|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-294 |
0e+00 |
|
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: 628.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:COG0055 89 GRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIH 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 81 NIAKGHGGTSVFAGVGERTREGNDLYHEFLDANVIakdadgnaisegSKVALVYGQMNEPPGARARVALSGLTIAEYFRD 160
Cdd:COG0055 169 NIAKEHGGVSVFAGVGERTREGNDLYREMKESGVL------------DKTALVFGQMNEPPGARLRVALTALTMAEYFRD 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 161 VENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITSTNKGSITSVQAVYVPADDLTDPAPATS 240
Cdd:COG0055 237 EEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATT 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 371560958 241 FAHLDATTVLNRAISELGIYPAVDPLDSTSRVLEPRVVGQEHYETARAVQSILQ 294
Cdd:COG0055 317 FAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQ 370
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
1-294 |
0e+00 |
|
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: 560.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:TIGR01039 86 GRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 81 NIAKGHGGTSVFAGVGERTREGNDLYHEFLDANVIakdadgnaisegSKVALVYGQMNEPPGARARVALSGLTIAEYFRD 160
Cdd:TIGR01039 166 NIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVI------------DKTALVYGQMNEPPGARMRVALTGLTMAEYFRD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 161 VENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITSTNKGSITSVQAVYVPADDLTDPAPATS 240
Cdd:TIGR01039 234 EQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATT 313
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 371560958 241 FAHLDATTVLNRAISELGIYPAVDPLDSTSRVLEPRVVGQEHYETARAVQSILQ 294
Cdd:TIGR01039 314 FAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQ 367
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
1-275 |
0e+00 |
|
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: 557.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:cd01133 10 GRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELIN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 81 NIAKGHGGTSVFAGVGERTREGNDLYHEFLDANVIAKDadgnaisEGSKVALVYGQMNEPPGARARVALSGLTIAEYFRD 160
Cdd:cd01133 90 NIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLD-------GLSKVALVYGQMNEPPGARARVALTGLTMAEYFRD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 161 VENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITSTNKGSITSVQAVYVPADDLTDPAPATS 240
Cdd:cd01133 163 EEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPATT 242
|
250 260 270
....*....|....*....|....*....|....*
gi 371560958 241 FAHLDATTVLNRAISELGIYPAVDPLDSTSRVLEP 275
Cdd:cd01133 243 FAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
1-294 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 556.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:CHL00060 104 GRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELIN 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 81 NIAKGHGGTSVFAGVGERTREGNDLYHEFLDANVIakdaDGNAISEgSKVALVYGQMNEPPGARARVALSGLTIAEYFRD 160
Cdd:CHL00060 184 NIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVI----NEQNIAE-SKVALVYGQMNEPPGARMRVGLTALTMAEYFRD 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 161 VENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITSTNKGSITSVQAVYVPADDLTDPAPATS 240
Cdd:CHL00060 259 VNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATT 338
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 371560958 241 FAHLDATTVLNRAISELGIYPAVDPLDSTSRVLEPRVVGQEHYETARAVQSILQ 294
Cdd:CHL00060 339 FAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQ 392
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
1-293 |
3.17e-126 |
|
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: 367.23 E-value: 3.17e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:TIGR03305 81 SRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIH 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 81 NIAKGHGGTSVFAGVGERTREGNDLYHEFLDANVIakdadgnaisegSKVALVYGQMNEPPGARARVALSGLTIAEYFRD 160
Cdd:TIGR03305 161 NMVGQHQGVSIFCGIGERCREGEELYREMKEAGVL------------DNTVMVFGQMNEPPGARFRVGHTALTMAEYFRD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 161 VENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITSTNKGSITSVQAVYVPADDLTDPAPATS 240
Cdd:TIGR03305 229 DEKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHT 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 371560958 241 FAHLDATTVLNRAISELGIYPAVDPLDSTSRVLEPRVVGQEHYETARAVQSIL 293
Cdd:TIGR03305 309 FSHLSASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTL 361
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
1-272 |
1.89e-121 |
|
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: 348.68 E-value: 1.89e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:cd19476 10 GRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLAR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 81 NIAKGHGGTSVFAGVGERTREGNDLYHEFLDANVIakdadgnaisegSKVALVYGQMNEPPGARARVALSGLTIAEYFRD 160
Cdd:cd19476 90 NQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAM------------ERTVVVANTANDPPGARMRVPYTGLTIAEYFRD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 161 VEnQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITSTN--KGSITSVQAVYVPADDLTDPAPA 238
Cdd:cd19476 158 NG-QHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDPIPD 236
|
250 260 270
....*....|....*....|....*....|....
