|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-460 |
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: 1007.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 1 MATGKIVQVIGAVVDAEFPQDSVPKVYDALEV-MNGKEKLVLEVQQQLGGGIVRCIAMGTSDGLSRGLKVEDLGHPIEVP 79
Cdd:COG0055 3 MNTGKIVQVIGPVVDVEFPEGELPAIYNALEVeNEGGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 80 VGKATLGRIMNVLGTPIDMKGEIETEERWSIHREAPTYEELSNSQELLETGIKVMDLICPFAKGGKVGLFGGAGVGKTVN 159
Cdd:COG0055 83 VGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 160 MMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD-EGRDV 238
Cdd:COG0055 163 IMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 239 LLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDA 318
Cdd:COG0055 243 LLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 319 TVVLSRQIASLGIYPAVDPLDSTSRQLDPLVVGQEHYDVARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKIQ 398
Cdd:COG0055 323 TTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARARKIQ 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490366925 399 RFLSQPFFVAEVFTGSPGKFVSLKDTIRGFKGILNGDYDHLPEQAFYMVGTIEEAVEKAKKL 460
Cdd:COG0055 403 RFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKL 464
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
2-460 |
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: 921.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 2 ATGKIVQVIGAVVDAEFPQDSVPKVYDALEVMNGKE-KLVLEVQQQLGGGIVRCIAMGTSDGLSRGLKVEDLGHPIEVPV 80
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNRAEsELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 81 GKATLGRIMNVLGTPIDMKGEIETEERWSIHREAPTYEELSNSQELLETGIKVMDLICPFAKGGKVGLFGGAGVGKTVNM 160
Cdd:TIGR01039 81 GKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 161 MELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDE-GRDVL 239
Cdd:TIGR01039 161 QELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEqGQDVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 240 LFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDAT 319
Cdd:TIGR01039 241 LFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 320 VVLSRQIASLGIYPAVDPLDSTSRQLDPLVVGQEHYDVARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKIQR 399
Cdd:TIGR01039 321 TVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQR 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490366925 400 FLSQPFFVAEVFTGSPGKFVSLKDTIRGFKGILNGDYDHLPEQAFYMVGTIEEAVEKAKKL 460
Cdd:TIGR01039 401 FLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
3-460 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 799.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 3 TGKIVQVIGAVVDAEFPQDSVPKVYDALEVMNGKE-----KLVLEVQQQLGGGIVRCIAMGTSDGLSRGLKVEDLGHPIE 77
Cdd:CHL00060 16 LGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTagqeiNVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 78 VPVGKATLGRIMNVLGTPIDMKGEIETEERWSIHREAPTYEELSNSQELLETGIKVMDLICPFAKGGKVGLFGGAGVGKT 157
Cdd:CHL00060 96 VPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 158 VNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVLD-------KVSLVYGQMNEPPGNRLRVALTGLTMAEK 230
Cdd:CHL00060 176 VLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 231 FRDEGR-DVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSP 309
Cdd:CHL00060 256 FRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 310 ATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPLVVGQEHYDVARGVQSILQRYQELKDIIAILGMDELSEEDKL 389
Cdd:CHL00060 336 ATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRL 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490366925 390 VVARARKIQRFLSQPFFVAEVFTGSPGKFVSLKDTIRGFKGILNGDYDHLPEQAFYMVGTIEEAVEKAKKL 460
Cdd:CHL00060 416 TVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANL 486
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
4-453 |
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: 569.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 4 GKIVQVIGAVVDAEFPQDsVPKVYDALEVMNGKEkLVLEVQQQLGGGIVRCIAMGTSDGLSRGLKVEDLGHPIEVPVGKA 83
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDGE-LPAIHSVLRAGREGE-VVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 84 TLGRIMNVLGTPIDmKGEIETEERW-SIHREAPTYEELSNSQELLETGIKVMDLICPFAKGGKVGLFGGAGVGKTVNMME 162
Cdd:TIGR03305 79 TLSRMFDVFGNTID-RREPPKDVEWrSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 163 LIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD-EGRDVLLF 241
Cdd:TIGR03305 158 MIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDdEKQDVLLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 242 VDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVV 321
Cdd:TIGR03305 238 IDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLSASLV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 322 LSRQIASLGIYPAVDPLDSTSRQLDPLVVGQEHYDVARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKIQRFL 401
Cdd:TIGR03305 318 LSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRLERFL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 490366925 402 SQPFFVAEVFTGSPGKFVSLKDTIRGFKGILNGDYDHLPEQAFYMVGTIEEA 453
Cdd:TIGR03305 398 TQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDEA 449
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
77-347 |
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: 565.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 77 EVPVGKATLGRIMNVLGTPIDMKGEIETEERWSIHREAPTYEELSNSQELLETGIKVMDLICPFAKGGKVGLFGGAGVGK 156
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 157 TVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNV-----LDKVSLVYGQMNEPPGNRLRVALTGLTMAEKF 231
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVinldgLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 232 RD-EGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPA 310
Cdd:cd01133 161 RDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPA 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 490366925 311 TTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDP 347
Cdd:cd01133 241 TTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
78-343 |
6.91e-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: 366.40 E-value: 6.91e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 78 VPVGKATLGRIMNVLGTPIDMKGEIETEERWSIHREAPTYEELSNSQELLETGIKVMDLICPFAKGGKVGLFGGAGVGKT 157
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 158 VNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRD 237
Cdd:cd19476 82 VLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 238 VLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKT--GSITSVQAVYVPADDLTDPSPATTFAH 315
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDggGSITAIPAVSTPGDDLTDPIPDNTFAI 241
|
250 260
....*....|....*....|....*...
