|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-169 |
1.69e-121 |
|
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: 350.16 E-value: 1.69e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 1 MNVIGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVA 80
Cdd:COG0055 92 FNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 81 KAHGGYSVFAGVGERTREGNDLYHEMIESGVNKhgggegsKAALVYGQMNEPPGARARVALTGLTVAEHFRD-QGQDVLF 159
Cdd:COG0055 172 KEHGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLL 244
|
170
....*....|
gi 374279412 160 FVDNIFRFTQ 169
Cdd:COG0055 245 FIDNIFRFTQ 254
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
1-169 |
1.25e-120 |
|
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: 341.12 E-value: 1.25e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 1 MNVIGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVA 80
Cdd:cd01133 13 FNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNIA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 81 KAHGGYSVFAGVGERTREGNDLYHEMIESGVNKHGGgeGSKAALVYGQMNEPPGARARVALTGLTVAEHFRDQ-GQDVLF 159
Cdd:cd01133 93 KAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDG--LSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEeGQDVLL 170
|
170
....*....|
gi 374279412 160 FVDNIFRFTQ 169
Cdd:cd01133 171 FIDNIFRFTQ 180
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
1-169 |
1.59e-105 |
|
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: 309.34 E-value: 1.59e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 1 MNVIGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVA 80
Cdd:TIGR01039 89 FNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 81 KAHGGYSVFAGVGERTREGNDLYHEMIESGVNKhgggegsKAALVYGQMNEPPGARARVALTGLTVAEHFRD-QGQDVLF 159
Cdd:TIGR01039 169 KEHGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLL 241
|
170
....*....|
gi 374279412 160 FVDNIFRFTQ 169
Cdd:TIGR01039 242 FIDNIFRFTQ 251
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
2-169 |
7.13e-105 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 308.89 E-value: 7.13e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 2 NVIGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAK 81
Cdd:CHL00060 108 NVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 82 AHGGYSVFAGVGERTREGNDLYHEMIESGV-NKHGGGEgSKAALVYGQMNEPPGARARVALTGLTVAEHFRDQG-QDVLF 159
Cdd:CHL00060 188 AHGGVSVFGGVGERTREGNDLYMEMKESGViNEQNIAE-SKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNkQDVLL 266
|
170
....*....|
gi 374279412 160 FVDNIFRFTQ 169
Cdd:CHL00060 267 FIDNIFRFVQ 276
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
42-169 |
1.27e-49 |
|
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: 1.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 42 GIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKahgGYSVFAGVGERTREGNDLYHEMIESGVNKhgggegsK 121
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALK-------R 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 374279412 122 AALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFVDNIFRFTQ 169
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAE 118
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
54-167 |
3.89e-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: 44.29 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 54 KGGKIGLFGGAGVGKTVLIMELINNVAKAHGGysVFAGVGERTREGNDLYHEMIESGVNKHGGGegskaalvygqmnepP 133
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG--VIYIDGEDILEEVLDQLLLIIVGGKKASGS---------------G 63
|
90 100 110
....*....|....*....|....*....|....
