|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-470 |
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: 979.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 1 MGIGRVTQVMGPVIDVRFEHNEVPKINNALVIDVPKEEgtlQLTLEVALQLGDDVVRTIAMDSTDGVQRGMDVKDTGKEI 80
Cdd:COG0055 3 MNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEGGG---ELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 81 SVPVGDETLGRVFNVLGETIDLKEEISDSVRRdPIHRQAPAFDELSTEVQILETGIKVVDLLAPYIKGGKIGLFGGAGVG 160
Cdd:COG0055 80 SVPVGEATLGRIFNVLGEPIDGKGPIEAKERR-PIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 161 KTVLIQELINNIAQEHGGISVFAGVGERTREGNDLYFEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDEQ 240
Cdd:COG0055 159 KTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 241 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTTKGSVTSIQAVFVPADDYTDPAPATAFA 320
Cdd:COG0055 239 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 321 HLDATTNLERKLTEMGIYPAVDPLASTSRALEPSIVGQEHYEVARDVQSTLQKYRELQDIIAILGMDELSDEDKQTVERA 400
Cdd:COG0055 319 HLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 401 RRIQFFLSQNFHVAEQFTGQKGSYVPVKTTVANFKDILDGKYDHIPEDAFRLVGSMDDVIAKAKDMGVEV 470
Cdd:COG0055 399 RKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAEA 468
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
3-466 |
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: 880.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 3 IGRVTQVMGPVIDVRFEHNEVPKINNALVIDVPKEEgtlQLTLEVALQLGDDVVRTIAMDSTDGVQRGMDVKDTGKEISV 82
Cdd:TIGR01039 2 KGKVVQVIGPVVDVEFEQGELPRIYNALKVQNRAES---ELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 83 PVGDETLGRVFNVLGETIDLKEEISDSvRRDPIHRQAPAFDELSTEVQILETGIKVVDLLAPYIKGGKIGLFGGAGVGKT 162
Cdd:TIGR01039 79 PVGKETLGRIFNVLGEPIDEKGPIPAK-ERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 163 VLIQELINNIAQEHGGISVFAGVGERTREGNDLYFEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDEQGQ 242
Cdd:TIGR01039 158 VLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 243 DVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTTKGSVTSIQAVFVPADDYTDPAPATAFAHL 322
Cdd:TIGR01039 238 DVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 323 DATTNLERKLTEMGIYPAVDPLASTSRALEPSIVGQEHYEVARDVQSTLQKYRELQDIIAILGMDELSDEDKQTVERARR 402
Cdd:TIGR01039 318 DATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613388749 403 IQFFLSQNFHVAEQFTGQKGSYVPVKTTVANFKDILDGKYDHIPEDAFRLVGSMDDVIAKAKDM 466
Cdd:TIGR01039 398 IQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
3-469 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 790.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 3 IGRVTQVMGPVIDVRFEHNEVPKINNALVIDVPKEEGT-LQLTLEVALQLGDDVVRTIAMDSTDGVQRGMDVKDTGKEIS 81
Cdd:CHL00060 16 LGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQeINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 82 VPVGDETLGRVFNVLGETIDLKEEISDSVRRdPIHRQAPAFDELSTEVQILETGIKVVDLLAPYIKGGKIGLFGGAGVGK 161
Cdd:CHL00060 96 VPVGGATLGRIFNVLGEPVDNLGPVDTRTTS-PIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 162 TVLIQELINNIAQEHGGISVFAGVGERTREGNDLYFEMSDSGVI-------KKTAMVFGQMNEPPGARMRVALSGLTMAE 234
Cdd:CHL00060 175 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVIneqniaeSKVALVYGQMNEPPGARMRVGLTALTMAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 235 YFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTTKGSVTSIQAVFVPADDYTDPA 314
Cdd:CHL00060 255 YFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 315 PATAFAHLDATTNLERKLTEMGIYPAVDPLASTSRALEPSIVGQEHYEVARDVQSTLQKYRELQDIIAILGMDELSDEDK 394
Cdd:CHL00060 335 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDR 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613388749 395 QTVERARRIQFFLSQNFHVAEQFTGQKGSYVPVKTTVANFKDILDGKYDHIPEDAFRLVGSMDDVIAKAKDMGVE 469
Cdd:CHL00060 415 LTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANLEVE 489
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
81-353 |
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: 574.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 81 SVPVGDETLGRVFNVLGETIDLKEEIsDSVRRDPIHRQAPAFDELSTEVQILETGIKVVDLLAPYIKGGKIGLFGGAGVG 160
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPI-KAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 161 KTVLIQELINNIAQEHGGISVFAGVGERTREGNDLYFEMSDSGVIK-----KTAMVFGQMNEPPGARMRVALSGLTMAEY 235
Cdd:cd01133 80 KTVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINldglsKVALVYGQMNEPPGARARVALTGLTMAEY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 236 FRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTTKGSVTSIQAVFVPADDYTDPAP 315
Cdd:cd01133 160 FRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAP 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 613388749 316 ATAFAHLDATTNLERKLTEMGIYPAVDPLASTSRALEP 353
Cdd:cd01133 240 ATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
4-458 |
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: 565.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 4 GRVTQVMGPVIDVRFEhNEVPKINNALVIDVPKEegtlqLTLEVALQLGDDVVRTIAMDSTDGVQRGMDVKDTGKEISVP 83
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFD-GELPAIHSVLRAGREGE-----VVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 84 VGDETLGRVFNVLGETIDLKEEISDsVRRDPIHRQAPAFDELSTEVQILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTV 163
Cdd:TIGR03305 75 VGKPTLSRMFDVFGNTIDRREPPKD-VEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 164 LIQELINNIAQEHGGISVFAGVGERTREGNDLYFEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDEQGQD 243
Cdd:TIGR03305 154 LLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 244 VLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTTKGSVTSIQAVFVPADDYTDPAPATAFAHLD 323
Cdd:TIGR03305 234 VLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 324 ATTNLERKLTEMGIYPAVDPLASTSRALEPSIVGQEHYEVARDVQSTLQKYRELQDIIAILGMDELSDEDKQTVERARRI 403
Cdd:TIGR03305 314 ASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 613388749 404 QFFLSQNFHVAEQFTGQKGSYVPVKTTVANFKDILDGKYDHIPEDAFRLVGSMDD 458
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 ... |
81-350 |
3.98e-127 |
|
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: 369.86 E-value: 3.98e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 81 SVPVGDETLGRVFNVLGETIDLKEEIsDSVRRDPIHRQAPAFDELSTEVQILETGIKVVDLLAPYIKGGKIGLFGGAGVG 160
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPI-KTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 161 KTVLIQELINNIAQEHGGISVFAGVGERTREGNDLYFEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDeQ 240
Cdd:cd19476 80 KTVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRD-N 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 241 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITST--TKGSVTSIQAVFVPADDYTDPAPATA 318
Cdd:cd19476 159 GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVkdGGGSITAIPAVSTPGDDLTDPIPDNT 238
|
250 260 270
....*....|....*....|....*....|..
