|
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: 627.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSNPIHAEAPLFTDQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:COG0055 89 GRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIH 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 81 NIAKGHGGVSVFAGVGERTREGNDLYHEFLDAGVIakdadgnptpegSKVALVFGQMNEPPGARARVALSGLTMAEYFRD 160
Cdd:COG0055 169 NIAKEHGGVSVFAGVGERTREGNDLYREMKESGVL------------DKTALVFGQMNEPPGARLRVALTALTMAEYFRD 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 161 EEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITSTTKGSITSVQAIYVPADDLTDPAPATS 240
Cdd:COG0055 237 EEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATT 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 371561010 241 FAHPDENTTLNRAISELGIYPAVDPLDSVSRVLTPAVVGQEHYDTARRVQETLQ 294
Cdd:COG0055 317 FAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQ 370
|
|
| 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: 553.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSNPIHAEAPLFTDQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:cd01133 10 GRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELIN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 81 NIAKGHGGVSVFAGVGERTREGNDLYHEFLDAGVIAKDadgnptpEGSKVALVFGQMNEPPGARARVALSGLTMAEYFRD 160
Cdd:cd01133 90 NIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLD-------GLSKVALVYGQMNEPPGARARVALTGLTMAEYFRD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 161 EEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITSTTKGSITSVQAIYVPADDLTDPAPATS 240
Cdd:cd01133 163 EEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPATT 242
|
250 260 270
....*....|....*....|....*....|....*
gi 371561010 241 FAHPDENTTLNRAISELGIYPAVDPLDSVSRVLTP 275
Cdd:cd01133 243 FAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| 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: 552.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSNPIHAEAPLFTDQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:TIGR01039 86 GRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 81 NIAKGHGGVSVFAGVGERTREGNDLYHEFLDAGVIakdadgnptpegSKVALVFGQMNEPPGARARVALSGLTMAEYFRD 160
Cdd:TIGR01039 166 NIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVI------------DKTALVYGQMNEPPGARMRVALTGLTMAEYFRD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 161 EEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITSTTKGSITSVQAIYVPADDLTDPAPATS 240
Cdd:TIGR01039 234 EQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATT 313
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 371561010 241 FAHPDENTTLNRAISELGIYPAVDPLDSVSRVLTPAVVGQEHYDTARRVQETLQ 294
Cdd:TIGR01039 314 FAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQ 367
|
|
| 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: 543.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSNPIHAEAPLFTDQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:CHL00060 104 GRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELIN 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 81 NIAKGHGGVSVFAGVGERTREGNDLYHEFLDAGVIAKDadgnpTPEGSKVALVFGQMNEPPGARARVALSGLTMAEYFRD 160
Cdd:CHL00060 184 NIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQ-----NIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRD 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 161 EEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITSTTKGSITSVQAIYVPADDLTDPAPATS 240
Cdd:CHL00060 259 VNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATT 338
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 371561010 241 FAHPDENTTLNRAISELGIYPAVDPLDSVSRVLTPAVVGQEHYDTARRVQETLQ 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 |
1.98e-131 |
|
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: 380.32 E-value: 1.98e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSNPIHAEAPLFTDQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:TIGR03305 81 SRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIH 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 81 NIAKGHGGVSVFAGVGERTREGNDLYHEFLDAGVIakdadgnptpegSKVALVFGQMNEPPGARARVALSGLTMAEYFRD 160
Cdd:TIGR03305 161 NMVGQHQGVSIFCGIGERCREGEELYREMKEAGVL------------DNTVMVFGQMNEPPGARFRVGHTALTMAEYFRD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 161 EEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITSTTKGSITSVQAIYVPADDLTDPAPATS 240
Cdd:TIGR03305 229 DEKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHT 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 371561010 241 FAHPDENTTLNRAISELGIYPAVDPLDSVSRVLTPAVVGQEHYDTARRVQETL 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 |
5.12e-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: 347.52 E-value: 5.12e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSNPIHAEAPLFTDQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:cd19476 10 GRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLAR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 81 NIAKGHGGVSVFAGVGERTREGNDLYHEFLDAGVIakdadgnptpegSKVALVFGQMNEPPGARARVALSGLTMAEYFRD 160
Cdd:cd19476 90 NQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAM------------ERTVVVANTANDPPGARMRVPYTGLTIAEYFRD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 161 eEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITST--TKGSITSVQAIYVPADDLTDPAPA 238
Cdd:cd19476 158 -NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVkdGGGSITAIPAVSTPGDDLTDPIPD 236
|
250 260 270
....*....|....*....|....*....|....
