|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
12-482 |
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: 937.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 12 TAAATGRIARVIGPVVDVEFPADAIPGIYHALTAEitlNGETHTVTFEVSQHLGDNLVRAISLQATDGLVRGAAVFDTGA 91
Cdd:COG0055 1 MAMNTGKIVQVIGPVVDVEFPEGELPAIYNALEVE---NEGGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 92 PISVPVGDGVKGHIFNVLGQPLDVAEsEIQYTERWPIHRKPPSFDQLEGSTEMLETGIKVIDLLTPYIKGGKIGLFGGAG 171
Cdd:COG0055 78 PISVPVGEATLGRIFNVLGEPIDGKG-PIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 172 VGKTVLIQEMITRVARNFGGTSVFAGVGERTREGNDLWVEMEESGVLKDTALVFGQMDEPPGTRLRVALSALTMAEYFRD 251
Cdd:COG0055 157 VGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 252 VQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITSTKGHSITSMQAVYVPADDYTDPAPAAT 331
Cdd:COG0055 237 EEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 332 FAHLDATTELSREIASRGLYPAVDPLTSTSRILDPQYIGKEHYDVAIRVKQILQKNKELQDIIAILGVDELSEEDKIVVS 411
Cdd:COG0055 317 FAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2577762856 412 RARRIQQFLSQNTYTAKQFTGVEGSTVSIKDTVEGFKAICDGDVDHIAEQAFFNVGALDDVERQWAKIQES 482
Cdd:COG0055 397 RARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAE 467
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
15-472 |
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: 811.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 15 ATGRIARVIGPVVDVEFPADAIPGIYHALTAEITLNGEthtVTFEVSQHLGDNLVRAISLQATDGLVRGAAVFDTGAPIS 94
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNRAESE---LTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 95 VPVGDGVKGHIFNVLGQPLDVAEsEIQYTERWPIHRKPPSFDQLEGSTEMLETGIKVIDLLTPYIKGGKIGLFGGAGVGK 174
Cdd:TIGR01039 78 VPVGKETLGRIFNVLGEPIDEKG-PIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 175 TVLIQEMITRVARNFGGTSVFAGVGERTREGNDLWVEMEESGVLKDTALVFGQMDEPPGTRLRVALSALTMAEYFRDVQN 254
Cdd:TIGR01039 157 TVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 255 QDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITSTKGHSITSMQAVYVPADDYTDPAPAATFAH 334
Cdd:TIGR01039 237 QDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 335 LDATTELSREIASRGLYPAVDPLTSTSRILDPQYIGKEHYDVAIRVKQILQKNKELQDIIAILGVDELSEEDKIVVSRAR 414
Cdd:TIGR01039 317 LDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2577762856 415 RIQQFLSQNTYTAKQFTGVEGSTVSIKDTVEGFKAICDGDVDHIAEQAFFNVGALDDV 472
Cdd:TIGR01039 397 RIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEV 454
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
1-487 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 740.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 1 MTATATEQGARTAAATGRIARVIGPVVDVEFPADAIPGIYHALTAEITLN-GETHTVTFEVSQHLGDNLVRAISLQATDG 79
Cdd:CHL00060 1 INPTGPGVSTLEEKNLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTaGQEINVTCEVQQLLGNNRVRAVAMSATDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 80 LVRGAAVFDTGAPISVPVGDGVKGHIFNVLGQPLDvAESEIQYTERWPIHRKPPSFDQLEGSTEMLETGIKVIDLLTPYI 159
Cdd:CHL00060 81 LMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVD-NLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 160 KGGKIGLFGGAGVGKTVLIQEMITRVARNFGGTSVFAGVGERTREGNDLWVEMEESGVLKD-------TALVFGQMDEPP 232
Cdd:CHL00060 160 RGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEqniaeskVALVYGQMNEPP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 233 GTRLRVALSALTMAEYFRDVQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITSTKGHSITS 312
Cdd:CHL00060 240 GARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 313 MQAVYVPADDYTDPAPAATFAHLDATTELSREIASRGLYPAVDPLTSTSRILDPQYIGKEHYDVAIRVKQILQKNKELQD 392
Cdd:CHL00060 320 IQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 393 IIAILGVDELSEEDKIVVSRARRIQQFLSQNTYTAKQFTGVEGSTVSIKDTVEGFKAICDGDVDHIAEQAFFNVGALDDV 472
Cdd:CHL00060 400 IIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEA 479
|
490
....*....|....*
gi 2577762856 473 ERQWAKIQESTGSTK 487
Cdd:CHL00060 480 TAKAANLEVESKLKK 494
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
94-366 |
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: 531.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 94 SVPVGDGVKGHIFNVLGQPLDVAEsEIQYTERWPIHRKPPSFDQLEGSTEMLETGIKVIDLLTPYIKGGKIGLFGGAGVG 173
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERG-PIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 174 KTVLIQEMITRVARNFGGTSVFAGVGERTREGNDLWVEMEESGV-----LKDTALVFGQMDEPPGTRLRVALSALTMAEY 248
Cdd:cd01133 80 KTVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVinldgLSKVALVYGQMNEPPGARARVALTGLTMAEY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 249 FRDVQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITSTKGHSITSMQAVYVPADDYTDPAP 328
Cdd:cd01133 160 FRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAP 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 2577762856 329 AATFAHLDATTELSREIASRGLYPAVDPLTSTSRILDP 366
Cdd:cd01133 240 ATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| 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: 530.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 17 GRIARVIGPVVDVEFPADaIPGIYHALTAeitlnGETHTVTFEVSQHLGDNLVRAISLQATDGLVRGAAVFDTGAPISVP 96
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDGE-LPAIHSVLRA-----GREGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 97 VGDGVKGHIFNVLGQPLDVAESEIQYTERwPIHRKPPSFDQLEGSTEMLETGIKVIDLLTPYIKGGKIGLFGGAGVGKTV 176
Cdd:TIGR03305 75 VGKPTLSRMFDVFGNTIDRREPPKDVEWR-SVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 177 LIQEMITRVARNFGGTSVFAGVGERTREGNDLWVEMEESGVLKDTALVFGQMDEPPGTRLRVALSALTMAEYFRDVQNQD 256
Cdd:TIGR03305 154 LLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 257 VLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITSTKGHSITSMQAVYVPADDYTDPAPAATFAHLD 336
Cdd:TIGR03305 234 VLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 337 ATTELSREIASRGLYPAVDPLTSTSRILDPQYIGKEHYDVAIRVKQILQKNKELQDIIAILGVDELSEEDKIVVSRARRI 416
Cdd:TIGR03305 314 ASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2577762856 417 QQFLSQNTYTAKQFTGVEGSTVSIKDTVEGFKAICDGDVDHIAEQAFFNVGALDD 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 ... |
94-363 |
2.08e-113 |
|
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: 335.58 E-value: 2.08e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 94 SVPVGDGVKGHIFNVLGQPLDVAeSEIQYTERWPIHRKPPSFDQLEGSTEMLETGIKVIDLLTPYIKGGKIGLFGGAGVG 173
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGL-PPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 174 KTVLIQEMITRVARNFGGTSVFAGVGERTREGNDLWVEMEESGVLKDTALVFGQMDEPPGTRLRVALSALTMAEYFRDvQ 253
Cdd:cd19476 80 KTVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRD-N 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 254 NQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITSTKGH--SITSMQAVYVPADDYTDPAPAAT 331
Cdd:cd19476 159 GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGggSITAIPAVSTPGDDLTDPIPDNT 238
|
250 260 270
....*....|....*....|....*....|..