gi 613388749 319 FAHLDATTNLERKLTEMGIYPAVDPLASTSRA 350
Cdd:cd19476 239 FAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
135-348 |
2.73e-96 |
|
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: 288.87 E-value: 2.73e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 135 GIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQehgGISVFAGVGERTREGNDLYFEMSDSGVIKKTAMVFGQ 214
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 215 MNEPPGARMRVALSGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTT- 293
Cdd:pfam00006 78 SDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKg 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 613388749 294 -KGSVTSIQAVFVPADDYTDPAPATAFAHLDATTNLERKLTEMGIYPAVDPLASTS 348
Cdd:pfam00006 157 kGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 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 ... |
355-462 |
5.83e-65 |
|
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: 204.63 E-value: 5.83e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 355 IVGQEHYEVARDVQSTLQKYRELQDIIAILGMDELSDEDKQTVERARRIQFFLSQNFHVAEQFTGQKGSYVPVKTTVANF 434
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 613388749 435 KDILDGKYDHIPEDAFRLVGSMDDVIAK 462
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
4-412 |
1.93e-63 |
|
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: 211.43 E-value: 1.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 4 GRVTQVMGPVIDVRfehneVP--KINNALVIDVPKEEGTLqltLEVaLQLGDDVVRTIAMDSTDGVQRGMDVKDTGKEIS 81
Cdd:COG1157 21 GRVTRVVGLLIEAV-----GPdaSIGELCEIETADGRPVL---AEV-VGFRGDRVLLMPLGDLEGISPGARVVPTGRPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 82 VPVGDETLGRVFNVLGETIDLKEEISDSVRRdPIHRQAPAFdeLS----TEVqiLETGIKVVDLLAPYIKGGKIGLFGGA 157
Cdd:COG1157 92 VPVGDGLLGRVLDGLGRPLDGKGPLPGEERR-PLDAPPPNP--LErariTEP--LDTGVRAIDGLLTVGRGQRIGIFAGS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 158 GVGKTVLIQELINNIAQEhggISVFAGVGERTRE-----GNDLYFE-MSDSGVIKKTAmvfgqmNEPPGARMRVALSGLT 231
Cdd:COG1157 167 GVGKSTLLGMIARNTEAD---VNVIALIGERGREvrefiEDDLGEEgLARSVVVVATS------DEPPLMRLRAAYTATA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 232 MAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTTKGSVTSIQAVFVPADDYT 311
Cdd:COG1157 238 IAEYFRD-QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 312 DPAPATAFAHLDATTNLERKLTEMGIYPAVDPLASTSRALePSIVGQEHYEVARDVQSTLQKYRELQDIIAI----LGMD 387
Cdd:COG1157 317 DPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM-PDIVSPEHRALARRLRRLLARYEENEDLIRIgayqPGSD 395
|
410 420
....*....|....*....|....*
gi 613388749 388 ELSDEdkqTVERARRIQFFLSQNFH 412
Cdd:COG1157 396 PELDE---AIALIPAIEAFLRQGMD 417
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
81-349 |
2.26e-59 |
|
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: 195.86 E-value: 2.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 81 SVPVGDETLGRVFNVLGETIDLKEEISDSVRRdPIHRQAPAFDELSTEVQILETGIKVVDLLAPYIKGGKIGLFGGAGVG 160
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERR-PLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 161 KTVLIQELINNIAQEhggISVFAGVGERTREGNDLYFEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDeQ 240
Cdd:cd01136 80 KSTLLGMIARNTDAD---VNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRD-Q 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 241 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTTKGSVTSIQAVFVPADDYTDPAPATAFA 320
Cdd:cd01136 156 GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRS 235
|
250 260
....*....|....*....|....*....
gi 613388749 321 HLDATTNLERKLTEMGIYPAVDPLASTSR 349
Cdd:cd01136 236 ILDGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
4-417 |
1.73e-52 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 183.03 E-value: 1.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 4 GRVTQVMGPVIDVrfehnEVPKINNALVIDVPKEEGTLQLTLEVaLQLGDDVVRTIAMDSTDGVQRGMDVKDTGKEISVP 83
Cdd:PRK06936 25 GRVTQVTGTILKA-----VVPGVRIGELCYLRNPDNSLSLQAEV-IGFAQHQALLTPLGEMYGISSNTEVSPTGTMHQVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 84 VGDETLGRVFNVLGETIDLKEEISDSVRRdPIHRQAPAFDELSTEVQILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTV 163
Cdd:PRK06936 99 VGEHLLGRVLDGLGQPFDGGHPPEPAAWY-PVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKST 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 164 LIQELINNIAQEhggISVFAGVGERTREGNDlyFEMSDSGV--IKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDeQG 241
Cdd:PRK06936 178 LLASLIRSAEVD---VTVLALIGERGREVRE--FIESDLGEegLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRD-QG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 242 QDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTTKGSVTSIQAVFVPADDYTDPAPATAFAH 321
Cdd:PRK06936 252 KRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVADETRSI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 322 LDATTNLERKLTEMGIYPAVDPLASTSRALEpSIVGQEHYEVARDVQSTLQKYRELQDIIAI----LGMDELSDEdkqTV 397
Cdd:PRK06936 332 LDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDKEADQ---AI 407
|
410 420
....*....|....*....|
gi 613388749 398 ERARRIQFFLSQNFHVAEQF 417
Cdd:PRK06936 408 ERIGAIRGFLRQGTHELSHF 427
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
62-410 |
3.51e-52 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 182.32 E-value: 3.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 62 DSTDGVQRGMDVKDTGKEISVPVGDETLGRVFNVLGETIDLKEEISDSVRRDpihrQAPAFDELSTEV--QILETGIKVV 139
Cdd:PRK06820 79 ASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWREL----DCPPPSPLTRQPieQMLTTGIRAI 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 140 DLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYFEMSDSGVIKKTAMVFGQMNEPP 219
Cdd:PRK06820 155 DGILSCGEGQRIGIFAAAGVGKSTLLGMLCADSAAD---VMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 220 GARMRVALSGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTTKGSVTS 299
Cdd:PRK06820 232 LERLKGLSTATTIAEYFRD-RGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 300 IQAVFVPADDYTDPAPATAFAHLDATTNLERKLTEMGIYPAVDPLASTSRALePSIVGQEHYEVARDVQSTLQKYRELQD 379
Cdd:PRK06820 311 FYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQEIEL 389
|
330 340 350
....*....|....*....|....*....|....*
gi 613388749 380 IIAI----LGMDELSDEdkqTVERARRIQFFLSQN 410
Cdd:PRK06820 390 LVRVgeyqAGEDLQADE---ALQRYPAICAFLQQD 421
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
4-417 |
1.43e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 167.21 E-value: 1.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 4 GRVTQVMGPVIDVRFEHNEVPKINNALVidvpKEEGTLQLTLEVaLQLGDDVVRTIAMDSTDGVQRGMDVKDTGKEISVP 83
Cdd:PRK07721 20 GKVSRVIGLMIESKGPESSIGDVCYIHT----KGGGDKAIKAEV-VGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 84 VGDETLGRVFNVLGETIDlKEEISDSVRRDPIHRQAPAFDELSTEVQILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTV 163
Cdd:PRK07721 95 VGSGLIGQVLDALGEPLD-GSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKST 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 164 LIQELINNIAQEhggISVFAGVGERTREGNDlyFEMSDSGV--IKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDeQG 241
Cdd:PRK07721 174 LMGMIARNTSAD---LNVIALIGERGREVRE--FIERDLGPegLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRD-QG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 242 QDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTTKGSVTSIQAVFVPADDYTDPAPATAFAH 321
Cdd:PRK07721 248 LNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTVRGI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 322 LDATTNLERKLTEMGIYPAVDPLASTSRALePSIVGQEHYEVARDVQSTLQKYRELQDIIAILGMDELSDED-KQTVERA 400
Cdd:PRK07721 328 LDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINIGAYKRGSSREiDEAIQFY 406
|
410
....*....|....*..
