|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
12-473 |
0e+00 |
|
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439825 [Multi-domain] Cd Length: 468 Bit Score: 976.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 12 STPITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQG-KLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPIS 90
Cdd:COG0055 1 MAMNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEGGgELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 91 VPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKT 170
Cdd:COG0055 81 VPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 171 VFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGARARVALTGLTIAEYFR 250
Cdd:COG0055 161 VLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD-----KTALVFGQMNEPPGARLRVALTALTMAEYFR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 251 DEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPAT 330
Cdd:COG0055 236 DEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPAT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 331 TFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTV 410
Cdd:COG0055 316 TFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTV 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224510813 411 ERARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIEDVV 473
Cdd:COG0055 396 ARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAV 458
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
15-473 |
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 224510813 15 ITGKVTAVIGAIVDVHFEQSELPAILNALEIKTP-QGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPV 93
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNRaESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 94 GRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFI 173
Cdd:TIGR01039 81 GKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 174 QELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGARARVALTGLTIAEYFRDEE 253
Cdd:TIGR01039 161 QELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID-----KTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 254 GQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFA 333
Cdd:TIGR01039 236 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 334 HLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERA 413
Cdd:TIGR01039 316 HLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 414 RKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIEDVV 473
Cdd:TIGR01039 396 RRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVV 455
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
16-473 |
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 224510813 16 TGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQG-----KLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPIS 90
Cdd:CHL00060 16 LGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTagqeiNVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 91 VPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKT 170
Cdd:CHL00060 96 VPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 171 VFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLE--GESKVALVFGQMNEPPGARARVALTGLTIAEY 248
Cdd:CHL00060 176 VLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQniAESKVALVYGQMNEPPGARMRVGLTALTMAEY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 249 FRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAP 328
Cdd:CHL00060 256 FRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 329 ATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKL 408
Cdd:CHL00060 336 ATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRL 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224510813 409 TVERARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIEDVV 473
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 ... |
90-365 |
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 224510813 90 SVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGK 169
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 170 TVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYF 249
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 250 RDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPA 329
Cdd:cd01133 161 RDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPA 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 224510813 330 TTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLD 365
Cdd:cd01133 241 TTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILD 276
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
17-471 |
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 224510813 17 GKVTAVIGAIVDVHFEQsELPAILNALEIKTpQGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRE 96
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDG-ELPAIHSVLRAGR-EGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 97 TLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQEL 176
Cdd:TIGR03305 79 TLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 177 INNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQD 256
Cdd:TIGR03305 159 IHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLD-----NTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 257 VLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLD 336
Cdd:TIGR03305 234 VLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 337 ATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKI 416
Cdd:TIGR03305 314 ASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 224510813 417 QRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIED 471
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 ... |
90-363 |
5.12e-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: 5.12e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 90 SVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGK 169
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 170 TVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVinlegESKVALVFGQMNEPPGARARVALTGLTIAEYF 249
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGA-----MERTVVVANTANDPPGARMRVPYTGLTIAEYF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 250 RDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTK--KGSVTSVQAVYVPADDLTDPA 327
Cdd:cd19476 156 RD-NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDPI 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 224510813 328 PATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRL 363
Cdd:cd19476 235 PDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
143-361 |
7.26e-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: 7.26e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 143 GIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKahgGFSVFTGVGERTREGNDLYREMKETGVInlegeSKVA 222
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL-----KRTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 223 LVFGQMNEPPGARARVALTGLTIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERI 302
Cdd:pfam00006 73 VVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224510813 303 TTT--KKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKS 361
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 ... |
368-473 |
2.08e-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: 2.08e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 368 VVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASF 447
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*.
gi 224510813 448 KAVLEGKYDNIPEHAFYMVGGIEDVV 473
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAV 106
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
9-423 |
7.11e-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: 7.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 9 AAQSTPITGKVTAVIGAIVDVhfeqSELPAILNAL-EIKTPQGKLVL-EVaqhLG--ENTVRTIAMDGTEGLVRGEKVLD 84
Cdd:COG1157 13 ELPPVRVSGRVTRVVGLLIEA----VGPDASIGELcEIETADGRPVLaEV---VGfrGDRVLLMPLGDLEGISPGARVVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 85 TGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGG 164
Cdd:COG1157 86 TGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 165 AGVGKTVfiqeLINNIAKahggfsvFTG--------VGERTREGND-LYREMKEtgvinlEGESKVALVFGQMNEPPGAR 235
Cdd:COG1157 166 SGVGKST----LLGMIAR-------NTEadvnvialIGERGREVREfIEDDLGE------EGLARSVVVVATSDEPPLMR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 236 ARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQA 315
Cdd:COG1157 229 LRAAYTATAIAEYFRD-QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 316 VYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDaAVVGQEHYDVASKVQETLQTYKSLQDIIA 395
Cdd:COG1157 308 VLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMP-DIVSPEHRALARRLRRLLARYEENEDLIR 386
|
410 420 430
....*....|....*....|....*....|..
