|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
39-500 |
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: 982.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 39 STPITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQG-KLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPIS 117
Cdd:COG0055 1 MAMNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEGGgELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 118 VPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKT 197
Cdd:COG0055 81 VPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 198 VFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGARARVALTGLTIAEYFR 277
Cdd:COG0055 161 VLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD-----KTALVFGQMNEPPGARLRVALTALTMAEYFR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 278 DEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPAT 357
Cdd:COG0055 236 DEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPAT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 358 TFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTV 437
Cdd:COG0055 316 TFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTV 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365477 438 ERARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIEDVV 500
Cdd:COG0055 396 ARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAV 458
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
42-500 |
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: 904.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 42 ITGKVTAVIGAIVDVHFEQSELPAILNALEIKTP-QGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPV 120
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNRaESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 121 GRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFI 200
Cdd:TIGR01039 81 GKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 201 QELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGARARVALTGLTIAEYFRDEE 280
Cdd:TIGR01039 161 QELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID-----KTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 281 GQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFA 360
Cdd:TIGR01039 236 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 361 HLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERA 440
Cdd:TIGR01039 316 HLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 441 RKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIEDVV 500
Cdd:TIGR01039 396 RRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVV 455
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
33-500 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 819.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 33 MASAAQSTPITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQG-----KLVLEVAQHLGENTVRTIAMDGTEGLVRGE 107
Cdd:CHL00060 6 PGVSTLEEKNLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTagqeiNVTCEVQQLLGNNRVRAVAMSATDGLMRGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 108 KVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIG 187
Cdd:CHL00060 86 EVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 188 LFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLE--GESKVALVFGQMNEPPGARARV 265
Cdd:CHL00060 166 LFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQniAESKVALVYGQMNEPPGARMRV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 266 ALTGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYV 345
Cdd:CHL00060 246 GLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 346 PADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILG 425
Cdd:CHL00060 326 PADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILG 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365477 426 MDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIEDVV 500
Cdd:CHL00060 406 LDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEAT 480
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
117-392 |
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: 613.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 117 SVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGK 196
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 197 TVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYF 276
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 277 RDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPA 356
Cdd:cd01133 161 RDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPA 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 398365477 357 TTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLD 392
Cdd:cd01133 241 TTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILD 276
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
44-498 |
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: 590.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 44 GKVTAVIGAIVDVHFEQsELPAILNALEIKTpQGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRE 123
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDG-ELPAIHSVLRAGR-EGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 124 TLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQEL 203
Cdd:TIGR03305 79 TLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 204 INNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQD 283
Cdd:TIGR03305 159 IHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLD-----NTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 284 VLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLD 363
Cdd:TIGR03305 234 VLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 364 ATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKI 443
Cdd:TIGR03305 314 ASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 398365477 444 QRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIED 498
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 ... |
117-390 |
2.36e-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: 382.19 E-value: 2.36e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 117 SVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGK 196
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 197 TVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVinlegESKVALVFGQMNEPPGARARVALTGLTIAEYF 276
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGA-----MERTVVVANTANDPPGARMRVPYTGLTIAEYF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 277 RDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTK--KGSVTSVQAVYVPADDLTDPA 354
Cdd:cd19476 156 RD-NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDPI 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 398365477 355 PATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRL 390
Cdd:cd19476 235 PDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
170-388 |
6.58e-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: 276.54 E-value: 6.58e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 170 GIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKahgGFSVFTGVGERTREGNDLYREMKETGVInlegeSKVA 249
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL-----KRTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 250 LVFGQMNEPPGARARVALTGLTIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERI 329
Cdd:pfam00006 73 VVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365477 330 TTT--KKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKS 388
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 ... |
395-500 |
8.78e-71 |
|
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: 220.81 E-value: 8.78e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 395 VVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASF 474
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*.
gi 398365477 475 KAVLEGKYDNIPEHAFYMVGGIEDVV 500
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAV 106
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
34-450 |
5.91e-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: 224.52 E-value: 5.91e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 34 ASAAQSTPITGKVTAVIGAIVDVhfeqSELPAILNAL-EIKTPQGKLVL-EVaqhLG--ENTVRTIAMDGTEGLVRGEKV 109
Cdd:COG1157 11 LEELPPVRVSGRVTRVVGLLIEA----VGPDASIGELcEIETADGRPVLaEV---VGfrGDRVLLMPLGDLEGISPGARV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 110 LDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLF 189
Cdd:COG1157 84 VPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 190 GGAGVGKTVfiqeLINNIAKahggfsvFTG--------VGERTREGND-LYREMKEtgvinlEGESKVALVFGQMNEPPG 260
Cdd:COG1157 164 AGSGVGKST----LLGMIAR-------NTEadvnvialIGERGREVREfIEDDLGE------EGLARSVVVVATSDEPPL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 261 ARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSV 340
Cdd:COG1157 227 MRLRAAYTATAIAEYFRD-QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 341 QAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDaAVVGQEHYDVASKVQETLQTYKSLQDI 420
Cdd:COG1157 306 YTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMP-DIVSPEHRALARRLRRLLARYEENEDL 384
|
410 420 430
....*....|....*....|....*....|....