gi 374279412 134 GARARVALTGLtvaehfRDQGQDVLFFvDNIFRF 167
Cdd:smart00382 64 ELRLRLALALA------RKLKPDVLIL-DEITSL 90
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-169 |
1.69e-121 |
|
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: 350.16 E-value: 1.69e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 1 MNVIGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVA 80
Cdd:COG0055 92 FNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 81 KAHGGYSVFAGVGERTREGNDLYHEMIESGVNKhgggegsKAALVYGQMNEPPGARARVALTGLTVAEHFRD-QGQDVLF 159
Cdd:COG0055 172 KEHGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLL 244
|
170
....*....|
gi 374279412 160 FVDNIFRFTQ 169
Cdd:COG0055 245 FIDNIFRFTQ 254
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
1-169 |
1.25e-120 |
|
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: 341.12 E-value: 1.25e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 1 MNVIGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVA 80
Cdd:cd01133 13 FNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNIA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 81 KAHGGYSVFAGVGERTREGNDLYHEMIESGVNKHGGgeGSKAALVYGQMNEPPGARARVALTGLTVAEHFRDQ-GQDVLF 159
Cdd:cd01133 93 KAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDG--LSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEeGQDVLL 170
|
170
....*....|
gi 374279412 160 FVDNIFRFTQ 169
Cdd:cd01133 171 FIDNIFRFTQ 180
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
1-169 |
1.59e-105 |
|
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: 309.34 E-value: 1.59e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 1 MNVIGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVA 80
Cdd:TIGR01039 89 FNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 81 KAHGGYSVFAGVGERTREGNDLYHEMIESGVNKhgggegsKAALVYGQMNEPPGARARVALTGLTVAEHFRD-QGQDVLF 159
Cdd:TIGR01039 169 KEHGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLL 241
|
170
....*....|
gi 374279412 160 FVDNIFRFTQ 169
Cdd:TIGR01039 242 FIDNIFRFTQ 251
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
2-169 |
7.13e-105 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 308.89 E-value: 7.13e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 2 NVIGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAK 81
Cdd:CHL00060 108 NVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 82 AHGGYSVFAGVGERTREGNDLYHEMIESGV-NKHGGGEgSKAALVYGQMNEPPGARARVALTGLTVAEHFRDQG-QDVLF 159
Cdd:CHL00060 188 AHGGVSVFGGVGERTREGNDLYMEMKESGViNEQNIAE-SKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNkQDVLL 266
|
170
....*....|
gi 374279412 160 FVDNIFRFTQ 169
Cdd:CHL00060 267 FIDNIFRFVQ 276
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
1-169 |
9.30e-74 |
|
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: 222.33 E-value: 9.30e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 1 MNVIGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVA 80
Cdd:cd19476 13 LDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 81 KAHGGYSVFAGVGERTREGNDLYHEMIESGVNkhgggegSKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFF 160
Cdd:cd19476 93 KAHAGVVVFAGIGERGREVNDLYEEFTKSGAM-------ERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLI 165
|
....*....
gi 374279412 161 VDNIFRFTQ 169
Cdd:cd19476 166 IDDISRYAE 174
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
1-169 |
3.78e-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: 213.53 E-value: 3.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 1 MNVIGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVA 80
Cdd:TIGR03305 84 FDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNMV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 81 KAHGGYSVFAGVGERTREGNDLYHEMIESGVNKHgggegskAALVYGQMNEPPGARARVALTGLTVAEHFR-DQGQDVLF 159
Cdd:TIGR03305 164 GQHQGVSIFCGIGERCREGEELYREMKEAGVLDN-------TVMVFGQMNEPPGARFRVGHTALTMAEYFRdDEKQDVLL 236
|
170
....*....|
gi 374279412 160 FVDNIFRFTQ 169
Cdd:TIGR03305 237 LIDNIFRFIQ 246
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
42-169 |
1.27e-49 |
|
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: 1.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 42 GIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKahgGYSVFAGVGERTREGNDLYHEMIESGVNKhgggegsK 121
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALK-------R 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 374279412 122 AALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFVDNIFRFTQ 169
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAE 118
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
2-167 |
2.28e-35 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 123.82 E-value: 2.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 2 NVIGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAK 81
Cdd:cd01136 14 DALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 82 AhggYSVFAGVGERTREGNdlyhEMIEsgvnKHGGGEG-SKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFF 160
Cdd:cd01136 94 D---VNVIALIGERGREVR----EFIE----KDLGEEGlKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLL 162
|
....*..
gi 374279412 161 VDNIFRF 167
Cdd:cd01136 163 MDSLTRF 169
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
5-167 |
1.14e-31 |
|
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: 117.44 E-value: 1.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 5 GEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKAHg 84
Cdd:COG1157 107 GRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIARN-TEAD- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 85 gYSVFAGVGERTREGNdlyhEMIEsgvnKHGGGEG-SKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFVDN 163
Cdd:COG1157 185 -VNVIALIGERGREVR----EFIE----DDLGEEGlARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDS 255
|
....
