|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
9-478 |
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: 951.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 9 TGSVGRVTQVIGAVVDVAFE-GELPKILNALETSN-NGNRLVLEIAQHLGENVVRTIAMDSTDGLVRGQEVTDTGSPIMV 86
Cdd:COG0055 2 AMNTGKIVQVIGPVVDVEFPeGELPAIYNALEVENeGGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 87 PVGNETLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTV 166
Cdd:COG0055 82 PVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 167 LIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESNVNKhgggegsKAALVYGQMNEPPGARARVALTGLTVAEHF 246
Cdd:COG0055 162 LIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALTMAEYF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 247 RD-QGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERITTTTTGSITSVQAIYVPADDLTDPAPA 325
Cdd:COG0055 235 RDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 326 TSFAHLDATTVLSRSIAEKGIYPAVDPLDSTSRMLDPLVVGEEHYEVARKVQSTLQRYKALQDIIAILGMDELSEEDKVA 405
Cdd:COG0055 315 TTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLT 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517055036 406 VARARKIERFLSQPFFVAEVFTGSPGKLVALEDTIKGFKGLVNGEYDHLPEAAFYMVGSMDEAVEKAKKLVAA 478
Cdd:COG0055 395 VARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAE 467
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
11-475 |
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: 847.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 11 SVGRVTQVIGAVVDVAFE-GELPKILNALETSN-NGNRLVLEIAQHLGENVVRTIAMDSTDGLVRGQEVTDTGSPIMVPV 88
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEqGELPRIYNALKVQNrAESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 89 GNETLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLI 168
Cdd:TIGR01039 81 GKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 169 MELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESNVNKhgggegsKAALVYGQMNEPPGARARVALTGLTVAEHFRD 248
Cdd:TIGR01039 161 QELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTMAEYFRD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 249 -QGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERITTTTTGSITSVQAIYVPADDLTDPAPATS 327
Cdd:TIGR01039 234 eQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 328 FAHLDATTVLSRSIAEKGIYPAVDPLDSTSRMLDPLVVGEEHYEVARKVQSTLQRYKALQDIIAILGMDELSEEDKVAVA 407
Cdd:TIGR01039 314 FAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517055036 408 RARKIERFLSQPFFVAEVFTGSPGKLVALEDTIKGFKGLVNGEYDHLPEAAFYMVGSMDEAVEKAKKL 475
Cdd:TIGR01039 394 RARRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
3-475 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 820.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 3 EAATPKTGSVGRVTQVIGAVVDVAF-EGELPKILNALETSNNGN-----RLVLEIAQHLGENVVRTIAMDSTDGLVRGQE 76
Cdd:CHL00060 7 GVSTLEEKNLGRITQIIGPVLDVAFpPGKMPNIYNALVVKGRDTagqeiNVTCEVQQLLGNNRVRAVAMSATDGLMRGME 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 77 VTDTGSPIMVPVGNETLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGL 156
Cdd:CHL00060 87 VIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 157 FGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESNV-NKHGGGEgSKAALVYGQMNEPPGARARV 235
Cdd:CHL00060 167 FGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGViNEQNIAE-SKVALVYGQMNEPPGARMRV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 236 ALTGLTVAEHFRDQG-QDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERITTTTTGSITSVQAIYV 314
Cdd:CHL00060 246 GLTALTMAEYFRDVNkQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 315 PADDLTDPAPATSFAHLDATTVLSRSIAEKGIYPAVDPLDSTSRMLDPLVVGEEHYEVARKVQSTLQRYKALQDIIAILG 394
Cdd:CHL00060 326 PADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 395 MDELSEEDKVAVARARKIERFLSQPFFVAEVFTGSPGKLVALEDTIKGFKGLVNGEYDHLPEAAFYMVGSMDEAVEKAKK 474
Cdd:CHL00060 406 LDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAAN 485
|
.
gi 517055036 475 L 475
Cdd:CHL00060 486 L 486
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
85-362 |
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: 560.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 85 MVPVGNETLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLFGGAGVGK 164
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 165 TVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESNVNKHGGGegSKAALVYGQMNEPPGARARVALTGLTVAE 244
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDGL--SKVALVYGQMNEPPGARARVALTGLTMAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 245 HFRDQ-GQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERITTTTTGSITSVQAIYVPADDLTDPA 323
Cdd:cd01133 159 YFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPA 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 517055036 324 PATSFAHLDATTVLSRSIAEKGIYPAVDPLDSTSRMLDP 362
Cdd:cd01133 239 PATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
13-468 |
0e+00 |
|
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: 554.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 13 GRVTQVIGAVVDVAFEGELPKILNALETSNNGNrLVLEIAQHLGENVVRTIAMDSTDGLVRGQEVTDTGSPIMVPVGNET 92
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDGELPAIHSVLRAGREGE-VVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 93 LGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELI 172
Cdd:TIGR03305 80 LSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 173 NNVAKAHGGYSVFAGVGERTREGNDLYHEMIESNVNKHgggegskAALVYGQMNEPPGARARVALTGLTVAEHFRD-QGQ 251
Cdd:TIGR03305 160 HNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDN-------TVMVFGQMNEPPGARFRVGHTALTMAEYFRDdEKQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 252 DVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERITTTTTGSITSVQAIYVPADDLTDPAPATSFAHL 331
Cdd:TIGR03305 233 DVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 332 DATTVLSRSIAEKGIYPAVDPLDSTSRMLDPLVVGEEHYEVARKVQSTLQRYKALQDIIAILGMDELSEEDKVAVARARK 411
Cdd:TIGR03305 313 SASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 517055036 412 IERFLSQPFFVAEVFTGSPGKLVALEDTIKGFKGLVNGEYDHLPEAAFYMVGSMDEA 468
Cdd:TIGR03305 393 LERFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDEA 449
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
86-359 |
2.76e-124 |
|
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: 362.93 E-value: 2.76e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 86 VPVGNETLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKT 165
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 166 VLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESNVNkhgggegSKAALVYGQMNEPPGARARVALTGLTVAEH 245
