|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-172 |
2.51e-124 |
|
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: 357.48 E-value: 2.51e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHG 80
Cdd:COG0055 96 GEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 GYSVFAGVGERTREGNDLYHEMIESNVNKlgggegsKAALVYGQMNEPPGARARVALTGLTIAENFRD-EGQDVLFFVDN 159
Cdd:COG0055 176 GVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDN 248
|
170
....*....|...
gi 2486681384 160 IFRFTQAGSEVSA 172
Cdd:COG0055 249 IFRFTQAGSEVSA 261
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
1-172 |
2.83e-122 |
|
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: 345.36 E-value: 2.83e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHG 80
Cdd:cd01133 17 GEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNIAKAHG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 GYSVFAGVGERTREGNDLYHEMIESNVNKLGGgeGSKAALVYGQMNEPPGARARVALTGLTIAENFRD-EGQDVLFFVDN 159
Cdd:cd01133 97 GYSVFAGVGERTREGNDLYHEMKESGVINLDG--LSKVALVYGQMNEPPGARARVALTGLTMAEYFRDeEGQDVLLFIDN 174
|
170
....*....|...
gi 2486681384 160 IFRFTQAGSEVSA 172
Cdd:cd01133 175 IFRFTQAGSEVSA 187
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
1-172 |
8.50e-108 |
|
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: 315.51 E-value: 8.50e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHG 80
Cdd:TIGR01039 93 GEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 GYSVFAGVGERTREGNDLYHEMIESNVNKlgggegsKAALVYGQMNEPPGARARVALTGLTIAENFRDE-GQDVLFFVDN 159
Cdd:TIGR01039 173 GYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTMAEYFRDEqGQDVLLFIDN 245
|
170
....*....|...
gi 2486681384 160 IFRFTQAGSEVSA 172
Cdd:TIGR01039 246 IFRFTQAGSEVSA 258
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
1-172 |
1.88e-107 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 315.44 E-value: 1.88e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHG 80
Cdd:CHL00060 111 GEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 GYSVFAGVGERTREGNDLYHEMIESNVNKLGGGEGSKAALVYGQMNEPPGARARVALTGLTIAENFRDEG-QDVLFFVDN 159
Cdd:CHL00060 191 GVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNkQDVLLFIDN 270
|
170
....*....|...
gi 2486681384 160 IFRFTQAGSEVSA 172
Cdd:CHL00060 271 IFRFVQAGSEVSA 283
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
38-172 |
4.26e-52 |
|
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: 165.22 E-value: 4.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 38 GIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKahgGYSVFAGVGERTREGNDLYHEMIESNVNKlgggegsK 117
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALK-------R 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2486681384 118 AALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDNIFRFTQAGSEVSA 172
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISL 125
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
50-169 |
2.23e-06 |
|
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: 45.06 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 50 KGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESNVNKLGGGEgskaalvygqmnepp 129
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGEL--------------- 65
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2486681384 130 gaRARVALTGLtiaenfRDEGQDVLFFvDNIFRFTQAGSE 169
Cdd:smart00382 66 --RLRLALALA------RKLKPDVLIL-DEITSLLDAEQE 96
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-172 |
2.51e-124 |
|
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: 357.48 E-value: 2.51e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHG 80
Cdd:COG0055 96 GEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 GYSVFAGVGERTREGNDLYHEMIESNVNKlgggegsKAALVYGQMNEPPGARARVALTGLTIAENFRD-EGQDVLFFVDN 159
Cdd:COG0055 176 GVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDN 248
|
170
....*....|...
gi 2486681384 160 IFRFTQAGSEVSA 172
Cdd:COG0055 249 IFRFTQAGSEVSA 261
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
1-172 |
2.83e-122 |
|
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: 345.36 E-value: 2.83e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHG 80
Cdd:cd01133 17 GEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNIAKAHG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 GYSVFAGVGERTREGNDLYHEMIESNVNKLGGgeGSKAALVYGQMNEPPGARARVALTGLTIAENFRD-EGQDVLFFVDN 159
Cdd:cd01133 97 GYSVFAGVGERTREGNDLYHEMKESGVINLDG--LSKVALVYGQMNEPPGARARVALTGLTMAEYFRDeEGQDVLLFIDN 174
|
170
....*....|...
