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Conserved domains on  [gi|1896828761|gb|QNL13486|]
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ATP synthase beta subunit, partial [Bradyrhizobium diazoefficiens]

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 ...
 3-156 3.61e-109

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: 318.19  E-value: 3.61e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   3 RAIHQEAPTYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREG 82
Cdd:COG0055   111 RPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREG 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896828761  83 NDLYHEFIESKVNadphnpdpsvkSKCALVFGQMNEPPGARARVALTGLTIAEDFRD-KGQDVLFFVDNIFRFTQ 156
Cdd:COG0055   191 NDLYREMKESGVL-----------DKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQ 254
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 3-156 3.61e-109

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: 318.19  E-value: 3.61e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   3 RAIHQEAPTYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREG 82
Cdd:COG0055   111 RPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREG 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896828761  83 NDLYHEFIESKVNadphnpdpsvkSKCALVFGQMNEPPGARARVALTGLTIAEDFRD-KGQDVLFFVDNIFRFTQ 156
Cdd:COG0055   191 NDLYREMKESGVL-----------DKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQ 254
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 3-156 4.75e-107

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: 306.45  E-value: 4.75e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   3 RAIHQEAPTYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREG 82
Cdd:cd01133    32 WPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNIAKAHGGYSVFAGVGERTREG 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896828761  83 NDLYHEFIESKVnadphnPDPSVKSKCALVFGQMNEPPGARARVALTGLTIAEDFRD-KGQDVLFFVDNIFRFTQ 156
Cdd:cd01133   112 NDLYHEMKESGV------INLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYFRDeEGQDVLLFIDNIFRFTQ 180
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 4-156 1.60e-93

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: 278.14  E-value: 1.60e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   4 AIHQEAPTYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREGN 83
Cdd:TIGR01039 109 PIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTREGN 188

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896828761  84 DLYHEFIESkvnadphnpdpSVKSKCALVFGQMNEPPGARARVALTGLTIAEDFRD-KGQDVLFFVDNIFRFTQ 156
Cdd:TIGR01039 189 DLYHEMKES-----------GVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQ 251
atpB CHL00060
ATP synthase CF1 beta subunit
 3-156 2.43e-91

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 273.84  E-value: 2.43e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   3 RAIHQEAPTYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREG 82
Cdd:CHL00060  126 SPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREG 205

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896828761  83 NDLYHEFIESKVnADPHNPDpsvKSKCALVFGQMNEPPGARARVALTGLTIAEDFRD-KGQDVLFFVDNIFRFTQ 156
Cdd:CHL00060  206 NDLYMEMKESGV-INEQNIA---ESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQ 276
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 25-156 9.67e-50

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: 158.67  E-value: 9.67e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761  25 GIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKahgGYSVFAGVGERTREGNDLYHEFIESKVNAdphnpdps 104
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALK-------- 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1896828761 105 vksKCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRFTQ 156
Cdd:pfam00006  70 ---RTVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAE 118
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 37-96 9.75e-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: 40.05  E-value: 9.75e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   37 KGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREGNDLYHEFIESKVNA 96
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 ...
 3-156 3.61e-109

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: 318.19  E-value: 3.61e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   3 RAIHQEAPTYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREG 82
Cdd:COG0055   111 RPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREG 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896828761  83 NDLYHEFIESKVNadphnpdpsvkSKCALVFGQMNEPPGARARVALTGLTIAEDFRD-KGQDVLFFVDNIFRFTQ 156
Cdd:COG0055   191 NDLYREMKESGVL-----------DKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQ 254
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 3-156 4.75e-107

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: 306.45  E-value: 4.75e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   3 RAIHQEAPTYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREG 82
Cdd:cd01133    32 WPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNIAKAHGGYSVFAGVGERTREG 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896828761  83 NDLYHEFIESKVnadphnPDPSVKSKCALVFGQMNEPPGARARVALTGLTIAEDFRD-KGQDVLFFVDNIFRFTQ 156
Cdd:cd01133   112 NDLYHEMKESGV------INLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYFRDeEGQDVLLFIDNIFRFTQ 180
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 4-156 1.60e-93

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: 278.14  E-value: 1.60e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   4 AIHQEAPTYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREGN 83
Cdd:TIGR01039 109 PIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTREGN 188

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896828761  84 DLYHEFIESkvnadphnpdpSVKSKCALVFGQMNEPPGARARVALTGLTIAEDFRD-KGQDVLFFVDNIFRFTQ 156
Cdd:TIGR01039 189 DLYHEMKES-----------GVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQ 251
atpB CHL00060
ATP synthase CF1 beta subunit
 3-156 2.43e-91

