|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
38-504 |
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: 984.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 38 GKIVAVIGAVVDVQFD-DNLPPILNALEVDN-RSPRLVLEVAQHLGENTVRTIAMDGTEGLVRGQKVLDTGYPIRIPVGA 115
Cdd:COG0055 6 GKIVQVIGPVVDVEFPeGELPAIYNALEVENeGGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 116 ETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME 195
Cdd:COG0055 86 ATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIME 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 196 LINNVAKAHGGYSVFAGVGERTREGNDLYNEMIEGGVISlkdktsKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG 275
Cdd:COG0055 166 LIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD------KTALVFGQMNEPPGARLRVALTALTMAEYFRDEEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 276 QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH 355
Cdd:COG0055 240 QDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 356 LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIIGQEHYNVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVARAR 435
Cdd:COG0055 320 LDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARAR 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665388824 436 KIQRFLSQPFQVAEVFTGHAGKLVPLEQTIKGFSAILAGDYDHLPEVAFYMVGPIEEVVEKADRLAKEA 504
Cdd:COG0055 400 KIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAEA 468
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
38-500 |
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: 869.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 38 GKIVAVIGAVVDVQF-DDNLPPILNALEVDNR-SPRLVLEVAQHLGENTVRTIAMDGTEGLVRGQKVLDTGYPIRIPVGA 115
Cdd:TIGR01039 3 GKVVQVIGPVVDVEFeQGELPRIYNALKVQNRaESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 116 ETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME 195
Cdd:TIGR01039 83 ETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 196 LINNVAKAHGGYSVFAGVGERTREGNDLYNEMIEGGVISlkdktsKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG 275
Cdd:TIGR01039 163 LINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID------KTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 276 QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH 355
Cdd:TIGR01039 237 QDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 356 LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIIGQEHYNVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVARAR 435
Cdd:TIGR01039 317 LDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERAR 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665388824 436 KIQRFLSQPFQVAEVFTGHAGKLVPLEQTIKGFSAILAGDYDHLPEVAFYMVGPIEEVVEKADRL 500
Cdd:TIGR01039 397 RIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
38-505 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 832.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 38 GKIVAVIGAVVDVQF-DDNLPPILNALEVDNRSP-----RLVLEVAQHLGENTVRTIAMDGTEGLVRGQKVLDTGYPIRI 111
Cdd:CHL00060 17 GRITQIIGPVLDVAFpPGKMPNIYNALVVKGRDTagqeiNVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 112 PVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTV 191
Cdd:CHL00060 97 PVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 192 LIMELINNVAKAHGGYSVFAGVGERTREGNDLYNEMIEGGVISLKD-KTSKVALVYGQMNEPPGARARVALTGLTVAEYF 270
Cdd:CHL00060 177 LIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNiAESKVALVYGQMNEPPGARMRVGLTALTMAEYF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 271 RDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTKKGSITSVQAIYVPADDLTDPAPA 350
Cdd:CHL00060 257 RDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 351 TTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIIGQEHYNVARGVQKILQDYKSLQDIIAILGMDELSEEDKLT 430
Cdd:CHL00060 337 TTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLT 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665388824 431 VARARKIQRFLSQPFQVAEVFTGHAGKLVPLEQTIKGFSAILAGDYDHLPEVAFYMVGPIEEVVEKADRLAKEAA 505
Cdd:CHL00060 417 VARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANLEVESK 491
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
110-387 |
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: 610.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 110 RIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGK 189
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 190 TVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYNEMIEGGVISLKDKtSKVALVYGQMNEPPGARARVALTGLTVAEY 269
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDGL-SKVALVYGQMNEPPGARARVALTGLTMAEY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 270 FRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTKKGSITSVQAIYVPADDLTDPAP 349
Cdd:cd01133 160 FRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAP 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 665388824 350 ATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDP 387
Cdd:cd01133 240 ATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
38-492 |
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: 579.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 38 GKIVAVIGAVVDVQFDDNLPPILNALEVdNRSPRLVLEVAQHLGENTVRTIAMDGTEGLVRGQKVLDTGYPIRIPVGAET 117
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDGELPAIHSVLRA-GREGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 118 LGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELI 197
Cdd:TIGR03305 80 LSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 198 NNVAKAHGGYSVFAGVGERTREGNDLYNEMIEGGVIslkDKTskvALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQD 277
Cdd:TIGR03305 160 HNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVL---DNT---VMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 278 VLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLD 357
Cdd:TIGR03305 234 VLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 358 ATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIIGQEHYNVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVARARKI 437
Cdd:TIGR03305 314 ASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 665388824 438 QRFLSQPFQVAEVFTGHAGKLVPLEQTIKGFSAILAGDYDHLPEVAFYMVGPIEE 492
Cdd:TIGR03305 394 ERFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDE 448
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
110-384 |
8.19e-139 |
|
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: 401.06 E-value: 8.19e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 110 RIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGK 189
