|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
2-294 |
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: 621.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 2 GRM-NVVGEPIDERGPVGRPNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:COG0055 89 GRIfNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIH 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 81 NIAKGHGGTSVFAGVGERTREGNDLYHEFLDAGVIakdadgnaisegSKVALVYGQMNEPPGARARVALSGLTIAEYFRD 160
Cdd:COG0055 169 NIAKEHGGVSVFAGVGERTREGNDLYREMKESGVL------------DKTALVFGQMNEPPGARLRVALTALTMAEYFRD 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 161 VENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERITSTNKGSITSVQAVYVPADDLTDPAPATS 240
Cdd:COG0055 237 EEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATT 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 371561014 241 FAHLDATTVLNRAISELGIYPAVDPLDSTSRVLEPRTVGQEHYDTARAVRRSLQ 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 ... |
2-275 |
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: 553.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 2 GR-MNVVGEPIDERGPVGRPNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:cd01133 10 GRiFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELIN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 81 NIAKGHGGTSVFAGVGERTREGNDLYHEFLDAGVIAKDadgnaisEGSKVALVYGQMNEPPGARARVALSGLTIAEYFRD 160
Cdd:cd01133 90 NIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLD-------GLSKVALVYGQMNEPPGARARVALTGLTMAEYFRD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 161 VENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERITSTNKGSITSVQAVYVPADDLTDPAPATS 240
Cdd:cd01133 163 EEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPATT 242
|
250 260 270
....*....|....*....|....*....|....*
gi 371561014 241 FAHLDATTVLNRAISELGIYPAVDPLDSTSRVLEP 275
Cdd:cd01133 243 FAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
2-294 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 551.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 2 GRM-NVVGEPIDERGPVGRPNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:CHL00060 104 GRIfNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELIN 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 81 NIAKGHGGTSVFAGVGERTREGNDLYHEFLDAGVIakdaDGNAISEgSKVALVYGQMNEPPGARARVALSGLTIAEYFRD 160
Cdd:CHL00060 184 NIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVI----NEQNIAE-SKVALVYGQMNEPPGARMRVGLTALTMAEYFRD 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 161 VENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERITSTNKGSITSVQAVYVPADDLTDPAPATS 240
Cdd:CHL00060 259 VNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATT 338
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 371561014 241 FAHLDATTVLNRAISELGIYPAVDPLDSTSRVLEPRTVGQEHYDTARAVRRSLQ 294
Cdd:CHL00060 339 FAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQ 392
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
2-294 |
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: 548.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 2 GR-MNVVGEPIDERGPVGRPNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:TIGR01039 86 GRiFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 81 NIAKGHGGTSVFAGVGERTREGNDLYHEFLDAGVIakdadgnaisegSKVALVYGQMNEPPGARARVALSGLTIAEYFRD 160
Cdd:TIGR01039 166 NIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVI------------DKTALVYGQMNEPPGARMRVALTGLTMAEYFRD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 161 VENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERITSTNKGSITSVQAVYVPADDLTDPAPATS 240
Cdd:TIGR01039 234 EQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATT 313
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 371561014 241 FAHLDATTVLNRAISELGIYPAVDPLDSTSRVLEPRTVGQEHYDTARAVRRSLQ 294
Cdd:TIGR01039 314 FAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQ 367
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
2-293 |
1.84e-129 |
|
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: 375.32 E-value: 1.84e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 2 GRM-NVVGEPIDERGPVGRPNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:TIGR03305 81 SRMfDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIH 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 81 NIAKGHGGTSVFAGVGERTREGNDLYHEFLDAGVIakdadgnaisegSKVALVYGQMNEPPGARARVALSGLTIAEYFRD 160
Cdd:TIGR03305 161 NMVGQHQGVSIFCGIGERCREGEELYREMKEAGVL------------DNTVMVFGQMNEPPGARFRVGHTALTMAEYFRD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 161 VENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERITSTNKGSITSVQAVYVPADDLTDPAPATS 240
Cdd:TIGR03305 229 DEKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHT 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 371561014 241 FAHLDATTVLNRAISELGIYPAVDPLDSTSRVLEPRTVGQEHYDTARAVRRSL 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 ... |
2-272 |
7.13e-120 |
|
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: 344.44 E-value: 7.13e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 2 GR-MNVVGEPIDERGPVGRPNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:cd19476 10 GRiLDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLAR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 81 NIAKGHGGTSVFAGVGERTREGNDLYHEFLDAGVIakdadgnaisegSKVALVYGQMNEPPGARARVALSGLTIAEYFRD 160
Cdd:cd19476 90 NQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAM------------ERTVVVANTANDPPGARMRVPYTGLTIAEYFRD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 161 VEnQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERITSTN--KGSITSVQAVYVPADDLTDPAPA 238
Cdd:cd19476 158 NG-QHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDPIPD 236
|
250 260 270
....*....|....*....|....*....|....