gi 613388749 401 RRIQFFLSQNFHVAEQF 417
Cdd:PRK07721 407 PQIISFLKQGTDEKATF 423
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
80-411 |
2.64e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 166.40 E-value: 2.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 80 ISVPVGDETLGRVFNVLGETIDLKEEISDSvRRDPIHRQAPAFDELSTEVQILETGIKVVDLLAPYIKGGKIGLFGGAGV 159
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYE-RYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 160 GKTVLIQELINN-IAQehggISVFAGVGERTREGNDlYFEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRD 238
Cdd:PRK08472 169 GKSTLMGMIVKGcLAP----IKVVALIGERGREIPE-FIEKNLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 239 eQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITST-TKGSVTSIQAVFVPADDYTDPAPAT 317
Cdd:PRK08472 244 -QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEeGKGSITAFFTVLVEGDDMSDPIADQ 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 318 AFAHLDATTNLERKLTEMGIYPAVDPLASTSRALEpSIVGQEHYEVARDVQSTLQKYRELQDIIAI----LGMDELSDEd 393
Cdd:PRK08472 323 SRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENEVLIRIgayqKGNDKELDE- 400
|
330
....*....|....*...
gi 613388749 394 kqTVERARRIQFFLSQNF 411
Cdd:PRK08472 401 --AISKKEFMEQFLKQNP 416
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
59-409 |
2.03e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 163.99 E-value: 2.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 59 IAMDSTDGVQRGMDVKDTGKEISVPVGDETLGRVFNVLGETIDlkeEISDSVRRDPIHRQAPAFDELSTE--VQILETGI 136
Cdd:PRK06793 68 LPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLN---EEAENIPLQKIKLDAPPIHAFEREeiTDVFETGI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 137 KVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGND-LYFEMSDSGvIKKTAMVFGQM 215
Cdd:PRK06793 145 KSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKAD---INVISLVGERGREVKDfIRKELGEEG-MRKSVVVVATS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 216 NEPPGARMRVALSGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAvGYQPTLATEMGQLQERITSTTKG 295
Cdd:PRK06793 221 DESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQKG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 296 SVTSIQAVFVPADDYTDPAPATAFAHLDATTNLERKLTEMGIYPAVDPLASTSRALEpSIVGQEHYEVARDVQSTLQKYR 375
Cdd:PRK06793 299 SITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPNHWQLANEMRKILSIYK 377
|
330 340 350
....*....|....*....|....*....|....*..
gi 613388749 376 ElQDIIAILGMDELSDEDKQTVERARRIQF---FLSQ 409
Cdd:PRK06793 378 E-NELYFKLGTIQENAENAYIFECKNKVEGintFLKQ 413
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
90-410 |
2.76e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 163.63 E-value: 2.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 90 GRVFNVLGETIDLKEEISDSVRRDPIHRQAPAFDELSTEVQILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELi 169
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 170 nniAQEHGGISV-FAGVGERTREGNDlYFEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDeQGQDVLLFI 248
Cdd:PRK06002 186 ---ARADAFDTVvIALVGERGREVRE-FLEDTLADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRD-RGENVLLIV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 249 DNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI--TSTTKGSVTSIQAVFVPADDYTDPAPATAFAHLDATT 326
Cdd:PRK06002 261 DSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHI 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 327 NLERKLTEMGIYPAVDPLASTSRALEPSIVGQEHYEVARdVQSTLQKYRELQDIIAILGMDELSDED-KQTVERARRIQF 405
Cdd:PRK06002 341 VLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSR-LKSMIARFEETRDLRLIGGYRAGSDPDlDQAVDLVPRIYE 419
|
....*
gi 613388749 406 FLSQN 410
Cdd:PRK06002 420 ALRQS 424
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
66-411 |
2.78e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 161.02 E-value: 2.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 66 GVQRGMDVKDTGKEISVPVGDETLGRVFNVLGETIDLKEEISDSVRrdpIHRQAPAFDELSTEV--QILETGIKVVDLLA 143
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQR---ASRHSPPINPLSRRPitEPLDVGVRAINAML 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 144 PYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYFEMSDSGVIKKTAMVFGQMNEPPGARM 223
Cdd:PRK08972 158 TVGKGQRMGLFAGSGVGKSVLLGMMTRGTTAD---VIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 224 RVALSGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI--TSTTKGSVTSIQ 301
Cdd:PRK08972 235 KGCETATTIAEYFRD-QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAgnGGPGQGSITAFY 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 302 AVFVPADDYTDPAPATAFAHLDATTNLERKLTEMGIYPAVDPLASTSRALePSIVGQEHYEVARDVQSTLQKYRELQDII 381
Cdd:PRK08972 314 TVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLI 392
|
330 340 350
....*....|....*....|....*....|....