gi 371561010 239 TSFAHPDENTTLNRAISELGIYPAVDPLDSVSRV 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 |
8.78e-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: 270.77 E-value: 8.78e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 45 GIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKGhggVSVFAGVGERTREGNDLYHEFLDAGVIAKdadgnpt 124
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASAD---VVVYALIGERGREVREFIEELLGSGALKR------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 125 pegskVALVFGQMNEPPGARARVALSGLTMAEYFRDEeGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDM 204
Cdd:pfam00006 71 -----TVVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 371561010 205 GQLQERITSTT--KGSITSVQAIYVPADDLTDPAPATSFAHPDENTTLNRAISELGIYPAVDPLDSVS 270
Cdd:pfam00006 145 ARLLERAGRVKgkGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
1-272 |
3.80e-56 |
|
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: 181.99 E-value: 3.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSNPIHAEAPLFTDQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:cd01136 10 GRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIAR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 81 NIAkghGGVSVFAGVGERTREGNdlyhEFLDagviakdadGNPTPEG-SKVALVFGQMNEPPGARARVALSGLTMAEYFR 159
Cdd:cd01136 90 NTD---ADVNVIALIGERGREVR----EFIE---------KDLGEEGlKRSVLVVATSDESPLLRVRAAYTATAIAEYFR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 160 DEeGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITSTTKGSITSVQAIYVPADDLTDPAPAT 239
Cdd:cd01136 154 DQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADE 232
|
250 260 270
....*....|....*....|....*....|...
gi 371561010 240 SFAHPDENTTLNRAISELGIYPAVDPLDSVSRV 272
Cdd:cd01136 233 VRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
1-293 |
9.33e-51 |
|
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: 172.52 E-value: 9.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSNPIHAEAPLFTDQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:COG1157 100 GRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIAR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 81 NIAkghGGVSVFAGVGERTREGNdlyhEFLDagviakDADGnptPEG-SKVALVFGQMNEPPGARARVALSGLTMAEYFR 159
Cdd:COG1157 180 NTE---ADVNVIALIGERGREVR----EFIE------DDLG---EEGlARSVVVVATSDEPPLMRLRAAYTATAIAEYFR 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 160 DeEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITSTTKGSITsvqAIY---VPADDLTDPa 236
Cdd:COG1157 244 D-QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSIT---AFYtvlVEGDDMNDP- 318
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371561010 237 patsFAhpDE-------NTTLNRAISELGIYPAVDPLDSVSRVLtPAVVGQEHYDTARRVQETL 293
Cdd:COG1157 319 ----IA--DAvrgildgHIVLSRKLAERGHYPAIDVLASISRVM-PDIVSPEHRALARRLRRLL 375
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
1-271 |
7.56e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 157.47 E-value: 7.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVA-KSNPIHAEAPLFTDQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELI 79
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGtRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 80 NniAKGHGGVsVFAGVGERTREgndlYHEFLDaGVIAKDAdgnptpegSKVALVFGQMNEPPGARARVALSGLTMAEYFR 159
Cdd:PRK06002 187 R--ADAFDTV-VIALVGERGRE----VREFLE-DTLADNL--------KKAVAVVATSDESPMMRRLAPLTATAIAEYFR 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 160 DeEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERI--TSTTKGSITSVQAIYVPADDLTDPAP 237
Cdd:PRK06002 251 D-RGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVA 329
|
250 260 270
....*....|....*....|....*....|....