gi 490366925 316 LDATVVLSRQIASLGIYPAVDPLDSTSR 343
Cdd:cd19476 242 LDGQIVLSRELARKGIYPAINVLDSTSR 269
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
130-342 |
1.24e-92 |
|
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: 279.24 E-value: 1.24e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 130 GIKVMDLICPFAKGGKVGLFGGAGVGKTVNMMELIRNIAiehSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQ 209
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQAS---ADVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 210 MNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITST--K 287
Cdd:pfam00006 78 SDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVkgK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490366925 288 TGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTS 342
Cdd:pfam00006 158 GGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 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 ... |
349-456 |
1.05e-80 |
|
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: 244.70 E-value: 1.05e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 349 VVGQEHYDVARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKIQRFLSQPFFVAEVFTGSPGKFVSLKDTIRGF 428
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 490366925 429 KGILNGDYDHLPEQAFYMVGTIEEAVEK 456
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
3-432 |
4.69e-69 |
|
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: 226.07 E-value: 4.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 3 TGKIVQVIGAVVDAEFPQdsvPKVYDALEVMNGKEKLVL-EVqqqLG--GGIVRCIAMGTSDGLSRGLKVEDLGHPIEVP 79
Cdd:COG1157 20 SGRVTRVVGLLIEAVGPD---ASIGELCEIETADGRPVLaEV---VGfrGDRVLLMPLGDLEGISPGARVVPTGRPLSVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 80 VGKATLGRIMNVLGTPIDMKGEIETEERWSIHREAPTYEELSNSQELLETGIKVMDLICPFAKGGKVGLFGGAGVGKTVN 159
Cdd:COG1157 94 VGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 160 MMELIRNIA--IehsgySVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRD 237
Cdd:COG1157 174 LGMIARNTEadV-----NVIALIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 238 VLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLD 317
Cdd:COG1157 249 VLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAVRGILD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 318 ATVVLSRQIASLGIYPAVDPLDSTSRqLDPLVVGQEHYDVARGVQSILQRYQELKDIIAI----LGMDELSEEdklVVAR 393
Cdd:COG1157 329 GHIVLSRKLAERGHYPAIDVLASISR-VMPDIVSPEHRALARRLRRLLARYEENEDLIRIgayqPGSDPELDE---AIAL 404
|
410 420 430
....*....|....*....|....*....|....*....
gi 490366925 394 ARKIQRFLSQpffvaevftgSPGKFVSLKDTIRGFKGIL 432
Cdd:COG1157 405 IPAIEAFLRQ----------GMDERVSFEESLAQLAELL 433
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
77-343 |
9.60e-59 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 193.93 E-value: 9.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 77 EVPVGKATLGRIMNVLGTPIDMKGEIETEERWSIHREAPTYEELSNSQELLETGIKVMDLICPFAKGGKVGLFGGAGVGK 156
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 157 TVNMMELIRNIAiehSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGR 236
Cdd:cd01136 81 STLLGMIARNTD---ADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 237 DVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHL 316
Cdd:cd01136 158 KVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRSIL 237
|
250 260
....*....|....*....|....*..
gi 490366925 317 DATVVLSRQIASLGIYPAVDPLDSTSR 343
Cdd:cd01136 238 DGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
60-403 |
2.09e-53 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 185.02 E-value: 2.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 60 SDGLSRGLKVEDLGHPIEVPVGKATLGRIMNVLGTPIDMKGEIETEERwSIHREAPTYEELSNSQELLETGIKVMDLICP 139
Cdd:PRK06820 81 SDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWR-ELDCPPPSPLTRQPIEQMLTTGIRAIDGILS 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 140 FAKGGKVGLFGGAGVGKTVnmmeLIRNIAiEHSGYSV--FAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNR 217
Cdd:PRK06820 160 CGEGQRIGIFAAAGVGKST----LLGMLC-ADSAADVmvLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALER 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 218 LRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAV 297
Cdd:PRK06820 235 LKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYTV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 298 YVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDVARGVQSILQRYQELKDIIAI 377
Cdd:PRK06820 315 LVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQEIELLVRV 393
|
330 340 350
....*....|....*....|....*....|
gi 490366925 378 ----LGMDELSEEdklVVARARKIQRFLSQ 403
Cdd:PRK06820 394 geyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
1-377 |
9.55e-53 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 183.36 E-value: 9.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 1 MATGKIVQVIGAVVDA---EFPQDSVPKVydalEVMNGKekLVLEVqqqLGGGIVRCIAMGTSD--GLSRGLKVEDLGHP 75
Cdd:PRK08972 24 VASGKLVRVVGLTLEAtgcRAPVGSLCSI----ETMAGE--LEAEV---VGFDGDLLYLMPIEElrGVLPGARVTPLGEQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 76 IEVPVGKATLGRIMNVLGTPIDMKGEIETEERWSIHreAPTYEELSNSQ--ELLETGIKVMDLICPFAKGGKVGLFGGAG 153
Cdd:PRK08972 95 SGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRH--SPPINPLSRRPitEPLDVGVRAINAMLTVGKGQRMGLFAGSG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 154 VGKTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD 233
Cdd:PRK08972 173 VGKSVLLGMMTRGTTAD---VIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCETATTIAEYFRD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 234 EGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKTGSITSVQAVYVPADDLTDPSPAT 311
Cdd:PRK08972 250 QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAgnGGPGQGSITAFYTVLTEGDDLQDPIADA 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490366925 312 TFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDVARGVQSILQRYQELKDIIAI 377
Cdd:PRK08972 330 SRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLISI 394
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
57-405 |
7.14e-52 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 180.58 E-value: 7.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 57 MGTSDGLSRGLKVEDLGHPIEVPVGKATLGRIMNVLGTPIDMKGEIETE----ERWSIHREAPTYEELSNSQELLETGIK 132
Cdd:PRK08149 61 IGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTVgpisEERVIDVAPPSYAERRPIREPLITGVR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 133 VMD--LICpfAKGGKVGLFGGAGVGKTVNMmelirNIAIEHSGYSVF--AGVGERTREGNDFYHEMTDSNVLDKVSLVYG 208
Cdd:PRK08149 141 AIDglLTC--GVGQRMGIFASAGCGKTSLM-----NMLIEHSEADVFviGLIGERGREVTEFVESLRASSRREKCVLVYA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 209 QMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKT 288
Cdd:PRK08149 214 TSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 289 GSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPlVVGQEHYDVARGVQSILQRY 368
Cdd:PRK08149 294 GSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQ-VTDPKHRQLAAAFRKLLTRL 372
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 490366925 369 QELKDIIAiLG---MDELSEEDKLVVARArKIQRFLSQPF 405
Cdd:PRK08149 373 EELQLFID-LGeyrRGENADNDRAMDKRP-ALEAFLKQDV 410
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
4-403 |
1.80e-49 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 174.56 E-value: 1.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 4 GKIVQVIGAVVDAefpqdSVP--KVYDALEVMNGKEKLVL--EVQqqlggGIVRCIA----MGTSDGLSRGLKVEDLGHP 75
Cdd:PRK06936 25 GRVTQVTGTILKA-----VVPgvRIGELCYLRNPDNSLSLqaEVI-----GFAQHQAlltpLGEMYGISSNTEVSPTGTM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 76 IEVPVGKATLGRIMNVLGTPIDMKGEIETEERWSIHREAPTYEELSNSQELLETGIKVMDLICPFAKGGKVGLFGGAGVG 155
Cdd:PRK06936 95 HQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 156 KTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEG 235
Cdd:PRK06936 175 KSTLLASLIRSAEVD---VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 236 RDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAH 315
Cdd:PRK06936 252 KRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVADETRSI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 316 LDATVVLSRQIASLGIYPAVDPLDSTSRQLDPlVVGQEHYDVARGVQSILQRYQELKDIIAI----LGMDELSEEdklVV 391
Cdd:PRK06936 332 LDGHIILSRKLAAANHYPAIDVLRSASRVMNQ-IVSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDKEADQ---AI 407
|
410
....*....|..
