|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-467 |
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: 959.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 1 MATGKIVQIIGAVVDVEFPQSAVPGVYDALKV-VEAKERLVLEVQQQLGGGVVRAIVMGSSDGLRRGMTVENTGAPISVP 79
Cdd:COG0055 3 MNTGKIVQVIGPVVDVEFPEGELPAIYNALEVeNEGGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 80 VGTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAAPSYEEQSNATELLETGVKVIDLICPFAKGGKIGLFGGAGVGKTVN 159
Cdd:COG0055 83 VGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 160 MMELINNIALQHSGLSVFAGVGERTREGNDFYHEMQEAGVVNiekpeesKVAMVYGQMNEPPGNRLRVALTGLTMAERFR 239
Cdd:COG0055 163 IMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALTMAEYFR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 240 D-EGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSVQAVYVPADDLTDPSPAT 318
Cdd:COG0055 236 DeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPAT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 319 TFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRQLDPLVVGQEHYDIARGVQQTLQRYKELKDIIAILGMDELSETDKQVV 398
Cdd:COG0055 316 TFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTV 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521099455 399 ARARKIERFLTQPYHVAEVFTGDPGIYVPLKETLRGFKGLLAGDYDDVPEQAFMYCGAIDDALENAKKL 467
Cdd:COG0055 396 ARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKL 464
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
2-467 |
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: 859.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 2 ATGKIVQIIGAVVDVEFPQSAVPGVYDALKVVEAKE-RLVLEVQQQLGGGVVRAIVMGSSDGLRRGMTVENTGAPISVPV 80
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNRAEsELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 81 GTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAAPSYEEQSNATELLETGVKVIDLICPFAKGGKIGLFGGAGVGKTVNM 160
Cdd:TIGR01039 81 GKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 161 MELINNIALQHSGLSVFAGVGERTREGNDFYHEMQEAGVVNiekpeesKVAMVYGQMNEPPGNRLRVALTGLTMAERFRD 240
Cdd:TIGR01039 161 QELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTMAEYFRD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 241 E-GRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSVQAVYVPADDLTDPSPATT 319
Cdd:TIGR01039 234 EqGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 320 FAHLDATVVLNRNIAAMGLYPAIDPLDSTSRQLDPLVVGQEHYDIARGVQQTLQRYKELKDIIAILGMDELSETDKQVVA 399
Cdd:TIGR01039 314 FAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521099455 400 RARKIERFLTQPYHVAEVFTGDPGIYVPLKETLRGFKGLLAGDYDDVPEQAFMYCGAIDDALENAKKL 467
Cdd:TIGR01039 394 RARRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
3-467 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 790.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 3 TGKIVQIIGAVVDVEFPQSAVPGVYDALKV-----VEAKERLVLEVQQQLGGGVVRAIVMGSSDGLRRGMTVENTGAPIS 77
Cdd:CHL00060 16 LGRITQIIGPVLDVAFPPGKMPNIYNALVVkgrdtAGQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 78 VPVGTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAAPSYEEQSNATELLETGVKVIDLICPFAKGGKIGLFGGAGVGKT 157
Cdd:CHL00060 96 VPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 158 VNMMELINNIALQHSGLSVFAGVGERTREGNDFYHEMQEAGVVNIEKPEESKVAMVYGQMNEPPGNRLRVALTGLTMAER 237
Cdd:CHL00060 176 VLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 238 FRDEGR-DVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSVQAVYVPADDLTDPSP 316
Cdd:CHL00060 256 FRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 317 ATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRQLDPLVVGQEHYDIARGVQQTLQRYKELKDIIAILGMDELSETDKQ 396
Cdd:CHL00060 336 ATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRL 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099455 397 VVARARKIERFLTQPYHVAEVFTGDPGIYVPLKETLRGFKGLLAGDYDDVPEQAFMYCGAIDDALENAKKL 467
Cdd:CHL00060 416 TVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANL 486
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
77-354 |
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: 558.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 77 SVPVGTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAAPSYEEQSNATELLETGVKVIDLICPFAKGGKIGLFGGAGVGK 156
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 157 TVNMMELINNIALQHSGLSVFAGVGERTREGNDFYHEMQEAGVVNIEkpEESKVAMVYGQMNEPPGNRLRVALTGLTMAE 236
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLD--GLSKVALVYGQMNEPPGARARVALTGLTMAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 237 RFRD-EGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSVQAVYVPADDLTDPS 315
Cdd:cd01133 159 YFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPA 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 521099455 316 PATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRQLDP 354
Cdd:cd01133 239 PATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
4-460 |
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: 553.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 4 GKIVQIIGAVVDVEFPQSaVPGVYDALKVVEAKErLVLEVQQQLGGGVVRAIVMGSSDGLRRGMTVENTGAPISVPVGTK 83
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDGE-LPAIHSVLRAGREGE-VVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 84 TLGRIMNVLGDAIDERGEIGAEELYSIHRAAPSYEEQSNATELLETGVKVIDLICPFAKGGKIGLFGGAGVGKTVNMMEL 163
Cdd:TIGR03305 79 TLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 164 INNIALQHSGLSVFAGVGERTREGNDFYHEMQEAGVVNiekpeesKVAMVYGQMNEPPGNRLRVALTGLTMAERFRD-EG 242
Cdd:TIGR03305 159 IHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLD-------NTVMVFGQMNEPPGARFRVGHTALTMAEYFRDdEK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 243 RDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSVQAVYVPADDLTDPSPATTFAH 322
Cdd:TIGR03305 232 QDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSH 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 323 LDATVVLNRNIAAMGLYPAIDPLDSTSRQLDPLVVGQEHYDIARGVQQTLQRYKELKDIIAILGMDELSETDKQVVARAR 402
Cdd:TIGR03305 312 LSASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRAR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 521099455 403 KIERFLTQPYHVAEVFTGDPGIYVPLKETLRGFKGLLAGDYDDVPEQAFMYCGAIDDA 460
Cdd:TIGR03305 392 RLERFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDEA 449
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
77-350 |
1.64e-117 |
|
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: 345.21 E-value: 1.64e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 77 SVPVGTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAAPSYEEQSNATELLETGVKVIDLICPFAKGGKIGLFGGAGVGK 156
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 157 TVNMMELINNIALQHSGLSVFAGVGERTREGNDFYHEMQEAGVvniekpeESKVAMVYGQMNEPPGNRLRVALTGLTMAE 236
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGA-------MERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 237 RFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTK--KGSITSVQAVYVPADDLTDP 314
Cdd:cd19476 154 YFRDNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDP 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 521099455 315 SPATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSR 350
Cdd:cd19476 234 IPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSR 269
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
130-349 |
1.41e-89 |
|