gi 2577762856 332 FAHLDATTELSREIASRGLYPAVDPLTSTSRI 363
Cdd:cd19476 239 FAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
148-361 |
7.98e-93 |
|
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: 280.78 E-value: 7.98e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 148 GIKVIDLLTPYIKGGKIGLFGGAGVGKTVLIQeMITRVARNfgGTSVFAGVGERTREGNDLWVEMEESGVLKDTALVFGQ 227
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAG-MIARQASA--DVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 228 MDEPPGTRLRVALSALTMAEYFRDvQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITSTKG 307
Cdd:pfam00006 78 SDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2577762856 308 H--SITSMQAVYVPADDYTDPAPAATFAHLDATTELSREIASRGLYPAVDPLTSTS 361
Cdd:pfam00006 157 KggSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
10-450 |
3.43e-65 |
|
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: 216.82 E-value: 3.43e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 10 ARTAAATGRIARVIGPVVDVEFPADAI-------PGIYHALTAEItlngethtVTFEvsqhlgDNLVRAISLQATDGLVR 82
Cdd:COG1157 14 LPPVRVSGRVTRVVGLLIEAVGPDASIgelceieTADGRPVLAEV--------VGFR------GDRVLLMPLGDLEGISP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 83 GAAVFDTGAPISVPVGDGVKGHIFNVLGQPLDvAESEIQYTERWPIHRKPPSFDQLEGSTEMLETGIKVIDLLTPYIKGG 162
Cdd:COG1157 80 GARVVPTGRPLSVPVGDGLLGRVLDGLGRPLD-GKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 163 KIGLFGGAGVGKTVLIQeMITRvarnfgGTS----VFAGVGERTREGNDLwVE--MEESGvLKDTALVFGQMDEPPGTRL 236
Cdd:COG1157 159 RIGIFAGSGVGKSTLLG-MIAR------NTEadvnVIALIGERGREVREF-IEddLGEEG-LARSVVVVATSDEPPLMRL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 237 RVALSALTMAEYFRDvQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERI-TSTKGhSITSMQA 315
Cdd:COG1157 230 RAAYTATAIAEYFRD-QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAgNGGKG-SITAFYT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 316 VYVPADDYTDPAPAATFAHLDATTELSREIASRGLYPAVDPLTSTSRILdPQYIGKEHYDVAIRVKQILQKNKELQDIIA 395
Cdd:COG1157 308 VLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM-PDIVSPEHRALARRLRRLLARYEENEDLIR 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2577762856 396 IlG---------VDElseedkiVVSRARRIQQFLSQNTytakqftgveGSTVSIKDTVEGFKAI 450
Cdd:COG1157 387 I-GayqpgsdpeLDE-------AIALIPAIEAFLRQGM----------DERVSFEESLAQLAEL 432
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
94-363 |
6.03e-57 |
|
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: 190.08 E-value: 6.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 94 SVPVGDGVKGHIFNVLGQPLDVAEsEIQYTERWPIHRKPPSFDQLEGSTEMLETGIKVIDLLTPYIKGGKIGLFGGAGVG 173
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKG-LPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 174 KTVLIqEMITRVARNfgGTSVFAGVGERTREGNDLWVEMEESGVLKDTALVFGQMDEPPGTRLRVALSALTMAEYFRDvQ 253
Cdd:cd01136 80 KSTLL-GMIARNTDA--DVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRD-Q 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 254 NQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITSTKGHSITSMQAVYVPADDYTDPAPAATFA 333
Cdd:cd01136 156 GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRS 235
|
250 260 270
....*....|....*....|....*....|
gi 2577762856 334 HLDATTELSREIASRGLYPAVDPLTSTSRI 363
Cdd:cd01136 236 ILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| ATP-synt_F1_beta_C |
cd18110 |
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ... |
369-473 |
2.68e-56 |
|
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: 182.68 E-value: 2.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 369 IGKEHYDVAIRVKQILQKNKELQDIIAILGVDELSEEDKIVVSRARRIQQFLSQNTYTAKQFTGVEGSTVSIKDTVEGFK 448
Cdd:cd18110 2 VGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGFK 81
|
90 100
....*....|....*....|....*
gi 2577762856 449 AICDGDVDHIAEQAFFNVGALDDVE 473
Cdd:cd18110 82 EILDGEYDDLPEQAFYMVGTIDEAV 106
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
21-422 |
3.64e-51 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 179.42 E-value: 3.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 21 RVIGPVVDVEFPADAIPGIyhaltAEITLNGETHTVTFEvSQHLGDNLVRAI-SL-QATDGLVRGAAVFDTGAPISVPVG 98
Cdd:PRK08149 12 RIQGPIIEAELPDVAIGEI-----CEIRAGWHSNEVIAR-AQVVGFQRERTIlSLiGNAQGLSRQVVLKPTGKPLSVWVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 99 DGVKGHIFNVLGQ---PLDVAESEIQYTERWPIHRKPPSFDQLEGSTEMLETGIKVID-LLTPYIkGGKIGLFGGAGVGK 174
Cdd:PRK08149 86 EALLGAVLDPTGKiveRFDAPPTVGPISEERVIDVAPPSYAERRPIREPLITGVRAIDgLLTCGV-GQRMGIFASAGCGK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 175 TVLIQEMITR-VARNFggtsVFAGVGERTREGNDLWVEMEESGVLKDTALVFGQMDEPPGTRLRVALSALTMAEYFRDvQ 253
Cdd:PRK08149 165 TSLMNMLIEHsEADVF----VIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRD-Q 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 254 NQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITSTKGHSITSMQAVYVPADDYTDPAPAATFA 333
Cdd:PRK08149 240 GKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 334 HLDATTELSREIASRGLYPAVDPLTSTSRILDpQYIGKEHYDVAIRVKQILQKNKELQDIIailgvdELSE-------ED 406
Cdd:PRK08149 320 ILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFG-QVTDPKHRQLAAAFRKLLTRLEELQLFI------DLGEyrrgenaDN 392
|
410
....*....|....*.
gi 2577762856 407 KIVVSRARRIQQFLSQ 422
Cdd:PRK08149 393 DRAMDKRPALEAFLKQ 408
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
83-424 |
1.38e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 175.26 E-value: 1.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 83 GAAVFDTGAPISVPVGDGVKGHIFNVLGQPLDvAESEIQYTERWPIHRKPpsFDQLEGS--TEMLETGIKVIDLLTPYIK 160
Cdd:PRK08472 80 GDKVFISKEGLNIPVGRNLLGRVVDPLGRPID-GKGAIDYERYAPIMKAP--IAAMKRGliDEVFSVGVKSIDGLLTCGK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 161 GGKIGLFGGAGVGKTVLIQeMITRvarnfgGTS----VFAGVGERTREGNDlWVEMEESGVLKDTALVFGQMDEPPGTRL 236
Cdd:PRK08472 157 GQKLGIFAGSGVGKSTLMG-MIVK------GCLapikVVALIGERGREIPE-FIEKNLGGDLENTVIVVATSDDSPLMRK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 237 RVALSALTMAEYFRDvQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITSTKGH-SITSMQA 315
Cdd:PRK08472 229 YGAFCAMSVAEYFKN-QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGKgSITAFFT 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 316 VYVPADDYTDPAPAATFAHLDATTELSREIASRGLYPAVDPLTSTSRILDpQYIGKEHYDVAIRVKQILQKNKELQDIIA 395
Cdd:PRK08472 308 VLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENEVLIR 386
|
330 340 350
....*....|....*....|....*....|....