gi 224510813 396 I----LGMDElsEQDKlTVERARKIQRFLSQP 423
Cdd:COG1157 387 IgayqPGSDP--ELDE-AIALIPAIEAFLRQG 415
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
90-363 |
1.21e-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: 1.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 90 SVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGK 169
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 170 TVFIQELINNIAKAhggFSVFTGVGERTREgndlYREMKEtGVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYF 249
Cdd:cd01136 81 STLLGMIARNTDAD---VNVIALIGERGRE----VREFIE-KDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 250 RDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPA 329
Cdd:cd01136 153 RDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIAD 231
|
250 260 270
....*....|....*....|....*....|....
gi 224510813 330 TTFAHLDATTVLSRGISELGIYPAVDPLDSKSRL 363
Cdd:cd01136 232 EVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
71-422 |
3.33e-51 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 180.01 E-value: 3.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 71 DGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRkPIHADPPSFAEQSTSAEILETGIKVVDLL 150
Cdd:PRK06820 79 ASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWR-ELDCPPPSPLTRQPIEQMLTTGIRAIDGI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 151 APYARGGKIGLFGGAGVGKTVFIQELInniAKAHGGFSVFTGVGERTREgndlYREMKETgVINLEGESKVALVFGQMNE 230
Cdd:PRK06820 158 LSCGEGQRIGIFAAAGVGKSTLLGMLC---ADSAADVMVLALIGERGRE----VREFLEQ-VLTPEARARTVVVVATSDR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 231 PPGARARVALTGLTIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSV 310
Cdd:PRK06820 230 PALERLKGLSTATTIAEYFRDR-GKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSI 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 311 TSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDaAVVGQEHYDVASKVQETLQTYKSL 390
Cdd:PRK06820 309 TAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMP-QIVSAGQLAMAQKLRRMLACYQEI 387
|
330 340 350
....*....|....*....|....*....|....*
gi 224510813 391 QDIIAIlgMDELSEQDKLT---VERARKIQRFLSQ 422
Cdd:PRK06820 388 ELLVRV--GEYQAGEDLQAdeaLQRYPAICAFLQQ 420
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
74-422 |
8.04e-51 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 178.79 E-value: 8.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 74 EGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPY 153
Cdd:PRK06936 80 YGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 154 ARGGKIGLFGGAGVGKTVFIQELINNiakAHGGFSVFTGVGERTREgndlYREMKETGvINLEGESKVALVFGQMNEPPG 233
Cdd:PRK06936 160 GEGQRMGIFAAAGGGKSTLLASLIRS---AEVDVTVLALIGERGRE----VREFIESD-LGEEGLRKAVLVVATSDRPSM 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 234 ARARVALTGLTIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSV 313
Cdd:PRK06936 232 ERAKAGFVATSIAEYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 314 QAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDaAVVGQEHYDVASKVQETLQTYKSLQDI 393
Cdd:PRK06936 311 YTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELL 389
|
330 340 350
....*....|....*....|....*....|...
gi 224510813 394 IAI----LGMDELSEQdklTVERARKIQRFLSQ 422
Cdd:PRK06936 390 LQIgeyqKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
16-423 |
1.35e-50 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 178.42 E-value: 1.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 16 TGKVTAVIGAIVDVhfeqSELPAILNAL-EIKTPQGKLvLEVAQHLG-ENTVRTIAMDGT-EGLVRGEKVLDTGGPISVP 92
Cdd:PRK09099 25 TGKVVEVIGTLLRV----SGLDVTLGELcELRQRDGTL-LQRAEVVGfSRDVALLSPFGElGGLSRGTRVIGLGRPLSVP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 93 VGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVf 172
Cdd:PRK09099 100 VGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKST- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 173 iqeLINNIAK-AHGGFSVFTGVGERTREgndlYREMKETgVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRD 251
Cdd:PRK09099 179 ---LMGMFARgTQCDVNVIALIGERGRE----VREFIEL-ILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 252 EeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATT 331
Cdd:PRK09099 251 R-GLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 332 FAHLDATTVLSRGISELGIYPAVDPLDSKSRLLdAAVVGQEHYDVASKVQETLQTYKSLQDIIAI----LGMDELSEQdk 407
Cdd:PRK09099 330 RGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVADE-- 406
|
410
....*....|....*.