gi 374279412 164 IFRF 167
Cdd:COG1157 256 LTRF 259
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
2-167 |
7.01e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 112.78 E-value: 7.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 2 NVIGEPVDEAGPLTTA-HKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinnvA 80
Cdd:PRK06002 111 NALGEPIDGLGPLAPGtRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML----A 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 81 KAHGGYSV-FAGVGERTREgndlYHEMIESGVnkhgGGEGSKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLF 159
Cdd:PRK06002 187 RADAFDTVvIALVGERGRE----VREFLEDTL----ADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLL 258
|
....*...
gi 374279412 160 FVDNIFRF 167
Cdd:PRK06002 259 IVDSVTRF 266
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
2-167 |
1.68e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 95.43 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 2 NVIGEPVDEAGPLTT-AHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVA 80
Cdd:PRK08927 104 NALGEPIDGKGPLPQgPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNAD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 81 KAhggYSVFAGVGERTREgndlYHEMIESGVnkhgGGEG-SKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLF 159
Cdd:PRK08927 184 AD---VSVIGLIGERGRE----VQEFLQDDL----GPEGlARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLC 252
|
....*...
gi 374279412 160 FVDNIFRF 167
Cdd:PRK08927 253 LMDSVTRF 260
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
2-167 |
3.92e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 91.67 E-value: 3.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 2 NVIGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLiMELINNVAK 81
Cdd:PRK08472 104 DPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTL-MGMIVKGCL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 82 AHggYSVFAGVGERTREgndlYHEMIEsgvnKHGGGEGSKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFV 161
Cdd:PRK08472 183 AP--IKVVALIGERGRE----IPEFIE----KNLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIM 252
|
....*.
gi 374279412 162 DNIFRF 167
Cdd:PRK08472 253 DSVTRF 258
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
4-167 |
3.95e-22 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 91.35 E-value: 3.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 4 IGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvakAH 83
Cdd:PRK06936 111 LGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRS---AE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 84 GGYSVFAGVGERTREgndlYHEMIESGVnkhgGGEG-SKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFVD 162
Cdd:PRK06936 188 VDVTVLALIGERGRE----VREFIESDL----GEEGlRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMD 259
|
....*
gi 374279412 163 NIFRF 167
Cdd:PRK06936 260 SVTRF 264
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
2-167 |
6.77e-22 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 90.82 E-value: 6.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 2 NVIGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvak 81
Cdd:PRK08149 98 KIVERFDAPPTVGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH--- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 82 AHGGYSVFAGVGERTREGNDLYHEMIESGvnkhgggEGSKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFV 161
Cdd:PRK08149 175 SEADVFVIGLIGERGREVTEFVESLRASS-------RREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFI 247
|
....*.
gi 374279412 162 DNIFRF 167
Cdd:PRK08149 248 DSMTRY 253
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
1-167 |
8.29e-21 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 87.95 E-value: 8.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 1 MNVIGEPVDeAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinnVA 80
Cdd:PRK06820 110 LDGLGAPID-GGPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGML---CA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 81 KAHGGYSVFAGVGERTREgndlYHEMIESGVNKHGGgegSKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFF 160
Cdd:PRK06820 186 DSAADVMVLALIGERGRE----VREFLEQVLTPEAR---ARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLM 258
|
....*..
gi 374279412 161 VDNIFRF 167
Cdd:PRK06820 259 ADSLTRY 265
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
1-167 |
7.72e-19 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 82.08 E-value: 7.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 1 MNVIGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLiMELINNVA 80
Cdd:PRK07721 104 LDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTL-MGMIARNT 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 81 KAHggYSVFAGVGERTREgndlYHEMIEsgvnKHGGGEG-SKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLF 159
Cdd:PRK07721 183 SAD--LNVIALIGERGRE----VREFIE----RDLGPEGlKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVML 252
|
....*...
gi 374279412 160 FVDNIFRF 167
Cdd:PRK07721 253 MMDSVTRV 260
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
4-169 |
1.54e-18 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 81.29 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 4 IGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLI-MELINNVAKA 82
Cdd:PRK08972 111 VGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLgMMTRGTTADV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 83 hggySVFAGVGERTREGNDLYHEMIesgvnkhgGGEG-SKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFV 161
Cdd:PRK08972 191 ----IVVGLVGERGREVKEFIEEIL--------GEEGrARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLM 258
|
....*...