gi 2486681384 160 IFRFTQAGSEVSA 172
Cdd:cd01133 175 IFRFTQAGSEVSA 187
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
1-172 |
8.50e-108 |
|
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: 315.51 E-value: 8.50e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHG 80
Cdd:TIGR01039 93 GEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 GYSVFAGVGERTREGNDLYHEMIESNVNKlgggegsKAALVYGQMNEPPGARARVALTGLTIAENFRDE-GQDVLFFVDN 159
Cdd:TIGR01039 173 GYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTMAEYFRDEqGQDVLLFIDN 245
|
170
....*....|...
gi 2486681384 160 IFRFTQAGSEVSA 172
Cdd:TIGR01039 246 IFRFTQAGSEVSA 258
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
1-172 |
1.88e-107 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 315.44 E-value: 1.88e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHG 80
Cdd:CHL00060 111 GEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 GYSVFAGVGERTREGNDLYHEMIESNVNKLGGGEGSKAALVYGQMNEPPGARARVALTGLTIAENFRDEG-QDVLFFVDN 159
Cdd:CHL00060 191 GVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNkQDVLLFIDN 270
|
170
....*....|...
gi 2486681384 160 IFRFTQAGSEVSA 172
Cdd:CHL00060 271 IFRFVQAGSEVSA 283
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
1-172 |
4.52e-75 |
|
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: 225.80 E-value: 4.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHG 80
Cdd:cd19476 17 GEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKAHA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 GYSVFAGVGERTREGNDLYHEMIESNVNklgggegSKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDNI 160
Cdd:cd19476 97 GVVVFAGIGERGREVNDLYEEFTKSGAM-------ERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDI 169
|
170
....*....|..
gi 2486681384 161 FRFTQAGSEVSA 172
Cdd:cd19476 170 SRYAEALREMSA 181
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
1-171 |
1.96e-68 |
|
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: 214.30 E-value: 1.96e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHG 80
Cdd:TIGR03305 88 GNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNMVGQHQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 GYSVFAGVGERTREGNDLYHEMIESNVNklgggegSKAALVYGQMNEPPGARARVALTGLTIAENFR-DEGQDVLFFVDN 159
Cdd:TIGR03305 168 GVSIFCGIGERCREGEELYREMKEAGVL-------DNTVMVFGQMNEPPGARFRVGHTALTMAEYFRdDEKQDVLLLIDN 240
|
170
....*....|..
gi 2486681384 160 IFRFTQAGSEVS 171
Cdd:TIGR03305 241 IFRFIQAGSEVS 252
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
38-172 |
4.26e-52 |
|
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: 165.22 E-value: 4.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 38 GIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKahgGYSVFAGVGERTREGNDLYHEMIESNVNKlgggegsK 117
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALK-------R 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2486681384 118 AALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDNIFRFTQAGSEVSA 172
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISL 125
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
1-171 |
1.58e-34 |
|
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: 121.90 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAhg 80
Cdd:cd01136 17 GEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDAD-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 gYSVFAGVGERTREGNdlyhEMIEsnvNKLGGGEGSKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDNI 160
Cdd:cd01136 95 -VNVIALIGERGREVR----EFIE---KDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSL 166
|
170
....*....|.
gi 2486681384 161 FRFTQAGSEVS 171
Cdd:cd01136 167 TRFAMAQREVG 177
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
1-170 |
8.15e-30 |
|
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: 112.43 E-value: 8.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKAHg 80
Cdd:COG1157 107 GRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIARN-TEAD- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 gYSVFAGVGERTREGNdlyhEMIESNVnklgGGEG-SKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDN 159
Cdd:COG1157 185 -VNVIALIGERGREVR----EFIEDDL----GEEGlARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDS 255
|
170
....*....|.
gi 2486681384 160 IFRFTQAGSEV 170
Cdd:COG1157 256 LTRFAMAQREI 266
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
1-170 |
6.77e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 107.78 E-value: 6.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKR-AIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinnvAKAH 79
Cdd:PRK06002 114 GEPIDGLGPLAPGTRPmSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML----ARAD 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 80 GGYSV-FAGVGERTREgndlYHEMIESNVnklgGGEGSKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVD 158
Cdd:PRK06002 190 AFDTVvIALVGERGRE----VREFLEDTL----ADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVD 261
|
170
....*....|..
