|
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: 981.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 1 MGIGRVTQVMGPVIDVRFEHNEVPEINNALHIEVPKEDgalQLTLEVALQLGDDVVRTIAMDSTDGVQRGMEVKDTGRDI 80
Cdd:COG0055 3 MNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEGGG---ELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 81 SVPVGDVTLGRVFNVLGETIDLDEKIDDSVRRdPIHRQAPGFDELSTKVEILETGIKVVDLLAPYIKGGKIGLFGGAGVG 160
Cdd:COG0055 80 SVPVGEATLGRIFNVLGEPIDGKGPIEAKERR-PIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 161 KTVLIQELINNIAQEHGGISVFAGVGERTREGNDLYYEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDEE 240
Cdd:COG0055 159 KTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 241 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERISSTNKGSVTSIQAVFVPADDYTDPAPATTFA 320
Cdd:COG0055 239 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 321 HLDSTTNLERKLTEMGIYPAVDPLASTSRALEPSVVGQEHYDVAREVQSTLQKYRELQDIIAILGMDELSDEDKQTVERA 400
Cdd:COG0055 319 HLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 401 RRIQFFLSQNFHVAEQFTGQKGSYVPVKTTVADFRDILDGKYDHIPEDAFRLVGSMEDVIEKAKDMGVEV 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: 883.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 3 IGRVTQVMGPVIDVRFEHNEVPEINNALHIEVPKEDgalQLTLEVALQLGDDVVRTIAMDSTDGVQRGMEVKDTGRDISV 82
Cdd:TIGR01039 2 KGKVVQVIGPVVDVEFEQGELPRIYNALKVQNRAES---ELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 83 PVGDVTLGRVFNVLGETIDLDEKIDDSvRRDPIHRQAPGFDELSTKVEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKT 162
Cdd:TIGR01039 79 PVGKETLGRIFNVLGEPIDEKGPIPAK-ERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 163 VLIQELINNIAQEHGGISVFAGVGERTREGNDLYYEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDEEGQ 242
Cdd:TIGR01039 158 VLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 243 DVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERISSTNKGSVTSIQAVFVPADDYTDPAPATTFAHL 322
Cdd:TIGR01039 238 DVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 323 DSTTNLERKLTEMGIYPAVDPLASTSRALEPSVVGQEHYDVAREVQSTLQKYRELQDIIAILGMDELSDEDKQTVERARR 402
Cdd:TIGR01039 318 DATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487747832 403 IQFFLSQNFHVAEQFTGQKGSYVPVKTTVADFRDILDGKYDHIPEDAFRLVGSMEDVIEKAKDM 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: 781.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 3 IGRVTQVMGPVIDVRFEHNEVPEINNALHIEVPKEDGA-LQLTLEVALQLGDDVVRTIAMDSTDGVQRGMEVKDTGRDIS 81
Cdd:CHL00060 16 LGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQeINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 82 VPVGDVTLGRVFNVLGETIDLDEKIDDSVRRdPIHRQAPGFDELSTKVEILETGIKVVDLLAPYIKGGKIGLFGGAGVGK 161
Cdd:CHL00060 96 VPVGGATLGRIFNVLGEPVDNLGPVDTRTTS-PIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 162 TVLIQELINNIAQEHGGISVFAGVGERTREGNDLYYEMSDSGVI-------KKTAMVFGQMNEPPGARMRVALSGLTMAE 234
Cdd:CHL00060 175 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVIneqniaeSKVALVYGQMNEPPGARMRVGLTALTMAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 235 YFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERISSTNKGSVTSIQAVFVPADDYTDPA 314
Cdd:CHL00060 255 YFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 315 PATTFAHLDSTTNLERKLTEMGIYPAVDPLASTSRALEPSVVGQEHYDVAREVQSTLQKYRELQDIIAILGMDELSDEDK 394
Cdd:CHL00060 335 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDR 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487747832 395 QTVERARRIQFFLSQNFHVAEQFTGQKGSYVPVKTTVADFRDILDGKYDHIPEDAFRLVGSMEDVIEKAKDMGVE 469
Cdd:CHL00060 415 LTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANLEVE 489
|
|
| 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: 570.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 4 GRVTQVMGPVIDVRFEhNEVPEINNALHIEVPKEdgalqLTLEVALQLGDDVVRTIAMDSTDGVQRGMEVKDTGRDISVP 83
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFD-GELPAIHSVLRAGREGE-----VVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 84 VGDVTLGRVFNVLGETIDLDEKIDDsVRRDPIHRQAPGFDELSTKVEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTV 163
Cdd:TIGR03305 75 VGKPTLSRMFDVFGNTIDRREPPKD-VEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 164 LIQELINNIAQEHGGISVFAGVGERTREGNDLYYEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDEEGQD 243
Cdd:TIGR03305 154 LLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 244 VLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERISSTNKGSVTSIQAVFVPADDYTDPAPATTFAHLD 323
Cdd:TIGR03305 234 VLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 324 STTNLERKLTEMGIYPAVDPLASTSRALEPSVVGQEHYDVAREVQSTLQKYRELQDIIAILGMDELSDEDKQTVERARRI 403
Cdd:TIGR03305 314 ASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 487747832 404 QFFLSQNFHVAEQFTGQKGSYVPVKTTVADFRDILDGKYDHIPEDAFRLVGSMED 458
Cdd:TIGR03305 394 ERFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDE 448
|
|
| 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: 568.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 81 SVPVGDVTLGRVFNVLGETIDLDEKIDdSVRRDPIHRQAPGFDELSTKVEILETGIKVVDLLAPYIKGGKIGLFGGAGVG 160
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIK-AKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 161 KTVLIQELINNIAQEHGGISVFAGVGERTREGNDLYYEMSDSGVIK-----KTAMVFGQMNEPPGARMRVALSGLTMAEY 235
Cdd:cd01133 80 KTVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINldglsKVALVYGQMNEPPGARARVALTGLTMAEY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 236 FRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERISSTNKGSVTSIQAVFVPADDYTDPAP 315
Cdd:cd01133 160 FRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAP 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 487747832 316 ATTFAHLDSTTNLERKLTEMGIYPAVDPLASTSRALEP 353
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 ... |
81-350 |
6.69e-126 |
|
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: 366.78 E-value: 6.69e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 81 SVPVGDVTLGRVFNVLGETIDLDEKIDDSVRRdPIHRQAPGFDELSTKVEILETGIKVVDLLAPYIKGGKIGLFGGAGVG 160
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRR-PIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 161 KTVLIQELINNIAQEHGGISVFAGVGERTREGNDLYYEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDeE 240
Cdd:cd19476 80 KTVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRD-N 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 241 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERISSTN--KGSVTSIQAVFVPADDYTDPAPATT 318
Cdd:cd19476 159 GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDPIPDNT 238
|
250 260 270
....*....|....*....|....*....|..
