|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-473 |
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: 1027.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 1 MTRGRVIQVMGPVVDVKFENGHLPAIYNALKIqhqarnENEVDIDLTLEVALHLGDDTVRTIAMASTDGLIRGMEVVDTG 80
Cdd:COG0055 3 MNTGKIVQVIGPVVDVEFPEGELPAIYNALEV------ENEGGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 81 APISVPVGDVTLGRVFNVLGEPIDLQDDIPAEARRdPIHRPAPKFEELATEVEILETGIKVVDLLAPYIKGGKIGLFGGA 160
Cdd:COG0055 77 APISVPVGEATLGRIFNVLGEPIDGKGPIEAKERR-PIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 161 GVGKTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYHEMKDSGVISKTAMVFGQMNEPPGARMRVALTGLTMAEYFR 240
Cdd:COG0055 156 GVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 241 DEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTSKGSITSIQAIYVPADDYTDPAPAT 320
Cdd:COG0055 236 DEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPAT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 321 TFSHLDATTNLERKLAEMGIYPAVDPLASTSRALAPEIVGEEHYQVARRVQQTLQRYKELQDIIAILGMDELSDEDKLVV 400
Cdd:COG0055 316 TFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTV 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496156186 401 HRARRIQFFLSQNFHVAEQFTGQPGSYVPVKETVRGFKEILDGKYDHLPEDAFRLVGRIEEVVEKAKAMGVEV 473
Cdd:COG0055 396 ARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAEA 468
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
2-469 |
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: 945.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 2 TRGRVIQVMGPVVDVKFENGHLPAIYNALKIQhqarneNEVDIDLTLEVALHLGDDTVRTIAMASTDGLIRGMEVVDTGA 81
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQ------NRAESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 82 PISVPVGDVTLGRVFNVLGEPIDLQDDIPAEARrDPIHRPAPKFEELATEVEILETGIKVVDLLAPYIKGGKIGLFGGAG 161
Cdd:TIGR01039 75 PISVPVGKETLGRIFNVLGEPIDEKGPIPAKER-WPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 162 VGKTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYHEMKDSGVISKTAMVFGQMNEPPGARMRVALTGLTMAEYFRD 241
Cdd:TIGR01039 154 VGKTVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 242 EQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTSKGSITSIQAIYVPADDYTDPAPATT 321
Cdd:TIGR01039 234 EQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 322 FSHLDATTNLERKLAEMGIYPAVDPLASTSRALAPEIVGEEHYQVARRVQQTLQRYKELQDIIAILGMDELSDEDKLVVH 401
Cdd:TIGR01039 314 FAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496156186 402 RARRIQFFLSQNFHVAEQFTGQPGSYVPVKETVRGFKEILDGKYDHLPEDAFRLVGRIEEVVEKAKAM 469
Cdd:TIGR01039 394 RARRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
4-472 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 855.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 4 GRVIQVMGPVVDVKFENGHLPAIYNALKIQhqARNENEVDIDLTLEVALHLGDDTVRTIAMASTDGLIRGMEVVDTGAPI 83
Cdd:CHL00060 17 GRITQIIGPVLDVAFPPGKMPNIYNALVVK--GRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 84 SVPVGDVTLGRVFNVLGEPIDLQDDIPAEARRdPIHRPAPKFEELATEVEILETGIKVVDLLAPYIKGGKIGLFGGAGVG 163
Cdd:CHL00060 95 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTS-PIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 164 KTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYHEMKDSGVI-------SKTAMVFGQMNEPPGARMRVALTGLTMA 236
Cdd:CHL00060 174 KTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVIneqniaeSKVALVYGQMNEPPGARMRVGLTALTMA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 237 EYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTSKGSITSIQAIYVPADDYTDP 316
Cdd:CHL00060 254 EYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 317 APATTFSHLDATTNLERKLAEMGIYPAVDPLASTSRALAPEIVGEEHYQVARRVQQTLQRYKELQDIIAILGMDELSDED 396
Cdd:CHL00060 334 APATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEED 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496156186 397 KLVVHRARRIQFFLSQNFHVAEQFTGQPGSYVPVKETVRGFKEILDGKYDHLPEDAFRLVGRIEEVVEKAKAMGVE 472
Cdd:CHL00060 414 RLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANLEVE 489
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
4-461 |
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: 591.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 4 GRVIQVMGPVVDVKFEnGHLPAIYNALKIQHQArnenevdiDLTLEVALHLGDDTVRTIAMASTDGLIRGMEVVDTGAPI 83
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFD-GELPAIHSVLRAGREG--------EVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 84 SVPVGDVTLGRVFNVLGEPIDlQDDIPAEARRDPIHRPAPKFEELATEVEILETGIKVVDLLAPYIKGGKIGLFGGAGVG 163
Cdd:TIGR03305 72 KAPVGKPTLSRMFDVFGNTID-RREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 164 KTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYHEMKDSGVISKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDEQ 243
Cdd:TIGR03305 151 KTVLLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 244 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTSKGSITSIQAIYVPADDYTDPAPATTFS 323
Cdd:TIGR03305 231 KQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 324 HLDATTNLERKLAEMGIYPAVDPLASTSRALAPEIVGEEHYQVARRVQQTLQRYKELQDIIAILGMDELSDEDKLVVHRA 403
Cdd:TIGR03305 311 HLSASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRA 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 496156186 404 RRIQFFLSQNFHVAEQFTGQPGSYVPVKETVRGFKEILDGKYDHLPEDAFRLVGRIEE 461
Cdd:TIGR03305 391 RRLERFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDE 448
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
84-356 |
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: 589.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 84 SVPVGDVTLGRVFNVLGEPIDLQDDIPAEaRRDPIHRPAPKFEELATEVEILETGIKVVDLLAPYIKGGKIGLFGGAGVG 163
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAK-ERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 164 KTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYHEMKDSGVI-----SKTAMVFGQMNEPPGARMRVALTGLTMAEY 238
Cdd:cd01133 80 KTVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVInldglSKVALVYGQMNEPPGARARVALTGLTMAEY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 239 FRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTSKGSITSIQAIYVPADDYTDPAP 318
Cdd:cd01133 160 FRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAP 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 496156186 319 ATTFSHLDATTNLERKLAEMGIYPAVDPLASTSRALAP 356
Cdd:cd01133 240 ATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
84-353 |
1.98e-128 |
|
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: 373.33 E-value: 1.98e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 84 SVPVGDVTLGRVFNVLGEPIDLQDDIPAEARRdPIHRPAPKFEELATEVEILETGIKVVDLLAPYIKGGKIGLFGGAGVG 163
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRR-PIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 164 KTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYHEMKDSGVISKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDeQ 243
Cdd:cd19476 80 KTVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRD-N 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 244 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITST--SKGSITSIQAIYVPADDYTDPAPATT 321
Cdd:cd19476 159 GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVkdGGGSITAIPAVSTPGDDLTDPIPDNT 238
|
250 260 270
....*....|....*....|....*....|..