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 190 TVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYNEMIEGGVislkdkTSKVALVYGQMNEPPGARARVALTGLTVAEY 269
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGA------MERTVVVANTANDPPGARMRVPYTGLTIAEY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 270 FRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTK--KGSITSVQAIYVPADDLTDP 347
Cdd:cd19476 155 FRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDP 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 665388824 348 APATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRI 384
Cdd:cd19476 234 IPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
163-382 |
9.40e-94 |
|
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: 283.48 E-value: 9.40e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 163 GIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKahgGYSVFAGVGERTREGNDLYNEMIEGGVISlkdktsKV 242
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALK------RT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 243 ALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQER 322
Cdd:pfam00006 72 VVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665388824 323 ITTT--KKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTS 382
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 ... |
389-496 |
6.40e-76 |
|
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: 233.91 E-value: 6.40e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 389 IIGQEHYNVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFQVAEVFTGHAGKLVPLEQTIKGF 468
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 665388824 469 SAILAGDYDHLPEVAFYMVGPIEEVVEK 496
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
38-472 |
6.40e-66 |
|
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: 219.13 E-value: 6.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 38 GKIVAVIGAVVDVQfddnLP--PILNALEVDNRSPRLVL-EVaqhLG--ENTVRTIAMDGTEGLVRGQKVLDTGYPIRIP 112
Cdd:COG1157 21 GRVTRVVGLLIEAV----GPdaSIGELCEIETADGRPVLaEV---VGfrGDRVLLMPLGDLEGISPGARVVPTGRPLSVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 113 VGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVL 192
Cdd:COG1157 94 VGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 193 IMELINNvAKAHggYSVFAGVGERTREgndlYNEMIEggvislKDKT----SKVALVYGQMNEPPGARARVALTGLTVAE 268
Cdd:COG1157 174 LGMIARN-TEAD--VNVIALIGERGRE----VREFIE------DDLGeeglARSVVVVATSDEPPLMRLRAAYTATAIAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 269 YFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTKKGSITsvqAIY---VPADDLT 345
Cdd:COG1157 241 YFRDQ-GKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSIT---AFYtvlVEGDDMN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 346 DPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIIGQEHYNVARGVQKILQDYKSLQDIIAI----LGMD 421
Cdd:COG1157 317 DPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM-PDIVSPEHRALARRLRRLLARYEENEDLIRIgayqPGSD 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 665388824 422 ELSEEdklTVARARKIQRFLSQPfqVAEVftghagklVPLEQTIKGFSAIL 472
Cdd:COG1157 396 PELDE---AIALIPAIEAFLRQG--MDER--------VSFEESLAQLAELL 433
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
110-384 |
1.19e-60 |
|
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: 200.09 E-value: 1.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 110 RIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGK 189
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 190 TVLIMELINNVAKAhggYSVFAGVGERTREgndlYNEMIEGgvISLKDKTSKVALVYGQMNEPPGARARVALTGLTVAEY 269
Cdd:cd01136 81 STLLGMIARNTDAD---VNVIALIGERGRE----VREFIEK--DLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 270 FRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTKKGSITSVQAIYVPADDLTDPAP 349
Cdd:cd01136 152 FRDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIA 230
|
250 260 270
....*....|....*....|....*....|....*
gi 665388824 350 ATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRI 384
Cdd:cd01136 231 DEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
94-473 |
4.63e-58 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 198.37 E-value: 4.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 94 EGLVRGQKVLDTGYPIRIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPY 173
Cdd:PRK08472 75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTC 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 174 AKGGKIGLFGGAGVGKTVLiMELINNVAKAHggYSVFAGVGERTREgndlYNEMIEGgviSLKDKTSKVALVYGQMNEPP 253
Cdd:PRK08472 155 GKGQKLGIFAGSGVGKSTL-MGMIVKGCLAP--IKVVALIGERGRE----IPEFIEK---NLGGDLENTVIVVATSDDSP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 254 GARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTK-KGSIT 332
Cdd:PRK08472 225 LMRKYGAFCAMSVAEYFKNQ-GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSIT 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 333 SVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDpNIIGQEHYNVARGVQKILQDYKSLQ 412
Cdd:PRK08472 304 AFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENE 382
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665388824 413 DIIAI----LGMD-ELSEedklTVARARKIQRFLSQPFQvaevftghagKLVPLEQTIKGFSAILA 473
Cdd:PRK08472 383 VLIRIgayqKGNDkELDE----AISKKEFMEQFLKQNPN----------ELFPFEQTFEQLEEILR 434
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
91-443 |
1.38e-53 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 186.94 E-value: 1.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 91 DGTEGLVRGQKVLDTGYPIRIPVGAETLGRIINVIGEPIDErGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLL 170
Cdd:PRK06820 79 ASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 171 APYAKGGKIGLFGGAGVGKTVLIMELinnVAKAHGGYSVFAGVGERTREgndlYNEMIEGgVISLKDKTSKVALVyGQMN 250
Cdd:PRK06820 158 LSCGEGQRIGIFAAAGVGKSTLLGML---CADSAADVMVLALIGERGRE----VREFLEQ-VLTPEARARTVVVV-ATSD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 251 EPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTKKGS 330
Cdd:PRK06820 229 RPALERLKGLSTATTIAEYFRDR-GKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGS 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 331 ITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIIGQEHYNVARGVQKILQDYKS 410
Cdd:PRK06820 308 ITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQE 386
|
330 340 350
....*....|....*....|....*....|....*..