gi 371561014 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 |
1.02e-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: 273.46 E-value: 1.02e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 45 GIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKGhggTSVFAGVGERTREGNDLYHEFLDAGVIAKdadgnai 124
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASAD---VVVYALIGERGREVREFIEELLGSGALKR------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 125 segskVALVYGQMNEPPGARARVALSGLTIAEYFRDvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDM 204
Cdd:pfam00006 71 -----TVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 371561014 205 GALQERITSTN--KGSITSVQAVYVPADDLTDPAPATSFAHLDATTVLNRAISELGIYPAVDPLDSTS 270
Cdd:pfam00006 145 ARLLERAGRVKgkGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
2-272 |
4.21e-54 |
|
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: 176.60 E-value: 4.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 2 GR-MNVVGEPIDERGPVGRPNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:cd01136 10 GRvIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIAR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 81 NIAkghGGTSVFAGVGERTREGNdlyhEFLDagviaKDADGNAISegsKVALVYGQMNEPPGARARVALSGLTIAEYFRD 160
Cdd:cd01136 90 NTD---ADVNVIALIGERGREVR----EFIE-----KDLGEEGLK---RSVLVVATSDESPLLRVRAAYTATAIAEYFRD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 161 vENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERITSTNKGSITSVQAVYVPADDLTDPAPATS 240
Cdd:cd01136 155 -QGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEV 233
|
250 260 270
....*....|....*....|....*....|..
gi 371561014 241 FAHLDATTVLNRAISELGIYPAVDPLDSTSRV 272
Cdd:cd01136 234 RSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
8-291 |
4.75e-47 |
|
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: 162.89 E-value: 4.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 8 GEPIDERGPVGRPNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiakghg 87
Cdd:COG1157 107 GRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIARN------ 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 88 gTS----VFAGVGERTREGNdlyhEFLDagviakDADGnaiSEG-SKVALVYGQMNEPPGARARVALSGLTIAEYFRDvE 162
Cdd:COG1157 181 -TEadvnVIALIGERGREVR----EFIE------DDLG---EEGlARSVVVVATSDEPPLMRLRAAYTATAIAEYFRD-Q 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 163 NQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERITSTNKGSITSVQAVYVPADDLTDPAPATSFA 242
Cdd:COG1157 246 GKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAVRG 325
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 371561014 243 HLDATTVLNRAISELGIYPAVDPLDSTSRVLePRTVGQEHYDTARAVRR 291
Cdd:COG1157 326 ILDGHIVLSRKLAERGHYPAIDVLASISRVM-PDIVSPEHRALARRLRR 373
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
2-271 |
1.89e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 156.70 E-value: 1.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 2 GR-MNVVGEPIDERGPVGR-PNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELi 79
Cdd:PRK06002 107 GRvINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 80 nniAKGHG-GTSVFAGVGERTREgndlYHEFLDagviakDADGNAISegsKVALVYGQMNEPPGARARVALSGLTIAEYF 158
Cdd:PRK06002 186 ---ARADAfDTVVIALVGERGRE----VREFLE------DTLADNLK---KAVAVVATSDESPMMRRLAPLTATAIAEYF 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 159 RDvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERI--TSTNKGSITSVQAVYVPADDLTDPA 236
Cdd:PRK06002 250 RD-RGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPV 328
|
250 260 270
....*....|....*....|....*....|....*
gi 371561014 237 PATSFAHLDATTVLNRAISELGIYPAVDPLDSTSR 271
Cdd:PRK06002 329 ADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISR 363
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
2-291 |
1.61e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 148.29 E-value: 1.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 2 GR-MNVVGEPIDERGPVGRP-----NCEPIHAEAPEFVDQstesaILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLI 75
Cdd:PRK08472 100 GRvVDPLGRPIDGKGAIDYEryapiMKAPIAAMKRGLIDE-----VFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 76 qeliNNIAKG-HGGTSVFAGVGERTREgndlYHEFldagvIAKDADGNAisegSKVALVYGQMNEPPGARARVALSGLTI 154
Cdd:PRK08472 175 ----GMIVKGcLAPIKVVALIGERGRE----IPEF-----IEKNLGGDL----ENTVIVVATSDDSPLMRKYGAFCAMSV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 155 AEYFRDvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERITST-NKGSITSVQAVYVPADDLT 233
Cdd:PRK08472 238 AEYFKN-QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEeGKGSITAFFTVLVEGDDMS 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 371561014 234 DPAPATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRVLEpRTVGQEHYDTARAVRR 291
Cdd:PRK08472 317 DPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKR 373
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
2-293 |