gi 496156186 322 FSHLDATTNLERKLAEMGIYPAVDPLASTSRA 353
Cdd:cd19476 239 FAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
138-351 |
2.81e-100 |
|
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: 299.27 E-value: 2.81e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 138 GIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELIHNIAQehgGISVFAGVGERTREGNDLYHEMKDSGVISKTAMVFGQ 217
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 218 MNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTS- 296
Cdd:pfam00006 78 SDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKg 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496156186 297 -KGSITSIQAIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLASTS 351
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 ... |
358-465 |
1.07e-72 |
|
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: 224.66 E-value: 1.07e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 358 IVGEEHYQVARRVQQTLQRYKELQDIIAILGMDELSDEDKLVVHRARRIQFFLSQNFHVAEQFTGQPGSYVPVKETVRGF 437
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 496156186 438 KEILDGKYDHLPEDAFRLVGRIEEVVEK 465
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
56-441 |
6.29e-72 |
|
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: 233.77 E-value: 6.29e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 56 DDTVRTIAMASTDGLIRGMEVVDTGAPISVPVGDVTLGRVFNVLGEPIDLQDDIPAEARRdPIHRPAPKFEELATEVEIL 135
Cdd:COG1157 63 GDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERR-PLDAPPPNPLERARITEPL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 136 ETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTRE-----GNDLYHE-MKDSGVIS 209
Cdd:COG1157 142 DTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIARNTEAD---VNVIALIGERGREvrefiEDDLGEEgLARSVVVV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 210 KTAmvfgqmNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQ 289
Cdd:COG1157 219 ATS------DEPPLMRLRAAYTATAIAEYFRD-QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 290 ERITSTSKGSITsiqAIY---VPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLASTSRaLAPEIVGEEHYQV 366
Cdd:COG1157 292 ERAGNGGKGSIT---AFYtvlVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISR-VMPDIVSPEHRAL 367
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496156186 367 ARRVQQTLQRYKELQDIIAI----LGMDELSDEdklVVHRARRIQFFLSQNFHvaeqftgqpgSYVPVKETVRGFKEIL 441
Cdd:COG1157 368 ARRLRRLLARYEENEDLIRIgayqPGSDPELDE---AIALIPAIEAFLRQGMD----------ERVSFEESLAQLAELL 433
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
84-352 |
4.19e-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: 197.78 E-value: 4.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 84 SVPVGDVTLGRVFNVLGEPIDLQDDIPAEARRdPIHRPAPKFEELATEVEILETGIKVVDLLAPYIKGGKIGLFGGAGVG 163
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERR-PLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 164 KTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYHEMKDSGVISKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDeQ 243
Cdd:cd01136 80 KSTLLGMIARNTDAD---VNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRD-Q 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 244 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTSKGSITSIQAIYVPADDYTDPAPATTFS 323
Cdd:cd01136 156 GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRS 235
|
250 260
....*....|....*....|....*....
gi 496156186 324 HLDATTNLERKLAEMGIYPAVDPLASTSR 352
Cdd:cd01136 236 ILDGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
57-413 |
8.32e-57 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 194.65 E-value: 8.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 57 DTVRTIAMASTDGLIRGMEVVDTGAPISVPVGDVTLGRVFNVLGEPIDlqDDIPAEARRDPIHRPAPKFEELATEVEILE 136
Cdd:PRK06820 71 EMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPID--GGPPLTGQWRELDCPPPSPLTRQPIEQMLT 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 137 TGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYHEMKDSGVISKTAMVFG 216
Cdd:PRK06820 149 TGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCADSAAD---VMVLALIGERGREVREFLEQVLTPEARARTVVVVA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 217 QMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTS 296
Cdd:PRK06820 226 TSDRPALERLKGLSTATTIAEYFRD-RGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSD 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 297 KGSITSIQAIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLASTSRALaPEIVGEEHYQVARRVQQTLQR 376
Cdd:PRK06820 305 RGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLAC 383
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 496156186 377 YKELQDIIAI----LGMDELSDEdklVVHRARRIQFFLSQN 413
Cdd:PRK06820 384 YQEIELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQD 421
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
3-420 |
4.45e-55 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 189.96 E-value: 4.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 3 RGRVIQVMGPVvdvkfenghLPAIYNALKIQH--QARNENEvDIDLTLEVALHLGDDTVRTiAMASTDGLIRGMEVVDTG 80
Cdd:PRK06936 24 RGRVTQVTGTI---------LKAVVPGVRIGElcYLRNPDN-SLSLQAEVIGFAQHQALLT-PLGEMYGISSNTEVSPTG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 81 APISVPVGDVTLGRVFNVLGEPIDlQDDIPAEARRDPIHR--PAPKFEELATEVeiLETGIKVVDLLAPYIKGGKIGLFG 158
Cdd:PRK06936 93 TMHQVGVGEHLLGRVLDGLGQPFD-GGHPPEPAAWYPVYAdaPAPMSRRLIETP--LSLGVRVIDGLLTCGEGQRMGIFA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 159 GAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGND-LYHEMKDSGvISKTAMVFGQMNEPPGARMRVALTGLTMAE 237
Cdd:PRK06936 170 AAGGGKSTLLASLIRSAEVD---VTVLALIGERGREVREfIESDLGEEG-LRKAVLVVATSDRPSMERAKAGFVATSIAE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 238 YFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTSKGSITSIQAIYVPADDYTDPA 317
Cdd:PRK06936 246 YFRD-QGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 318 PATTFSHLDATTNLERKLAEMGIYPAVDPLASTSRALApEIVGEEHYQVARRVQQTLQRYKELQDIIAI----LGMDELS 393
Cdd:PRK06936 325 ADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDKEA 403
|
410 420
....*....|....*....|....*..
gi 496156186 394 DEdklVVHRARRIQFFLSQNFHVAEQF 420
Cdd:PRK06936 404 DQ---AIERIGAIRGFLRQGTHELSHF 427
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
93-413 |
3.15e-53 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 185.20 E-value: 3.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 93 GRVFNVLGEPIDLQDDIPAEARRDPIHRPAPKFEELATEVEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELi 172
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 173 hniAQEHGGISV-FAGVGERTREGNDLYHE-MKDSgvISKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLF 250
Cdd:PRK06002 186 ---ARADAFDTVvIALVGERGREVREFLEDtLADN--LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRD-RGENVLLI 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 251 IDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI--TSTSKGSITSIQAIYVPADDYTDPAPATTFSHLDAT 328
Cdd:PRK06002 260 VDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGH 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 329 TNLERKLAEMGIYPAVDPLASTSRaLAPEIVGEEHYQVARRVQQTLQRYKELQDIIAILGMDELSDED-KLVVHRARRIQ 407
Cdd:PRK06002 340 IVLDRAIAEQGRYPAVDPLASISR-LARHAWTPEQRKLVSRLKSMIARFEETRDLRLIGGYRAGSDPDlDQAVDLVPRIY 418
|
....*.
