|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
6-467 |
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: 976.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 6 STPITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQG-KLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPIS 84
Cdd:COG0055 1 MAMNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEGGgELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 85 VPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKT 164
Cdd:COG0055 81 VPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 165 VFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGARARVALTGLTIAEYFR 244
Cdd:COG0055 161 VLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD-----KTALVFGQMNEPPGARLRVALTALTMAEYFR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 245 DEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPAT 324
Cdd:COG0055 236 DEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPAT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 325 TFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTV 404
Cdd:COG0055 316 TFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTV 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300193118 405 ERARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIEDVV 467
Cdd:COG0055 396 ARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAV 458
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
9-467 |
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: 896.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 9 ITGKVTAVIGAIVDVHFEQSELPAILNALEIKTP-QGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPV 87
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNRaESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 88 GRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFI 167
Cdd:TIGR01039 81 GKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 168 QELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGARARVALTGLTIAEYFRDEE 247
Cdd:TIGR01039 161 QELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID-----KTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 248 GQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFA 327
Cdd:TIGR01039 236 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 328 HLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERA 407
Cdd:TIGR01039 316 HLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 408 RKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIEDVV 467
Cdd:TIGR01039 396 RRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVV 455
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
10-467 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 815.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 10 TGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQG-----KLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPIS 84
Cdd:CHL00060 16 LGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTagqeiNVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 85 VPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKT 164
Cdd:CHL00060 96 VPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 165 VFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLE--GESKVALVFGQMNEPPGARARVALTGLTIAEY 242
Cdd:CHL00060 176 VLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQniAESKVALVYGQMNEPPGARMRVGLTALTMAEY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 243 FRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAP 322
Cdd:CHL00060 256 FRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 323 ATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKL 402
Cdd:CHL00060 336 ATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRL 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300193118 403 TVERARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIEDVV 467
Cdd:CHL00060 416 TVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEAT 480
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
84-359 |
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: 609.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 84 SVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGK 163
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 164 TVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYF 243
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 244 RDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPA 323
Cdd:cd01133 161 RDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPA 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 300193118 324 TTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLD 359
Cdd:cd01133 241 TTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILD 276
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
11-465 |
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: 588.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 11 GKVTAVIGAIVDVHFEQsELPAILNALEIKTpQGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRE 90
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDG-ELPAIHSVLRAGR-EGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 91 TLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQEL 170
Cdd:TIGR03305 79 TLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 171 INNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQD 250
Cdd:TIGR03305 159 IHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLD-----NTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 251 VLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLD 330
Cdd:TIGR03305 234 VLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 331 ATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKI 410
Cdd:TIGR03305 314 ASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 300193118 411 QRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIED 465
Cdd:TIGR03305 394 ERFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDE 448
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
84-357 |
4.18e-131 |
|
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: 380.26 E-value: 4.18e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 84 SVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGK 163
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 164 TVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVinlegESKVALVFGQMNEPPGARARVALTGLTIAEYF 243
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGA-----MERTVVVANTANDPPGARMRVPYTGLTIAEYF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 244 RDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTK--KGSVTSVQAVYVPADDLTDPA 321
Cdd:cd19476 156 RD-NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDPI 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 300193118 322 PATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRL 357
Cdd:cd19476 235 PDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
137-355 |
6.07e-91 |
|
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: 275.39 E-value: 6.07e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 137 GIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKahgGFSVFTGVGERTREGNDLYREMKETGVInlegeSKVA 216
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL-----KRTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 217 LVFGQMNEPPGARARVALTGLTIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERI 296
Cdd:pfam00006 73 VVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300193118 297 TTT--KKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKS 355
Cdd:pfam00006 152 GRVkgKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 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 ... |
362-467 |
1.78e-70 |
|
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: 218.89 E-value: 1.78e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 362 VVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASF 441
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*.
gi 300193118 442 KAVLEGKYDNIPEHAFYMVGGIEDVV 467
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAV 106
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
1-417 |
5.64e-68 |
|
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: 223.75 E-value: 5.64e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 1 ASAAQSTPITGKVTAVIGAIVDVhfeqSELPAILNAL-EIKTPQGKLVL-EVaqhLG--ENTVRTIAMDGTEGLVRGEKV 76
Cdd:COG1157 11 LEELPPVRVSGRVTRVVGLLIEA----VGPDASIGELcEIETADGRPVLaEV---VGfrGDRVLLMPLGDLEGISPGARV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 77 LDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLF 156
Cdd:COG1157 84 VPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 157 GGAGVGKTVfiqeLINNIAKahggfsvFTG--------VGERTREGND-LYREMKEtgvinlEGESKVALVFGQMNEPPG 227
Cdd:COG1157 164 AGSGVGKST----LLGMIAR-------NTEadvnvialIGERGREVREfIEDDLGE------EGLARSVVVVATSDEPPL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 228 ARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSV 307
Cdd:COG1157 227 MRLRAAYTATAIAEYFRD-QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 308 QAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDaAVVGQEHYDVASKVQETLQTYKSLQDI 387
Cdd:COG1157 306 YTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMP-DIVSPEHRALARRLRRLLARYEENEDL 384
|
410 420 430
....*....|....*....|....*....|....