gi 487747832 319 FAHLDSTTNLERKLTEMGIYPAVDPLASTSRA 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 |
1.23e-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: 289.64 E-value: 1.23e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 135 GIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQehgGISVFAGVGERTREGNDLYYEMSDSGVIKKTAMVFGQ 214
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 215 MNEPPGARMRVALSGLTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERISSTN- 293
Cdd:pfam00006 78 SDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKg 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 487747832 294 -KGSVTSIQAVFVPADDYTDPAPATTFAHLDSTTNLERKLTEMGIYPAVDPLASTS 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 |
7.79e-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: 204.25 E-value: 7.79e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 355 VVGQEHYDVAREVQSTLQKYRELQDIIAILGMDELSDEDKQTVERARRIQFFLSQNFHVAEQFTGQKGSYVPVKTTVADF 434
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 487747832 435 RDILDGKYDHIPEDAFRLVGSMEDVIEK 462
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
4-412 |
6.47e-62 |
|
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: 207.58 E-value: 6.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 4 GRVTQVMGPVIDVRfehneVPE--INNALHIEVPKEDGALqltLEVaLQLGDDVVRTIAMDSTDGVQRGMEVKDTGRDIS 81
Cdd:COG1157 21 GRVTRVVGLLIEAV-----GPDasIGELCEIETADGRPVL---AEV-VGFRGDRVLLMPLGDLEGISPGARVVPTGRPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 82 VPVGDVTLGRVFNVLGETIDLDEKIDDSVRRdPIHRQAPGFdeLSTKV--EILETGIKVVDLLAPYIKGGKIGLFGGAGV 159
Cdd:COG1157 92 VPVGDGLLGRVLDGLGRPLDGKGPLPGEERR-PLDAPPPNP--LERARitEPLDTGVRAIDGLLTVGRGQRIGIFAGSGV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 160 GKTVLIQELINNIAQEhggISVFAGVGERTRE-----GNDLYYE-MSDSGVIKKTAmvfgqmNEPPGARMRVALSGLTMA 233
Cdd:COG1157 169 GKSTLLGMIARNTEAD---VNVIALIGERGREvrefiEDDLGEEgLARSVVVVATS------DEPPLMRLRAAYTATAIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 234 EYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERISSTNKGSVTSIQAVFVPADDYTDP 313
Cdd:COG1157 240 EYFRDQ-GKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 314 APATTFAHLDSTTNLERKLTEMGIYPAVDPLASTSRALePSVVGQEHYDVAREVQSTLQKYRELQDIIAI----LGMDEL 389
Cdd:COG1157 319 IADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM-PDIVSPEHRALARRLRRLLARYEENEDLIRIgayqPGSDPE 397
|
410 420
....*....|....*....|...
gi 487747832 390 SDEdkqTVERARRIQFFLSQNFH 412
Cdd:COG1157 398 LDE---AIALIPAIEAFLRQGMD 417
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
81-349 |
7.85e-58 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 191.62 E-value: 7.85e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 81 SVPVGDVTLGRVFNVLGETIDLDEKIDDSVRRdPIHRQAPgfDELSTKV--EILETGIKVVDLLAPYIKGGKIGLFGGAG 158
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERR-PLIAAPP--NPLKRAPieQPLPTGVRAIDGLLTCGEGQRIGIFAGSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 159 VGKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYYEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRD 238
Cdd:cd01136 78 VGKSTLLGMIARNTDAD---VNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 239 EeGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERISSTNKGSVTSIQAVFVPADDYTDPAPATT 318
Cdd:cd01136 155 Q-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEV 233
|
250 260 270
....*....|....*....|....*....|.
gi 487747832 319 FAHLDSTTNLERKLTEMGIYPAVDPLASTSR 349
Cdd:cd01136 234 RSILDGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
4-417 |
9.32e-52 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 181.10 E-value: 9.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 4 GRVTQVMGPVIDVrfehnEVP--EINNALHIEVPKEDGALQLtlEVaLQLGDDVVRTIAMDSTDGVQRGMEVKDTGRDIS 81
Cdd:PRK06936 25 GRVTQVTGTILKA-----VVPgvRIGELCYLRNPDNSLSLQA--EV-IGFAQHQALLTPLGEMYGISSNTEVSPTGTMHQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 82 VPVGDVTLGRVFNVLGETIDLDEKIDDSVRRdPIHRQAPgfDELSTKV--EILETGIKVVDLLAPYIKGGKIGLFGGAGV 159
Cdd:PRK06936 97 VGVGEHLLGRVLDGLGQPFDGGHPPEPAAWY-PVYADAP--APMSRRLieTPLSLGVRVIDGLLTCGEGQRMGIFAAAGG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 160 GKTVLIQELINNIAQEhggISVFAGVGERTREGND-LYYEMSDSGvIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRD 238
Cdd:PRK06936 174 GKSTLLASLIRSAEVD---VTVLALIGERGREVREfIESDLGEEG-LRKAVLVVATSDRPSMERAKAGFVATSIAEYFRD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 239 EeGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERISSTNKGSVTSIQAVFVPADDYTDPAPATT 318
Cdd:PRK06936 250 Q-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVADET 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 319 FAHLDSTTNLERKLTEMGIYPAVDPLASTSRALEpSVVGQEHYDVAREVQSTLQKYRELQDIIAI----LGMDELSDEdk 394
Cdd:PRK06936 329 RSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDKEADQ-- 405
|
410 420
....*....|....*....|...