gi 371561010 238 ATSFAHPDENTTLNRAISELGIYPAVDPLDSVSR 271
Cdd:PRK06002 330 DSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISR 363
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
1-288 |
1.28e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 154.07 E-value: 1.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSNPIhAEAPLFT-DQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIqeli 79
Cdd:PRK08472 100 GRVVDPLGRPIDGKGAIDYERYAPI-MKAPIAAmKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLM---- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 80 NNIAKG-HGGVSVFAGVGERTREgndlYHEFldagvIAKDADGNPTpegsKVALVFGQMNEPPGARARVALSGLTMAEYF 158
Cdd:PRK08472 175 GMIVKGcLAPIKVVALIGERGRE----IPEF-----IEKNLGGDLE----NTVIVVATSDDSPLMRKYGAFCAMSVAEYF 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 159 RDEeGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITST-TKGSITSVQAIYVPADDLTDPAP 237
Cdd:PRK08472 242 KNQ-GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEeGKGSITAFFTVLVEGDDMSDPIA 320
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 371561010 238 ATSFAHPDENTTLNRAISELGIYPAVDPLDSVSRVLTPaVVGQEHYDTARR 288
Cdd:PRK08472 321 DQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMND-IISPEHKLAARK 370
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
1-293 |
1.56e-40 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 146.05 E-value: 1.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSNPIHAEAPLFTDQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:PRK06936 105 GRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIR 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 81 NIAkghGGVSVFAGVGERTREgndlYHEFLDAgviakdadgNPTPEGSKVA-LVFGQMNEPPGARARVALSGLTMAEYFR 159
Cdd:PRK06936 185 SAE---VDVTVLALIGERGRE----VREFIES---------DLGEEGLRKAvLVVATSDRPSMERAKAGFVATSIAEYFR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 160 DEeGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITSTTKGSITSVQAIYVPADDLTDPAPAT 239
Cdd:PRK06936 249 DQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVADE 327
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 371561010 240 SFAHPDENTTLNRAISELGIYPAVDPLDSVSRVLTpAVVGQEHYDTARRVQETL 293
Cdd:PRK06936 328 TRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELL 380
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
1-293 |
1.59e-40 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 145.73 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVA-KSNPIHAEAPLfTDQSTEaEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELI 79
Cdd:PRK06820 107 GRILDGLGAPIDGGPPLTGQwRELDCPPPSPL-TRQPIE-QMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLC 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 80 NNIAkghGGVSVFAGVGERTREgndlYHEFLDAgviakdadgNPTPEG-SKVALVFGQMNEPPGARARVALSGLTMAEYF 158
Cdd:PRK06820 185 ADSA---ADVMVLALIGERGRE----VREFLEQ---------VLTPEArARTVVVVATSDRPALERLKGLSTATTIAEYF 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 159 RDEeGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITSTTKGSITSVQAIYVPADDLTDPAPA 238
Cdd:PRK06820 249 RDR-GKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVAD 327
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 371561010 239 TSFAHPDENTTLNRAISELGIYPAVDPLDSVSRVLtPAVVGQEHYDTARRVQETL 293
Cdd:PRK06820 328 EVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRML 381
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
1-293 |
1.01e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 143.69 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSNPIHAEA--PLFTDQSTEAeiLVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQEL 78
Cdd:PRK08972 105 GRVIDGVGNPLDGLGPIYTDQRASRHSPPinPLSRRPITEP--LDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMM 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 79 INNIAkghGGVSVFAGVGERTREGNDLYHEFLdagviakdadgnpTPEGSKVALVFGQ-MNEPPGARARVALSGLTMAEY 157
Cdd:PRK08972 183 TRGTT---ADVIVVGLVGERGREVKEFIEEIL-------------GEEGRARSVVVAApADTSPLMRLKGCETATTIAEY 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 158 FRDEeGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERIT--STTKGSITSVQAIYVPADDLTDP 235
Cdd:PRK08972 247 FRDQ-GLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGngGPGQGSITAFYTVLTEGDDLQDP 325
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 371561010 236 APATSFAHPDENTTLNRAISELGIYPAVDPLDSVSRVLtPAVVGQEHYDTARRVQETL 293
Cdd:PRK08972 326 IADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVY 382
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
1-293 |
8.33e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 138.70 E-value: 8.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERG-PVGVAksnpihaeaPLFTDQSTE--------AEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGK 71