gi 398365477 421 IAI----LGMDElsEQDKlTVERARKIQRFLSQP 450
Cdd:COG1157 385 IRIgayqPGSDP--ELDE-AIALIPAIEAFLRQG 415
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
117-390 |
1.11e-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: 202.79 E-value: 1.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 117 SVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGK 196
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 197 TVFIQELINNIAKAhggFSVFTGVGERTREgndlYREMKEtGVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYF 276
Cdd:cd01136 81 STLLGMIARNTDAD---VNVIALIGERGRE----VREFIE-KDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 277 RDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPA 356
Cdd:cd01136 153 RDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIAD 231
|
250 260 270
....*....|....*....|....*....|....
gi 398365477 357 TTFAHLDATTVLSRGISELGIYPAVDPLDSKSRL 390
Cdd:cd01136 232 EVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
33-449 |
1.87e-51 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 181.10 E-value: 1.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 33 MASAAQSTP---ITGKVTAVIGAIVDV---HFEQSELPAILNALEIKTPQGKLVLEVAQH-----LGEntvrtiamdgTE 101
Cdd:PRK06936 11 LRHAIVGSRliqIRGRVTQVTGTILKAvvpGVRIGELCYLRNPDNSLSLQAEVIGFAQHQalltpLGE----------MY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 102 GLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYA 181
Cdd:PRK06936 81 GISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 182 RGGKIGLFGGAGVGKTVFIQELINNiakAHGGFSVFTGVGERTREgndlYREMKETGvINLEGESKVALVFGQMNEPPGA 261
Cdd:PRK06936 161 EGQRMGIFAAAGGGKSTLLASLIRS---AEVDVTVLALIGERGRE----VREFIESD-LGEEGLRKAVLVVATSDRPSME 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 262 RARVALTGLTIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQ 341
Cdd:PRK06936 233 RAKAGFVATSIAEYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 342 AVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDaAVVGQEHYDVASKVQETLQTYKSLQDII 421
Cdd:PRK06936 312 TVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELLL 390
|
410 420 430
....*....|....*....|....*....|..
gi 398365477 422 AI----LGMDELSEQdklTVERARKIQRFLSQ 449
Cdd:PRK06936 391 QIgeyqKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
23-450 |
3.55e-51 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 180.35 E-value: 3.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 23 PLLSTSWKRCMASAAQSTpITGKVTAVIGAIVDVhfeqSELPAILNAL-EIKTPQGKLvLEVAQHLG-ENTVRTIAMDGT 100
Cdd:PRK09099 6 SRLADALERELAALPAVR-RTGKVVEVIGTLLRV----SGLDVTLGELcELRQRDGTL-LQRAEVVGfSRDVALLSPFGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 101 -EGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAP 179
Cdd:PRK09099 80 lGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 180 YARGGKIGLFGGAGVGKTVfiqeLINNIAK-AHGGFSVFTGVGERTREgndlYREMKETgVINLEGESKVALVFGQMNEP 258
Cdd:PRK09099 160 LGEGQRMGIFAPAGVGKST----LMGMFARgTQCDVNVIALIGERGRE----VREFIEL-ILGEDGMARSVVVCATSDRS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 259 PGARARVALTGLTIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVT 338
Cdd:PRK09099 231 SIERAKAAYVATAIAEYFRDR-GLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSIT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 339 SVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLdAAVVGQEHYDVASKVQETLQTYKSLQ 418
Cdd:PRK09099 310 ALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVE 388
|
410 420 430
....*....|....*....|....*....|....*.
gi 398365477 419 DIIAI----LGMDELSEQdklTVERARKIQRFLSQP 450
Cdd:PRK09099 389 TLLQVgeyrAGSDPVADE---AIAKIDAIRDFLSQR 421
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
1-449 |
4.69e-51 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 180.01 E-value: 4.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 1 MVLPRLYTATSRAAFKAAKQSAPllstswkrcmasaAQSTPITGKVTAVIGAIVDVHF---EQSELPAIlnaleikTPQG 77
Cdd:PRK06820 1 MKLPDIARLTPRLQQQLTRPSAP-------------PEGLRYRGPIVEIGPTLLRASLpgvAQGELCRI-------EPQG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 78 KLVLEVAqhLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRkPIHADPPSF 157
Cdd:PRK06820 61 MLAEVVS--IEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWR-ELDCPPPSP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 158 AEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELInniAKAHGGFSVFTGVGERTREgndlYREMKET 237
Cdd:PRK06820 138 LTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLC---ADSAADVMVLALIGERGRE----VREFLEQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 238 gVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPT 317
Cdd:PRK06820 211 -VLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDR-GKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 318 LATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDaAVVG 397
Cdd:PRK06820 289 VFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMP-QIVS 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 398365477 398 QEHYDVASKVQETLQTYKSLQDIIAIlgMDELSEQDKLT---VERARKIQRFLSQ 449
Cdd:PRK06820 368 AGQLAMAQKLRRMLACYQEIELLVRV--GEYQAGEDLQAdeaLQRYPAICAFLQQ 420
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
114-425 |
2.37e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 178.65 E-value: 2.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 114 GPISVPVGRETLGRIINVIGEPIDERGPIKSKLRK-PIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGA 192
Cdd:PRK06002 95 GPLRIRPDPSWKGRVINALGEPIDGLGPLAPGTRPmSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGS 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 193 GVGKTVfiqeLINNIAKAHGGFSVFTG-VGERTREgndlYREM-KETGVINLegeSKVALVFGQMNEPPGARARVALTGL 270
Cdd:PRK06002 175 GVGKST----LLAMLARADAFDTVVIAlVGERGRE----VREFlEDTLADNL---KKAVAVVATSDESPMMRRLAPLTAT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 271 TIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERI--TTTKKGSVTSVQAVYVPAD 348
Cdd:PRK06002 244 AIAEYFRDR-GENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGD 322
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365477 349 DLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHyDVASKVQETLQTYKSLQDIIAILG 425