2.89e-39 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 142.65 E-value: 2.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 2 GR-MNVVGEPIDERGPVGRpNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:PRK06820 107 GRiLDGLGAPIDGGPPLTG-QWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 81 NIAkghGGTSVFAGVGERTREgndlYHEFLDAgVIAKDADgnaisegSKVALVYGQMNEPPGARARVALSGLTIAEYFRD 160
Cdd:PRK06820 186 DSA---ADVMVLALIGERGRE----VREFLEQ-VLTPEAR-------ARTVVVVATSDRPALERLKGLSTATTIAEYFRD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 161 vENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERITSTNKGSITSVQAVYVPADDLTDPAPATS 240
Cdd:PRK06820 251 -RGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEV 329
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 371561014 241 FAHLDATTVLNRAISELGIYPAVDPLDSTSRVLePRTVGQEHYDTARAVRRSL 293
Cdd:PRK06820 330 RSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRML 381
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
2-291 |
6.34e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 139.06 E-value: 6.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 2 GR-MNVVGEPIDERGPVGRPNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIqeliN 80
Cdd:PRK08972 105 GRvIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLL----G 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 81 NIAKGHGGTSVFAG-VGERTREGNDLYHEFLD------AGVIAKDADGNaisegskvalvygqmnepPGARARVALSGLT 153
Cdd:PRK08972 181 MMTRGTTADVIVVGlVGERGREVKEFIEEILGeegrarSVVVAAPADTS------------------PLMRLKGCETATT 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 154 IAEYFRDvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERIT--STNKGSITSVQAVYVPADD 231
Cdd:PRK08972 243 IAEYFRD-QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGngGPGQGSITAFYTVLTEGDD 321
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 232 LTDPAPATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRVLePRTVGQEHYDTARAVRR 291
Cdd:PRK08972 322 LQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQ 380
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
2-293 |
1.30e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 135.49 E-value: 1.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 2 GR-MNVVGEPIDERGPVGR-PNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELI 79
Cdd:PRK08927 100 GRvVNALGEPIDGKGPLPQgPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 80 NNIAkghGGTSVFAGVGERTREgndlYHEFLDagviakDADGnaiSEGSKVA-LVYGQMNEPPGARARVALSGLTIAEYF 158
Cdd:PRK08927 180 RNAD---ADVSVIGLIGERGRE----VQEFLQ------DDLG---PEGLARSvVVVATSDEPALMRRQAAYLTLAIAEYF 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 159 RDvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERI--TSTNKGSITSVQAVYVPADDLTDPA 236
Cdd:PRK08927 244 RD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPV 322
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 371561014 237 PATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRVLePRTVGQEHYDTARAVRRSL 293
Cdd:PRK08927 323 ADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLM 378
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
7-293 |
3.24e-36 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 134.49 E-value: 3.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 7 VGEPIDERGPVGRPNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAkgh 86
Cdd:PRK06936 111 LGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSAE--- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 87 GGTSVFAGVGERTREgndlYHEFLDAGVIAkdadgnaisEGSKVA-LVYGQMNEPPGARARVALSGLTIAEYFRDvENQD 165
Cdd:PRK06936 188 VDVTVLALIGERGRE----VREFIESDLGE---------EGLRKAvLVVATSDRPSMERAKAGFVATSIAEYFRD-QGKR 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 166 VLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERITSTNKGSITSVQAVYVPADDLTDPAPATSFAHLD 245
Cdd:PRK06936 254 VLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVADETRSILD 333
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 371561014 246 ATTVLNRAISELGIYPAVDPLDSTSRVLEpRTVGQEHYDTARAVRRSL 293
Cdd:PRK06936 334 GHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELL 380
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
24-293 |
1.05e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 132.79 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 24 PIHA-EAPEFVDqstesaILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiAKGHggTSVFAGVGERTREG 102
Cdd:PRK06793 127 PIHAfEREEITD------VFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKAD--INVISLVGERGREV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 103 NDLyhefldagvIAKDADGNAISegsKVALVYGQMNEPPGARARVALSGLTIAEYFRDvENQDVLFFVDNIFRFTQAGAE 182
Cdd:PRK06793 198 KDF---------IRKELGEEGMR---KSVVVVATSDESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRS 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 183 VSALLGRIPSAvGYQPTLATDMGALQERITSTNKGSITSVQAVYVPADDLTDPAPATSFAHLDATTVLNRAISELGIYPA 262
Cdd:PRK06793 265 VDIAVKELPIG-GKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPA 343
|
250 260 270
....*....|....*....|....*....|.