gi 374279412 162 DNIFRFTQ 169
Cdd:PRK08972 259 DSLTRYAQ 266
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
1-167 |
3.53e-18 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 80.41 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 1 MNVIGEPVDEAGPLTTAHKraIHQDAPAY--VEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINN 78
Cdd:PRK06793 102 LSANGEVLNEEAENIPLQK--IKLDAPPIhaFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 79 vAKAHggYSVFAGVGERTREGNDLyhemiesgVNKHGGGEG-SKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDV 157
Cdd:PRK06793 180 -AKAD--INVISLVGERGREVKDF--------IRKELGEEGmRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNV 248
|
170
....*....|
gi 374279412 158 LFFVDNIFRF 167
Cdd:PRK06793 249 LLMMDSVTRF 258
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
5-167 |
7.55e-18 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 79.56 E-value: 7.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 5 GEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTvlimELINNVAK-AH 83
Cdd:PRK05922 107 GNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 84 GGYSVFAGVGERTREGNDLyhemiesgVNKHGGG-EGSKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFVD 162
Cdd:PRK05922 183 STINVIALIGERGREVREY--------IEQHKEGlAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMD 254
|
....*
gi 374279412 163 NIFRF 167
Cdd:PRK05922 255 SLSRW 259
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
4-167 |
1.75e-17 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 78.27 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 4 IGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvakAH 83
Cdd:PRK09099 112 LGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARG---TQ 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 84 GGYSVFAGVGERTREgndlYHEMIESGVnkhgGGEG-SKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFVD 162
Cdd:PRK09099 189 CDVNVIALIGERGRE----VREFIELIL----GEDGmARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMD 260
|
....*
gi 374279412 163 NIFRF 167
Cdd:PRK09099 261 SLTRF 265
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
27-169 |
2.97e-15 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 71.91 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 27 PAYVEQSTeAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINnvaKAHGGYSVFAGVGERTREgndlYHEM 106
Cdd:PRK07594 128 PAMVRQPI-TQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGRE----VREF 199
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374279412 107 IESGVNKHGggeGSKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFVDNIFRFTQ 169
Cdd:PRK07594 200 IDFTLSEET---RKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYAR 259
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
2-162 |
3.11e-15 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 71.87 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 2 NVIGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAK 81
Cdd:PRK13343 109 DPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN-QK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 82 AHGGYSVFAGVGERTREGNdlyhEMIESgVNKHGGGEGSkaALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFV 161
Cdd:PRK13343 188 DSDVICVYVAIGQKASAVA----RVIET-LREHGALEYT--TVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVY 260
|
.
gi 374279412 162 D 162
Cdd:PRK13343 261 D 261
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
39-169 |
9.74e-15 |
|
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: 9.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 39 LVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinnvAKahggYS-----VFAGVGERTREGNDLYHEMIESGVNK 113
Cdd:cd01134 60 LLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSL----SK----WSnsdvvIYVGCGERGNEMAEVLEEFPELKDPI 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 374279412 114 HGGGEGSKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFVDNIFRFTQ 169
Cdd:cd01134 132 TGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAE 187
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
1-169 |
5.23e-14 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 68.60 E-value: 5.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 1 MNVIGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLiMELINNVA 80
Cdd:PRK05688 114 LDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVL-LGMMTRFT 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 81 KAHggYSVFAGVGERTREgndlYHEMIESGVnkhgGGEG-SKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLF 159
Cdd:PRK05688 193 EAD--IIVVGLIGERGRE----VKEFIEHIL----GEEGlKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLL 262
|
170
....*....|
gi 374279412 160 FVDNIFRFTQ 169
Cdd:PRK05688 263 LMDSLTRFAQ 272
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
1-167 |
6.38e-14 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 68.38 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 1 MNVIGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLiMELINNVA 80
Cdd:PRK07196 101 INGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVL-LGMITRYT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 81 KAHggYSVFAGVGERTREgndlYHEMIESGVnkhgGGEG-SKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLF 159
Cdd:PRK07196 180 QAD--VVVVGLIGERGRE----VKEFIEHSL----QAAGmAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLL 249
|
....*...