gi 665388824 411 LQDIIAI----LGMDELSEEdklTVARARKIQRFLSQ 443
Cdd:PRK06820 387 IELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
99-386 |
2.31e-52 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 183.66 E-value: 2.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 99 GQKVLDTGyPIRIPVGAETLGRIINVIGEPIDERGPIDT-DKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPYAKGG 177
Cdd:PRK06002 88 GDAVFRKG-PLRIRPDPSWKGRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQ 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 178 KIGLFGGAGVGKTVLIMELinnvAKAHGGYSV-FAGVGERTREgndlYNEMIEGgviSLKDKTSKVALVYGQMNEPPGAR 256
Cdd:PRK06002 167 RIGIFAGSGVGKSTLLAML----ARADAFDTVvIALVGERGRE----VREFLED---TLADNLKKAVAVVATSDESPMMR 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 257 ARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERI--TTTKKGSITSV 334
Cdd:PRK06002 236 RLAPLTATAIAEYFRDR-GENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGI 314
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 665388824 335 QAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMD 386
Cdd:PRK06002 315 FSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLAR 366
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
95-417 |
6.59e-51 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 179.51 E-value: 6.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 95 GLVRGQKVLDTGYPIRIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPYA 174
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 175 KGGKIGLFGGAGVGKTVLI-MELINNVAKAhggySVFAGVGERTREgndlYNEMIEGgvISLKDKTSKVALVYGQMNEPP 253
Cdd:PRK08972 161 KGQRMGLFAGSGVGKSVLLgMMTRGTTADV----IVVGLVGERGRE----VKEFIEE--ILGEEGRARSVVVAAPADTSP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 254 GARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITT--TKKGSI 331
Cdd:PRK08972 231 LMRLKGCETATTIAEYFRDQ-GLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNggPGQGSI 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 332 TSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIIGQEHYNVARGVQKILQDYKSL 411
Cdd:PRK08972 310 TAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQN 388
|
....*.
gi 665388824 412 QDIIAI 417
Cdd:PRK08972 389 RDLISI 394
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
38-444 |
9.87e-51 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 179.19 E-value: 9.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 38 GKIVAVIGAVVDVQ-FDDNLPPILNALEVDNRsprlVLEVAQHLG-ENTVRTIAMDGT-EGLVRGQKVLDTGYPIRIPVG 114
Cdd:PRK09099 26 GKVVEVIGTLLRVSgLDVTLGELCELRQRDGT----LLQRAEVVGfSRDVALLSPFGElGGLSRGTRVIGLGRPLSVPVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 115 AETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIM 194
Cdd:PRK09099 102 PALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 195 ELINNvakAHGGYSVFAGVGERTREGNDlYNEMIEGgvislKDKTSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQe 274
Cdd:PRK09099 182 MFARG---TQCDVNVIALIGERGREVRE-FIELILG-----EDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDR- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 275 GQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFA 354
Cdd:PRK09099 252 GLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVRG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 355 HLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIIGQEHYNVARGVQKILQDYKSLQDIIAI----LGMDELSEEdklT 430
Cdd:PRK09099 332 ILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVADE---A 407
|
410
....*....|....
gi 665388824 431 VARARKIQRFLSQP 444
Cdd:PRK09099 408 IAKIDAIRDFLSQR 421
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
94-443 |
7.54e-49 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 174.17 E-value: 7.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 94 EGLVRGQKVLDTGYPIRIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPY 173
Cdd:PRK06936 80 YGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 174 AKGGKIGLFGGAGVGKTVLIMELINNvakAHGGYSVFAGVGERTREgndlYNEMIEG--GVISLKdktsKVALVYGQMNE 251
Cdd:PRK06936 160 GEGQRMGIFAAAGGGKSTLLASLIRS---AEVDVTVLALIGERGRE----VREFIESdlGEEGLR----KAVLVVATSDR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 252 PPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTKKGSI 331
Cdd:PRK06936 229 PSMERAKAGFVATSIAEYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 332 TSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDpNIIGQEHYNVARGVQKILQDYKSL 411
Cdd:PRK06936 308 TALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEV 386
|
330 340 350
....*....|....*....|....*....|....*.
gi 665388824 412 QDIIAI----LGMDELSEEdklTVARARKIQRFLSQ 443
Cdd:PRK06936 387 ELLLQIgeyqKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
99-417 |
1.16e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 170.67 E-value: 1.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 99 GQKVLDTGYPIRIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPYAKGGK 178
Cdd:PRK07721 81 GCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 179 IGLFGGAGVGKTVLiMELINNVAKAHggYSVFAGVGERTREgndlYNEMIEG--GVISLKdktsKVALVYGQMNEPPGAR 256
Cdd:PRK07721 161 VGIFAGSGVGKSTL-MGMIARNTSAD--LNVIALIGERGRE----VREFIERdlGPEGLK----RSIVVVATSDQPALMR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 257 ARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTKKGSITSVQA 336
Cdd:PRK07721 230 IKGAYTATAIAEYFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 337 IYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIIGQEHYNVARGVQKILQDYKSLQDIIA 416
Cdd:PRK07721 309 VLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLIN 387
|
.