gi 487747832 395 qTVERARRIQFFLSQNFHVAEQF 417
Cdd:PRK06936 406 -AIERIGAIRGFLRQGTHELSHF 427
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
62-410 |
3.11e-51 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 179.62 E-value: 3.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 62 DSTDGVQRGMEVKDTGRDISVPVGDVTLGRVFNVLGETIDLDEKIDDSVRrdPIHRQAPgfDELSTKV--EILETGIKVV 139
Cdd:PRK06820 79 ASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWR--ELDCPPP--SPLTRQPieQMLTTGIRAI 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 140 DLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYYEMSDSGVIKKTAMVFGQMNEPP 219
Cdd:PRK06820 155 DGILSCGEGQRIGIFAAAGVGKSTLLGMLCADSAAD---VMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 220 GARMRVALSGLTMAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERISSTNKGSVTS 299
Cdd:PRK06820 232 LERLKGLSTATTIAEYFRDR-GKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 300 IQAVFVPADDYTDPAPATTFAHLDSTTNLERKLTEMGIYPAVDPLASTSRALePSVVGQEHYDVAREVQSTLQKYRELQD 379
Cdd:PRK06820 311 FYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQEIEL 389
|
330 340 350
....*....|....*....|....*....|....*
gi 487747832 380 IIAI----LGMDELSDEdkqTVERARRIQFFLSQN 410
Cdd:PRK06820 390 LVRVgeyqAGEDLQADE---ALQRYPAICAFLQQD 421
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
4-417 |
2.41e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 163.74 E-value: 2.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 4 GRVTQVMGPVIDVRFEHNEVPEINNALhievPKEDGALQLTLEVaLQLGDDVVRTIAMDSTDGVQRGMEVKDTGRDISVP 83
Cdd:PRK07721 20 GKVSRVIGLMIESKGPESSIGDVCYIH----TKGGGDKAIKAEV-VGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 84 VGDVTLGRVFNVLGETIDlDEKIDDSVRRDPIHRQAPGFDELSTKVEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTV 163
Cdd:PRK07721 95 VGSGLIGQVLDALGEPLD-GSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKST 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 164 LIQELINNIAQEhggISVFAGVGERTREGND-LYYEMSDSGvIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDEeGQ 242
Cdd:PRK07721 174 LMGMIARNTSAD---LNVIALIGERGREVREfIERDLGPEG-LKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQ-GL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 243 DVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERISSTNKGSVTSIQAVFVPADDYTDPAPATTFAHL 322
Cdd:PRK07721 249 NVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTVRGIL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 323 DSTTNLERKLTEMGIYPAVDPLASTSRALePSVVGQEHYDVAREVQSTLQKYRELQDIIAILGMDELSDED-KQTVERAR 401
Cdd:PRK07721 329 DGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINIGAYKRGSSREiDEAIQFYP 407
|
410
....*....|....*.
gi 487747832 402 RIQFFLSQNFHVAEQF 417
Cdd:PRK07721 408 QIISFLKQGTDEKATF 423
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
80-411 |
3.47e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 163.32 E-value: 3.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 80 ISVPVGDVTLGRVFNVLGETIDLDEKIDDS----VRRDPIHRQAPGFDElstkvEILETGIKVVDLLAPYIKGGKIGLFG 155
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYEryapIMKAPIAAMKRGLID-----EVFSVGVKSIDGLLTCGKGQKLGIFA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 156 GAGVGKTVLIQELINN-IAQehggISVFAGVGERTREGNDlYYEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAE 234
Cdd:PRK08472 165 GSGVGKSTLMGMIVKGcLAP----IKVVALIGERGREIPE-FIEKNLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 235 YFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERISST-NKGSVTSIQAVFVPADDYTDP 313
Cdd:PRK08472 240 YFKNQ-GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEeGKGSITAFFTVLVEGDDMSDP 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 314 APATTFAHLDSTTNLERKLTEMGIYPAVDPLASTSRALEpSVVGQEHYDVAREVQSTLQKYRELQDIIAI----LGMDEL 389
Cdd:PRK08472 319 IADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENEVLIRIgayqKGNDKE 397
|
330 340
....*....|....*....|..
gi 487747832 390 SDEdkqTVERARRIQFFLSQNF 411
Cdd:PRK08472 398 LDE---AISKKEFMEQFLKQNP 416
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
90-410 |
8.07e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 162.47 E-value: 8.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 90 GRVFNVLGETIDLDEKIDDSVRRDPIHRQAPGfdELS-TKVEI-LETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQE 167
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPMSIDATAPP--AMTrARVETgLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAM 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 168 LinniAQEHGGISV-FAGVGERTREGNDLYYE-MSDSgvIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDEeGQDVL 245
Cdd:PRK06002 185 L----ARADAFDTVvIALVGERGREVREFLEDtLADN--LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDR-GENVL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 246 LFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI--SSTNKGSVTSIQAVFVPADDYTDPAPATTFAHLD 323
Cdd:PRK06002 258 LIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLD 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 324 STTNLERKLTEMGIYPAVDPLASTSRaLEPSVVGQEHYDVAREVQSTLQKYRELQDIIAILGMDELSDED-KQTVERARR 402
Cdd:PRK06002 338 GHIVLDRAIAEQGRYPAVDPLASISR-LARHAWTPEQRKLVSRLKSMIARFEETRDLRLIGGYRAGSDPDlDQAVDLVPR 416
|
....*...
gi 487747832 403 IQFFLSQN 410
Cdd:PRK06002 417 IYEALRQS 424
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
59-409 |
1.69e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 158.60 E-value: 1.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 59 IAMDSTDGVQRGMEVKDTGRDISVPVGDVTLGRVFNVLGETIDLDEkidDSVRRDPIHRQAPGFDELSTK--VEILETGI 136
Cdd:PRK06793 68 LPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEA---ENIPLQKIKLDAPPIHAFEREeiTDVFETGI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 137 KVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGND-LYYEMSDSGvIKKTAMVFGQM 215
Cdd:PRK06793 145 KSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKAD---INVISLVGERGREVKDfIRKELGEEG-MRKSVVVVATS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 216 NEPPGARMRVALSGLTMAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAvGYQPTLATEMGQLQERISSTNKG 295
Cdd:PRK06793 221 DESHLMQLRAAKLATSIAEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQKG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 296 SVTSIQAVFVPADDYTDPAPATTFAHLDSTTNLERKLTEMGIYPAVDPLASTSRALEpSVVGQEHYDVAREVQSTLQKYR 375
Cdd:PRK06793 299 SITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPNHWQLANEMRKILSIYK 377
|
330 340 350
....*....|....*....|....*....|....*..