gi 2577762856 396 I----LGVD-ELSEedkiVVSRARRIQQFLSQNT 424
Cdd:PRK08472 387 IgayqKGNDkELDE----AISKKEFMEQFLKQNP 416
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
12-396 |
7.63e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 173.73 E-value: 7.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 12 TAAATGRIARVIGpvvdVEFPADAIPGIYHALTAEITLNGE--THTVTFEvsqhlgDNLVRAISLQATDGLVRGAAVFDT 89
Cdd:PRK08972 22 RAVASGKLVRVVG----LTLEATGCRAPVGSLCSIETMAGEleAEVVGFD------GDLLYLMPIEELRGVLPGARVTPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 90 GAPISVPVGDGVKGHIFNVLGQPLDvAESEIQYTERWPIHRKPPSFDQLEGSTEMLETGIKVIDLLTPYIKGGKIGLFGG 169
Cdd:PRK08972 92 GEQSGLPVGMSLLGRVIDGVGNPLD-GLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 170 AGVGKTVLIQeMITRvarnfgGTS----VFAGVGERTREGNDLWVEMEESGVLKDTALVFGQMDEPPGTRLRVALSALTM 245
Cdd:PRK08972 171 SGVGKSVLLG-MMTR------GTTadviVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCETATTI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 246 AEYFRDvQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITSTKGH--SITSMQAVYVPADDY 323
Cdd:PRK08972 244 AEYFRD-QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGqgSITAFYTVLTEGDDL 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2577762856 324 TDPAPAATFAHLDATTELSREIASRGLYPAVDPLTSTSRILdPQYIGKEHYDVAIRVKQILQKNKELQDIIAI 396
Cdd:PRK08972 323 QDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLISI 394
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
83-398 |
4.16e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 171.72 E-value: 4.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 83 GAAVFDTGaPISVPVGDGVKGHIFNVLGQPLDVAESEIQYTERWPIHRKPPSFDQLEGSTEMLETGIKVIDLLTPYIKGG 162
Cdd:PRK06002 88 GDAVFRKG-PLRIRPDPSWKGRVINALGEPIDGLGPLAPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQ 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 163 KIGLFGGAGVGKTVLIQeMITRvARNFGgTSVFAGVGERTREGNDLwveMEES--GVLKDTALVFGQMDEPPGTRLRVAL 240
Cdd:PRK06002 167 RIGIFAGSGVGKSTLLA-MLAR-ADAFD-TVVIALVGERGREVREF---LEDTlaDNLKKAVAVVATSDESPMMRRLAPL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 241 SALTMAEYFRDvQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERI-TSTKGH-SITSMQAVYV 318
Cdd:PRK06002 241 TATAIAEYFRD-RGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgPGAEGGgSITGIFSVLV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 319 PADDYTDPAPAATFAHLDATTELSREIASRGLYPAVDPLTSTSRILDPQYIGkEHYDVAIRVKQILQKNKELQDIIAILG 398
Cdd:PRK06002 320 DGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTP-EQRKLVSRLKSMIARFEETRDLRLIGG 398
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
8-424 |
2.31e-47 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 169.55 E-value: 2.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 8 QGARTAAATGRIARVIGPVVDVEFPADAIPGIYHALTAEITLNGETHTVTFEVSQHLgdnlvrAISLQATDGLVRGAAVF 87
Cdd:PRK06936 16 VGSRLIQIRGRVTQVTGTILKAVVPGVRIGELCYLRNPDNSLSLQAEVIGFAQHQAL------LTPLGEMYGISSNTEVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 88 DTGAPISVPVGDGVKGHIFNVLGQPLDVAESeIQYTERWPIHRKPPSFDQLEGSTEMLETGIKVIDLLTPYIKGGKIGLF 167
Cdd:PRK06936 90 PTGTMHQVGVGEHLLGRVLDGLGQPFDGGHP-PEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 168 GGAGVGKTVLIQeMITRVARnfGGTSVFAGVGERTREGND-LWVEMEESGvLKDTALVFGQMDEPPGTRLRVALSALTMA 246
Cdd:PRK06936 169 AAAGGGKSTLLA-SLIRSAE--VDVTVLALIGERGREVREfIESDLGEEG-LRKAVLVVATSDRPSMERAKAGFVATSIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 247 EYFRDvQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITSTKGHSITSMQAVYVPADDYTDP 326
Cdd:PRK06936 245 EYFRD-QGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 327 APAATFAHLDATTELSREIASRGLYPAVDPLTSTSRILDpQYIGKEHYDVAIRVKQILQKNKELQDIIAI----LGVDEL 402
Cdd:PRK06936 324 VADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDKE 402
|
410 420
....*....|....*....|..
gi 2577762856 403 SEEdkiVVSRARRIQQFLSQNT 424
Cdd:PRK06936 403 ADQ---AIERIGAIRGFLRQGT 421
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
3-424 |
2.75e-47 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 169.56 E-value: 2.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 3 ATATEQGARTAAA---TGRIARVIGPVVDVEFPADAIPGIYHALTAEITLNGETHTVTFEvsqhlgdnlvRAISLQA--- 76
Cdd:PRK09099 9 ADALERELAALPAvrrTGKVVEVIGTLLRVSGLDVTLGELCELRQRDGTLLQRAEVVGFS----------RDVALLSpfg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 77 -TDGLVRGAAVFDTGAPISVPVGDGVKGHIFNVLGQPLDvAESEIQYTERWPIHRKPPSFDQLEGSTEMLETGIKVIDLL 155
Cdd:PRK09099 79 eLGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPID-GGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 156 TPYIKGGKIGLFGGAGVGKTVLIQeMITRVARnfGGTSVFAGVGERTREGNDlWVE--MEESGVLKdTALVFGQMDEPPG 233
Cdd:PRK09099 158 MTLGEGQRMGIFAPAGVGKSTLMG-MFARGTQ--CDVNVIALIGERGREVRE-FIEliLGEDGMAR-SVVVCATSDRSSI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 234 TRLRVALSALTMAEYFRDvQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITSTKGHSITSM 313
Cdd:PRK09099 233 ERAKAAYVATAIAEYFRD-RGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 314 QAVYVPADDYTDPAPAATFAHLDATTELSREIASRGLYPAVDPLTSTSRILdPQYIGKEHYDVAIRVKQILQKNKELQDI 393
Cdd:PRK09099 312 YTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETL 390
|
410 420 430
....*....|....*....|....*....|....*
gi 2577762856 394 IAI----LGVDELSEEdkiVVSRARRIQQFLSQNT 424
Cdd:PRK09099 391 LQVgeyrAGSDPVADE---AIAKIDAIRDFLSQRT 422
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
17-430 |
2.96e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 169.13 E-value: 2.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 17 GRIARVIGPVVDVEFPADAIPGIYHALTAEitlnGETHTVTFEVsqhLG--DNLVRAISLQATDGLVRGAAVFDTGAPIS 94
Cdd:PRK07721 20 GKVSRVIGLMIESKGPESSIGDVCYIHTKG----GGDKAIKAEV---VGfkDEHVLLMPYTEVAEIAPGCLVEATGKPLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 95 VPVGDGVKGHIFNVLGQPLDVAESEiQYTERWPIHRKPPSFDQLEGSTEMLETGIKVIDLLTPYIKGGKIGLFGGAGVGK 174
Cdd:PRK07721 93 VKVGSGLIGQVLDALGEPLDGSALP-KGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 175 TVLIQeMItrvARNFGG-TSVFAGVGERTREGNDlWVEME--ESGvLKDTALVFGQMDEPPGTRLRVALSALTMAEYFRD 251
Cdd:PRK07721 172 STLMG-MI---ARNTSAdLNVIALIGERGREVRE-FIERDlgPEG-LKRSIVVVATSDQPALMRIKGAYTATAIAEYFRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 252 vQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERiTSTKGH-SITSMQAVYVPADDYTDPAPAA 330
Cdd:PRK07721 246 -QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLER-TGTNASgSITAFYTVLVDGDDMNEPIADT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 331 TFAHLDATTELSREIASRGLYPAVDPLTSTSRILdPQYIGKEHYDVAIRVKQILQKNKELQDIIAILGVDE-LSEEDKIV 409
Cdd:PRK07721 324 VRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINIGAYKRgSSREIDEA 402
|
410 420
....*....|....*....|.