gi 300193118 388 IAI----LGMDElsEQDKlTVERARKIQRFLSQP 417
Cdd:COG1157 385 IRIgayqPGSDP--ELDE-AIALIPAIEAFLRQG 415
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
84-357 |
1.05e-61 |
|
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: 202.02 E-value: 1.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 84 SVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGK 163
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 164 TVFIQELINNIAKAhggFSVFTGVGERTREgndlYREMKEtGVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYF 243
Cdd:cd01136 81 STLLGMIARNTDAD---VNVIALIGERGRE----VREFIE-KDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 244 RDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPA 323
Cdd:cd01136 153 RDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIAD 231
|
250 260 270
....*....|....*....|....*....|....
gi 300193118 324 TTFAHLDATTVLSRGISELGIYPAVDPLDSKSRL 357
Cdd:cd01136 232 EVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
65-416 |
2.92e-51 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 180.01 E-value: 2.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 65 DGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRkPIHADPPSFAEQSTSAEILETGIKVVDLL 144
Cdd:PRK06820 79 ASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWR-ELDCPPPSPLTRQPIEQMLTTGIRAIDGI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 145 APYARGGKIGLFGGAGVGKTVFIQELInniAKAHGGFSVFTGVGERTREgndlYREMKETgVINLEGESKVALVFGQMNE 224
Cdd:PRK06820 158 LSCGEGQRIGIFAAAGVGKSTLLGMLC---ADSAADVMVLALIGERGRE----VREFLEQ-VLTPEARARTVVVVATSDR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 225 PPGARARVALTGLTIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSV 304
Cdd:PRK06820 230 PALERLKGLSTATTIAEYFRDR-GKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSI 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 305 TSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDaAVVGQEHYDVASKVQETLQTYKSL 384
Cdd:PRK06820 309 TAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMP-QIVSAGQLAMAQKLRRMLACYQEI 387
|
330 340 350
....*....|....*....|....*....|....*
gi 300193118 385 QDIIAIlgMDELSEQDKLT---VERARKIQRFLSQ 416
Cdd:PRK06820 388 ELLVRV--GEYQAGEDLQAdeaLQRYPAICAFLQQ 420
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
2-416 |
4.43e-51 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 179.18 E-value: 4.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 2 SAAQSTP---ITGKVTAVIGAIVDV---HFEQSELPAILNALEIKTPQGKLVLEVAQH-----LGEntvrtiamdgTEGL 70
Cdd:PRK06936 13 HAIVGSRliqIRGRVTQVTGTILKAvvpGVRIGELCYLRNPDNSLSLQAEVIGFAQHQalltpLGE----------MYGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 71 VRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARG 150
Cdd:PRK06936 83 SSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 151 GKIGLFGGAGVGKTVFIQELINNiakAHGGFSVFTGVGERTREgndlYREMKETGvINLEGESKVALVFGQMNEPPGARA 230
Cdd:PRK06936 163 QRMGIFAAAGGGKSTLLASLIRS---AEVDVTVLALIGERGRE----VREFIESD-LGEEGLRKAVLVVATSDRPSMERA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 231 RVALTGLTIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAV 310
Cdd:PRK06936 235 KAGFVATSIAEYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 311 YVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDaAVVGQEHYDVASKVQETLQTYKSLQDIIAI 390
Cdd:PRK06936 314 LVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELLLQI 392
|
410 420 430
....*....|....*....|....*....|
gi 300193118 391 ----LGMDELSEQdklTVERARKIQRFLSQ 416
Cdd:PRK06936 393 geyqKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
10-417 |
1.18e-50 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 178.42 E-value: 1.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 10 TGKVTAVIGAIVDVhfeqSELPAILNAL-EIKTPQGKLvLEVAQHLG-ENTVRTIAMDGT-EGLVRGEKVLDTGGPISVP 86
Cdd:PRK09099 25 TGKVVEVIGTLLRV----SGLDVTLGELcELRQRDGTL-LQRAEVVGfSRDVALLSPFGElGGLSRGTRVIGLGRPLSVP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 87 VGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVf 166
Cdd:PRK09099 100 VGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKST- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 167 iqeLINNIAK-AHGGFSVFTGVGERTREgndlYREMKETgVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRD 245
Cdd:PRK09099 179 ---LMGMFARgTQCDVNVIALIGERGRE----VREFIEL-ILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 246 EeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATT 325
Cdd:PRK09099 251 R-GLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 326 FAHLDATTVLSRGISELGIYPAVDPLDSKSRLLdAAVVGQEHYDVASKVQETLQTYKSLQDIIAI----LGMDELSEQdk 401
Cdd:PRK09099 330 RGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVADE-- 406
|
410
....*....|....*.