gi 374279412 160 FVDNIFRF 167
Cdd:PRK07196 250 LVDSLTRY 257
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
2-162 |
1.18e-10 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 58.34 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 2 NVIGEPVDEAGPLTTAHKRAIHQDAPAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAK 81
Cdd:cd01132 16 DALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTAIAIDTIIN-QK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 82 AHGGYSVFAGVGERTREGNDLYHEMIESGVNKHgggegskAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFV 161
Cdd:cd01132 95 GKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEY-------TIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGKHALIIY 167
|
.
gi 374279412 162 D 162
Cdd:cd01132 168 D 168
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
37-167 |
6.73e-10 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 56.72 E-value: 6.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 37 QILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVlimeLINNVAKAHGGYSVFAG-VGERTREGNDLYHEMIesgvnkhg 115
Cdd:PRK07960 157 HVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSV----LLGMMARYTQADVIVVGlIGERGREVKDFIENIL-------- 224
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 374279412 116 GGEG-SKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFVDNIFRF 167
Cdd:PRK07960 225 GAEGrARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRY 277
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
39-158 |
6.76e-08 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 50.94 E-value: 6.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 39 LVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinnvAKahggYS-----VFAGVGERTRE--------------- 98
Cdd:PRK04192 211 LITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQL----AK----WAdadivIYVGCGERGNEmtevleefpelidpk 282
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 374279412 99 -GNDLYHEMIesgvnkhgggegskaaLVYGQMNEPPGAR-ARVaLTGLTVAEHFRDQGQDVL 158
Cdd:PRK04192 283 tGRPLMERTV----------------LIANTSNMPVAAReASI-YTGITIAEYYRDMGYDVL 327
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
88-169 |
4.10e-07 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 48.86 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 88 VFAGVGERTREGNDLYHEMIESGVNKHGGGEGSKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFVDNIFRF 167
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRW 765
|
..
gi 374279412 168 TQ 169
Cdd:PRK14698 766 AE 767
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
54-167 |
3.89e-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: 44.29 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 54 KGGKIGLFGGAGVGKTVLIMELINNVAKAHGGysVFAGVGERTREGNDLYHEMIESGVNKHGGGegskaalvygqmnepP 133
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG--VIYIDGEDILEEVLDQLLLIIVGGKKASGS---------------G 63
|
90 100 110
....*....|....*....|....*....|....
gi 374279412 134 GARARVALTGLtvaehfRDQGQDVLFFvDNIFRF 167
Cdd:smart00382 64 ELRLRLALALA------RKLKPDVLIL-DEITSL 90
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
39-126 |
1.30e-04 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 41.55 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 39 LVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTV----LIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMiESGVNKH 114
Cdd:PRK14698 211 LITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVdgdtLILTKEFGLIKIKDLYEILDGKGKKTVEGNEEWTEL-EEPITLY 289
|
90
....*....|....*.
gi 374279412 115 GGGEGS----KAALVY 126
Cdd:PRK14698 290 GYKDGKiveiKATHVY 305
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
44-168 |
3.85e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 39.68 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 44 KVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAG-VGERTREGNDLyhemiesgvnkhgggEGSKA 122
Cdd:PRK12608 122 RVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDM---------------RRSVK 186
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 374279412 123 ALVYGQMN-EPPGARARVALTGLTVAEHFRDQGQDVLFFVDNIFRFT 168
Cdd:PRK12608 187 GEVYASTFdRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLA 233
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
44-167 |
7.99e-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: 38.73 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 44 KVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAG-VGERTREGNDlyheMIESGvnkhgggegsKA 122
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRSV----------KG 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 374279412 123 ALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFVDNIFRF 167
Cdd:cd01128 71 EVVASTFDEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRL 115
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
26-164 |
8.75e-04 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 38.87 E-value: 8.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374279412 26 APAYVEQSTEAQILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINN-------VAKAHGGYSVFAGVGERTRE 98
Cdd:PTZ00185 160 APNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINqvrinqqILSKNAVISIYVSIGQRCSN 239
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 374279412 99 GNDLYHEMIESGVNKHGGGEGSKAAlvygqmnEPPGARARVALTGLTVAEHFRDQGQDVLFFVDNI 164
Cdd:PTZ00185 240 VARIHRLLRSYGALRYTTVMAATAA-------EPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDL 298
|
|
| |