gi 2577762856 410 VSRARRIQQFLSQNTYTAKQF 430
Cdd:PRK07721 403 IQFYPQIISFLKQGTDEKATF 423
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
77-423 |
1.91e-46 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 167.30 E-value: 1.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 77 TDGLVRGAAVFDTGAPISVPVGDGVKGHIFNVLGQPLDvaESEIQYTERWPIHRKPPSFDQLEGSTEMLETGIKVIDLLT 156
Cdd:PRK06820 81 SDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPID--GGPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGIL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 157 PYIKGGKIGLFGGAGVGKTVLIQeMITrvARNFGGTSVFAGVGERTREGNDLWVEMEESGVLKDTALVFGQMDEPPGTRL 236
Cdd:PRK06820 159 SCGEGQRIGIFAAAGVGKSTLLG-MLC--ADSAADVMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 237 RVALSALTMAEYFRDvQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITSTKGHSITSMQAV 316
Cdd:PRK06820 236 KGLSTATTIAEYFRD-RGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYTV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 317 YVPADDYTDPAPAATFAHLDATTELSREIASRGLYPAVDPLTSTSRILdPQYIGKEHYDVAIRVKQILQKNKELQDIIAI 396
Cdd:PRK06820 315 LVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQEIELLVRV 393
|
330 340 350
....*....|....*....|....*....|.
gi 2577762856 397 ----LGVDELSEEdkiVVSRARRIQQFLSQN 423
Cdd:PRK06820 394 geyqAGEDLQADE---ALQRYPAICAFLQQD 421
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
74-422 |
1.50e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 159.51 E-value: 1.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 74 LQATDGLVRGAAVFDTGAPISVPVGDGVKGHIFNVLGQPLD-----VAESEIQYTERW--PIHRKPPSfdqlegstEMLE 146
Cdd:PRK05688 82 VGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDgkgpmKAEDWVPMDGPTinPLNRHPIS--------EPLD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 147 TGIKVIDLLTPYIKGGKIGLFGGAGVGKTVLIQeMITRVARnfGGTSVFAGVGERTREGNDLWVEMEESGVLKDTALVFG 226
Cdd:PRK05688 154 VGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLG-MMTRFTE--ADIIVVGLIGERGREVKEFIEHILGEEGLKRSVVVAS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 227 QMDEPPGTRLRVALSALTMAEYFRDvQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITSTK 306
Cdd:PRK05688 231 PADDAPLMRLRAAMYCTRIAEYFRD-KGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 307 --GHSITSMQAVYVPADDYTDPAPAATFAHLDATTELSREIASRGLYPAVDPLTSTSRILdPQYIGKEHYDVAIRVKQIL 384
Cdd:PRK05688 310 pgGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLW 388
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2577762856 385 QKNKELQDIIAI----LGVDelsEEDKIVVSRARRIQQFLSQ 422
Cdd:PRK05688 389 SRYQQSRDLISVgayvAGGD---PETDLAIARFPHLVQFLRQ 427
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
46-422 |
1.08e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 156.68 E-value: 1.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 46 EITLNGETHTVTFEVSQHLGDNLVraISLQATDGLVRGAAVFDTGAPISVPVGDGVKGHIFNVLGQPLDvAESEIQYTER 125
Cdd:PRK06793 44 DVCFVGEHNVLCEVIAIEKENNML--LPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLN-EEAENIPLQK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 126 WPIHRKPPSFDQLEGSTEMLETGIKVIDLLTPYIKGGKIGLFGGAGVGKTVLIQeMITRVARnfGGTSVFAGVGERTREG 205
Cdd:PRK06793 121 IKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLG-MIAKNAK--ADINVISLVGERGREV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 206 ND-LWVEMEESGvLKDTALVFGQMDEPPGTRLRVALSALTMAEYFRDvQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPsa 284
Cdd:PRK06793 198 KDfIRKELGEEG-MRKSVVVVATSDESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVKELP-- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 285 VGYQPNLADE-MGLLQERITSTKGHSITSMQAVYVPADDYTDPAPAATFAHLDATTELSREIASRGLYPAVDPLTSTSRI 363
Cdd:PRK06793 274 IGGKTLLMESyMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRI 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2577762856 364 LDpQYIGKEHYDVAIRVKQILQKNKELQDIIAILGVDELSEEDKIVVSRARR--IQQFLSQ 422
Cdd:PRK06793 354 ME-EIVSPNHWQLANEMRKILSIYKENELYFKLGTIQENAENAYIFECKNKVegINTFLKQ 413
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
79-423 |
1.69e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 150.81 E-value: 1.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 79 GLVRGAAVFDTGAPISVPVGDGVKGHIFNVLGQPLDvaeSEIQYTERWPIHRKPPSFDQLEGST--EMLETGIKVIDLLT 156
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLD---GKGQLGGSTPLQQQLPQIHPLQRRAvdTPLDVGVNAINGLL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 157 PYIKGGKIGLFGGAGVGKTVLIQeMITRVARnfGGTSVFAGVGERTREGNDlWVE--MEESGVLKdTALVFGQMDEPPGT 234
Cdd:PRK07196 151 TIGKGQRVGLMAGSGVGKSVLLG-MITRYTQ--ADVVVVGLIGERGREVKE-FIEhsLQAAGMAK-SVVVAAPADESPLM 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 235 RLRVALSALTMAEYFRDvQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQEriTSTKGHSITSMQ 314
Cdd:PRK07196 226 RIKATELCHAIATYYRD-KGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAE--SAGNSSGNGTMT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 315 AVYV---PADDYTDPAPAATFAHLDATTELSREIASRGLYPAVDPLTSTSRILDpQYIGKEHYDVAIRVKQILQKNKELQ 391
Cdd:PRK07196 303 AIYTvlaEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMAIK 381
|
330 340 350
....*....|....*....|....*....|....*.