gi 2486681384 159 NIFRFTQAGSEV 170
Cdd:PRK06002 262 SVTRFAHAAREV 273
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
1-170 |
9.88e-22 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 90.58 E-value: 9.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvakAHG 80
Cdd:PRK06936 112 GQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRS---AEV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 GYSVFAGVGERTREgndlYHEMIESNVnklgGGEG-SKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDN 159
Cdd:PRK06936 189 DVTVLALIGERGRE----VREFIESDL----GEEGlRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDS 260
|
170
....*....|.
gi 2486681384 160 IFRFTQAGSEV 170
Cdd:PRK06936 261 VTRFARAQREI 271
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
1-171 |
1.16e-21 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 90.42 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVT-ASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAh 79
Cdd:PRK08927 107 GEPIDGKGPLPQgPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 80 ggYSVFAGVGERTREgndlYHEMIESNVnklgGGEG-SKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVD 158
Cdd:PRK08927 186 --VSVIGLIGERGRE----VQEFLQDDL----GPEGlARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMD 255
|
170
....*....|...
gi 2486681384 159 NIFRFTQAGSEVS 171
Cdd:PRK08927 256 SVTRFAMAQREIG 268
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
1-170 |
2.15e-21 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 89.36 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLiMELINNVAKAHg 80
Cdd:PRK08472 107 GRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTL-MGMIVKGCLAP- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 gYSVFAGVGERTREgndlYHEMIESNVnklgGGEGSKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDNI 160
Cdd:PRK08472 185 -IKVVALIGERGRE----IPEFIEKNL----GGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSV 255
|
170
....*....|
gi 2486681384 161 FRFTQAGSEV 170
Cdd:PRK08472 256 TRFAMAQREI 265
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
5-166 |
9.25e-21 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 87.74 E-value: 9.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 5 DEAGPIVTASK-RAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvakAHGGYS 83
Cdd:PRK08149 104 DAPPTVGPISEeRVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVF 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 84 VFAGVGERTREGNDLYHEMIESnvnklggGEGSKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDNIFRF 163
Cdd:PRK08149 181 VIGLIGERGREVTEFVESLRAS-------SRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRY 253
|
...
gi 2486681384 164 TQA 166
Cdd:PRK08149 254 ARA 256
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
1-171 |
7.70e-20 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 85.25 E-value: 7.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDeAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinnVAKAHG 80
Cdd:PRK06820 114 GAPID-GGPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGML---CADSAA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 GYSVFAGVGERTREgndlYHEMIESNvnkLGGGEGSKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDNI 160
Cdd:PRK06820 190 DVMVLALIGERGRE----VREFLEQV---LTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSL 262
|
170
....*....|.
gi 2486681384 161 FRFTQAGSEVS 171
Cdd:PRK06820 263 TRYARAAREIG 273
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
1-170 |
4.92e-19 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 82.85 E-value: 4.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLiMELINNVAKAHg 80
Cdd:PRK07721 108 GEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTL-MGMIARNTSAD- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 gYSVFAGVGERTREgndlYHEMIESNVnklgGGEG-SKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDN 159
Cdd:PRK07721 186 -LNVIALIGERGRE----VREFIERDL----GPEGlKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDS 256
|
170
....*....|.
gi 2486681384 160 IFRFTQAGSEV 170
Cdd:PRK07721 257 VTRVAMAQREI 267
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
1-170 |
4.34e-18 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 80.20 E-value: 4.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvakAHG 80
Cdd:PRK09099 113 GEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARG---TQC 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 GYSVFAGVGERTREgndlYHEMIEsnvnKLGGGEG-SKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDN 159
Cdd:PRK09099 190 DVNVIALIGERGRE----VREFIE----LILGEDGmARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDS 261
|
170
....*....|.
gi 2486681384 160 IFRFTQAGSEV 170
Cdd:PRK09099 262 LTRFARAQREI 272
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
1-171 |
4.41e-18 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 80.13 E-value: 4.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLI-MELINNVAKAh 79
Cdd:PRK08972 112 GNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLgMMTRGTTADV- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 80 ggySVFAGVGERTREGNDLYHEMIesnvnklgGGEG-SKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVD 158
Cdd:PRK08972 191 ---IVVGLVGERGREVKEFIEEIL--------GEEGrARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMD 259
|
170
....*....|...
gi 2486681384 159 NIFRFTQAGSEVS 171
Cdd:PRK08972 260 SLTRYAQAQREIA 272
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
1-170 |
6.52e-17 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 76.94 E-value: 6.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKraIHQDAPAY--VEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKA 78
Cdd:PRK06793 106 GEVLNEEAENIPLQK--IKLDAPPIhaFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 79 HggYSVFAGVGERTREGNDLyhemiesnVNKLGGGEG-SKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFV 157
Cdd:PRK06793 183 D--INVISLVGERGREVKDF--------IRKELGEEGmRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMM 252
|
170
....*....|...