gi 665388824 417 I 417
Cdd:PRK07721 388 I 388
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
93-417 |
3.14e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 161.27 E-value: 3.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 93 TEGLVRGQKVLDTGYPIRIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEiLVTGIKVVDLLAP 172
Cdd:PRK07594 73 TIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRELPDVCWKDYDAMPPPAMVRQPITQP-LMTGIRAIDSVAT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 173 YAKGGKIGLFGGAGVGKTVLIMELINnvaKAHGGYSVFAGVGERTREgndlYNEMIEggvISLKDKTSK-VALVYGQMNE 251
Cdd:PRK07594 152 CGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGRE----VREFID---FTLSEETRKrCVIVVATSDR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 252 PPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTKKGSI 331
Cdd:PRK07594 222 PALERVRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSI 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 332 TSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIIGQEHYNVARGVQKILQDYKSL 411
Cdd:PRK07594 301 TAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEV 379
|
....*.
gi 665388824 412 QDIIAI 417
Cdd:PRK07594 380 ELLIRI 385
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
93-443 |
5.04e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 160.91 E-value: 5.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 93 TEGLVRGQKVLDTGYPIRIPVGAETLGRIINVIGEPIDErgPIDTDKTAAIHAEAPEFVQMSVEQ--EILVTGIKVVDLL 170
Cdd:PRK06793 73 TEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIHAFEREEitDVFETGIKSIDSM 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 171 APYAKGGKIGLFGGAGVGKTVLIMELINNvAKAHggYSVFAGVGERTREGND-LYNEMIEGGVislkdktSKVALVYGQM 249
Cdd:PRK06793 151 LTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKAD--INVISLVGERGREVKDfIRKELGEEGM-------RKSVVVVATS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 250 NEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAvGYQPTLATDMGSMQERITTTKKG 329
Cdd:PRK06793 221 DESHLMQLRAAKLATSIAEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQKG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 330 SITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDpNIIGQEHYNVARGVQKILQDYK 409
Cdd:PRK06793 299 SITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPNHWQLANEMRKILSIYK 377
|
330 340 350
....*....|....*....|....*....|....*..
gi 665388824 410 SlQDIIAILGMDELSEEDKLTVARARK---IQRFLSQ 443
Cdd:PRK06793 378 E-NELYFKLGTIQENAENAYIFECKNKvegINTFLKQ 413
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
73-473 |
1.82e-43 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 159.00 E-value: 1.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 73 VLEVAQHLGENTVRTI--AMDGTEGLVRGQKVLDTGYPIRIPVGAETLGRIINVIGEPIDERGPIDTDKTA----AIHAE 146
Cdd:PRK08149 42 VIARAQVVGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTVGPIseerVIDVA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 147 APEFVQMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvakAHGGYSVFAGVGERTREgndlYNE 226
Cdd:PRK08149 122 PPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGERGRE----VTE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 227 MIEggviSLK--DKTSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPS 304
Cdd:PRK08149 195 FVE----SLRasSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQ-GKRVVLFIDSMTRYARALRDVALAAGELPA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 305 AVGYQPTLATDMGSMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRI 384
Cdd:PRK08149 270 RRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 385 MDpNIIGQEHYNVARGVQKILQDYKSLQDIIAiLGMDELSE--EDKLTVARARKIQRFLSQPFQVAEVFtghagklvplE 462
Cdd:PRK08149 350 FG-QVTDPKHRQLAAAFRKLLTRLEELQLFID-LGEYRRGEnaDNDRAMDKRPALEAFLKQDVAEKSSF----------S 417
|
410
....*....|.
gi 665388824 463 QTIKGFSAILA 473
Cdd:PRK08149 418 DTLERLNEFAA 428
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
94-443 |
1.08e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 157.58 E-value: 1.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 94 EGLVRGQKVLDTGYPIRIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPY 173
Cdd:PRK05688 86 AGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTV 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 174 AKGGKIGLFGGAGVGKTVLiMELINNVAKAHggYSVFAGVGERTREGNDLYNEMIegGVISLKdktsKVALVYGQMNEPP 253
Cdd:PRK05688 166 GRGQRLGLFAGTGVGKSVL-LGMMTRFTEAD--IIVVGLIGERGREVKEFIEHIL--GEEGLK----RSVVVASPADDAP 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 254 GARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTKKG--SI 331
Cdd:PRK05688 237 LMRLRAAMYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGggSI 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 332 TSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIIGQEHYNVARGVQKILQDYKSL 411
Cdd:PRK05688 316 TAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQQS 394
|
330 340 350
....*....|....*....|....*....|....*.
