01133   32 WPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNIAKAHGGYSVFAGVGERTREG 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 299737694  81 NDLYHEFIESKVnadphnPDPNVKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQ-GQDVLFFVDNIFRFTQA 155
Cdd:cd01133  112 NDLYHEMKESGV------INLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEeGQDVLLFIDNIFRFTQA 181
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 2-155 2.26e-96

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: 285.46  E-value: 2.26e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694    2 AIHQEAPSYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREGN 81
Cdd:TIGR01039 109 PIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTREGN 188

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 299737694   82 DLYHEFIESkvnadphnpdpNVKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRD-QGQDVLFFVDNIFRFTQA 155
Cdd:TIGR01039 189 DLYHEMKES-----------GVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQA 252
atpB CHL00060
ATP synthase CF1 beta subunit
 1-155 2.87e-94

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 281.16  E-value: 2.87e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694   1 RAIHQEAPSYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREG 80
Cdd:CHL00060 126 SPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREG 205

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 299737694  81 NDLYHEFIESKVnADPHNPDpnvKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQG-QDVLFFVDNIFRFTQA 155
Cdd:CHL00060 206 NDLYMEMKESGV-INEQNIA---ESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNkQDVLLFIDNIFRFVQA 277
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 23-155 1.04e-51

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: 163.68  E-value: 1.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694   23 GIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKahgGYSVFAGVGERTREGNDLYHEFIESKVNAdphnpdpn 102
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALK-------- 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 299737694  103 vksKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:pfam00006  70 ---RTVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEA 119
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 35-94 5.93e-05

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 40.82  E-value: 5.93e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694    35 KGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREGNDLYHEFIESKVNA 94
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 ...
 1-155 1.89e-111

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: 323.97  E-value: 1.89e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694   1 RAIHQEAPSYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREG 80
Cdd:COG0055  111 RPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREG 190

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 299737694  81 NDLYHEFIESKVNadphnpdpnvkSKCALVFGQMNEPPGARARVGLTGLTVAEHFRD-QGQDVLFFVDNIFRFTQA 155
Cdd:COG0055  191 NDLYREMKESGVL-----------DKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQA 255
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 1-155 3.62e-110

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: 314.16  E-value: 3.62e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694   1 RAIHQEAPSYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREG 80
Cdd:cd01133   32 WPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNIAKAHGGYSVFAGVGERTREG 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 299737694  81 NDLYHEFIESKVnadphnPDPNVKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQ-GQDVLFFVDNIFRFTQA 155
Cdd:cd01133  112 NDLYHEMKESGV------INLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEeGQDVLLFIDNIFRFTQA 181
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 2-155 2.26e-96

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: 285.46  E-value: 2.26e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694    2 AIHQEAPSYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREGN 81
Cdd:TIGR01039 109 PIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTREGN 188

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 299737694   82 DLYHEFIESkvnadphnpdpNVKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRD-QGQDVLFFVDNIFRFTQA 155
Cdd:TIGR01039 189 DLYHEMKES-----------GVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQA 252
atpB CHL00060
ATP synthase CF1 beta subunit
 1-155 2.87e-94

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 281.16  E-value: 2.87e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694   1 RAIHQEAPSYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREG 80
Cdd:CHL00060 126 SPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREG 205

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 299737694  81 NDLYHEFIESKVnADPHNPDpnvKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQG-QDVLFFVDNIFRFTQA 155
Cdd:CHL00060 206 NDLYMEMKESGV-INEQNIA---ESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNkQDVLLFIDNIFRFVQA 277
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 1-155 1.40e-66

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: 203.46  E-value: 1.40e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694   1 RAIHQEAPSYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREG 80
Cdd:cd19476   32 RPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKAHAGVVVFAGIGERGREV 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 299737694  81 NDLYHEFIESKvnadphnpdpnVKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:cd19476  112 NDLYEEFTKSG-----------AMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDISRYAEA 175
alt_F1F0_F1_bet TIGR03305
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ...
 1-155 3.91e-64

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: 202.36  E-value: 3.91e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694    1 RAIHQEAPSYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREG 80
Cdd:TIGR03305 103 RSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNMVGQHQGVSIFCGIGERCREG 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 299737694   81 NDLYHEFIESkvnadphnpdpNVKSKCALVFGQMNEPPGARARVGLTGLTVAEHFR-DQGQDVLFFVDNIFRFTQA 155
Cdd:TIGR03305 183 EELYREMKEA-----------GVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRdDEKQDVLLLIDNIFRFIQA 247
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 23-155 1.04e-51

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: 163.68  E-value: 1.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694   23 GIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKahgGYSVFAGVGERTREGNDLYHEFIESKVNAdphnpdpn 102
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALK-------- 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 299737694  103 vksKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:pfam00006  70 ---RTVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEA 119
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 1-155 2.02e-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: 2.02e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694   1 RAIHQEAPSYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAhggYSVFAGVGERTREG 80
Cdd:cd01136   32 RPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDAD---VNVIALIGERGREV 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 299737694  81 NdlyhEFIEskvnadpHNPDPNVKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:cd01136  109 R----EFIE-------KDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSLTRFAMA 172
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 1-155 3.36e-26