gi 2486681384 158 DNIFRFTQAGSEV 170
Cdd:PRK06793 253 DSVTRFADARRSV 265
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
23-171 |
7.84e-17 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 76.53 E-value: 7.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 23 PAYVEQSTeAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINnvaKAHGGYSVFAGVGERTREGNDLYHEM 102
Cdd:PRK07594 128 PAMVRQPI-TQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGREVREFIDFT 203
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486681384 103 IESNVNKlgggegsKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDNIFRFTQAGSEVS 171
Cdd:PRK07594 204 LSEETRK-------RCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIA 265
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
1-171 |
8.36e-16 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 73.78 E-value: 8.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTvlimELINNVAK-AH 79
Cdd:PRK05922 107 GNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 80 GGYSVFAGVGERTREgndlYHEMIESNVNKLgggEGSKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDN 159
Cdd:PRK05922 183 STINVIALIGERGRE----VREYIEQHKEGL---AAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDS 255
|
170
....*....|..
gi 2486681384 160 IFRFTQAGSEVS 171
Cdd:PRK05922 256 LSRWIAALQEVA 267
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
35-171 |
1.03e-14 |
|
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: 69.91 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 35 LVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinnvAKahggYS-----VFAGVGERTREGNDLYHEMIESNVNK 109
Cdd:cd01134 60 LLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSL----SK----WSnsdvvIYVGCGERGNEMAEVLEEFPELKDPI 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2486681384 110 LGGGEGSKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDNIFRFTQAGSEVS 171
Cdd:cd01134 132 TGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREIS 193
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
1-171 |
7.46e-14 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 67.99 E-value: 7.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLiMELINNVAKAHg 80
Cdd:PRK07196 105 GEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVL-LGMITRYTQAD- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 gYSVFAGVGERTREgndlYHEMIEsnvNKLGGGEGSKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDNI 160
Cdd:PRK07196 183 -VVVVGLIGERGRE----VKEFIE---HSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSL 254
|
170
....*....|.
gi 2486681384 161 FRFTQAGSEVS 171
Cdd:PRK07196 255 TRYAMAQREIA 265
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
1-171 |
1.31e-13 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 67.45 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLiMELINNVAKAHg 80
Cdd:PRK05688 118 GRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVL-LGMMTRFTEAD- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 gYSVFAGVGERTREgndlYHEMIEsnvnKLGGGEG-SKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDN 159
Cdd:PRK05688 196 -IIVVGLIGERGRE----VKEFIE----HILGEEGlKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDS 266
|
170
....*....|..
gi 2486681384 160 IFRFTQAGSEVS 171
Cdd:PRK05688 267 LTRFAQAQREIA 278
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
33-171 |
5.10e-12 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 62.88 E-value: 5.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 33 QILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVlimeLINNVAKAHGGYSVFAG-VGERTREGNDLyhemIEsnvNKLG 111
Cdd:PRK07960 157 HVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSV----LLGMMARYTQADVIVVGlIGERGREVKDF----IE---NILG 225
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 112 GGEGSKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDNIFRFTQAGSEVS 171
Cdd:PRK07960 226 AEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIA 285
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
1-171 |
7.16e-12 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 62.63 E-value: 7.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKAHG 80
Cdd:PRK13343 112 GRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN-QKDSD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 GYSVFAGVGERTREGNdlyhEMIESnVNKLGGGEGSkaALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDNI 160
Cdd:PRK13343 191 VICVYVAIGQKASAVA----RVIET-LREHGALEYT--TVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDL 263
|
170
....*....|.
gi 2486681384 161 FRFTQAGSEVS 171
Cdd:PRK13343 264 SKHAAAYRELS 274
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
1-171 |
2.36e-09 |
|
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: 54.87 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKAHG 80
Cdd:cd01132 19 GNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTAIAIDTIIN-QKGKK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 GYSVFAGVGERTREGNDLYHEMIESnvnklggGEGSKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDNI 160
Cdd:cd01132 98 VYCIYVAIGQKRSTVAQIVKTLEEH-------GAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGKHALIIYDDL 170
|
170
....*....|.