gi 496156186 408 FFLSQN 413
Cdd:PRK06002 419 EALRQS 424
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
79-420 |
1.71e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 177.61 E-value: 1.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 79 TGAPISVPVGDVTLGRVFNVLGEPIDlQDDIPAEARRDPIHRPAPKFEELATEVEILETGIKVVDLLAPYIKGGKIGLFG 158
Cdd:PRK07721 87 TGKPLEVKVGSGLIGQVLDALGEPLD-GSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 159 GAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYHemKDSGV--ISKTAMVFGQMNEPPGARMRVALTGLTMA 236
Cdd:PRK07721 166 GSGVGKSTLMGMIARNTSAD---LNVIALIGERGREVREFIE--RDLGPegLKRSIVVVATSDQPALMRIKGAYTATAIA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 237 EYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTSKGSITSIQAIYVPADDYTDP 316
Cdd:PRK07721 241 EYFRD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEP 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 317 APATTFSHLDATTNLERKLAEMGIYPAVDPLASTSRaLAPEIVGEEHYQVARRVQQTLQRYKELQDIIAI----LGMDEL 392
Cdd:PRK07721 320 IADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSR-VMNHIVSPEHKEAANRFRELLSTYQNSEDLINIgaykRGSSRE 398
|
330 340
....*....|....*....|....*...
gi 496156186 393 SDEdklVVHRARRIQFFLSQNFHVAEQF 420
Cdd:PRK07721 399 IDE---AIQFYPQIISFLKQGTDEKATF 423
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
64-384 |
2.89e-50 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 176.72 E-value: 2.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 64 MASTDGLIRGMEVVDTGAPISVPVGDVTLGRVFNVLGEpIDLQDDIPAEAR----RDPIHRPAPKFEELATEVEILETGI 139
Cdd:PRK08149 61 IGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGK-IVERFDAPPTVGpiseERVIDVAPPSYAERRPIREPLITGV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 140 KVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYHEMKDSGVISKTAMVFGQMN 219
Cdd:PRK08149 140 RAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHSEAD---VFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 220 EPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTSKGS 299
Cdd:PRK08149 217 FSSVDRCNAALVATTVAEYFRD-QGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 300 ITSIQAIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLASTSRaLAPEIVGEEHYQVARRVQQTLQRYKE 379
Cdd:PRK08149 296 ITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSR-VFGQVTDPKHRQLAAAFRKLLTRLEE 374
|
....*
gi 496156186 380 LQDII 384
Cdd:PRK08149 375 LQLFI 379
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
1-413 |
7.49e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 175.94 E-value: 7.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 1 MTRGRVIQVMGPVVDVKfenghlpAIYNALKIQHQARNENEVDIDLTLEValhLGDDTVRTIAM--ASTDGLIRGMEVVD 78
Cdd:PRK08927 16 VIYGRVVAVRGLLVEVA-------GPIHALSVGARIVVETRGGRPVPCEV---VGFRGDRALLMpfGPLEGVRRGCRAVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 79 TGAPISVPVGDVTLGRVFNVLGEPIDLQDDIPAEARRDPIHRPAPKFEELATEVEILETGIKVVDLLAPYIKGGKIGLFG 158
Cdd:PRK08927 86 ANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 159 GAGVGKTVLIQELIHNIAQEhggISVFAGVGERTRE-----GNDLYHE-MKDSGVISKTAmvfgqmNEPPGARMRVALTG 232
Cdd:PRK08927 166 GSGVGKSVLLSMLARNADAD---VSVIGLIGERGREvqeflQDDLGPEgLARSVVVVATS------DEPALMRRQAAYLT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 233 LTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI--TSTSKGSITSIQAIYVPA 310
Cdd:PRK08927 237 LAIAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 311 DDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLASTSRALaPEIVGEEHYQVARRVQQTLQRYKELQDIIAI---- 386
Cdd:PRK08927 316 DDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRLgayr 394
|
410 420
....*....|....*....|....*..
gi 496156186 387 LGMDELSDEdklVVHRARRIQFFLSQN 413
Cdd:PRK08927 395 AGSDPEVDE---AIRLNPALEAFLRQG 418
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
83-441 |
1.59e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 174.87 E-value: 1.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 83 ISVPVGDVTLGRVFNVLGEPIDLQDDIPAEaRRDPIHRPAPKFEELATEVEILETGIKVVDLLAPYIKGGKIGLFGGAGV 162
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYE-RYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 163 GKTVLIQELIHN-IAQehggISVFAGVGERTREGNDLYHEMKDsGVISKTAMVFGQMNEPPGARMRVALTGLTMAEYFRD 241
Cdd:PRK08472 169 GKSTLMGMIVKGcLAP----IKVVALIGERGREIPEFIEKNLG-GDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 242 eQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITST-SKGSITSIQAIYVPADDYTDPAPAT 320
Cdd:PRK08472 244 -QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEeGKGSITAFFTVLVEGDDMSDPIADQ 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 321 TFSHLDATTNLERKLAEMGIYPAVDPLASTSRaLAPEIVGEEHYQVARRVQQTLQRYKELQDIIAI----LGMDELSDEd 396
Cdd:PRK08472 323 SRSILDGHIVLSRELTDFGIYPPINILNSASR-VMNDIISPEHKLAARKFKRLYSLLKENEVLIRIgayqKGNDKELDE- 400
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 496156186 397 klVVHRARRIQFFLSQNFHvaEQFtgqpgsyvPVKETVRGFKEIL 441
Cdd:PRK08472 401 --AISKKEFMEQFLKQNPN--ELF--------PFEQTFEQLEEIL 433
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
69-386 |
3.43e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 168.73 E-value: 3.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 69 GLIRGMEVVDTGAPISVPVGDVTLGRVFNVLGEPIDLQDDIPAEARrdpIHRPAPKFEELATEV--EILETGIKVVDLLA 146
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQR---ASRHSPPINPLSRRPitEPLDVGVRAINAML 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 147 PYIKGGKIGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYHEMKDSGVISKTAMVFGQMNEPPGARM 226
Cdd:PRK08972 158 TVGKGQRMGLFAGSGVGKSVLLGMMTRGTTAD---VIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 227 RVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTS--KGSITSIQ 304
Cdd:PRK08972 235 KGCETATTIAEYFRD-QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGpgQGSITAFY 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 305 AIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLASTSRaLAPEIVGEEHYQVARRVQQTLQRYKELQDII 384
Cdd:PRK08972 314 TVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISR-VMPMVISEEHLEAMRRVKQVYSLYQQNRDLI 392
|
..