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 273.84  E-value: 2.43e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   3 RAIHQEAPTYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREG 82
Cdd:CHL00060  126 SPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREG 205

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896828761  83 NDLYHEFIESKVnADPHNPDpsvKSKCALVFGQMNEPPGARARVALTGLTIAEDFRD-KGQDVLFFVDNIFRFTQ 156
Cdd:CHL00060  206 NDLYMEMKESGV-INEQNIA---ESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQ 276
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 2-156 1.80e-65

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: 200.76  E-value: 1.80e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   2 LRAIHQEAPTYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTRE 81
Cdd:cd19476    31 RRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKAHAGVVVFAGIGERGRE 110

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896828761  82 GNDLYHEFIESKvnadphnpdpsVKSKCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRFTQ 156
Cdd:cd19476   111 VNDLYEEFTKSG-----------AMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDISRYAE 174
alt_F1F0_F1_bet TIGR03305
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ...
 3-156 1.44e-61

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: 195.81  E-value: 1.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   3 RAIHQEAPTYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREG 82
Cdd:TIGR03305 103 RSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNMVGQHQGVSIFCGIGERCREG 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896828761  83 NDLYHEFIESkvnadphnpdpSVKSKCALVFGQMNEPPGARARVALTGLTIAEDFR-DKGQDVLFFVDNIFRFTQ 156
Cdd:TIGR03305 183 EELYREMKEA-----------GVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRdDEKQDVLLLIDNIFRFIQ 246
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 25-156 9.67e-50

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: 158.67  E-value: 9.67e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761  25 GIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKahgGYSVFAGVGERTREGNDLYHEFIESKVNAdphnpdps 104
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALK-------- 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1896828761 105 vksKCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRFTQ 156
Cdd:pfam00006  70 ---RTVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAE 118
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 3-154 7.18e-31

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: 111.88  E-value: 7.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   3 RAIHQEAPTYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAhggYSVFAGVGERTREG 82
Cdd:cd01136    32 RPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDAD---VNVIALIGERGREV 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896828761  83 NdlyhEFIEskvnadpHNPDPSVKSKCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRF 154
Cdd:cd01136   109 R----EFIE-------KDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSLTRF 169
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 3-154 2.46e-24

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: 97.02  E-value: 2.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   3 RAIHQEAPTYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNvAKAHggYSVFAGVGERTREG 82
Cdd:COG1157   122 RPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIARN-TEAD--VNVIALIGERGREV 198

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896828761  83 NdlyhEFIEskvnadpHNPDPSVKSKCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRF 154
Cdd:COG1157   199 R----EFIE-------DDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRF 259
PRK08149 PRK08149
FliI/YscN family ATPase;
1-154 1.53e-22

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 91.98  E-value: 1.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   1 GLRAIHQEAPTYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNvakAHGGYSVFAGVGERTR 80
Cdd:PRK08149  114 EERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGERGR 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896828761  81 EgndlYHEFIESKVNAdphnpdpSVKSKCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRF 154
Cdd:PRK08149  191 E----VTEFVESLRAS-------SRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRY 253
fliI PRK06002
flagellar protein export ATPase FliI;
3-154 4.80e-22

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 90.83  E-value: 4.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   3 RAIHQEAPTYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELinnvAKAHGGYSV-FAGVGERTRE 81
Cdd:PRK06002  130 MSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML----ARADAFDTVvIALVGERGRE 205

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896828761  82 gndlYHEFIESKVNADphnpdpsvKSKCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRF 154
Cdd:PRK06002  206 ----VREFLEDTLADN--------LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVDSVTRF 266
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
2-154 1.22e-19

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 84.10  E-value: 1.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   2 LRAIHQEAPTYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELinnVAKAHGGYSVFAGVGERTRE 81
Cdd:PRK06820  127 WRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGML---CADSAADVMVLALIGERGRE 203

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896828761  82 gndlYHEFIEskvnadpHNPDPSVKSKCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRF 154
Cdd:PRK06820  204 ----VREFLE-------QVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRY 265
fliI PRK08472
flagellar protein export ATPase FliI;
20-154 2.23e-18

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 80.50  E-value: 2.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761  20 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNvAKAHggYSVFAGVGERTREgndlYHEFIESKVNADPH 99
Cdd:PRK08472  139 EVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKG-CLAP--IKVVALIGERGRE----IPEFIEKNLGGDLE 211