gi 487747832 376 ElQDIIAILGMDELSDEDKQTVERARRIQF---FLSQ 409
Cdd:PRK06793 378 E-NELYFKLGTIQENAENAYIFECKNKVEGintFLKQ 413
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
52-409 |
5.02e-43 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 157.42 E-value: 5.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 52 GDDVVRTiAMDSTDGVQRGMEVKDTGRDISVPVGDVTLGRVFNVLGETIDLDEKID------DSVRRDPIHRQApgfdel 125
Cdd:PRK07594 62 GSKALLS-PFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRELPDvcwkdyDAMPPPAMVRQP------ 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 126 stKVEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYYEMSDSGVI 205
Cdd:PRK07594 135 --ITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDAD---SNVLVLIGERGREVREFIDFTLSEETR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 206 KKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQL 285
Cdd:PRK07594 210 KRCVIVVATSDRPALERVRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 286 QERISSTNKGSVTSIQAVFVPADDYTDPAPATTFAHLDSTTNLERKLTEMGIYPAVDPLASTSRALePSVVGQEHYDVAR 365
Cdd:PRK07594 289 LERTGMGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAA 367
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 487747832 366 EVQSTLQKYRELQDIIAI----LGMDELSDedkQTVERARRIQFFLSQ 409
Cdd:PRK07594 368 ILRRCLALYQEVELLIRIgeyqRGVDTDTD---KAIDTYPDICTFLRQ 412
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
4-409 |
9.88e-43 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 156.85 E-value: 9.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 4 GRVTQVMGPVIDVRFEHNEVPEInnalhIEVPKEDGALQLTLEVaLQLGDDVVRTIAMDSTDGVQRGMEVKDTGRDISVP 83
Cdd:PRK09099 26 GKVVEVIGTLLRVSGLDVTLGEL-----CELRQRDGTLLQRAEV-VGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 84 VGDVTLGRVFNVLGETIDLDEKIDDSVRRdPIHRQAPgfDELSTKV--EILETGIKVVDLLAPYIKGGKIGLFGGAGVGK 161
Cdd:PRK09099 100 VGPALLGRVIDGLGEPIDGGGPLDCDELV-PVIAAPP--DPMSRRMveAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 162 TVLIQELINNIAQEhggISVFAGVGERTREGNDLYYEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDEeG 241
Cdd:PRK09099 177 STLMGMFARGTQCD---VNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDR-G 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 242 QDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERISSTNKGSVTSIQAVFVPADDYTDPAPATTFAH 321
Cdd:PRK09099 253 LRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVRGI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 322 LDSTTNLERKLTEMGIYPAVDPLASTSRALePSVVGQEHYDVAREVQSTLQKYRELQDIIAI----LGMDELSDEdkqTV 397
Cdd:PRK09099 333 LDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVADE---AI 408
|
410
....*....|..
gi 487747832 398 ERARRIQFFLSQ 409
Cdd:PRK09099 409 AKIDAIRDFLSQ 420
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
66-411 |
1.28e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 156.40 E-value: 1.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 66 GVQRGMEVKDTGRDISVPVGDVTLGRVFNVLGETIDLDEKIDDSVRrdpIHRQAPGFDELSTKV--EILETGIKVVDLLA 143
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQR---ASRHSPPINPLSRRPitEPLDVGVRAINAML 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 144 PYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYYEMSDSGVIKKTAMVFGQMNEPPGARM 223
Cdd:PRK08972 158 TVGKGQRMGLFAGSGVGKSVLLGMMTRGTTAD---VIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 224 RVALSGLTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI--SSTNKGSVTSIQ 301
Cdd:PRK08972 235 KGCETATTIAEYFRD-QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAgnGGPGQGSITAFY 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 302 AVFVPADDYTDPAPATTFAHLDSTTNLERKLTEMGIYPAVDPLASTSRALePSVVGQEHYDVAREVQSTLQKYRELQDII 381
Cdd:PRK08972 314 TVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLI 392
|
330 340 350
....*....|....*....|....*....|....
gi 487747832 382 AILGMDELSDedkQTVERARRIQ----FFLSQNF 411
Cdd:PRK08972 393 SIGAYKQGSD---PRIDNAIRLQpamnAFLQQTM 423
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
57-410 |
1.08e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 153.98 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 57 RTIAM--DSTDGVQRGMEVKDTGRDISVPVGDVTLGRVFNVLGETIDLDEKIDDSVRRDPIHRQAPGFDELSTKVEILET 134
Cdd:PRK08927 65 RALLMpfGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPYPLRAPPPPAHSRARVGEPLDL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 135 GIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTRE-----GNDLYYE-MSDSGVIKKT 208
Cdd:PRK08927 145 GVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGREvqeflQDDLGPEgLARSVVVVAT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 209 AmvfgqmNEPPGARMRVALSGLTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQER 288
Cdd:PRK08927 222 S------DEPALMRRQAAYLTLAIAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLER 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 289 I--SSTNKGSVTSIQAVFVPADDYTDPAPATTFAHLDSTTNLERKLTEMGIYPAVDPLASTSRALePSVVGQEHYDVARE 366
Cdd:PRK08927 295 AgpGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRR 373
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 487747832 367 VQSTLQKYRELQDIIAI----LGMDELSDEdkqTVERARRIQFFLSQN 410
Cdd:PRK08927 374 ARQLMATYADMEELIRLgayrAGSDPEVDE---AIRLNPALEAFLRQG 418
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
63-383 |
1.06e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 151.42 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 63 STDGVQRGMEVK---DTGRdisVPVGDVTLGRVFNVLGETID------------LDEKIDDSVRRDPIHrqapgfdelst 127
Cdd:PRK05688 84 SVAGIAPGARVVplaDTGR---LPMGMSMLGRVLDGAGRALDgkgpmkaedwvpMDGPTINPLNRHPIS----------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 128 kvEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYYEMSDSGVIKK 207
Cdd:PRK05688 150 --EPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEAD---IIVVGLIGERGREVKEFIEHILGEEGLKR 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 208 TAMVFGQMNEPPGARMRVALSGLTMAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQE 287
Cdd:PRK05688 225 SVVVASPADDAPLMRLRAAMYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 288 RISSTNKG--SVTSIQAVFVPADDYTDPAPATTFAHLDSTTNLERKLTEMGIYPAVDPLASTSRALePSVVGQEHYDVAR 365
Cdd:PRK05688 304 RAGNAEPGggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQ 382
|
330
....*....|....*...
gi 487747832 366 EVQSTLQKYRELQDIIAI 383
Cdd:PRK05688 383 RFKQLWSRYQQSRDLISV 400
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
61-381 |
1.47e-40 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 150.53 E-value: 1.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 61 MDSTDGVQRGMEVKDTGRDISVPVGDVTLGRVFNVLGETID-LDEKIDDSVRRD--PIHRQAPGFDELSTKVEILETGIK 137
Cdd:PRK08149 61 IGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVErFDAPPTVGPISEerVIDVAPPSYAERRPIREPLITGVR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 138 VVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYYEMSDSGVIKKTAMVFGQMNE 217
Cdd:PRK08149 141 AIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHSEAD---VFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDF 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 218 PPGARMRVALSGLTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERISSTNKGSV 297
Cdd:PRK08149 218 SSVDRCNAALVATTVAEYFRD-QGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 298 TSIQAVFVPADDYTDPAPATTFAHLDSTTNLERKLTEMGIYPAVDPLASTSRALEpSVVGQEHYDVAREVQSTLQKYREL 377
Cdd:PRK08149 297 TAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFG-QVTDPKHRQLAAAFRKLLTRLEEL 375
|
....