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: 271.54 E-value: 1.41e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 130 GVKVIDLICPFAKGGKIGLFGGAGVGKTVnmmeLINNIALQHS-GLSVFAGVGERTREGNDFYHEMQEAGVVniekpeeS 208
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTV----LAGMIARQASaDVVVYALIGERGREVREFIEELLGSGAL-------K 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 209 KVAMVYGQMNEPPGNRLRVALTGLTMAERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQE 288
Cdd:pfam00006 70 RTVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521099455 289 RITST--KKGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTS 349
Cdd:pfam00006 150 RAGRVkgKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
3-439 |
6.43e-70 |
|
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: 228.38 E-value: 6.43e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 3 TGKIVQIIGAVVDVEFPQSAVpGvyDALKVVEAKERLVL-EVqqqLG--GGvvRAIVM--GSSDGLRRGMTVENTGAPIS 77
Cdd:COG1157 20 SGRVTRVVGLLIEAVGPDASI-G--ELCEIETADGRPVLaEV---VGfrGD--RVLLMplGDLEGISPGARVVPTGRPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 78 VPVGTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAAPSYEEQSNATELLETGVKVIDLICPFAKGGKIGLFGGAGVGKT 157
Cdd:COG1157 92 VPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 158 VNMMELINN-------IALqhsglsvfagVGERTREGNDFY-HEMQEAG----VVniekpeeskvamVYGQMNEPPGNRL 225
Cdd:COG1157 172 TLLGMIARNteadvnvIAL----------IGERGREVREFIeDDLGEEGlarsVV------------VVATSDEPPLMRL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 226 RVALTGLTMAERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSVQAVY 305
Cdd:COG1157 230 RAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 306 VPADDLTDPSPATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRqLDPLVVGQEHYDIARGVQQTLQRYKELKDIIAI- 384
Cdd:COG1157 310 VEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISR-VMPDIVSPEHRALARRLRRLLARYEENEDLIRIg 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 521099455 385 ---LGMDElsETDkQVVARARKIERFLTQPYHVAevftgdpgiyVPLKETLRGFKGLL 439
Cdd:COG1157 389 ayqPGSDP--ELD-EAIALIPAIEAFLRQGMDER----------VSFEESLAQLAELL 433
|
|
| ATP-synt_F1_beta_C |
cd18110 |
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ... |
356-462 |
2.44e-68 |
|
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: 213.11 E-value: 2.44e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 356 VVGQEHYDIARGVQQTLQRYKELKDIIAILGMDELSETDKQVVARARKIERFLTQPYHVAEVFTGDPGIYVPLKETLRGF 435
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*..
gi 521099455 436 KGLLAGDYDDVPEQAFMYCGAIDDALE 462
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVE 107
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
77-350 |
9.24e-60 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 196.63 E-value: 9.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 77 SVPVGTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAAPSYEEQSNATELLETGVKVIDLICPFAKGGKIGLFGGAGVGK 156
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 157 TVNMMELINNIAlqhSGLSVFAGVGERTREGNDFY-HEMQEAGVvniekpeeSKVAMVYGQMNEPPGNRLRVALTGLTMA 235
Cdd:cd01136 81 STLLGMIARNTD---ADVNVIALIGERGREVREFIeKDLGEEGL--------KRSVLVVATSDESPLLRVRAAYTATAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 236 ERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSVQAVYVPADDLTDPS 315
Cdd:cd01136 150 EYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPI 229
|
250 260 270
....*....|....*....|....*....|....*
gi 521099455 316 PATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSR 350
Cdd:cd01136 230 ADEVRSILDGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
59-410 |
1.52e-53 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 185.79 E-value: 1.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 59 SSDGLRRGMTVENTGAPISVPVGTKTLGRIMNVLGDAIDErGEIGAEELYSIHRAAPSYEEQSNATELLETGVKVIDLIC 138
Cdd:PRK06820 80 SSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGIL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 139 PFAKGGKIGLFGGAGVGKTVnmmeLINNIAlQHS--GLSVFAGVGERTREGNDFYHEmqeagvvNIEKPEESKVAMVYGQ 216
Cdd:PRK06820 159 SCGEGQRIGIFAAAGVGKST----LLGMLC-ADSaaDVMVLALIGERGREVREFLEQ-------VLTPEARARTVVVVAT 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 217 MNEPPGNRLRVALTGLTMAERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKG 296
Cdd:PRK06820 227 SDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 297 SITSVQAVYVPADDLTDPSPATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRQLdPLVVGQEHYDIARGVQQTLQRYK 376
Cdd:PRK06820 307 SITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQ 385
|
330 340 350
....*....|....*....|....*....|....*...
gi 521099455 377 ELKDIIAI----LGMDelSETDkQVVARARKIERFLTQ 410
Cdd:PRK06820 386 EIELLVRVgeyqAGED--LQAD-EALQRYPAICAFLQQ 420
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
9-440 |
1.55e-53 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 185.20 E-value: 1.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 9 IIGAVVDVEFPQSAVPGVYDALKVVEAKErlVLEVQQQLGGGVVRAIV--MGSSDGLRRGMTVENTGAPISVPVGTKTLG 86
Cdd:PRK08149 13 IQGPIIEAELPDVAIGEICEIRAGWHSNE--VIARAQVVGFQRERTILslIGNAQGLSRQVVLKPTGKPLSVWVGEALLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 87 RIMNVLGdAIDER-----GEIGAEELYSIHRAAPSYEEQSNATELLETGVKVID--LICpfAKGGKIGLFGGAGVGKTVN 159
Cdd:PRK08149 91 AVLDPTG-KIVERfdappTVGPISEERVIDVAPPSYAERRPIREPLITGVRAIDglLTC--GVGQRMGIFASAGCGKTSL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 160 MMELINnialqHSGLSVF--AGVGERTREGNDFYHEMQEAgvvniekPEESKVAMVYGQMNEPPGNRLRVALTGLTMAER 237
Cdd:PRK08149 168 MNMLIE-----HSEADVFviGLIGERGREVTEFVESLRAS-------SRREKCVLVYATSDFSSVDRCNAALVATTVAEY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 238 FRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSVQAVYVPADDLTDPSPA 317
Cdd:PRK08149 236 FRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 318 TTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRQLDPlVVGQEHYDIARGVQQTLQRYKELKDIIAiLG---MDELSETD 394
Cdd:PRK08149 316 EIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQ-VTDPKHRQLAAAFRKLLTRLEELQLFID-LGeyrRGENADND 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 521099455 395 KQVVARArKIERFLTQPYHVAEVFtgdpgiyvplKETLRGFKGLLA 440
Cdd:PRK08149 394 RAMDKRP-ALEAFLKQDVAEKSSF----------SDTLERLNEFAA 428
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
61-410 |
1.62e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 172.18 E-value: 1.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 61 DGLRRGMTVENTGAPISVPVGTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAAPSYEEQSNATELLETGVKVIDLICPF 140
Cdd:PRK08472 75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTC 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 141 AKGGKIGLFGGAGVGKTVNMMELINNIALQhsgLSVFAGVGERTREGNDFYHEmqeagvvNIEKPEESKVAMVyGQMNEP 220
Cdd:PRK08472 155 GKGQKLGIFAGSGVGKSTLMGMIVKGCLAP---IKVVALIGERGREIPEFIEK-------NLGGDLENTVIVV-ATSDDS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 221 PGNRLRVALTGLTMAERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTK-KGSIT 299
Cdd:PRK08472 224 PLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSIT 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 300 SVQAVYVPADDLTDPSPATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRQLDPlVVGQEHYDIARGVQQTLQRYKELK 379
Cdd:PRK08472 304 AFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMND-IISPEHKLAARKFKRLYSLLKENE 382
|
330 340 350
....*....|....*....|....*....|....*.