gi 490366925 392 ARARKIQRFLSQ 403
Cdd:PRK06936 408 ERIGAIRGFLRQ 419
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
4-377 |
1.89e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 174.53 E-value: 1.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 4 GKIVQVIGAVVDAEFPQDSVPKVYDALEVMNGKEKLVLEVqqqLGGGIVRCIAMGTSD--GLSRGLKVEDLGHPIEVPVG 81
Cdd:PRK07721 20 GKVSRVIGLMIESKGPESSIGDVCYIHTKGGGDKAIKAEV---VGFKDEHVLLMPYTEvaEIAPGCLVEATGKPLEVKVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 82 KATLGRIMNVLGTPIDMKGEIETEERWSIHREAPTYEELSNSQELLETGIKVMDLICPFAKGGKVGLFGGAGVGKTVNMM 161
Cdd:PRK07721 97 SGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 162 ELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLF 241
Cdd:PRK07721 177 MIARNTSAD---LNVIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLM 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 242 VDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVV 321
Cdd:PRK07721 254 MDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFV 333
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 490366925 322 LSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDVARGVQSILQRYQELKDIIAI 377
Cdd:PRK07721 334 LDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
61-433 |
8.27e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 172.56 E-value: 8.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 61 DGLSRGLKVEDLGHPIEVPVGKATLGRIMNVLGTPIDMKGEIETEERWSIHRE--APTYEELSNsqELLETGIKVMDLIC 138
Cdd:PRK08472 75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKApiAAMKRGLID--EVFSVGVKSIDGLL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 139 PFAKGGKVGLFGGAGVGKTVNMMELIRNiaiEHSGYSVFAGVGERTREGNDFYHEMTDSNvLDKVSLVYGQMNEPPGNRL 218
Cdd:PRK08472 153 TCGKGQKLGIFAGSGVGKSTLMGMIVKG---CLAPIKVVALIGERGREIPEFIEKNLGGD-LENTVIVVATSDDSPLMRK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 219 RVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKT-GSITSVQAV 297
Cdd:PRK08472 229 YGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGkGSITAFFTV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 298 YVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPlVVGQEHYDVARGVQSILQRYQELKDIIAI 377
Cdd:PRK08472 309 LVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMND-IISPEHKLAARKFKRLYSLLKENEVLIRI 387
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490366925 378 ----LGMD-ELSEedklVVARARKIQRFLSQpffvaevftgSPGKFVSLKDTIRGFKGILN 433
Cdd:PRK08472 388 gayqKGNDkELDE----AISKKEFMEQFLKQ----------NPNELFPFEQTFEQLEEILR 434
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
2-404 |
1.11e-48 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 172.65 E-value: 1.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 2 ATGKIVQVIGAVVdaefpqdsvpKVyDALEVMNGKeklVLEVQQQLGG--------GIVRCIAM----GTSDGLSRGLKV 69
Cdd:PRK09099 24 RTGKVVEVIGTLL----------RV-SGLDVTLGE---LCELRQRDGTllqraevvGFSRDVALlspfGELGGLSRGTRV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 70 EDLGHPIEVPVGKATLGRIMNVLGTPIDMKGEIETEERWSIHREAPTYEELSNSQELLETGIKVMDLICPFAKGGKVGLF 149
Cdd:PRK09099 90 IGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 150 GGAGVGKTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAE 229
Cdd:PRK09099 170 APAGVGKSTLMGMFARGTQCD---VNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 230 KFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSP 309
Cdd:PRK09099 247 YFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 310 ATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDVARGVQSILQRYQELKDIIAI----LGMDELSE 385
Cdd:PRK09099 327 EEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVAD 405
|
410
....*....|....*....