gi 371560958 239 TSFAHLDATTVLNRAISELGIYPAVDPLDSTSRV 272
Cdd:cd19476 237 NTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
45-270 |
5.49e-92 |
|
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: 271.54 E-value: 5.49e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 45 GIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKGhggTSVFAGVGERTREGNDLYHEFLDANVIAKdadgnai 124
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASAD---VVVYALIGERGREVREFIEELLGSGALKR------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 125 segskVALVYGQMNEPPGARARVALSGLTIAEYFRDvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDM 204
Cdd:pfam00006 71 -----TVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 371560958 205 GQLQERITSTN--KGSITSVQAVYVPADDLTDPAPATSFAHLDATTVLNRAISELGIYPAVDPLDSTS 270
Cdd:pfam00006 145 ARLLERAGRVKgkGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
1-272 |
1.00e-55 |
|
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: 180.83 E-value: 1.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:cd01136 10 GRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIAR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 81 NIAkghGGTSVFAGVGERTREGNdlyhEFLDanviaKDADGNAISegsKVALVYGQMNEPPGARARVALSGLTIAEYFRD 160
Cdd:cd01136 90 NTD---ADVNVIALIGERGREVR----EFIE-----KDLGEEGLK---RSVLVVATSDESPLLRVRAAYTATAIAEYFRD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 161 vENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITSTNKGSITSVQAVYVPADDLTDPAPATS 240
Cdd:cd01136 155 -QGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEV 233
|
250 260 270
....*....|....*....|....*....|..
gi 371560958 241 FAHLDATTVLNRAISELGIYPAVDPLDSTSRV 272
Cdd:cd01136 234 RSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
1-293 |
2.03e-49 |
|
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: 169.06 E-value: 2.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:COG1157 100 GRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIAR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 81 NiakghggTS----VFAGVGERTREGNdlyhEFLDAN----------VIAKDADgnaisegskvalvygqmnEPPGARAR 146
Cdd:COG1157 180 N-------TEadvnVIALIGERGREVR----EFIEDDlgeeglarsvVVVATSD------------------EPPLMRLR 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 147 VALSGLTIAEYFRDvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITSTNKGSITSVQAVY 226
Cdd:COG1157 231 AAYTATAIAEYFRD-QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVL 309
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 371560958 227 VPADDLTDPAPATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRVLePRVVGQEHYETARAVQSIL 293
Cdd:COG1157 310 VEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM-PDIVSPEHRALARRLRRLL 375
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
1-271 |
1.20e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 162.47 E-value: 1.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAA-EVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELi 79
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 80 nniAKGHG-GTSVFAGVGERTREgndlYHEFLDanviakDADGNAISegsKVALVYGQMNEPPGARARVALSGLTIAEYF 158
Cdd:PRK06002 186 ---ARADAfDTVVIALVGERGRE----VREFLE------DTLADNLK---KAVAVVATSDESPMMRRLAPLTATAIAEYF 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 159 RDvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERI--TSTNKGSITSVQAVYVPADDLTDPA 236
Cdd:PRK06002 250 RD-RGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPV 328
|
250 260 270
....*....|....*....|....*....|....*
gi 371560958 237 PATSFAHLDATTVLNRAISELGIYPAVDPLDSTSR 271
Cdd:PRK06002 329 ADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISR 363
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
1-287 |
5.68e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 157.54 E-value: 5.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIhAKAP------EFVDQstdasILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL 74
Cdd:PRK08472 100 GRVVDPLGRPIDGKGAIDYERYAPI-MKAPiaamkrGLIDE-----VFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 75 IqeliNNIAKG-HGGTSVFAGVGERTREgndlYHEFldanvIAKDADGNAisegSKVALVYGQMNEPPGARARVALSGLT 153
Cdd:PRK08472 174 M----GMIVKGcLAPIKVVALIGERGRE----IPEF-----IEKNLGGDL----ENTVIVVATSDDSPLMRKYGAFCAMS 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 154 IAEYFRDvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITST-NKGSITSVQAVYVPADDL 232
Cdd:PRK08472 237 VAEYFKN-QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEeGKGSITAFFTVLVEGDDM 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 371560958 233 TDPAPATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRVLEpRVVGQEHYETAR 287
Cdd:PRK08472 316 SDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAAR 369
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
1-293 |