Cdd:cd19476 82 VLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAM-------ERTVVVANTANDPPGARMRVPYTGLTIAEY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 246 FRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERITTTTTGS--ITSVQAIYVPADDLTDPA 323
Cdd:cd19476 155 FRDNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGgsITAIPAVSTPGDDLTDPI 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 517055036 324 PATSFAHLDATTVLSRSIAEKGIYPAVDPLDSTSRM 359
Cdd:cd19476 235 PDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
138-357 |
8.72e-86 |
|
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: 262.29 E-value: 8.72e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 138 GIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNVAKahgGYSVFAGVGERTREGNDLYHEMIESNVNKhgggegsK 217
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALK-------R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 218 AALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQER 297
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517055036 298 ITTTTTGSIT--SVQAIYVPADDLTDPAPATSFAHLDATTVLSRSIAEKGIYPAVDPLDSTS 357
Cdd:pfam00006 151 AGRVKGKGGSitALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| ATP-synt_F1_beta_C |
cd18110 |
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ... |
364-471 |
2.24e-75 |
|
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: 231.60 E-value: 2.24e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 364 VVGEEHYEVARKVQSTLQRYKALQDIIAILGMDELSEEDKVAVARARKIERFLSQPFFVAEVFTGSPGKLVALEDTIKGF 443
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 517055036 444 KGLVNGEYDHLPEAAFYMVGSMDEAVEK 471
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
12-419 |
4.56e-68 |
|
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: 224.14 E-value: 4.56e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 12 VGRVTQVIGAVVDV----AFEGELPKILNAletsnNGNRLvleiaqhLGEnVV-----RTIAM--DSTDGLVRGQEVTDT 80
Cdd:COG1157 20 SGRVTRVVGLLIEAvgpdASIGELCEIETA-----DGRPV-------LAE-VVgfrgdRVLLMplGDLEGISPGARVVPT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 81 GSPIMVPVGNETLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLFGGA 160
Cdd:COG1157 87 GRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 161 GVGKTVLIMELINNvAKAHggYSVFAGVGERTREGNdlyhEMIEsnvnKHGGGEG-SKAALVYGQMNEPPGARARVALTG 239
Cdd:COG1157 167 GVGKSTLLGMIARN-TEAD--VNVIALIGERGREVR----EFIE----DDLGEEGlARSVVVVATSDEPPLMRLRAAYTA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 240 LTVAEHFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERittTTTGSITSVQAIY---VPA 316
Cdd:COG1157 236 TAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLER---AGNGGKGSITAFYtvlVEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 317 DDLTDPAPATSFAHLDATTVLSRSIAEKGIYPAVDPLDSTSRMLdPLVVGEEHYEVARKVQSTLQRYKALQDIIAI---- 392
Cdd:COG1157 313 DDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM-PDIVSPEHRALARRLRRLLARYEENEDLIRIgayq 391
|
410 420
....*....|....*....|....*..
gi 517055036 393 LGMDELSEEdkvAVARARKIERFLSQP 419
Cdd:COG1157 392 PGSDPELDE---AIALIPAIEAFLRQG 415
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
85-358 |
6.07e-58 |
|
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: 192.39 E-value: 6.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 85 MVPVGNETLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLFGGAGVGK 164
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 165 TVLIMELINNVAKAhggYSVFAGVGERTREGNdlyhEMIEsnvnKHGGGEG-SKAALVYGQMNEPPGARARVALTGLTVA 243
Cdd:cd01136 81 STLLGMIARNTDAD---VNVIALIGERGREVR----EFIE----KDLGEEGlKRSVLVVATSDESPLLRVRAAYTATAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 244 EHFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERittTTTGSITSVQAIY---VPADDLT 320
Cdd:cd01136 150 EYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLER---AGNGEKGSITAFYtvlVEGDDFN 226
|
250 260 270
....*....|....*....|....*....|....*...
gi 517055036 321 DPAPATSFAHLDATTVLSRSIAEKGIYPAVDPLDSTSR 358
Cdd:cd01136 227 DPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
13-418 |
2.80e-54 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 188.10 E-value: 2.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 13 GRVTQV----IGAVVDVAFEGELPKILNaletsnngNRLVLEIAQHLGENVVRTiAMDSTDGLVRGQEVTDTGSPIMVPV 88
Cdd:PRK06820 31 GPIVEIgptlLRASLPGVAQGELCRIEP--------QGMLAEVVSIEQEMALLS-PFASSDGLRCGQWVTPLGHMHQVQV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 89 GNETLGRIMNVIGEPVDeAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLI 168
Cdd:PRK06820 102 GADLAGRILDGLGAPID-GGPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 169 MELinnVAKAHGGYSVFAGVGERTREgndlYHEMIESNVNKHGGgegSKAALVYGQMNEPPGARARVALTGLTVAEHFRD 248
Cdd:PRK06820 181 GML---CADSAADVMVLALIGERGRE----VREFLEQVLTPEAR---ARTVVVVATSDRPALERLKGLSTATTIAEYFRD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 249 QGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERITTTTTGSITSVQAIYVPADDLTDPAPATSF 328
Cdd:PRK06820 251 RGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 329 AHLDATTVLSRSIAEKGIYPAVDPLDSTSRMLdPLVVGEEHYEVARKVQSTLQRYKALQDIIAI----LGMDELSEEdkv 404
Cdd:PRK06820 331 SLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQEIELLVRVgeyqAGEDLQADE--- 406
|
410
....*....|....
gi 517055036 405 AVARARKIERFLSQ 418
Cdd:PRK06820 407 ALQRYPAICAFLQQ 420
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
13-418 |
3.08e-51 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 179.95 E-value: 3.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 13 GRVTQVIG----AVVDVAFEGELPKILNALETSNngnrLVLEI---AQHlgenVVRTIAMDSTDGLVRGQEVTDTGSPIM 85
Cdd:PRK06936 25 GRVTQVTGtilkAVVPGVRIGELCYLRNPDNSLS----LQAEVigfAQH----QALLTPLGEMYGISSNTEVSPTGTMHQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 86 VPVGNETLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKT 165
Cdd:PRK06936 97 VGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 166 VLIMELINNvakAHGGYSVFAGVGERTREgndlYHEMIESNVnkhgGGEG-SKAALVYGQMNEPPGARARVALTGLTVAE 244
Cdd:PRK06936 177 TLLASLIRS---AEVDVTVLALIGERGRE----VREFIESDL----GEEGlRKAVLVVATSDRPSMERAKAGFVATSIAE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 245 HFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERITTTTTGSITSVQAIYVPADDLTDPAP 324
Cdd:PRK06936 246 YFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 325 ATSFAHLDATTVLSRSIAEKGIYPAVDPLDSTSRMLDPlVVGEEHYEVARKVQSTLQRYKALQDIIAI----LGMDELSE 400
Cdd:PRK06936 326 DETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQ-IVSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDKEAD 404
|
410
....*....|....*...