gi 490366925 386 EdklVVARARKIQRFLSQP 404
Cdd:PRK09099 406 E---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
86-379 |
5.78e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 168.25 E-value: 5.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 86 GRIMNVLGTPIDMKGEIET-EERWSIHREAPTYEELSNSQELLETGIKVMDLICPFAKGGKVGLFGGAGVGKTVNMMELI 164
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 165 RNIAIEHSgysVFAGVGERTREGNDFYHEMTDSNvLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDN 244
Cdd:PRK06002 187 RADAFDTV---VIALVGERGREVREFLEDTLADN-LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVDS 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 245 IYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVL 322
Cdd:PRK06002 263 VTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVL 342
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 490366925 323 SRQIASLGIYPAVDPLDSTSRqLDPLVVGQEHYDVARGVQSILQRYQELKDIIAILG 379
Cdd:PRK06002 343 DRAIAEQGRYPAVDPLASISR-LARHAWTPEQRKLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
2-403 |
3.98e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 163.36 E-value: 3.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 2 ATGKIVQVIGAVVDAEFPQDSVPkvyDALEVMNGKEKLVLEVQQQL---GGGIVRCIAMGTSDGLSRGLKVEDLGHPIEV 78
Cdd:PRK05688 27 VEGRLLRMVGLTLEAEGLRAAVG---SRCLVINDDSYHPVQVEAEVmgfSGDKVFLMPVGSVAGIAPGARVVPLADTGRL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 79 PVGKATLGRIMNVLGTPIDMKGEIETEERwsIHREAPTYEELSNS--QELLETGIKVMDLICPFAKGGKVGLFGGAGVGK 156
Cdd:PRK05688 104 PMGMSMLGRVLDGAGRALDGKGPMKAEDW--VPMDGPTINPLNRHpiSEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 157 TV--NMMELIRNIAIehsgySVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDE 234
Cdd:PRK05688 182 SVllGMMTRFTEADI-----IVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 235 GRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKT--GSITSVQAVYVPADDLTDPSPATT 312
Cdd:PRK05688 257 GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPggGSITAFYTVLSEGDDQQDPIADSA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 313 FAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDVARGVQSILQRYQELKDIIAI----LGMDelsEEDK 388
Cdd:PRK05688 337 RGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQQSRDLISVgayvAGGD---PETD 412
|
410
....*....|....*
gi 490366925 389 LVVARARKIQRFLSQ 403
Cdd:PRK05688 413 LAIARFPHLVQFLRQ 427
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
4-377 |
1.78e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 161.30 E-value: 1.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 4 GKIVQVIGAVVDAEFPQDSVpKVYDALEVMNGKEKLVL-EVqqqLGGGIVRCIAM--GTSDGLSRGLKVEDLGHPIEVPV 80
Cdd:PRK08927 19 GRVVAVRGLLVEVAGPIHAL-SVGARIVVETRGGRPVPcEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAVRP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 81 GKATLGRIMNVLGTPIDMKGEI-ETEERWSIHREAPTYEELSNSQELLETGIKVMDLICPFAKGGKVGLFGGAGVGKTVN 159
Cdd:PRK08927 95 SRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 160 MMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVL 239
Cdd:PRK08927 175 LSMLARNADAD---VSVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 240 LFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKTGSITSVQAVYVPADDLTDPSPATTFAHLD 317
Cdd:PRK08927 252 CLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILD 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 318 ATVVLSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDVARGVQSILQRYQELKDIIAI 377
Cdd:PRK08927 332 GHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
58-377 |
4.86e-43 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 157.04 E-value: 4.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 58 GTSDGLSRGLKVEDLGHPIEVPVGKATLGRIMNVLGTPIDmkGEIETEERWSIHREAPTYEELSN--SQELLeTGIKVMD 135
Cdd:PRK07594 71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLD--GRELPDVCWKDYDAMPPPAMVRQpiTQPLM-TGIRAID 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 136 LICPFAKGGKVGLFGGAGVGKTVNMMELIrniAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPG 215
Cdd:PRK07594 148 SVATCGEGQRVGIFSAPGVGKSTLLAMLC---NAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPAL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 216 NRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQ 295
Cdd:PRK07594 225 ERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFY 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 296 AVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDVARGVQSILQRYQELKDII 375
Cdd:PRK07594 305 TVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEVELLI 383
|
..
gi 490366925 376 AI 377
Cdd:PRK07594 384 RI 385
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
62-403 |
5.36e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 154.28 E-value: 5.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 62 GLSRGLKVEDLGHPIEVPVGKATLGRIMNVLGTPIDMKGEIETEERWSIHREAPTYEELSNSQELLETGIKVMDLICPFA 141
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 142 KGGKVGLFGGAGVGKTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVA 221
Cdd:PRK07196 154 KGQRVGLMAGSGVGKSVLLGMITRYTQAD---VVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKAT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 222 LTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT-------LAEEMGvlqeriTSTKTGSITSV 294
Cdd:PRK07196 231 ELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSafsiiprLAESAG------NSSGNGTMTAI 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 295 QAVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPlVVGQEHYDVARGVQSILQRYQELKDI 374
Cdd:PRK07196 305 YTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQ-VIGSQQAKAASLLKQCYADYMAIKPL 383
|
330 340 350
....*....|....*....|....*....|...
gi 490366925 375 IA----ILGMDELSEEdklVVARARKIQRFLSQ 403
Cdd:PRK07196 384 IPlggyVAGADPMADQ---AVHYYPAITQFLRQ 413
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
60-403 |
8.09e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 153.98 E-value: 8.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 60 SDGLSRGLKVEDLGHPIEVPVGKATLGRIMNVLGTPIDMKGEIETEERwsIHREAPTYEELSNSQ--ELLETGIKVMDLI 137
Cdd:PRK06793 73 TEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQK--IKLDAPPIHAFEREEitDVFETGIKSIDSM 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 138 CPFAKGGKVGLFGGAGVGKTVNMMELIRNiaiEHSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNR 217