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1896828761 100 NpdpsvkskCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRF 154
Cdd:PRK08472  212 N--------TVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRF 258
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
 20-156 1.14e-17

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


Pssm-ID: 410878 [Multi-domain]  Cd Length: 288  Bit Score: 77.23  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761  20 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELinnvAKahggYS-----VFAGVGERTREGNDLYHEFIESKv 94
Cdd:cd01134    58 VPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSL----SK----WSnsdvvIYVGCGERGNEMAEVLEEFPELK- 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896828761  95 naDPHNPDPSVKSKCaLVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRFTQ 156
Cdd:cd01134   129 --DPITGESLMERTV-LIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAE 187
fliI PRK08927
flagellar protein export ATPase FliI;
25-154 2.72e-17

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 77.33  E-value: 2.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761  25 GIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAhggYSVFAGVGERTREgndlYHEFIEskvnaDPHNPDPS 104
Cdd:PRK08927  145 GVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGRE----VQEFLQ-----DDLGPEGL 212

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1896828761 105 VKSkcALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRF 154
Cdd:PRK08927  213 ARS--VVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRF 260
fliI PRK07721
flagellar protein export ATPase FliI;
9-154 6.55e-17

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 76.30  E-value: 6.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   9 APTYTDQSTE--------AEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAkahGGYSVFAGVGERTR 80
Cdd:PRK07721  121 APVSTDQDPPnplkrppiREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIARNTS---ADLNVIALIGERGR 197

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896828761  81 EgndlYHEFIESKVNadphnpdPSVKSKCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRF 154
Cdd:PRK07721  198 E----VREFIERDLG-------PEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRV 260
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
5-154 6.75e-17

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 76.33  E-value: 6.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   5 IHQEAPTYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNvakAHGGYSVFAGVGERTREgnd 84
Cdd:PRK06936  129 VYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRS---AEVDVTVLALIGERGRE--- 202

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761  85 lYHEFIEskvnadpHNPDPSVKSKCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRF 154
Cdd:PRK06936  203 -VREFIE-------SDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRF 264
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
19-156 2.84e-16

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 74.60  E-value: 2.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761  19 AEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINnvaKAHGGYSVFAGVGERTREgndlYHEFIESKVnadp 98
Cdd:PRK07594  136 TQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGRE----VREFIDFTL---- 204

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1896828761  99 hnpDPSVKSKCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRFTQ 156
Cdd:PRK07594  205 ---SEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYAR 259
fliI PRK06793
flagellar protein export ATPase FliI;
2-154 1.36e-15

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 72.70  E-value: 1.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   2 LRAIHQEAPTYTDQSTE--AEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNvAKAHggYSVFAGVGERT 79
Cdd:PRK06793  118 LQKIKLDAPPIHAFEREeiTDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKAD--INVISLVGERG 194

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896828761  80 REGNDlyheFIESKVNADPhnpdpsvKSKCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRF 154
Cdd:PRK06793  195 REVKD----FIRKELGEEG-------MRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRF 258
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
 20-145 1.01e-13

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 67.11  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761  20 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELinnvAKahggYS-----VFAGVGERTREGNDLYHEFIESKv 94
Cdd:PRK04192  209 EPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQL----AK----WAdadivIYVGCGERGNEMTEVLEEFPELI- 279

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1896828761  95 naDPHNPDPSVKSKCaLVFGQMNEPPGAR-ARVaLTGLTIAEDFRDKGQDVL 145
Cdd:PRK04192  280 --DPKTGRPLMERTV-LIANTSNMPVAAReASI-YTGITIAEYYRDMGYDVL 327
fliI PRK08972
flagellar protein export ATPase FliI;
20-156 1.73e-13

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 66.65  E-value: 1.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761  20 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAkahGGYSVFAGVGERTREgndlYHEFIESKVNADPh 99
Cdd:PRK08972  144 EPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTT---ADVIVVGLVGERGRE----VKEFIEEILGEEG- 215

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1896828761 100 npdpsvKSKCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRFTQ 156
Cdd:PRK08972  216 ------RARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQ 266
PRK05922 PRK05922
type III secretion system ATPase; Validated
 20-154 7.05e-13

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 64.93  E-value: 7.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761  20 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTvliqELINNVAK-AHGGYSVFAGVGERTREgndlYHEFIESKVNADP 98
Cdd:PRK05922  139 EIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGRE----VREYIEQHKEGLA 210