Cdd:PRK06002 323 DHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQR-KLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
44-423 |
4.97e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 177.22 E-value: 4.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 44 GKVTAVIGAIVDVHFEQSELPAILNALEIKTPQGKLVLEVAQHLGENtVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRE 123
Cdd:PRK07721 20 GKVSRVIGLMIESKGPESSIGDVCYIHTKGGGDKAIKAEVVGFKDEH-VLLMPYTEVAEIAPGCLVEATGKPLEVKVGSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 124 TLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVfiqeL 203
Cdd:PRK07721 99 LIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKST----L 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 204 INNIAK-AHGGFSVFTGVGERTREgndlYREMKETGvINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEeGQ 282
Cdd:PRK07721 175 MGMIARnTSADLNVIALIGERGRE----VREFIERD-LGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQ-GL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 283 DVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHL 362
Cdd:PRK07721 249 NVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTVRGIL 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365477 363 DATTVLSRGISELGIYPAVDPLDSKSRLLDaAVVGQEHYDVASKVQETLQTYKSLQDIIAI 423
Cdd:PRK07721 329 DGHFVLDRQLANKGQYPAINVLKSVSRVMN-HIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
42-423 |
5.62e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 174.40 E-value: 5.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 42 ITGKVTAVIGAIVDVHFEQSELpAILNALEIKTPQGKLVL-EVaqhLGENTVRTIAM--DGTEGLVRGEKVLDTGGPISV 118
Cdd:PRK08927 17 IYGRVVAVRGLLVEVAGPIHAL-SVGARIVVETRGGRPVPcEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 119 PVGRETLGRIINVIGEPIDERGPI-KSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKT 197
Cdd:PRK08927 93 RPSRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 198 VFIQELINNIAKAhggFSVFTGVGERTREgndlYREMKETgVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFR 277
Cdd:PRK08927 173 VLLSMLARNADAD---VSVIGLIGERGRE----VQEFLQD-DLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 278 DeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERI--TTTKKGSVTSVQAVYVPADDLTDPAP 355
Cdd:PRK08927 245 D-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPVA 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365477 356 ATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAvVGQEHYDVASKVQETLQTYKSLQDIIAI 423
Cdd:PRK08927 324 DAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGC-NDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
41-423 |
1.98e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 172.96 E-value: 1.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 41 PITGKVTAVIGaivdVHFEQSELPAILNAL-EIKTPQGKLVLEVAQHLGENTVrTIAMDGTEGLVRGEKVLDTGGPISVP 119
Cdd:PRK08972 24 VASGKLVRVVG----LTLEATGCRAPVGSLcSIETMAGELEAEVVGFDGDLLY-LMPIEELRGVLPGARVTPLGEQSGLP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 120 VGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVf 199
Cdd:PRK08972 99 VGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSV- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 200 iqeLINNIAKAHGGFSVFTG-VGERTREGNDLYREmketgVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRD 278
Cdd:PRK08972 178 ---LLGMMTRGTTADVIVVGlVGERGREVKEFIEE-----ILGEEGRARSVVVAAPADTSPLMRLKGCETATTIAEYFRD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 279 eEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITT--TKKGSVTSVQAVYVPADDLTDPAPA 356
Cdd:PRK08972 250 -QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNggPGQGSITAFYTVLTEGDDLQDPIAD 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365477 357 TTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLdAAVVGQEHYDVASKVQETLQTYKSLQDIIAI 423
Cdd:PRK08972 329 ASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLISI 394
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
101-449 |
3.04e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 172.56 E-value: 3.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 101 EGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPY 180
Cdd:PRK08472 75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTC 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 181 ARGGKIGLFGGAGVGKTVFIQELINNiAKAHggFSVFTGVGERTRE---------GNDLyremkETGVInlegeskvalV 251
Cdd:PRK08472 155 GKGQKLGIFAGSGVGKSTLMGMIVKG-CLAP--IKVVALIGERGREipefieknlGGDL-----ENTVI----------V 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 252 FGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITT 331
Cdd:PRK08472 217 VATSDDSPLMRKYGAFCAMSVAEYFKN-QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 332 TK-KGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDaAVVGQEHYDVASKVQET 410
Cdd:PRK08472 296 EEgKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRL 374
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 398365477 411 LQTYKSLQDIIAI----LGMD-ELSEqdklTVERARKIQRFLSQ 449
Cdd:PRK08472 375 YSLLKENEVLIRIgayqKGNDkELDE----AISKKEFMEQFLKQ 414
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
76-449 |
9.05e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 171.31 E-value: 9.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 76 QGKLVLEVAQHLGENTVrTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPP 155
Cdd:PRK06793 50 EHNVLCEVIAIEKENNM-LLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 156 SFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVfiqeLINNIAK-AHGGFSVFTGVGERTREGNDLYRem 234
Cdd:PRK06793 129 HAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST----LLGMIAKnAKADINVISLVGERGREVKDFIR-- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 235 KETGVinlEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAvGY 314
Cdd:PRK06793 203 KELGE---EGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVKELPIG-GK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 315 QPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDaA 394
Cdd:PRK06793 278 TLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-E 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 398365477 395 VVGQEHYDVASKVQETLQTYKSlQDIIAILGMDELSEQDKLTVERARK---IQRFLSQ 449
Cdd:PRK06793 357 IVSPNHWQLANEMRKILSIYKE-NELYFKLGTIQENAENAYIFECKNKvegINTFLKQ 413