gi 487747832 378 QDII 381
Cdd:PRK08149 376 QLFI 379
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
66-410 |
2.83e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 150.04 E-value: 2.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 66 GVQRGMEVKDTGRDISVPVGDVTLGRVFNVLGETIDLDEKIDDSVrrdPIHRQAPGFDELSTKV--EILETGIKVVDLLA 143
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGST---PLQQQLPQIHPLQRRAvdTPLDVGVNAINGLL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 144 PYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYYEMSDSGVIKKTAMVFGQMNEPPGARM 223
Cdd:PRK07196 151 TIGKGQRVGLMAGSGVGKSVLLGMITRYTQAD---VVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRI 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 224 RVALSGLTMAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI-SSTNKGSVTSIQA 302
Cdd:PRK07196 228 KATELCHAIATYYRDK-GHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGTMTAIYT 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 303 VFVPADDYTDPAPATTFAHLDSTTNLERKLTEMGIYPAVDPLASTSRALEpSVVGQEHYDVAREVQSTLQKYRELQDIIA 382
Cdd:PRK07196 307 VLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMAIKPLIP 385
|
330 340 350
....*....|....*....|....*....|..
gi 487747832 383 ----ILGMDELSDedkQTVERARRIQFFLSQN 410
Cdd:PRK07196 386 lggyVAGADPMAD---QAVHYYPAITQFLRQE 414
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
82-409 |
1.08e-31 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 126.44 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 82 VPVGDVTLGRVFNVLGETIDLDEKIDDSVRRDPIhrqAPGFDELS-TKVE-ILETGIKVVDLLAPYIKGGKIGLFGGAGV 159
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGALI---TPPFNPLQrTPIEhVLDTGVRAINALLTVGRGQRMGLFAGSGV 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 160 GKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYYEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDE 239
Cdd:PRK07960 187 GKSVLLGMMARYTQAD---VIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDR 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 240 eGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERISS--TNKGSVTSIQAVFVPADDYTDPAPAT 317
Cdd:PRK07960 264 -GQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQDPIADS 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 318 TFAHLDSTTNLERKLTEMGIYPAVDPLASTSRALEpSVVGQEHYDVAREVQSTLQKYRELQDIIAI----LGMDELSDed 393
Cdd:PRK07960 343 ARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMT-ALIDEQHYARVRQFKQLLSSFQRNRDLVSVgayaKGSDPMLD-- 419
|
330
....*....|....*.
gi 487747832 394 kQTVERARRIQFFLSQ 409
Cdd:PRK07960 420 -KAIALWPQLEAFLQQ 434
|
|
| 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 |
3.28e-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: 114.92 E-value: 3.28e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487747832 3 IGRVTQVMGPVIDVRFEHNEVPEINNALHIevpKEDGALQLTLEVALQLGDDVVRTIAMDSTDGVQRGMEVKDTGRDI 80
Cdd:cd18115 2 TGKIVQVIGPVVDVEFPEGELPPIYNALEV---KGDDGKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
47-416 |
6.18e-31 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 125.03 E-value: 6.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 47 VALQLGDDVVRTIAMDSTDGVQRGMEVKDTGRDISVPVGDVTLGRVFNVLGETIDLDEKIDDSVRRdPIHRQAPGFDELS 126
Cdd:PRK13343 62 FAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARR-PLERPAPAIIERD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 127 TKVEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELInnIAQEHGG-ISVFAGVGERTREGNDLYYEMSDSGVI 205
Cdd:PRK13343 141 FVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAI--INQKDSDvICVYVAIGQKASAVARVIETLREHGAL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 206 KKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQL 285
Cdd:PRK13343 219 EYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 286 QERISSTNK----GSVTSIQAVFVPADDYTDPAPATTFAHLDSTTNLERKLTEMGIYPAVDPLASTSRalepsVVGQEHY 361
Cdd:PRK13343 298 LERAAKLSPelggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR-----VGGKAQH 372
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487747832 362 DVAREVQSTLQ----KYRELQdIIAILGMDeLSDEDKQTVERARRIQFFLSQNFH----VAEQ 416
Cdd:PRK13343 373 PAIRKESGRLRldyaQFLELE-AFTRFGGL-LDAGTQKQITRGRRLRELLKQPRFsplsVEEQ 433
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
49-412 |
1.06e-30 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 123.40 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 49 LQLGDDVVRTIAMDSTDGV-QRGMEVKDTGRDISVPVGDVTLGRVFNVLGETIDLDEKIDDSVRRD-------PIHRQAP 120
Cdd:PRK04196 44 LEVSEDKAVVQVFEGTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDingapinPVAREYP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 121 GfdelstkvEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKtvliQELINNIAQ-------EHGGISVFAGVGERTREGN 193
Cdd:PRK04196 124 E--------EFIQTGISAIDGLNTLVRGQKLPIFSGSGLPH----NELAAQIARqakvlgeEENFAVVFAAMGITFEEAN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 194 DLYYEMSDSGVIKKTAMVFGQMNEPPGARM---RVAlsgLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPS 270
Cdd:PRK04196 192 FFMEDFEETGALERSVVFLNLADDPAIERIltpRMA---LTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 271 AVGYQPTLATEMGQLQER--ISSTNKGSVTSIQAVFVPADDYTDPAPattfahlDST---TN----LERKLTEMGIYPAV 341
Cdd:PRK04196 269 RRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyiTEgqivLSRELHRKGIYPPI 341
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487747832 342 DPLASTSRaLEPSVVG-----QEHYDVAREVQSTLQKYRELQDIIAILGMDELSDEDKQTVERARRI-QFFLSQNFH 412
Cdd:PRK04196 342 DVLPSLSR-LMKDGIGegktrEDHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFeREFVNQGFD 417
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
70-409 |
1.10e-30 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 123.09 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 70 GMEVKDTGRDISVPVGDVTLGRVFNVLGETIDLDEKIDDSvRRDPIHRQAPGFDELSTKVEILETGIKVVDLLAPYIKGG 149
Cdd:PRK05922 80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKT-HLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQ 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 150 KIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDlYYEMSDSGVI-KKTAMVFGQMNEPPGARMRVALS 228
Cdd:PRK05922 159 RIGVFSEPGSGKSSLLSTIAKGSKST---INVIALIGERGREVRE-YIEQHKEGLAaQRTIIIASPAHETAPTKVIAGRA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 229 GLTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERISSTNKGSVTSIQAVFVPA- 307
Cdd:PRK05922 235 AMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAILHYPn 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 308 --DDYTDPAPATTFAHLdSTTNLERKLTEmgiyPAVDPLASTSRALEpSVVGQEHYDVAREVQSTLQKYRELQDIIAILG 385
Cdd:PRK05922 314 hpDIFTDYLKSLLDGHF-FLTPQGKALAS----PPIDILTSLSRSAR-QLALPHHYAAAEELRSLLKAYHEALDIIQLGA 387
|
330 340
....*....|....*....|....*...