gi 224510813 408 lTVERARKIQRFLSQP 423
Cdd:PRK09099 407 -AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
87-398 |
2.00e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 177.88 E-value: 2.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 87 GPISVPVGRETLGRIINVIGEPIDERGPIKSKLRK-PIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGA 165
Cdd:PRK06002 95 GPLRIRPDPSWKGRVINALGEPIDGLGPLAPGTRPmSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGS 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 166 GVGKTVfiqeLINNIAKAHGGFSVFTG-VGERTREgndlYREM-KETGVINLegeSKVALVFGQMNEPPGARARVALTGL 243
Cdd:PRK06002 175 GVGKST----LLAMLARADAFDTVVIAlVGERGRE----VREFlEDTLADNL---KKAVAVVATSDESPMMRRLAPLTAT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 244 TIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERI--TTTKKGSVTSVQAVYVPAD 321
Cdd:PRK06002 244 AIAEYFRDR-GENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGD 322
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224510813 322 DLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHyDVASKVQETLQTYKSLQDIIAILG 398
Cdd:PRK06002 323 DHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQR-KLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
17-396 |
6.90e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 176.45 E-value: 6.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 17 GKVTAVIGAIVDVHFEQSELPAILNALEIKTPQGKLVLEVAQHLGENtVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRE 96
Cdd:PRK07721 20 GKVSRVIGLMIESKGPESSIGDVCYIHTKGGGDKAIKAEVVGFKDEH-VLLMPYTEVAEIAPGCLVEATGKPLEVKVGSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 97 TLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVfiqeL 176
Cdd:PRK07721 99 LIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKST----L 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 177 INNIAK-AHGGFSVFTGVGERTREgndlYREMKETGvINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEeGQ 255
Cdd:PRK07721 175 MGMIARnTSADLNVIALIGERGRE----VREFIERD-LGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQ-GL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 256 DVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHL 335
Cdd:PRK07721 249 NVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTVRGIL 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224510813 336 DATTVLSRGISELGIYPAVDPLDSKSRLLDaAVVGQEHYDVASKVQETLQTYKSLQDIIAI 396
Cdd:PRK07721 329 DGHFVLDRQLANKGQYPAINVLKSVSRVMN-HIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
15-396 |
5.60e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 174.01 E-value: 5.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 15 ITGKVTAVIGAIVDVHFEQSELpAILNALEIKTPQGKLVL-EVaqhLGENTVRTIAM--DGTEGLVRGEKVLDTGGPISV 91
Cdd:PRK08927 17 IYGRVVAVRGLLVEVAGPIHAL-SVGARIVVETRGGRPVPcEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 92 PVGRETLGRIINVIGEPIDERGPI-KSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKT 170
Cdd:PRK08927 93 RPSRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 171 VFIQELINNIAKAhggFSVFTGVGERTREgndlYREMKETgVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFR 250
Cdd:PRK08927 173 VLLSMLARNADAD---VSVIGLIGERGRE----VQEFLQD-DLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 251 DeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERI--TTTKKGSVTSVQAVYVPADDLTDPAP 328
Cdd:PRK08927 245 D-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPVA 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224510813 329 ATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAvVGQEHYDVASKVQETLQTYKSLQDIIAI 396
Cdd:PRK08927 324 DAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGC-NDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
14-396 |
1.79e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 172.58 E-value: 1.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 14 PITGKVTAVIGaivdVHFEQSELPAILNAL-EIKTPQGKLVLEVAQHLGENTVrTIAMDGTEGLVRGEKVLDTGGPISVP 92
Cdd:PRK08972 24 VASGKLVRVVG----LTLEATGCRAPVGSLcSIETMAGELEAEVVGFDGDLLY-LMPIEELRGVLPGARVTPLGEQSGLP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 93 VGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVf 172
Cdd:PRK08972 99 VGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSV- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 173 iqeLINNIAKAHGGFSVFTG-VGERTREGNDLYREmketgVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRD 251
Cdd:PRK08972 178 ---LLGMMTRGTTADVIVVGlVGERGREVKEFIEE-----ILGEEGRARSVVVAAPADTSPLMRLKGCETATTIAEYFRD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 252 eEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITT--TKKGSVTSVQAVYVPADDLTDPAPA 329
Cdd:PRK08972 250 -QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNggPGQGSITAFYTVLTEGDDLQDPIAD 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224510813 330 TTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLdAAVVGQEHYDVASKVQETLQTYKSLQDIIAI 396
Cdd:PRK08972 329 ASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLISI 394
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
74-422 |
4.81e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 171.41 E-value: 4.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 74 EGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPY 153
Cdd:PRK08472 75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTC 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 154 ARGGKIGLFGGAGVGKTVFIQELINNiAKAHggFSVFTGVGERTregndlyREMKETGVINLEGE-SKVALVFGQMNEPP 232
Cdd:PRK08472 155 GKGQKLGIFAGSGVGKSTLMGMIVKG-CLAP--IKVVALIGERG-------REIPEFIEKNLGGDlENTVIVVATSDDSP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 233 GARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTK-KGSVT 311
Cdd:PRK08472 225 LMRKYGAFCAMSVAEYFKN-QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSIT 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 312 SVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDaAVVGQEHYDVASKVQETLQTYKSLQ 391
Cdd:PRK08472 304 AFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENE 382
|
330 340 350
....*....|....*....|....*....|....*.