gi 2486681384 161 FRFTQAGSEVS 171
Cdd:cd01132 171 SKQAVAYRQMS 181
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
35-171 |
1.44e-08 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 52.86 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 35 LVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinnvAKahggYS-----VFAGVGERTREGNDLYHEMIESNVNK 109
Cdd:PRK04192 211 LITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQL----AK----WAdadivIYVGCGERGNEMTEVLEEFPELIDPK 282
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486681384 110 LGGGEGSKAALVYGQMNEPPGAR-ARVaLTGLTIAENFRDEGQDVLFFVDNIFRFTQAGSEVS 171
Cdd:PRK04192 283 TGRPLMERTVLIANTSNMPVAAReASI-YTGITIAEYYRDMGYDVLLMADSTSRWAEALREIS 344
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
84-172 |
2.86e-08 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 52.33 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 84 VFAGVGERTREGNDLYHEMIESNVNKLGGGEGSKAALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDNIFRF 163
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRW 765
|
....*....
gi 2486681384 164 TQAGSEVSA 172
Cdd:PRK14698 766 AEALREISG 774
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
50-169 |
2.23e-06 |
|
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: 45.06 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 50 KGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESNVNKLGGGEgskaalvygqmnepp 129
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGEL--------------- 65
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2486681384 130 gaRARVALTGLtiaenfRDEGQDVLFFvDNIFRFTQAGSE 169
Cdd:smart00382 66 --RLRLALALA------RKLKPDVLIL-DEITSLLDAEQE 96
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
40-166 |
8.22e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 41.61 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 40 KVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAG-VGERTREGNDLyhemiesnvnklgggEGSKA 118
Cdd:PRK12608 122 RVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDM---------------RRSVK 186
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2486681384 119 ALVYGQMN-EPPGARARVALTGLTIAENFRDEGQDVLFFVDNIFRFTQA 166
Cdd:PRK12608 187 GEVYASTFdRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARA 235
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
1-154 |
9.46e-05 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 41.59 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKAHG 80
Cdd:PRK09281 112 GQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIIN-QKGKD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 GYSVFAGVGERtregndlyhemiESNVnklgggegskAALV-----YGQM----------NEPPGARARVALTGLTIAEN 145
Cdd:PRK09281 191 VICIYVAIGQK------------ASTV----------AQVVrkleeHGAMeytivvaataSDPAPLQYLAPYAGCAMGEY 248
|
....*....
gi 2486681384 146 FRDEGQDVL 154
Cdd:PRK09281 249 FMDNGKDAL 257
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
40-166 |
2.77e-04 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 39.88 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 40 KVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAG-VGERTREGNDlyheMIESnvnklgggegSKA 118
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRS----------VKG 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2486681384 119 ALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDNIFRFTQA 166
Cdd:cd01128 71 EVVASTFDEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARA 118
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
35-104 |
3.17e-04 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 40.39 E-value: 3.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486681384 35 LVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTV----LIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIE 104
Cdd:PRK14698 211 LITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVdgdtLILTKEFGLIKIKDLYEILDGKGKKTVEGNEEWTELEE 284
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
1-171 |
1.65e-03 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 38.02 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 1 GEPVDEAGPIVTASKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKAHG 80
Cdd:CHL00059 91 AKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN-QKGQN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 81 GYSVFAGVGERTREgndlyhemIESNVNKLGGGEGSKAALVYGQMNEPPGARARVA-LTGLTIAENFRDEGQDVLFFVDN 159
Cdd:CHL00059 170 VICVYVAIGQKASS--------VAQVVTTLQERGAMEYTIVVAETADSPATLQYLApYTGAALAEYFMYRGRHTLIIYDD 241
|
170
....*....|..
gi 2486681384 160 IFRFTQAGSEVS 171
Cdd:CHL00059 242 LSKQAQAYRQMS 253
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
40-171 |
5.51e-03 |
|
transcription termination factor Rho; This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding. [Transcription, Transcription factors]
Pssm-ID: 162030 [Multi-domain] Cd Length: 415 Bit Score: 36.59 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486681384 40 KVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGG-YSVFAGVGERTREGNDlyheMIESnvnklgggegSKA 118
Cdd:TIGR00767 157 RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEvELIVLLIDERPEEVTD----MQRS----------VKG 222
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2486681384 119 ALVYGQMNEPPGARARVALTGLTIAENFRDEGQDVLFFVDNIFRFTQAGSEVS 171
Cdd:TIGR00767 223 EVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVT 275
|
|
| |