gi 613388749 382 AILGMDELSDedkQTVERARRIQ----FFLSQNF 411
Cdd:PRK08972 393 SIGAYKQGSD---PRIDNAIRLQpamnAFLQQTM 423
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
52-409 |
6.99e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 159.73 E-value: 6.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 52 GDDVVRTiAMDSTDGVQRGMDVKDTGKEISVPVGDETLGRVFNVLGETIDLKEEIS------DSVRRDPIHRQAPAfdel 125
Cdd:PRK07594 62 GSKALLS-PFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRELPDvcwkdyDAMPPPAMVRQPIT---- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 126 stevQILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYFEMSDSGVI 205
Cdd:PRK07594 137 ----QPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDAD---SNVLVLIGERGREVREFIDFTLSEETR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 206 KKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQL 285
Cdd:PRK07594 210 KRCVIVVATSDRPALERVRALFVATTIAEFFRD-NGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 286 QERITSTTKGSVTSIQAVFVPADDYTDPAPATAFAHLDATTNLERKLTEMGIYPAVDPLASTSRALePSIVGQEHYEVAR 365
Cdd:PRK07594 289 LERTGMGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAA 367
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 613388749 366 DVQSTLQKYRELQDIIAI----LGMDELSDedkQTVERARRIQFFLSQ 409
Cdd:PRK07594 368 ILRRCLALYQEVELLIRIgeyqRGVDTDTD---KAIDTYPDICTFLRQ 412
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
57-410 |
2.56e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 158.22 E-value: 2.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 57 RTIAM--DSTDGVQRGMDVKDTGKEISVPVGDETLGRVFNVLGETIDLKEEISDSVRRDPIHRQAPAFDELSTEVQILET 134
Cdd:PRK08927 65 RALLMpfGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPYPLRAPPPPAHSRARVGEPLDL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 135 GIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDlyFEMSDSGV--IKKTAMVF 212
Cdd:PRK08927 145 GVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGREVQE--FLQDDLGPegLARSVVVV 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 213 GQMNEPPGARMRVALSGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI--T 290
Cdd:PRK08927 220 ATSDEPALMRRQAAYLTLAIAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 291 STTKGSVTSIQAVFVPADDYTDPAPATAFAHLDATTNLERKLTEMGIYPAVDPLASTSRALePSIVGQEHYEVARDVQST 370
Cdd:PRK08927 299 PIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQL 377
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 613388749 371 LQKYRELQDIIAI----LGMDELSDEdkqTVERARRIQFFLSQN 410
Cdd:PRK08927 378 MATYADMEELIRLgayrAGSDPEVDE---AIRLNPALEAFLRQG 418
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
4-409 |
1.27e-42 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 156.47 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 4 GRVTQVMGPVIdvrfehnEVPKINNAL--VIDVPKEEGTLQLTLEVaLQLGDDVVRTIAMDSTDGVQRGMDVKDTGKEIS 81
Cdd:PRK09099 26 GKVVEVIGTLL-------RVSGLDVTLgeLCELRQRDGTLLQRAEV-VGFSRDVALLSPFGELGGLSRGTRVIGLGRPLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 82 VPVGDETLGRVFNVLGETIDLKEEIsDSVRRDPIHRQAPafDELSTEV--QILETGIKVVDLLAPYIKGGKIGLFGGAGV 159
Cdd:PRK09099 98 VPVGPALLGRVIDGLGEPIDGGGPL-DCDELVPVIAAPP--DPMSRRMveAPLPTGVRIVDGLMTLGEGQRMGIFAPAGV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 160 GKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYFEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDe 239
Cdd:PRK09099 175 GKSTLMGMFARGTQCD---VNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRD- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 240 QGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTTKGSVTSIQAVFVPADDYTDPAPATAF 319
Cdd:PRK09099 251 RGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 320 AHLDATTNLERKLTEMGIYPAVDPLASTSRALePSIVGQEHYEVARDVQSTLQKYRELQDIIAI----LGMDELSDEdkq 395
Cdd:PRK09099 331 GILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVADE--- 406
|
410
....*....|....
gi 613388749 396 TVERARRIQFFLSQ 409
Cdd:PRK09099 407 AIAKIDAIRDFLSQ 420
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
63-383 |
2.75e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 152.96 E-value: 2.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 63 STDGVQRGMDVKDTGKEISVPVGDETLGRVFNVLGETIDLKEEIS--DSVRRDPihrqaPAFDELSTE--VQILETGIKV 138
Cdd:PRK05688 84 SVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKaeDWVPMDG-----PTINPLNRHpiSEPLDVGIRS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 139 VDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYFEMSDSGVIKKTAMVFGQMNEP 218
Cdd:PRK05688 159 INGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEAD---IIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 219 PGARMRVALSGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTTKG--S 296
Cdd:PRK05688 236 PLMRLRAAMYCTRIAEYFRD-KGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGggS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 297 VTSIQAVFVPADDYTDPAPATAFAHLDATTNLERKLTEMGIYPAVDPLASTSRALePSIVGQEHYEVARDVQSTLQKYRE 376
Cdd:PRK05688 315 ITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQQ 393
|
....*..
gi 613388749 377 LQDIIAI 383
Cdd:PRK05688 394 SRDLISV 400
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
61-381 |
9.15e-41 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 150.91 E-value: 9.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 61 MDSTDGVQRGMDVKDTGKEISVPVGDETLGRVFNVLG---ETIDLKEEISDSVRRDPIHRQAPAFDELSTEVQILETGIK 137
Cdd:PRK08149 61 IGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGkivERFDAPPTVGPISEERVIDVAPPSYAERRPIREPLITGVR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 138 VVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYFEMSDSGVIKKTAMVFGQMNE 217
Cdd:PRK08149 141 AIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHSEAD---VFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDF 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 218 PPGARMRVALSGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTTKGSV 297
Cdd:PRK08149 218 SSVDRCNAALVATTVAEYFRD-QGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 298 TSIQAVFVPADDYTDPAPATAFAHLDATTNLERKLTEMGIYPAVDPLASTSRALEpSIVGQEHYEVARDVQSTLQKYREL 377
Cdd:PRK08149 297 TAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFG-QVTDPKHRQLAAAFRKLLTRLEEL 375
|
....
gi 613388749 378 QDII 381
Cdd:PRK08149 376 QLFI 379
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
84-410 |
6.06e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 148.89 E-value: 6.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 84 VGDETLGRVFNVLGETIDLKEEISDSVrrdPIHRQAPAFDELSTEV--QILETGIKVVDLLAPYIKGGKIGLFGGAGVGK 161
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGST---PLQQQLPQIHPLQRRAvdTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 162 TVLIQELINNIAQEhggISVFAGVGERTREGNDLYFEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDeQG 241
Cdd:PRK07196 169 SVLLGMITRYTQAD---VVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRD-KG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 242 QDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI-TSTTKGSVTSIQAVFVPADDYTDPAPATAFA 320
Cdd:PRK07196 245 HDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGTMTAIYTVLAEGDDQQDPIVDCARA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 321 HLDATTNLERKLTEMGIYPAVDPLASTSRALEpSIVGQEHYEVARDVQSTLQKYRELQDIIA----ILGMDELSDedkQT 396
Cdd:PRK07196 325 VLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMAIKPLIPlggyVAGADPMAD---QA 400
|
330
....*....|....
gi 613388749 397 VERARRIQFFLSQN 410
Cdd:PRK07196 401 VHYYPAITQFLRQE 414
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
82-409 |
4.37e-33 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 130.29 E-value: 4.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 82 VPVGDETLGRVFNVLGETIDlKEEISDSVRRDPIHrqAPAFDELSTE--VQILETGIKVVDLLAPYIKGGKIGLFGGAGV 159
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLD-GLPAPDTGETGALI--TPPFNPLQRTpiEHVLDTGVRAINALLTVGRGQRMGLFAGSGV 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 160 GKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYFEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDe 239
Cdd:PRK07960 187 GKSVLLGMMARYTQAD---VIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRD- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 240 QGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITS--TTKGSVTSIQAVFVPADDYTDPAPAT 317
Cdd:PRK07960 263 RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQDPIADS 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 318 AFAHLDATTNLERKLTEMGIYPAVDPLASTSRALEpSIVGQEHYEVARDVQSTLQKYRELQDIIAI----LGMDELSDed 393
Cdd:PRK07960 343 ARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMT-ALIDEQHYARVRQFKQLLSSFQRNRDLVSVgayaKGSDPMLD-- 419
|
330
....*....|....*.