gi 487747832 386 MDELSDEDkqtVERARR----IQFFLSQ 409
Cdd:PRK05922 388 YVPGQDAH---LDRAVKllpsIKQFLSQ 412
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
82-357 |
8.18e-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: 8.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 82 VPVGDVTLGRVFNVLGETIDLDEKIDDSVRRD-------PIHRQAPGfdelstkvEILETGIKVVDLLAPYIKGGKIGLF 154
Cdd:cd01135 4 LPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDingppinPVARIYPE--------EMIQTGISAIDVMNTLVRGQKLPIF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 155 GGAGVGKtvliQELINNIA-------QEHGGISVFAGVGERTREGNDLYYEMSDSGVIKKTAMVFGQMNEPPGARMRVAL 227
Cdd:cd01135 76 SGSGLPH----NELAAQIArqagvvgSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 228 SGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERISSTN--KGSVTSIQAVFV 305
Cdd:cd01135 152 MALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEgrKGSITQIPILTM 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 487747832 306 PADDYTDPAPATTFAHLDSTTNLERKLTEMGIYPAVDPLASTSRaLEPSVVG 357
Cdd:cd01135 232 PNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR-LMKSGIG 282
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
109-349 |
6.05e-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: 112.28 E-value: 6.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 109 SVRRDPIHRQAPGFDELsTKVEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGER 188
Cdd:cd01134 38 NVQRWPVRQPRPVKEKL-PPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSLSKWSNSD---VVIYVGCGER 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 189 treGNDL------YYEMSD----SGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDeEGQDVLLFIDNIFRFTQAG 258
Cdd:cd01134 114 ---GNEMaevleeFPELKDpitgESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRD-MGYNVSLMADSTSRWAEAL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 259 SEVSALLGRMPSAVGYQPTLATEMGQLQERI-------SSTNKGSVTSIQAVFVPADDYTDPAPATTFAHLDSTTNLERK 331
Cdd:cd01134 190 REISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrclgSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKK 269
|
250
....*....|....*...
gi 487747832 332 LTEMGIYPAVDPLASTSR 349
Cdd:cd01134 270 LAQRRHFPSINWLISYSK 287
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
129-412 |
2.81e-27 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 114.88 E-value: 2.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 129 VEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERtreGNdlyyEMSD------- 201
Cdd:PRK04192 208 VEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQLAKWADAD---IVIYVGCGER---GN----EMTEvleefpe 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 202 -----SG--VIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGY 274
Cdd:PRK04192 278 lidpkTGrpLMERTVLIANTSNMPVAAREASIYTGITIAEYYRDM-GYDVLLMADSTSRWAEALREISGRLEEMPGEEGY 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 275 QPTLATEMGQLQER-----ISSTNKGSVTSIQAVFVPADDYTDPApattfahldsTTN----------LERKLTEMGIYP 339
Cdd:PRK04192 357 PAYLASRLAEFYERagrvkTLGGEEGSVTIIGAVSPPGGDFSEPV----------TQNtlrivkvfwaLDAELADRRHFP 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 340 AVDPLASTSRALE------PSVVGQEHYDVAREVQSTLQKYRELQDIIAILGMDELSDEDKQTVERARRIQF-FLSQN-F 411
Cdd:PRK04192 427 AINWLTSYSLYLDqvapwwEENVDPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARLIREdFLQQNaF 506
|
.
gi 487747832 412 H 412
Cdd:PRK04192 507 D 507
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
6-412 |
3.19e-23 |
|
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: 102.11 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 6 VTQVMGPVI---DVRFehnevPEINNALHIEVPkeDGALQL--TLEVAlqlGDDVVRTIaMDSTDGVQ-RGMEVKDTGRD 79
Cdd:TIGR01040 5 VSGVNGPLVildNVKF-----PRFAEIVNLTLP--DGTVRSgqVLEVS---GNKAVVQV-FEGTSGIDaKKTTCEFTGDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 80 ISVPVGDVTLGRVFNVLGETID-----LDEKIDDsVRRDPIHRQAPGFDElstkvEILETGIKVVDLLAPYIKGGKIGLF 154
Cdd:TIGR01040 74 LRTPVSEDMLGRVFNGSGKPIDkgppvLAEDYLD-INGQPINPYARIYPE-----EMIQTGISAIDVMNSIARGQKIPIF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 155 GGAGV-------------GKTVLIQELINNIAQEHGGIsVFAGVGERTREGNDLYYEMSDSGVIKKTAMVFGQMNEPPGA 221
Cdd:TIGR01040 148 SAAGLphneiaaqicrqaGLVKLPTKDVHDGHEDNFAI-VFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 222 RMRVALSGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERISSTN--KGSVTS 299
Cdd:TIGR01040 227 RIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrNGSITQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 300 IQAVFVPADDYTDPAPATTFAHLDSTTNLERKLTEMGIYPAVDPLASTSRaLEPSVVGQ-----EHYDVAREVQSTLQKY 374
Cdd:TIGR01040 307 IPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSR-LMKSAIGEgmtrkDHSDVSNQLYACYAIG 385
|
410 420 430
....*....|....*....|....*....|....*....