gi 2577762856 392 DIIA----ILGVDELSEEdkiVVSRARRIQQFLSQN 423
Cdd:PRK07196 382 PLIPlggyVAGADPMADQ---AVHYYPAITQFLRQE 414
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
17-396 |
2.22e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 147.82 E-value: 2.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 17 GRIARVIGPVVDVEFPADAIpgiyhALTAEITL-NGETHTVTFEVSQHLGDNLVrAISLQATDGLVRGAAVFDTGAPISV 95
Cdd:PRK08927 19 GRVVAVRGLLVEVAGPIHAL-----SVGARIVVeTRGGRPVPCEVVGFRGDRAL-LMPFGPLEGVRRGCRAVIANAAAAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 96 PVGDGVKGHIFNVLGQPLDVAESEIQYTERWPIHRKPPSFDQLEGSTEMLETGIKVIDLLTPYIKGGKIGLFGGAGVGKT 175
Cdd:PRK08927 93 RPSRAWLGRVVNALGEPIDGKGPLPQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 176 VLiqemITRVARNFGG-TSVFAGVGERTRE-----GNDLWVEmeesGvLKDTALVFGQMDEPPGTRLRVALSALTMAEYF 249
Cdd:PRK08927 173 VL----LSMLARNADAdVSVIGLIGERGREvqeflQDDLGPE----G-LARSVVVVATSDEPALMRRQAAYLTLAIAEYF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 250 RDvQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERI---TSTKGhSITSMQAVYVPADDYTDP 326
Cdd:PRK08927 244 RD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpgPIGEG-TITGLFTVLVDGDDHNEP 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 327 APAATFAHLDATTELSREIASRGLYPAVDPLTSTSRILdPQYIGKEHYDVAIRVKQILQKNKELQDIIAI 396
Cdd:PRK08927 322 VADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
76-405 |
5.30e-34 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 132.77 E-value: 5.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 76 ATDGLVRGAAVFDTGAPISVPVGDGVKGHIFNVLGQPLDVAE-SEIQYTErwpIHRKPPSFDQLEGSTEMLETGIKVIDL 154
Cdd:PRK07594 72 STIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRElPDVCWKD---YDAMPPPAMVRQPITQPLMTGIRAIDS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 155 LTPYIKGGKIGLFGGAGVGKTVLIQeMITRVARnfGGTSVFAGVGERTREGNDLWVEMEESGVLKDTALVFGQMDEPPGT 234
Cdd:PRK07594 149 VATCGEGQRVGIFSAPGVGKSTLLA-MLCNAPD--ADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 235 RLRVALSALTMAEYFRDvQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITSTKGHSITSMQ 314
Cdd:PRK07594 226 RVRALFVATTIAEFFRD-NGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFY 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 315 AVYVPADDYTDPAPAATFAHLDATTELSREIASRGLYPAVDPLTSTSRILdPQYIGKEHYDVAIRVKQILQKNKELQDII 394
Cdd:PRK07594 305 TVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEVELLI 383
|
330
....*....|....*
gi 2577762856 395 AI----LGVDELSEE 405
Cdd:PRK07594 384 RIgeyqRGVDTDTDK 398
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
17-390 |
1.50e-33 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 131.83 E-value: 1.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 17 GRIARVIGPVVD---VEFPADAIPGIyhaltaEITLNGETHTVTFEVSQHLGDNLVrAISLQATDGLVRGAAVF------ 87
Cdd:PRK07960 29 GRLTRATGLVLEatgLQLPLGATCVI------ERQNGSETHEVESEVVGFNGQRLF-LMPLEEVEGILPGARVYarnisg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 88 -DTGAPISVPVGDGVKGHIFNVLGQPLD-VAESEIQYteRWPIHRKPPSFDQLEGSTEMLETGIKVIDLLTPYIKGGKIG 165
Cdd:PRK07960 102 eGLQSGKQLPLGPALLGRVLDGSGKPLDgLPAPDTGE--TGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 166 LFGGAGVGKTVLIQEMitrvARNFGGTSVFAG-VGERTREGNDLWVEMEESGVLKDTALVFGQMDEPPGTRLRVALSALT 244
Cdd:PRK07960 180 LFAGSGVGKSVLLGMM----ARYTQADVIVVGlIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 245 MAEYFRDvQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITS--TKGHSITSMQAVYVPADD 322
Cdd:PRK07960 256 IAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDD 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2577762856 323 YTDPAPAATFAHLDATTELSREIASRGLYPAVDPLTSTSRILdPQYIGKEHYDVAIRVKQIL---QKNKEL 390
Cdd:PRK07960 335 QQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAM-TALIDEQHYARVRQFKQLLssfQRNRDL 404
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
19-426 |
4.81e-33 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 130.72 E-value: 4.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 19 IARVIGPVVDVEfpadAIPGIYHALTAEITL-NGETHTVtfEVSQHLGDNLVRAIsLQATDGL-VRGAAVFDTGAPISVP 96
Cdd:PRK04196 7 VSEIKGPLLFVE----GVEGVAYGEIVEIELpNGEKRRG--QVLEVSEDKAVVQV-FEGTTGLdLKDTKVRFTGEPLKLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 97 VGDGVKGHIFNVLGQPLD-----VAEseiqytERWPIH--------RKPPSfdqlegstEMLETGIKVIDLLTPYIKGGK 163
Cdd:PRK04196 80 VSEDMLGRIFDGLGRPIDggpeiIPE------KRLDINgapinpvaREYPE--------EFIQTGISAIDGLNTLVRGQK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 164 IGLFGGAGVgKTVLIQEMITRVARNFGGTS----VFAGVGERTREGNDLWVEMEESGVLKDTALVFGQMDEPPGTRLRVA 239
Cdd:PRK04196 146 LPIFSGSGL-PHNELAAQIARQAKVLGEEEnfavVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 240 LSALTMAEYFRDVQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQER---ITSTKGhSITSMQAV 316
Cdd:PRK04196 225 RMALTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagrIKGKKG-SITQIPIL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 317 YVPADDYTDPAPaatfahlDAT---TE----LSREIASRGLYPAVDPLTSTSRILDpQYIGK-----EHYDVAIRVKQIL 384
Cdd:PRK04196 304 TMPDDDITHPIP-------DLTgyiTEgqivLSRELHRKGIYPPIDVLPSLSRLMK-DGIGEgktreDHKDVANQLYAAY 375
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2577762856 385 QKNKELQDIIAILGVDELSEEDKIVVSRARRI-QQFLSQNTYT 426
Cdd:PRK04196 376 ARGKDLRELAAIVGEEALSERDRKYLKFADAFeREFVNQGFDE 418
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
92-365 |
1.87e-31 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 122.33 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 92 PISVPVGDGVKGHIFNVLGQPLD-----VAES--EIQYTERWPIHRKPPSfdqlegstEMLETGIKVIDLLTPYIKGGKI 164
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDggppiLPEDylDINGPPINPVARIYPE--------EMIQTGISAIDVMNTLVRGQKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 165 GLFGGAGV-GKTVLIQemITRVARNFGGTS----VFAGVGERTREGNDLWVEMEESGVLKDTALVFGQMDEPPGTRLRVA 239
Cdd:cd01135 73 PIFSGSGLpHNELAAQ--IARQAGVVGSEEnfaiVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 240 LSALTMAEYFRDVQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITSTKGH--SITSMQAVY 317
Cdd:cd01135 151 RMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRkgSITQIPILT 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2577762856 318 VPADDYTDPAPaatfahlDAT---TE----LSREIASRGLYPAVDPLTSTSRILD 365
Cdd:cd01135 231 MPNDDITHPIP-------DLTgyiTEgqiyLDRDLHNKGIYPPIDVLPSLSRLMK 278
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
15-93 |
3.73e-31 |
|
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: 114.92 E-value: 3.73e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2577762856 15 ATGRIARVIGPVVDVEFPADAIPGIYHALTAEitlNGETHTVTFEVSQHLGDNLVRAISLQATDGLVRGAAVFDTGAPI 93
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFPEGELPPIYNALEVK---GDDGKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
92-362 |
2.14e-30 |
|
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: 119.60 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 92 PISVPVGDGVKGHIFNVLGQPLDV-AESE---I---QYTERWPIHRKPPSFDQLEGSTEMLeTGIKVIDLLTPYIKGGKI 164
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEViAETGsifIprgVNVQRWPVRQPRPVKEKLPPNVPLL-TGQRVLDTLFPVAKGGTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 165 GLFGGAGVGKTVLIQEmitrVARNfgGTS---VFAGVGERtreGND----------LWVEMEESGVLKDTALVFGQMDEP 231