gi 300193118 402 lTVERARKIQRFLSQP 417
Cdd:PRK09099 407 -AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
81-392 |
1.75e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 177.88 E-value: 1.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 81 GPISVPVGRETLGRIINVIGEPIDERGPIKSKLRK-PIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGA 159
Cdd:PRK06002 95 GPLRIRPDPSWKGRVINALGEPIDGLGPLAPGTRPmSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGS 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 160 GVGKTVfiqeLINNIAKAHGGFSVFTG-VGERTREgndlYREM-KETGVINLegeSKVALVFGQMNEPPGARARVALTGL 237
Cdd:PRK06002 175 GVGKST----LLAMLARADAFDTVVIAlVGERGRE----VREFlEDTLADNL---KKAVAVVATSDESPMMRRLAPLTAT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 238 TIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERI--TTTKKGSVTSVQAVYVPAD 315
Cdd:PRK06002 244 AIAEYFRDR-GENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGD 322
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300193118 316 DLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHyDVASKVQETLQTYKSLQDIIAILG 392
Cdd:PRK06002 323 DHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQR-KLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
11-390 |
6.07e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 176.45 E-value: 6.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 11 GKVTAVIGAIVDVHFEQSELPAILNALEIKTPQGKLVLEVAQHLGENtVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRE 90
Cdd:PRK07721 20 GKVSRVIGLMIESKGPESSIGDVCYIHTKGGGDKAIKAEVVGFKDEH-VLLMPYTEVAEIAPGCLVEATGKPLEVKVGSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 91 TLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVfiqeL 170
Cdd:PRK07721 99 LIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKST----L 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 171 INNIAK-AHGGFSVFTGVGERTREgndlYREMKETGvINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEeGQ 249
Cdd:PRK07721 175 MGMIARnTSADLNVIALIGERGRE----VREFIERD-LGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQ-GL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 250 DVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHL 329
Cdd:PRK07721 249 NVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTVRGIL 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300193118 330 DATTVLSRGISELGIYPAVDPLDSKSRLLDaAVVGQEHYDVASKVQETLQTYKSLQDIIAI 390
Cdd:PRK07721 329 DGHFVLDRQLANKGQYPAINVLKSVSRVMN-HIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
9-390 |
4.93e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 174.01 E-value: 4.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 9 ITGKVTAVIGAIVDVHFEQSELpAILNALEIKTPQGKLVL-EVaqhLGENTVRTIAM--DGTEGLVRGEKVLDTGGPISV 85
Cdd:PRK08927 17 IYGRVVAVRGLLVEVAGPIHAL-SVGARIVVETRGGRPVPcEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 86 PVGRETLGRIINVIGEPIDERGPI-KSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKT 164
Cdd:PRK08927 93 RPSRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 165 VFIQELINNIAKAhggFSVFTGVGERTREgndlYREMKETgVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFR 244
Cdd:PRK08927 173 VLLSMLARNADAD---VSVIGLIGERGRE----VQEFLQD-DLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 245 DeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERI--TTTKKGSVTSVQAVYVPADDLTDPAP 322
Cdd:PRK08927 245 D-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPVA 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300193118 323 ATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAvVGQEHYDVASKVQETLQTYKSLQDIIAI 390
Cdd:PRK08927 324 DAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGC-NDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
8-390 |
1.58e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 172.58 E-value: 1.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 8 PITGKVTAVIGaivdVHFEQSELPAILNAL-EIKTPQGKLVLEVAQHLGENTVrTIAMDGTEGLVRGEKVLDTGGPISVP 86
Cdd:PRK08972 24 VASGKLVRVVG----LTLEATGCRAPVGSLcSIETMAGELEAEVVGFDGDLLY-LMPIEELRGVLPGARVTPLGEQSGLP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 87 VGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVf 166
Cdd:PRK08972 99 VGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSV- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 167 iqeLINNIAKAHGGFSVFTG-VGERTREGNDLYREmketgVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRD 245
Cdd:PRK08972 178 ---LLGMMTRGTTADVIVVGlVGERGREVKEFIEE-----ILGEEGRARSVVVAAPADTSPLMRLKGCETATTIAEYFRD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 246 eEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITT--TKKGSVTSVQAVYVPADDLTDPAPA 323
Cdd:PRK08972 250 -QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNggPGQGSITAFYTVLTEGDDLQDPIAD 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300193118 324 TTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLdAAVVGQEHYDVASKVQETLQTYKSLQDIIAI 390
Cdd:PRK08972 329 ASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLISI 394
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
68-416 |
4.25e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 171.41 E-value: 4.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 68 EGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPY 147
Cdd:PRK08472 75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTC 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 148 ARGGKIGLFGGAGVGKTVFIQELINNiAKAHggFSVFTGVGERTregndlyREMKETGVINLEGE-SKVALVFGQMNEPP 226
Cdd:PRK08472 155 GKGQKLGIFAGSGVGKSTLMGMIVKG-CLAP--IKVVALIGERG-------REIPEFIEKNLGGDlENTVIVVATSDDSP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 227 GARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTK-KGSVT 305
Cdd:PRK08472 225 LMRKYGAFCAMSVAEYFKN-QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSIT 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 306 SVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDaAVVGQEHYDVASKVQETLQTYKSLQ 385
Cdd:PRK08472 304 AFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENE 382
|
330 340 350
....*....|....*....|....*....|....*.