gi 487747832 375 RELQDIIAILGMDELSDEDKQTVERARRIQ-FFLSQNFH 412
Cdd:TIGR01040 386 KDVQAMKAVVGEEALSSEDLLYLEFLDKFEkNFIAQGPY 424
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
5-402 |
1.85e-21 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 96.26 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 5 RVTQVMGPVIDVRFE---HNEVPEINNAlhievpkeDGalqLTLEVALQLGDDVVRTIAMDSTDGVQRGMEVKDTGRDIS 81
Cdd:PRK02118 7 KITDITGNVITVEAEgvgYGELATVERK--------DG---SSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 82 VPVGDVTLGRVFNVLGETIDLDEKIDDsvrrDPIHRQAPGFDELSTKV--EILETGIKVVDLLAPYIKGGKIGLFGGAGV 159
Cdd:PRK02118 76 VTYSESLLGRRFNGSGKPIDGGPELEG----EPIEIGGPSVNPVKRIVprEMIRTGIPMIDVFNTLVESQKIPIFSVSGE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 160 GktvlIQELINNIA-QEHGGISVFAGVGERtregNDLYY----EMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAE 234
Cdd:PRK02118 152 P----YNALLARIAlQAEADIIILGGMGLT----FDDYLffkdTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 235 YFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQER-ISSTNKGSVTSIQAVFVPADDYTDP 313
Cdd:PRK02118 224 KFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKaVDFEDGGSITIIAVTTMPGDDVTHP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 314 APattfahlDSTTnlerKLTEMGIY---PAVDPLASTSRaLEPSVVGQEHYDVAREVQSTLQK----YRELQDIIAiLGM 386
Cdd:PRK02118 304 VP-------DNTG----YITEGQFYlrrGRIDPFGSLSR-LKQLVIGKKTREDHGDLMNAMIRlyadSREAKEKMA-MGF 370
|
410
....*....|....*.
gi 487747832 387 DeLSDEDKQTVERARR 402
Cdd:PRK02118 371 K-LSNWDEKLLKFSEL 385
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
80-349 |
1.96e-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: 93.78 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 80 ISVPVGDVTLGRVFNVLGETIDLDEKIDDSVRRdPIHRQAPGFDELSTKVEILETGIKVVDLLAPYIKGGKIGLFGGAGV 159
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERR-RVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 160 GKT-VLIQELINNiaQEHGGISVFAGVGERTREGNDLYYEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRD 238
Cdd:cd01132 81 GKTaIAIDTIINQ--KGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 239 eEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERISSTNK----GSVTSIQAVFVPADDYTDPA 314
Cdd:cd01132 159 -NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGSLTALPIIETQAGDVSAYI 237
|
250 260 270
....*....|....*....|....*....|....*
gi 487747832 315 PATTFAHLDSTTNLERKLTEMGIYPAVDPLASTSR 349
Cdd:cd01132 238 PTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
168-404 |
4.88e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 93.55 E-value: 4.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 168 LINNIAQEH-------GGISVFAGVGERTREGNDLYYEM-------SDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMA 233
Cdd:PRK14698 666 LLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEFpklkdpkTGKPLMERTVLIANTSNMPVAAREASIYTGITIA 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 234 EYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI-------SSTNKGSVTSIQAVFVP 306
Cdd:PRK14698 746 EYFRDM-GYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPP 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 307 ADDYTDPAPATTFAHLDSTTNLERKLTEMGIYPAVDPLASTSRALEpSVVGQEHYDVARE-------VQSTLQKYRELQD 379
Cdd:PRK14698 825 GGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVD-AVKDWWHKNVDPEwkamrdkAMELLQKEAELQE 903
|
250 260
....*....|....*....|....*
gi 487747832 380 IIAILGMDELSDEDKQTVERARRIQ 404
Cdd:PRK14698 904 IVRIVGPDALPERERAILLVARMLR 928
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
47-269 |
7.90e-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: 92.02 E-value: 7.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 47 VALQLGDDVVRTIAMDSTDGVQRGMEVKDTGRDISVPVGDVTLGRVFNVLGETIDLDEKIDDSVRRdPIHRQAPGFDELS 126
Cdd:COG0056 62 MALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERR-PVERPAPGVIDRQ 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 127 TKVEILETGIKVVDLLAPyikggkIG------LFGGAGVGKT-VLIQELINniaQEHGGI-----------SVFAGVGER 188
Cdd:COG0056 141 PVHEPLQTGIKAIDAMIP------IGrgqrelIIGDRQTGKTaIAIDTIIN---QKGKDViciyvaigqkaSTVAQVVET 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 189 TREGNDLYYemsdsgvikkTAMVFGQMNEPPGARMRVALSGLTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRM 268
Cdd:COG0056 212 LEEHGAMEY----------TIVVAATASDPAPLQYIAPYAGCAMGEYFMD-QGKDVLIVYDDLSKHAVAYRELSLLLRRP 280
|
.
gi 487747832 269 P 269
Cdd:COG0056 281 P 281
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
44-269 |
2.79e-19 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 90.12 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 44 TLEVALQLGDDVVRTIAMDSTDGVQRGMEVKDTGRDISVPVGDVTLGRVFNVLGETIDLDEKIDDSVRRdPIHRQAPG-F 122
Cdd:PRK09281 59 VYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETR-PVERKAPGvI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 123 DELSTKvEILETGIKVVDLLAPyikggkIG------LFGGAGVGKT-VLIQELINniaQEHGGI-----------SVFAG 184
Cdd:PRK09281 138 DRKSVH-EPLQTGIKAIDAMIP------IGrgqrelIIGDRQTGKTaIAIDTIIN---QKGKDViciyvaigqkaSTVAQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 185 VGERTREGNDLYYemsdSGVIKKTAmvfgqmNEPPGARMRVALSGLTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSAL 264
Cdd:PRK09281 208 VVRKLEEHGAMEY----TIVVAATA------SDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQLSLL 276
|
....*
gi 487747832 265 LGRMP 269
Cdd:PRK09281 277 LRRPP 281
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
53-405 |
7.88e-19 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 89.33 E-value: 7.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 53 DDVVRTIAMDSTDGVQRGMEVKDTGRDISVPVGDVTLGRVFNVLGETIDLD------EKIDDSVRRDPIHRQAPGFDELS 126
Cdd:PTZ00185 88 DGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPVGlltrsrALLESEQTLGKVDAGAPNIVSRS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 127 TKVEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKT-VLIQELIN------NIAQEHGGISVFAGVGERTREGNDLYYEM 199
Cdd:PTZ00185 168 PVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTsIAVSTIINqvrinqQILSKNAVISIYVSIGQRCSNVARIHRLL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 200 SDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLA 279
Cdd:PTZ00185 248 RSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMN-RGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVF 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 280 TEMGQLQERIS----STNKGSVTSIQAVFVPADDYTDPAPATTFAHLDSTTNLERKLTEMGIYPAVDPLASTSRaLEPSV 355
Cdd:PTZ00185 327 YLHSRLLERAAmlspGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSR-VGSSA 405