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
80-457 |
6.24e-45 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 163.24 E-value: 6.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 80 VLEVAQHLGENTVRTI--AMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEpIDER------GPIKSKLRkPIH 151
Cdd:PRK08149 42 VIARAQVVGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGK-IVERfdapptVGPISEER-VID 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 152 ADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNiakAHGGFSVFTGVGERTREGNDLY 231
Cdd:PRK08149 120 VAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGERGREVTEFV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 232 REMKETGvinleGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSA 311
Cdd:PRK08149 197 ESLRASS-----RREKCVLVYATSDFSSVDRCNAALVATTVAEYFRD-QGKRVVLFIDSMTRYARALRDVALAAGELPAR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 312 VGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLL 391
Cdd:PRK08149 271 RGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVF 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365477 392 DaAVVGQEHYDVASKVQETLQTYKSLQDIIAiLG---MDELSEQDKlTVERARKIQRFLSQPFAVAEVF 457
Cdd:PRK08149 351 G-QVTDPKHRQLAAAFRKLLTRLEELQLFID-LGeyrRGENADNDR-AMDKRPALEAFLKQDVAEKSSF 416
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
101-449 |
5.52e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 158.36 E-value: 5.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 101 EGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPY 180
Cdd:PRK05688 86 AGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTV 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 181 ARGGKIGLFGGAGVGKTVFIqelinniakahGGFSVFTG--------VGERTREGNDLYREmketgVINLEGESKVALVF 252
Cdd:PRK05688 166 GRGQRLGLFAGTGVGKSVLL-----------GMMTRFTEadiivvglIGERGREVKEFIEH-----ILGEEGLKRSVVVA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 253 GQMNEPPGARARVALTGLTIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTT 332
Cdd:PRK05688 230 SPADDAPLMRLRAAMYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 333 KKG--SVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLdAAVVGQEHYDVASKVQET 410
Cdd:PRK05688 309 EPGggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQL 387
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 398365477 411 LQTYKSLQDIIAI----LGMDelSEQDkLTVERARKIQRFLSQ 449
Cdd:PRK05688 388 WSRYQQSRDLISVgayvAGGD--PETD-LAIARFPHLVQFLRQ 427
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
71-451 |
5.13e-42 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 156.14 E-value: 5.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 71 EIKTPQGKL----VLEVAqhlGENTVRTIaMDGTEGL-VRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSK 145
Cdd:PRK04196 30 EIELPNGEKrrgqVLEVS---EDKAVVQV-FEGTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 146 LRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKtvfiQELINNI---AKAHGGFS----VFT 218
Cdd:PRK04196 106 KRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPH----NELAAQIarqAKVLGEEEnfavVFA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 219 GVGERTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGAR---ARVAltgLTIAEYFRDEEGQDVLLFIDNIFRFT 295
Cdd:PRK04196 182 AMGITFEEANFFMEDFEETGALE-----RSVVFLNLADDPAIERiltPRMA---LTAAEYLAFEKGMHVLVILTDMTNYC 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 296 QAGSEVSALLGRIPSAVGYQPTLATDMGLLQER--ITTTKKGSVTSVQAVYVPADDLTDPAPattfahlDAT-------T 366
Cdd:PRK04196 254 EALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyitegqI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 367 VLSRGISELGIYPAVDPLDSKSRLLDAAvVG-----QEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERAR 441
Cdd:PRK04196 327 VLSRELHRKGIYPPIDVLPSLSRLMKDG-IGegktrEDHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFAD 405
|
410
....*....|.
gi 398365477 442 KI-QRFLSQPF 451
Cdd:PRK04196 406 AFeREFVNQGF 416
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
100-423 |
6.68e-42 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 155.11 E-value: 6.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 100 TEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERgPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAP 179
Cdd:PRK07594 73 TIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVAT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 180 YARGGKIGLFGGAGVGKTVFIQELINniaKAHGGFSVFTGVGERTREgndlYREMKETgVINLEGESKVALVFGQMNEPP 259
Cdd:PRK07594 152 CGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGRE----VREFIDF-TLSEETRKRCVIVVATSDRPA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 260 GARARVALTGLTIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTS 339
Cdd:PRK07594 224 LERVRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 340 VQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLdAAVVGQEHYDVASKVQETLQTYKSLQD 419
Cdd:PRK07594 303 FYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEVEL 381
|
....
gi 398365477 420 IIAI 423
Cdd:PRK07594 382 LIRI 385
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
102-449 |
5.14e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 152.74 E-value: 5.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 102 GLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKlrKPIHADPPSF--AEQSTSAEILETGIKVVDLLAP 179
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGS--TPLQQQLPQIhpLQRRAVDTPLDVGVNAINGLLT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 180 YARGGKIGLFGGAGVGKTVfiqeLINNIAKAHGGFSVFTG-VGERTREgndlYREMKETGvINLEGESKVALVFGQMNEP 258
Cdd:PRK07196 152 IGKGQRVGLMAGSGVGKSV----LLGMITRYTQADVVVVGlIGERGRE----VKEFIEHS-LQAAGMAKSVVVAAPADES 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 259 PGARARVALTGLTIAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTK-KGSV 337
Cdd:PRK07196 223 PLMRIKATELCHAIATYYRDK-GHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSgNGTM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 338 TSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLdAAVVGQEHYDVASKVQETLQTYKSL 417
Cdd:PRK07196 302 TAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCM-SQVIGSQQAKAASLLKQCYADYMAI 380
|
330 340 350
....*....|....*....|....*....|....*.