gi 300193118 386 DIIAI----LGMD-ELSEqdklTVERARKIQRFLSQ 416
Cdd:PRK08472 383 VLIRIgayqKGNDkELDE----AISKKEFMEQFLKQ 414
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
43-416 |
1.70e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 169.77 E-value: 1.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 43 QGKLVLEVAQHLGENTVrTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPP 122
Cdd:PRK06793 50 EHNVLCEVIAIEKENNM-LLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 123 SFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVfiqeLINNIAK-AHGGFSVFTGVGERTREGNDLYRem 201
Cdd:PRK06793 129 HAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST----LLGMIAKnAKADINVISLVGERGREVKDFIR-- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 202 KETGVinlEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAvGY 281
Cdd:PRK06793 203 KELGE---EGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVKELPIG-GK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 282 QPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDaA 361
Cdd:PRK06793 278 TLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-E 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 300193118 362 VVGQEHYDVASKVQETLQTYKSlQDIIAILGMDELSEQDKLTVERARK---IQRFLSQ 416
Cdd:PRK06793 357 IVSPNHWQLANEMRKILSIYKE-NELYFKLGTIQENAENAYIFECKNKvegINTFLKQ 413
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
47-424 |
5.57e-45 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 162.86 E-value: 5.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 47 VLEVAQHLGENTVRTI--AMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEpIDER------GPIKSKLRkPIH 118
Cdd:PRK08149 42 VIARAQVVGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGK-IVERfdapptVGPISEER-VID 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 119 ADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNiakAHGGFSVFTGVGERTREGNDLY 198
Cdd:PRK08149 120 VAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGERGREVTEFV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 199 REMKETGvinleGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSA 278
Cdd:PRK08149 197 ESLRASS-----RREKCVLVYATSDFSSVDRCNAALVATTVAEYFRD-QGKRVVLFIDSMTRYARALRDVALAAGELPAR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 279 VGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLL 358
Cdd:PRK08149 271 RGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVF 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300193118 359 DaAVVGQEHYDVASKVQETLQTYKSLQDIIAiLG---MDELSEQDKlTVERARKIQRFLSQPFAVAEVF 424
Cdd:PRK08149 351 G-QVTDPKHRQLAAAFRKLLTRLEELQLFID-LGeyrRGENADNDR-AMDKRPALEAFLKQDVAEKSSF 416
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
68-416 |
5.86e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 157.58 E-value: 5.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 68 EGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPY 147
Cdd:PRK05688 86 AGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTV 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 148 ARGGKIGLFGGAGVGKTVFIqelinniakahGGFSVFTG--------VGERTREGNDLYREmketgVINLEGESKVALVF 219
Cdd:PRK05688 166 GRGQRLGLFAGTGVGKSVLL-----------GMMTRFTEadiivvglIGERGREVKEFIEH-----ILGEEGLKRSVVVA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 220 GQMNEPPGARARVALTGLTIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTT 299
Cdd:PRK05688 230 SPADDAPLMRLRAAMYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 300 KKG--SVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLdAAVVGQEHYDVASKVQET 377
Cdd:PRK05688 309 EPGggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQL 387
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 300193118 378 LQTYKSLQDIIAI----LGMDelSEQDkLTVERARKIQRFLSQ 416
Cdd:PRK05688 388 WSRYQQSRDLISVgayvAGGD--PETD-LAIARFPHLVQFLRQ 427
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
67-390 |
3.73e-42 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 155.11 E-value: 3.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 67 TEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERgPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAP 146
Cdd:PRK07594 73 TIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVAT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 147 YARGGKIGLFGGAGVGKTVFIQELINniaKAHGGFSVFTGVGERTREgndlYREMKETgVINLEGESKVALVFGQMNEPP 226
Cdd:PRK07594 152 CGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGRE----VREFIDF-TLSEETRKRCVIVVATSDRPA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 227 GARARVALTGLTIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTS 306
Cdd:PRK07594 224 LERVRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 307 VQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLdAAVVGQEHYDVASKVQETLQTYKSLQD 386
Cdd:PRK07594 303 FYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEVEL 381
|
....
gi 300193118 387 IIAI 390
Cdd:PRK07594 382 LIRI 385
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
38-418 |
9.31e-42 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 154.60 E-value: 9.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 38 EIKTPQGKL----VLEVAqhlGENTVRTIaMDGTEGL-VRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSK 112
Cdd:PRK04196 30 EIELPNGEKrrgqVLEVS---EDKAVVQV-FEGTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 113 LRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKtvfiQELINNI---AKAHGGFS----VFT 185
Cdd:PRK04196 106 KRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPH----NELAAQIarqAKVLGEEEnfavVFA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 186 GVGERTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGAR---ARVAltgLTIAEYFRDEEGQDVLLFIDNIFRFT 262
Cdd:PRK04196 182 AMGITFEEANFFMEDFEETGALE-----RSVVFLNLADDPAIERiltPRMA---LTAAEYLAFEKGMHVLVILTDMTNYC 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 263 QAGSEVSALLGRIPSAVGYQPTLATDMGLLQER--ITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIS 340
Cdd:PRK04196 254 EALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELH 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 341 ELGIYPAVDPLDSKSRLLDAAV----VGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKI-QRFLS 415
Cdd:PRK04196 334 RKGIYPPIDVLPSLSRLMKDGIgegkTREDHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFeREFVN 413
|
...
gi 300193118 416 QPF 418
Cdd:PRK04196 414 QGF 416
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
69-416 |
5.68e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 151.97 E-value: 5.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 69 GLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKlrKPIHADPPSF--AEQSTSAEILETGIKVVDLLAP 146
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGS--TPLQQQLPQIhpLQRRAVDTPLDVGVNAINGLLT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 147 YARGGKIGLFGGAGVGKTVfiqeLINNIAKAHGGFSVFTG-VGERTREgndlYREMKETGvINLEGESKVALVFGQMNEP 225
Cdd:PRK07196 152 IGKGQRVGLMAGSGVGKSV----LLGMITRYTQADVVVVGlIGERGRE----VKEFIEHS-LQAAGMAKSVVVAAPADES 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 226 PGARARVALTGLTIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTK-KGSV 304
Cdd:PRK07196 223 PLMRIKATELCHAIATYYRDK-GHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSgNGTM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 305 TSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLdAAVVGQEHYDVASKVQETLQTYKSL 384
Cdd:PRK07196 302 TAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCM-SQVIGSQQAKAASLLKQCYADYMAI 380
|
330 340 350
....*....|....*....|....*....|....*.
gi 300193118 385 QDIIA----ILGMDELSEQdklTVERARKIQRFLSQ 416
Cdd:PRK07196 381 KPLIPlggyVAGADPMADQ---AVHYYPAITQFLRQ 413
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
10-83 |
1.29e-37 |
|
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of FoF1-ATP synthase, N-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic.