gi 517055036 401 EdkvAVARARKIERFLSQ 418
Cdd:PRK06936 405 Q---AIERIGAIRGFLRQ 419
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
84-448 |
4.19e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 176.80 E-value: 4.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 84 IMVPVGNETLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLFGGAGVG 163
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 164 KTVLiMELINNVAKAHggYSVFAGVGERTREgndlYHEMIESNVnkhgGGEGSKAALVYGQMNEPPGARARVALTGLTVA 243
Cdd:PRK08472 170 KSTL-MGMIVKGCLAP--IKVVALIGERGRE----IPEFIEKNL----GGDLENTVIVVATSDDSPLMRKYGAFCAMSVA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 244 EHFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERitTTTTGSITSVQAIY---VPADDLT 320
Cdd:PRK08472 239 EYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMER--AGKEEGKGSITAFFtvlVEGDDMS 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 321 DPAPATSFAHLDATTVLSRSIAEKGIYPAVDPLDSTSRMLDPlVVGEEHYEVARKVQSTLQRYKALQDIIAI----LGMD 396
Cdd:PRK08472 317 DPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMND-IISPEHKLAARKFKRLYSLLKENEVLIRIgayqKGND 395
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 517055036 397 -ELSEedkvAVARARKIERFLSQpffvaevftgSPGKLVALEDTIKGFKGLVN 448
Cdd:PRK08472 396 kELDE----AISKKEFMEQFLKQ----------NPNELFPFEQTFEQLEEILR 434
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
94-418 |
6.01e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 171.33 E-value: 6.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 94 GRIMNVIGEPVDEAGPLVTA-HKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELi 172
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGtRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 173 nnvAKAHGGYSV-FAGVGERTREgndlYHEMIESNVnkhgGGEGSKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQ 251
Cdd:PRK06002 186 ---ARADAFDTVvIALVGERGRE----VREFLEDTL----ADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 252 DVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERI--TTTTTGSITSVQAIYVPADDLTDPAPATSFA 329
Cdd:PRK06002 255 NVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIRG 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 330 HLDATTVLSRSIAEKGIYPAVDPLDSTSRMLDPLVVGEEHyEVARKVQSTLQRYKALQDIIAILGMDELSEED-KVAVAR 408
Cdd:PRK06002 335 TLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQR-KLVSRLKSMIARFEETRDLRLIGGYRAGSDPDlDQAVDL 413
|
330
....*....|
gi 517055036 409 ARKIERFLSQ 418
Cdd:PRK06002 414 VPRIYEALRQ 423
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
13-450 |
1.52e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 169.90 E-value: 1.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 13 GRVTQVIGAVVD----VAFEGELPKILnalETSNNGNRLVLEIAQHLGENVVrTIAMDSTDGLVRGQEVTDTGSPIMVPV 88
Cdd:PRK07721 20 GKVSRVIGLMIEskgpESSIGDVCYIH---TKGGGDKAIKAEVVGFKDEHVL-LMPYTEVAEIAPGCLVEATGKPLEVKV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 89 GNETLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLi 168
Cdd:PRK07721 96 GSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTL- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 169 MELINNVAKAHggYSVFAGVGERTREgndlYHEMIESNVnkhgGGEG-SKAALVYGQMNEPPGARARVALTGLTVAEHFR 247
Cdd:PRK07721 175 MGMIARNTSAD--LNVIALIGERGRE----VREFIERDL----GPEGlKRSIVVVATSDQPALMRIKGAYTATAIAEYFR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 248 DQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERITTTTTGSITSVQAIYVPADDLTDPAPATS 327
Cdd:PRK07721 245 DQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 328 FAHLDATTVLSRSIAEKGIYPAVDPLDSTSRMLdPLVVGEEHYEVARKVQSTLQRYKALQDIIAILGMDE-LSEEDKVAV 406
Cdd:PRK07721 325 RGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINIGAYKRgSSREIDEAI 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 517055036 407 ARARKIERFLSQPffVAEVFTgspgklvaLEDTIKGFKGLVNGE 450
Cdd:PRK07721 404 QFYPQIISFLKQG--TDEKAT--------FEESIQALLSLFGKG 437
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
70-392 |
8.05e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 167.95 E-value: 8.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 70 GLVRGQEVTDTGSPIMVPVGNETLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYA 149
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 150 RGGKIGLFGGAGVGKTVLI-MELINNVAKAhggySVFAGVGERTREGNDLYHEMIesnvnkhgGGEG-SKAALVYGQMNE 227
Cdd:PRK08972 161 KGQRMGLFAGSGVGKSVLLgMMTRGTTADV----IVVGLVGERGREVKEFIEEIL--------GEEGrARSVVVAAPADT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 228 PPGARARVALTGLTVAEHFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERITTTTTGSIT 307
Cdd:PRK08972 229 SPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGS 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 308 sVQAIYV---PADDLTDPAPATSFAHLDATTVLSRSIAEKGIYPAVDPLDSTSRMLdPLVVGEEHYEVARKVQSTLQRYK 384
Cdd:PRK08972 309 -ITAFYTvltEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQ 386
|
....*...