gi 398365477 418 QDIIA----ILGMDELSEQdklTVERARKIQRFLSQ 449
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 ... |
43-116 |
4.19e-38 |
|
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: 133.80 E-value: 4.19e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365477 43 TGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQG-KLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPI 116
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 ... |
115-395 |
7.33e-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: 134.66 E-value: 7.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 115 PISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGV 194
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 195 GKtvfiQELINNIA------KAHGGFS-VFTGVGERTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGARARVAL 267
Cdd:cd01135 81 PH----NELAAQIArqagvvGSEENFAiVFAAMGVTMEEARFFKDDFEETGALE-----RVVLFLNLANDPTIERIITPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 268 TGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQER--ITTTKKGSVTSVQAVYV 345
Cdd:cd01135 152 MALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTM 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 398365477 346 PADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAV 395
Cdd:cd01135 232 PNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGI 281
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
72-423 |
7.74e-35 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 136.07 E-value: 7.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 72 IKTPQGKLVLEV-AQHLGENTVRTIAM--DGTEGLVRGEKVLDTGGPIS-------VPVGRETLGRIINVIGEPIDERGP 141
Cdd:PRK07960 54 IERQNGSETHEVeSEVVGFNGQRLFLMplEEVEGILPGARVYARNISGEglqsgkqLPLGPALLGRVLDGSGKPLDGLPA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 142 IKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVfiqeLINNIAKAHGGFSVFTG-V 220
Cdd:PRK07960 134 PDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSV----LLGMMARYTQADVIVVGlI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 221 GERTREGNDLYREmketgVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSE 300
Cdd:PRK07960 210 GERGREVKDFIEN-----ILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQRE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 301 VSALLGRIPSAVGYQPTLATDMGLLQERITT--TKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIY 378
Cdd:PRK07960 284 IALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHY 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 398365477 379 PAVDPLDSKSRLLdAAVVGQEHYDVASKVQETLQTYKSLQDIIAI 423
Cdd:PRK07960 364 PAIDIEASISRAM-TALIDEQHYARVRQFKQLLSSFQRNRDLVSV 407
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
59-452 |
1.54e-32 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 129.25 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 59 EQSELPAILNAL-EIKTPQGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPID 137
Cdd:PRK05922 32 EAQGLSACLGELcQISLSKSPPILAEVIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 138 ERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTvfiqELINNIAK-AHGGFSV 216
Cdd:PRK05922 112 GKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSKSTINV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 217 FTGVGERTREGNDlYREMKETGVinleGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQ 296
Cdd:PRK05922 188 IALIGERGREVRE-YIEQHKEGL----AAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 297 AGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAV-YVP--ADDLTDPAPATTFAHLDATTVLSRGIS 373
Cdd:PRK05922 262 ALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIlHYPnhPDIFTDYLKSLLDGHFFLTPQGKALAS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 374 elgiyPAVDPLDSKSRLLDAAVVgQEHYDVASKVQETLQTYKSLQDIIAiLGMdELSEQDKlTVERARK----IQRFLSQ 449
Cdd:PRK05922 342 -----PPIDILTSLSRSARQLAL-PHHYAAAEELRSLLKAYHEALDIIQ-LGA-YVPGQDA-HLDRAVKllpsIKQFLSQ 412
|
...