gi 521099455 380 DIIAI----LGMD-ELSETdkqvVARARKIERFLTQ 410
Cdd:PRK08472 383 VLIRIgayqKGNDkELDEA----ISKKEFMEQFLKQ 414
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
4-413 |
7.04e-48 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 170.32 E-value: 7.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 4 GKIVQIIGAVVdvefpQSAVPGVYDA----LKVVEAKERLVLEV---QQQlgggVVRAIVMGSSDGLRRGMTVENTGAPI 76
Cdd:PRK06936 25 GRVTQVTGTIL-----KAVVPGVRIGelcyLRNPDNSLSLQAEVigfAQH----QALLTPLGEMYGISSNTEVSPTGTMH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 77 SVPVGTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAAPSYEEQSNATELLETGVKVIDLICPFAKGGKIGLFGGAGVGK 156
Cdd:PRK06936 96 QVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 157 TVNMMELINNIALQhsgLSVFAGVGERTREGNDFY-HEMQEAGVvniekpeeSKVAMVYGQMNEPPGNRLRVALTGLTMA 235
Cdd:PRK06936 176 STLLASLIRSAEVD---VTVLALIGERGREVREFIeSDLGEEGL--------RKAVLVVATSDRPSMERAKAGFVATSIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 236 ERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSVQAVYVPADDLTDPS 315
Cdd:PRK06936 245 EYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 316 PATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRQLDPlVVGQEHYDIARGVQQTLQRYKELKDIIAI----LGMDelS 391
Cdd:PRK06936 325 ADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQ-IVSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQD--K 401
|
410 420
....*....|....*....|..
gi 521099455 392 ETDkQVVARARKIERFLTQPYH 413
Cdd:PRK06936 402 EAD-QAIERIGAIRGFLRQGTH 422
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
78-384 |
1.79e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 169.50 E-value: 1.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 78 VPVGTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAAPSYEEQSNATELLETGVKVIDLICPFAKGGKIGLFGGAGVGKT 157
Cdd:PRK08972 97 LPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 158 V--NMMELINNIALQHSGLsvfagVGERTREGNDFYHEmqeagvvnIEKPEESKVAMVYGQ-MNEPPGNRLRVALTGLTM 234
Cdd:PRK08972 177 VllGMMTRGTTADVIVVGL-----VGERGREVKEFIEE--------ILGEEGRARSVVVAApADTSPLMRLKGCETATTI 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 235 AERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKKGSITSVQAVYVPADDLT 312
Cdd:PRK08972 244 AEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAgnGGPGQGSITAFYTVLTEGDDLQ 323
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099455 313 DPSPATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRQLdPLVVGQEHYDIARGVQQTLQRYKELKDIIAI 384
Cdd:PRK08972 324 DPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLISI 394
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
4-384 |
4.19e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 168.36 E-value: 4.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 4 GKIVQIIGAVVDVEFPQSAVPgvyDALKVVEAKErlvlevqqqlGGGVVRAIVMGSSD---------GLRR---GMTVEN 71
Cdd:PRK07721 20 GKVSRVIGLMIESKGPESSIG---DVCYIHTKGG----------GDKAIKAEVVGFKDehvllmpytEVAEiapGCLVEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 72 TGAPISVPVGTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAAPSYEEQSNATELLETGVKVIDLICPFAKGGKIGLFGG 151
Cdd:PRK07721 87 TGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 152 AGVGKTVnmmeLINNIALQHSG-LSVFAGVGERTREGNDFyhemqeagvvnIEK---PEE-SKVAMVYGQMNEPPGNRLR 226
Cdd:PRK07721 167 SGVGKST----LMGMIARNTSAdLNVIALIGERGREVREF-----------IERdlgPEGlKRSIVVVATSDQPALMRIK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 227 VALTGLTMAERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSVQAVYV 306
Cdd:PRK07721 232 GAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLV 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521099455 307 PADDLTDPSPATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRQLdPLVVGQEHYDIARGVQQTLQRYKELKDIIAI 384
Cdd:PRK07721 312 DGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
4-410 |
6.90e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 167.85 E-value: 6.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 4 GKIVQIIGAVVDVEFPQSAVpGVYDALKVVEAKERLVL-EVqqqLGGGVVRAIVM--GSSDGLRRGMTVENTGAPISVPV 80
Cdd:PRK08927 19 GRVVAVRGLLVEVAGPIHAL-SVGARIVVETRGGRPVPcEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAVRP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 81 GTKTLGRIMNVLGDAIDERGEI-GAEELYSIHRAAPSYEEQSNATELLETGVKVIDLICPFAKGGKIGLFGGAGVGKTVN 159
Cdd:PRK08927 95 SRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 160 MMELINNIAlqhSGLSVFAGVGERTREGNDFYHE-MQEAGVvniekpeeSKVAMVYGQMNEPPGNRLRVALTGLTMAERF 238
Cdd:PRK08927 175 LSMLARNAD---ADVSVIGLIGERGREVQEFLQDdLGPEGL--------ARSVVVVATSDEPALMRRQAAYLTLAIAEYF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 239 RDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKKGSITSVQAVYVPADDLTDPSP 316
Cdd:PRK08927 244 RDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPVA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 317 ATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRQLdPLVVGQEHYDIARGVQQTLQRYKELKDIIAI----LGMDelSE 392
Cdd:PRK08927 324 DAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRLgayrAGSD--PE 400
|
410
....*....|....*...