Cdd:cd01134 80 AIPGPFGCGKTVISQS----LSKW--SNSdvvIYVGCGER---GNEmaevleefpeLKDPITGESLMERTVLIANTSNMP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 232 PGTRLRVALSALTMAEYFRDvQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQER--ITSTKGH- 308
Cdd:cd01134 151 VAAREASIYTGITIAEYFRD-MGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERagRVRCLGSp 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2577762856 309 ----SITSMQAVYVPADDYTDPAPAATFAHLDATTELSREIASRGLYPAVDPLTSTSR 362
Cdd:cd01134 230 gregSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
14-430 |
4.39e-30 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 123.35 E-value: 4.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 14 AATGRIARVIGPVVDVEFPADAipGIY-------HALTAEIT-LNGETHTV-TFEvsqhlgdnlvraislqATDGLVRGA 84
Cdd:PRK04192 2 MTKGKIVRVSGPLVVAEGMGGA--RMYevvrvgeEGLIGEIIrIEGDKATIqVYE----------------ETSGIKPGE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 85 AVFDTGAPISVPVGDGVKGHIFNVLGQPLDV------------------------------------------------- 115
Cdd:PRK04192 64 PVEFTGEPLSVELGPGLLGSIFDGIQRPLDElaeksgdflergvyvpaldrekkweftptvkvgdkveagdilgtvqetp 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 116 ---------------------------------------AESEIQYTERWPIhRKPPSFDQLEGSTEMLETGIKVIDLLT 156
Cdd:PRK04192 144 siehkimvppgvsgtvkeivsegdytvddtiavlededgEGVELTMMQKWPV-RRPRPYKEKLPPVEPLITGQRVIDTFF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 157 PYIKGGKIGLFGGAGVGKTVLIQEmitrVARNfggtS-----VFAGVGERtreGNdlwvEMEEsgVLKDtalvFGQMDEP 231
Cdd:PRK04192 223 PVAKGGTAAIPGPFGSGKTVTQHQ----LAKW----AdadivIYVGCGER---GN----EMTE--VLEE----FPELIDP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 232 -PGTRL--R-----------VA------LSALTMAEYFRDvQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNL 291
Cdd:PRK04192 282 kTGRPLmeRtvliantsnmpVAareasiYTGITIAEYYRD-MGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 292 ADEMGLLQER--ITSTKGH---SITSMQAVYVPADDYTDPAPAATFAHLDATTELSREIASRGLYPAVDPLTSTSR---I 363
Cdd:PRK04192 361 ASRLAEFYERagRVKTLGGeegSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYSLyldQ 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2577762856 364 LDPQY---IGKEHYDVAIRVKQILQKNKELQDIIAILGVDELSEEDKIVVSRARRIQQ-FLSQN------TYT--AKQF 430
Cdd:PRK04192 441 VAPWWeenVDPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARLIREdFLQQNafdpvdTYCppEKQY 519
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
72-422 |
4.08e-28 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 116.16 E-value: 4.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 72 ISLQATDGLVRGAAVFDTGAPISVPVGDGVKGHIFNVLGQPLDVAESeIQYTERWPIHRKPPSFDQLEGSTEMLETGIKV 151
Cdd:PRK05922 69 MSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQ-LPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 152 IDLLTPYIKGGKIGLFGGAGVGKTVLiqemITRVARNFGGT-SVFAGVGERTREGNDlWVEMEESGVLKD-TALVFGQMD 229
Cdd:PRK05922 148 IDAFLTLGKGQRIGVFSEPGSGKSSL----LSTIAKGSKSTiNVIALIGERGREVRE-YIEQHKEGLAAQrTIIIASPAH 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 230 EPPGTRLRVALSALTMAEYFRDvQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITSTKGHS 309
Cdd:PRK05922 223 ETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGS 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 310 ITSMQAV-YVP--ADDYTDPAPAATFAHLDATTElSREIASrglyPAVDPLTSTSRILDpQYIGKEHYDVAIRVKQILQK 386
Cdd:PRK05922 302 ITALYAIlHYPnhPDIFTDYLKSLLDGHFFLTPQ-GKALAS----PPIDILTSLSRSAR-QLALPHHYAAAEELRSLLKA 375
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2577762856 387 NKELQDIIAI----LGVD-ELSEEDKIVVSrarrIQQFLSQ 422
Cdd:PRK05922 376 YHEALDIIQLgayvPGQDaHLDRAVKLLPS----IKQFLSQ 412
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
60-363 |
1.88e-27 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 115.01 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 60 VSQHLGDNLVRAISLQATDGLVRGAAVFDTGAPISVPVGDGVKGHIFNVLGQPLDvAESEIQYTERWPIHRKPPSFDQLE 139
Cdd:PRK13343 62 FAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLD-GGGPLQATARRPLERPAPAIIERD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 140 GSTEMLETGIKVIDLLTPYIKGGKIGLFGGAGVGKTVL-IQEMITRvaRNFGGTSVFAGVGERTREGNDLWVEMEESGVL 218
Cdd:PRK13343 141 FVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIaIDAIINQ--KDSDVICVYVAIGQKASAVARVIETLREHGAL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 219 KDTALVFGQMDEPPGTRLRVALSALTMAEYFRDvQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYqPnlADEMGL- 297
Cdd:PRK13343 219 EYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAY-P--GDIFYLh 294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2577762856 298 --LQERIT----STKGHSITSMQAVYVPADDYTDPAPAATFAHLDATTELSREIASRGLYPAVDPLTSTSRI 363
Cdd:PRK13343 295 srLLERAAklspELGGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRV 366
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
89-425 |
2.18e-20 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 93.63 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 89 TGAPISVPVGDGVKGHIFNVLGQPLD-----VAES--EIQYTERWPIHRKPPSfdqlegstEMLETGIKVIDLLTPYIKG 161
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDkgppvLAEDylDINGQPINPYARIYPE--------EMIQTGISAIDVMNSIARG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 162 GKIGLFGGAGVGKTVlIQEMITRVA---------------RNFggTSVFAGVGERTREGNDLWVEMEESGVLKDTALVFG 226
Cdd:TIGR01040 142 QKIPIFSAAGLPHNE-IAAQICRQAglvklptkdvhdgheDNF--AIVFAAMGVNMETARFFKQDFEENGSMERVCLFLN 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 227 QMDEPPGTRLRVALSALTMAEYFRDVQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERITSTK 306
Cdd:TIGR01040 219 LANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVE 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 307 GH--SITSMQAVYVPADDYTDPAPAATFAHLDATTELSREIASRGLYPAVDPLTSTSRILDPQyIG-----KEHYDVAIR 379
Cdd:TIGR01040 299 GRngSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSA-IGegmtrKDHSDVSNQ 377
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2577762856 380 VKQILQKNKELQDIIAILGVDELSEEDKIVVSRARRIQQ-FLSQNTY 425
Cdd:TIGR01040 378 LYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQGPY 424
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
194-425 |
3.45e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 94.32 E-value: 3.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 194 VFAGVGERTREGNDLwveMEESGVLKD----------TALVFGQMDEPPGTRLRVALSALTMAEYFRDVqNQDVLLFIDN 263
Cdd:PRK14698 686 IYIGCGERGNEMTDV---LEEFPKLKDpktgkplmerTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYDVALMADS 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 264 IFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERI-------TSTKGHSITSMQAVYVPADDYTDPAPAATFAHLD 336
Cdd:PRK14698 762 TSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVK 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 337 ATTELSREIASRGLYPAVDPLTSTSRILDP------QYIGKEHYDVAIRVKQILQKNKELQDIIAILGVDELSEEDKIVV 410
Cdd:PRK14698 842 VFWALDADLARRRHFPAINWLTSYSLYVDAvkdwwhKNVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAIL 921
|
250
....*....|....*.