gi 517055036 385 ALQDIIAI 392
Cdd:PRK08972 387 QNRDLISI 394
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
4-419 |
1.76e-45 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 164.17 E-value: 1.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 4 AATPKTGSVGRVTQVIGAVVDV----AFEGELPKILNALETsnngnrlVLEIAQHLG--ENVVRTIAMDSTDGLVRGQEV 77
Cdd:PRK09099 17 AALPAVRRTGKVVEVIGTLLRVsgldVTLGELCELRQRDGT-------LLQRAEVVGfsRDVALLSPFGELGGLSRGTRV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 78 TDTGSPIMVPVGNETLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLF 157
Cdd:PRK09099 90 IGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 158 GGAGVGKTVLIMELINNvakAHGGYSVFAGVGERTREgndlYHEMIESNVnkhgGGEG-SKAALVYGQMNEPPGARARVA 236
Cdd:PRK09099 170 APAGVGKSTLMGMFARG---TQCDVNVIALIGERGRE----VREFIELIL----GEDGmARSVVVCATSDRSSIERAKAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 237 LTGLTVAEHFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERittTTTGSITSVQAIY-VP 315
Cdd:PRK09099 239 YVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLER---AGMGETGSITALYtVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 316 ADDLT--DPAPATSFAHLDATTVLSRSIAEKGIYPAVDPLDSTSRMLdPLVVGEEHYEVARKVQSTLQRYKALQDIIAI- 392
Cdd:PRK09099 316 AEDESgsDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVg 394
|
410 420 430
....*....|....*....|....*....|
gi 517055036 393 ---LGMDELSEEdkvAVARARKIERFLSQP 419
Cdd:PRK09099 395 eyrAGSDPVADE---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
13-418 |
8.92e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 162.46 E-value: 8.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 13 GRVTQVIGAVVDVAFEGELPKILNALETSNNGNRLVleIAQHLGENVVRTIAM--DSTDGLVRGQEVTDTGSPIMVPVGN 90
Cdd:PRK08927 19 GRVVAVRGLLVEVAGPIHALSVGARIVVETRGGRPV--PCEVVGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAVRPSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 91 ETLGRIMNVIGEPVDEAGPLVT-AHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIM 169
Cdd:PRK08927 97 AWLGRVVNALGEPIDGKGPLPQgPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 170 ELINNVAKAhggYSVFAGVGERTREgndlYHEMIESNVnkhgGGEG-SKAALVYGQMNEPPGARARVALTGLTVAEHFRD 248
Cdd:PRK08927 177 MLARNADAD---VSVIGLIGERGRE----VQEFLQDDL----GPEGlARSVVVVATSDEPALMRRQAAYLTLAIAEYFRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 249 QGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERiTTTTTGSITSVQAIY---VPADDLTDPAPA 325
Cdd:PRK08927 246 QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLER-AGPGPIGEGTITGLFtvlVDGDDHNEPVAD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 326 TSFAHLDATTVLSRSIAEKGIYPAVDPLDSTSRMLdPLVVGEEHYEVARKVQSTLQRYKALQDIIAI----LGMDELSEE 401
Cdd:PRK08927 325 AVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRLgayrAGSDPEVDE 403
|
410
....*....|....*..
gi 517055036 402 dkvAVARARKIERFLSQ 418
Cdd:PRK08927 404 ---AIRLNPALEAFLRQ 417
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
63-418 |
1.05e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 153.98 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 63 IAMDSTDGLVRGQEVTDTGSPIMVPVGNETLGRIMNVIGEPVDEAGPLVTAHKrsIHQDAPTY--VEQSTEAQILVTGIK 140
Cdd:PRK06793 68 LPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQK--IKLDAPPIhaFEREEITDVFETGIK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 141 VVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNvAKAHggYSVFAGVGERTREGNDLyhemiesnVNKHGGGEG-SKAA 219
Cdd:PRK06793 146 SIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKAD--INVISLVGERGREVKDF--------IRKELGEEGmRKSV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 220 LVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAvGYQPTLATDMGQMQERIT 299
Cdd:PRK06793 215 VVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 300 TTTTGSITSVQAIYVPADDLTDPAPATSFAHLDATTVLSRSIAEKGIYPAVDPLDSTSRMLDPlVVGEEHYEVARKVQST 379
Cdd:PRK06793 294 KTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEE-IVSPNHWQLANEMRKI 372
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 517055036 380 LQRYKAlQDIIAILGMDELSEEDKVAVARARKIE---RFLSQ 418
Cdd:PRK06793 373 LSIYKE-NELYFKLGTIQENAENAYIFECKNKVEginTFLKQ 413
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
18-420 |
4.79e-41 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 152.07 E-value: 4.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 18 VIGAVVDVAFEGELPKILNALETSNngnrlVLEIAQHLGENVVRTI--AMDSTDGLVRGQEVTDTGSPIMVPVGNETLGR 95
Cdd:PRK08149 17 IIEAELPDVAIGEICEIRAGWHSNE-----VIARAQVVGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 96 IMNVIGEPVDEAGPLVTA----HKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMEL 171
Cdd:PRK08149 92 VLDPTGKIVERFDAPPTVgpisEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNML 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 172 INNvakAHGGYSVFAGVGERTREGNDLYHEMIESnvnkhggGEGSKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQ 251
Cdd:PRK08149 172 IEH---SEADVFVIGLIGERGREVTEFVESLRAS-------SRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 252 DVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERITTTTTGSITSVQAIYVPADDLTDPAPATSFAHL 331
Cdd:PRK08149 242 RVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSIL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 332 DATTVLSRSIAEKGIYPAVDPLDSTSRMLDPlVVGEEHYEVARKVQSTLQRYKALQDIIAiLGMDELSE--EDKVAVARA 409
Cdd:PRK08149 322 DGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQ-VTDPKHRQLAAAFRKLLTRLEELQLFID-LGEYRRGEnaDNDRAMDKR 399
|
410
....*....|.
gi 517055036 410 RKIERFLSQPF 420
Cdd:PRK08149 400 PALEAFLKQDV 410
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
67-436 |
1.61e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 151.04 E-value: 1.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 67 STDGLVRGQEVTDTGSPIMVPVGNETLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLA 146
Cdd:PRK05688 84 SVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 147 PYARGGKIGLFGGAGVGKTVLiMELINNVAKAHggYSVFAGVGERTREgndlYHEMIESNVnkhgGGEG-SKAALVYGQM 225
Cdd:PRK05688 164 TVGRGQRLGLFAGTGVGKSVL-LGMMTRFTEAD--IIVVGLIGERGRE----VKEFIEHIL----GEEGlKRSVVVASPA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 226 NEPPGARARVALTGLTVAEHFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERiTTTTTGS 305
Cdd:PRK05688 233 DDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVER-AGNAEPG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 306 ITSVQAIYV---PADDLTDPAPATSFAHLDATTVLSRSIAEKGIYPAVDPLDSTSRMLdPLVVGEEHYEVARKVQSTLQR 382
Cdd:PRK05688 312 GGSITAFYTvlsEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSR 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 517055036 383 YKALQDIIAI----LGMDelsEEDKVAVARARKIERFLSQPFFVAEVFTGSPGKLVAL 436
Cdd:PRK05688 391 YQQSRDLISVgayvAGGD---PETDLAIARFPHLVQFLRQGLRENVSLAQSREQLAAI 445
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
70-436 |
2.42e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 150.43 E-value: 2.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 70 GLVRGQEVTDTGSPIMVPVGNETLGRIMNVIGEPVDEAGPL-----VTAHKRSIHQdaptyVEQSTEAQILVTGIKVVDL 144
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLggstpLQQQLPQIHP-----LQRRAVDTPLDVGVNAING 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 145 LAPYARGGKIGLFGGAGVGKTVLiMELINNVAKAHggYSVFAGVGERTREgndlYHEMIESNVnkhgGGEG-SKAALVYG 223
Cdd:PRK07196 149 LLTIGKGQRVGLMAGSGVGKSVL-LGMITRYTQAD--VVVVGLIGERGRE----VKEFIEHSL----QAAGmAKSVVVAA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 224 QMNEPPGARARVALTGLTVAEHFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQEriTTTTT 303
Cdd:PRK07196 218 PADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAE--SAGNS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 304 GSITSVQAIYV---PADDLTDPAPATSFAHLDATTVLSRSIAEKGIYPAVDPLDSTSRMLDPlVVGEEHYEVARKVQSTL 380
Cdd:PRK07196 296 SGNGTMTAIYTvlaEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQ-VIGSQQAKAASLLKQCY 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 381 QRYKALQDIIA----ILGMDELSEEdkvAVARARKIERFLSQPFFVAEVFTGSPGKLVAL 436
Cdd:PRK07196 375 ADYMAIKPLIPlggyVAGADPMADQ---AVHYYPAITQFLRQEVGHPALFSASVEQLTGM 431
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
67-409 |
8.46e-40 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 148.56 E-value: 8.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 67 STDGLVRGQEVTDTGSPIMVPVGNETLGRIMNVIGEPVDEAgPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLA 146
Cdd:PRK07594 72 STIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 147 PYARGGKIGLFGGAGVGKTVLIMELINnvaKAHGGYSVFAGVGERTREgndlYHEMIESNVNKHGGgegSKAALVYGQMN 226
Cdd:PRK07594 151 TCGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGRE----VREFIDFTLSEETR---KRCVIVVATSD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 227 EPPGARARVALTGLTVAEHFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERITTTTTGSI 306
Cdd:PRK07594 221 RPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSI 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 307 TSVQAIYVPADDLTDPAPATSFAHLDATTVLSRSIAEKGIYPAVDPLDSTSRMLdPLVVGEEHyevaRKVQSTLQRYKAL 386
Cdd:PRK07594 301 TAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEH----RQLAAILRRCLAL 375
|
330 340
....*....|....*....|....