9.70e-42 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 149.19 E-value: 9.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRsPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:PRK06820 107 GRILDGLGAPIDGGPPLTGQWR-ELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 81 NIAkghGGTSVFAGVGERTREgndlYHEFLDANVIAKDAdgnaisegSKVALVYGQMNEPPGARARVALSGLTIAEYFRD 160
Cdd:PRK06820 186 DSA---ADVMVLALIGERGRE----VREFLEQVLTPEAR--------ARTVVVVATSDRPALERLKGLSTATTIAEYFRD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 161 vENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITSTNKGSITSVQAVYVPADDLTDPAPATS 240
Cdd:PRK06820 251 -RGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEV 329
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 371560958 241 FAHLDATTVLNRAISELGIYPAVDPLDSTSRVLePRVVGQEHYETARAVQSIL 293
Cdd:PRK06820 330 RSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRML 381
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
1-293 |
1.02e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 146.38 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIqeliN 80
Cdd:PRK08972 105 GRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLL----G 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 81 NIAKGHGGTSVFAG-VGERTREGNDLYHEFLD------ANVIAKDADGNaisegskvalvygqmnepPGARARVALSGLT 153
Cdd:PRK08972 181 MMTRGTTADVIVVGlVGERGREVKEFIEEILGeegrarSVVVAAPADTS------------------PLMRLKGCETATT 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 154 IAEYFRDvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERIT--STNKGSITSVQAVYVPADD 231
Cdd:PRK08972 243 IAEYFRD-QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGngGPGQGSITAFYTVLTEGDD 321
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 371560958 232 LTDPAPATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRVLePRVVGQEHYETARAVQSIL 293
Cdd:PRK08972 322 LQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVY 382
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
1-293 |
1.37e-39 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 143.35 E-value: 1.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:PRK06936 105 GRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIR 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 81 NIAkghGGTSVFAGVGERTREgndlYHEFLDANVIAkdadgnaisEGSKVA-LVYGQMNEPPGARARVALSGLTIAEYFR 159
Cdd:PRK06936 185 SAE---VDVTVLALIGERGRE----VREFIESDLGE---------EGLRKAvLVVATSDRPSMERAKAGFVATSIAEYFR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 160 DvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITSTNKGSITSVQAVYVPADDLTDPAPAT 239
Cdd:PRK06936 249 D-QGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVADE 327
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 371560958 240 SFAHLDATTVLNRAISELGIYPAVDPLDSTSRVLEpRVVGQEHYETARAVQSIL 293
Cdd:PRK06936 328 TRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELL 380
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
1-293 |
7.64e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 138.57 E-value: 7.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAA-EVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELI 79
Cdd:PRK08927 100 GRVVNALGEPIDGKGPLPQgPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 80 NNIAkghGGTSVFAGVGERTREgndlYHEFLDANViakDADGNAISegskvALVYGQMNEPPGARARVALSGLTIAEYFR 159
Cdd:PRK08927 180 RNAD---ADVSVIGLIGERGRE----VQEFLQDDL---GPEGLARS-----VVVVATSDEPALMRRQAAYLTLAIAEYFR 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 160 DvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERI--TSTNKGSITSVQAVYVPADDLTDPAP 237
Cdd:PRK08927 245 D-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPVA 323
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 371560958 238 ATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRVLePRVVGQEHYETARAVQSIL 293
Cdd:PRK08927 324 DAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLM 378
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
1-293 |
5.18e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 133.56 E-value: 5.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:PRK06793 99 GKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 81 NiAKGHggTSVFAGVGERTREGNDLyhefldanvIAKDADGNAISegsKVALVYGQMNEPPGARARVALSGLTIAEYFRD 160
Cdd:PRK06793 179 N-AKAD--INVISLVGERGREVKDF---------IRKELGEEGMR---KSVVVVATSDESHLMQLRAAKLATSIAEYFRD 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 161 vENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAvGYQPTLSTDMGQLQERITSTNKGSITSVQAVYVPADDLTDPAPATS 240
Cdd:PRK06793 244 -QGNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLA 321
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 371560958 241 FAHLDATTVLNRAISELGIYPAVDPLDSTSRVLEpRVVGQEHYETARAVQSIL 293
Cdd:PRK06793 322 RGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPNHWQLANEMRKIL 373
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
1-293 |