gi 371561014 263 VDPLDSTSRVLEpRTVGQEHYDTARAVRRSL 293
Cdd:PRK06793 344 ISVLDSVSRIME-EIVSPNHWQLANEMRKIL 373
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
1-293 |
1.15e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 130.23 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 1 GGRMNVVGEPIDERG-PVGRPNCePIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELI 79
Cdd:PRK07721 101 GQVLDALGEPLDGSAlPKGLAPV-STDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 80 NNIAkghGGTSVFAGVGERTREgndlYHEFldagvIAKDADgnaiSEG-SKVALVYGQMNEPPGARARVALSGLTIAEYF 158
Cdd:PRK07721 180 RNTS---ADLNVIALIGERGRE----VREF-----IERDLG----PEGlKRSIVVVATSDQPALMRIKGAYTATAIAEYF 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 159 RDvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERITSTNKGSITSVQAVYVPADDLTDPAPA 238
Cdd:PRK07721 244 RD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIAD 322
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 371561014 239 TSFAHLDATTVLNRAISELGIYPAVDPLDSTSRVLePRTVGQEHYDTARAVRRSL 293
Cdd:PRK07721 323 TVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELL 376
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
8-293 |
2.81e-32 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 123.73 E-value: 2.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 8 GEPIDERGPVGRPNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELinniAKG-H 86
Cdd:PRK09099 113 GEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMF----ARGtQ 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 87 GGTSVFAGVGERTREGNDLYHEFLDAGVIAKDADGNAISEGSKValvygqmneppgARARVALSGLTIAEYFRDvENQDV 166
Cdd:PRK09099 189 CDVNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSI------------ERAKAAYVATAIAEYFRD-RGLRV 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 167 LFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERITSTNKGSITSVQAVYVPADDLTDPAPATSFAHLDA 246
Cdd:PRK09099 256 LLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVRGILDG 335
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 371561014 247 TTVLNRAISELGIYPAVDPLDSTSRVLePRTVGQEHYDTARAVRRSL 293
Cdd:PRK09099 336 HMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLL 381
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
42-293 |
5.99e-32 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 122.75 E-value: 5.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 42 LVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINniAKGhGGTSVFAGVGERTREgndlYHEFLDAgVIAKDADg 121
Cdd:PRK07594 139 LMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN--APD-ADSNVLVLIGERGRE----VREFIDF-TLSEETR- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 122 naisegSKVALVYGQMNEPPGARARVALSGLTIAEYFRDvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLA 201
Cdd:PRK07594 210 ------KRCVIVVATSDRPALERVRALFVATTIAEFFRD-NGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVF 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 202 TDMGALQERITSTNKGSITSVQAVYVPADDLTDPAPATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRVLePRTVGQE 281
Cdd:PRK07594 283 SALPRLLERTGMGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHE 361
|
250
....*....|..