gi 665388824 412 QDIIAI----LGMDelsEEDKLTVARARKIQRFLSQ 443
Cdd:PRK05688 395 RDLISVgayvAGGD---PETDLAIARFPHLVQFLRQ 427
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
38-417 |
2.31e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 156.29 E-value: 2.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 38 GKIVAVIGAVVDVQFDDNLPPILNALEVDNRSPRLVL-EVaqhLGENTVRTIAM--DGTEGLVRGQKVLDTGYPIRIPVG 114
Cdd:PRK08927 19 GRVVAVRGLLVEVAGPIHALSVGARIVVETRGGRPVPcEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAVRPS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 115 AETLGRIINVIGEPIDERGPIDTDKTA-AIHAEAPEFVQMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLI 193
Cdd:PRK08927 96 RAWLGRVVNALGEPIDGKGPLPQGPVPyPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 194 MELINNVAKAhggYSVFAGVGERTREgndlYNEMIEG--GVISLKdktsKVALVYGQMNEPPGARARVALTGLTVAEYFR 271
Cdd:PRK08927 176 SMLARNADAD---VSVIGLIGERGRE----VQEFLQDdlGPEGLA----RSVVVVATSDEPALMRRQAAYLTLAIAEYFR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 272 DQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERIT--TTKKGSITSVQAIYVPADDLTDPAP 349
Cdd:PRK08927 245 DQ-GKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGpgPIGEGTITGLFTVLVDGDDHNEPVA 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665388824 350 ATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIIGQEHYNVARGVQKILQDYKSLQDIIAI 417
Cdd:PRK08927 324 DAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
95-443 |
6.20e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 149.66 E-value: 6.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 95 GLVRGQKVLDTGYPIRIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPYA 174
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 175 KGGKIGLFGGAGVGKTVLiMELINNVAKAHggYSVFAGVGERTREgndlYNEMIEGGVISlkDKTSKVALVYGQMNEPPG 254
Cdd:PRK07196 154 KGQRVGLMAGSGVGKSVL-LGMITRYTQAD--VVVVGLIGERGRE----VKEFIEHSLQA--AGMAKSVVVAAPADESPL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 255 ARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTK-KGSITS 333
Cdd:PRK07196 225 MRIKATELCHAIATYYRDK-GHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSgNGTMTA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 334 VQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDpNIIGQEHYNVARGVQKILQDYKSLQD 413
Cdd:PRK07196 304 IYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMAIKP 382
|
330 340 350
....*....|....*....|....*....|....
gi 665388824 414 IIA----ILGMDELSEEdklTVARARKIQRFLSQ 443
Cdd:PRK07196 383 LIPlggyVAGADPMADQ---AVHYYPAITQFLRQ 413
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
92-445 |
1.51e-37 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 143.43 E-value: 1.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 92 GTEGL-VRGQKVLDTGYPIRIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLL 170
Cdd:PRK04196 58 GTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 171 APYAKGGKIGLFGGAGVGKTVLIMELINNvAKAHGGYS----VFAGVGERTREGNDLYNEMIEGGVIslkdktSKVALVY 246
Cdd:PRK04196 138 NTLVRGQKLPIFSGSGLPHNELAAQIARQ-AKVLGEEEnfavVFAAMGITFEEANFFMEDFEETGAL------ERSVVFL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 247 GQMNEPPGAR---ARVAltgLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQER- 322
Cdd:PRK04196 211 NLADDPAIERiltPRMA---LTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERa 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 323 -ITTTKKGSITSVQAIYVPADDLTDPAPattfahlDAT-------TVLSRAIAELGIYPAVDPLDSTSRIMDpNIIG--- 391
Cdd:PRK04196 288 gRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyitegqIVLSRELHRKGIYPPIDVLPSLSRLMK-DGIGegk 359
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665388824 392 --QEHYNV--------ARGVQkilqdyksLQDIIAILGMDELSEEDKLTVARARKI-QRFLSQPF 445
Cdd:PRK04196 360 trEDHKDVanqlyaayARGKD--------LRELAAIVGEEALSERDRKYLKFADAFeREFVNQGF 416
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
108-391 |
4.33e-36 |
|
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: 135.43 E-value: 4.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 108 PIRIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGV 187
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 188 GKTVLIMELINNvAKAHGGYS----VFAGVGERTREGNDLYNEMIEGGVISlkdktsKVALVYGQMNEPPGARARVALTG 263
Cdd:cd01135 81 PHNELAAQIARQ-AGVVGSEEnfaiVFAAMGVTMEEARFFKDDFEETGALE------RVVLFLNLANDPTIERIITPRMA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 264 LTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQER--ITTTKKGSITSVQAIYVPA 341
Cdd:cd01135 154 LTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTMPN 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 665388824 342 DDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDpNIIG 391
Cdd:cd01135 234 DDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMK-SGIG 282
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
38-109 |
1.21e-35 |
|
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: 127.25 E-value: 1.21e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665388824 38 GKIVAVIGAVVDVQFD-DNLPPILNALEVDNRSP-RLVLEVAQHLGENTVRTIAMDGTEGLVRGQKVLDTGYPI 109
Cdd:cd18115 3 GKIVQVIGPVVDVEFPeGELPPIYNALEVKGDDGkKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
90-417 |
4.61e-34 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 133.76 E-value: 4.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 90 MDGTEGLVRGQKVLDTGYPI-------RIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVT 162
Cdd:PRK07960 82 LEEVEGILPGARVYARNISGeglqsgkQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 163 GIKVVDLLAPYAKGGKIGLFGGAGVGKTVlimeLINNVAKAHGGYSVFAG-VGERTREGNDlYNEMIEGgvislKDKTSK 241
Cdd:PRK07960 162 GVRAINALLTVGRGQRMGLFAGSGVGKSV----LLGMMARYTQADVIVVGlIGERGREVKD-FIENILG-----AEGRAR 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 242 VALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQE 321
Cdd:PRK07960 232 SVVIAAPADVSPLLRMQGAAYATRIAEDFRDR-GQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 322 RITT--TKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIIGQEHYNVAR 399
Cdd:PRK07960 311 RAGNgiSGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAM-TALIDEQHYARVR 389
|
330
....*....|....*...