9.24e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 130.23 E-value: 9.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEER------GPVAAEvRSPihakaPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL 74
Cdd:PRK07721 101 GQVLDALGEPLDGSalpkglAPVSTD-QDP-----PNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 75 IQELINNIAkghGGTSVFAGVGERTREgndlYHEFldanvIAKDADgnaiSEG-SKVALVYGQMNEPPGARARVALSGLT 153
Cdd:PRK07721 175 MGMIARNTS---ADLNVIALIGERGRE----VREF-----IERDLG----PEGlKRSIVVVATSDQPALMRIKGAYTATA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 154 IAEYFRDvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITSTNKGSITSVQAVYVPADDLT 233
Cdd:PRK07721 239 IAEYFRD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMN 317
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 234 DPAPATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRVLePRVVGQEHYETARAVQSIL 293
Cdd:PRK07721 318 EPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELL 376
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
1-287 |
2.01e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 129.85 E-value: 2.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:PRK05688 111 GRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTR 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 81 NIAkghGGTSVFAGVGERTREgndlYHEFLDaNVIAKdadgnaisEGSKVALVYGQ-MNEPPGARARVALSGLTIAEYFR 159
Cdd:PRK05688 191 FTE---ADIIVVGLIGERGRE----VKEFIE-HILGE--------EGLKRSVVVASpADDAPLMRLRAAMYCTRIAEYFR 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 160 DvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITSTNKG--SITSVQAVYVPADDLTDPAP 237
Cdd:PRK05688 255 D-KGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGggSITAFYTVLSEGDDQQDPIA 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 371560958 238 ATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRVLePRVVGQEHYETAR 287
Cdd:PRK05688 334 DSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQ 382
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
1-293 |
7.28e-34 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 127.96 E-value: 7.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELin 80
Cdd:PRK09099 106 GRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMF-- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 81 niAKG-HGGTSVFAGVGERTREGNDLYHEFLDANVIAKDADGNAISEGSKVAlvygqmneppgaRARVALSGLTIAEYFR 159
Cdd:PRK09099 184 --ARGtQCDVNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIE------------RAKAAYVATAIAEYFR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 160 DvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITSTNKGSITSVQAVYVPADDLTDPAPAT 239
Cdd:PRK09099 250 D-RGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEE 328
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 371560958 240 SFAHLDATTVLNRAISELGIYPAVDPLDSTSRVLePRVVGQEHYETARAVQSIL 293
Cdd:PRK09099 329 VRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLL 381
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
1-293 |
1.70e-32 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 124.29 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERgPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:PRK07594 99 GRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 81 niAKGhGGTSVFAGVGERTREgndlYHEFLDaNVIAKDADgnaisegSKVALVYGQMNEPPGARARVALSGLTIAEYFRD 160
Cdd:PRK07594 178 --APD-ADSNVLVLIGERGRE----VREFID-FTLSEETR-------KRCVIVVATSDRPALERVRALFVATTIAEFFRD 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 161 vENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITSTNKGSITSVQAVYVPADDLTDPAPATS 240
Cdd:PRK07594 243 -NGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFYTVLVEGDDMNEPLADEV 321
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 371560958 241 FAHLDATTVLNRAISELGIYPAVDPLDSTSRVLePRVVGQEHYETARAVQSIL 293
Cdd:PRK07594 322 RSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCL 373
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
1-294 |
3.47e-31 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 120.48 E-value: 3.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGpvAAEVRsPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:PRK08149 97 GKIVERFDAPPTVGP--ISEER-VIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 81 niakgHGGTSVF--AGVGERTREGNDLYHEFldanviakdadgNAISEGSKVALVYGQMNEPPGARARVALSGLTIAEYF 158
Cdd:PRK08149 174 -----HSEADVFviGLIGERGREVTEFVESL------------RASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 159 RDvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITSTNKGSITSVQAVYVPADDLTDPAPA 238
Cdd:PRK08149 237 RD-QGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGD 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 371560958 239 TSFAHLDATTVLNRAISELGIYPAVDPLDSTSRVLEpRVVGQEHYETARAVQSILQ 294
Cdd:PRK08149 316 EIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFG-QVTDPKHRQLAAAFRKLLT 370
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