gi 398365477 450 PFA 452
Cdd:PRK05922 413 PLS 415
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
43-486 |
2.79e-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: 129.43 E-value: 2.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 43 TGKVTAVIGAIVDVHfeqsELPAILNALEIKTPQGklVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGR 122
Cdd:TIGR00962 27 VGTVVSVGDGIARVY----GLENVMSGELIEFEGG--VQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 123 ETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKT-VFIQ 201
Cdd:TIGR00962 101 GLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTaVAID 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 202 ELINNiaKAHGGFSVFTGVGERTREGNDLYREMKETGVInlegeSKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEG 281
Cdd:TIGR00962 181 TIINQ--KDSDVYCIYVAIGQKASTVAQVVRKLEEHGAM-----AYTIVVAATASDSASLQYLAPYTGCTMGEYFRD-NG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 282 QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTK----KGSVTSVQAVYVPADDLTDPAPAT 357
Cdd:TIGR00962 253 KHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNdekgGGSLTALPIIETQAGDVSAYIPTN 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 358 TFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVgQEHYDVASKVQETLQTYKSLqDIIAILGMDeLSEQDKLTV 437
Cdd:TIGR00962 333 VISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQI-KAMKQVAGSLRLELAQYREL-EAFSQFASD-LDEATKKQL 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 398365477 438 ERARKIQRFLSQPfavaevftgiPGKLVRLKDTVASFKAVLEGKYDNIP 486
Cdd:TIGR00962 410 ERGQRVVELLKQP----------QYKPLSVEEQVVILFAGTKGYLDDIP 448
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
83-389 |
3.82e-28 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 117.32 E-value: 3.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 83 VAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQST 162
Cdd:PRK13343 62 FAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 163 SAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVF-IQELINNiaKAHGGFSVFTGVGERTREGNDLYREMKETGVIn 241
Cdd:PRK13343 142 VTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIaIDAIINQ--KDSDVICVYVAIGQKASAVARVIETLREHGAL- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 242 legeSKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD 321
Cdd:PRK13343 219 ----EYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYL 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365477 322 MGLLQERITTTKK----GSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSR 389
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 ... |
80-449 |
1.30e-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: 115.20 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 80 VLEVAqhlGENTVRTIaMDGTEGL-VRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFA 158
Cdd:TIGR01040 41 VLEVS---GNKAVVQV-FEGTSGIdAKKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 159 EQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKtvfiQELINNIAKAHG---------------GFS-VFTGVGE 222
Cdd:TIGR01040 117 ARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPH----NEIAAQICRQAGlvklptkdvhdghedNFAiVFAAMGV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 223 RTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVS 302
Cdd:TIGR01040 193 NMETARFFKQDFEENGSME-----RVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 303 ALLGRIPSAVGYQPTLATDMGLLQERI--TTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPA 380
Cdd:TIGR01040 268 AAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPP 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365477 381 VDPLDSKSRLLDAAV----VGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIQR-FLSQ 449
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 ... |
154-389 |
4.61e-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: 4.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 154 PPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELinniAK-AHGGFSVFTGVGERtreGNDLYR 232
Cdd:cd01134 47 PRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSL----SKwSNSDVVIYVGCGER---GNEMAE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 233 EMKE--TGVINLEGES---KVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGR 307
Cdd:cd01134 120 VLEEfpELKDPITGESlmeRTVLIANTSNMPVAAREASIYTGITIAEYFRD-MGYNVSLMADSTSRWAEALREISGRLEE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 308 IPSAVGYQPTLATDMGLLQERI-------TTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPA 380
Cdd:cd01134 199 MPAEEGYPAYLGARLAEFYERAgrvrclgSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPS 278
|
....*....
gi 398365477 381 VDPLDSKSR 389
Cdd:cd01134 279 INWLISYSK 287
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
116-449 |
1.53e-23 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 104.09 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 116 ISVPVGREtlGRIINVIG-------EPI----DERGPIKS-KL------RKPIHadppsFAEQSTSAEILETGIKVVDLL 177
Cdd:PRK04192 149 IMVPPGVS--GTVKEIVSegdytvdDTIavleDEDGEGVElTMmqkwpvRRPRP-----YKEKLPPVEPLITGQRVIDTF 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 178 APYARGGKIGLFGGAGVGKTVFIQELinniAK-AHGGFSVFTGVGERtreGNdlyrEMKEtgVIN----LE----GES-- 246
Cdd:PRK04192 222 FPVAKGGTAAIPGPFGSGKTVTQHQL----AKwADADIVIYVGCGER---GN----EMTE--VLEefpeLIdpktGRPlm 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 247 -KVALVFGQMNEPPGAR-ARVaLTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGL 324
Cdd:PRK04192 289 eRTVLIANTSNMPVAAReASI-YTGITIAEYYRD-MGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 325 LQER---ITT--TKKGSVTSVQAVYVPADDLTDPapaTTFAHLDATTV---LSRGISELGIYPAVDPLDSKSRLLD---- 392
Cdd:PRK04192 367 FYERagrVKTlgGEEGSVTIIGAVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADRRHFPAINWLTSYSLYLDqvap 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 393 --AAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKI-QRFLSQ 449
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 ... |
116-309 |
2.95e-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: 93.39 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 116 ISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVG 195
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 196 KT-VFIQELINNiaKAHGGFSVFTGVGERTREGNDLYREMKETGVINlegesKVALVFGQMNEPPGARARVALTGLTIAE 274
Cdd:cd01132 82 KTaIAIDTIINQ--KGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAME-----YTIVVAATASDPAPLQYLAPYAGCAMGE 154
|
170 180 190
....*....|....*....|....*....|....*
gi 398365477 275 YFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIP 309
Cdd:cd01132 155 YFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPP 188
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
216-461 |
1.25e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 95.86 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 216 VFTGVGERTREGNDLYREMKE-----TGVINLEgesKVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDN 290
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFPKlkdpkTGKPLME---RTVLIANTSNMPVAAREASIYTGITIAEYFRD-MGYDVALMADS 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 291 IFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERI-------TTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLD 363
Cdd:PRK14698 762 TSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVK 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 364 ATTVLSRGISELGIYPAVDPLDSKSRLLDAAV------VGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTV 437
Cdd:PRK14698 842 VFWALDADLARRRHFPAINWLTSYSLYVDAVKdwwhknVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAIL 921
|
250 260
....*....|....*....|....