gi 224510813 392 DIIAI----LGMD-ELSEqdklTVERARKIQRFLSQ 422
Cdd:PRK08472 383 VLIRIgayqKGNDkELDE----AISKKEFMEQFLKQ 414
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
49-422 |
1.92e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 169.77 E-value: 1.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 49 QGKLVLEVAQHLGENTVrTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPP 128
Cdd:PRK06793 50 EHNVLCEVIAIEKENNM-LLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 129 SFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVfiqeLINNIAK-AHGGFSVFTGVGERTREGNDLYRem 207
Cdd:PRK06793 129 HAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST----LLGMIAKnAKADINVISLVGERGREVKDFIR-- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 208 KETGVinlEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAvGY 287
Cdd:PRK06793 203 KELGE---EGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVKELPIG-GK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 288 QPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDaA 367
Cdd:PRK06793 278 TLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-E 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 224510813 368 VVGQEHYDVASKVQETLQTYKSlQDIIAILGMDELSEQDKLTVERARK---IQRFLSQ 422
Cdd:PRK06793 357 IVSPNHWQLANEMRKILSIYKE-NELYFKLGTIQENAENAYIFECKNKvegINTFLKQ 413
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
53-430 |
6.27e-45 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 162.86 E-value: 6.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 53 VLEVAQHLGENTVRTI--AMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEpIDER------GPIKSKLRkPIH 124
Cdd:PRK08149 42 VIARAQVVGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGK-IVERfdapptVGPISEER-VID 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 125 ADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNiakAHGGFSVFTGVGERTREGNDLY 204
Cdd:PRK08149 120 VAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGERGREVTEFV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 205 REMKETGvinleGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSA 284
Cdd:PRK08149 197 ESLRASS-----RREKCVLVYATSDFSSVDRCNAALVATTVAEYFRD-QGKRVVLFIDSMTRYARALRDVALAAGELPAR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 285 VGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLL 364
Cdd:PRK08149 271 RGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVF 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224510813 365 DaAVVGQEHYDVASKVQETLQTYKSLQDIIAiLG---MDELSEQDKlTVERARKIQRFLSQPFAVAEVF 430
Cdd:PRK08149 351 G-QVTDPKHRQLAAAFRKLLTRLEELQLFID-LGeyrRGENADNDR-AMDKRPALEAFLKQDVAEKSSF 416
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
74-422 |
6.56e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 157.58 E-value: 6.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 74 EGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPY 153
Cdd:PRK05688 86 AGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTV 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 154 ARGGKIGLFGGAGVGKTVFIqelinniakahGGFSVFTG--------VGERTREGNDLYREmketgVINLEGESKVALVF 225
Cdd:PRK05688 166 GRGQRLGLFAGTGVGKSVLL-----------GMMTRFTEadiivvglIGERGREVKEFIEH-----ILGEEGLKRSVVVA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 226 GQMNEPPGARARVALTGLTIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTT 305
Cdd:PRK05688 230 SPADDAPLMRLRAAMYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 306 KKG--SVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLdAAVVGQEHYDVASKVQET 383
Cdd:PRK05688 309 EPGggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQL 387
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 224510813 384 LQTYKSLQDIIAI----LGMDelSEQDkLTVERARKIQRFLSQ 422
Cdd:PRK05688 388 WSRYQQSRDLISVgayvAGGD--PETD-LAIARFPHLVQFLRQ 427
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
73-396 |
4.17e-42 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 155.11 E-value: 4.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 73 TEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERgPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAP 152
Cdd:PRK07594 73 TIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVAT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 153 YARGGKIGLFGGAGVGKTVFIQELINniaKAHGGFSVFTGVGERTREgndlYREMKETgVINLEGESKVALVFGQMNEPP 232
Cdd:PRK07594 152 CGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGRE----VREFIDF-TLSEETRKRCVIVVATSDRPA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 233 GARARVALTGLTIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTS 312
Cdd:PRK07594 224 LERVRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 313 VQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLdAAVVGQEHYDVASKVQETLQTYKSLQD 392
Cdd:PRK07594 303 FYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEVEL 381
|
....
gi 224510813 393 IIAI 396
Cdd:PRK07594 382 LIRI 385
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
44-424 |
1.04e-41 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 154.60 E-value: 1.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 44 EIKTPQGKL----VLEVAqhlGENTVRTIaMDGTEGL-VRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSK 118
Cdd:PRK04196 30 EIELPNGEKrrgqVLEVS---EDKAVVQV-FEGTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 119 LRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKtvfiQELINNI---AKAHGGFS----VFT 191
Cdd:PRK04196 106 KRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPH----NELAAQIarqAKVLGEEEnfavVFA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 192 GVGERTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGAR---ARVAltgLTIAEYFRDEEGQDVLLFIDNIFRFT 268
Cdd:PRK04196 182 AMGITFEEANFFMEDFEETGALE-----RSVVFLNLADDPAIERiltPRMA---LTAAEYLAFEKGMHVLVILTDMTNYC 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 269 QAGSEVSALLGRIPSAVGYQPTLATDMGLLQER--ITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIS 346
Cdd:PRK04196 254 EALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELH 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 347 ELGIYPAVDPLDSKSRLLDAAV----VGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKI-QRFLS 421
Cdd:PRK04196 334 RKGIYPPIDVLPSLSRLMKDGIgegkTREDHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFeREFVN 413
|
...
gi 224510813 422 QPF 424
Cdd:PRK04196 414 QGF 416
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
75-422 |
6.32e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 151.97 E-value: 6.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 75 GLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKlrKPIHADPPSF--AEQSTSAEILETGIKVVDLLAP 152
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGS--TPLQQQLPQIhpLQRRAVDTPLDVGVNAINGLLT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 153 YARGGKIGLFGGAGVGKTVfiqeLINNIAKAHGGFSVFTG-VGERTREgndlYREMKETGvINLEGESKVALVFGQMNEP 231
Cdd:PRK07196 152 IGKGQRVGLMAGSGVGKSV----LLGMITRYTQADVVVVGlIGERGRE----VKEFIEHS-LQAAGMAKSVVVAAPADES 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 232 PGARARVALTGLTIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTK-KGSV 310
Cdd:PRK07196 223 PLMRIKATELCHAIATYYRDK-GHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSgNGTM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 311 TSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLdAAVVGQEHYDVASKVQETLQTYKSL 390
Cdd:PRK07196 302 TAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCM-SQVIGSQQAKAASLLKQCYADYMAI 380
|
330 340 350
....*....|....*....|....*....|....*.