gi 521099455 393 TDkQVVARARKIERFLTQ 410
Cdd:PRK08927 401 VD-EAIRLNPALEAFLRQ 417
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
2-411 |
4.22e-45 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 163.02 E-value: 4.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 2 ATGKIVQIIGAVVDVefpqSAVPGVYDALKVVEAKERLVLEVQQQLGGGVVRAIV--MGSSDGLRRGMTVENTGAPISVP 79
Cdd:PRK09099 24 RTGKVVEVIGTLLRV----SGLDVTLGELCELRQRDGTLLQRAEVVGFSRDVALLspFGELGGLSRGTRVIGLGRPLSVP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 80 VGTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAAPSYEEQSNATELLETGVKVIDLICPFAKGGKIGLFGGAGVGKTVN 159
Cdd:PRK09099 100 VGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 160 MMELINNIALQhsgLSVFAGVGERTREGNDFY-HEMQEAGVvniekpeeSKVAMVYGQMNEPPGNRLRVALTGLTMAERF 238
Cdd:PRK09099 180 MGMFARGTQCD---VNVIALIGERGREVREFIeLILGEDGM--------ARSVVVCATSDRSSIERAKAAYVATAIAEYF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 239 RDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSVQAVYVPADDLTDPSPAT 318
Cdd:PRK09099 249 RDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 319 TFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRQLdPLVVGQEHYDIARGVQQTLQRYKELKDIIAI----LGMDELSEtd 394
Cdd:PRK09099 329 VRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVAD-- 405
|
410
....*....|....*..
gi 521099455 395 kQVVARARKIERFLTQP 411
Cdd:PRK09099 406 -EAIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
60-410 |
1.71e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 161.30 E-value: 1.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 60 SDGLRRGMTVENTGAPISVPVGTKTLGRIMNVLGDAIDErgEIGAEELYSIHRAAPSYE--EQSNATELLETGVKVIDLI 137
Cdd:PRK06793 73 TEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIHafEREEITDVFETGIKSIDSM 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 138 CPFAKGGKIGLFGGAGVGKTVNMMELINNialQHSGLSVFAGVGERTREGNDFYH-EMQEAGVvniekpeeSKVAMVYGQ 216
Cdd:PRK06793 151 LTIGIGQKIGIFAGSGVGKSTLLGMIAKN---AKADINVISLVGERGREVKDFIRkELGEEGM--------RKSVVVVAT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 217 MNEPPGNRLRVALTGLTMAERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPsaVGYQPTLAEE-MGVLQERITSTKK 295
Cdd:PRK06793 220 SDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP--IGGKTLLMESyMKKLLERSGKTQK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 296 GSITSVQAVYVPADDLTDPSPATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRQLDPlVVGQEHYDIARGVQQTLQRY 375
Cdd:PRK06793 298 GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEE-IVSPNHWQLANEMRKILSIY 376
|
330 340 350
....*....|....*....|....*....|....*...
gi 521099455 376 KElKDIIAILGMDELSETDKQVVARARKIE---RFLTQ 410
Cdd:PRK06793 377 KE-NELYFKLGTIQENAENAYIFECKNKVEginTFLKQ 413
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
86-410 |
2.62e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 160.93 E-value: 2.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 86 GRIMNVLGDAIDERGEIGA-EELYSIHRAAPSYEEQSNATELLETGVKVIDLICPFAKGGKIGLFGGAGVGKT--VNMME 162
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKStlLAMLA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 163 linnialQHSGLS--VFAGVGERTREGNDFYHE-MQEAgvvniekpeESKVAMVYGQMNEPPGNRLRVALTGLTMAERFR 239
Cdd:PRK06002 187 -------RADAFDtvVIALVGERGREVREFLEDtLADN---------LKKAVAVVATSDESPMMRRLAPLTATAIAEYFR 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 240 DEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKKGSITSVQAVYVPADDLTDPSPA 317
Cdd:PRK06002 251 DRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVAD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 318 TTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRqLDPLVVGQEHYDIARGVQQTLQRYKELKDIIAILGMDELSETD-KQ 396
Cdd:PRK06002 331 SIRGTLDGHIVLDRAIAEQGRYPAVDPLASISR-LARHAWTPEQRKLVSRLKSMIARFEETRDLRLIGGYRAGSDPDlDQ 409
|
330
....*....|....
gi 521099455 397 VVARARKIERFLTQ 410
Cdd:PRK06002 410 AVDLVPRIYEALRQ 423
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
80-440 |
4.80e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 160.06 E-value: 4.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 80 VGTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAAPSYEEQSNATELLETGVKVIDLICPFAKGGKIGLFGGAGVGKTVn 159
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSV- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 160 mmeLINNIALQHSGLSVFAG-VGERTREGNDFY-HEMQEAGVvniekpeeSKVAMVYGQMNEPPGNRLRVALTGLTMAER 237
Cdd:PRK07196 171 ---LLGMITRYTQADVVVVGlIGERGREVKEFIeHSLQAAGM--------AKSVVVAAPADESPLMRIKATELCHAIATY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 238 FRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT-------LAEEMGvlqeriTSTKKGSITSVQAVYVPADD 310
Cdd:PRK07196 240 YRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSafsiiprLAESAG------NSSGNGTMTAIYTVLAEGDD 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 311 LTDPSPATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRQLDPlVVGQEHYDIARGVQQTLQRYKELKDIIA----ILG 386
Cdd:PRK07196 314 QQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQ-VIGSQQAKAASLLKQCYADYMAIKPLIPlggyVAG 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 521099455 387 MDELSEtdkQVVARARKIERFLTQpyhvaevftgDPGIYVPLKETLRGFKGLLA 440
Cdd:PRK07196 393 ADPMAD---QAVHYYPAITQFLRQ----------EVGHPALFSASVEQLTGMFP 433
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
49-410 |
2.65e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 152.96 E-value: 2.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 49 GGVVRAIVMGSSDGLRRGMTVENTGAPISVPVGTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAAPSYEEQSNATELLE 128
Cdd:PRK05688 74 GDKVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 129 TGVKVIDLICPFAKGGKIGLFGGAGVGKTV--NMMELINNIALQHSGLsvfagVGERTREGNDFY-HEMQEAGVvniekp 205
Cdd:PRK05688 154 VGIRSINGLLTVGRGQRLGLFAGTGVGKSVllGMMTRFTEADIIVVGL-----IGERGREVKEFIeHILGEEGL------ 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 206 eeSKVAMVYGQMNEPPGNRLRVALTGLTMAERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGV 285
Cdd:PRK05688 223 --KRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 286 LQERITSTKK--GSITSVQAVYVPADDLTDPSPATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRQLdPLVVGQEHYD 363
Cdd:PRK05688 301 LVERAGNAEPggGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLR 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 521099455 364 IARGVQQTLQRYKELKDIIAI----LGMDelSETDkQVVARARKIERFLTQ 410
Cdd:PRK05688 380 RAQRFKQLWSRYQQSRDLISVgayvAGGD--PETD-LAIARFPHLVQFLRQ 427
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
58-384 |
2.70e-39 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 147.02 E-value: 2.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 58 GSSDGLRRGMTVENTGAPISVPVGTKTLGRIMNVLGDAIDERG--EIGAEELYSIhrAAPSYEEQSNATELLeTGVKVID 135
Cdd:PRK07594 71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRElpDVCWKDYDAM--PPPAMVRQPITQPLM-TGIRAID 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 136 LICPFAKGGKIGLFGGAGVGKTVNMMELINniaLQHSGLSVFAGVGERTREGNDFYHEmqeagvvNIEKPEESKVAMVYG 215
Cdd:PRK07594 148 SVATCGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGREVREFIDF-------TLSEETRKRCVIVVA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 216 QMNEPPGNRLRVALTGLTMAERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKK 295
Cdd:PRK07594 218 TSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 296 GSITSVQAVYVPADDLTDPSPATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRQLdPLVVGQEHYDIARGVQQTLQRY 375
Cdd:PRK07594 298 GSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALY 376
|
....*....