gi 517055036 387 -QDIIAILGMDELSEEDKVAVARA 409
Cdd:PRK07594 376 yQEVELLIRIGEYQRGVDTDTDKA 399
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
11-84 |
2.47e-36 |
|
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of FoF1-ATP synthase, N-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: 349739 [Multi-domain] Cd Length: 76 Bit Score: 128.79 E-value: 2.47e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517055036 11 SVGRVTQVIGAVVDVAF-EGELPKILNALET-SNNGNRLVLEIAQHLGENVVRTIAMDSTDGLVRGQEVTDTGSPI 84
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFpEGELPPIYNALEVkGDDGKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
6-421 |
2.22e-33 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 131.44 E-value: 2.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 6 TPKTGSVGRVTQVIGAVVDvAFEGELPKILNALETSNNGNRLVLEIAQHLGENVVRTIAM--DSTDGLVRGQEV------ 77
Cdd:PRK07960 22 LPAVRRYGRLTRATGLVLE-ATGLQLPLGATCVIERQNGSETHEVESEVVGFNGQRLFLMplEEVEGILPGARVyarnis 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 78 -TDTGSPIMVPVGNETLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGL 156
Cdd:PRK07960 101 gEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 157 FGGAGVGKTVLImeliNNVAKAHGGYSVFAG-VGERTREGNDLYHEMIesnvnkhgGGEG-SKAALVYGQMNEPPGARAR 234
Cdd:PRK07960 181 FAGSGVGKSVLL----GMMARYTQADVIVVGlIGERGREVKDFIENIL--------GAEGrARSVVIAAPADVSPLLRMQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 235 VALTGLTVAEHFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERITTTTTGSITsVQAIYV 314
Cdd:PRK07960 249 GAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGS-ITAFYT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 315 ---PADDLTDPAPATSFAHLDATTVLSRSIAEKGIYPAVDPLDSTSRMLDPLvVGEEHYEVARKVQSTLQRYKALQDIIA 391
Cdd:PRK07960 328 vltEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAL-IDEQHYARVRQFKQLLSSFQRNRDLVS 406
|
410 420 430
....*....|....*....|....*....|....
gi 517055036 392 I----LGMDELSEEdkvAVARARKIERFLSQPFF 421
Cdd:PRK07960 407 VgayaKGSDPMLDK---AIALWPQLEAFLQQGIF 437
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
74-450 |
1.14e-30 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 123.48 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 74 GQEVTDTGSPIMVPVGNETLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGK 153
Cdd:PRK05922 80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 154 IGLFGGAGVGKTvlimELINNVAK-AHGGYSVFAGVGERTREgndlyhemIESNVNKHGGG-EGSKAALVYGQMNEPPGA 231
Cdd:PRK05922 160 IGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGRE--------VREYIEQHKEGlAAQRTIIIASPAHETAPT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 232 RARVALTGLTVAEHFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERITTTTTGSITSVQA 311
Cdd:PRK05922 228 KVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 312 I-YVP--ADDLTDPAPATSFAHLDATTVlSRSIAEkgiyPAVDPLDSTSRMLDPLVVgEEHYEVARKVQSTLQRYKALQD 388
Cdd:PRK05922 308 IlHYPnhPDIFTDYLKSLLDGHFFLTPQ-GKALAS----PPIDILTSLSRSARQLAL-PHHYAAAEELRSLLKAYHEALD 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517055036 389 IIAI----LGMDElsEEDKvAVARARKIERFLSQPFfvaevftgspGKLVALEDTIKGFKGLVNGE 450
Cdd:PRK05922 382 IIQLgayvPGQDA--HLDR-AVKLLPSIKQFLSQPL----------SSYCALHNTLKQLEALLKHE 434
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
6-278 |
1.12e-28 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 118.48 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 6 TPKTGSVGRVTqvigAVVD-VAFEGELPKI-LNALETSNNGnrlVLEIAQHLGENVVRTIAMDSTDGLVRGQEVTDTGSP 83
Cdd:PRK13343 22 QPDAREIGRVE----SVGDgIAFVSGLPDAaLDELLRFEGG---SRGFAFNLEEELVGAVLLDDTADILAGTEVRRTGRV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 84 IMVPVGNETLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLFGGAGVG 163
Cdd:PRK13343 95 LEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 164 KTVLIMELINNvAKAHGGYSVFAGVGERTREGNdlyhEMIESnVNKHGGGEGSkaALVYGQMNEPPGARARVALTGLTVA 243
Cdd:PRK13343 175 KTAIAIDAIIN-QKDSDVICVYVAIGQKASAVA----RVIET-LREHGALEYT--TVVVAEASDPPGLQYLAPFAGCAIA 246
|
250 260 270
....*....|....*....|....*....|....*
gi 517055036 244 EHFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIP 278
Cdd:PRK13343 247 EYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPP 281
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
22-420 |
2.22e-27 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 114.15 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 22 VVDVAFeGELPKIlnalETSNNGNRL--VLEIAqhlGENVVRTIaMDSTDGL-VRGQEVTDTGSPIMVPVGNETLGRIMN 98
Cdd:PRK04196 20 VEGVAY-GEIVEI----ELPNGEKRRgqVLEVS---EDKAVVQV-FEGTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 99 VIGEPVDEAGPLVTAHKRSIHQDA--PTYVEQSTEaqILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNvA 176
Cdd:PRK04196 91 GLGRPIDGGPEIIPEKRLDINGAPinPVAREYPEE--FIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIARQ-A 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 177 KAHGGYS----VFAGVGERTREGNDLYHEMIESnvnkhggGEGSKAALVYGQMNEPPGAR---ARVAltgLTVAEHFR-D 248
Cdd:PRK04196 168 KVLGEEEnfavVFAAMGITFEEANFFMEDFEET-------GALERSVVFLNLADDPAIERiltPRMA---LTAAEYLAfE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 249 QGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERITTTTTGSITSVQ--AIYVPADDLTDPAPat 326
Cdd:PRK04196 238 KGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQipILTMPDDDITHPIP-- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 327 sfahlDAT-------TVLSRSIAEKGIYPAVDPLDSTSRMLDpLVVG-----EEHYEVARKVQSTLQRYKALQDIIAILG 394
Cdd:PRK04196 316 -----DLTgyitegqIVLSRELHRKGIYPPIDVLPSLSRLMK-DGIGegktrEDHKDVANQLYAAYARGKDLRELAAIVG 389
|
410 420
....*....|....*....|....*..