gi 665388824 400 GVQKILQDYKSLQDIIAI 417
Cdd:PRK07960 390 QFKQLLSSFQRNRDLVSV 407
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
68-445 |
2.04e-29 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 120.01 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 68 RSPRLVLEVAQHLGENTVrTIAMDGTEGLVRGQKVLDTGYPIRIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEA 147
Cdd:PRK05922 50 KSPPILAEVIGFHNRTTL-LMSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 148 PEFVQMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTvlimELINNVAK-AHGGYSVFAGVGERTREGNDLYNE 226
Cdd:PRK05922 129 PSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVREYIEQ 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 227 MIEGgvislkDKTSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAV 306
Cdd:PRK05922 205 HKEG------LAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQ-GHRVLFIMDSLSRWIAALQEVALARGETLSAH 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 307 GYQPTLATDMGSMQERITTTKKGSITSVQAI-YVP--ADDLTDPAPATTFAHLDATTVlSRAIAElgiyPAVDPLDSTSR 383
Cdd:PRK05922 278 HYAASVFHHVSEFTERAGNNDKGSITALYAIlHYPnhPDIFTDYLKSLLDGHFFLTPQ-GKALAS----PPIDILTSLSR 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665388824 384 iMDPNIIGQEHYNVARGVQKILQDYKSLQDIIAiLGMDELSEEDKLTvaRARK----IQRFLSQPF 445
Cdd:PRK05922 353 -SARQLALPHHYAAAEELRSLLKAYHEALDIIQ-LGAYVPGQDAHLD--RAVKllpsIKQFLSQPL 414
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
73-473 |
7.41e-29 |
|
proton translocating ATP synthase, F1 alpha 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. The alpha-subunit contains a highly conserved adenine-specific noncatalytic nucleotide-binding domain. The conserved amino acid sequence is Gly-X-X-X-X-Gly-Lys. Proton translocating ATP synthase F1, alpha subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), B subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 273365 [Multi-domain] Cd Length: 501 Bit Score: 119.41 E-value: 7.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 73 VLEVAQHLGENTVRTIAMDGTEGLVRGQKVLDTGYPIRIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFV- 151
Cdd:TIGR00962 58 VQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIe 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 152 QMSVEQEiLVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKAHGGYSVFAGVGERTREGNDLYNEMIEGG 231
Cdd:TIGR00962 138 RKSVHEP-LQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTIIN-QKDSDVYCIYVAIGQKASTVAQVVRKLEEHG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 232 viSLKDKTskvaLVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPT 311
Cdd:TIGR00962 216 --AMAYTI----VVAATASDSASLQYLAPYTGCTMGEYFRDN-GKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGD 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 312 LATDMGSMQERITTTK----KGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRI--- 384
Cdd:TIGR00962 289 VFYLHSRLLERAAKLNdekgGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVgga 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 385 MDPNIIGQehynVARGVQKILQDYKSLqDIIAILGMDeLSEEDKLTVARARKIQRFLSQPF--------QVAEVFTGHAG 456
Cdd:TIGR00962 369 AQIKAMKQ----VAGSLRLELAQYREL-EAFSQFASD-LDEATKKQLERGQRVVELLKQPQykplsveeQVVILFAGTKG 442
|
410
....*....|....*....
gi 665388824 457 KL--VPLEQTIKGFSAILA 473
Cdd:TIGR00962 443 YLddIPVDKIRKFEQALLA 461
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
76-384 |
1.36e-28 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 118.48 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 76 VAQHLGENTVRTIAMDGTEGLVRGQKVLDTGYPIRIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSV 155
Cdd:PRK13343 62 FAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 156 EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKAHGGYSVFAGVGErtregndlynemieggvisl 235
Cdd:PRK13343 142 VTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN-QKDSDVICVYVAIGQ-------------------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 236 kdKTSKVALV------YGQM----------NEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALL 299
Cdd:PRK13343 201 --KASAVARVietlreHGALeyttvvvaeaSDPPGLQYLAPFAGCAIAEYFRDQ-GQDALIVYDDLSKHAAAYRELSLLL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 300 GRIPSAVGYQPTLATDMGSMQERITTTKK----GSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAV 375
Cdd:PRK13343 278 RRPPGREAYPGDIFYLHSRLLERAAKLSPelggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAV 357
|
....*....
gi 665388824 376 DPLDSTSRI 384
Cdd:PRK13343 358 DVGLSVSRV 366
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
158-383 |
9.80e-26 |
|
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: 106.50 E-value: 9.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 158 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinnvAKahggYS-----VFAGVGERTregndlyNEMIEggV 232
Cdd:cd01134 58 VPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSL----SK----WSnsdvvIYVGCGERG-------NEMAE--V 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 233 IS----LKDKTS------KVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRI 302
Cdd:cd01134 121 LEefpeLKDPITgeslmeRTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSLMADSTSRWAEALREISGRLEEM 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 303 PSAVGYQPTLATDMGSMQERI-------TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAV 375
Cdd:cd01134 200 PAEEGYPAYLGARLAEFYERAgrvrclgSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSI 279
|
....*...