gi 521099455 376 KELKDIIAI 384
Cdd:PRK07594 377 QEVELLIRI 385
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
65-410 |
1.15e-34 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 134.53 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 65 RGMTVENTGAPISVPVGTKTLGRIMNVLGDAIDerGEIGAEELYSIHRAAPSYE--EQSNATELLETGVKVIDLICPFAK 142
Cdd:PRK07960 97 RNISGEGLQSGKQLPLGPALLGRVLDGSGKPLD--GLPAPDTGETGALITPPFNplQRTPIEHVLDTGVRAINALLTVGR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 143 GGKIGLFGGAGVGKTV--NMMELINNIALQHSGLsvfagVGERTREGNDFyhemqeagVVNIEKPE-ESKVAMVYGQMNE 219
Cdd:PRK07960 175 GQRMGLFAGSGVGKSVllGMMARYTQADVIVVGL-----IGERGREVKDF--------IENILGAEgRARSVVIAAPADV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 220 PPGNRLRVALTGLTMAERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITS--TKKGS 297
Cdd:PRK07960 242 SPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGS 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 298 ITSVQAVYVPADDLTDPSPATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRQLDPLvVGQEHYDIARGVQQTLQRYKE 377
Cdd:PRK07960 322 ITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAL-IDEQHYARVRQFKQLLSSFQR 400
|
330 340 350
....*....|....*....|....*....|....*..
gi 521099455 378 LKDIIAI----LGMDELSEtdkQVVARARKIERFLTQ 410
Cdd:PRK07960 401 NRDLVSVgayaKGSDPMLD---KAIALWPQLEAFLQQ 434
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
5-413 |
9.16e-34 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 132.26 E-value: 9.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 5 KIVQIIGAVVDVEfpqsAVPGV-YDALKVVEAK---ERL--VLEVQqqlgGGVVRAIVMGSSDGL-RRGMTVENTGAPIS 77
Cdd:PRK04196 6 TVSEIKGPLLFVE----GVEGVaYGEIVEIELPngeKRRgqVLEVS----EDKAVVQVFEGTTGLdLKDTKVRFTGEPLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 78 VPVGTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAA--PSYEEQSNatELLETGVKVIDLICPFAKGGKIGLFGGAGVG 155
Cdd:PRK04196 78 LPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPVAREYPE--EFIQTGISAIDGLNTLVRGQKLPIFSGSGLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 156 KTvnmmELINNIALQHSGLS-------VFAGVGERTREGNDFYHEMQEAGVVNiekpeesKVAMVYGQMNEPPGNRL--- 225
Cdd:PRK04196 156 HN----ELAAQIARQAKVLGeeenfavVFAAMGITFEEANFFMEDFEETGALE-------RSVVFLNLADDPAIERIltp 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 226 RVALTgltMAERFR-DEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQER--ITSTKKGSITSVQ 302
Cdd:PRK04196 225 RMALT---AAEYLAfEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 303 AVYVPADDLTDPSPATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRQLDpLVVG-----QEHYDIARGVQQTLQRYKE 377
Cdd:PRK04196 302 ILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMK-DGIGegktrEDHKDVANQLYAAYARGKD 380
|
410 420 430
....*....|....*....|....*....|....*..
gi 521099455 378 LKDIIAILGMDELSETDKQVVARARKIE-RFLTQPYH 413
Cdd:PRK04196 381 LRELAAIVGEEALSERDRKYLKFADAFErEFVNQGFD 417
|
|
| 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 |
1.62e-32 |
|
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: 118.39 E-value: 1.62e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099455 2 ATGKIVQIIGAVVDVEFPQSAVPGVYDALKVV-EAKERLVLEVQQQLGGGVVRAIVMGSSDGLRRGMTVENTGAPI 76
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFPEGELPPIYNALEVKgDDGKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
52-411 |
1.29e-28 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 118.09 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 52 VRAIVMGSSDGLRRGMTVENTGAPISVPVGTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAAPSYEEQSNATELLETGV 131
Cdd:PRK13343 71 VGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 132 KVIDLICPFAKGGKIGLFGGAGVGKTVNMMELINNialQHSG--LSVFAGVGERTREGNDFYHEMQEAGVvniekPEESK 209
Cdd:PRK13343 151 KVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN---QKDSdvICVYVAIGQKASAVARVIETLREHGA-----LEYTT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 210 VamVYGQMNEPPGNRLRVALTGLTMAERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQER 289
Cdd:PRK13343 223 V--VVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLER 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 290 IT--STKK--GSITSVQAVYVPADDLTDPSPATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRqldplVVGQEHYDIA 365
Cdd:PRK13343 301 AAklSPELggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR-----VGGKAQHPAI 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 521099455 366 RGVQQTLQ----RYKELKdIIAILGMDELSETDKQvVARARKIERFLTQP 411
Cdd:PRK13343 376 RKESGRLRldyaQFLELE-AFTRFGGLLDAGTQKQ-ITRGRRLRELLKQP 423
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
75-350 |
2.44e-28 |
|
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: 113.47 E-value: 2.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 75 PISVPVGTKTLGRIMNVLGDAIDERGEIGAEELYSIH--------RAAPSyeeqsnatELLETGVKVIDLICPFAKGGKI 146
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINgppinpvaRIYPE--------EMIQTGISAIDVMNTLVRGQKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 147 GLFGGAGvgktVNMMELINNIALQHSGLS-------VFAGVGERTREGNDFYHEMQEAGVVNiekpeesKVAMVYGQMNE 219
Cdd:cd01135 73 PIFSGSG----LPHNELAAQIARQAGVVGseenfaiVFAAMGVTMEEARFFKDDFEETGALE-------RVVLFLNLAND 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 220 PPGNRLRVALTGLTMAERFR-DEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQER--ITSTKKG 296
Cdd:cd01135 142 PTIERIITPRMALTTAEYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKG 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 521099455 297 SITSVQAVYVPADDLTDPSPATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSR 350
Cdd:cd01135 222 SITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
75-412 |
9.38e-28 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 114.62 E-value: 9.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 75 PISVPVGTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAAPSYEEQSNATELLETGVKVIDLICPFAKGGKIGLFGGAGV 154
Cdd:PRK05922 89 PPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 155 GKTvnmmELINNIAL-QHSGLSVFAGVGERTREGNDFYHEMQEAgvvniekPEESKVAMVYGQMNEPPGNRLRVALTGLT 233
Cdd:PRK05922 169 GKS----SLLSTIAKgSKSTINVIALIGERGREVREYIEQHKEG-------LAAQRTIIIASPAHETAPTKVIAGRAAMT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 234 MAERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSVQAV-YVP--ADD 310
Cdd:PRK05922 238 IAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIlHYPnhPDI 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 311 LTDPSPATtfahLDATVVLNRNIAAMGlYPAIDPLDSTSRQLDPLVVgQEHYDIARGVQQTLQRYKELKDIIAI----LG 386
Cdd:PRK05922 318 FTDYLKSL----LDGHFFLTPQGKALA-SPPIDILTSLSRSARQLAL-PHHYAAAEELRSLLKAYHEALDIIQLgayvPG 391
|
330 340
....*....|....*....|....*.