gi 398365477 438 ERARKIQRFLSQPFAVAEVFTGIP 461
Cdd:PRK14698 922 LVARMLREDYLQQDAFDEVDTYCP 945
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
46-113 |
1.33e-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: 82.59 E-value: 1.33e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365477 46 VTAVIGAIVDVHFEQSELPAILNALEIKTP-QGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTG 113
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVeFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
43-309 |
1.51e-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: 91.25 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 43 TGKVTAVIGAIVDVHfeqsELP-AILNALeIKTPQGklVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVG 121
Cdd:COG0056 28 VGTVLSVGDGIARVY----GLPnAMAGEL-LEFPGG--VYGMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 122 RETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKT-VFI 200
Cdd:COG0056 101 EALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTaIAI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 201 QELINNiaKAHGGFSVFTGVGERtregndlyremketgvinlegESKVALV------FGQM----------NEPPGARAR 264
Cdd:COG0056 181 DTIINQ--KGKDVICIYVAIGQK---------------------ASTVAQVvetleeHGAMeytivvaataSDPAPLQYI 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 398365477 265 VALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIP 309
Cdd:COG0056 238 APYAGCAMGEYFMD-QGKDVLIVYDDLSKHAVAYRELSLLLRRPP 281
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
45-390 |
1.54e-19 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 90.86 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 45 KVTAVIGAIVDVhfeQSELPAILNALEIKTPQGKLVLEVAqHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRET 124
Cdd:PRK02118 7 KITDITGNVITV---EAEGVGYGELATVERKDGSSLAQVI-RLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 125 LGRIINVIGEPIDeRGPIKSKlrKPIHADPPSF--AEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGktvfIQE 202
Cdd:PRK02118 83 LGRRFNGSGKPID-GGPELEG--EPIEIGGPSVnpVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEP----YNA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 203 LINNIA-KAHGGFSVFTGVGERTREGNDLYREMKETGVInlegeSKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEG 281
Cdd:PRK02118 156 LLARIAlQAEADIIILGGMGLTFDDYLFFKDTFENAGAL-----DRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 282 QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQER-ITTTKKGSVTSVQAVYVPADDLTDPAPATTFA 360
Cdd:PRK02118 231 KKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKaVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGY 310
|
330 340 350
....*....|....*....|....*....|
gi 398365477 361 HLDATTVLSRGiselgiypAVDPLDSKSRL 390
Cdd:PRK02118 311 ITEGQFYLRRG--------RIDPFGSLSRL 332
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
80-309 |
1.01e-18 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 88.97 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 80 VLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPS-FA 158
Cdd:PRK09281 59 VYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGvID 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 159 EQSTSaEILETGIKVVDLLAPYARGGKIGLFGGAGVGKT-VFIQELINNiaKAHGGFSVFTGVGERtregndlyremket 237
Cdd:PRK09281 139 RKSVH-EPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTaIAIDTIINQ--KGKDVICIYVAIGQK-------------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 238 gvinlegESKVALV------FGQM----------NEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEV 301
Cdd:PRK09281 202 -------ASTVAQVvrkleeHGAMeytivvaataSDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQL 273
|
....*...
gi 398365477 302 SALLGRIP 309
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, ... |
400-468 |
6.69e-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: 6.69e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365477 400 HYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGKLVRLK 468
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIK 69
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
95-417 |
1.00e-12 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 70.45 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 95 IAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPID------ERGPIKSKLR-KPIHADPPSFAEQSTSAEIL 167
Cdd:PTZ00185 94 ILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrSRALLESEQTlGKVDAGAPNIVSRSPVNYNL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 168 ETGIKVVDLLAPYARGGKIGLFGGAGVGKT-VFIQELIN------NIAKAHGGFSVFTGVGERTREGNDLYREMKETGVI 240
Cdd:PTZ00185 174 LTGFKAVDTMIPIGRGQRELIVGDRQTGKTsIAVSTIINqvrinqQILSKNAVISIYVSIGQRCSNVARIHRLLRSYGAL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 241 NLegeskVALVFGQMNEPPGARARVALTGLTIAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLAT 320
Cdd:PTZ00185 254 RY-----TTVMAATAAEPAGLQYLAPYSGVTMGEYFMN-RGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFY 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 321 DMGLLQERITTTKK----GSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAvV 396
Cdd:PTZ00185 328 LHSRLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSA-Q 406
|
330 340
....*....|....*....|.
gi 398365477 397 GQEHYDVASKVQETLQTYKSL 417
Cdd:PTZ00185 407 NVAMKAVAGKLKGILAEYRKL 427
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
83-474 |
1.03e-12 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 69.99 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 83 VAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQST 162
Cdd:CHL00059 41 IALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 163 SAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKT-VFIQELINNiaKAHGGFSVFTGVGERTREGNDLYREMKETGVIn 241
Cdd:CHL00059 121 VYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTaVATDTILNQ--KGQNVICVYVAIGQKASSVAQVVTTLQERGAM- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 242 legesKVALVFGQMNEPPGARARVA-LTGLTIAEYFRdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYqptlAT 320
Cdd:CHL00059 198 -----EYTIVVAETADSPATLQYLApYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAY----PG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 321 DMGLLQERI--------TTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLD 392
Cdd:CHL00059 268 DVFYLHSRLleraaklsSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGS 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 393 AAVVgQEHYDVASKVQETLQTYKSLQDIIAIlgmdeLSEQDKLT---VERARKIQRFLSQ----PFAVAE----VFTGIP 461
Cdd:CHL00059 348 AAQI-KAMKQVAGKLKLELAQFAELEAFAQF-----ASDLDKATqnqLARGQRLRELLKQsqsaPLTVEEqvatIYTGTN 421
|
410
....*....|....