gi 371561014 282 HYDTARAVRRSL 293
Cdd:PRK07594 362 HRQLAAILRRCL 373
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
2-287 |
1.13e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 116.75 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 2 GR-MNVVGEPIDERGPVGRPNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:PRK05688 111 GRvLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTR 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 81 NIAkghGGTSVFAGVGERTREgndlYHEFLDAgvIAKDadgnaisEGSKVALVYGQ-MNEPPGARARVALSGLTIAEYFR 159
Cdd:PRK05688 191 FTE---ADIIVVGLIGERGRE----VKEFIEH--ILGE-------EGLKRSVVVASpADDAPLMRLRAAMYCTRIAEYFR 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 160 DvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERITSTNKG--SITSVQAVYVPADDLTDPAP 237
Cdd:PRK05688 255 D-KGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGggSITAFYTVLSEGDDQQDPIA 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 371561014 238 ATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRVLePRTVGQEHYDTAR 287
Cdd:PRK05688 334 DSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQ 382
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
16-294 |
3.64e-29 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 115.09 E-value: 3.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 16 PVGRPNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINniakgHGGTSVF--A 93
Cdd:PRK08149 109 VGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIE-----HSEADVFviG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 94 GVGERTREGNDLYHEFldagviakdadgNAISEGSKVALVYGQMNEPPGARARVALSGLTIAEYFRDvENQDVLFFVDNI 173
Cdd:PRK08149 184 LIGERGREVTEFVESL------------RASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRD-QGKRVVLFIDSM 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 174 FRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERITSTNKGSITSVQAVYVPADDLTDPAPATSFAHLDATTVLNRA 253
Cdd:PRK08149 251 TRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRK 330
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 371561014 254 ISELGIYPAVDPLDSTSRVLEPRTvGQEHYDTARAVRRSLQ 294
Cdd:PRK08149 331 LAAKGHYPAIDVLKSVSRVFGQVT-DPKHRQLAAAFRKLLT 370
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
2-290 |
5.58e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 114.60 E-value: 5.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 2 GRM-NVVGEPIDERGPVGrpNCEPIHAEAPEF--VDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIqel 78
Cdd:PRK07196 98 GRViNGLGEPLDGKGQLG--GSTPLQQQLPQIhpLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLL--- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 79 iNNIAKGHGGTSVFAG-VGERTREgndlYHEFLDAgviAKDADGNAisegsKVALVYGQMNEPPGARARVALSGLTIAEY 157
Cdd:PRK07196 173 -GMITRYTQADVVVVGlIGERGRE----VKEFIEH---SLQAAGMA-----KSVVVAAPADESPLMRIKATELCHAIATY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 158 FRDvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERI-TSTNKGSITSVQAVYVPADDLTDPA 236
Cdd:PRK07196 240 YRD-KGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGTMTAIYTVLAEGDDQQDPI 318
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 371561014 237 PATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRVLEpRTVGQEHYDTARAVR 290
Cdd:PRK07196 319 VDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLK 371
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
39-293 |
2.94e-24 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 101.40 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 39 SAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIqeliNNIAKGHGGTSVFAG-VGERTREGNDLYHEFLDAG---- 113
Cdd:PRK07960 156 EHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLL----GMMARYTQADVIVVGlIGERGREVKDFIENILGAEgrar 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 114 --VIAKDADgnaISegskvalvygqmnepPGARARVALSGLTIAEYFRDvENQDVLFFVDNIFRFTQAGAEVSALLGRIP 191
Cdd:PRK07960 232 svVIAAPAD---VS---------------PLLRMQGAAYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPP 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 192 SAVGYQPTLATDMGALQERITS--TNKGSITSVQAVYVPADDLTDPAPATSFAHLDATTVLNRAISELGIYPAVDPLDST 269
Cdd:PRK07960 293 ATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASI 372
|
250 260
....*....|....*....|....
gi 371561014 270 SRVLEpRTVGQEHYDTARAVRRSL 293
Cdd:PRK07960 373 SRAMT-ALIDEQHYARVRQFKQLL 395
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
16-271 |
2.09e-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: 96.87 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 16 PV--GRPNCEPIHAEAPefvdqstesaiLVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELinniAK-GHGGTSVF 92
Cdd:cd01134 43 PVrqPRPVKEKLPPNVP-----------LLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSL----SKwSNSDVVIY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 93 AGVGERTREGNDLYHEFLDAGVIAKdadGNAISEgsKVALVYGQMNEPPGARARVALSGLTIAEYFRDVeNQDVLFFVDN 172
Cdd:cd01134 108 VGCGERGNEMAEVLEEFPELKDPIT---GESLME--RTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSLMADS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 173 IFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQER------ITSTNK-GSITSVQAVYVPADDLTDpaPATSfAHLD 245
Cdd:cd01134 182 TSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERagrvrcLGSPGReGSVTIVGAVSPPGGDFSE--PVTQ-ATLR 258
|
250 260
....*....|....*....|....*....