Cdd:PRK07721 101 GQVLDALGEPLDGSAlPKGLA---------PVSTDQDPPnplkrppiREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 72 TVLIQELINNIAkghGGVSVFAGVGERTREgndlYHEFldagvIAKDADgnptPEG-SKVALVFGQMNEPPGARARVALS 150
Cdd:PRK07721 172 STLMGMIARNTS---ADLNVIALIGERGRE----VREF-----IERDLG----PEGlKRSIVVVATSDQPALMRIKGAYT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 151 GLTMAEYFRDEeGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITSTTKGSITSVQAIYVPAD 230
Cdd:PRK07721 236 ATAIAEYFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGD 314
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 371561010 231 DLTDPAPATSFAHPDENTTLNRAISELGIYPAVDPLDSVSRVLtPAVVGQEHYDTARRVQETL 293
Cdd:PRK07721 315 DMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELL 376
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
1-288 |
1.20e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 138.19 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSN-PIHAEAPLFTDQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELI 79
Cdd:PRK08927 100 GRVVNALGEPIDGKGPLPQGPVPyPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 80 NNIAkghGGVSVFAGVGERTREgndlYHEFLDagviakDADGnptPEGSKVA-LVFGQMNEPPGARARVALSGLTMAEYF 158
Cdd:PRK08927 180 RNAD---ADVSVIGLIGERGRE----VQEFLQ------DDLG---PEGLARSvVVVATSDEPALMRRQAAYLTLAIAEYF 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 159 RDeEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERI--TSTTKGSITSVQAIYVPADDLTDPA 236
Cdd:PRK08927 244 RD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPV 322
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 371561010 237 PATSFAHPDENTTLNRAISELGIYPAVDPLDSVSRVLtPAVVGQEHYDTARR 288
Cdd:PRK08927 323 ADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRR 373
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
1-293 |
3.96e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 133.95 E-value: 3.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDErgPVGVAKSNPIHAEAPLFTDQSTE--AEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQEL 78
Cdd:PRK06793 99 GKVLSANGEVLNE--EAENIPLQKIKLDAPPIHAFEREeiTDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMI 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 79 INNiAKGHggVSVFAGVGERTREGNDLYHEFLDAgviakdadgnptpEG-SKVALVFGQMNEPPGARARVALSGLTMAEY 157
Cdd:PRK06793 177 AKN-AKAD--INVISLVGERGREVKDFIRKELGE-------------EGmRKSVVVVATSDESHLMQLRAAKLATSIAEY 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 158 FRDEeGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAvGYQPTLATDMGQLQERITSTTKGSITSVQAIYVPADDLTDPAP 237
Cdd:PRK06793 241 FRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVP 318
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 371561010 238 ATSFAHPDENTTLNRAISELGIYPAVDPLDSVSRVLTpAVVGQEHYDTARRVQETL 293
Cdd:PRK06793 319 DLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPNHWQLANEMRKIL 373
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
1-293 |
9.94e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 127.92 E-value: 9.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSNPIHAEA--PLFTDQSTEAeiLVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQEL 78
Cdd:PRK05688 111 GRVLDGAGRALDGKGPMKAEDWVPMDGPTinPLNRHPISEP--LDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMM 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 79 INNIAkghGGVSVFAGVGERTREgndlYHEFLDagviakDADGnptPEGSKVALVFGQ-MNEPPGARARVALSGLTMAEY 157
Cdd:PRK05688 189 TRFTE---ADIIVVGLIGERGRE----VKEFIE------HILG---EEGLKRSVVVASpADDAPLMRLRAAMYCTRIAEY 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 158 FRDEeGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITSTTKG--SITSVQAIYVPADDLTDP 235
Cdd:PRK05688 253 FRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGggSITAFYTVLSEGDDQQDP 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 371561010 236 APATSFAHPDENTTLNRAISELGIYPAVDPLDSVSRVLtPAVVGQEHYDTARRVQETL 293
Cdd:PRK05688 332 IADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLW 388
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
1-282 |
1.53e-33 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 126.99 E-value: 1.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSNPIHAEAPLFTDQSTeAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:PRK07594 99 GRVIDGFGRPLDGRELPDVCWKDYDAMPPPAMVRQPI-TQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 81 niAKGhGGVSVFAGVGERTREgndlYHEFLDAgVIAKDADgnptpegSKVALVFGQMNEPPGARARVALSGLTMAEYFRD 160
Cdd:PRK07594 178 --APD-ADSNVLVLIGERGRE----VREFIDF-TLSEETR-------KRCVIVVATSDRPALERVRALFVATTIAEFFRD 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 161 EeGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITSTTKGSITSVQAIYVPADDLTDPAPATS 240
Cdd:PRK07594 243 N-GKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFYTVLVEGDDMNEPLADEV 321
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 371561010 241 FAHPDENTTLNRAISELGIYPAVDPLDSVSRVLtPAVVGQEH 282