gi 521099455 387 MDElsETDKqVVARARKIERFLTQPY 412
Cdd:PRK05922 392 QDA--HLDR-AVKLLPSIKQFLSQPL 414
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
1-410 |
6.74e-24 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 104.48 E-value: 6.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 1 MATGKIVQIIGAVVDVEFPQSAvpGVYDALKVveAKERLVLEVQQqLGGGVVRAIVMGSSDGLRRGMTVENTGAPISVPV 80
Cdd:PRK04192 2 MTKGKIVRVSGPLVVAEGMGGA--RMYEVVRV--GEEGLIGEIIR-IEGDKATIQVYEETSGIKPGEPVEFTGEPLSVEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 81 GTKTLGRI-----------MNVLGDAIdERG------------------------------------------------- 100
Cdd:PRK04192 77 GPGLLGSIfdgiqrpldelAEKSGDFL-ERGvyvpaldrekkweftptvkvgdkveagdilgtvqetpsiehkimvppgv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 101 -----EIGAEELYSIH------------------------RAAPSYEEQSNATELLETGVKVIDLICPFAKGGKIGLFGG 151
Cdd:PRK04192 156 sgtvkEIVSEGDYTVDdtiavlededgegveltmmqkwpvRRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 152 AGVGKTVnmmelinniaLQHSgLS--------VFAGVGERtreGNdfyhEMQEagVVNiEKPEeskvamvygqMNEP-PG 222
Cdd:PRK04192 236 FGSGKTV----------TQHQ-LAkwadadivIYVGCGER---GN----EMTE--VLE-EFPE----------LIDPkTG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 223 NRL--R-----------VA------LTGLTMAERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLA--- 280
Cdd:PRK04192 285 RPLmeRtvliantsnmpVAareasiYTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLAsrl 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 281 ----EEMGVLqeRITSTKKGSITSVQAVYVPADDLTDP-SPAT-----TFAHLDAtvvlnrNIAAMGLYPAIDPLDSTSR 350
Cdd:PRK04192 365 aefyERAGRV--KTLGGEEGSVTIIGAVSPPGGDFSEPvTQNTlrivkVFWALDA------ELADRRHFPAINWLTSYSL 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521099455 351 QLDPL------VVGQEHYDIARGVQQTLQRYKELKDIIAILGMDELSETDKQVVARARKI-ERFLTQ 410
Cdd:PRK04192 437 YLDQVapwweeNVDPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQ 503
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
5-406 |
1.40e-23 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 102.80 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 5 KIVQIIGAVVDVEfpqsaVPGV-YDALKVVEAKERLVLEVQQQLGGGVVRAIVMGSSDGLRRGMTVENTGAPISVPVGTK 83
Cdd:PRK02118 7 KITDITGNVITVE-----AEGVgYGELATVERKDGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 84 TLGRIMNVLGDAID-------ERGEIGAEELYSIHRAAPSyeeqsnatELLETGVKVIDLICPFAKGGKIGLFGGAGvgK 156
Cdd:PRK02118 82 LLGRRFNGSGKPIDggpelegEPIEIGGPSVNPVKRIVPR--------EMIRTGIPMIDVFNTLVESQKIPIFSVSG--E 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 157 TVNmmELINNIALQ-HSGLSVFAGVGERTREGNDFYHEMQEAGVVniekpeeSKVAMVYGQMNEPPGNRLRVALTGLTMA 235
Cdd:PRK02118 152 PYN--ALLARIALQaEADIIILGGMGLTFDDYLFFKDTFENAGAL-------DRTVMFIHTASDPPVECLLVPDMALAVA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 236 ERFR-DEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKK-GSITSVQAVYVPADDLTD 313
Cdd:PRK02118 223 EKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEDgGSITIIAVTTMPGDDVTH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 314 PSPATTFAHLDATVVLNRNiaamglypAIDPLDSTSRqLDPLVVGQEHYDIARGVQQTLQR-YKELKDIIAILGMD-ELS 391
Cdd:PRK02118 303 PVPDNTGYITEGQFYLRRG--------RIDPFGSLSR-LKQLVIGKKTREDHGDLMNAMIRlYADSREAKEKMAMGfKLS 373
|
410
....*....|....*
gi 521099455 392 ETDKQVVARARKIER 406
Cdd:PRK02118 374 NWDEKLLKFSELFES 388
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
112-350 |
9.68e-23 |
|
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: 97.65 E-value: 9.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 112 RAAPSYEEQSNATELLETGVKVIDLICPFAKGGKIGLFGGAGVGKTVnmmelinniaLQHSgLS--------VFAGVGER 183
Cdd:cd01134 45 RQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTV----------ISQS-LSkwsnsdvvIYVGCGER 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 184 treGNDFYHEMQEAGVVNIEKPEES---KVAMVYGQMNEPPGNRLRVALTGLTMAERFRDEGRDVLLFIDNIYRYTLAGT 260
Cdd:cd01134 114 ---GNEMAEVLEEFPELKDPITGESlmeRTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 261 EVSALLGRMPSAVGYQPTLAEEMGVLQERI-------TSTKKGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLNRNI 333
Cdd:cd01134 191 EISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrclgSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKL 270
|
250
....*....|....*..