gi 517055036 395 MDELSEEDKVAVARARKIE-RFLSQPF 420
Cdd:PRK04196 390 EEALSERDRKYLKFADAFErEFVNQGF 416
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
86-361 |
1.60e-22 |
|
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: 96.91 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 86 VPVGNETLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKT 165
Cdd:cd01135 4 LPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLPHN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 166 VLIMELINNvAKAHGGYS----VFAGVGERTREGNDLYHEMIESnvnkhggGEGSKAALVYGQMNEPPGARARVALTGLT 241
Cdd:cd01135 84 ELAAQIARQ-AGVVGSEEnfaiVFAAMGVTMEEARFFKDDFEET-------GALERVVLFLNLANDPTIERIITPRMALT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 242 VAEHFR-DQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERITTTTTGSITSVQ--AIYVPADD 318
Cdd:cd01135 156 TAEYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQipILTMPNDD 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 517055036 319 LTDPAPatsfahlDAT-------TVLSRSIAEKGIYPAVDPLDSTSRMLD 361
Cdd:cd01135 236 ITHPIP-------DLTgyitegqIYLDRDLHNKGIYPPIDVLPSLSRLMK 278
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
111-358 |
7.83e-22 |
|
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: 95.33 E-value: 7.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 111 VTAHKRSIHQDAPtYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELinnvAKahggYS-----VF 185
Cdd:cd01134 37 VNVQRWPVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSL----SK----WSnsdvvIY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 186 AGVGERTREGNDLYHEMIESNVNKHGGGEGSKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFVDNIFRFTQ 265
Cdd:cd01134 108 VGCGERGNEMAEVLEEFPELKDPITGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 266 AGSEVSALLGRIPSAVGYQPTLATDMGQMQERI-------TTTTTGSITSVQAIYVPADDLTDpaPATSfAHLDATTV-- 336
Cdd:cd01134 188 ALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrclgSPGREGSVTIVGAVSPPGGDFSE--PVTQ-ATLRIVQVfw 264
|
250 260
....*....|....*....|...
gi 517055036 337 -LSRSIAEKGIYPAVDPLDSTSR 358
Cdd:cd01134 265 gLDKKLAQRRHFPSINWLISYSK 287
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
369-436 |
5.89e-21 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 86.34 E-value: 5.89e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517055036 369 HYEVARKVQSTLQRYKALQDIIAILGMDELSEEDKVAVARARKIERFLSQPFFVAEVFTGSPGKLVAL 436
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPI 68
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
184-430 |
1.07e-19 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 92.39 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 184 VFAGVGERTREGNDLYHEMIESNVNKHGGGEGSKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFVDNIFRF 263
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRW 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 264 TQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERITTTTTG-------SITSVQAIYVPADDLTDPAPATSFAHLDATTV 336
Cdd:PRK14698 766 AEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLgsdyrvgSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWA 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 337 LSRSIAEKGIYPAVDPLDSTSRMLDPLV------VGEEHYEVARKVQSTLQRYKALQDIIAILGMDELSEEDKVAVARAR 410
Cdd:PRK14698 846 LDADLARRRHFPAINWLTSYSLYVDAVKdwwhknVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAILLVAR 925
|
250 260
....*....|....*....|.