gi 224510813 391 QDIIA----ILGMDELSEQdklTVERARKIQRFLSQ 422
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 ... |
16-89 |
1.41e-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: 1.41e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224510813 16 TGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQG-KLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPI 89
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 ... |
88-368 |
9.12e-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: 9.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 88 PISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGV 167
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 168 GKtvfiQELINNIA------KAHGGFS-VFTGVGERTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGARARVAL 240
Cdd:cd01135 81 PH----NELAAQIArqagvvGSEENFAiVFAAMGVTMEEARFFKDDFEETGALE-----RVVLFLNLANDPTIERIITPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 241 TGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQER--ITTTKKGSVTSVQAVYV 318
Cdd:cd01135 152 MALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTM 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 224510813 319 PADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAV 368
Cdd:cd01135 232 PNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGI 281
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
45-396 |
5.38e-35 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 136.07 E-value: 5.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 45 IKTPQGKLVLEV-AQHLGENTVRTIAM--DGTEGLVRGEKVLDTGGPIS-------VPVGRETLGRIINVIGEPIDERGP 114
Cdd:PRK07960 54 IERQNGSETHEVeSEVVGFNGQRLFLMplEEVEGILPGARVYARNISGEglqsgkqLPLGPALLGRVLDGSGKPLDGLPA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 115 IKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVfiqeLINNIAKAHGGFSVFTG-V 193
Cdd:PRK07960 134 PDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSV----LLGMMARYTQADVIVVGlI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 194 GERTREGNDLYREmketgVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSE 273
Cdd:PRK07960 210 GERGREVKDFIEN-----ILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQRE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 274 VSALLGRIPSAVGYQPTLATDMGLLQERITT--TKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIY 351
Cdd:PRK07960 284 IALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHY 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 224510813 352 PAVDPLDSKSRLLdAAVVGQEHYDVASKVQETLQTYKSLQDIIAI 396
Cdd:PRK07960 364 PAIDIEASISRAM-TALIDEQHYARVRQFKQLLSSFQRNRDLVSV 407
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
32-425 |
7.21e-33 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 129.64 E-value: 7.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 32 EQSELPAILNAL-EIKTPQGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPID 110
Cdd:PRK05922 32 EAQGLSACLGELcQISLSKSPPILAEVIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 111 ERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTvfiqELINNIAK-AHGGFSV 189
Cdd:PRK05922 112 GKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSKSTINV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 190 FTGVGERTREGNDlYREMKETGVinleGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQ 269
Cdd:PRK05922 188 IALIGERGREVRE-YIEQHKEGL----AAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 270 AGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAV-YVP--ADDLTDPAPATTFAHLDATTVLSRGIS 346
Cdd:PRK05922 262 ALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIlHYPnhPDIFTDYLKSLLDGHFFLTPQGKALAS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 347 elgiyPAVDPLDSKSRLLDAAVVgQEHYDVASKVQETLQTYKSLQDIIAiLGMdELSEQDKlTVERARK----IQRFLSQ 422
Cdd:PRK05922 342 -----PPIDILTSLSRSARQLAL-PHHYAAAEELRSLLKAYHEALDIIQ-LGA-YVPGQDA-HLDRAVKllpsIKQFLSQ 412
|
...
gi 224510813 423 PFA 425
Cdd:PRK05922 413 PLS 415
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
16-459 |
3.72e-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: 3.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 16 TGKVTAVIGAIVDVHfeqsELPAILNALEIKTPQGklVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGR 95
Cdd:TIGR00962 27 VGTVVSVGDGIARVY----GLENVMSGELIEFEGG--VQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 96 ETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKT-VFIQ 174
Cdd:TIGR00962 101 GLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTaVAID 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 175 ELINNiaKAHGGFSVFTGVGERTREGNDLYREMKETGVInlegeSKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEG 254
Cdd:TIGR00962 181 TIINQ--KDSDVYCIYVAIGQKASTVAQVVRKLEEHGAM-----AYTIVVAATASDSASLQYLAPYTGCTMGEYFRD-NG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 255 QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTK----KGSVTSVQAVYVPADDLTDPAPAT 330
Cdd:TIGR00962 253 KHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNdekgGGSLTALPIIETQAGDVSAYIPTN 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 331 TFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVgQEHYDVASKVQETLQTYKSLqDIIAILGMDeLSEQDKLTV 410
Cdd:TIGR00962 333 VISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQI-KAMKQVAGSLRLELAQYREL-EAFSQFASD-LDEATKKQL 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 224510813 411 ERARKIQRFLSQPfavaevftgiPGKLVRLKDTVASFKAVLEGKYDNIP 459
Cdd:TIGR00962 410 ERGQRVVELLKQP----------QYKPLSVEEQVVILFAGTKGYLDDIP 448
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
56-362 |
4.37e-28 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 116.94 E-value: 4.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 56 VAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQST 135