Cdd:PRK07594 322 RSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEH 362
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
1-293 |
2.35e-33 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 126.42 E-value: 2.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSNPIHAEAPLFTDQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELin 80
Cdd:PRK09099 106 GRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMF-- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 81 niAKG-HGGVSVFAGVGERTREGNDLYHEFLDAGVIAKDADGNPTPEGSKVAlvfgqmneppgaRARVALSGLTMAEYFR 159
Cdd:PRK09099 184 --ARGtQCDVNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIE------------RAKAAYVATAIAEYFR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 160 DEeGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITSTTKGSITSVQAIYVPADDLTDPAPAT 239
Cdd:PRK09099 250 DR-GLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEE 328
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 371561010 240 SFAHPDENTTLNRAISELGIYPAVDPLDSVSRVLtPAVVGQEHYDTARRVQETL 293
Cdd:PRK09099 329 VRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLL 381
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
1-294 |
1.21e-32 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 124.34 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDergPVGVAKSNPIHAEAPLFTDQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:PRK08149 97 GKIVERFDAPPT---VGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 81 NIAkghGGVSVFAGVGERTREGNDLYHEFldagviakdadgNPTPEGSKVALVFGQMNEPPGARARVALSGLTMAEYFRD 160
Cdd:PRK08149 174 HSE---ADVFVIGLIGERGREVTEFVESL------------RASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 161 eEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITSTTKGSITSVQAIYVPADDLTDPAPATS 240
Cdd:PRK08149 239 -QGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEI 317
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 371561010 241 FAHPDENTTLNRAISELGIYPAVDPLDSVSRVLTpAVVGQEHYDTARRVQETLQ 294
Cdd:PRK08149 318 RSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFG-QVTDPKHRQLAAAFRKLLT 370
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
1-291 |
3.17e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 123.46 E-value: 3.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGvaKSNPIHAEAPLFTDQSTEA--EILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQEL 78
Cdd:PRK07196 98 GRVINGLGEPLDGKGQLG--GSTPLQQQLPQIHPLQRRAvdTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 79 INNIakgHGGVSVFAGVGERTREGNDLYHEFLDAGVIAKDAdgnptpegskvaLVFGQMNEPPGARARVALSGLTMAEYF 158
Cdd:PRK07196 176 TRYT---QADVVVVGLIGERGREVKEFIEHSLQAAGMAKSV------------VVAAPADESPLMRIKATELCHAIATYY 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 159 RDEeGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERI-TSTTKGSITSVQAIYVPADDLTDPAP 237
Cdd:PRK07196 241 RDK-GHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGTMTAIYTVLAEGDDQQDPIV 319
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 371561010 238 ATSFAHPDENTTLNRAISELGIYPAVDPLDSVSRVLTpAVVGQEHYDTARRVQE 291
Cdd:PRK07196 320 DCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQ 372
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
1-293 |
2.77e-26 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 107.18 E-value: 2.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPID--------ERGPVGVAKSNPIhAEAPLftdqsteAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKT 72
Cdd:PRK07960 118 GRVLDGSGKPLDglpapdtgETGALITPPFNPL-QRTPI-------EHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKS 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 73 VLIQELINNIakgHGGVSVFAGVGERTREGNDLYHEFLDAG------VIAKDADGNPTpegskvalvfgqmneppgARAR 146
Cdd:PRK07960 190 VLLGMMARYT---QADVIVVGLIGERGREVKDFIENILGAEgrarsvVIAAPADVSPL------------------LRMQ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 147 VALSGLTMAEYFRDEeGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITS--TTKGSITSVQA 224
Cdd:PRK07960 249 GAAYATRIAEDFRDR-GQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYT 327
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 371561010 225 IYVPADDLTDPAPATSFAHPDENTTLNRAISELGIYPAVDPLDSVSRVLTpAVVGQEHYDTARRVQETL 293
Cdd:PRK07960 328 VLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMT-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 |
9.54e-26 |
|
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: 103.07 E-value: 9.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSNPIHAEAPLFTDQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKtvliQELIN 80
Cdd:cd01135 12 GRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLPH----NELAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 81 NIAKGHGGVS-------VFAGVGERTREGNDLYHEFLDAGVIakdadgnptpegSKVALVFGQMNEPPGARARVALSGLT 153