Cdd:PRK06793 151 LTIGIGQKIGIFAGSGVGKSTLLGMIAKN---AKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQ 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 218 LRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPsaVGYQPTLAEE-MGVLQERITSTKTGSITSVQA 296
Cdd:PRK06793 228 LRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP--IGGKTLLMESyMKKLLERSGKTQKGSITGIYT 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 297 VYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPlVVGQEHYDVARGVQSILQRYQElKDIIA 376
Cdd:PRK06793 306 VLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEE-IVSPNHWQLANEMRKILSIYKE-NELYF 383
|
330 340 350
....*....|....*....|....*....|
gi 490366925 377 ILGMDELSEEDKLVVARARK---IQRFLSQ 403
Cdd:PRK06793 384 KLGTIQENAENAYIFECKNKvegINTFLKQ 413
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
64-377 |
7.12e-37 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 140.69 E-value: 7.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 64 SRGLKVEDLGHPIEVPVGKATLGRIMNVLGTPIDMKGEIETEERWSIHreAPTYEELSNS--QELLETGIKVMDLICPFA 141
Cdd:PRK07960 96 ARNISGEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALI--TPPFNPLQRTpiEHVLDTGVRAINALLTVG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 142 KGGKVGLFGGAGVGKTVNMMELIRniaIEHSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVA 221
Cdd:PRK07960 174 RGQRMGLFAGSGVGKSVLLGMMAR---YTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 222 LTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITS--TKTGSITSVQAVYV 299
Cdd:PRK07960 251 AYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLT 330
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490366925 300 PADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPLvVGQEHYDVARGVQSILQRYQELKDIIAI 377
Cdd:PRK07960 331 EGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAL-IDEQHYARVRQFKQLLSSFQRNRDLVSV 407
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
31-405 |
1.40e-34 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 134.18 E-value: 1.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 31 EVMNGKeklVLEVQqqlgGGIVRCIAMGTSDGLS-RGLKVEDLGHPIEVPVGKATLGRIMNVLGTPIDMKGEIETEERWS 109
Cdd:PRK04196 37 EKRRGQ---VLEVS----EDKAVVQVFEGTTGLDlKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 110 IHREA--PTYEELsnSQELLETGIKVMDLICPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYS---VFAGVGERT 184
Cdd:PRK04196 110 INGAPinPVAREY--PEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIARQAKVLGEEENfavVFAAMGITF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 185 REGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRL---RVAltgLTMAE--KFrDEGRDVLLFVDNIYRYTLAGTEVSALL 259
Cdd:PRK04196 188 EEANFFMEDFEETGALERSVVFLNLADDPAIERIltpRMA---LTAAEylAF-EKGMHVLVILTDMTNYCEALREISAAR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 260 GRMPSAVGYQPTLAEEMGVLQER--ITSTKTGSITSVQAVYVPADDLTDPSPattfahlDAT-------VVLSRQIASLG 330
Cdd:PRK04196 264 EEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyitegqIVLSRELHRKG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 331 IYPAVDPLDSTSRQLDpLVVG-----QEHYDVARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKI-QRFLSQP 404
Cdd:PRK04196 337 IYPPIDVLPSLSRLMK-DGIGegktrEDHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFeREFVNQG 415
|
.
gi 490366925 405 F 405
Cdd:PRK04196 416 F 416
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
2-76 |
1.18e-33 |
|
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: 121.08 E-value: 1.18e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490366925 2 ATGKIVQVIGAVVDAEFPQDSVPKVYDALEV-MNGKEKLVLEVQQQLGGGIVRCIAMGTSDGLSRGLKVEDLGHPI 76
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFPEGELPPIYNALEVkGDDGKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
7-429 |
1.89e-31 |
|
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: 125.96 E-value: 1.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 7 VQVIGAVVDAefpQDSVPKVYDALEVM--------NGKEKLVLEVQQQLGGGIVrciaMGTSDGLSRGLKVEDLGHPIEV 78
Cdd:TIGR00962 24 AEEVGTVVSV---GDGIARVYGLENVMsgeliefeGGVQGIALNLEEDSVGAVI----MGDYSDIREGSTVKRTGRILEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 79 PVGKATLGRIMNVLGTPIDMKGEIETEERWSIHREAPTYEELSNSQELLETGIKVMDLICPFAKGGKVGLFGGAGVGKTV 158
Cdd:TIGR00962 97 PVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 159 NMMELIRNIAIEHSgYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDV 238
Cdd:TIGR00962 177 VAIDTIINQKDSDV-YCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDNGKHA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 239 LLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTK----TGSITSVQAVYVPADDLTDPSPATTFA 314
Cdd:TIGR00962 256 LIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNdekgGGSLTALPIIETQAGDVSAYIPTNVIS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 315 HLDATVVLSRQIASLGIYPAVDPLDSTSRqldplvVG-----QEHYDVARGVQSILQRYQELkDIIAILGMDeLSEEDKL 389
Cdd:TIGR00962 336 ITDGQIFLESDLFNSGIRPAINVGLSVSR------VGgaaqiKAMKQVAGSLRLELAQYREL-EAFSQFASD-LDEATKK 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 490366925 390 VVARARKIQRFLSQPFF--------VAEVFTGSPG--KFVSLKDtIRGFK 429
Cdd:TIGR00962 408 QLERGQRVVELLKQPQYkplsveeqVVILFAGTKGylDDIPVDK-IRKFE 456
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
63-405 |
7.91e-31 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 123.48 E-value: 7.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 63 LSRGLKVEDLGHPIEVPVGKATLGRIMNVLGTPIDMKGEIETEERWSIHREAPTYEELSNSQELLETGIKVMDLICPFAK 142
Cdd:PRK05922 77 VALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 143 GGKVGLFGGAGVGKTvnmmELIRNIAI-EHSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVA 221
Cdd:PRK05922 157 GQRIGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 222 LTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAV-YVP 300
Cdd:PRK05922 233 RAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIlHYP 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 301 --ADDLTDPSPATtfahLDATVVLSRQIASLGiYPAVDPLDSTSRQLDPLVVgQEHYDVARGVQSILQRYQELKDIIAiL 378
Cdd:PRK05922 313 nhPDIFTDYLKSL----LDGHFFLTPQGKALA-SPPIDILTSLSRSARQLAL-PHHYAAAEELRSLLKAYHEALDIIQ-L 385
|
330 340
....*....|....*....|....*....