gi 496156186 385 AI 386
Cdd:PRK08972 393 SI 394
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
56-386 |
6.86e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 168.37 E-value: 6.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 56 DDTVRTIAMASTDGLIRGMEVVDTGAPISVPVGDVTLGRVFNVLGEPIDLQDDIPAEAR------------RDPIHRPap 123
Cdd:PRK05688 74 GDKVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWvpmdgptinplnRHPISEP-- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 124 kfeelateveiLETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYHEMK 203
Cdd:PRK05688 152 -----------LDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEAD---IIVVGLIGERGREVKEFIEHIL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 204 DSGVISKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLAT 283
Cdd:PRK05688 218 GEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRD-KGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 284 EMGQLQERITSTSKG--SITSIQAIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLASTSRALaPEIVGE 361
Cdd:PRK05688 297 KLPKLVERAGNAEPGggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDP 375
|
330 340
....*....|....*....|....*
gi 496156186 362 EHYQVARRVQQTLQRYKELQDIIAI 386
Cdd:PRK05688 376 EHLRRAQRFKQLWSRYQQSRDLISV 400
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
66-395 |
6.06e-46 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 165.51 E-value: 6.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 66 STDGLIRGMEVVDTGAPISVPVGDVTLGRVFNVLGEPIDLQDDI-----------PAEARRDPIHRPapkfeelatevei 134
Cdd:PRK07594 72 STIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRELPdvcwkdydampPPAMVRQPITQP------------- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 135 LETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELIhniAQEHGGISVFAGVGERTREGNDLYHEMKDSGVISKTAMV 214
Cdd:PRK07594 139 LMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLC---NAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 215 FGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITS 294
Cdd:PRK07594 216 VATSDRPALERVRALFVATTIAEFFRD-NGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGM 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 295 TSKGSITSIQAIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLASTSRALaPEIVGEEHYQVARRVQQTL 374
Cdd:PRK07594 295 GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCL 373
|
330 340
....*....|....*....|....*
gi 496156186 375 QRYKELQDIIAI----LGMDELSDE 395
Cdd:PRK07594 374 ALYQEVELLIRIgeyqRGVDTDTDK 398
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
68-412 |
2.82e-45 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 163.79 E-value: 2.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 68 DGLIRGMEVVDTGAPISVPVGDVTLGRVFNVLGEPIDLQDDIPAEARRDPIHRPAPKFEELATEVEiLETGIKVVDLLAP 147
Cdd:PRK09099 81 GGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAP-LPTGVRIVDGLMT 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 148 YIKGGKIGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYHEMKDSGVISKTAMVFGQMNEPPGARMR 227
Cdd:PRK09099 160 LGEGQRMGIFAPAGVGKSTLMGMFARGTQCD---VNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 228 VALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTSKGSITSIQAIY 307
Cdd:PRK09099 237 AAYVATAIAEYFRD-RGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 308 VPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLASTSRALaPEIVGEEHYQVARRVQQTLQRYKELQDIIAI- 386
Cdd:PRK09099 316 AEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVg 394
|
330 340
....*....|....*....|....*....
gi 496156186 387 ---LGMDELSDEdklVVHRARRIQFFLSQ 412
Cdd:PRK09099 395 eyrAGSDPVADE---AIAKIDAIRDFLSQ 420
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
67-412 |
9.23e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 162.07 E-value: 9.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 67 TDGLIRGMEVVDTGAPISVPVGDVTLGRVFN----VLGEP---IDLQDdIPAEArrDPIHrpAPKFEELAtevEILETGI 139
Cdd:PRK06793 73 TEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSangeVLNEEaenIPLQK-IKLDA--PPIH--AFEREEIT---DVFETGI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 140 KVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGND-LYHEMKDSGvISKTAMVFGQM 218
Cdd:PRK06793 145 KSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKAD---INVISLVGERGREVKDfIRKELGEEG-MRKSVVVVATS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 219 NEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAvGYQPTLATEMGQLQERITSTSKG 298
Cdd:PRK06793 221 DESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQKG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 299 SITSIQAIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLASTSRALApEIVGEEHYQVARRVQQTLQRYK 378
Cdd:PRK06793 299 SITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPNHWQLANEMRKILSIYK 377
|
330 340 350
....*....|....*....|....*....|....*..
gi 496156186 379 ElQDIIAILGMDELSDEDKLVVHRARRIQF---FLSQ 412
Cdd:PRK06793 378 E-NELYFKLGTIQENAENAYIFECKNKVEGintFLKQ 413
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
69-413 |
4.00e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 157.75 E-value: 4.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 69 GLIRGMEVVDTGAPISVPVGDVTLGRVFNVLGEPID----LQDDIPAEARRDPIH----RPAPkfeelatevEILETGIK 140
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDgkgqLGGSTPLQQQLPQIHplqrRAVD---------TPLDVGVN 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 141 VVDLLAPYIKGGKIGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLY-HEMKDSGvISKTAMVFGQMN 219
Cdd:PRK07196 145 AINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQAD---VVVVGLIGERGREVKEFIeHSLQAAG-MAKSVVVAAPAD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 220 EPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI-TSTSKG 298
Cdd:PRK07196 221 ESPLMRIKATELCHAIATYYRD-KGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 299 SITSIQAIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLASTSRALApEIVGEEHYQVARRVQQTLQRYK 378
Cdd:PRK07196 300 TMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYM 378
|
330 340 350
....*....|....*....|....*....|....*....
gi 496156186 379 ELQDIIA----ILGMDELSDEdklVVHRARRIQFFLSQN 413
Cdd:PRK07196 379 AIKPLIPlggyVAGADPMADQ---AVHYYPAITQFLRQE 414
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
50-448 |
1.73e-37 |
|
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: 143.30 E-value: 1.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 50 VALHLGDDTVRTIAMASTDGLIRGMEVVDTGAPISVPVGDVTLGRVFNVLGEPIDLQDDIPAEARRdPIHRPAPKFEELA 129
Cdd:TIGR00962 61 IALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFS-PVEKIAPGVIERK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 130 TEVEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELIHNIAQEHgGISVFAGVGERTREGNDLYHEMKDSGVIS 209
Cdd:TIGR00962 140 SVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTIINQKDSD-VYCIYVAIGQKASTVAQVVRKLEEHGAMA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 210 KTAMVFGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQ 289
Cdd:TIGR00962 219 YTIVVAATASDSASLQYLAPYTGCTMGEYFRD-NGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 290 ERITSTS----KGSITSIQAIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLASTSRalapeiVG----- 360
Cdd:TIGR00962 298 ERAAKLNdekgGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSR------VGgaaqi 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 361 EEHYQVARRVQQTLQRYKELqDIIAILGMDeLSDEDKLVVHRARRIQFFLSQ-NFH---VAEQ----FTGQPG--SYVPV 430
Cdd:TIGR00962 372 KAMKQVAGSLRLELAQYREL-EAFSQFASD-LDEATKKQLERGQRVVELLKQpQYKplsVEEQvvilFAGTKGylDDIPV 449
|
410
....*....|....*...