Cdd:cd01135 88 QIARQAGVVGseenfaiVFAAMGVTMEEARFFKDDFEETGAL------------ERVVLFLNLANDPTIERIITPRMALT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 154 MAEYFRDEEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQER--ITSTTKGSITSVQAIYVPADD 231
Cdd:cd01135 156 TAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTMPNDD 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 371561010 232 LTDPAPatsfahpdENT--------TLNRAISELGIYPAVDPLDSVSR 271
Cdd:cd01135 236 ITHPIP--------DLTgyitegqiYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
1-277 |
1.12e-23 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 99.59 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSNPIHAEAPLFTDQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTvliqELIN 80
Cdd:PRK05922 100 GRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS----SLLS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 81 NIAKG-HGGVSVFAGVGERTREGNDLyhefldagvIAKDADGnptPEGSKVALVFGQMNEPPGARARVALSGLTMAEYFR 159
Cdd:PRK05922 176 TIAKGsKSTINVIALIGERGREVREY---------IEQHKEG---LAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFR 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 160 DeEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITSTTKGSITSVQAI-YVP--ADDLTD-- 234
Cdd:PRK05922 244 D-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIlHYPnhPDIFTDyl 322
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 371561010 235 ----------PAPATSFAHPDEN--TTLNRAISELGI---YPAVDPLDSVSRVLTPAV 277
Cdd:PRK05922 323 kslldghfflTPQGKALASPPIDilTSLSRSARQLALphhYAAAEELRSLLKAYHEAL 380
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
40-271 |
9.83e-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: 94.95 E-value: 9.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 40 EILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELinniAK-GHGGVSVFAGVGERTREGNDLYHEFLDAGVIAKd 118
Cdd:cd01134 58 VPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSL----SKwSNSDVVIYVGCGERGNEMAEVLEEFPELKDPIT- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 119 adGNPTPEgsKVALVFGQMNEPPGARARVALSGLTMAEYFRDeEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQP 198
Cdd:cd01134 133 --GESLME--RTVLIANTSNMPVAAREASIYTGITIAEYFRD-MGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 199 TLATDMGQLQERI-------TSTTKGSITSVQAIYVPADDLTDpaPATSfahpdeNTT--------LNRAISELGIYPAV 263
Cdd:cd01134 208 YLGARLAEFYERAgrvrclgSPGREGSVTIVGAVSPPGGDFSE--PVTQ------ATLrivqvfwgLDKKLAQRRHFPSI 279
|
....*...
gi 371561010 264 DPLDSVSR 271
Cdd:cd01134 280 NWLISYSK 287
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
1-272 |
5.96e-21 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 92.29 E-value: 5.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSNPIHAEAPLFTDQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL-IQELI 79
Cdd:PRK13343 105 GRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIaIDAII 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 80 NNiaKGHGGVSVFAGVGERTREGndlyhefldAGVIAK----DADGNPTpegskvaLVFGQMNEPPGARARVALSGLTMA 155
Cdd:PRK13343 185 NQ--KDSDVICVYVAIGQKASAV---------ARVIETlrehGALEYTT-------VVVAEASDPPGLQYLAPFAGCAIA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 156 EYFRDeEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITSTTK----GSITSVQAIYVPADD 231
Cdd:PRK13343 247 EYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPelggGSLTALPIIETLAGE 325
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 371561010 232 LTDPAPATSFAHPDENTTLNRAISELGIYPAVDPLDSVSRV 272
Cdd:PRK13343 326 LSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRV 366
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
1-271 |
3.63e-19 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 86.80 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSNPIHAEAPLFTDQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKtvliQELIN 80
Cdd:PRK04196 86 GRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPH----NELAA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 81 NIAK-----GHGG--VSVFAGVGERTREGNDLYHEFLDAGVIakdadgnptpegSKVALVFGQMNEPPGAR---ARVAls 150
Cdd:PRK04196 162 QIARqakvlGEEEnfAVVFAAMGITFEEANFFMEDFEETGAL------------ERSVVFLNLADDPAIERiltPRMA-- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 151 gLTMAEYFRDEEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQER--ITSTTKGSITSVQAIYVP 228
Cdd:PRK04196 228 -LTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMP 306
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 371561010 229 ADDLTDPAPATSFAHPDENTTLNRAISELGIYPAVDPLDSVSR 271
Cdd:PRK04196 307 DDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
1-277 |
3.80e-17 |
|
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: 80.92 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDeRGPVGVAKS------NPIHAEAPLFTDqsteaEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKtvl 74