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: 102.03  E-value: 3.36e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694   1 RAIHQEAPSYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNvAKAHggYSVFAGVGERTREG 80
Cdd:COG1157  122 RPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIARN-TEAD--VNVIALIGERGREV 198

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 299737694  81 NdlyhEFIEskvnadpHNPDPNVKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:COG1157  199 R----EFIE-------DDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMA 262
PRK08149 PRK08149
FliI/YscN family ATPase;
1-155 4.29e-24

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 96.22  E-value: 4.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694   1 RAIHQEAPSYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNvakAHGGYSVFAGVGERTREg 80
Cdd:PRK08149 116 RVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGERGRE- 191

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 299737694  81 ndlYHEFIESKVNADPhnpdpnvKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:PRK08149 192 ---VTEFVESLRASSR-------REKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARA 256
fliI PRK06002
flagellar protein export ATPase FliI;
1-155 5.54e-24

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 96.22  E-value: 5.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694   1 RAIHQEAPSYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELinnvAKAHGGYSV-FAGVGERTRE 79
Cdd:PRK06002 130 MSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML----ARADAFDTVvIALVGERGRE 205

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 299737694  80 gndlYHEFIESKVNADphnpdpnvKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:PRK06002 206 ----VREFLEDTLADN--------LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHA 269
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
1-155 3.46e-21

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 88.33  E-value: 3.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694   1 RAIHQEAPSYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELinnVAKAHGGYSVFAGVGERTREg 80
Cdd:PRK06820 128 RELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGML---CADSAADVMVLALIGERGRE- 203

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 299737694  81 ndlYHEFIEskvnadpHNPDPNVKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:PRK06820 204 ---VREFLE-------QVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARA 268
fliI PRK08472
flagellar protein export ATPase FliI;
18-155 2.42e-19

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 83.20  E-value: 2.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694  18 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNvAKAHggYSVFAGVGERTREgndlYHEFIESKVNADPH 97
Cdd:PRK08472 139 EVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKG-CLAP--IKVVALIGERGRE----IPEFIEKNLGGDLE 211

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 299737694  98 NpdpnvkskCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:PRK08472 212 N--------TVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMA 261
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
3-155 2.64e-19

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 82.88  E-value: 2.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694   3 IHQEAPSYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNvakAHGGYSVFAGVGERTREgnd 82
Cdd:PRK06936 129 VYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRS---AEVDVTVLALIGERGRE--- 202

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 299737694  83 lYHEFIEskvnadpHNPDPNVKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:PRK06936 203 -VREFIE-------SDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARA 267
fliI PRK08927
flagellar protein export ATPase FliI;
23-155 4.11e-19

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 82.33  E-value: 4.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694  23 GIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAhggYSVFAGVGERTREgndlYHEFIEskvnaDPHNPDPN 102
Cdd:PRK08927 145 GVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGRE----VQEFLQ-----DDLGPEGL 212

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 299737694 103 VKSkcALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:PRK08927 213 ARS--VVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMA 263
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
 18-155 4.32e-19

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


Pssm-ID: 410878 [Multi-domain]  Cd Length: 288  Bit Score: 81.08  E-value: 4.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694  18 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELinnvAKahggYS-----VFAGVGERTREGNDLYHEFIESKv 92
Cdd:cd01134   58 VPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSL----SK----WSnsdvvIYVGCGERGNEMAEVLEEFPELK- 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 299737694  93 naDPHNPDPNVKSKCaLVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:cd01134  129 --DPITGESLMERTV-LIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEA 188
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
17-155 3.10e-17

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 77.30  E-value: 3.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694  17 AEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINnvaKAHGGYSVFAGVGERTREgndlYHEFIESKVnadp 96
Cdd:PRK07594 136 TQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGRE----VREFIDFTL---- 204

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 299737694  97 hnpDPNVKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:PRK07594 205 ---SEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARA 260
fliI PRK07721
flagellar protein export ATPase FliI;
18-155 6.29e-17

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 76.30  E-value: 6.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694  18 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAkahGGYSVFAGVGERTREgndlYHEFIESKVNadph 97
Cdd:PRK07721 140 EPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIARNTS---ADLNVIALIGERGRE----VREFIERDLG---- 208

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 299737694  98 npdPNVKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:PRK07721 209 ---PEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMA 263
fliI PRK06793
flagellar protein export ATPase FliI;
18-155 8.00e-17

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 76.17  E-value: 8.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694  18 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNvAKAHggYSVFAGVGERTREGNDlyheFIESKVNADPh 97
Cdd:PRK06793 138 DVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKAD--INVISLVGERGREVKD----FIRKELGEEG- 209

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 299737694  98 npdpnvKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:PRK06793 210 ------MRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADA 261
PRK05922 PRK05922
type III secretion system ATPase; Validated
 8-155 2.08e-15

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 71.86  E-value: 2.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694   8 PSYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTvliqELINNVAK-AHGGYSVFAGVGERTREgndlYHE 86
Cdd:PRK05922 129 PSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGRE----VRE 200