gi 613388749 394 kQTVERARRIQFFLSQ 409
Cdd:PRK07960 420 -KAIALWPQLEAFLQQ 434
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
69-412 |
5.49e-32 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 127.25 E-value: 5.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 69 RGMDVKDT-----GKEISVPVGDETLGRVFNVLGETIDLKEEISDSVRRD-------PIHRQAPAfdelstevQILETGI 136
Cdd:PRK04196 60 TGLDLKDTkvrftGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDingapinPVAREYPE--------EFIQTGI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 137 KVVDLLAPYIKGGKIGLFGGAGVGKtvliQELINNIAQ-------EHGGISVFAGVGERTREGNdlYF--EMSDSGVIKK 207
Cdd:PRK04196 132 SAIDGLNTLVRGQKLPIFSGSGLPH----NELAAQIARqakvlgeEENFAVVFAAMGITFEEAN--FFmeDFEETGALER 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 208 TAMVFGQMNEPPGARM---RVAlsgLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQ 284
Cdd:PRK04196 206 SVVFLNLADDPAIERIltpRMA---LTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLAT 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 285 LQER--ITSTTKGSVTSIQAVFVPADDYTDPAPatafahlDAT---TN----LERKLTEMGIYPAVDPLASTSRaLEPSI 355
Cdd:PRK04196 283 IYERagRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyiTEgqivLSRELHRKGIYPPIDVLPSLSR-LMKDG 354
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613388749 356 VG-----QEHYEVARDVQSTLQKYRELQDIIAILGMDELSDEDKQTVERARRI-QFFLSQNFH 412
Cdd:PRK04196 355 IGegktrEDHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFeREFVNQGFD 417
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
47-416 |
6.19e-32 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 127.72 E-value: 6.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 47 VALQLGDDVVRTIAMDSTDGVQRGMDVKDTGKEISVPVGDETLGRVFNVLGETIDLKEEISDSVRRdPIHRQAPAFDELS 126
Cdd:PRK13343 62 FAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARR-PLERPAPAIIERD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 127 TEVQILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELInnIAQEHGG-ISVFAGVGERTREGNDLYFEMSDSGVI 205
Cdd:PRK13343 141 FVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAI--INQKDSDvICVYVAIGQKASAVARVIETLREHGAL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 206 KKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQL 285
Cdd:PRK13343 219 EYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 286 QERITSTTK----GSVTSIQAVFVPADDYTDPAPATAFAHLDATTNLERKLTEMGIYPAVDPLASTSR----ALEPSIvg 357
Cdd:PRK13343 298 LERAAKLSPelggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRvggkAQHPAI-- 375
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613388749 358 qehYEVARDVQSTLQKYRELQdIIAILGMDeLSDEDKQTVERARRIQFFLSQNFH----VAEQ 416
Cdd:PRK13343 376 ---RKESGRLRLDYAQFLELE-AFTRFGGL-LDAGTQKQITRGRRLRELLKQPRFsplsVEEQ 433
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
3-80 |
1.95e-31 |
|
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: 115.31 E-value: 1.95e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613388749 3 IGRVTQVMGPVIDVRFEHNEVPKINNALVIdvpKEEGTLQLTLEVALQLGDDVVRTIAMDSTDGVQRGMDVKDTGKEI 80
Cdd:cd18115 2 TGKIVQVIGPVVDVEFPEGELPPIYNALEV---KGDDGKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
81-409 |
9.61e-31 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 123.48 E-value: 9.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 81 SVPVGDETLGRVFNVLGETIDLKEEISDSvRRDPIHRQAPAFDELSTEVQILETGIKVVDLLAPYIKGGKIGLFGGAGVG 160
Cdd:PRK05922 91 SLHLSDHLLGRVLDGFGNPLDGKEQLPKT-HLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 161 KTVLIQELINNIAQEhggISVFAGVGERTREGNDlYFEMSDSGVI-KKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDe 239
Cdd:PRK05922 170 KSSLLSTIAKGSKST---INVIALIGERGREVRE-YIEQHKEGLAaQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRD- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 240 QGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTTKGSVTSIQAVFVPA---DDYTDPAPA 316
Cdd:PRK05922 245 QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAILHYPnhpDIFTDYLKS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 317 TAFAHLdATTNLERKLTEmgiyPAVDPLASTSRALEpSIVGQEHYEVARDVQSTLQKYRELQDIIAILGMDELSDEDkqt 396
Cdd:PRK05922 325 LLDGHF-FLTPQGKALAS----PPIDILTSLSRSAR-QLALPHHYAAAEELRSLLKAYHEALDIIQLGAYVPGQDAH--- 395
|
330
....*....|....*..
gi 613388749 397 VERARR----IQFFLSQ 409
Cdd:PRK05922 396 LDRAVKllpsIKQFLSQ 412
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
82-349 |
8.10e-29 |
|
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: 114.63 E-value: 8.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 82 VPVGDETLGRVFNVLGETIDLKEEISDSVRRD-------PIHRQAPAfdelstevQILETGIKVVDLLAPYIKGGKIGLF 154
Cdd:cd01135 4 LPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDingppinPVARIYPE--------EMIQTGISAIDVMNTLVRGQKLPIF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 155 GGAGVGKtvliQELINNIA-------QEHGGISVFAGVGERTREGNDLYFEMSDSGVIKKTAMVFGQMNEPPGARMRVAL 227
Cdd:cd01135 76 SGSGLPH----NELAAQIArqagvvgSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 228 SGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQER--ITSTTKGSVTSIQAVFV 305
Cdd:cd01135 152 MALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTM 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 613388749 306 PADDYTDPAPatafahlDAT---TN----LERKLTEMGIYPAVDPLASTSR 349
Cdd:cd01135 232 PNDDITHPIP-------DLTgyiTEgqiyLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
1-439 |
1.45e-28 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 118.73 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 1 MGIGRVTQVMGPVIDVRFEH----NEVPKINN----ALVIDVPKEEGTLQLTLEVA-LQLGDDVVRTIAMDST------- 64
Cdd:PRK04192 2 MTKGKIVRVSGPLVVAEGMGgarmYEVVRVGEegliGEIIRIEGDKATIQVYEETSgIKPGEPVEFTGEPLSVelgpgll 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 65 ----DGVQRGMDV--KDTG----KEISVP---------------VGDE-----TLGRV-------------FNVLGETID 101
Cdd:PRK04192 82 gsifDGIQRPLDElaEKSGdfleRGVYVPaldrekkweftptvkVGDKveagdILGTVqetpsiehkimvpPGVSGTVKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 102 LKEE----ISDSV----------------RRDPIHRQAPAFDELsTEVQILETGIKVVDLLAPYIKGGKIGLFGGAGVGK 161
Cdd:PRK04192 162 IVSEgdytVDDTIavlededgegveltmmQKWPVRRPRPYKEKL-PPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 162 TVLIQELINNIAQEhggISVFAGVGERtreGNdlyfEMSD------------SG--VIKKTAMVFGQMNEPPGARMRVAL 227