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1896828761  99 HNpdpsvksKCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRF 154
Cdd:PRK05922  211 AQ-------RTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRW 259
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 22-154 1.46e-12

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 64.02  E-value: 1.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761  22 LVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNvakAHGGYSVFAGVGERTREgndlYHEFIESKVNADPhnp 101
Cdd:PRK09099  147 LPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARG---TQCDVNVIALIGERGRE----VREFIELILGEDG--- 216

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1896828761 102 dpsvKSKCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRF 154
Cdd:PRK09099  217 ----MARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRF 265
fliI PRK07960
flagellum-specific ATP synthase FliI;
20-154 1.06e-11

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 61.34  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761  20 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELinnvAKAHGGYSVFAG-VGERTREGNDlyheFIESKVNADP 98
Cdd:PRK07960  157 HVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMM----ARYTQADVIVVGlIGERGREVKD----FIENILGAEG 228

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1896828761  99 hnpdpsvKSKCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRF 154
Cdd:PRK07960  229 -------RARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRY 277
fliI PRK05688
flagellar protein export ATPase FliI;
20-156 1.06e-11

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 61.28  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761  20 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQeLINNVAKAHggYSVFAGVGERTREgndlYHEFIEskvnadpH 99
Cdd:PRK05688  150 EPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLG-MMTRFTEAD--IIVVGLIGERGRE----VKEFIE-------H 215

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1896828761 100 NPDPSVKSKCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRFTQ 156
Cdd:PRK05688  216 ILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQ 272
fliI PRK07196
flagellar protein export ATPase FliI;
22-154 1.58e-11

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 61.06  E-value: 1.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761  22 LVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIQeLINNVAKAHggYSVFAGVGERTREgndlYHEFIEskvnadpHNP 101
Cdd:PRK07196  139 LDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLG-MITRYTQAD--VVVVGLIGERGRE----VKEFIE-------HSL 204

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1896828761 102 DPSVKSKCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRF 154
Cdd:PRK07196  205 QAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRY 257
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 71-156 1.49e-08

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 52.72  E-value: 1.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   71 VFAGVGERTREGNDLYHEFIESKvnaDPHNPDPsVKSKCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDN 150
Cdd:PRK14698   686 IYIGCGERGNEMTDVLEEFPKLK---DPKTGKP-LMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADS 761


                   ....*.
gi 1896828761  151 IFRFTQ 156
Cdd:PRK14698   762 TSRWAE 767
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 3-149 1.53e-07

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 49.53  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   3 RAIHQEAPTYTDQSTEAEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVL-IQELINNvaKAHGGYSVFAGVGERT-- 79
Cdd:PRK13343  127 RPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIaIDAIINQ--KDSDVICVYVAIGQKAsa 204

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1896828761  80 -REGNDLYHEFieskvNADPHnpdpsvkskCALVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVD 149
Cdd:PRK13343  205 vARVIETLREH-----GALEY---------TTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYD 261
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 37-96 9.75e-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: 40.05  E-value: 9.75e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761   37 KGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAGVGERTREGNDLYHEFIESKVNA 96
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS 60
PRK12608 PRK12608
transcription termination factor Rho; Provisional
 27-155 2.11e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237150 [Multi-domain]  Cd Length: 380  Bit Score: 40.07  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761  27 KVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAG-VGERTREGNDLYHefieskvnadphnpdpSV 105
Cdd:PRK12608  122 RVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDMRR----------------SV 185

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1896828761 106 KSKcalVFGQMN-EPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRFT 155
Cdd:PRK12608  186 KGE---VYASTFdRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLA 233
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 22-91 7.03e-04

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 38.85  E-value: 7.03e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896828761   22 LVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTV------LIQELinNVAKAHGGYSVFAGVGERTREGNDLYHEFIE 91
Cdd:PRK14698   211 LITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVdgdtliLTKEF--GLIKIKDLYEILDGKGKKTVEGNEEWTELEE 284
rho_factor_C cd01128
C-terminal ATP binding domain of transcription termination factor rho; Transcription ...
 27-154 4.41e-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: 36.03  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896828761  27 KVVDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNVAKAHGGYSVFAG-VGERTREGNDlyheFIESkVNADphnpdpsv 105
Cdd:cd01128     5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRS-VKGE-------- 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1896828761 106 kskcaLVFGQMNEPPGARARVALTGLTIAEDFRDKGQDVLFFVDNIFRF 154
Cdd:cd01128    72 -----VVASTFDEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRL 115
 
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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