gi 2577762856 411 SRARRIQQ-FLSQNTY 425
Cdd:PRK14698 922 LVARMLREdYLQQDAF 937
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
93-363 |
7.02e-19 |
|
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: 86.46 E-value: 7.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 93 ISVPVGDGVKGHIFNVLGQPLDvAESEIQYTERWPIHRKPPSFDQLEGSTEMLETGIKVIDLLTPYIKGGKIGLFGGAGV 172
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPID-GKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 173 GKT-VLIQEMITRVARNFggTSVFAGVGERTREGNDLWVEMEESGVLKDTALVFGQMDEPPGTRLRVALSALTMAEYFRD 251
Cdd:cd01132 81 GKTaIAIDTIINQKGKKV--YCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 252 vQNQDVLLFIDNIFRFTQAGSEVSTLLGR------MPSAVGY--------QPNLADEMGllqeritstkGHSITSMQAVY 317
Cdd:cd01132 159 -NGKHALIIYDDLSKQAVAYRQMSLLLRRppgreaYPGDVFYlhsrllerAAKLSDELG----------GGSLTALPIIE 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2577762856 318 VPADDYTDPAPAATFAHLDATTELSREIASRGLYPAVDPLTSTSRI 363
Cdd:cd01132 228 TQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRV 273
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
72-331 |
3.58e-16 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 80.46 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 72 ISLQ---ATDGLVRGAAVFDTGAPISVPVGDGVKGHIFNVLGQPLDVA------ESEIQYTERWPIHRKPPSfdqlegst 142
Cdd:PRK02118 50 VTLQvfgGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGpelegePIEIGGPSVNPVKRIVPR-------- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 143 EMLETGIKVIDLLTPYIKGGKIGLFGGAGVGktvlIQEMITRVA-RNFGGTSVFAGVGERTREGNDLWVEMEESGVLKDT 221
Cdd:PRK02118 122 EMIRTGIPMIDVFNTLVESQKIPIFSVSGEP----YNALLARIAlQAEADIIILGGMGLTFDDYLFFKDTFENAGALDRT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 222 ALVFGQMDEPPGTRLRVALSALTMAEYFRDVQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQER 301
Cdd:PRK02118 198 VMFIHTASDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEK 277
|
250 260 270
....*....|....*....|....*....|.
gi 2577762856 302 ITSTK-GHSITSMQAVYVPADDYTDPAPAAT 331
Cdd:PRK02118 278 AVDFEdGGSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
19-90 |
1.38e-15 |
|
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: 71.04 E-value: 1.38e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2577762856 19 IARVIGPVVDVEFPADAIPGIYHALTAEITlngETHTVTFEVSQHLGDNLVRAISLQATDGLVRGAAVFDTG 90
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVELV---EFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
373-432 |
1.83e-14 |
|
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: 68.24 E-value: 1.83e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 373 HYDVAIRVKQILQKNKELQDIIAILGVDELSEEDKIVVSRARRIQQFLSQNTYTAKQFTG 432
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIED 60
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
2-282 |
2.36e-13 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 72.02 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 2 TATATEQGARTAAATGrIARVIG-PVVD----VEFPAdaipGIYhaltaEITLNGETHTVtfevsqhlGdnlvrAISLQA 76
Cdd:PRK09281 22 EAEVEEVGTVISVGDG-IARVYGlDNVMagelLEFPG----GVY-----GIALNLEEDNV--------G-----AVILGD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 77 TDGLVRGAAVFDTGAPISVPVGDGVKGHIFNVLGQPLDvAESEIQYTERWPIHRKPPSFDQLEGSTEMLETGIKVIDLLT 156
Cdd:PRK09281 79 YEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPID-GKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 157 PyikggkIG------LFGGAGVGKT-VLIQEMItrvarNFGGTSVF-------------AGVgertregndlwVEM-EES 215
Cdd:PRK09281 158 P------IGrgqrelIIGDRQTGKTaIAIDTII-----NQKGKDVIciyvaigqkastvAQV-----------VRKlEEH 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2577762856 216 GVLKDTALVFGQMDEPPGTRLRVALSALTMAEYFRDvQNQDVLLFIDNIFRFTQAGSEVSTLLGRMP 282
Cdd:PRK09281 216 GAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQLSLLLRRPP 281
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
2-363 |
1.35e-10 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 63.52 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 2 TATATEQGARTAAATGRIARVIGPVVDVeFPADAIPGIYHALTAEITLNGETHT--VTFEVSQhlgDNLVRAISLQATDG 79
Cdd:PTZ00185 26 AAPGQKSFFKATEMIGYVHSIDGTIATL-IPAPGNPGVAYNTIIMIQVSPTTFAagLVFNLEK---DGRIGIILMDNITE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 80 LVRGAAVFDTGAPISVPVGDGVKGHIFNVLGQPLDVA---------ESEIQYTErwpIHRKPPSFDQLEGSTEMLETGIK 150
Cdd:PTZ00185 102 VQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPVGlltrsrallESEQTLGK---VDAGAPNIVSRSPVNYNLLTGFK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 151 VIDLLTPYIKGGKIGLFGGAGVGKT-VLIQEMITRVARN------FGGTSVFAGVGERTREGNDLWVEMEESGVLKDTAL 223
Cdd:PTZ00185 179 AVDTMIPIGRGQRELIVGDRQTGKTsIAVSTIINQVRINqqilskNAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 224 VFGQMDEPPGTRLRVALSALTMAEYFRDvQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLLQERIT 303
Cdd:PTZ00185 259 MAATAAEPAGLQYLAPYSGVTMGEYFMN-RGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAA 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2577762856 304 ----STKGHSITSMQAVYVPADDYTDPAPAATFAHLDATTELSREIASRGLYPAVDPLTSTSRI 363
Cdd:PTZ00185 338 mlspGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRV 401
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
83-282 |
1.28e-07 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 53.81 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 83 GAAVFDTGAPISVPVGDGVKGHIFNVLGQPLDvAESEIQYTERWPIHRKPPSFDQLEGSTEMLETGIKVIDLLTPYIKGG 162
Cdd:CHL00059 64 GSSVKATGKIAQIPVSEAYLGRVVNALAKPID-GKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 163 KIGLFGGAGVGKT-VLIQEMITRVARNfgGTSVFAGVGERTREGNDLWVEMEESGVLKDTALVFGQMDEPPGTRLRVALS 241
Cdd:CHL00059 143 RELIIGDRQTGKTaVATDTILNQKGQN--VICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYT 220
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2577762856 242 ALTMAEYFRdVQNQDVLLFIDNIFRFTQAGSEVSTLLGRMP 282
Cdd:CHL00059 221 GAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPP 260
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
119-214 |
6.89e-07 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 51.95 E-value: 6.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 119 EIQYTERWPIHRKPPSFDQLEGSTEMLeTGIKVIDLLTPYIKGGKIGLFGGAGVGKTVLIQEMItrVARNFGGTSV---- 194
Cdd:PRK14698 186 ELKMYQRWPVRVKRPYKEKLPPEVPLI-TGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDGDTLI--LTKEFGLIKIkdly 262
|
90 100
....*....|....*....|..