gi 496156186 431 KEtVRGFKEILdgkYDHL 448
Cdd:TIGR00962 450 DK-IRKFEQAL---LAYL 463
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
4-83 |
2.43e-37 |
|
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: 131.10 E-value: 2.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 4 GRVIQVMGPVVDVKFENGHLPAIYNALKIQhqarneNEVDIDLTLEVALHLGDDTVRTIAMASTDGLIRGMEVVDTGAPI 83
Cdd:cd18115 3 GKIVQVIGPVVDVEFPEGELPPIYNALEVK------GDDGKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
73-442 |
5.44e-37 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 140.81 E-value: 5.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 73 GMEVVDTGAPISVPVGDVTLGRVFNVLGEPIDLQDDIPaEARRDPIHRPAPKFEELATEVEILETGIKVVDLLAPYIKGG 152
Cdd:PRK05922 80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLP-KTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQ 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 153 KIGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYHEMKDSGVISKTAMVFGQMNEPPGARMRVALTG 232
Cdd:PRK05922 159 RIGVFSEPGSGKSSLLSTIAKGSKST---INVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 233 LTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTSKGSITSIQAI-YVP-- 309
Cdd:PRK05922 236 MTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIlHYPnh 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 310 ADDYTDPAPATTFSHLdATTNLERKLAEmgiyPAVDPLASTSRAlAPEIVGEEHYQVARRVQQTLQRYKELQDIIAILGM 389
Cdd:PRK05922 315 PDIFTDYLKSLLDGHF-FLTPQGKALAS----PPIDILTSLSRS-ARQLALPHHYAAAEELRSLLKAYHEALDIIQLGAY 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 496156186 390 DELSDEDklvVHRARRIqfflsqnFHVAEQFTGQP-GSYVPVKETVRGFKEILD 442
Cdd:PRK05922 389 VPGQDAH---LDRAVKL-------LPSIKQFLSQPlSSYCALHNTLKQLEALLK 432
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
66-415 |
9.54e-37 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 140.73 E-value: 9.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 66 STDGL-IRGMEVVDTGAPISVPVGDVTLGRVFNVLGEPIDLQDDIPAEARRD-------PIHRPAPKfeelatevEILET 137
Cdd:PRK04196 58 GTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDingapinPVAREYPE--------EFIQT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 138 GIKVVDLLAPYIKGGKIGLFGGAGvgktvliqeLIHN-----IAQ-------EHGGISVFAGVGERTREGNDLYHEMKDS 205
Cdd:PRK04196 130 GISAIDGLNTLVRGQKLPIFSGSG---------LPHNelaaqIARqakvlgeEENFAVVFAAMGITFEEANFFMEDFEET 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 206 GVISKTAMVFGQMNEPPGARM---RVAltgLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLA 282
Cdd:PRK04196 201 GALERSVVFLNLADDPAIERIltpRMA---LTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMY 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 283 TEMGQLQER--ITSTSKGSITSIQAIYVPADDYTDPAPattfshlDAT---TN----LERKLAEMGIYPAVDPLASTSRa 353
Cdd:PRK04196 278 TDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyiTEgqivLSRELHRKGIYPPIDVLPSLSR- 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496156186 354 LAPEIVG-----EEHYQVARRVQQTLQRYKELQDIIAILGMDELSDEDKLVVHRARRI-QFFLSQNFH 415
Cdd:PRK04196 350 LMKDGIGegktrEDHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFeREFVNQGFD 417
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
85-386 |
3.88e-35 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 136.07 E-value: 3.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 85 VPVGDVTLGRVFNVLGEPIDlqdDIPA--EARRDPIHrpAPKFEELA-TEVE-ILETGIKVVDLLAPYIKGGKIGLFGGA 160
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLD---GLPApdTGETGALI--TPPFNPLQrTPIEhVLDTGVRAINALLTVGRGQRMGLFAGS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 161 GVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYHEMKDSGVISKTAMVFGQMNEPPGARMRVALTGLTMAEYFR 240
Cdd:PRK07960 185 GVGKSVLLGMMARYTQAD---VIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFR 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 241 DeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITS--TSKGSITSIQAIYVPADDYTDPAP 318
Cdd:PRK07960 262 D-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQDPIA 340
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496156186 319 ATTFSHLDATTNLERKLAEMGIYPAVDPLASTSRALApEIVGEEHYQVARRVQQTLQRYKELQDIIAI 386
Cdd:PRK07960 341 DSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMT-ALIDEQHYARVRQFKQLLSSFQRNRDLVSV 407
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
82-352 |
1.08e-34 |
|
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: 130.81 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 82 PISVPVGDVTLGRVFNVLGEPIDLQDDIPAEARRD-------PIHRPAPKfeelatevEILETGIKVVDLLAPYIKGGKI 154
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDingppinPVARIYPE--------EMIQTGISAIDVMNTLVRGQKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 155 GLFGGAGvgktvliqeLIHN-----IA-------QEHGGISVFAGVGERTREGNDLYHEMKDSGVISKTAMVFGQMNEPP 222
Cdd:cd01135 73 PIFSGSG---------LPHNelaaqIArqagvvgSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 223 GARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQER--ITSTSKGSI 300
Cdd:cd01135 144 IERIITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSI 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 496156186 301 TSIQAIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLASTSR 352
Cdd:cd01135 224 TQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
50-472 |
4.09e-34 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 133.89 E-value: 4.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 50 VALHLGDDTVRTIAMASTDGLIRGMEVVDTGAPISVPVGDVTLGRVFNVLGEPIDLQDDIPAEARRdPIHRPAPKFEELA 129
Cdd:PRK13343 62 FAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARR-PLERPAPAIIERD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 130 TEVEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELIhnIAQEHGG-ISVFAGVGERTREGNDLYHEMKDSGVI 208
Cdd:PRK13343 141 FVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAI--INQKDSDvICVYVAIGQKASAVARVIETLREHGAL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 209 SKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQL 288
Cdd:PRK13343 219 EYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 289 QERITSTSK----GSITSIQAIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLASTSR----ALAPEIvg 360
Cdd:PRK13343 298 LERAAKLSPelggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRvggkAQHPAI-- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 361 eehYQVARRVQQTLQRYKELQdIIAILGMDeLSDEDKLVVHRARRIQFFLSQNFH----VAEQ----FTGQPGSYVPVK- 431
Cdd:PRK13343 376 ---RKESGRLRLDYAQFLELE-AFTRFGGL-LDAGTQKQITRGRRLRELLKQPRFsplsVEEQiallYALNEGLLDAVPl 450