gi 490366925 379 GMDELSEEDKL--VVARARKIQRFLSQPF 405
Cdd:PRK05922 386 GAYVPGQDAHLdrAVKLLPSIKQFLSQPL 414
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
75-343 |
8.76e-31 |
|
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: 120.02 E-value: 8.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 75 PIEVPVGKATLGRIMNVLGTPIDMKGEIETEERWSIH--------REAPtyeelsnsQELLETGIKVMDLICPFAKGGKV 146
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINgppinpvaRIYP--------EEMIQTGISAIDVMNTLVRGQKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 147 GLFGGAGVGKTVNMMELIRNIAIEHSGYS---VFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALT 223
Cdd:cd01135 73 PIFSGSGLPHNELAAQIARQAGVVGSEENfaiVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 224 GLTMAEKFR-DEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQER--ITSTKTGSITSVQAVYVP 300
Cdd:cd01135 153 ALTTAEYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTMP 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 490366925 301 ADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSR 343
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
28-406 |
1.25e-28 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 118.09 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 28 DALEVMNGKEKLVLEVQQQLgggiVRCIAMGTSDGLSRGLKVEDLGHPIEVPVGKATLGRIMNVLGTPIDMKGEIETEER 107
Cdd:PRK13343 51 ELLRFEGGSRGFAFNLEEEL----VGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATAR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 108 WSIHREAPTYEELSNSQELLETGIKVMDLICPFAKGGKVGLFGGAGVGKTVNMMELIrnIAIEHSG-YSVFAGVGERTRE 186
Cdd:PRK13343 127 RPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAI--INQKDSDvICVYVAIGQKASA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 187 GNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAV 266
Cdd:PRK13343 205 VARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGRE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 267 GYQPTLAEEMGVLQERIT----STKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTS 342
Cdd:PRK13343 285 AYPGDIFYLHSRLLERAAklspELGGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVS 364
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490366925 343 RqldplvVG--QEH---YDVARGVQSILQRYQELKdIIAILGMDeLSEEDKLVVARARKIQRFLSQPFF 406
Cdd:PRK13343 365 R------VGgkAQHpaiRKESGRLRLDYAQFLELE-AFTRFGGL-LDAGTQKQITRGRRLRELLKQPRF 425
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
1-403 |
1.05e-26 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 112.95 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 1 MATGKIVQVIGAVVDAEFpqDSVPKVYDALEVmnGKEKLVLEVQQQLGGgivRCIAM---GTSdGLSRGLKVEDLGHPIE 77
Cdd:PRK04192 2 MTKGKIVRVSGPLVVAEG--MGGARMYEVVRV--GEEGLIGEIIRIEGD---KATIQvyeETS-GIKPGEPVEFTGEPLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 78 VPVGKATLGRIM------------------------------------------------NVLGT-------------PI 96
Cdd:PRK04192 74 VELGPGLLGSIFdgiqrpldelaeksgdflergvyvpaldrekkweftptvkvgdkveagDILGTvqetpsiehkimvPP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 97 DMKGEIET---------EE-------------------RWSIhREAPTYEELSNSQELLETGIKVMDLICPFAKGGKVGL 148
Cdd:PRK04192 154 GVSGTVKEivsegdytvDDtiavlededgegveltmmqKWPV-RRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 149 FGGAGVGKTVnmmeLIRNIAiehsGYS-----VFAGVGERtreGNdfyhEMTDsnVLdkvslvygqmNEPP-------GN 216
Cdd:PRK04192 233 PGPFGSGKTV----TQHQLA----KWAdadivIYVGCGER---GN----EMTE--VL----------EEFPelidpktGR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 217 RL--R-----------VA------LTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLA---- 273
Cdd:PRK04192 286 PLmeRtvliantsnmpVAareasiYTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLAsrla 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 274 ---EEMGVLqeRITSTKTGSITSVQAVYVPADDLTDP-SPAT-----TFAHLDATVVLSRQiaslgiYPAVDPLDSTSRQ 344
Cdd:PRK04192 366 efyERAGRV--KTLGGEEGSVTIIGAVSPPGGDFSEPvTQNTlrivkVFWALDAELADRRH------FPAINWLTSYSLY 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490366925 345 LDPL------VVGQEHYDVARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKI-QRFLSQ 403
Cdd:PRK04192 438 LDQVapwweeNVDPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQ 503
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
107-343 |
7.01e-26 |
|
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.
Pssm-ID: 410878 [Multi-domain] Cd Length: 288 Bit Score: 106.50 E-value: 7.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 107 RWSIHREAPTYEELSnSQELLETGIKVMDLICPFAKGGKVGLFGGAGVGKTVnmmelirniaIEH--SGYS-----VFAG 179
Cdd:cd01134 41 RWPVRQPRPVKEKLP-PNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTV----------ISQslSKWSnsdvvIYVG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 180 VGER----TREGNDFYH---EMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAG 252
Cdd:cd01134 110 CGERgnemAEVLEEFPElkdPITGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEAL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 253 TEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKT-------GSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQ 325
Cdd:cd01134 190 REISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRClgspgreGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKK 269
|
250
....*....|....*...
gi 490366925 326 IASLGIYPAVDPLDSTSR 343
Cdd:cd01134 270 LAQRRHFPSINWLISYSK 287
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
76-343 |
3.25e-23 |
|
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: 98.78 E-value: 3.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 76 IEVPVGKATLGRIMNVLGTPIDMKGEIETEERWSIHREAPTYEELSNSQELLETGIKVMDLICPFAKGGKVGLFGGAGVG 155
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 156 KTVNMMELIrniaIEHSG---YSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFR 232
Cdd:cd01132 82 KTAIAIDTI----INQKGkkvYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 233 DEGRDVLLFVDNIYRYTLAGTEVSALLGR------MPSAVGY-QPTLAEEMGVLQERItstKTGSITSVQAVYVPADDLT 305
Cdd:cd01132 158 DNGKHALIIYDDLSKQAVAYRQMSLLLRRppgreaYPGDVFYlHSRLLERAAKLSDEL---GGGSLTALPIIETQAGDVS 234
|
250 260 270
....*....|....*....|....*....|....*...