Pssm-ID: 349739 [Multi-domain] Cd Length: 76 Bit Score: 132.26 E-value: 1.29e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300193118 10 TGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQG-KLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPI 83
Cdd:cd18115 2 TGKIVQVIGPVVDVEFPEGELPPIYNALEVKGDDGkKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
82-362 |
8.35e-36 |
|
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: 133.89 E-value: 8.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 82 PISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGV 161
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 162 GKtvfiQELINNIA------KAHGGFS-VFTGVGERTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGARARVAL 234
Cdd:cd01135 81 PH----NELAAQIArqagvvGSEENFAiVFAAMGVTMEEARFFKDDFEETGALE-----RVVLFLNLANDPTIERIITPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 235 TGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQER--ITTTKKGSVTSVQAVYV 312
Cdd:cd01135 152 MALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTM 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 300193118 313 PADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAV 362
Cdd:cd01135 232 PNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGI 281
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
39-390 |
4.91e-35 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 136.07 E-value: 4.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 39 IKTPQGKLVLEV-AQHLGENTVRTIAM--DGTEGLVRGEKVLDTGGPIS-------VPVGRETLGRIINVIGEPIDERGP 108
Cdd:PRK07960 54 IERQNGSETHEVeSEVVGFNGQRLFLMplEEVEGILPGARVYARNISGEglqsgkqLPLGPALLGRVLDGSGKPLDGLPA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 109 IKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVfiqeLINNIAKAHGGFSVFTG-V 187
Cdd:PRK07960 134 PDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSV----LLGMMARYTQADVIVVGlI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 188 GERTREGNDLYREmketgVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSE 267
Cdd:PRK07960 210 GERGREVKDFIEN-----ILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQRE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 268 VSALLGRIPSAVGYQPTLATDMGLLQERITT--TKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIY 345
Cdd:PRK07960 284 IALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHY 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 300193118 346 PAVDPLDSKSRLLdAAVVGQEHYDVASKVQETLQTYKSLQDIIAI 390
Cdd:PRK07960 364 PAIDIEASISRAM-TALIDEQHYARVRQFKQLLSSFQRNRDLVSV 407
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
26-419 |
6.64e-33 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 129.64 E-value: 6.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 26 EQSELPAILNAL-EIKTPQGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPID 104
Cdd:PRK05922 32 EAQGLSACLGELcQISLSKSPPILAEVIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 105 ERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTvfiqELINNIAK-AHGGFSV 183
Cdd:PRK05922 112 GKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSKSTINV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 184 FTGVGERTREGNDlYREMKETGVinleGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQ 263
Cdd:PRK05922 188 IALIGERGREVRE-YIEQHKEGL----AAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 264 AGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAV-YVP--ADDLTDPAPATTFAHLDATTVLSRGIS 340
Cdd:PRK05922 262 ALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIlHYPnhPDIFTDYLKSLLDGHFFLTPQGKALAS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 341 elgiyPAVDPLDSKSRLLDAAVVgQEHYDVASKVQETLQTYKSLQDIIAiLGMdELSEQDKlTVERARK----IQRFLSQ 416
Cdd:PRK05922 342 -----PPIDILTSLSRSARQLAL-PHHYAAAEELRSLLKAYHEALDIIQ-LGA-YVPGQDA-HLDRAVKllpsIKQFLSQ 412
|
...
gi 300193118 417 PFA 419
Cdd:PRK05922 413 PLS 415
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
10-453 |
3.42e-32 |
|
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: 128.66 E-value: 3.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 10 TGKVTAVIGAIVDVHfeqsELPAILNALEIKTPQGklVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGR 89
Cdd:TIGR00962 27 VGTVVSVGDGIARVY----GLENVMSGELIEFEGG--VQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 90 ETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKT-VFIQ 168
Cdd:TIGR00962 101 GLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTaVAID 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 169 ELINNiaKAHGGFSVFTGVGERTREGNDLYREMKETGVInlegeSKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEG 248
Cdd:TIGR00962 181 TIINQ--KDSDVYCIYVAIGQKASTVAQVVRKLEEHGAM-----AYTIVVAATASDSASLQYLAPYTGCTMGEYFRD-NG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 249 QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTK----KGSVTSVQAVYVPADDLTDPAPAT 324
Cdd:TIGR00962 253 KHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNdekgGGSLTALPIIETQAGDVSAYIPTN 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 325 TFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVgQEHYDVASKVQETLQTYKSLqDIIAILGMDeLSEQDKLTV 404
Cdd:TIGR00962 333 VISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQI-KAMKQVAGSLRLELAQYREL-EAFSQFASD-LDEATKKQL 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 300193118 405 ERARKIQRFLSQPfavaevftgiPGKLVRLKDTVASFKAVLEGKYDNIP 453
Cdd:TIGR00962 410 ERGQRVVELLKQP----------QYKPLSVEEQVVILFAGTKGYLDDIP 448
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
50-356 |
4.08e-28 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 116.94 E-value: 4.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 50 VAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQST 129
Cdd:PRK13343 62 FAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 130 SAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVF-IQELINNiaKAHGGFSVFTGVGERTREGNDLYREMKETGVIn 208