Cdd:TIGR01040 84 GRVFNGSGKPID-KGPPVLAEDyldingQPINPYARIYPE-----EMIQTGISAIDVMNSIARGQKIPIFSAAGLPH--- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 75 iqeliNNIAkghGGVSVFAGVGERTREGNDLYHE------FLDAGV-------IAKDADGNPTPEgsKVALVFGQMNEPP 141
Cdd:TIGR01040 155 -----NEIA---AQICRQAGLVKLPTKDVHDGHEdnfaivFAAMGVnmetarfFKQDFEENGSME--RVCLFLNLANDPT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 142 GARARVALSGLTMAEYFRDEEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITSTT--KGSI 219
Cdd:TIGR01040 225 IERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrNGSI 304
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 371561010 220 TSVQAIYVPADDLTDPAPATSFAHPDENTTLNRAISELGIYPAVDPLDSVSRVLTPAV 277
Cdd:TIGR01040 305 TQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAI 362
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
1-272 |
8.22e-16 |
|
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: 75.67 E-value: 8.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSNPIHAEAPLFTDQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKT-VLIQELI 79
Cdd:cd01132 12 GRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTaIAIDTII 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 80 NNiaKGHGGVSVFAGVGERTREGNDLYHEFLDAGVIAKdadgnptpegskVALVFGQMNEPPGARARVALSGLTMAEYFR 159
Cdd:cd01132 92 NQ--KGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEY------------TIVVAATASDPAPLQYLAPYAGCAMGEYFR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 160 DEeGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYqPTlatDM----GQLQERITSTTK----GSITSVQAIYVPADD 231
Cdd:cd01132 158 DN-GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAY-PG---DVfylhSRLLERAAKLSDelggGSLTALPIIETQAGD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 371561010 232 LTDPAPATSFAHPDENTTLNRAISELGIYPAVDPLDSVSRV 272
Cdd:cd01132 233 VSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRV 273
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
40-271 |
1.06e-15 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 77.13 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 40 EILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELinniAK-GHGGVSVFAGVGERTREGNDLYHEFLDagviAKD 118
Cdd:PRK04192 209 EPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQL----AKwADADIVIYVGCGERGNEMTEVLEEFPE----LID 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 119 -ADGNPTPEgsKVALVFGQMNEPPGAR-ARVaLSGLTMAEYFRDeEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGY 196
Cdd:PRK04192 281 pKTGRPLME--RTVLIANTSNMPVAAReASI-YTGITIAEYYRD-MGYDVLLMADSTSRWAEALREISGRLEEMPGEEGY 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 197 QPTLATDMGQLQER----IT-STTKGSITSVQAIYVPADDLTDpaPATSfahpdeNTT--------LNRAISELGIYPAV 263
Cdd:PRK04192 357 PAYLASRLAEFYERagrvKTlGGEEGSVTIIGAVSPPGGDFSE--PVTQ------NTLrivkvfwaLDAELADRRHFPAI 428
|
....*...
gi 371561010 264 DPLDSVSR 271
Cdd:PRK04192 429 NWLTSYSL 436
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
89-270 |
1.56e-13 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 70.82 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 89 VSVFAGVGERTREGNDLYHEFLDAgviaKDAD-GNPTPEgsKVALVFGQMNEPPGARARVALSGLTMAEYFRDEeGQDVL 167
Cdd:PRK14698 684 VVIYIGCGERGNEMTDVLEEFPKL----KDPKtGKPLME--RTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYDVA 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 168 FFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITSTTK-------GSITSVQAIYVPADDLTDPAPATS 240
Cdd:PRK14698 757 LMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTlgsdyrvGSVSVIGAVSPPGGDFSEPVVQNT 836
|
170 180 190
....*....|....*....|....*....|
gi 371561010 241 FAHPDENTTLNRAISELGIYPAVDPLDSVS 270
Cdd:PRK14698 837 LRVVKVFWALDADLARRRHFPAINWLTSYS 866
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
1-293 |
2.03e-13 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 70.06 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPID-------ERGPVGVAKSNPIHAEAPlftdqsteAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGktv 73
Cdd:PRK02118 84 GRRFNGSGKPIDggpelegEPIEIGGPSVNPVKRIVP--------REMIRTGIPMIDVFNTLVESQKIPIFSVSGEP--- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 74 lIQELINNIA-KGHGGVSVFAGVGERTREGNDLYHEFLDAGVIakdadgnptpegSKVALVFGQMNEPPGARARVALSGL 152
Cdd:PRK02118 153 -YNALLARIAlQAEADIIILGGMGLTFDDYLFFKDTFENAGAL------------DRTVMFIHTASDPPVECLLVPDMAL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 153 TMAEYFRDEEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQER-ITSTTKGSITSVQAIYVPADD 231
Cdd:PRK02118 220 AVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKaVDFEDGGSITIIAVTTMPGDD 299
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 371561010 232 LTDPAPatsfahpdENTTLnraISELGIY---PAVDPLDSVSRvLTPAVVGQEHYDTARRVQETL 293
Cdd:PRK02118 300 VTHPVP--------DNTGY---ITEGQFYlrrGRIDPFGSLSR-LKQLVIGKKTREDHGDLMNAM 352
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