gi 371561014 246 ATTV---LNRAISELGIYPAVDPLDSTSR 271
Cdd:cd01134 259 IVQVfwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
1-271 |
5.06e-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: 95.75 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 1 GGRMNVVGEPIDERGPVGRPNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGV-GKTVLIQelI 79
Cdd:cd01135 12 GRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLpHNELAAQ--I 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 80 NNIAKGHGGTS----VFAGVGERTREGNDLYHEFLDAGVIakdadgnaisegSKVALVYGQMNEPPGARARVALSGLTIA 155
Cdd:cd01135 90 ARQAGVVGSEEnfaiVFAAMGVTMEEARFFKDDFEETGAL------------ERVVLFLNLANDPTIERIITPRMALTTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 156 EYFRDVENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQER--ITSTNKGSITSVQAVYVPADDLT 233
Cdd:cd01135 158 EYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTMPNDDIT 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 371561014 234 DPAPatsfahlDAT-------TVLNRAISELGIYPAVDPLDSTSR 271
Cdd:cd01135 238 HPIP-------DLTgyitegqIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
8-294 |
3.12e-22 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 95.74 E-value: 3.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 8 GEPIDERGPVGRPNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTvliqELINNIAKGHG 87
Cdd:PRK05922 107 GNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKGSK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 88 GT-SVFAGVGERTREGNDLyhefldagvIAKDADGNAiseGSKVALVYGQMNEPPGARARVALSGLTIAEYFRDvENQDV 166
Cdd:PRK05922 183 STiNVIALIGERGREVREY---------IEQHKEGLA---AQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 167 LFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERITSTNKGSITSVQAV-YVP--ADDLTDPAPATSFAH 243
Cdd:PRK05922 250 LFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIlHYPnhPDIFTDYLKSLLDGH 329
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 371561014 244 LDATTVlNRAISElgiyPAVDPLDSTSRVLEPRTVgQEHYDTARAVRRSLQ 294
Cdd:PRK05922 330 FFLTPQ-GKALAS----PPIDILTSLSRSARQLAL-PHHYAAAEELRSLLK 374
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
2-271 |
7.24e-16 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 77.17 E-value: 7.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 2 GR-MNVVGEPIDERGPVGRPNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 80
Cdd:PRK04196 86 GRiFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIAR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 81 NiAKGHGGTS----VFAGVGERTREGNDLYHEFLDAGVIakdadgnaisegSKVALVYGQMNEPPGAR---ARVALsglT 153
Cdd:PRK04196 166 Q-AKVLGEEEnfavVFAAMGITFEEANFFMEDFEETGAL------------ERSVVFLNLADDPAIERiltPRMAL---T 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 154 IAEYFRDVENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQER--ITSTNKGSITSVQAVYVPADD 231
Cdd:PRK04196 230 AAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDD 309
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 371561014 232 LTDPAPatsfahlDAT-------TVLNRAISELGIYPAVDPLDSTSR 271
Cdd:PRK04196 310 ITHPIP-------DLTgyitegqIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
2-272 |
1.26e-15 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 76.49 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 2 GR-MNVVGEPIDERGPVGRPNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL-IQELI 79
Cdd:PRK13343 105 GRvIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIaIDAII 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 80 NNiaKGHGGTSVFAGVGERTREGndlyhefldAGVIAK----DADGNAIsegskvaLVYGQMNEPPGARARVALSGLTIA 155
Cdd:PRK13343 185 NQ--KDSDVICVYVAIGQKASAV---------ARVIETlrehGALEYTT-------VVVAEASDPPGLQYLAPFAGCAIA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 156 EYFRDvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERITSTNK----GSITSVQAVYVPADD 231
Cdd:PRK13343 247 EYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPelggGSLTALPIIETLAGE 325
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 371561014 232 LTDPAPATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRV 272
Cdd:PRK13343 326 LSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRV 366
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
42-274 |
4.11e-15 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 75.20 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 42 LVTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELinniAKgHGGTS--VFAGVGERTREGNDLYHEFLDAgviaKD- 118
Cdd:PRK04192 211 LITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQL----AK-WADADivIYVGCGERGNEMTEVLEEFPEL----IDp 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 119 ADGNAISEgsKVALVYGQMNEPPGAR-ARVaLSGLTIAEYFRDvenQ--DVLFFVDNIFRFTQAGAEVSALLGRIPSAVG 195
Cdd:PRK04192 282 KTGRPLME--RTVLIANTSNMPVAAReASI-YTGITIAEYYRD---MgyDVLLMADSTSRWAEALREISGRLEEMPGEEG 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 196 YQPTLATDMGALQER----IT-STNKGSITSVQAVYVPADDLTDpaPATS--------FAHLDAttvlNRAISELgiYPA 262
Cdd:PRK04192 356 YPAYLASRLAEFYERagrvKTlGGEEGSVTIIGAVSPPGGDFSE--PVTQntlrivkvFWALDA----ELADRRH--FPA 427
|
250
....*....|..