gi 490366925 306 DPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSR 343
Cdd:cd01132 235 AYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
58-403 |
2.70e-21 |
|
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: 95.94 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 58 GTSDGLSRGLKVEDLGHPIEVPVGKATLGRIMNVLGTPIDMKGEIETEERW-----SIHREAPTYEElsnsqELLETGIK 132
Cdd:TIGR01040 56 GTSGIDAKKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLdingqPINPYARIYPE-----EMIQTGIS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 133 VMDLICPFAKGGKVGLFGGAGVGKTVNMMELIRNIAI-------EHSGYS-----VFAGVGERTREGNDFYHEMTDSNVL 200
Cdd:TIGR01040 131 AIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLvklptkdVHDGHEdnfaiVFAAMGVNMETARFFKQDFEENGSM 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 201 DKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDE-GRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVL 279
Cdd:TIGR01040 211 ERVCLFLNLANDPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 280 QERI--TSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRqLDPLVVGQ----- 352
Cdd:TIGR01040 291 YERAgrVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSR-LMKSAIGEgmtrk 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 490366925 353 EHYDVARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKIQR-FLSQ 403
Cdd:TIGR01040 370 DHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQ 421
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
354-422 |
3.11e-21 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 87.11 E-value: 3.11e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490366925 354 HYDVARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKIQRFLSQPFFVAEVFTGSPGKFVSLK 422
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIK 69
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
159-415 |
2.02e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 94.70 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 159 NMMELIRNIAIEH-------SGYSVFAGVGERTREGNDFYHEM-------TDSNVLDKVSLVYGQMNEPPGNRLRVALTG 224
Cdd:PRK14698 662 NMPTLLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEFpklkdpkTGKPLMERTVLIANTSNMPVAAREASIYTG 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 225 LTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI-------TSTKTGSITSVQAV 297
Cdd:PRK14698 742 ITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAV 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 298 YVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPLV------VGQEHYDVARGVQSILQRYQEL 371
Cdd:PRK14698 822 SPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKdwwhknVDPEWKAMRDKAMELLQKEAEL 901
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490366925 372 KDIIAILGMDELSEEDKLVVARARKIQR-FLSQPFFvAEVFTGSP 415
Cdd:PRK14698 902 QEIVRIVGPDALPERERAILLVARMLREdYLQQDAF-DEVDTYCP 945
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
5-388 |
1.91e-19 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 90.09 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 5 KIVQVIGAV--VDAEFPQdsvpkvYDALEVMNGKEKLVLEVQQQLGGGIVRCIAMGTSDGLSRGLKVEDLGHPIEVPVGK 82
Cdd:PRK02118 7 KITDITGNVitVEAEGVG------YGELATVERKDGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 83 ATLGRIMNVLGTPIDMKGEIETEErwsIHREAPTYEELSNSQ--ELLETGIKVMDLICPFAKGGKVGLFGGAgvGKTVNm 160
Cdd:PRK02118 81 SLLGRRFNGSGKPIDGGPELEGEP---IEIGGPSVNPVKRIVprEMIRTGIPMIDVFNTLVESQKIPIFSVS--GEPYN- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 161 mELIRNIAIE-HSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFR-DEGRDV 238
Cdd:PRK02118 155 -ALLARIALQaEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 239 LLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTK-TGSITSVQAVYVPADDLTDPSPATTFAHLD 317
Cdd:PRK02118 234 LVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEdGGSITIIAVTTMPGDDVTHPVPDNTGYITE 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490366925 318 ATVVLSRQiaslgiypAVDPLDSTSRqLDPLVVG----QEHYDVArgvQSILQRYQELKDIIAILGMD-ELSEEDK 388
Cdd:PRK02118 314 GQFYLRRG--------RIDPFGSLSR-LKQLVIGkktrEDHGDLM---NAMIRLYADSREAKEKMAMGfKLSNWDE 377
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
52-263 |
2.41e-17 |
|
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: 84.32 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 52 VRCIAMGTSDGLSRGLKVEDLGHPIEVPVGKATLGRIMNVLGTPIDMKGEIETEERWSIHREAPTYEELSNSQELLETGI 131
Cdd:COG0056 71 VGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 132 KVMDLICPFAKGGKVGLFGGAGVGKTVnmmelirnIAIE------HSG-YSVFAGVGERtregndfyhemtDSNVldkVS 204
Cdd:COG0056 151 KAIDAMIPIGRGQRELIIGDRQTGKTA--------IAIDtiinqkGKDvICIYVAIGQK------------ASTV---AQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 205 LV-----YGQM----------NEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNI------YRytlagtEVSALLGRMP 263
Cdd:COG0056 208 VVetleeHGAMeytivvaataSDPAPLQYIAPYAGCAMGEYFMDQGKDVLIVYDDLskhavaYR------ELSLLLRRPP 281
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
6-73 |
1.20e-16 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 74.12 E-value: 1.20e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490366925 6 IVQVIGAVVDAEFPQDSVPKVYDALEV-MNGKEKLVLEVQQQLGGGIVRCIAMGTSDGLSRGLKVEDLG 73
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVeLVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
52-263 |
2.84e-16 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 80.88 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 52 VRCIAMGTSDGLSRGLKVEDLGHPIEVPVGKATLGRIMNVLGTPIDMKGEIETEERWSIHREAPTYEELSNSQELLETGI 131
Cdd:PRK09281 71 VGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 132 KVMDLICPFAKGGKVGLFGGAGVGKTVnmmelirnIAIE------HSG-YSVFAGVGERtregndfyhEMTDSNVLDKVS 204
Cdd:PRK09281 151 KAIDAMIPIGRGQRELIIGDRQTGKTA--------IAIDtiinqkGKDvICIYVAIGQK---------ASTVAQVVRKLE 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490366925 205 lVYGQM----------NEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNI------YRytlagtEVSALLGRMP 263
Cdd:PRK09281 214 -EHGAMeytivvaataSDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLskqavaYR------QLSLLLRRPP 281
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
50-371 |
2.70e-13 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 72.00 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 50 GIVRCIAMGTSDGLSRGLKVEDLGHPIEVPVGKATLGRIMNVLG--TPIDM----KGEIETEERW-SIHREAPTYEELSN 122
Cdd:PTZ00185 89 GRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGheVPVGLltrsRALLESEQTLgKVDAGAPNIVSRSP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 123 SQELLETGIKVMDLICPFAKGGKVGLFGGAGVGKT-------VNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMT 195
Cdd:PTZ00185 169 VNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTsiavstiINQVRINQQILSKNAVISIYVSIGQRCSNVARIHRLLR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 196 DSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEE 275
Cdd:PTZ00185 249 SYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 276 MGVLQERITSTKT----GSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRqldplvVG 351
Cdd:PTZ00185 329 HSRLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSR------VG 402
|
330 340
....*....|....*....|....*
gi 490366925 352 QEHYDVA-RGV----QSILQRYQEL 371
Cdd:PTZ00185 403 SSAQNVAmKAVagklKGILAEYRKL 427
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
57-343 |
6.10e-13 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 70.38 E-value: 6.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 57 MGTSDGLSRGLKVEDLGHPIEVPVGKATLGRIMNVLGTPIDMKGEIETEERWSIHREAPTYEELSNSQELLETGIKVMDL 136
Cdd:CHL00059 55 MGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 137 ICPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEhSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGN 216
Cdd:CHL00059 135 MIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQ-NVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 217 RLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGY-------QPTLAEEMGVLQERITStktG 289
Cdd:CHL00059 214 QYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYpgdvfylHSRLLERAAKLSSQLGE---G 290
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 490366925 290 SITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSR 343
Cdd:CHL00059 291 SMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSR 344
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
62-354 |
2.42e-09 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 58.94 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 62 GLSRGLKVEDLGHPIEvpvGKATLGRIMNVLGTPIDmkgeiETEERWSIHREAPTYEElsnSQELLETG-----IKVMDL 136
Cdd:PRK12608 58 NLRTGDVVEGVARPRE---RYRVLVRVDSVNGTDPE-----KLARRPHFDDLTPLHPR---ERLRLETGsddlsMRVVDL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 137 ICPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAG-VGERTREGNDFYHEMTdsnvldkvSLVYGQMN-EPP 214
Cdd:PRK12608 127 VAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDMRRSVK--------GEVYASTFdRPP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 215 GNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLA--------------GTEVSALLGrmPSAVGYQPTLAEEMGVLQ 280
Cdd:PRK12608 199 DEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAynnevessgrtlsgGVDARALQR--PKRLFGAARNIEEGGSLT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 281 erITST---KTGSitsvqavyvPADDLtdpspatTFAHLDAT----VVLSRQIASLGIYPAVDPLDSTSRQLDPLVVGQE 353
Cdd:PRK12608 277 --IIATalvDTGS---------RMDEV-------IFEEFKGTgnmeIVLDRELADKRVFPAIDIAKSGTRREELLLDSKE 338
|
.