1-290 |
3.89e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 120.38 E-value: 3.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEvrSPIHAKAPEF--VDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIqel 78
Cdd:PRK07196 98 GRVINGLGEPLDGKGQLGGS--TPLQQQLPQIhpLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLL--- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 79 iNNIAKGHGGTSVFAG-VGERTREgndlYHEFLDAnviAKDADGNAisegsKVALVYGQMNEPPGARARVALSGLTIAEY 157
Cdd:PRK07196 173 -GMITRYTQADVVVVGlIGERGRE----VKEFIEH---SLQAAGMA-----KSVVVAAPADESPLMRIKATELCHAIATY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 158 FRDvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERI-TSTNKGSITSVQAVYVPADDLTDPA 236
Cdd:PRK07196 240 YRD-KGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGTMTAIYTVLAEGDDQQDPI 318
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 371560958 237 PATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRVLEpRVVGQEHYETARAVQ 290
Cdd:PRK07196 319 VDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLK 371
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
1-293 |
7.59e-25 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 103.32 E-value: 7.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIqeliN 80
Cdd:PRK07960 118 GRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLL----G 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 81 NIAKGHGGTSVFAG-VGERTREGNDLYHEFLDAN------VIAKDADgnaISegskvalvygqmnepPGARARVALSGLT 153
Cdd:PRK07960 194 MMARYTQADVIVVGlIGERGREVKDFIENILGAEgrarsvVIAAPAD---VS---------------PLLRMQGAAYATR 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 154 IAEYFRDvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITS--TNKGSITSVQAVYVPADD 231
Cdd:PRK07960 256 IAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDD 334
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 371560958 232 LTDPAPATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRVLEpRVVGQEHYETARAVQSIL 293
Cdd:PRK07960 335 QQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMT-ALIDEQHYARVRQFKQLL 395
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
1-271 |
1.08e-23 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 97.29 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGV-GKTVLIQelI 79
Cdd:cd01135 12 GRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLpHNELAAQ--I 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 80 NNIAKGHGGTS----VFAGVGERTREGNDLYHEFLDANVIakdadgnaisegSKVALVYGQMNEPPGARARVALSGLTIA 155
Cdd:cd01135 90 ARQAGVVGSEEnfaiVFAAMGVTMEEARFFKDDFEETGAL------------ERVVLFLNLANDPTIERIITPRMALTTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 156 EYFRDVENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQER--ITSTNKGSITSVQAVYVPADDLT 233
Cdd:cd01135 158 EYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTMPNDDIT 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 371560958 234 DPAPatsfahlDAT-------TVLNRAISELGIYPAVDPLDSTSR 271
Cdd:cd01135 238 HPIP-------DLTgyitegqIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
1-294 |
1.14e-23 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 99.59 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTvliqELIN 80
Cdd:PRK05922 100 GRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS----SLLS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 81 NIAKGHGGT-SVFAGVGERTREGNDLyhefldanvIAKDADGNAiseGSKVALVYGQMNEPPGARARVALSGLTIAEYFR 159
Cdd:PRK05922 176 TIAKGSKSTiNVIALIGERGREVREY---------IEQHKEGLA---AQRTIIIASPAHETAPTKVIAGRAAMTIAEYFR 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 160 DvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITSTNKGSITSVQAV-YVP--ADDLTDPA 236
Cdd:PRK05922 244 D-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIlHYPnhPDIFTDYL 322
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 371560958 237 PATSFAHLDATTVlNRAISElgiyPAVDPLDSTSRVLEpRVVGQEHYETARAVQSILQ 294
Cdd:PRK05922 323 KSLLDGHFFLTPQ-GKALAS----PPIDILTSLSRSAR-QLALPHHYAAAEELRSLLK 374
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
42-271 |
3.97e-23 |
|
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: 96.10 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 42 LVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELinniAK-GHGGTSVFAGVGERTREGNDLYHEFLDANVIAKdad 120
Cdd:cd01134 60 LLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSL----SKwSNSDVVIYVGCGERGNEMAEVLEEFPELKDPIT--- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 121 GNAISEgsKVALVYGQMNEPPGARARVALSGLTIAEYFRDVeNQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTL 200
Cdd:cd01134 133 GESLME--RTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 201 STDMGQLQER------ITSTNK-GSITSVQAVYVPADDLTDpaPATSfAHLDATTV---LNRAISELGIYPAVDPLDSTS 270
Cdd:cd01134 210 GARLAEFYERagrvrcLGSPGReGSVTIVGAVSPPGGDFSE--PVTQ-ATLRIVQVfwgLDKKLAQRRHFPSINWLISYS 286
|
.