Cdd:PRK04192 241 TVTQHQLAKWADAD---IVIYVGCGER---GN----EMTEvleefpelidpkTGrpLMERTVLIANTSNMPVAAREASIY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 228 SGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQER----IT-STTKGSVTSIQA 302
Cdd:PRK04192 311 TGITIAEYYRD-MGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvKTlGGEEGSVTIIGA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 303 VFVPADDYTDP-APAT-----AFAHLDAttnlerKLTEMGIYPAVDPLASTSR---ALEPSI---VGQEHYEVARDVQST 370
Cdd:PRK04192 390 VSPPGGDFSEPvTQNTlrivkVFWALDA------ELADRRHFPAINWLTSYSLyldQVAPWWeenVDPDWRELRDEAMDL 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613388749 371 LQKYRELQDIIAILGMDELSDEDKQTVERARRIQF-FLSQN-FHVAEqftgqkgSYVPVKTTVANFKDILD 439
Cdd:PRK04192 464 LQREAELQEIVRLVGPDALPEEDRLILEVARLIREdFLQQNaFDPVD-------TYCPPEKQYEMLKLILT 527
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
109-349 |
2.42e-28 |
|
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: 113.44 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 109 SVRRDPIHRQAPAFDELSTEVqILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGER 188
Cdd:cd01134 38 NVQRWPVRQPRPVKEKLPPNV-PLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSLSKWSNSD---VVIYVGCGER 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 189 treGND----------LYFEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDeQGQDVLLFIDNIFRFTQAG 258
Cdd:cd01134 114 ---GNEmaevleefpeLKDPITGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRD-MGYNVSLMADSTSRWAEAL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 259 SEVSALLGRMPSAVGYQPTLATEMGQLQER------ITSTTK-GSVTSIQAVFVPADDYTDP-APAT-----AFAHLDAt 325
Cdd:cd01134 190 REISGRLEEMPAEEGYPAYLGARLAEFYERagrvrcLGSPGReGSVTIVGAVSPPGGDFSEPvTQATlrivqVFWGLDK- 268
|
250 260
....*....|....*....|....
gi 613388749 326 tnlerKLTEMGIYPAVDPLASTSR 349
Cdd:cd01134 269 -----KLAQRRHFPSINWLISYSK 287
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
47-412 |
3.95e-22 |
|
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: 98.64 E-value: 3.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 47 VALQLGDDVVRTIAMDSTDG----VQ-----RGMDVKD-----TGKEISVPVGDETLGRVFNVLGETID-----LKEEIS 107
Cdd:TIGR01040 27 VNLTLPDGTVRSGQVLEVSGnkavVQvfegtSGIDAKKttcefTGDILRTPVSEDMLGRVFNGSGKPIDkgppvLAEDYL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 108 DsVRRDPIHRQAPAFDElstevQILETGIKVVDLLAPYIKGGKIGLFGGAGV-------------GKTVLIQELINNIAQ 174
Cdd:TIGR01040 107 D-INGQPINPYARIYPE-----EMIQTGISAIDVMNSIARGQKIPIFSAAGLphneiaaqicrqaGLVKLPTKDVHDGHE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 175 EHGGIsVFAGVGERTREGNDLYFEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDEQGQDVLLFIDNIFRF 254
Cdd:TIGR01040 181 DNFAI-VFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 255 TQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTT--KGSVTSIQAVFVPADDYTDPAPATAFAHLDATTNLERKL 332
Cdd:TIGR01040 260 ADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 333 TEMGIYPAVDPLASTSRaLEPSIVGQ-----EHYEVARDVQSTLQKYRELQDIIAILGMDELSDEDKQTVERARRIQ-FF 406
Cdd:TIGR01040 340 HNRQIYPPINVLPSLSR-LMKSAIGEgmtrkDHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEkNF 418
|
....*.
gi 613388749 407 LSQNFH 412
Cdd:TIGR01040 419 IAQGPY 424
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
80-349 |
4.25e-21 |
|
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: 92.62 E-value: 4.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 80 ISVPVGDETLGRVFNVLGETIDLKEEISDSVRRdPIHRQAPAFDELSTEVQILETGIKVVDLLAPYIKGGKIGLFGGAGV 159
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERR-RVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 160 GKT-VLIQELINNiaQEHGGISVFAGVGERTREGNDLYFEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRD 238
Cdd:cd01132 81 GKTaIAIDTIINQ--KGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 239 eQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTTK----GSVTSIQAVFVPADDYTDPA 314
Cdd:cd01132 159 -NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGSLTALPIIETQAGDVSAYI 237
|
250 260 270
....*....|....*....|....*....|....*
gi 613388749 315 PATAFAHLDATTNLERKLTEMGIYPAVDPLASTSR 349
Cdd:cd01132 238 PTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
47-269 |
1.47e-20 |
|
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: 94.34 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 47 VALQLGDDVVRTIAMDSTDGVQRGMDVKDTGKEISVPVGDETLGRVFNVLGETIDLKEEISDSVRRdPIHRQAPAFDELS 126
Cdd:COG0056 62 MALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERR-PVERPAPGVIDRQ 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 127 TEVQILETGIKVVDLLAPyikggkIG------LFGGAGVGKT-VLIQELINniaQEHGGI-----------SVFAGVGER 188
Cdd:COG0056 141 PVHEPLQTGIKAIDAMIP------IGrgqrelIIGDRQTGKTaIAIDTIIN---QKGKDViciyvaigqkaSTVAQVVET 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 189 TREGndlyfemsdsGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRM 268
Cdd:COG0056 212 LEEH----------GAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMD-QGKDVLIVYDDLSKHAVAYRELSLLLRRP 280
|
.
gi 613388749 269 P 269
Cdd:COG0056 281 P 281
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
5-402 |
6.04e-20 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 92.02 E-value: 6.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 5 RVTQVMGPVIDVRFE---HNEVPKINN------ALVIDVPKEEGTLQLtlevalqlgddvvrtiaMDSTDGVQRGMDVKD 75
Cdd:PRK02118 7 KITDITGNVITVEAEgvgYGELATVERkdgsslAQVIRLDGDKVTLQV-----------------FGGTRGISTGDEVVF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 76 TGKEISVPVGDETLGRVFNVLGETIDLKEEISDsvrrDPIHRQAPAFDELSTEV--QILETGIKVVDLLAPYIKGGKIGL 153
Cdd:PRK02118 70 LGRPMQVTYSESLLGRRFNGSGKPIDGGPELEG----EPIEIGGPSVNPVKRIVprEMIRTGIPMIDVFNTLVESQKIPI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 154 FGGAGVGktvlIQELINNIA-QEHGGISVFAGVGERtregND--LYF--EMSDSGVIKKTAMVFGQMNEPPGARMRVALS 228
Cdd:PRK02118 146 FSVSGEP----YNALLARIAlQAEADIIILGGMGLT----FDdyLFFkdTFENAGALDRTVMFIHTASDPPVECLLVPDM 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 229 GLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQER-ITSTTKGSVTSIQAVFVPA 307
Cdd:PRK02118 218 ALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKaVDFEDGGSITIIAVTTMPG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 308 DDYTDPAPatafahlDATTnlerKLTEMGIY---PAVDPLASTSRaLEPSIVGQEHYEVARDVQSTLQK----YRELQDI 380
Cdd:PRK02118 298 DDVTHPVP-------DNTG----YITEGQFYlrrGRIDPFGSLSR-LKQLVIGKKTREDHGDLMNAMIRlyadSREAKEK 365
|
410 420
....*....|....*....|..