1-272 |
3.71e-07 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 51.12 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIDERGPVGVAKSNPIHAEAPLFTDQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKT-VLIQELI 79
Cdd:CHL00059 84 GRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTaVATDTIL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 80 NNiaKGHGGVSVFAGVGERTREGNDLYHEFLDAG------VIAKDADgnptpegSKVALvfgQMNEPpgararvaLSGLT 153
Cdd:CHL00059 164 NQ--KGQNVICVYVAIGQKASSVAQVVTTLQERGameytiVVAETAD-------SPATL---QYLAP--------YTGAA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 154 MAEYFRdEEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITSTTK----GSITSVQAIYVPA 229
Cdd:CHL00059 224 LAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSqlgeGSMTALPIVETQA 302
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 371561010 230 DDLTDPAPATSFAHPDENTTLNRAISELGIYPAVDPLDSVSRV 272
Cdd:CHL00059 303 GDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRV 345
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
1-276 |
9.75e-07 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 50.04 E-value: 9.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 1 GRIMNVIGEPIdergPVGVAKSN-----------PIHAEAPLFTDQSTEAEILVTGIKVIDLLAPYAKGGKIGLFGGAGV 69
Cdd:PTZ00185 125 GKVVNPLGHEV----PVGLLTRSralleseqtlgKVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQT 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 70 GKT-VLIQELINN------IAKGHGGVSVFAGVGERTREGNDLYHEFLDAGVIakdadgnptpegSKVALVFGQMNEPPG 142
Cdd:PTZ00185 201 GKTsIAVSTIINQvrinqqILSKNAVISIYVSIGQRCSNVARIHRLLRSYGAL------------RYTTVMAATAAEPAG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 143 ARARVALSGLTMAEYFRDeEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQLQERITSTTK----GS 218
Cdd:PTZ00185 269 LQYLAPYSGVTMGEYFMN-RGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPgkggGS 347
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 371561010 219 ITSVQAIYVPADDLTDPAPATSFAHPDENTTLNRAISELGIYPAVDPLDSVSRVLTPA 276
Cdd:PTZ00185 348 VTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSA 405
|
|
| 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 |
2.03e-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: 42.85 E-value: 2.03e-05
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
57-189 |
5.22e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.75 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 57 KGGKIGLFGGAGVGKTVLIQELINNIAKGHGgvsvfagvgertregndlyhefldaGVIAKDADGNPTPEGSKVALVFGQ 136
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG-------------------------GVIYIDGEDILEEVLDQLLLIIVG 55
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 371561010 137 MNEPPGARARVALSGLTMAEYFRdeegQDVLFFvDNIFRFTQAGSEVSALLGR 189
Cdd:smart00382 56 GKKASGSGELRLRLALALARKLK----PDVLIL-DEITSLLDAEQEALLLLLE 103
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
30-192 |
8.07e-05 |
|
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: 43.52 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 30 PLFTDQ----STEAEILVTgiKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKGHGGVSVFAG-VGERTREGND 104
Cdd:TIGR00767 138 PLYPNErlrlETSTEDLST--RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEVELIVLlIDERPEEVTD 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 105 LYHEfLDAGVIAKDADgnptpegskvalvfgqmnEPPGARARVALSGLTMAEYfRDEEGQDVLFFVDNIFRFTQAGSEVS 184
Cdd:TIGR00767 216 MQRS-VKGEVVASTFD------------------EPASRHVQVAEMVIEKAKR-LVEHKKDVVILLDSITRLARAYNTVT 275
|
....*...
gi 371561010 185 ALLGRIPS 192
Cdd:TIGR00767 276 PASGKVLS 283
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
47-192 |
9.16e-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: 42.96 E-value: 9.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 47 KVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKGHGGVSVFAG-VGERTREGNDLyHEFLDAGVIAKDADgnptp 125
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTDM-RRSVKGEVVASTFD----- 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 371561010 126 egskvalvfgqmnEPPGARARVALSGLTMAEYfRDEEGQDVLFFVDNIFRFTQAGSEVSALLGRIPS 192
Cdd:cd01128 79 -------------EPPERHVQVAEMVIEKAKR-LVEHGKDVVILLDSITRLARAYNTVVPSSGKTLS 131
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
47-189 |
4.48e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 41.22 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561010 47 KVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKGHGGVSVFAG-VGERTREGNDLYHEfLDAGVIAKDADgnptp 125
Cdd:PRK12608 122 RVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDMRRS-VKGEVYASTFD----- 195
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 371561010 126 egskvalvfgqmnEPPgaRARVALSGLTMAEYFRD-EEGQDVLFFVDNIFRFTQAGSEVSALLGR 189
Cdd:PRK12608 196 -------------RPP--DEHIRVAELVLERAKRLvEQGKDVVILLDSLTRLARAYNNEVESSGR 245
|
|
| |