Cdd:PRK13343 142 VTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIaIDAIINQ--KDSDVICVYVAIGQKASAVARVIETLREHGAL- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 209 legeSKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD 288
Cdd:PRK13343 219 ----EYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYL 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300193118 289 MGLLQERITTTKK----GSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSR 356
Cdd:PRK13343 294 HSRLLERAAKLSPelggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
47-416 |
1.60e-27 |
|
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: 114.82 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 47 VLEVAqhlGENTVRTIaMDGTEGL-VRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFA 125
Cdd:TIGR01040 41 VLEVS---GNKAVVQV-FEGTSGIdAKKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 126 EQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKtvfiQELINNIAKAHG---------------GFS-VFTGVGE 189
Cdd:TIGR01040 117 ARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPH----NEIAAQICRQAGlvklptkdvhdghedNFAiVFAAMGV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 190 RTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVS 269
Cdd:TIGR01040 193 NMETARFFKQDFEENGSME-----RVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 270 ALLGRIPSAVGYQPTLATDMGLLQERI--TTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPA 347
Cdd:TIGR01040 268 AAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPP 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300193118 348 VDPLDSKSRLLDAAV----VGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIQR-FLSQ 416
Cdd:TIGR01040 348 INVLPSLSRLMKSAIgegmTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQ 421
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
121-356 |
3.75e-24 |
|
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: 101.88 E-value: 3.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 121 PPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELinniAK-AHGGFSVFTGVGERtreGNDLYR 199
Cdd:cd01134 47 PRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSL----SKwSNSDVVIYVGCGER---GNEMAE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 200 EMKE--TGVINLEGES---KVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGR 274
Cdd:cd01134 120 VLEEfpELKDPITGESlmeRTVLIANTSNMPVAAREASIYTGITIAEYFRD-MGYNVSLMADSTSRWAEALREISGRLEE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 275 IPSAVGYQPTLATDMGLLQERI-------TTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPA 347
Cdd:cd01134 199 MPAEEGYPAYLGARLAEFYERAgrvrclgSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPS 278
|
....*....
gi 300193118 348 VDPLDSKSR 356
Cdd:cd01134 279 INWLISYSK 287
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
83-416 |
2.65e-23 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 102.94 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 83 ISVPVGREtlGRIINVIG-------EPI----DERGPIKS-KL------RKPIHadppsFAEQSTSAEILETGIKVVDLL 144
Cdd:PRK04192 149 IMVPPGVS--GTVKEIVSegdytvdDTIavleDEDGEGVElTMmqkwpvRRPRP-----YKEKLPPVEPLITGQRVIDTF 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 145 APYARGGKIGLFGGAGVGKTVFIQELinniAK-AHGGFSVFTGVGERtreGNdlyrEMKEtgVIN----LE----GES-- 213
Cdd:PRK04192 222 FPVAKGGTAAIPGPFGSGKTVTQHQL----AKwADADIVIYVGCGER---GN----EMTE--VLEefpeLIdpktGRPlm 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 214 -KVALVFGQMNEPPGAR-ARVaLTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGL 291
Cdd:PRK04192 289 eRTVLIANTSNMPVAAReASI-YTGITIAEYYRD-MGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 292 LQER---ITT--TKKGSVTSVQAVYVPADDLTDPapaTTFAHLDATTV---LSRGISELGIYPAVDPLDSKSRLLD---- 359
Cdd:PRK04192 367 FYERagrVKTlgGEEGSVTIIGAVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADRRHFPAINWLTSYSLYLDqvap 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 360 --AAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKI-QRFLSQ 416
Cdd:PRK04192 444 wwEENVDPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQ 503
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
83-276 |
4.02e-21 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 93.01 E-value: 4.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 83 ISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVG 162
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 163 KT-VFIQELINNiaKAHGGFSVFTGVGERTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGARARVALTGLTIAE 241
Cdd:cd01132 82 KTaIAIDTIINQ--KGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAME-----YTIVVAATASDPAPLQYLAPYAGCAMGE 154
|
170 180 190
....*....|....*....|....*....|....*
gi 300193118 242 YFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIP 276
Cdd:cd01132 155 YFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPP 188
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
183-428 |
1.16e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 95.47 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 183 VFTGVGERTREGNDLYREMKE-----TGVINLEgesKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDN 257
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFPKlkdpkTGKPLME---RTVLIANTSNMPVAAREASIYTGITIAEYFRD-MGYDVALMADS 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 258 IFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERI-------TTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLD 330
Cdd:PRK14698 762 TSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVK 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 331 ATTVLSRGISELGIYPAVDPLDSKSRLLDAAV------VGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTV 404
Cdd:PRK14698 842 VFWALDADLARRRHFPAINWLTSYSLYVDAVKdwwhknVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAIL 921
|
250 260
....*....|....*....|....