Cdd:PRK13343 62 FAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 136 SAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVF-IQELINNiaKAHGGFSVFTGVGERTREGNDLYREMKETGVIn 214
Cdd:PRK13343 142 VTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIaIDAIINQ--KDSDVICVYVAIGQKASAVARVIETLREHGAL- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 215 legeSKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD 294
Cdd:PRK13343 219 ----EYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYL 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224510813 295 MGLLQERITTTKK----GSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSR 362
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 ... |
53-422 |
1.71e-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: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 53 VLEVAqhlGENTVRTIaMDGTEGL-VRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFA 131
Cdd:TIGR01040 41 VLEVS---GNKAVVQV-FEGTSGIdAKKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 132 EQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKtvfiQELINNIAKAHG---------------GFS-VFTGVGE 195
Cdd:TIGR01040 117 ARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPH----NEIAAQICRQAGlvklptkdvhdghedNFAiVFAAMGV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 196 RTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVS 275
Cdd:TIGR01040 193 NMETARFFKQDFEENGSME-----RVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 276 ALLGRIPSAVGYQPTLATDMGLLQERI--TTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPA 353
Cdd:TIGR01040 268 AAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPP 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224510813 354 VDPLDSKSRLLDAAV----VGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIQR-FLSQ 422
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 ... |
127-362 |
3.93e-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: 3.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 127 PPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELinniAK-AHGGFSVFTGVGERtreGNDLYR 205
Cdd:cd01134 47 PRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSL----SKwSNSDVVIYVGCGER---GNEMAE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 206 EMKE--TGVINLEGES---KVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGR 280
Cdd:cd01134 120 VLEEfpELKDPITGESlmeRTVLIANTSNMPVAAREASIYTGITIAEYFRD-MGYNVSLMADSTSRWAEALREISGRLEE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 281 IPSAVGYQPTLATDMGLLQERI-------TTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPA 353
Cdd:cd01134 199 MPAEEGYPAYLGARLAEFYERAgrvrclgSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPS 278
|
....*....
gi 224510813 354 VDPLDSKSR 362
Cdd:cd01134 279 INWLISYSK 287
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
89-422 |
2.81e-23 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 102.94 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 89 ISVPVGREtlGRIINVIG-------EPI----DERGPIKS-KL------RKPIHadppsFAEQSTSAEILETGIKVVDLL 150
Cdd:PRK04192 149 IMVPPGVS--GTVKEIVSegdytvdDTIavleDEDGEGVElTMmqkwpvRRPRP-----YKEKLPPVEPLITGQRVIDTF 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 151 APYARGGKIGLFGGAGVGKTVFIQELinniAK-AHGGFSVFTGVGERtreGNdlyrEMKEtgVIN----LE----GES-- 219
Cdd:PRK04192 222 FPVAKGGTAAIPGPFGSGKTVTQHQL----AKwADADIVIYVGCGER---GN----EMTE--VLEefpeLIdpktGRPlm 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 220 -KVALVFGQMNEPPGAR-ARVaLTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGL 297
Cdd:PRK04192 289 eRTVLIANTSNMPVAAReASI-YTGITIAEYYRD-MGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 298 LQER---ITT--TKKGSVTSVQAVYVPADDLTDPapaTTFAHLDATTV---LSRGISELGIYPAVDPLDSKSRLLD---- 365
Cdd:PRK04192 367 FYERagrVKTlgGEEGSVTIIGAVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADRRHFPAINWLTSYSLYLDqvap 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 366 --AAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKI-QRFLSQ 422
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 ... |
89-282 |
4.17e-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: 4.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 89 ISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVG 168
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 169 KT-VFIQELINNiaKAHGGFSVFTGVGERTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGARARVALTGLTIAE 247
Cdd:cd01132 82 KTaIAIDTIINQ--KGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAME-----YTIVVAATASDPAPLQYLAPYAGCAMGE 154
|
170 180 190
....*....|....*....|....*....|....*
gi 224510813 248 YFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIP 282
Cdd:cd01132 155 YFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPP 188
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
189-434 |
1.23e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 95.47 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 189 VFTGVGERTREGNDLYREMKE-----TGVINLEgesKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDN 263
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFPKlkdpkTGKPLME---RTVLIANTSNMPVAAREASIYTGITIAEYFRD-MGYDVALMADS 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 264 IFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERI-------TTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLD 336
Cdd:PRK14698 762 TSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVK 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 337 ATTVLSRGISELGIYPAVDPLDSKSRLLDAAV------VGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTV 410
Cdd:PRK14698 842 VFWALDADLARRRHFPAINWLTSYSLYVDAVKdwwhknVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAIL 921
|
250 260
....*....|....*....|....