gi 613388749 381 IAiLGMDeLSDEDKQTVERARR 402
Cdd:PRK02118 366 MA-MGFK-LSNWDEKLLKFSEL 385
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
44-269 |
1.04e-19 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 91.67 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 44 TLEVALQLGDDVVRTIAMDSTDGVQRGMDVKDTGKEISVPVGDETLGRVFNVLGETIDLKEEISDSVRRdPIHRQAPA-F 122
Cdd:PRK09281 59 VYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETR-PVERKAPGvI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 123 DELSTEvQILETGIKVVDLLAPyikggkIG------LFGGAGVGKT-VLIQELINniaQEHGGI-----------SVFAG 184
Cdd:PRK09281 138 DRKSVH-EPLQTGIKAIDAMIP------IGrgqrelIIGDRQTGKTaIAIDTIIN---QKGKDViciyvaigqkaSTVAQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 185 VGERTREgndlYFEMSDSGVIKKTAmvfgqmNEPPGARMRVALSGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSAL 264
Cdd:PRK09281 208 VVRKLEE----HGAMEYTIVVAATA------SDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQLSLL 276
|
....*
gi 613388749 265 LGRMP 269
Cdd:PRK09281 277 LRRPP 281
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
72-404 |
3.61e-19 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 90.85 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 72 DVKDTGKEISVPVGDETLG-RVFNVLGETIDLkEEISDSvrrdpiHRQAPAFDELsTEVQILETGIKVVDllapyIKGGK 150
Cdd:PRK14698 589 ELKKAGIEIHNYLSGENMSyEMFRKFAKFVGL-EEIAEN------HLQHILFDEI-VEINYISEGQEVYD-----ITTET 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 151 IGLFGGAgvgktvlIQELINNIAQEH-------GGISVFAGVGERTREGNDLYFEM-------SDSGVIKKTAMVFGQMN 216
Cdd:PRK14698 656 HNFIGGN-------MPTLLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEFpklkdpkTGKPLMERTVLIANTSN 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 217 EPPGARMRVALSGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTTK-- 294
Cdd:PRK14698 729 MPVAAREASIYTGITIAEYFRD-MGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTlg 807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 295 -----GSVTSIQAVFVPADDYTDPAPATAFAHLDATTNLERKLTEMGIYPAVDPLASTSRALEP------SIVGQEHYEV 363
Cdd:PRK14698 808 sdyrvGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAvkdwwhKNVDPEWKAM 887
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 613388749 364 ARDVQSTLQKYRELQDIIAILGMDELSDEDKQTVERARRIQ 404
Cdd:PRK14698 888 RDKAMELLQKEAELQEIVRIVGPDALPERERAILLVARMLR 928
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
53-405 |
2.71e-18 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 87.40 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 53 DDVVRTIAMDSTDGVQRGMDVKDTGKEISVPVGDETLGRVFNVLGETIDL------KEEISDSVRRDPIHRQAPAFDELS 126
Cdd:PTZ00185 88 DGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPVglltrsRALLESEQTLGKVDAGAPNIVSRS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 127 TEVQILETGIKVVDLLAPYIKGGKIGLFGGAGVGKT-VLIQELIN------NIAQEHGGISVFAGVGERTREGNDLYFEM 199
Cdd:PTZ00185 168 PVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTsIAVSTIINqvrinqQILSKNAVISIYVSIGQRCSNVARIHRLL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 200 SDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLA 279
Cdd:PTZ00185 248 RSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMN-RGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVF 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 280 TEMGQLQERITSTTK----GSVTSIQAVFVPADDYTDPAPATAFAHLDATTNLERKLTEMGIYPAVDPLASTSRaLEPSI 355
Cdd:PTZ00185 327 YLHSRLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSR-VGSSA 405
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 613388749 356 VGQEHYEVARDVQSTLQKYRElqdiiaiLGMDELSDEDKQTVERARRIQF 405
Cdd:PTZ00185 406 QNVAMKAVAGKLKGILAEYRK-------LAADSVGGSQVQTVPMIRGARF 448
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
360-429 |
2.43e-17 |
|
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: 76.33 E-value: 2.43e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 360 HYEVARDVQSTLQKYRELQDIIAILGMDELSDEDKQTVERARRIQFFLSQNFHVAEQFTGQKGSYVPVKT 429
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
6-77 |
6.37e-17 |
|
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: 74.89 E-value: 6.37e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613388749 6 VTQVMGPVIDVRFEHNEVPKINNALVIDVPKEEGtlqLTLEVALQLGDDVVRTIAMDSTDGVQRGMDVKDTG 77
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVEFGS---LVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
37-422 |
3.59e-16 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 80.78 E-value: 3.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 37 EEGTLQltleVALQLGDDVVRTIAMDSTDGVQRGMDVKDTGKEISVPVGDETLGRVFNVLGETIDLKEEISDSVRRdPIH 116
Cdd:CHL00059 35 EDGTIG----IALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESR-LIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 117 RQAPAFDELSTEVQILETGIKVVDLLAPYIKGGKIGLFGGAGVGKT-VLIQELINNIAQehGGISVFAGVGERTREGNDL 195
Cdd:CHL00059 110 SPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTaVATDTILNQKGQ--NVICVYVAIGQKASSVAQV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 196 YFEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRdEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQ 275
Cdd:CHL00059 188 VTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 276 PTLATEMGQLQERITSTTK----GSVTSIQAVFVPADDYTDPAPATAFAHLDATTNLERKLTEMGIYPAVDPLASTSR-- 349
Cdd:CHL00059 267 GDVFYLHSRLLERAAKLSSqlgeGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRvg 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 350 -ALEPSIVGQehyeVARDVQSTLQKYRELQDIIAIlgmdeLSDEDKQT---VERARRIQFFLSQN----FHVAEQ----F 417
Cdd:CHL00059 347 sAAQIKAMKQ----VAGKLKLELAQFAELEAFAQF-----ASDLDKATqnqLARGQRLRELLKQSqsapLTVEEQvatiY 417
|
....*
gi 613388749 418 TGQKG 422
Cdd:CHL00059 418 TGTNG 422
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
66-377 |
2.25e-11 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 65.11 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 66 GVQRGMDVKDtgkEISVPVGDETLGRVFNVLGetidlkeeisdsvrRDPIHRQA-PAFDELS----TEVQILETG----- 135
Cdd:PRK12608 58 NLRTGDVVEG---VARPRERYRVLVRVDSVNG--------------TDPEKLARrPHFDDLTplhpRERLRLETGsddls 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 136 IKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEHGGISVFAG-VGERTREGNDlyFEMSDSGvikktaMVFGQ 214