gi 490366925 354 H 354
Cdd:PRK12608 339 L 339
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
112-382 |
2.29e-06 |
|
transcription termination factor Rho; This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding. [Transcription, Transcription factors]
Pssm-ID: 162030 [Multi-domain] Cd Length: 415 Bit Score: 49.69 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 112 REAPTYEELS----NSQELLETG-----IKVMDLICPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSG-YSVFAGVG 181
Cdd:TIGR00767 128 KNRVLFENLTplypNERLRLETStedlsTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEvELIVLLID 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 182 ERTREgndfyheMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGR 261
Cdd:TIGR00767 208 ERPEE-------VTDMQRSVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGK 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 262 MPSAvGYQPTL-------------AEEMGVLQerITST---KTGSitsvqavyvPADDLtdpspatTFAHLDAT----VV 321
Cdd:TIGR00767 281 VLSG-GVDANAlhrpkrffgaarnIEEGGSLT--IIATaliDTGS---------RMDEV-------IFEEFKGTgnmeLH 341
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490366925 322 LSRQIASLGIYPAVDPLDSTSRQlDPLVVGQEHydvargvqsiLQRYQELKDIIAilGMDE 382
Cdd:TIGR00767 342 LDRKLADRRIFPAIDIKKSGTRK-EELLLTPEE----------LQKIWVLRKIIS--PMDS 389
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
81-194 |
3.22e-05 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 46.55 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 81 GKATLGRIMNVLGTPIDMKGEIETEERWSIHREAPTYEELSNSQELLeTGIKVMDLICPFAKGGKVGLFGGAGVGKTVNM 160
Cdd:PRK14698 166 GEYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLI-TGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDG 244
|
90 100 110
....*....|....*....|....*....|....*....
gi 490366925 161 MELIRN-----IAIEHSgYSVFAGVGERTREGNDFYHEM 194
Cdd:PRK14698 245 DTLILTkefglIKIKDL-YEILDGKGKKTVEGNEEWTEL 282
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
132-366 |
1.56e-04 |
|
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: 43.35 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 132 KVMDLICPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAG-VGERTREGNDFyHEMTDSNVldkvslVYGQM 210
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTDM-RRSVKGEV------VASTF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 211 NEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAvGYQPTLA-------------EEMG 277
Cdd:cd01128 78 DEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSG-GVDANALhkpkrffgaarniEEGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 278 VLQerITST---KTGSitsvqavyvPADDLtdpspatTFAHLDAT----VVLSRQIASLGIYPAVDPLDSTSRQlDPLVV 350
Cdd:cd01128 157 SLT--IIATalvDTGS---------RMDEV-------IFEEFKGTgnmeLVLDRKLAEKRIFPAIDILKSGTRK-EELLL 217
|
250
....*....|....*.
gi 490366925 351 GQEHYDVARGVQSILQ 366
Cdd:cd01128 218 TPEELQKIWLLRRILS 233
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
142-262 |
1.06e-03 |
|
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: 39.66 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366925 142 KGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGvgertregndfyhEMTDSNVLDKVSLVYGQMNEPPGNRLRVA 221
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG-------------EDILEEVLDQLLLIIVGGKKASGSGELRL 67
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 490366925 222 LTGLTMAEKFRDEgrdvLLFVDNIYRYTLAGTEVSALLGRM 262
Cdd:smart00382 68 RLALALARKLKPD----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 ... |
363-393 |
1.32e-03 |
|
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: 38.14 E-value: 1.32e-03
10 20 30
....*....|....*....|....*....|...
gi 490366925 363 SILQRYQELKDIIAILGMDELSEEDKLV--VAR 393
Cdd:cd18111 10 EILQEEAELQEIVQLVGPDALPEEDRLTleVAR 42
|
|
| 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 ... |
369-403 |
4.10e-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: 36.64 E-value: 4.10e-03
10 20 30
....*....|....*....|....*....|....*.
gi 490366925 369 QELKDIIAILGMDELSEEDKLVVARARKI-QRFLSQ 403
Cdd:cd18112 22 KDVRALAAIVGEEALSEEDRLYLEFADRFeREFINQ 57
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
350-404 |
5.68e-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: 35.49 E-value: 5.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 490366925 350 VGQEHYDVARGVQSILQRYQELKDIIAI----LGMDelSEEDKlVVARARKIQRFLSQP 404
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIgayqAGSD--PEIDE-AIAKRPAINAFLRQG 56
|
|
| |