gi 371560958 271 R 271
Cdd:cd01134 287 K 287
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
1-272 |
1.59e-19 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 88.05 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL-IQELI 79
Cdd:PRK13343 105 GRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIaIDAII 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 80 NNiaKGHGGTSVFAGVGERTREGndlyhefldANVIAK----DADGNAIsegskvaLVYGQMNEPPGARARVALSGLTIA 155
Cdd:PRK13343 185 NQ--KDSDVICVYVAIGQKASAV---------ARVIETlrehGALEYTT-------VVVAEASDPPGLQYLAPFAGCAIA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 156 EYFRDvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITSTNK----GSITSVQAVYVPADD 231
Cdd:PRK13343 247 EYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPelggGSLTALPIIETLAGE 325
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 371560958 232 LTDPAPATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRV 272
Cdd:PRK13343 326 LSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRV 366
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
1-271 |
2.72e-18 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 84.49 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:PRK04196 86 GRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIAR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 81 NiAKGHGGTS----VFAGVGERTREGNDLYHEFLDANVIakdadgnaisegSKVALVYGQMNEPPGAR---ARVAlsgLT 153
Cdd:PRK04196 166 Q-AKVLGEEEnfavVFAAMGITFEEANFFMEDFEETGAL------------ERSVVFLNLADDPAIERiltPRMA---LT 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 154 IAEYFRDVENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQER--ITSTNKGSITSVQAVYVPADD 231
Cdd:PRK04196 230 AAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDD 309
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 371560958 232 LTDPAPatsfahlDAT-------TVLNRAISELGIYPAVDPLDSTSR 271
Cdd:PRK04196 310 ITHPIP-------DLTgyitegqIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
42-274 |
5.74e-15 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 74.82 E-value: 5.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 42 LVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELinniAKgHGGTS--VFAGVGERTREGNDLYHEFLDAnviaKD- 118
Cdd:PRK04192 211 LITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQL----AK-WADADivIYVGCGERGNEMTEVLEEFPEL----IDp 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 119 ADGNAISEgsKVALVYGQMNEPPGAR-ARVaLSGLTIAEYFRDvenQ--DVLFFVDNIFRFTQAGAEVSALLGRIPSAVG 195
Cdd:PRK04192 282 KTGRPLME--RTVLIANTSNMPVAAReASI-YTGITIAEYYRD---MgyDVLLMADSTSRWAEALREISGRLEEMPGEEG 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 196 YQPTLSTDMGQLQER----IT-STNKGSITSVQAVYVPADDLTDpaPATS--------FAHLDAttvlNRAISELgiYPA 262
Cdd:PRK04192 356 YPAYLASRLAEFYERagrvKTlGGEEGSVTIIGAVSPPGGDFSE--PVTQntlrivkvFWALDA----ELADRRH--FPA 427
|
250
....*....|..