gi 521099455 334 AAMGLYPAIDPLDSTSR 350
Cdd:cd01134 271 AQRRHFPSINWLISYSK 287
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
159-410 |
1.42e-22 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 101.25 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 159 NMMELINNIALQH-------SGLSVFAGVGERTREGNDFYHEMQEAGVVNIEKPEESKVAMVYGQMNEPPGNRLRVALTG 231
Cdd:PRK14698 662 NMPTLLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTG 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 232 LTMAERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI-------TSTKKGSITSVQAV 304
Cdd:PRK14698 742 ITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAV 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 305 YVPADDLTDPSPATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSRQLDPLV------VGQEHYDIARGVQQTLQRYKEL 378
Cdd:PRK14698 822 SPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKdwwhknVDPEWKAMRDKAMELLQKEAEL 901
|
250 260 270
....*....|....*....|....*....|...
gi 521099455 379 KDIIAILGMDELSETDKQVVARARKI-ERFLTQ 410
Cdd:PRK14698 902 QEIVRIVGPDALPERERAILLVARMLrEDYLQQ 934
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
40-419 |
7.38e-20 |
|
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: 91.71 E-value: 7.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 40 VLEVQQQlgggvvRAIVM---GSSDGLRRGMTVENTGAPISVPVGTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAAPS 116
Cdd:TIGR01040 41 VLEVSGN------KAVVQvfeGTSGIDAKKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPIN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 117 YEEQSNATELLETGVKVIDLICPFAKGGKIGLFGGAGVGKtvnmmeliNNIALQhsgLSVFAGVGERTREGNDFYHEMQE 196
Cdd:TIGR01040 115 PYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPH--------NEIAAQ---ICRQAGLVKLPTKDVHDGHEDNF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 197 AGV-----VNIEKP-------EES----KVAMVYGQMNEPPGNRLRVALTGLTMAERFRDE-GRDVLLFIDNIYRYTLAG 259
Cdd:TIGR01040 184 AIVfaamgVNMETArffkqdfEENgsmeRVCLFLNLANDPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADAL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 260 TEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKKGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLNRNIAAMG 337
Cdd:TIGR01040 264 REVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 338 LYPAIDPLDSTSRqLDPLVVGQ-----EHYDIArgvQQTLQRYKELKDII---AILGMDELSETDKQVVARARKIER-FL 408
Cdd:TIGR01040 344 IYPPINVLPSLSR-LMKSAIGEgmtrkDHSDVS---NQLYACYAIGKDVQamkAVVGEEALSSEDLLYLEFLDKFEKnFI 419
|
410
....*....|..
gi 521099455 409 TQ-PYHVAEVFT 419
Cdd:TIGR01040 420 AQgPYENRTIFE 431
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
361-430 |
1.02e-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: 80.18 E-value: 1.02e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 361 HYDIARGVQQTLQRYKELKDIIAILGMDELSETDKQVVARARKIERFLTQPYHVAEVFTGDPGIYVPLKE 430
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
6-73 |
4.01e-18 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 78.36 E-value: 4.01e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521099455 6 IVQIIGAVVDVEFPQSAVPGVYDALKV-VEAKERLVLEVQQQLGGGVVRAIVMGSSDGLRRGMTVENTG 73
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVeLVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
76-350 |
3.02e-17 |
|
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: 81.45 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 76 ISVPVGTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAAPSYEEQSNATELLETGVKVIDLICPFAKGGKIGLFGGAGVG 155
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 156 KTVNMMELINNialQHSG--LSVFAGVGERTREGNDFYHEMQEAGvvniekpeeskvAMVY-----GQMNEPPGNRLRVA 228
Cdd:cd01132 82 KTAIAIDTIIN---QKGKkvYCIYVAIGQKRSTVAQIVKTLEEHG------------AMEYtivvaATASDPAPLQYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 229 LTGLTMAERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGR------MPSAVGY-QPTLAEEMGVLQERItstKKGSITSV 301
Cdd:cd01132 147 YAGCAMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRppgreaYPGDVFYlHSRLLERAAKLSDEL---GGGSLTAL 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 521099455 302 QAVYVPADDLTDPSPATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSR 350
Cdd:cd01132 224 PIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
52-270 |
4.85e-17 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 83.19 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 52 VRAIVMGSSDGLRRGMTVENTGAPISVPVGTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAAPSYEEQSNATELLETGV 131
Cdd:PRK09281 71 VGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 132 KVIDLICPFAKGGKIGLFGGAGVGKTVnmmelinnIAL-----QHSG--LSVFAGVGERtregndfyhemqEAGVVNIEK 204
Cdd:PRK09281 151 KAIDAMIPIGRGQRELIIGDRQTGKTA--------IAIdtiinQKGKdvICIYVAIGQK------------ASTVAQVVR 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521099455 205 PEESKVAMVY-----GQMNEPPGNRLRVALTGLTMAERFRDEGRDVLLFIDNI------YRytlagtEVSALLGRMP 270
Cdd:PRK09281 211 KLEEHGAMEYtivvaATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLskqavaYR------QLSLLLRRPP 281
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
50-350 |
1.06e-13 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 73.15 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 50 GVVRAIVMGSSDGLRRGMTVENTGAPISVPVGTKTLGRIMNVLGDAID------ERGEIGAEE-LYSIHRAAPSYEEQSN 122
Cdd:PTZ00185 89 GRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrSRALLESEQtLGKVDAGAPNIVSRSP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 123 ATELLETGVKVIDLICPFAKGGKIGLFGGAGVGKT-------VNMMELINNIALQHSGLSVFAGVGERTREGNDFYHEMQ 195
Cdd:PTZ00185 169 VNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTsiavstiINQVRINQQILSKNAVISIYVSIGQRCSNVARIHRLLR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 196 EAGVVNIEKPEESKVAmvygqmnEPPGNRLRVALTGLTMAERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGY 275
Cdd:PTZ00185 249 SYGALRYTTVMAATAA-------EPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAY 321
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521099455 276 QPTLAEEMGVLQER--ITSTKK--GSITSVQAVYVPADDLTDPSPATTFAHLDATVVLNRNIAAMGLYPAIDPLDSTSR 350
Cdd:PTZ00185 322 PGDVFYLHSRLLERaaMLSPGKggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSR 400
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
52-270 |
4.25e-12 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 68.07 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 52 VRAIVMGSSDGLRRGMTVENTGAPISVPVGTKTLGRIMNVLGDAIDERGEIGAEELYSIHRAAPSYEEQSNATELLETGV 131
Cdd:CHL00059 50 VGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 132 KVIDLICPFAKGGKIGLFGGAGVGKTVNMMELINNIALQhSGLSVFAGVGERTRegndfyhemQEAGVVNIekpEESKVA 211
Cdd:CHL00059 130 IAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQ-NVICVYVAIGQKAS---------SVAQVVTT---LQERGA 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099455 212 MVY-----GQMNEPPGNRLRVALTGLTMAERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMP 270
Cdd:CHL00059 197 MEYtivvaETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPP 260
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
62-361 |
3.89e-09 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 58.17 E-value: 3.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 62 GLRRGMTVENTGAPISvpvGTKTLGRIMNVLGDAIDERGEigaeeLYSIHRAAPSYEEQSnatELLETG-----VKVIDL 136
Cdd:PRK12608 58 NLRTGDVVEGVARPRE---RYRVLVRVDSVNGTDPEKLAR-----RPHFDDLTPLHPRER---LRLETGsddlsMRVVDL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 137 ICPFAKGGKIGLFGGAGVGKTVNMMELINNIALQHSGLSVFAG-VGERTREGNDFYHEMQeagvvniekpeeskvAMVYG 215
Cdd:PRK12608 127 VAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDMRRSVK---------------GEVYA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 216 QMN-EPPGNRLRVALTGLTMAERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAvgyqptlaeemGVLQERITSTK 294
Cdd:PRK12608 192 STFdRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAYNNEVESSGRTLSG-----------GVDARALQRPK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 295 K-----------GSITSVQAVYVP----ADDLtdpspatTFAHLDAT----VVLNRNIAAMGLYPAIDPLDSTSRQLDPL 355
Cdd:PRK12608 261 RlfgaarnieegGSLTIIATALVDtgsrMDEV-------IFEEFKGTgnmeIVLDRELADKRVFPAIDIAKSGTRREELL 333
|
....*.