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 496156186 432 ETVRGFKEILDGKYDHLPEDAFRLVGRIEEVVEKAKAMGVE 472
Cdd:PRK13343 451 ANIQAFEERLLEKLDARFAALSLALESPRELDEAWLAALEE 491
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
82-352 |
2.04e-32 |
|
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: 124.99 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 82 PISVPVGDVTLGRVFNVLGEPIDLQDD-----IP--AEARRDPIHRPAPKFEELATEvEILETGIKVVDLLAPYIKGGKI 154
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAEtgsifIPrgVNVQRWPVRQPRPVKEKLPPN-VPLLTGQRVLDTLFPVAKGGTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 155 GLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERtreGND----------LYHEMKDSGVISKTAMVFGQMNEPPGA 224
Cdd:cd01134 80 AIPGPFGCGKTVISQSLSKWSNSD---VVIYVGCGER---GNEmaevleefpeLKDPITGESLMERTVLIANTSNMPVAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 225 RMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI-------TSTSK 297
Cdd:cd01134 154 REASIYTGITIAEYFRD-MGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrclgSPGRE 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 496156186 298 GSITSIQAIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLASTSR 352
Cdd:cd01134 233 GSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
117-442 |
1.84e-31 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 127.21 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 117 PIHRPAPKFEELaTEVEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGN 196
Cdd:PRK04192 194 PVRRPRPYKEKL-PPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQLAKWADAD---IVIYVGCGERGNEMT 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 197 DLYHE---MKD--SG--VISKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLG 269
Cdd:PRK04192 270 EVLEEfpeLIDpkTGrpLMERTVLIANTSNMPVAAREASIYTGITIAEYYRD-MGYDVLLMADSTSRWAEALREISGRLE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 270 RMPSAVGYQPTLATEMGQLQER----IT-STSKGSITSIQAIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAV 344
Cdd:PRK04192 349 EMPGEEGYPAYLASRLAEFYERagrvKTlGGEEGSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 345 DPLASTSR---ALAP---EIVGEEHYQVARRVQQTLQRYKELQDIIAILGMDELSDEDKLVVHRARRIQF-FLSQN-FHV 416
Cdd:PRK04192 429 NWLTSYSLyldQVAPwweENVDPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARLIREdFLQQNaFDP 508
|
330 340
....*....|....*....|....*.
gi 496156186 417 AEqftgqpgSYVPVKETVRGFKEILD 442
Cdd:PRK04192 509 VD-------TYCPPEKQYEMLKLILT 527
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
50-398 |
2.23e-26 |
|
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: 111.35 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 50 VALHLGDDTVRTIAMASTDG------LIRGMEVVD--------TGAPISVPVGDVTLGRVFNVLGEPIDLQDDIPAEARR 115
Cdd:TIGR01040 27 VNLTLPDGTVRSGQVLEVSGnkavvqVFEGTSGIDakkttcefTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 116 DPIHRPAPKFEELATEvEILETGIKVVDLLAPYIKGGKIGLFGGAGV-------------GKTVLIQELIHNIAQEHGGI 182
Cdd:TIGR01040 107 DINGQPINPYARIYPE-EMIQTGISAIDVMNSIARGQKIPIFSAAGLphneiaaqicrqaGLVKLPTKDVHDGHEDNFAI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 183 sVFAGVGERTREGNDLYHEMKDSGVISKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGS 262
Cdd:TIGR01040 186 -VFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 263 EVSALLGRMPSAVGYQPTLATEMGQLQERI--TSTSKGSITSIQAIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGI 340
Cdd:TIGR01040 265 EVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQI 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496156186 341 YPAVDPLASTSRaLAPEIVGE-----EHYQVARRVQQTLQRYKELQDIIAILGMDELSDEDKL 398
Cdd:TIGR01040 345 YPPINVLPSLSR-LMKSAIGEgmtrkDHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLL 406
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
83-352 |
1.30e-25 |
|
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: 105.72 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 83 ISVPVGDVTLGRVFNVLGEPIDLQDDIPAEARRdPIHRPAPKFEELATEVEILETGIKVVDLLAPYIKGGKIGLFGGAGV 162
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERR-RVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 163 GKTVLIQELIHNiAQEHGGISVFAGVGERTREGNDLYHEMKDSGVISKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDe 242
Cdd:cd01132 81 GKTAIAIDTIIN-QKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRD- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 243 QGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTSK----GSITSIQAIYVPADDYTDPAP 318
Cdd:cd01132 159 NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGSLTALPIIETQAGDVSAYIP 238
|
250 260 270
....*....|....*....|....*....|....
gi 496156186 319 ATTFSHLDATTNLERKLAEMGIYPAVDPLASTSR 352
Cdd:cd01132 239 TNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
171-407 |
1.65e-22 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 101.25 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 171 LIHNIAQEH-------GGISVFAGVGERTREGNDLYHE---MKDSG----VISKTAMVFGQMNEPPGARMRVALTGLTMA 236
Cdd:PRK14698 666 LLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEfpkLKDPKtgkpLMERTVLIANTSNMPVAAREASIYTGITIA 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 237 EYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQER----ITSTSK---GSITSIQAIYVP 309
Cdd:PRK14698 746 EYFRD-MGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERagrvVTLGSDyrvGSVSVIGAVSPP 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 310 ADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLASTSRALAP------EIVGEEHYQVARRVQQTLQRYKELQDI 383
Cdd:PRK14698 825 GGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAvkdwwhKNVDPEWKAMRDKAMELLQKEAELQEI 904
|
250 260
....*....|....*....|....
gi 496156186 384 IAILGMDELSDEDKLVVHRARRIQ 407
Cdd:PRK14698 905 VRIVGPDALPERERAILLVARMLR 928
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
52-321 |
2.38e-22 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 98.95 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 52 LHLGDDTVRTIAMASTDGLIRGMEVVDTGAPISVPVGDVTLGRVFNVLGEPID-----LQDDIP-AEARRDPIHRPAPKf 125
Cdd:PRK02118 43 IRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDggpelEGEPIEiGGPSVNPVKRIVPR- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 126 eelatevEILETGIKVVDLLAPYIKGGKIGLFGGAGVGktvlIQELIHNIA-QEHGGISVFAGVGERTREGNDLYHEMKD 204
Cdd:PRK02118 122 -------EMIRTGIPMIDVFNTLVESQKIPIFSVSGEP----YNALLARIAlQAEADIIILGGMGLTFDDYLFFKDTFEN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 205 SGVISKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATE 284
Cdd:PRK02118 191 AGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSD 270
|
250 260 270
....*....|....*....|....*....|....*...