gi 224510813 411 ERARKIQRFLSQPFAVAEVFTGIP 434
Cdd:PRK14698 922 LVARMLREDYLQQDAFDEVDTYCP 945
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
18-363 |
1.94e-19 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 90.48 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 18 KVTAVIGAIVDVhfeQSELPAILNALEIKTPQGKLVLEVAqHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRET 97
Cdd:PRK02118 7 KITDITGNVITV---EAEGVGYGELATVERKDGSSLAQVI-RLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 98 LGRIINVIGEPIDeRGPIKSKlrKPIHADPPSF--AEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGktvfIQE 175
Cdd:PRK02118 83 LGRRFNGSGKPID-GGPELEG--EPIEIGGPSVnpVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEP----YNA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 176 LINNIA-KAHGGFSVFTGVGERTREGNDLYREMKETGVInlegeSKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEG 254
Cdd:PRK02118 156 LLARIAlQAEADIIILGGMGLTFDDYLFFKDTFENAGAL-----DRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 255 QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQER-ITTTKKGSVTSVQAVYVPADDLTDPAPATTFA 333
Cdd:PRK02118 231 KKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKaVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGY 310
|
330 340 350
....*....|....*....|....*....|
gi 224510813 334 HLDATTVLSRGiselgiypAVDPLDSKSRL 363
Cdd:PRK02118 311 ITEGQFYLRRG--------RIDPFGSLSRL 332
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
53-282 |
2.01e-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: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 53 VLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAE 132
Cdd:COG0056 59 VYGMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVID 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 133 QSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKT-VFIQELINNiaKAHGGFSVFTGVGERtregndlyremketg 211
Cdd:COG0056 139 RQPVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTaIAIDTIINQ--KGKDVICIYVAIGQK--------------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 212 vinlegESKVALV------FGQM----------NEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVS 275
Cdd:COG0056 202 ------ASTVAQVvetleeHGAMeytivvaataSDPAPLQYIAPYAGCAMGEYFMD-QGKDVLIVYDDLSKHAVAYRELS 274
|
....*..
gi 224510813 276 ALLGRIP 282
Cdd:COG0056 275 LLLRRPP 281
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
19-86 |
6.55e-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: 6.55e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224510813 19 VTAVIGAIVDVHFEQSELPAILNALEIKTP-QGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTG 86
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVeFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
53-282 |
1.49e-18 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 88.20 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 53 VLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPS-FA 131
Cdd:PRK09281 59 VYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGvID 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 132 EQSTSaEILETGIKVVDLLAPYARGGKIGLFGGAGVGKT-VFIQELINNiaKAHGGFSVFTGVGERtregndlyremket 210
Cdd:PRK09281 139 RKSVH-EPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTaIAIDTIINQ--KGKDVICIYVAIGQK-------------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 211 gvinlegESKVALV------FGQM----------NEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEV 274
Cdd:PRK09281 202 -------ASTVAQVvrkleeHGAMeytivvaataSDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQL 273
|
....*...
gi 224510813 275 SALLGRIP 282
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, ... |
373-441 |
7.51e-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: 7.51e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224510813 373 HYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGKLVRLK 441
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIK 69
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
68-390 |
8.80e-13 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 70.45 E-value: 8.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 68 IAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPID------ERGPIKSKLR-KPIHADPPSFAEQSTSAEIL 140
Cdd:PTZ00185 94 ILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrSRALLESEQTlGKVDAGAPNIVSRSPVNYNL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 141 ETGIKVVDLLAPYARGGKIGLFGGAGVGKT-VFIQELIN------NIAKAHGGFSVFTGVGERTREGNDLYREMKETGVI 213
Cdd:PTZ00185 174 LTGFKAVDTMIPIGRGQRELIVGDRQTGKTsIAVSTIINqvrinqQILSKNAVISIYVSIGQRCSNVARIHRLLRSYGAL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 214 NLegeskVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLAT 293
Cdd:PTZ00185 254 RY-----TTVMAATAAEPAGLQYLAPYSGVTMGEYFMN-RGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFY 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 294 DMGLLQERITTTKK----GSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAvV 369
Cdd:PTZ00185 328 LHSRLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSA-Q 406
|
330 340
....*....|....*....|.
gi 224510813 370 GQEHYDVASKVQETLQTYKSL 390
Cdd:PTZ00185 407 NVAMKAVAGKLKGILAEYRKL 427
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
56-447 |
1.36e-12 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 69.61 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 56 VAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQST 135
Cdd:CHL00059 41 IALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 136 SAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKT-VFIQELINNiaKAHGGFSVFTGVGERTREGNDLYREMKETGVIn 214
Cdd:CHL00059 121 VYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTaVATDTILNQ--KGQNVICVYVAIGQKASSVAQVVTTLQERGAM- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 215 legesKVALVFGQMNEPPGARARVA-LTGLTIAEYFRdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYqptlAT 293
Cdd:CHL00059 198 -----EYTIVVAETADSPATLQYLApYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAY----PG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 294 DMGLLQERI--------TTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLD 365
Cdd:CHL00059 268 DVFYLHSRLleraaklsSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGS 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 366 AAVVgQEHYDVASKVQETLQTYKSLQDIIAIlgmdeLSEQDKLT---VERARKIQRFLSQ----PFAVAE----VFTGIP 434
Cdd:CHL00059 348 AAQI-KAMKQVAGKLKLELAQFAELEAFAQF-----ASDLDKATqnqLARGQRLRELLKQsqsaPLTVEEqvatIYTGTN 421
|
410
....*....|....