gi 300193118 405 ERARKIQRFLSQPFAVAEVFTGIP 428
Cdd:PRK14698 922 LVARMLREDYLQQDAFDEVDTYCP 945
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
12-357 |
1.87e-19 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 90.48 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 12 KVTAVIGAIVDVhfeQSELPAILNALEIKTPQGKLVLEVAqHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRET 91
Cdd:PRK02118 7 KITDITGNVITV---EAEGVGYGELATVERKDGSSLAQVI-RLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 92 LGRIINVIGEPIDeRGPIKSKlrKPIHADPPSF--AEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGktvfIQE 169
Cdd:PRK02118 83 LGRRFNGSGKPID-GGPELEG--EPIEIGGPSVnpVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEP----YNA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 170 LINNIA-KAHGGFSVFTGVGERTREGNDLYREMKETGVInlegeSKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEG 248
Cdd:PRK02118 156 LLARIAlQAEADIIILGGMGLTFDDYLFFKDTFENAGAL-----DRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 249 QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQER-ITTTKKGSVTSVQAVYVPADDLTDPAPATTFA 327
Cdd:PRK02118 231 KKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKaVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGY 310
|
330 340 350
....*....|....*....|....*....|
gi 300193118 328 HLDATTVLSRGiselgiypAVDPLDSKSRL 357
Cdd:PRK02118 311 ITEGQFYLRRG--------RIDPFGSLSRL 332
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
47-276 |
1.93e-19 |
|
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: 90.87 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 47 VLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAE 126
Cdd:COG0056 59 VYGMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVID 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 127 QSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKT-VFIQELINNiaKAHGGFSVFTGVGERtregndlyremketg 205
Cdd:COG0056 139 RQPVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTaIAIDTIINQ--KGKDVICIYVAIGQK--------------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 206 vinlegESKVALV------FGQM----------NEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVS 269
Cdd:COG0056 202 ------ASTVAQVvetleeHGAMeytivvaataSDPAPLQYIAPYAGCAMGEYFMD-QGKDVLIVYDDLSKHAVAYRELS 274
|
....*..
gi 300193118 270 ALLGRIP 276
Cdd:COG0056 275 LLLRRPP 281
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
13-80 |
6.43e-19 |
|
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: 80.67 E-value: 6.43e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300193118 13 VTAVIGAIVDVHFEQSELPAILNALEIKTP-QGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTG 80
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVeFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
47-276 |
1.44e-18 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 88.20 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 47 VLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPS-FA 125
Cdd:PRK09281 59 VYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGvID 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 126 EQSTSaEILETGIKVVDLLAPYARGGKIGLFGGAGVGKT-VFIQELINNiaKAHGGFSVFTGVGERtregndlyremket 204
Cdd:PRK09281 139 RKSVH-EPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTaIAIDTIINQ--KGKDVICIYVAIGQK-------------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 205 gvinlegESKVALV------FGQM----------NEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEV 268
Cdd:PRK09281 202 -------ASTVAQVvrkleeHGAMeytivvaataSDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQL 273
|
....*...
gi 300193118 269 SALLGRIP 276
Cdd:PRK09281 274 SLLLRRPP 281
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
367-435 |
7.38e-18 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 77.87 E-value: 7.38e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300193118 367 HYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGKLVRLK 435
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIK 69
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
62-384 |
8.54e-13 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 70.45 E-value: 8.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 62 IAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPID------ERGPIKSKLR-KPIHADPPSFAEQSTSAEIL 134
Cdd:PTZ00185 94 ILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrSRALLESEQTlGKVDAGAPNIVSRSPVNYNL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 135 ETGIKVVDLLAPYARGGKIGLFGGAGVGKT-VFIQELIN------NIAKAHGGFSVFTGVGERTREGNDLYREMKETGVI 207
Cdd:PTZ00185 174 LTGFKAVDTMIPIGRGQRELIVGDRQTGKTsIAVSTIINqvrinqQILSKNAVISIYVSIGQRCSNVARIHRLLRSYGAL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 208 NLegeskVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLAT 287
Cdd:PTZ00185 254 RY-----TTVMAATAAEPAGLQYLAPYSGVTMGEYFMN-RGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFY 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 288 DMGLLQERITTTKK----GSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAvV 363
Cdd:PTZ00185 328 LHSRLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSA-Q 406
|
330 340
....*....|....*....|.
gi 300193118 364 GQEHYDVASKVQETLQTYKSL 384
Cdd:PTZ00185 407 NVAMKAVAGKLKGILAEYRKL 427
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
50-441 |
1.32e-12 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 69.61 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 50 VAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQST 129
Cdd:CHL00059 41 IALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 130 SAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKT-VFIQELINNiaKAHGGFSVFTGVGERTREGNDLYREMKETGVIn 208
Cdd:CHL00059 121 VYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTaVATDTILNQ--KGQNVICVYVAIGQKASSVAQVVTTLQERGAM- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 209 legesKVALVFGQMNEPPGARARVA-LTGLTIAEYFRdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYqptlAT 287
Cdd:CHL00059 198 -----EYTIVVAETADSPATLQYLApYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAY----PG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 288 DMGLLQERI--------TTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLD 359
Cdd:CHL00059 268 DVFYLHSRLleraaklsSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGS 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 360 AAVVgQEHYDVASKVQETLQTYKSLQDIIAIlgmdeLSEQDKLT---VERARKIQRFLSQ----PFAVAE----VFTGIP 428
Cdd:CHL00059 348 AAQI-KAMKQVAGKLKLELAQFAELEAFAQF-----ASDLDKATqnqLARGQRLRELLKQsqsaPLTVEEqvatIYTGTN 421
|
410
....*....|....