Cdd:PRK12608 121 MRVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTD--MRRSVKG------EVYAS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 215 MNEPPGARmRVALSGLTMAEYFRD-EQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAvgyqpTLATEMGQLQERITSTT 293
Cdd:PRK12608 193 TFDRPPDE-HIRVAELVLERAKRLvEQGKDVVILLDSLTRLARAYNNEVESSGRTLSG-----GVDARALQRPKRLFGAA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 294 K-----GSVTSIQAVFVP----ADDYTdpapataFAHLDATTNLE----RKLTEMGIYPAVDPLASTSRALEPSIVGQEH 360
Cdd:PRK12608 267 RnieegGSLTIIATALVDtgsrMDEVI-------FEEFKGTGNMEivldRELADKRVFPAIDIAKSGTRREELLLDSKEL 339
|
330 340
....*....|....*....|....*
gi 613388749 361 YEV--------ARDVQSTLQKYREL 377
Cdd:PRK12608 340 EKVrrlrralaSRKPVEAMEALLEK 364
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
4-78 |
6.46e-09 |
|
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: 52.31 E-value: 6.46e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613388749 4 GRVTQVMGPVIDVRFEhNEVPkINNALVIDVPKEEGTLQLTLEVALQLGDDVVrTIAMDSTDGVQRGMDVKDTGK 78
Cdd:cd01426 2 GRVIRVNGPLVEAELE-GEVA-IGEVCEIERGDGNNETVLKAEVIGFRGDRAI-LQLFESTRGLSRGALVEPTGR 73
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
137-349 |
3.10e-06 |
|
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: 48.36 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 137 KVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEHGGISVFAG-VGERTREGNDlyfeMSDSG---VIKKTamvf 212
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRSVkgeVVAST---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 213 gqMNEPPGARMRVALSGLTMAEYfRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAvGYQPTlATEMGQlqeRITST 292
Cdd:cd01128 77 --FDEPPERHVQVAEMVIEKAKR-LVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSG-GVDAN-ALHKPK---RFFGA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613388749 293 TK-----GSVTSIQAVFVPADDYTDPApatAFAHLDATTNLE----RKLTEMGIYPAVDPLASTSR 349
Cdd:cd01128 149 ARnieegGSLTIIATALVDTGSRMDEV---IFEEFKGTGNMElvldRKLAEKRIFPAIDILKSGTR 211
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
147-268 |
3.27e-06 |
|
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: 46.98 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 147 KGGKIGLFGGAGVGKTVLIQELINNIAQEHGGISVFAGVGERTREGNDLYFEMSDSGVIKKTamvfgqmnepPGARMRVA 226
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS----------GELRLRLA 70
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 613388749 227 lsgLTMAEYFRDEqgqdvLLFIDNIFRFTQAGSEVSALLGRM 268
Cdd:smart00382 71 ---LALARKLKPD-----VLILDEITSLLDAEQEALLLLLEE 104
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
117-388 |
7.55e-06 |
|
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: 48.14 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 117 RQAPAFDELS----TEVQILETG-----IKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEHGGISVFAG-VG 186
Cdd:TIGR00767 128 KNRVLFENLTplypNERLRLETStedlsTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEVELIVLlID 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 187 ERTREGNDLyfEMSDSG-VIKKTamvfgqMNEPPGARMRVALSGLTMAEYfRDEQGQDVLLFIDNIFRFTQAGSEVSALL 265
Cdd:TIGR00767 208 ERPEEVTDM--QRSVKGeVVAST------FDEPASRHVQVAEMVIEKAKR-LVEHKKDVVILLDSITRLARAYNTVTPAS 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 266 GRMPSAvGYQPTLAtemgQLQERITSTTK-----GSVTSIQAVFVPADDYTDpapATAFAHLDATTNLE----RKLTEMG 336
Cdd:TIGR00767 279 GKVLSG-GVDANAL----HRPKRFFGAARnieegGSLTIIATALIDTGSRMD---EVIFEEFKGTGNMElhldRKLADRR 350
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 613388749 337 IYPAVDPLASTSRAlEPSIVGQEHyevardvqstLQKYRELQDIIAilGMDE 388
Cdd:TIGR00767 351 IFPAIDIKKSGTRK-EELLLTPEE----------LQKIWVLRKIIS--PMDS 389
|
|
| ATP-synt_V_A-type_alpha_C |
cd18111 |
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of ... |
371-418 |
3.96e-05 |
|
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of the V1/A1 complex of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the 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 Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.
Pssm-ID: 349746 [Multi-domain] Cd Length: 105 Bit Score: 42.38 E-value: 3.96e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 613388749 371 LQKYRELQDIIAILGMDELSDEDKQTVERARRI-QFFLSQN-FHVAEQFT 418
Cdd:cd18111 12 LQEEAELQEIVQLVGPDALPEEDRLTLEVARMIrEDFLQQNaFDEVDTYC 61
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
117-349 |
1.04e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 41.28 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 117 RQAPAFDELS----TEVQILETGI------KVVDLLAPYIKG--GKIglfggagV-----GKTVLIQELINNIAQEHGGI 179
Cdd:PRK09376 128 RNRPLFENLTplypNERLRLETGNpedlstRIIDLIAPIGKGqrGLI-------VappkaGKTVLLQNIANSITTNHPEV 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 180 SVFAG-VGERTREGNDlyfeMSDS---GVIKKTamvfgqMNEPPGARMRVALSGLTMAEyfRD-EQGQDVLLFIDNIFRF 254
Cdd:PRK09376 201 HLIVLlIDERPEEVTD----MQRSvkgEVVAST------FDEPAERHVQVAEMVIEKAK--RLvEHGKDVVILLDSITRL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 255 TQAGSEVSALLGRM------PSAVgYQPT------LATEMGqlqeritsttkGSVTSIqavfvpaddytdpapATA---- 318
Cdd:PRK09376 269 ARAYNTVVPSSGKVlsggvdANAL-HRPKrffgaaRNIEEG-----------GSLTII---------------ATAlidt 321
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 613388749 319 --------FAHLDATTN----LERKLTEMGIYPAVDPLASTSR 349
Cdd:PRK09376 322 gsrmdeviFEEFKGTGNmelhLDRKLAEKRIFPAIDINRSGTR 364
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
86-201 |
1.51e-03 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 41.16 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388749 86 DETLGRVFNVLGETIDLKeeisdSVRRDPIHRQAPAFDELSTEVQILeTGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLI 165
Cdd:PRK14698 171 EEVIAKVKTPSGEIKELK-----MYQRWPVRVKRPYKEKLPPEVPLI-TGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDG 244
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 613388749 166 QELInnIAQEHGGISV------FAGVGERTREGNDLYFEMSD 201
Cdd:PRK14698 245 DTLI--LTKEFGLIKIkdlyeiLDGKGKKTVEGNEEWTELEE 284
|
|
| |