gi 371560958 263 VDPLDSTSRVLE 274
Cdd:PRK04192 428 INWLTSYSLYLD 439
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
1-272 |
1.38e-13 |
|
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: 69.12 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKT-VLIQELI 79
Cdd:cd01132 12 GRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTaIAIDTII 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 80 NNiaKGHGGTSVFAGVGERTREGndlyhefldANVIAKDADGNAISEGSKVAlvyGQMNEPPGARARVALSGLTIAEYFR 159
Cdd:cd01132 92 NQ--KGKKVYCIYVAIGQKRSTV---------AQIVKTLEEHGAMEYTIVVA---ATASDPAPLQYLAPYAGCAMGEYFR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 160 DvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITSTNK----GSITSVQAVYVPADDLTDP 235
Cdd:cd01132 158 D-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGSLTALPIIETQAGDVSAY 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 371560958 236 APATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRV 272
Cdd:cd01132 237 IPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRV 273
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
1-274 |
1.85e-13 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 70.14 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVR-----SPIHAKAPEFVDQstdasILVTGIKVIDLLAPYAKGGKIGLFGGAG------- 68
Cdd:TIGR01040 84 GRVFNGSGKPIDKGPPVLAEDYldingQPINPYARIYPEE-----MIQTGISAIDVMNSIARGQKIPIFSAAGlphneia 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 69 ---VGKTVLIQELINNIAKGHGG--TSVFA--GVGERTregndlyhefldANVIAKDADGNAISEgsKVALVYGQMNEPP 141
Cdd:TIGR01040 159 aqiCRQAGLVKLPTKDVHDGHEDnfAIVFAamGVNMET------------ARFFKQDFEENGSME--RVCLFLNLANDPT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 142 GARARVALSGLTIAEYFRDVENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITSTN--KGSI 219
Cdd:TIGR01040 225 IERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrNGSI 304
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 371560958 220 TSVQAVYVPADDLTDPAPATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRVLE 274
Cdd:TIGR01040 305 TQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMK 359
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
91-270 |
3.28e-13 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 69.67 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 91 VFAGVGERTREGNDLYHEFLDAnviaKDAD-GNAISEgsKVALVYGQMNEPPGARARVALSGLTIAEYFRDVeNQDVLFF 169
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFPKL----KDPKtGKPLME--RTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYDVALM 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 170 VDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERI-------TSTNKGSITSVQAVYVPADDLTDPAPATSFA 242
Cdd:PRK14698 759 ADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLR 838
|
170 180
....*....|....*....|....*...
gi 371560958 243 HLDATTVLNRAISELGIYPAVDPLDSTS 270
Cdd:PRK14698 839 VVKVFWALDADLARRRHFPAINWLTSYS 866
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
1-289 |
3.59e-10 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 60.05 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEeRGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGktvlIQELIN 80
Cdd:PRK02118 84 GRRFNGSGKPID-GGPELEGEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEP----YNALLA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 81 NIA-KGHGGTSVFAGVGERtregNDLYHEFLDANviakdADGNAISegsKVALVYGQMNEPPGARARVALSGLTIAEYFR 159
Cdd:PRK02118 159 RIAlQAEADIIILGGMGLT----FDDYLFFKDTF-----ENAGALD---RTVMFIHTASDPPVECLLVPDMALAVAEKFA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 160 DVENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQER-ITSTNKGSITSVQAVYVPADDLTDPAPa 238
Cdd:PRK02118 227 LEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKaVDFEDGGSITIIAVTTMPGDDVTHPVP- 305
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 371560958 239 tsfahlDATTVlnraISELGIY---PAVDPLDSTSRvLEPRVVGQEHYETARAV 289
Cdd:PRK02118 306 ------DNTGY----ITEGQFYlrrGRIDPFGSLSR-LKQLVIGKKTREDHGDL 348
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
1-191 |
1.64e-07 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 51.99 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVD-QSTDASiLVTGIKVIDLLAPYAKGGKIGLFGGAGVGKT-VLIQEL 78
Cdd:PRK09281 105 GRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDrKSVHEP-LQTGIKAIDAMIPIGRGQRELIIGDRQTGKTaIAIDTI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 79 INNiaKGHGGTSVFAGVGERtregndlyhefldanviakdadgnaiseGSKVALV------YGQM----------NEPPG 142
Cdd:PRK09281 184 INQ--KGKDVICIYVAIGQK----------------------------ASTVAQVvrkleeHGAMeytivvaataSDPAP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 371560958 143 ARARVALSGLTIAEYFRDvENQDVLFFVDNIFRftQAGA--EVSALLGRIP 191
Cdd:PRK09281 234 LQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSK--QAVAyrQLSLLLRRPP 281