gi 496156186 285 MGQLQERITSTSK-GSITSIQAIYVPADDYTDPAPATT 321
Cdd:PRK02118 271 LASRYEKAVDFEDgGSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
50-272 |
1.29e-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: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 50 VALHLGDDTVRTIAMASTDGLIRGMEVVDTGAPISVPVGDVTLGRVFNVLGEPIDLQDDIPAEARRdPIHRPAPKFEELA 129
Cdd:COG0056 62 MALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERR-PVERPAPGVIDRQ 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 130 TEVEILETGIKVVDLLAPyikggkIG------LFGGAGVGKTVLIQELIhnIAQEHGG-ISVFAGVGERTREGNDLYHEM 202
Cdd:COG0056 141 PVHEPLQTGIKAIDAMIP------IGrgqrelIIGDRQTGKTAIAIDTI--INQKGKDvICIYVAIGQKASTVAQVVETL 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 203 KDSGVISKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMP 272
Cdd:COG0056 213 EEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMD-QGKDVLIVYDDLSKHAVAYRELSLLLRRPP 281
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
47-272 |
2.50e-20 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 93.59 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 47 TLEVALHLGDDTVRTIAMASTDGLIRGMEVVDTGAPISVPVGDVTLGRVFNVLGEPIDLQDDIPAEARRdPIHRPAPKFE 126
Cdd:PRK09281 59 VYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETR-PVERKAPGVI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 127 ELATEVEILETGIKVVDLLAPyikggkIG------LFGGAGVGKTVLIQELIhnIAQEHGGI-----------SVFAGVG 189
Cdd:PRK09281 138 DRKSVHEPLQTGIKAIDAMIP------IGrgqrelIIGDRQTGKTAIAIDTI--INQKGKDViciyvaigqkaSTVAQVV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 190 ERTREgndlYHEMKDSGVISKTAmvfgqmNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLG 269
Cdd:PRK09281 210 RKLEE----HGAMEYTIVVAATA------SDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQLSLLLR 278
|
...
gi 496156186 270 RMP 272
Cdd:PRK09281 279 RPP 281
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
6-80 |
2.81e-20 |
|
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: 84.52 E-value: 2.81e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496156186 6 VIQVMGPVVDVKFENGHLPAIYNALKIQHQArnenevDIDLTLEVALHLGDDTVRTIAMASTDGLIRGMEVVDTG 80
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVE------FGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
45-381 |
1.13e-18 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 88.48 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 45 DLTLEVALHLGDDTVRTIAMASTDGLIRGMEVVDTGAPISVPVGDVTLGRVFNVLGEPIDLQDDIPAEARRdPIHRPAPK 124
Cdd:CHL00059 36 DGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESR-LIESPAPG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 125 FEELATEVEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELIHNiAQEHGGISVFAGVGERTREGNDLYHEMKD 204
Cdd:CHL00059 115 IISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN-QKGQNVICVYVAIGQKASSVAQVVTTLQE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 205 SGVISKTAMVFGQMNEPPGARMRVALTGLTMAEYFRdEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATE 284
Cdd:CHL00059 194 RGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 285 MGQLQERITSTSK----GSITSIQAIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLASTSRalapeiVG 360
Cdd:CHL00059 273 HSRLLERAAKLSSqlgeGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSR------VG 346
|
330 340
....*....|....*....|....*.
gi 496156186 361 -----EEHYQVARRVQQTLQRYKELQ 381
Cdd:CHL00059 347 saaqiKAMKQVAGKLKLELAQFAELE 372
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
363-432 |
7.19e-18 |
|
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: 77.87 E-value: 7.19e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 363 HYQVARRVQQTLQRYKELQDIIAILGMDELSDEDKLVVHRARRIQFFLSQNFHVAEQFTGQPGSYVPVKE 432
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
56-352 |
4.54e-15 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 77.39 E-value: 4.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 56 DDTVRTIAMASTDGLIRGMEVVDTGAPISVPVGDVTLGRVFNVLGE--PIDL----QDDIPAEARRDPIHRPAPKFEELA 129
Cdd:PTZ00185 88 DGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHevPVGLltrsRALLESEQTLGKVDAGAPNIVSRS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 130 TEVEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELIHN-------IAQEHGGISVFAGVGERTREGNDLYHEM 202
Cdd:PTZ00185 168 PVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINqvrinqqILSKNAVISIYVSIGQRCSNVARIHRLL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 203 KDSGVISKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLA 282
Cdd:PTZ00185 248 RSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMN-RGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVF 326
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496156186 283 TEMGQLQERITSTSK----GSITSIQAIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLASTSR 352
Cdd:PTZ00185 327 YLHSRLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSR 400
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
3-81 |
4.64e-14 |
|
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: 66.95 E-value: 4.64e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496156186 3 RGRVIQVMGPVVDVKFENGhlPAIYNALKIQHQARNEnevDIDLTLEVALHLGDdTVRTIAMASTDGLIRGMEVVDTGA 81
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGE--VAIGEVCEIERGDGNN---ETVLKAEVIGFRGD-RAILQLFESTRGLSRGALVEPTGR 73
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
88-352 |
2.59e-11 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 65.11 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 88 GDVTLGRVFNVLGEPidlqddiPAEARRdpihrpAPKFEELA----TEVEILETG-----IKVVDLLAPYIKGGKIGLFG 158
Cdd:PRK12608 74 RYRVLVRVDSVNGTD-------PEKLAR------RPHFDDLTplhpRERLRLETGsddlsMRVVDLVAPIGKGQRGLIVA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 159 GAGVGKTVLIQELIHNIAQEHGGISVFAG-VGERTREGNDLYHEMKdsgvisktAMVFGQMNEPPGARmRVALTGLTMAE 237
Cdd:PRK12608 141 PPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDMRRSVK--------GEVYASTFDRPPDE-HIRVAELVLER 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 238 YFRD-EQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAvgyqpTLATEMGQLQERITSTSK-----GSITSIQAIYVP-- 309
Cdd:PRK12608 212 AKRLvEQGKDVVILLDSLTRLARAYNNEVESSGRTLSG-----GVDARALQRPKRLFGAARnieegGSLTIIATALVDtg 286
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 496156186 310 --ADDYTdpapattFSHLDATTNLE----RKLAEMGIYPAVDPLASTSR 352