gi 665388824 376 DPLDSTSR 383
Cdd:cd01134 280 NWLISYSK 287
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
158-443 |
3.92e-25 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 108.72 E-value: 3.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 158 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinnvAKahggYS-----VFAGVGERTregndlyNEMIEggV 232
Cdd:PRK04192 209 EPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQL----AK----WAdadivIYVGCGERG-------NEMTE--V 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 233 IS----LKD-KTSK-----VALVYGQMNEPPGAR-ARVaLTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGR 301
Cdd:PRK04192 272 LEefpeLIDpKTGRplmerTVLIANTSNMPVAAReASI-YTGITIAEYYRDM-GYDVLLMADSTSRWAEALREISGRLEE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 302 IPSAVGYQPTLATDMGSMQER---ITT--TKKGSITSVQAIYVPADDLTDPapaTTFAHLDATTV---LSRAIAELGIYP 373
Cdd:PRK04192 350 MPGEEGYPAYLASRLAEFYERagrVKTlgGEEGSVTIIGAVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADRRHFP 426
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665388824 374 AVDPLDSTSRIMDpnIIGQE-HYNVARG-------VQKILQDYKSLQDIIAILGMDELSEEDKLTVARARKI-QRFLSQ 443
Cdd:PRK04192 427 AINWLTSYSLYLD--QVAPWwEENVDPDwrelrdeAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQ 503
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
73-452 |
5.39e-24 |
|
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: 104.80 E-value: 5.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 73 VLEVAqhlGENTVRTIaMDGTEGL-VRGQKVLDTGYPIRIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFV 151
Cdd:TIGR01040 41 VLEVS---GNKAVVQV-FEGTSGIdAKKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 152 QMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNV-------AKAHGGYS-----VFAGVGERTRE 219
Cdd:TIGR01040 117 ARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAglvklptKDVHDGHEdnfaiVFAAMGVNMET 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 220 GNDLYNEMIEGGvislkdKTSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALL 299
Cdd:TIGR01040 197 ARFFKQDFEENG------SMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 300 GRIPSAVGYQPTLATDMGSMQERI--TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDP 377
Cdd:TIGR01040 271 EEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 378 LDSTSRIMDpNIIGQ-----EHYNVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVARARKIQR-FLSQ-PFQVAEV 450
Cdd:TIGR01040 351 LPSLSRLMK-SAIGEgmtrkDHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQgPYENRTI 429
|
..
gi 665388824 451 FT 452
Cdd:TIGR01040 430 FE 431
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
394-461 |
9.08e-23 |
|
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: 91.74 E-value: 9.08e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665388824 394 HYNVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFQVAEVFTGHAGKLVPL 461
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPI 68
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
111-384 |
2.22e-20 |
|
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: 91.08 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 111 IPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKT 190
Cdd:cd01132 4 VPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 191 VLIMELINNvAKAHGGYSVFAGVGERTREGNDLYNEMIEGGVIslkDKTSKVAlvyGQMNEPPGARARVALTGLTVAEYF 270
Cdd:cd01132 84 AIAIDTIIN-QKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAM---EYTIVVA---ATASDPAPLQYLAPYAGCAMGEYF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 271 RDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGY-------QPTLATDMGSMQERItttKKGSITSVQAIYVPADD 343
Cdd:cd01132 157 RDN-GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYpgdvfylHSRLLERAAKLSDEL---GGGSLTALPIIETQAGD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 665388824 344 LTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRI 384
Cdd:cd01132 233 VSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRV 273
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
39-352 |
9.76e-20 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 91.63 E-value: 9.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 39 KIVAVIGAVVDVQFDDnlpPILNALEVDNRSPRLVLEVAQHLGENTVRTIAMDGTEGLVRGQKVLDTGYPIRIPVGAETL 118
Cdd:PRK02118 7 KITDITGNVITVEAEG---VGYGELATVERKDGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 119 GRIINVIGEPIDeRGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELin 198
Cdd:PRK02118 84 GRRFNGSGKPID-GGPELEGEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLARI-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 199 nVAKAHGGYSVFAGVGERTREGNDLYNEMIEGGVISlkdktsKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDV 278
Cdd:PRK02118 161 -ALQAEADIIILGGMGLTFDDYLFFKDTFENAGALD------RTVMFIHTASDPPVECLLVPDMALAVAEKFALEGKKKV 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665388824 279 LLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQER-ITTTKKGSITSVQAIYVPADDLTDPAPATT 352
Cdd:PRK02118 234 LVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKaVDFEDGGSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
73-303 |
2.16e-19 |
|
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439826 [Multi-domain] Cd Length: 504 Bit Score: 90.87 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 73 VLEVAQHLGENTVRTIAMDGTEGLVRGQKVLDTGYPIRIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQ 152
Cdd:COG0056 59 VYGMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVID 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 153 -MSVeQEILVTGIKVVDLLAPyakggkIG------LFGGAGVGKTVLIMELINNvAKAHGGYSVFAGVGErtregndlyn 225
Cdd:COG0056 139 rQPV-HEPLQTGIKAIDAMIP------IGrgqrelIIGDRQTGKTAIAIDTIIN-QKGKDVICIYVAIGQ---------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 226 emieggvislkdKTSKVALV------YGQM----------NEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFT 289
Cdd:COG0056 201 ------------KASTVAQVvetleeHGAMeytivvaataSDPAPLQYIAPYAGCAMGEYFMDQ-GKDVLIVYDDLSKHA 267
|
250
....*....|....