gi 371561014 263 VDPLDSTSRVLE 274
Cdd:PRK04192 428 INWLTSYSLYLD 439
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
91-270 |
2.51e-13 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 70.05 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 91 VFAGVGERTREGNDLYHEFLDAgviaKDAD-GNAISEgsKVALVYGQMNEPPGARARVALSGLTIAEYFRDVeNQDVLFF 169
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFPKL----KDPKtGKPLME--RTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYDVALM 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 170 VDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERI-------TSTNKGSITSVQAVYVPADDLTDPAPATSFA 242
Cdd:PRK14698 759 ADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLR 838
|
170 180
....*....|....*....|....*...
gi 371561014 243 HLDATTVLNRAISELGIYPAVDPLDSTS 270
Cdd:PRK14698 839 VVKVFWALDADLARRRHFPAINWLTSYS 866
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
2-274 |
1.53e-11 |
|
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: 64.36 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 2 GRM-NVVGEPIDeRGPVGRP------NCEPIHAEAPEFVDQstesaILVTGIKVIDLLAPYAKGGKIGLFGGAG------ 68
Cdd:TIGR01040 84 GRVfNGSGKPID-KGPPVLAedyldiNGQPINPYARIYPEE-----MIQTGISAIDVMNSIARGQKIPIFSAAGlphnei 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 69 ----VGKTVLIQELINNIAKGHGG--TSVFAGVGERTREGNDLYHEFLDAGVIakdadgnaisegSKVALVYGQMNEPPG 142
Cdd:TIGR01040 158 aaqiCRQAGLVKLPTKDVHDGHEDnfAIVFAAMGVNMETARFFKQDFEENGSM------------ERVCLFLNLANDPTI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 143 ARARVALSGLTIAEYFRDVENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERITSTN--KGSIT 220
Cdd:TIGR01040 226 ERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrNGSIT 305
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 371561014 221 SVQAVYVPADDLTDPAPATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRVLE 274
Cdd:TIGR01040 306 QIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMK 359
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
1-237 |
3.19e-11 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 63.51 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 1 GGRMNVVGEPIDeRGPvgRPNCEPIHAEAPEF--VDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGktvlIQEL 78
Cdd:PRK02118 84 GRRFNGSGKPID-GGP--ELEGEPIEIGGPSVnpVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEP----YNAL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 79 INNIA-KGHGGTSVFAGVGERTREGNDLYHEFLDAGVIakdadgnaisegSKVALVYGQMNEPPGARARVALSGLTIAEY 157
Cdd:PRK02118 157 LARIAlQAEADIIILGGMGLTFDDYLFFKDTFENAGAL------------DRTVMFIHTASDPPVECLLVPDMALAVAEK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 158 FRDVENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQER-ITSTNKGSITSVQAVYVPADDLTDPA 236
Cdd:PRK02118 225 FALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKaVDFEDGGSITIIAVTTMPGDDVTHPV 304
|
.