Cdd:PRK12608 287 srMDEVI-------FEEFKGTGNMEivldRELADKRVFPAIDIAKSGTR 328
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
140-352 |
1.88e-08 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 55.29 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 140 KVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAG-VGERTREGNDlyheMKDSG---VISKTamvf 215
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRSVkgeVVAST---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 216 gqMNEPPGARMRVALTGLTMAEYfRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAvGYQPTLAtemgQLQERITST 295
Cdd:cd01128 77 --FDEPPERHVQVAEMVIEKAKR-LVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSG-GVDANAL----HKPKRFFGA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496156186 296 SK-----GSITSIQAIYVpaddytdpapaTTFSHLD--------ATTNLE----RKLAEMGIYPAVDPLASTSR 352
Cdd:cd01128 149 ARnieegGSLTIIATALV-----------DTGSRMDevifeefkGTGNMElvldRKLAEKRIFPAIDILKSGTR 211
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
107-352 |
1.55e-07 |
|
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: 53.54 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 107 DDIPAEARRDPIhrpapkFEEL----ATEVEILETG-----IKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELIHNIAQ 177
Cdd:TIGR00767 121 GDDPEKAKNRVL------FENLtplyPNERLRLETStedlsTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITR 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 178 EHGGISVFAG-VGERTREGNDLYHEMKDSgVISKTamvfgqMNEPPGARMRVALTGLTMAEYfRDEQGQDVLLFIDNIFR 256
Cdd:TIGR00767 195 NHPEVELIVLlIDERPEEVTDMQRSVKGE-VVAST------FDEPASRHVQVAEMVIEKAKR-LVEHKKDVVILLDSITR 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 257 FTQAGSEVSALLGRMPSAvGYQPTLAtemgQLQERITSTSK-----GSITSIQAIYVPADDYTDpapATTFSHLDATTNL 331
Cdd:TIGR00767 267 LARAYNTVTPASGKVLSG-GVDANAL----HRPKRFFGAARnieegGSLTIIATALIDTGSRMD---EVIFEEFKGTGNM 338
|
250 260
....*....|....*....|....*
gi 496156186 332 E----RKLAEMGIYPAVDPLASTSR 352
Cdd:TIGR00767 339 ElhldRKLADRRIFPAIDIKKSGTR 363
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
150-271 |
2.43e-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: 47.37 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 150 KGGKIGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYHEMKDSGVISKTamvfgqmnepPGARMRVA 229
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS----------GELRLRLA 70
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 496156186 230 ltgLTMAEYFRDEqgqdvLLFIDNIFRFTQAGSEVSALLGRM 271
Cdd:smart00382 71 ---LALARKLKPD-----VLILDEITSLLDAEQEALLLLLEE 104
|
|
| 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 ... |
368-442 |
3.34e-06 |
|
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: 45.46 E-value: 3.34e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496156186 368 RRVQQTLQRYKELQDIIAILGMDELSDEDKLVVHRARRI-QFFLSQN-FHVAEqftgqpgSYVPVKETVRGFKEILD 442
Cdd:cd18111 6 TEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIrEDFLQQNaFDEVD-------TYCPLEKQYKMLKLILT 75
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
110-352 |
9.35e-06 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 47.83 E-value: 9.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 110 PAEARrdpiHRPApkFEEL----ATEVEILETGI------KVVDLLAPYIKG--GKIglfggagV-----GKTVLIQELI 172
Cdd:PRK09376 124 PEKAR----NRPL--FENLtplyPNERLRLETGNpedlstRIIDLIAPIGKGqrGLI-------VappkaGKTVLLQNIA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 173 HNIAQEHGGISVFAG-VGERTREGNDlyheMKDS---GVISKTamvfgqMNEPPGARMRVALTGLTMAEyfRD-EQGQDV 247
Cdd:PRK09376 191 NSITTNHPEVHLIVLlIDERPEEVTD----MQRSvkgEVVAST------FDEPAERHVQVAEMVIEKAK--RLvEHGKDV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 248 LLFIDNIFRFTQAGSEVSALLGRM------PSAVgYQPT------LATEMGqlqeritstskGSITSIqaiyvpaddytd 315
Cdd:PRK09376 259 VILLDSITRLARAYNTVVPSSGKVlsggvdANAL-HRPKrffgaaRNIEEG-----------GSLTII------------ 314
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 496156186 316 papAT----TFSHLD--------ATTN----LERKLAEMGIYPAVDPLASTSR 352
Cdd:PRK09376 315 ---ATalidTGSRMDevifeefkGTGNmelhLDRKLAEKRIFPAIDINRSGTR 364
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
359-415 |
1.27e-03 |
|
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family of ATPases that form part of the Type III secretion system (T3SS) present in Escherichia coli. T3SS is a macromolecular complex that creates a syringe-like apparatus extending from the bacterial cytosol across three membranes to the eukaryotic cytosol. This process is essential for pathogenicity. EscN is a functionally unique ATPase that provides an inner-membrane recognition gate for the T3SS chaperone-virulence effector complexes as well as a potential source of energy for their subsequent secretion.The C-terminal domain of T3SS ATPases mediates binding with multiple contact points along the chaperone.
Pssm-ID: 465691 [Multi-domain] Cd Length: 70 Bit Score: 37.41 E-value: 1.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496156186 359 VGEEHYQVARRVQQTLQRYKELQDIIAI----LGMDELSDEdklVVHRARRIQFFLSQNFH 415
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIgayqAGSDPEIDE---AIAKRPAINAFLRQGVD 58
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
114-204 |
3.59e-03 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 40.01 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496156186 114 RRDPIHRPAPKFEELATEVEILeTGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELIhnIAQEHGGISV------FAG 187
Cdd:PRK14698 191 QRWPVRVKRPYKEKLPPEVPLI-TGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDGDTLI--LTKEFGLIKIkdlyeiLDG 267
|
90
....*....|....*..
gi 496156186 188 VGERTREGNDLYHEMKD 204
Cdd:PRK14698 268 KGKKTVEGNEEWTELEE 284
|
|
| ATP-synt_V_A-type_beta_C |
cd18112 |
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 ... |
378-415 |
5.03e-03 |
|
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 complexes 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. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 349747 [Multi-domain] Cd Length: 95 Bit Score: 36.26 E-value: 5.03e-03
10 20 30
....*....|....*....|....*....|....*....
gi 496156186 378 KELQDIIAILGMDELSDEDKLVVHRARRI-QFFLSQNFH 415
Cdd:cd18112 22 KDVRALAAIVGEEALSEEDRLYLEFADRFeREFINQGFY 60
|
|
| |