gi 517055036 411 KI-ERFLSQPFFvAEVFTGSP 430
Cdd:PRK14698 926 MLrEDYLQQDAF-DEVDTYCP 945
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
84-418 |
2.60e-19 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 90.61 E-value: 2.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 84 IMVPVGNEtlGRIMNVIGE---PVDEAGPLVTAHKRSIH-----QDAP-----TYVEQSTEAQILVTGIKVVDLLAPYAR 150
Cdd:PRK04192 149 IMVPPGVS--GTVKEIVSEgdyTVDDTIAVLEDEDGEGVeltmmQKWPvrrprPYKEKLPPVEPLITGQRVIDTFFPVAK 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 151 GGKIGLFGGAGVGKTVLIMELinnvAKahggYS-----VFAGVGERTREGNDLYHEMIESNVNKHGGGEGSKAALVYGQM 225
Cdd:PRK04192 227 GGTAAIPGPFGSGKTVTQHQL----AK----WAdadivIYVGCGERGNEMTEVLEEFPELIDPKTGRPLMERTVLIANTS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 226 NEPPGAR-ARVaLTGLTVAEHFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERitttttg 304
Cdd:PRK04192 299 NMPVAAReASI-YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYER------- 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 305 sitsvqAIYV------------------PADDLTDpaPATSfAHLDATTV---LSRSIAEKGIYPAVDPLDSTSRMLDPL 363
Cdd:PRK04192 371 ------AGRVktlggeegsvtiigavspPGGDFSE--PVTQ-NTLRIVKVfwaLDAELADRRHFPAINWLTSYSLYLDQV 441
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517055036 364 ------VVGEEHYEVARKVQSTLQRYKALQDIIAILGMDELSEEDKVAVARARKI-ERFLSQ 418
Cdd:PRK04192 442 apwweeNVDPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQ 503
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
12-278 |
3.98e-18 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 86.66 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 12 VGRVTQVIGAVVDV-----AFEGELpkilnaLETSNNgnrlVLEIAQHLGENVVRTIAMDSTDGLVRGQEVTDTGSPIMV 86
Cdd:PRK09281 28 VGTVISVGDGIARVygldnVMAGEL------LEFPGG----VYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 87 PVGNETLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTV 166
Cdd:PRK09281 98 PVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 167 LIMELINNvAKAHGGYSVFAGVGERtregndlyhemiESNVnkhgggegskAALV-----YGQM----------NEPPGA 231
Cdd:PRK09281 178 IAIDTIIN-QKGKDVICIYVAIGQK------------ASTV----------AQVVrkleeHGAMeytivvaataSDPAPL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 517055036 232 RARVALTGLTVAEHFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIP 278
Cdd:PRK09281 235 QYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPP 281
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
86-278 |
8.27e-18 |
|
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: 83.38 E-value: 8.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 86 VPVGNETLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKT 165
Cdd:cd01132 4 VPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 166 VLIMELINNvAKAHGGYSVFAGVGERTREGNDLYHEMIESNVNKHgggegskAALVYGQMNEPPGARARVALTGLTVAEH 245
Cdd:cd01132 84 AIAIDTIIN-QKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEY-------TIVVAATASDPAPLQYLAPYAGCAMGEY 155
|
170 180 190
....*....|....*....|....*....|...
gi 517055036 246 FRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIP 278
Cdd:cd01132 156 FRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPP 188
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
15-81 |
9.28e-18 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 77.20 E-value: 9.28e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517055036 15 VTQVIGAVVDVAF-EGELPKILNALETS-NNGNRLVLEIAQHLGENVVRTIAMDSTDGLVRGQEVTDTG 81
Cdd:pfam02874 1 IVQVIGPVVDVEFgIGRLPGLLNALEVElVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
48-418 |
2.83e-16 |
|
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: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 48 VLEIAQHlgENVVRTiaMDSTDGL-VRGQEVTDTGSPIMVPVGNETLGRIMNVIGEPVDEaGPLVTAHK------RSIHQ 120
Cdd:TIGR01040 41 VLEVSGN--KAVVQV--FEGTSGIdAKKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDK-GPPVLAEDyldingQPINP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 121 DAPTYVEQsteaqILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNV-------AKAHGGYS-----VFAGV 188
Cdd:TIGR01040 116 YARIYPEE-----MIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAglvklptKDVHDGHEdnfaiVFAAM 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 189 GERTrEGNDLYHEMIESNvnkhggGEGSKAALVYGQMNEPPGARARVALTGLTVAEHFRDQ-GQDVLFFVDNIFRFTQAG 267
Cdd:TIGR01040 191 GVNM-ETARFFKQDFEEN------GSMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADAL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 268 SEVSALLGRIPSAVGYQPTLATDMGQMQERITTTTTGSITSVQ--AIYVPADDLTDPAPATSFAHLDATTVLSRSIAEKG 345
Cdd:TIGR01040 264 REVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQipILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQ 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517055036 346 IYPAVDPLDSTSRMLDPlVVGE-----EHYEVARKVQSTLQRYKALQDIIAILGMDELSEEDKVAVARARKIER-FLSQ 418
Cdd:TIGR01040 344 IYPPINVLPSLSRLMKS-AIGEgmtrkDHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQ 421
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
14-414 |
1.16e-14 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 75.84 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 14 RVTQVIGAVVDVAFEG----ELpkilnALETSNNGNRLvleiAQ--HLGENVVRTIAMDSTDGLVRGQEVTDTGSPIMVP 87
Cdd:PRK02118 7 KITDITGNVITVEAEGvgygEL-----ATVERKDGSSL----AQviRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 88 VGNETLGRIMNVIGEPVDeAGPLVTAHKRSIHQDAPTYVEQSTEAQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVL 167
Cdd:PRK02118 78 YSESLLGRRFNGSGKPID-GGPELEGEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 168 IMELinnVAKAHGGYSVFAGVGERtregNDLYHEMIESNVNkhgGGEGSKAALVYGQMNEPPGARARVALTGLTVAEHFR 247
Cdd:PRK02118 157 LARI---ALQAEADIIILGGMGLT----FDDYLFFKDTFEN---AGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 248 -DQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERITTTTTGSITSVQAI-YVPADDLTDPAPa 325
Cdd:PRK02118 227 lEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEDGGSITIIAVtTMPGDDVTHPVP- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 326 tsfahlDATTVlsrsIAEKGIY---PAVDPLDSTSRmLDPLVVGEEHYEVARKVQSTLQR-YKALQDIIAILGMD-ELSE 400
Cdd:PRK02118 306 ------DNTGY----ITEGQFYlrrGRIDPFGSLSR-LKQLVIGKKTREDHGDLMNAMIRlYADSREAKEKMAMGfKLSN 374
|
410
....*....|....