gi 224510813 435 GKLVRLK-DTVASF 447
Cdd:CHL00059 422 GYLDSLEiGQVRKF 435
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
87-362 |
1.81e-06 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 50.08 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 87 GPISVPVGRETLGRIINVIGepideRGPIKSKLRKPIHADPPSFAEQSTsaeILETG-----IKVVDLLAPYARGGKIGL 161
Cdd:PRK12608 67 GVARPRERYRVLVRVDSVNG-----TDPEKLARRPHFDDLTPLHPRERL---RLETGsddlsMRVVDLVAPIGKGQRGLI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 162 FGGAGVGKTVFIQELINNIAKAHGGFSVFTG-VGERTREGNDLYREMKetgvinleGEskvalVFGQMNEPPGARaRVAL 240
Cdd:PRK12608 139 VAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDMRRSVK--------GE-----VYASTFDRPPDE-HIRV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 241 TGLTIAEYFRD-EEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAvgyqptlATDMGLLQ--ERITTTKK-----GSVTS 312
Cdd:PRK12608 205 AELVLERAKRLvEQGKDVVILLDSLTRLARAYNNEVESSGRTLSG-------GVDARALQrpKRLFGAARnieegGSLTI 277
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 224510813 313 VQAVYVP----ADDLtdpapatTFAHLDAT----TVLSRGISELGIYPAVDPLDSKSR 362
Cdd:PRK12608 278 IATALVDtgsrMDEV-------IFEEFKGTgnmeIVLDRELADKRVFPAIDIAKSGTR 328
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
155-280 |
6.56e-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: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 155 RGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGESKVALVFgqmneppgA 234
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLAL--------A 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 224510813 235 RARvaltgltiaeyfrdeEGQDVLLFIDNIFRFTQAGSEVSALLGR 280
Cdd:smart00382 73 LAR---------------KLKPDVLILDEITSLLDAEQEALLLLLE 103
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
22-283 |
9.09e-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: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 22 VIGAIVDVHFEQSELPAILNALEIkTPQGKLVLEVAQHL----GENTVRTIAMDGTEGLVRGEKVLdtgGPISVPVGRET 97
Cdd:TIGR00767 34 LIFAILKAHAEQGGLIFGEGVLEI-LPDGFGFLRSPDSSylpgPDDIYVSPSQIRRFNLRTGDTIE---GQIRSPKEGER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 98 LGRIINVigEPIDERGPIKSKLRKPIHADPPSFAEQ----STSAEILETgiKVVDLLAPYARGGKIGLFGGAGVGKTVFI 173
Cdd:TIGR00767 110 YFALLKV--ESVNGDDPEKAKNRVLFENLTPLYPNErlrlETSTEDLST--RVLDLFAPIGKGQRGLIVAPPKAGKTVLL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 174 QELINNIAKAHGG-FSVFTGVGERTREGNDLYREMKetgvinleGESkVALVFgqmNEPPGARARVALTGLTIAEYfRDE 252
Cdd:TIGR00767 186 QKIAQAITRNHPEvELIVLLIDERPEEVTDMQRSVK--------GEV-VASTF---DEPASRHVQVAEMVIEKAKR-LVE 252
|
250 260 270
....*....|....*....|....*....|.
gi 224510813 253 EGQDVLLFIDNIFRFTQAGSEVSALLGRIPS 283
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, ... |
16-87 |
6.11e-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: 6.11e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224510813 16 TGKVTAVIGAIVDVHFEqsELPAILNALEIKTPQG----KLVLEVAQHLGENTVrTIAMDGTEGLVRGEKVLDTGG 87
Cdd:cd01426 1 KGRVIRVNGPLVEAELE--GEVAIGEVCEIERGDGnnetVLKAEVIGFRGDRAI-LQLFESTRGLSRGALVEPTGR 73
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
94-209 |
7.71e-04 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 42.32 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 94 GRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPsFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFI 173
Cdd:PRK14698 166 GEYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRP-YKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDG 244
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 224510813 174 QELI----NNIAKAHGGFSVFTGVGERTREGNDLYREMKE 209
Cdd:PRK14698 245 DTLIltkeFGLIKIKDLYEILDGKGKKTVEGNEEWTELEE 284
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
145-362 |
2.45e-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: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 145 KVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTG-VGERTREGNDLYREMKetgvinleGESkVAL 223
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTDMRRSVK--------GEV-VAS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 224 VFgqmNEPPGARARVALTGLTIAEYfRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAvgyqptlATDMGLLQ--ER 301
Cdd:cd01128 76 TF---DEPPERHVQVAEMVIEKAKR-LVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSG-------GVDANALHkpKR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224510813 302 ITTTKK-----GSVTSVQAVYVP----ADDLtdpapatTFAHLDAT----TVLSRGISELGIYPAVDPLDSKSR 362
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 ... |
379-422 |
3.94e-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: 3.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 224510813 379 KVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIqR--FLSQ 422
Cdd:cd18111 7 EAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMI-RedFLQQ 51
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
95-214 |
5.84e-03 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 39.19 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224510813 95 RETLGRIINVIG---EPIDERGPIKSKL--RKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGK 169
Cdd:PRK07165 77 KEYFGKIIDIDGniiYPEAQNPLSKKFLpnTSSIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGK 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 224510813 170 T-VFIQELINNiaKAHGGFSVFTGVGERTREGNDLYREMKETGVIN 214
Cdd:PRK07165 157 ThIALNTIINQ--KNTNVKCIYVAIGQKRENLSRIYETLKEHDALK 200
|
|
| |