gi 2577762856 195 --FAGVGERTREGNDLWVEMEE 214
Cdd:PRK14698 263 eiLDGKGKKTVEGNEEWTELEE 284
|
|
| 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 ... |
379-430 |
1.15e-06 |
|
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: 47.00 E-value: 1.15e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2577762856 379 RVKQILQKNKELQDIIAILGVDELSEEDKIVVSRARRIQQ-FLSQN------TYT--AKQF 430
Cdd:cd18111 7 EAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIREdFLQQNafdevdTYCplEKQY 67
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
104-283 |
1.26e-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: 47.37 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 104 HIFNVLGQPLDVAESEIQYTERWPIHrkPPSFDQLEGSTEMLETgiKVIDLLTPYIKGGKIGLFGGAGVGKTVLIQEMIT 183
Cdd:TIGR00767 115 KVESVNGDDPEKAKNRVLFENLTPLY--PNERLRLETSTEDLST--RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQ 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 184 RVARNFggTSVFAGV---GERTREGNDlwveMEESgvlKDTALVFGQMDEPPGTRLRVALSALTMAEyfRDVQN-QDVLL 259
Cdd:TIGR00767 191 AITRNH--PEVELIVlliDERPEEVTD----MQRS---VKGEVVASTFDEPASRHVQVAEMVIEKAK--RLVEHkKDVVI 259
|
170 180
....*....|....*....|....
gi 2577762856 260 FIDNIFRFTQAGSEVSTLLGRMPS 283
Cdd:TIGR00767 260 LLDSITRLARAYNTVTPASGKVLS 283
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
160-273 |
1.04e-04 |
|
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: 42.36 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 160 KGGKIGLFGGAGVGKTVLIQEMITRVARNFGGtsVFAGVGERTREGNDLWVEMEESGvlkdtalvfgqMDEPPGTRLRVA 239
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG--VIYIDGEDILEEVLDQLLLIIVG-----------GKKASGSGELRL 67
|
90 100 110
....*....|....*....|....*....|....
gi 2577762856 240 LSALTMAEYFRdvqnqDVLLFIDNIFRFTQAGSE 273
Cdd:smart00382 68 RLALALARKLK-----PDVLILDEITSLLDAEQE 96
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
143-363 |
3.77e-04 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 43.04 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 143 EMLETGIKVIDLLTPYIKGGKIGLFGGAGVGKT-VLIQEMITRvaRNFGGTSVFAGVGERTREGNDLWVEMEESGVLKDT 221
Cdd:PRK07165 125 EQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKThIALNTIINQ--KNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNT 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 222 ALvfgqMDEPPGTRLRVALS---ALTMAEYFRdvQNQDVLLFID------NIFRftqagsEVSTLLGR------MPSAVG 286
Cdd:PRK07165 203 II----IDAPSTSPYEQYLApyvAMAHAENIS--YNDDVLIVFDdltkhaNIYR------EIALLTNKpvgkeaFPGDMF 270
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2577762856 287 YQpnladEMGLLqERITSTKG-HSITSMQAVYVPADDYTDPAPAATFAHLDATTELSREIASRGLYPAVDPLTSTSRI 363
Cdd:PRK07165 271 FA-----HSKLL-ERAGKFKNrKTITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRT 342
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
150-362 |
1.45e-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: 40.27 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 150 KVIDLLTPYIKGGKIGLFGGAGVGKTVLIQEMITRVARNFGGTSVFAG-VGERTREGNDlwveMEESGvlkdTALVFGQ- 227
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRSV----KGEVVASt 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 228 MDEPPGTRLRVALSALTMAEyfRDV-QNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAvGYQPNLADEmgllQERITST- 305
Cdd:cd01128 77 FDEPPERHVQVAEMVIEKAK--RLVeHGKDVVILLDSITRLARAYNTVVPSSGKTLSG-GVDANALHK----PKRFFGAa 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2577762856 306 ----KGHSITSMQAVYVP----ADDytdpapaATFAHLDATTE----LSREIASRGLYPAVDPLTSTSR 362
Cdd:cd01128 150 rnieEGGSLTIIATALVDtgsrMDE-------VIFEEFKGTGNmelvLDRKLAEKRIFPAIDILKSGTR 211
|
|
| DEXSc_Pif1_like |
cd18037 |
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ... |
150-212 |
3.08e-03 |
|
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like helicases involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. The members of Pif1 helicase subfamily studied so far all appear to contribute to telomere maintenance. Pif1 is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350795 [Multi-domain] Cd Length: 183 Bit Score: 38.77 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2577762856 150 KVIDLLtpyIKGGKIGLFGGAGVGKTVLIQEMITRV----------------ARNFGGTSV--FAGVGeRTREGNDLWVE 211
Cdd:cd18037 4 RVLDLV---LDGKNVFFTGSAGTGKSYLLRRIIRALpsrpkrvavtastgiaACNIGGTTLhsFAGIG-LGSEPAEDLLE 79
|
.
gi 2577762856 212 M 212
Cdd:cd18037 80 R 80
|
|
| ATP-synt_V_A-type_beta_C |
cd18112 |
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 ... |
388-426 |
3.32e-03 |
|
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 349747 [Multi-domain] Cd Length: 95 Bit Score: 37.03 E-value: 3.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2577762856 388 KELQDIIAILGVDELSEEDKIVVSRARRI-QQFLSQNTYT 426
Cdd:cd18112 22 KDVRALAAIVGEEALSEEDRLYLEFADRFeREFINQGFYE 61
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
16-91 |
4.02e-03 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 36.14 E-value: 4.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2577762856 16 TGRIARVIGPVVDVEFPADaiPGIYHALTAEITLNGETHTVTFEVSQHLGDNlVRAISLQATDGLVRGAAVFDTGA 91
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGE--VAIGEVCEIERGDGNNETVLKAEVIGFRGDR-AILQLFESTRGLSRGALVEPTGR 73
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|
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