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 487747832 356 VGQEHYDVAREVQSTLQKYRElqdiiaiLGMDELSDEDKQTVERARRIQF 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 |
5.15e-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: 78.25 E-value: 5.15e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 360 HYDVAREVQSTLQKYRELQDIIAILGMDELSDEDKQTVERARRIQFFLSQNFHVAEQFTGQKGSYVPVKT 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 |
6.05e-18 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 77.97 E-value: 6.05e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487747832 6 VTQVMGPVIDVRFEHNEVPEINNALHIEVPKEDGalqLTLEVALQLGDDVVRTIAMDSTDGVQRGMEVKDTG 77
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVEFGS---LVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
37-422 |
1.07e-16 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 82.32 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 37 EDGalqlTLEVALQLGDDVVRTIAMDSTDGVQRGMEVKDTGRDISVPVGDVTLGRVFNVLGETIDLDEKIDDSVRRdPIH 116
Cdd:CHL00059 35 EDG----TIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESR-LIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 117 RQAPGFDELSTKVEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKT-VLIQELINNIAQehGGISVFAGVGERTREGNDL 195
Cdd:CHL00059 110 SPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTaVATDTILNQKGQ--NVICVYVAIGQKASSVAQV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 196 YYEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRdEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQ 275
Cdd:CHL00059 188 VTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 276 PTLATEMGQLQERISSTNK----GSVTSIQAVFVPADDYTDPAPATTFAHLDSTTNLERKLTEMGIYPAVDPLASTSR-- 349
Cdd:CHL00059 267 GDVFYLHSRLLERAAKLSSqlgeGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRvg 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 350 -ALEPSVVGQehydVAREVQSTLQKYRELQDIIAIlgmdeLSDEDKQT---VERARRIQFFLSQN----FHVAEQ----F 417
Cdd:CHL00059 347 sAAQIKAMKQ----VAGKLKLELAQFAELEAFAQF-----ASDLDKATqnqLARGQRLRELLKQSqsapLTVEEQvatiY 417
|
....*
gi 487747832 418 TGQKG 422
Cdd:CHL00059 418 TGTNG 422
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
105-349 |
4.20e-10 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 61.25 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 105 KIDDSVRRDPIHRQA-PGFDELS----TKVEILETG-----IKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQ 174
Cdd:PRK12608 80 RVDSVNGTDPEKLARrPHFDDLTplhpRERLRLETGsddlsMRVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 175 EHGGISVFAG-VGERTREGNDLYYEMSdsgvikktAMVFGQMNEPPGARmRVALSGLTMAEYFRD-EEGQDVLLFIDNIF 252
Cdd:PRK12608 160 NHPEVHLMVLlIDERPEEVTDMRRSVK--------GEVYASTFDRPPDE-HIRVAELVLERAKRLvEQGKDVVILLDSLT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 253 RFTQAGSEVSALLGRMPSAvgyqpTLATEMGQLQERISST-----NKGSVTSIQAVFVP----ADDYTdpapattFAHLD 323
Cdd:PRK12608 231 RLARAYNNEVESSGRTLSG-----GVDARALQRPKRLFGAarnieEGGSLTIIATALVDtgsrMDEVI-------FEEFK 298
|
250 260 270
....*....|....*....|....*....|
gi 487747832 324 STTNLE----RKLTEMGIYPAVDPLASTSR 349
Cdd:PRK12608 299 GTGNMEivldRELADKRVFPAIDIAKSGTR 328
|
|
| 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 |
8.88e-10 |
|
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: 55.01 E-value: 8.88e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487747832 4 GRVTQVMGPVIDVRFEhNEVPeINNALHIEVPKEDGALQLTLEVALQLGDDVVrTIAMDSTDGVQRGMEVKDTGR 78
Cdd:cd01426 2 GRVIRVNGPLVEAELE-GEVA-IGEVCEIERGDGNNETVLKAEVIGFRGDRAI-LQLFESTRGLSRGALVEPTGR 73
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
147-268 |
2.50e-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: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 147 KGGKIGLFGGAGVGKTVLIQELINNIAQEHGGISVFAGVGERTREGNDLYYEMSDSGVIKKTamvfgqmnepPGARMRVA 226
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS----------GELRLRLA 70
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 487747832 227 lsgLTMAEYFRDEegqdvLLFIDNIFRFTQAGSEVSALLGRM 268
Cdd:smart00382 71 ---LALARKLKPD-----VLILDEITSLLDAEQEALLLLLEE 104
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
137-349 |
2.68e-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: 48.74 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 137 KVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEHGGISVFAG-VGERTREGNDlyyeMSDSG---VIKKTamvf 212
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRSVkgeVVAST---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 213 gqMNEPPGARMRVALSGLTMAEYfRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAvGYQPTLAtemgQLQERISST 292
Cdd:cd01128 77 --FDEPPERHVQVAEMVIEKAKR-LVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSG-GVDANAL----HKPKRFFGA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487747832 293 -----NKGSVTSIQAVFVPADDYTDPApatTFAHLDSTTNLE----RKLTEMGIYPAVDPLASTSR 349
Cdd:cd01128 149 arnieEGGSLTIIATALVDTGSRMDEV---IFEEFKGTGNMElvldRKLAEKRIFPAIDILKSGTR 211
|
|
| 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 ... |
365-418 |
9.95e-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: 44.30 E-value: 9.95e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 487747832 365 REVQSTLQKYRELQDIIAILGMDELSDEDKQTVERARRI-QFFLSQN-FHVAEQFT 418
Cdd:cd18111 6 TEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIrEDFLQQNaFDEVDTYC 61
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
125-388 |
2.42e-05 |
|
transcription termination factor Rho; This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding. [Transcription, Transcription factors]
Pssm-ID: 162030 [Multi-domain] Cd Length: 415 Bit Score: 46.60 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 125 LSTKVEILETgiKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEHGGISVFAG-VGERTREGNDLyyEMSDSG 203
Cdd:TIGR00767 147 LETSTEDLST--RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEVELIVLlIDERPEEVTDM--QRSVKG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 204 -VIKKTamvfgqMNEPPGARMRVALSGLTMAEYfRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAvGYQPTLAtem 282
Cdd:TIGR00767 223 eVVAST------FDEPASRHVQVAEMVIEKAKR-LVEHKKDVVILLDSITRLARAYNTVTPASGKVLSG-GVDANAL--- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747832 283 gQLQERI--SSTN---KGSVTSIQAVFVPADDYTDpapATTFAHLDSTTNLE----RKLTEMGIYPAVDPLASTSRAlEP 353
Cdd:TIGR00767 292 -HRPKRFfgAARNieeGGSLTIIATALIDTGSRMD---EVIFEEFKGTGNMElhldRKLADRRIFPAIDIKKSGTRK-EE 366
|
250 260 270
....*....|....*....|....*....|....*
gi 487747832 354 SVVGQEHydvarevqstLQKYRELQDIIAilGMDE 388
Cdd:TIGR00767 367 LLLTPEE----------LQKIWVLRKIIS--PMDS 389
|
|
| |