gi 665388824 290 QAGSEVSALLGRIP 303
Cdd:COG0056 268 VAYRELSLLLRRPP 281
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
73-303 |
1.50e-18 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 88.20 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 73 VLEVAQHLGENTVRTIAMDGTEGLVRGQKVLDTGYPIRIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQ 152
Cdd:PRK09281 59 VYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVID 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 153 -MSVEqEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKAHGGYSVFAGVGErtregndlynemiegg 231
Cdd:PRK09281 139 rKSVH-EPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIIN-QKGKDVICIYVAIGQ---------------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 232 vislkdKTSKVALV------YGQM----------NEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEV 295
Cdd:PRK09281 201 ------KASTVAQVvrkleeHGAMeytivvaataSDPAPLQYLAPYAGCAMGEYFMDN-GKDALIVYDDLSKQAVAYRQL 273
|
....*...
gi 665388824 296 SALLGRIP 303
Cdd:PRK09281 274 SLLLRRPP 281
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
209-443 |
4.16e-18 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 87.77 E-value: 4.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 209 VFAGVGERTREGNDLYNEMIEggvisLKD-KTSK-----VALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFI 282
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFPK-----LKDpKTGKplmerTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYDVALMA 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 283 DNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERI-------TTTKKGSITSVQAIYVPADDLTDPAPATTFAH 355
Cdd:PRK14698 760 DSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRV 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 356 LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPnIIGQEHYNV-------ARGVQKILQDYKSLQDIIAILGMDELSEEDK 428
Cdd:PRK14698 840 VKVFWALDADLARRRHFPAINWLTSYSLYVDA-VKDWWHKNVdpewkamRDKAMELLQKEAELQEIVRIVGPDALPERER 918
|
250
....*....|....*.
gi 665388824 429 LTVARARKIQR-FLSQ 443
Cdd:PRK14698 919 AILLVARMLREdYLQQ 934
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
40-106 |
4.43e-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: 78.36 E-value: 4.43e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665388824 40 IVAVIGAVVDVQFD-DNLPPILNALEVDNRS-PRLVLEVAQHLGENTVRTIAMDGTEGLVRGQKVLDTG 106
Cdd:pfam02874 1 IVQVIGPVVDVEFGiGRLPGLLNALEVELVEfGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
88-411 |
1.68e-14 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 75.85 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 88 IAMDGTEGLVRGQKVLDTGYPIRIPVGAETLGRIINVIGEPID------ERGPIDTDKT-AAIHAEAPEFVQMSVEQEIL 160
Cdd:PTZ00185 94 ILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrSRALLESEQTlGKVDAGAPNIVSRSPVNYNL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 161 VTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINN-------VAKAHGGYSVFAGVGERTREGNDLYNEMIEGGVI 233
Cdd:PTZ00185 174 LTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINqvrinqqILSKNAVISIYVSIGQRCSNVARIHRLLRSYGAL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 234 SLKDKTSKVALvygqmnEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLA 313
Cdd:PTZ00185 254 RYTTVMAATAA------EPAGLQYLAPYSGVTMGEYFMNR-GRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVF 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 314 TDMGSMQERITTTKK----GSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRimdpni 389
Cdd:PTZ00185 327 YLHSRLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSR------ 400
|
330 340
....*....|....*....|....*..
gi 665388824 390 IGQEHYNVA-RGV----QKILQDYKSL 411
Cdd:PTZ00185 401 VGSSAQNVAmKAVagklKGILAEYRKL 427
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
76-303 |
6.30e-13 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 70.76 E-value: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 76 VAQHLGENTVRTIAMDGTEGLVRGQKVLDTGYPIRIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFV-QMS 154
Cdd:CHL00059 41 IALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIIsRRS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 155 VEqEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKAHGGYSVFAGVGERTREGNDLYNEMIEGGVIs 234
Cdd:CHL00059 121 VY-EPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN-QKGQNVICVYVAIGQKASSVAQVVTTLQERGAM- 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 235 lkDKTSKVAlvygQMNEPPGARARVA-LTGLTVAEYFRdQEGQDVLLFIDNIFRFTQAGSEVSALLGRIP 303
Cdd:CHL00059 198 --EYTIVVA----ETADSPATLQYLApYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPP 260
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
175-301 |
1.11e-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: 42.36 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388824 175 KGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYNEMIEGGVISLKDktskvalvygqmneppG 254
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSG----------------E 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 665388824 255 ARARVALTGLtvaeyfrdQEGQDVLLFIDNIFRFTQAGSEVSALLGR 301
Cdd:smart00382 65 LRLRLALALA--------RKLKPDVLILDEITSLLDAEQEALLLLLE 103
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
160-229 |
1.88e-03 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 41.16 E-value: 1.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665388824 160 LVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTV----LIMELINNVAKAHGGYSVFAGVGERTREGNDLYNEMIE 229
Cdd:PRK14698 211 LITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVdgdtLILTKEFGLIKIKDLYEILDGKGKKTVEGNEEWTELEE 284
|
|
| |