gi 517055036 401 EDKVAVARARKIER 414
Cdd:PRK02118 375 WDEKLLKFSELFES 388
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
51-278 |
3.95e-12 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 68.07 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 51 IAQHLGENVVRTIAMDSTDGLVRGQEVTDTGSPIMVPVGNETLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPTYVEQST 130
Cdd:CHL00059 41 IALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 131 EAQILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNvAKAHGGYSVFAGVGERT----------REGNDL-Y 199
Cdd:CHL00059 121 VYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN-QKGQNVICVYVAIGQKAssvaqvvttlQERGAMeY 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 200 HEMIESNVNkhgggegSKAALVYgqmneppgararVA-LTGLTVAEHFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIP 278
Cdd:CHL00059 200 TIVVAETAD-------SPATLQY------------LApYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPP 260
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
63-283 |
2.43e-11 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 65.83 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 63 IAMDSTDGLVRGQEVTDTGSPIMVPVGNETLGRIMNVIGEPVDEAgpLVTAHKRSIHQD---------APTYVEQSTEAQ 133
Cdd:PTZ00185 94 ILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPVG--LLTRSRALLESEqtlgkvdagAPNIVSRSPVNY 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 134 ILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINN-------VAKAHGGYSVFAGVGERTREGNDLyHEMIESN 206
Cdd:PTZ00185 172 NLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINqvrinqqILSKNAVISIYVSIGQRCSNVARI-HRLLRSY 250
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517055036 207 vnkhggGEGSKAALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGY 283
Cdd:PTZ00185 251 ------GALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAY 321
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
150-276 |
1.76e-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: 44.67 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 150 RGGKIGLFGGAGVGKTVLIMELINNVAKAHGGysVFAGVGERTREGNDLYHEMIESNVNKHGGGegskaalvygqmnepP 229
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG--VIYIDGEDILEEVLDQLLLIIVGGKKASGS---------------G 63
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 517055036 230 GARARVALTGLtvaehfRDQGQDVLFFvDNIFRFTQAGSEVSALLGR 276
Cdd:smart00382 64 ELRLRLALALA------RKLKPDVLIL-DEITSLLDAEQEALLLLLE 103
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
70-401 |
2.10e-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: 46.60 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 70 GLVRGQEVTDTgspIMVPVGNE---TLGRIMNVIGEPVDEAgplvtahKRSIHQDA--PTYVEQ----STEAQILVTgiK 140
Cdd:TIGR00767 90 NLRTGDTIEGQ---IRSPKEGEryfALLKVESVNGDDPEKA-------KNRVLFENltPLYPNErlrlETSTEDLST--R 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 141 VVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNVAKAHGG-YSVFAGVGERTREGNDlyheMIESnvnkhgggegSKAA 219
Cdd:TIGR00767 158 VLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEvELIVLLIDERPEEVTD----MQRS----------VKGE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 220 LVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAvGYQPTlatdmgqmqerit 299
Cdd:TIGR00767 224 VVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKVLSG-GVDAN------------- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 300 ttttgsitsvqAIYVP------------ADDLTDPAPA----------TSFAHLDAT----TVLSRSIAEKGIYPAVDPL 353
Cdd:TIGR00767 290 -----------ALHRPkrffgaarnieeGGSLTIIATAlidtgsrmdeVIFEEFKGTgnmeLHLDRKLADRRIFPAIDIK 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 517055036 354 DSTSRMlDPLVVGEEHYE---VARKVQSTLQRYKALQDIIAILGMDELSEE 401
Cdd:TIGR00767 359 KSGTRK-EELLLTPEELQkiwVLRKIISPMDSIEAMEFLISKLKKTKTNEE 408
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
140-400 |
1.04e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 44.31 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 140 KVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAG-VGERTREGNDLyhemiesnvnkhgggEGSKA 218
Cdd:PRK12608 122 RVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDM---------------RRSVK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 219 ALVYGQMN-EPPGARARVALTGLTVAEHFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAvgyqptlATDMGQMQ-E 296
Cdd:PRK12608 187 GEVYASTFdRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAYNNEVESSGRTLSG-------GVDARALQrP 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 297 RITTTTTGSITSVQAIYVPADDLTDP---APATSFAHLDAT----TVLSRSIAEKGIYPAVDPLDSTSRMLDPLVVGEEH 369
Cdd:PRK12608 260 KRLFGAARNIEEGGSLTIIATALVDTgsrMDEVIFEEFKGTgnmeIVLDRELADKRVFPAIDIAKSGTRREELLLDSKEL 339
|
250 260 270
....*....|....*....|....*....|.
gi 517055036 370 YEVARkvqstLQRykALQDIIAILGMDELSE 400
Cdd:PRK12608 340 EKVRR-----LRR--ALASRKPVEAMEALLE 363
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
13-82 |
6.65e-04 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 38.06 E-value: 6.65e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517055036 13 GRVTQVIGAVVDVAFEGELPK--ILNaLETSNNGNRLVL--EIAQHLGENVVrTIAMDSTDGLVRGQEVTDTGS 82
Cdd:cd01426 2 GRVIRVNGPLVEAELEGEVAIgeVCE-IERGDGNNETVLkaEVIGFRGDRAI-LQLFESTRGLSRGALVEPTGR 73
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
84-222 |
9.54e-04 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 41.93 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 84 IMVPVGNE------------TLGRIMNVIGEPVDEAGPLVTAHKRSIHQDAPtYVEQSTEAQILVTGIKVVDLLAPYARG 151
Cdd:PRK14698 149 IMVPPGIEgeiveiadegeyTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRP-YKEKLPPEVPLITGQRVIDTFFPQAKG 227
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517055036 152 GKIGLFGGAGVGKTV----LIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMiESNVNKHGGGEGS----KAALVY 222
Cdd:PRK14698 228 GTAAIPGPFGSGKCVdgdtLILTKEFGLIKIKDLYEILDGKGKKTVEGNEEWTEL-EEPITLYGYKDGKiveiKATHVY 305
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
365-419 |
1.07e-03 |
|
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family of ATPases that form part of the Type III secretion system (T3SS) present in Escherichia coli. T3SS is a macromolecular complex that creates a syringe-like apparatus extending from the bacterial cytosol across three membranes to the eukaryotic cytosol. This process is essential for pathogenicity. EscN is a functionally unique ATPase that provides an inner-membrane recognition gate for the T3SS chaperone-virulence effector complexes as well as a potential source of energy for their subsequent secretion.The C-terminal domain of T3SS ATPases mediates binding with multiple contact points along the chaperone.
Pssm-ID: 465691 [Multi-domain] Cd Length: 70 Bit Score: 37.41 E-value: 1.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 517055036 365 VGEEHYEVARKVQSTLQRYKALQDIIAI----LGMDelSEEDKvAVARARKIERFLSQP 419
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIgayqAGSD--PEIDE-AIAKRPAINAFLRQG 56
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
140-381 |
1.99e-03 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 39.88 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 140 KVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAG-VGERTREGNDlyheMIESnvnkhgggegSKA 218
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRS----------VKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 219 ALVYGQMNEPPGARARVALTGLTVAEHFRDQGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAvGYQPTlatdmgqmqeri 298
Cdd:cd01128 71 EVVASTFDEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSG-GVDAN------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055036 299 tttttgsitsvqAIYVPAD------------DLTDPAPA---TS-------FAHLDAT----TVLSRSIAEKGIYPAVDP 352
Cdd:cd01128 138 ------------ALHKPKRffgaarnieeggSLTIIATAlvdTGsrmdeviFEEFKGTgnmeLVLDRKLAEKRIFPAIDI 205
|
250 260
....*....|....*....|....*....
gi 517055036 353 LDSTSRMlDPLVVGEEHYEVARKVQSTLQ 381
Cdd:cd01128 206 LKSGTRK-EELLLTPEELQKIWLLRRILS 233
|
|
| |