gi 300193118 429 GKLVRLK-DTVASF 441
Cdd:CHL00059 422 GYLDSLEiGQVRKF 435
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
81-356 |
1.78e-06 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 50.08 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 81 GPISVPVGRETLGRIINVIGepideRGPIKSKLRKPIHADPPSFAEQSTsaeILETG-----IKVVDLLAPYARGGKIGL 155
Cdd:PRK12608 67 GVARPRERYRVLVRVDSVNG-----TDPEKLARRPHFDDLTPLHPRERL---RLETGsddlsMRVVDLVAPIGKGQRGLI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 156 FGGAGVGKTVFIQELINNIAKAHGGFSVFTG-VGERTREGNDLYREMKetgvinleGEskvalVFGQMNEPPGARaRVAL 234
Cdd:PRK12608 139 VAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDMRRSVK--------GE-----VYASTFDRPPDE-HIRV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 235 TGLTIAEYFRD-EEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAvgyqptlATDMGLLQ--ERITTTKK-----GSVTS 306
Cdd:PRK12608 205 AELVLERAKRLvEQGKDVVILLDSLTRLARAYNNEVESSGRTLSG-------GVDARALQrpKRLFGAARnieegGSLTI 277
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 300193118 307 VQAVYVP----ADDLtdpapatTFAHLDAT----TVLSRGISELGIYPAVDPLDSKSR 356
Cdd:PRK12608 278 IATALVDtgsrMDEV-------IFEEFKGTgnmeIVLDRELADKRVFPAIDIAKSGTR 328
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
149-274 |
6.46e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.83 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 149 RGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGESKVALVFgqmneppgA 228
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLAL--------A 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 300193118 229 RARvaltgltiaeyfrdeEGQDVLLFIDNIFRFTQAGSEVSALLGR 274
Cdd:smart00382 73 LAR---------------KLKPDVLILDEITSLLDAEQEALLLLLE 103
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
16-277 |
8.92e-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: 44.68 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 16 VIGAIVDVHFEQSELPAILNALEIkTPQGKLVLEVAQHL----GENTVRTIAMDGTEGLVRGEKVLdtgGPISVPVGRET 91
Cdd:TIGR00767 34 LIFAILKAHAEQGGLIFGEGVLEI-LPDGFGFLRSPDSSylpgPDDIYVSPSQIRRFNLRTGDTIE---GQIRSPKEGER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 92 LGRIINVigEPIDERGPIKSKLRKPIHADPPSFAEQ----STSAEILETgiKVVDLLAPYARGGKIGLFGGAGVGKTVFI 167
Cdd:TIGR00767 110 YFALLKV--ESVNGDDPEKAKNRVLFENLTPLYPNErlrlETSTEDLST--RVLDLFAPIGKGQRGLIVAPPKAGKTVLL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 168 QELINNIAKAHGG-FSVFTGVGERTREGNDLYREMKetgvinleGESkVALVFgqmNEPPGARARVALTGLTIAEYfRDE 246
Cdd:TIGR00767 186 QKIAQAITRNHPEvELIVLLIDERPEEVTDMQRSVK--------GEV-VASTF---DEPASRHVQVAEMVIEKAKR-LVE 252
|
250 260 270
....*....|....*....|....*....|.
gi 300193118 247 EGQDVLLFIDNIFRFTQAGSEVSALLGRIPS 277
Cdd:TIGR00767 253 HKKDVVILLDSITRLARAYNTVTPASGKVLS 283
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
10-81 |
6.03e-04 |
|
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: 38.45 E-value: 6.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300193118 10 TGKVTAVIGAIVDVHFEqsELPAILNALEIKTPQG----KLVLEVAQHLGENTVrTIAMDGTEGLVRGEKVLDTGG 81
Cdd:cd01426 1 KGRVIRVNGPLVEAELE--GEVAIGEVCEIERGDGnnetVLKAEVIGFRGDRAI-LQLFESTRGLSRGALVEPTGR 73
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
88-203 |
7.56e-04 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 42.32 E-value: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 88 GRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPsFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFI 167
Cdd:PRK14698 166 GEYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRP-YKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDG 244
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 300193118 168 QELI----NNIAKAHGGFSVFTGVGERTREGNDLYREMKE 203
Cdd:PRK14698 245 DTLIltkeFGLIKIKDLYEILDGKGKKTVEGNEEWTELEE 284
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
139-356 |
2.41e-03 |
|
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: 39.50 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 139 KVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTG-VGERTREGNDLYREMKetgvinleGESkVAL 217
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTDMRRSVK--------GEV-VAS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 218 VFgqmNEPPGARARVALTGLTIAEYfRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAvgyqptlATDMGLLQ--ER 295
Cdd:cd01128 76 TF---DEPPERHVQVAEMVIEKAKR-LVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSG-------GVDANALHkpKR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300193118 296 ITTTKK-----GSVTSVQAVYVP----ADDLtdpapatTFAHLDAT----TVLSRGISELGIYPAVDPLDSKSR 356
Cdd:cd01128 145 FFGAARnieegGSLTIIATALVDtgsrMDEV-------IFEEFKGTgnmeLVLDRKLAEKRIFPAIDILKSGTR 211
|
|
| ATP-synt_V_A-type_alpha_C |
cd18111 |
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of ... |
373-416 |
3.89e-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: 36.98 E-value: 3.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 300193118 373 KVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIqR--FLSQ 416
Cdd:cd18111 7 EAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMI-RedFLQQ 51
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
89-208 |
5.74e-03 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 39.19 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193118 89 RETLGRIINVIG---EPIDERGPIKSKL--RKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGK 163
Cdd:PRK07165 77 KEYFGKIIDIDGniiYPEAQNPLSKKFLpnTSSIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGK 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 300193118 164 T-VFIQELINNiaKAHGGFSVFTGVGERTREGNDLYREMKETGVIN 208
Cdd:PRK07165 157 ThIALNTIINQ--KNTNVKCIYVAIGQKRENLSRIYETLKEHDALK 200
|
|
| |