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
47-294 |
2.42e-05 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 44.89 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 47 KVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKGHGGTSVFAG-VGERTREGNDLyHEFLDANVIAKDADgnais 125
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTDM-RRSVKGEVVASTFD----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 126 egskvalvygqmnEPPGARARVALSGLTIAEyfRDVE-NQDVLFFVDNIFRFTQAGAEVSALLGRIPSAvgyqptlSTDM 204
Cdd:cd01128 79 -------------EPPERHVQVAEMVIEKAK--RLVEhGKDVVILLDSITRLARAYNTVVPSSGKTLSG-------GVDA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 205 GQLQ--ERITST-----NKGSITSVQAVYVP----ADDLTdpapatsFAHLDAT----TVLNRAISELGIYPAVDPLDST 269
Cdd:cd01128 137 NALHkpKRFFGAarnieEGGSLTIIATALVDtgsrMDEVI-------FEEFKGTgnmeLVLDRKLAEKRIFPAIDILKSG 209
|
250 260
....*....|....*....|....*
gi 371560958 270 SRvLEPRVVGQEHYETARAVQSILQ 294
Cdd:cd01128 210 TR-KEELLLTPEELQKIWLLRRILS 233
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
25-272 |
8.04e-05 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 43.88 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 25 IHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKT-VLIQELINN------IAKGHGGTSVFAGVGE 97
Cdd:PTZ00185 156 VDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTsIAVSTIINQvrinqqILSKNAVISIYVSIGQ 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 98 RTregndlyhefldANVIAKDADGNAISEGSKVALVYGQMNEPPGARARVALSGLTIAEYFRDvENQDVLFFVDNIFRFT 177
Cdd:PTZ00185 236 RC------------SNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMN-RGRHCLCVYDDLSKQA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 178 QAGAEVSALLGRIPSAVGYQPTLSTDMGQLQER--ITSTNK--GSITSVQAVYVPADDLTDPAPATSFAHLDATTVLNRA 253
Cdd:PTZ00185 303 VAYRQISLLLRRPPGREAYPGDVFYLHSRLLERaaMLSPGKggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTK 382
|
250
....*....|....*....
gi 371560958 254 ISELGIYPAVDPLDSTSRV 272
Cdd:PTZ00185 383 LFTGGQRPAVNIGLSVSRV 401
|
|
| ATP-synt_F1_beta_C |
cd18110 |
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ... |
277-294 |
8.26e-05 |
|
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of F0F1-ATP synthase, C-terminal domain. The F-ATP synthase (also called FoF1-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 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.
Pssm-ID: 349745 [Multi-domain] Cd Length: 108 Bit Score: 40.92 E-value: 8.26e-05
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
57-189 |
1.79e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.82 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 57 KGGKIGLFGGAGVGKTVLIQELINNIAKGHGGtsvfagvgertregndlyhefldanVIAKDADGNAISEGSKVALVYGQ 136
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG-------------------------VIYIDGEDILEEVLDQLLLIIVG 55
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 371560958 137 MNEPPGARARVALSGLTIAEYFRdvenQDVLFFvDNIFRFTQAGAEVSALLGR 189
Cdd:smart00382 56 GKKASGSGELRLRLALALARKLK----PDVLIL-DEITSLLDAEQEALLLLLE 103
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
1-272 |
2.65e-04 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 42.26 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 1 GRIRNVVGEPIEERGPVAAEVRSPIHAKAPEFVDQSTDASILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKT-VLIQELI 79
Cdd:CHL00059 84 GRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTaVATDTIL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 80 NNiaKGHGGTSVFAGVGERtregndlyhefldANVIAKDAdgNAISEGSKVA---LVYGQMNEPPGARARVALSGLTIAE 156
Cdd:CHL00059 164 NQ--KGQNVICVYVAIGQK-------------ASSVAQVV--TTLQERGAMEytiVVAETADSPATLQYLAPYTGAALAE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 157 YFRdVENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLSTDMGQLQERITSTNK----GSITSVQAVYVPADDL 232
Cdd:CHL00059 227 YFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSqlgeGSMTALPIVETQAGDV 305
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 371560958 233 TDPAPATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRV 272
Cdd:CHL00059 306 SAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRV 345
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
47-192 |
8.00e-04 |
|
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: 40.44 E-value: 8.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 47 KVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKGHggTSVFAGV---GERTREGNDLYHEfLDANVIAKDADgna 123
Cdd:TIGR00767 157 RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNH--PEVELIVlliDERPEEVTDMQRS-VKGEVVASTFD--- 230
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560958 124 isegskvalvygqmnEPPGARARVAlsGLTIAEYFRDVEN-QDVLFFVDNIFRFTQAGAEVSALLGRIPS 192
Cdd:TIGR00767 231 ---------------EPASRHVQVA--EMVIEKAKRLVEHkKDVVILLDSITRLARAYNTVTPASGKVLS 283
|
|
| |