gi 521099455 356 VVGQEH 361
Cdd:PRK12608 334 LDSKEL 339
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
132-373 |
1.56e-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: 46.99 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 132 KVIDLICPFAKGGKIGLFGGAGVGKTVNMMELINNIALQHSG--LSVFAgVGERTREGNDfyheMQEAgvvniekpeeSK 209
Cdd:TIGR00767 157 RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEveLIVLL-IDERPEEVTD----MQRS----------VK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 210 VAMVYGQMNEPPGNRLRVALTGLTMAERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAvgyqptlaeemGVLQER 289
Cdd:TIGR00767 222 GEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKVLSG-----------GVDANA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 290 ITSTKK-----------GSITSVQAVYVPADDLTDpspATTFAHLDAT----VVLNRNIAAMGLYPAIDPLDSTSRQlDP 354
Cdd:TIGR00767 291 LHRPKRffgaarnieegGSLTIIATALIDTGSRMD---EVIFEEFKGTgnmeLHLDRKLADRRIFPAIDIKKSGTRK-EE 366
|
250
....*....|....*....
gi 521099455 355 LVVGQEHYDIARGVQQTLQ 373
Cdd:TIGR00767 367 LLLTPEELQKIWVLRKIIS 385
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
132-387 |
4.73e-05 |
|
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: 44.89 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 132 KVIDLICPFAKGGKIGLFGGAGVGKTVNMMELINNIALQHSGLSVFAG-VGERTREGNDfyheMQEAgvVNIEkpeeskv 210
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRS--VKGE------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 211 aMVYGQMNEPPGNRLRVALTGLTMAERFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAvGYQPTlaeEMGVLQERI 290
Cdd:cd01128 72 -VVASTFDEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSG-GVDAN---ALHKPKRFF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 291 TSTKK----GSITSVQAVYVP----ADDLtdpspatTFAHLDAT----VVLNRNIAAMGLYPAIDPLDSTSRQlDPLVVG 358
Cdd:cd01128 147 GAARNieegGSLTIIATALVDtgsrMDEV-------IFEEFKGTgnmeLVLDRKLAEKRIFPAIDILKSGTRK-EELLLT 218
|
250 260
....*....|....*....|....*....
gi 521099455 359 QEHYDIARGVQQTLQRYKELKDIIAILGM 387
Cdd:cd01128 219 PEELQKIWLLRRILSPMDPIEAMEFLLKK 247
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
357-413 |
5.90e-04 |
|
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: 38.18 E-value: 5.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099455 357 VGQEHYDIARGVQQTLQRYKELKDIIAI----LGMDelSETDkQVVARARKIERFLTQPYH 413
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIgayqAGSD--PEID-EAIAKRPAINAFLRQGVD 58
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
133-254 |
1.26e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 40.89 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 133 VIDLICPFAKG--GKIglfggagV-----GKTVNMMELINNIALQHSGLSVFAG-VGERTREGNDfyheMQEAgvVNIEk 204
Cdd:PRK09376 159 IIDLIAPIGKGqrGLI-------VappkaGKTVLLQNIANSITTNHPEVHLIVLlIDERPEEVTD----MQRS--VKGE- 224
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 521099455 205 peeskvaMVYGQMNEPPGNRLRVALTGLTMAERFRDEGRDVLLFIDNIYR 254
Cdd:PRK09376 225 -------VVASTFDEPAERHVQVAEMVIEKAKRLVEHGKDVVILLDSITR 267
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
3-74 |
2.07e-03 |
|
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: 36.91 E-value: 2.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521099455 3 TGKIVQIIGAVVDVEFPQSavPGVYDALKVVEAKERLVLEVQQQ---LGGGVVRAIVMGSSDGLRRGMTVENTGA 74
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGE--VAIGEVCEIERGDGNNETVLKAEvigFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
125-350 |
2.39e-03 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 40.34 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 125 ELLETGVKVIDLICPFAKGGKIGLFGGAGVGKT---VNMMelIN----NIAlqhsglSVFAGVGERTREGNDFYHEMQEA 197
Cdd:PRK07165 125 EQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKThiaLNTI--INqkntNVK------CIYVAIGQKRENLSRIYETLKEH 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 198 GVVN----IEKPEESkvamVYGQMNEPpgnrlrvaLTGLTMAERFRDEgRDVLLFID------NIYRytlagtEVSALLG 267
Cdd:PRK07165 197 DALKntiiIDAPSTS----PYEQYLAP--------YVAMAHAENISYN-DDVLIVFDdltkhaNIYR------EIALLTN 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099455 268 R------MPSAVGYQPTlaeemgVLQERITSTK-KGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLNRNIAAMGLYP 340
Cdd:PRK07165 258 KpvgkeaFPGDMFFAHS------KLLERAGKFKnRKTITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLP 331
|
250
....*....|
gi 521099455 341 AIDPLDSTSR 350
Cdd:PRK07165 332 AIDIDLSVSR 341
|
|
| 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 ... |
376-410 |
3.26e-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: 3.26e-03
10 20 30
....*....|....*....|....*....|....*.
gi 521099455 376 KELKDIIAILGMDELSETDKQVVARARKIE-RFLTQ 410
Cdd:cd18112 22 KDVRALAAIVGEEALSEEDRLYLEFADRFErEFINQ 57
|
|
| |