gi 398365477 462 GKLVRLK-DTVASF 474
Cdd:CHL00059 422 GYLDSLEiGQVRKF 435
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
114-389 |
1.71e-06 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 50.08 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 114 GPISVPVGRETLGRIINVIGepideRGPIKSKLRKPIHADPPSFAEQSTsaeILETG-----IKVVDLLAPYARGGKIGL 188
Cdd:PRK12608 67 GVARPRERYRVLVRVDSVNG-----TDPEKLARRPHFDDLTPLHPRERL---RLETGsddlsMRVVDLVAPIGKGQRGLI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 189 FGGAGVGKTVFIQELINNIAKAHGGFSVFTG-VGERTREGNDLYREMKetgvinleGEskvalVFGQMNEPPGARaRVAL 267
Cdd:PRK12608 139 VAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDMRRSVK--------GE-----VYASTFDRPPDE-HIRV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 268 TGLTIAEYFRD-EEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAvgyqptlATDMGLLQ--ERITTTKK-----GSVTS 339
Cdd:PRK12608 205 AELVLERAKRLvEQGKDVVILLDSLTRLARAYNNEVESSGRTLSG-------GVDARALQrpKRLFGAARnieegGSLTI 277
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 398365477 340 VQAVYVP----ADDLtdpapatTFAHLDAT----TVLSRGISELGIYPAVDPLDSKSR 389
Cdd:PRK12608 278 IATALVDtgsrMDEV-------IFEEFKGTgnmeIVLDRELADKRVFPAIDIAKSGTR 328
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
182-307 |
4.34e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.60 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 182 RGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGESKVALVFgqmneppgA 261
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLAL--------A 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 398365477 262 RARvaltgltiaeyfrdeEGQDVLLFIDNIFRFTQAGSEVSALLGR 307
Cdd:smart00382 73 LAR---------------KLKPDVLILDEITSLLDAEQEALLLLLE 103
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
49-310 |
6.88e-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: 45.06 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 49 VIGAIVDVHFEQSELPAILNALEIkTPQGKLVLEVAQHL----GENTVRTIAMDGTEGLVRGEKVLdtgGPISVPVGRET 124
Cdd:TIGR00767 34 LIFAILKAHAEQGGLIFGEGVLEI-LPDGFGFLRSPDSSylpgPDDIYVSPSQIRRFNLRTGDTIE---GQIRSPKEGER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 125 LGRIINVigEPIDERGPIKSKLRKPIHADPPSFAEQ----STSAEILETgiKVVDLLAPYARGGKIGLFGGAGVGKTVFI 200
Cdd:TIGR00767 110 YFALLKV--ESVNGDDPEKAKNRVLFENLTPLYPNErlrlETSTEDLST--RVLDLFAPIGKGQRGLIVAPPKAGKTVLL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 201 QELINNIAKAHGG-FSVFTGVGERTREGNDLYREMKetgvinleGESkVALVFgqmNEPPGARARVALTGLTIAEYfRDE 279
Cdd:TIGR00767 186 QKIAQAITRNHPEvELIVLLIDERPEEVTDMQRSVK--------GEV-VASTF---DEPASRHVQVAEMVIEKAKR-LVE 252
|
250 260 270
....*....|....*....|....*....|.
gi 398365477 280 EGQDVLLFIDNIFRFTQAGSEVSALLGRIPS 310
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, ... |
43-114 |
2.89e-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: 39.22 E-value: 2.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365477 43 TGKVTAVIGAIVDVHFEqsELPAILNALEIKTPQG----KLVLEVAQHLGENTVrTIAMDGTEGLVRGEKVLDTGG 114
Cdd:cd01426 1 KGRVIRVNGPLVEAELE--GEVAIGEVCEIERGDGnnetVLKAEVIGFRGDRAI-LQLFESTRGLSRGALVEPTGR 73
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
121-236 |
7.59e-04 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 42.32 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 121 GRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPsFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFI 200
Cdd:PRK14698 166 GEYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRP-YKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDG 244
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 398365477 201 QELI----NNIAKAHGGFSVFTGVGERTREGNDLYREMKE 236
Cdd:PRK14698 245 DTLIltkeFGLIKIKDLYEILDGKGKKTVEGNEEWTELEE 284
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
172-389 |
1.93e-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: 39.88 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 172 KVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTG-VGERTREGNDLYREMKetgvinleGESkVAL 250
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTDMRRSVK--------GEV-VAS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 251 VFgqmNEPPGARARVALTGLTIAEYfRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAvgyqptlATDMGLLQ--ER 328
Cdd:cd01128 76 TF---DEPPERHVQVAEMVIEKAKR-LVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSG-------GVDANALHkpKR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365477 329 ITTTKK-----GSVTSVQAVYVP----ADDLtdpapatTFAHLDAT----TVLSRGISELGIYPAVDPLDSKSR 389
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 ... |
406-449 |
4.15e-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: 4.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 398365477 406 KVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIqR--FLSQ 449
Cdd:cd18111 7 EAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMI-RedFLQQ 51
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
122-241 |
4.94e-03 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 39.57 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365477 122 RETLGRIINVIG---EPIDERGPIKSKL--RKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGK 196
Cdd:PRK07165 77 KEYFGKIIDIDGniiYPEAQNPLSKKFLpnTSSIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGK 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 398365477 197 T-VFIQELINNiaKAHGGFSVFTGVGERTREGNDLYREMKETGVIN 241
Cdd:PRK07165 157 ThIALNTIINQ--KNTNVKCIYVAIGQKRENLSRIYETLKEHDALK 200
|
|
| |