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 299737694  87 FIESKVNADPHNpdpnvksKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:PRK05922 201 YIEQHKEGLAAQ-------RTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAA 262
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
 18-155 5.95e-15

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 70.58  E-value: 5.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694  18 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELinnvAKahggYS-----VFAGVGERTREGNDLYHEFIESKv 92
Cdd:PRK04192 209 EPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQL----AK----WAdadivIYVGCGERGNEMTEVLEEFPELI- 279

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 299737694  93 naDPHNPDPNVKSKCaLVFGQMNEPPGAR-ARVgLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:PRK04192 280 --DPKTGRPLMERTV-LIANTSNMPVAAReASI-YTGITIAEYYRDMGYDVLLMADSTSRWAEA 339
fliI PRK08972
flagellar protein export ATPase FliI;
18-155 9.25e-15

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 70.11  E-value: 9.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694  18 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAkahGGYSVFAGVGERTREgndlYHEFIESKVNADPh 97
Cdd:PRK08972 144 EPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTT---ADVIVVGLVGERGRE----VKEFIEEILGEEG- 215

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 299737694  98 npdpnvKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:PRK08972 216 ------RARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQA 267
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 20-155 1.87e-13

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 66.33  E-value: 1.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694  20 LVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELinnvakAHGG---YSVFAGVGERTREgndlYHEFIESKVNADP 96
Cdd:PRK09099 147 LPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMF------ARGTqcdVNVIALIGERGRE----VREFIELILGEDG 216

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 299737694  97 hnpdpnvKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:PRK09099 217 -------MARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARA 268
fliI PRK07196
flagellar protein export ATPase FliI;
20-155 5.39e-12

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 62.22  E-value: 5.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694  20 LVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQeLINNVAKAHggYSVFAGVGERTREgndlYHEFIESKVNADPhnp 99
Cdd:PRK07196 139 LDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLG-MITRYTQAD--VVVVGLIGERGRE----VKEFIEHSLQAAG--- 208

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 299737694 100 dpnvKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:PRK07196 209 ----MAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMA 260
fliI PRK05688
flagellar protein export ATPase FliI;
18-155 5.98e-12

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 62.06  E-value: 5.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694  18 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQeLINNVAKAHggYSVFAGVGERTREgndlYHEFIEskvnadpH 97
Cdd:PRK05688 150 EPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLG-MMTRFTEAD--IIVVGLIGERGRE----VKEFIE-------H 215

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 299737694  98 NPDPNVKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:PRK05688 216 ILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQA 273
fliI PRK07960
flagellum-specific ATP synthase FliI;
18-155 1.13e-09

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 55.56  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694  18 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELinnvAKAHGGYSVFAG-VGERTREGNDlyheFIESKVNADP 96
Cdd:PRK07960 157 HVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMM----ARYTQADVIVVGlIGERGREVKD----FIENILGAEG 228

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 299737694  97 hnpdpnvKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:PRK07960 229 -------RARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMA 280
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 69-155 1.92e-09

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 55.03  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694   69 VFAGVGERTREGNDLYHEFIESKvnaDPHNPDPnVKSKCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDN 148
Cdd:PRK14698  686 IYIGCGERGNEMTDVLEEFPKLK---DPKTGKP-LMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADS 761


                  ....*..
gi 299737694  149 IFRFTQA 155
Cdd:PRK14698  762 TSRWAEA 768
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 1-147 7.83e-09

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 53.00  E-value: 7.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694   1 RAIHQEAPSYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVL-IQELINNvaKAHGGYSVFAGVGERT-- 77
Cdd:PRK13343 127 RPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIaIDAIINQ--KDSDVICVYVAIGQKAsa 204

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 299737694  78 -REGNDLYHEFieskvNADPHnpdpnvkskCALVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVD 147
Cdd:PRK13343 205 vARVIETLREH-----GALEY---------TTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYD 261
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 35-94 5.93e-05

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 40.82  E-value: 5.93e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694    35 KGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREGNDLYHEFIESKVNA 94
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS 60
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 20-89 6.27e-04

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 38.85  E-value: 6.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 299737694   20 LVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTV------LIQELinNVAKAHGGYSVFAGVGERTREGNDLYHEFIE 89
Cdd:PRK14698  211 LITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVdgdtliLTKEF--GLIKIKDLYEILDGKGKKTVEGNEEWTELEE 284
rho_factor_C cd01128
C-terminal ATP binding domain of transcription termination factor rho; Transcription ...
 25-155 6.97e-03

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


Pssm-ID: 410872 [Multi-domain]  Cd Length: 249  Bit Score: 35.64  E-value: 6.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299737694  25 KVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAG-VGERTREGNDlyheFIESkVNADphnpdpnv 103
Cdd:cd01128    5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRS-VKGE-------- 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 299737694 104 kskcaLVFGQMNEPPGARARVGLTGLTVAEHFRDQGQDVLFFVDNIFRFTQA 155
Cdd:cd01128   72 -----VVASTFDEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARA 118
 
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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