gi 371561014 237 P 237
Cdd:PRK02118 305 P 305
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
2-272 |
6.27e-10 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 58.72 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 2 GR-MNVVGEPIDERGPVGRPNCEPIHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKT-VLIQELI 79
Cdd:cd01132 12 GRvVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTaIAIDTII 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 80 NNiaKGHGGTSVFAGVGERTREGNDLYHEFLDAG------VIAKDADGNAisegskvALVYgqmneppgararVA-LSGL 152
Cdd:cd01132 92 NQ--KGKKVYCIYVAIGQKRSTVAQIVKTLEEHGameytiVVAATASDPA-------PLQY------------LApYAGC 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 153 TIAEYFRDvENQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGALQERITSTNK----GSITSVQAVYVP 228
Cdd:cd01132 151 AMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGSLTALPIIETQ 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 371561014 229 ADDLTDPAPATSFAHLDATTVLNRAISELGIYPAVDPLDSTSRV 272
Cdd:cd01132 230 AGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRV 273
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
47-294 |
6.05e-08 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 53.17 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 47 KVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKGHGGTSVFAG-VGERTREGNDLyhefldagviakdadgnais 125
Cdd:PRK12608 122 RVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDM-------------------- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 126 EGSKVALVYGQMNEPPGARaRVALSGLTIAEYFRDVEN-QDVLFFVDNIFRFTQAGAEVSALLGRIPSAvgyqptlATDM 204
Cdd:PRK12608 182 RRSVKGEVYASTFDRPPDE-HIRVAELVLERAKRLVEQgKDVVILLDSLTRLARAYNNEVESSGRTLSG-------GVDA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 205 GALQ--ERITST-----NKGSITSVQAVYVP----ADDLTdpapatsFAHLDAT----TVLNRAISELGIYPAVDPLDST 269
Cdd:PRK12608 254 RALQrpKRLFGAarnieEGGSLTIIATALVDtgsrMDEVI-------FEEFKGTgnmeIVLDRELADKRVFPAIDIAKSG 326
|
250 260
....*....|....*....|....*
gi 371561014 270 SRvLEPRTVGQEHYDTARAVRRSLQ 294
Cdd:PRK12608 327 TR-REELLLDSKELEKVRRLRRALA 350
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
47-294 |
6.74e-08 |
|
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: 52.21 E-value: 6.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 47 KVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKGHGGTSVFAG-VGERTREGNDLyHEFLDAGVIAKDADgnais 125
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTDM-RRSVKGEVVASTFD----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 126 egskvalvygqmnEPPGARARVALSGLTIAEyfRDVE-NQDVLFFVDNIFRFTQAGAEVSALLGRIPSAvgyqptlATDM 204
Cdd:cd01128 79 -------------EPPERHVQVAEMVIEKAK--RLVEhGKDVVILLDSITRLARAYNTVVPSSGKTLSG-------GVDA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 205 GALQ--ERITST-----NKGSITSVQAVYVP----ADDLTdpapatsFAHLDAT----TVLNRAISELGIYPAVDPLDST 269
Cdd:cd01128 137 NALHkpKRFFGAarnieEGGSLTIIATALVDtgsrMDEVI-------FEEFKGTgnmeLVLDRKLAEKRIFPAIDILKSG 209
|
250 260
....*....|....*....|....*
gi 371561014 270 SRvLEPRTVGQEHYDTARAVRRSLQ 294
Cdd:cd01128 210 TR-KEELLLTPEELQKIWLLRRILS 233
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
25-272 |
1.51e-05 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 46.19 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 25 IHAEAPEFVDQSTESAILVTGIKVIDLLAPYAKGGKIGLFGGAGVGKT-VLIQELINN------IAKGHGGTSVFAGVGE 97
Cdd:PTZ00185 156 VDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTsIAVSTIINQvrinqqILSKNAVISIYVSIGQ 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 98 RTREGNDLYHEFLDAGVIakdadgnaisegSKVALVYGQMNEPPGARARVALSGLTIAEYFRDvENQDVLFFVDNIFRFT 177
Cdd:PTZ00185 236 RCSNVARIHRLLRSYGAL------------RYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMN-RGRHCLCVYDDLSKQA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 178 QAGAEVSALLGRIPSAVGYQPTLATDMGALQER--ITSTNK--GSITSVQAVYVPADDLTDPAPATSFAHLDATTVLNRA 253
Cdd:PTZ00185 303 VAYRQISLLLRRPPGREAYPGDVFYLHSRLLERaaMLSPGKggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTK 382
|
250
....*....|....*....
gi 371561014 254 ISELGIYPAVDPLDSTSRV 272
Cdd:PTZ00185 383 LFTGGQRPAVNIGLSVSRV 401
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
57-189 |
1.28e-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: 41.59 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371561014 57 KGGKIGLFGGAGVGKTVLIQELINNIAKGHGgtsvfagvgertregndlyhefldaGVIAKDADGNAISEGSKVALVYGQ 136
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG-------------------------GVIYIDGEDILEEVLDQLLLIIVG 55
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 371561014 137 MNEPPGARARVALSGLTIAEYFRdvenQDVLFFvDNIFRFTQAGAEVSALLGR 189
Cdd:smart00382 56 GKKASGSGELRLRLALALARKLK----PDVLIL-DEITSLLDAEQEALLLLLE 103
|
|
| ATP-synt_F1_beta_C |
cd18110 |
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ... |
278-294 |
1.33e-03 |
|
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: 37.46 E-value: 1.33e-03
|
| |
