|
Name |
Accession |
Description |
Interval |
E-value |
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
11-459 |
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: 940.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 11 GKVISVRGSIVDVLFEKHLPPVYTLLRAGRESQIAIEVLTQLDAHHVRGIALTPTEGLARGMAVEDTGGPLKAPVGREIL 90
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDGELPAIHSVLRAGREGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKPTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 91 SRMFDVFGNTIDRRKPPSDIQWRSIHQTPPPLMRRSTTSEIFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIH 170
Cdd:TIGR03305 81 SRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 171 NVVKQHQGVSIFCGIGERCREGEELYRDMKDAGVLPNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDERRDVLLLIDN 250
Cdd:TIGR03305 161 NMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQDVLLLIDN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 251 IFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERISTTDAGAIMSIQAVYVPADDFTDPSAVHTFSHLSASIVLSR 330
Cdd:TIGR03305 241 IFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLSASLVLSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 331 KRASEGLYPAIDPLQSNSKMATPGIVGERHYLLAQEIRQTLAQYSELKDIISMLGLEQLSPEDRNVVARARRLERFLTQP 410
Cdd:TIGR03305 321 KRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRLERFLTQP 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2605819 411 FFTTEQFTGIKGKSISLSDALDGCERILNDEFKDYSEGDLYMIGTIDEA 459
Cdd:TIGR03305 401 FFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDEA 449
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
9-462 |
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: 872.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 9 NLGKVISVRGSIVDVLFEK-HLPPVYTLLRAGRESQ--IAIEVLTQLDAHHVRGIALTPTEGLARGMAVEDTGGPLKAPV 85
Cdd:COG0055 4 NTGKIVQVIGPVVDVEFPEgELPAIYNALEVENEGGgeLVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 86 GREILSRMFDVFGNTIDRRKPPSDIQWRSIHQTPPPLMRRSTTSEIFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLL 165
Cdd:COG0055 84 GEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 166 TEMIHNVVKQHQGVSIFCGIGERCREGEELYRDMKDAGVLPNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDERRDVL 245
Cdd:COG0055 164 MELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 246 LLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERISTTDAGAIMSIQAVYVPADDFTDPSAVHTFSHLSAS 325
Cdd:COG0055 244 LFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDAT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 326 IVLSRKRASEGLYPAIDPLQSNSKMATPGIVGERHYLLAQEIRQTLAQYSELKDIISMLGLEQLSPEDRNVVARARRLER 405
Cdd:COG0055 324 TVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARARKIQR 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2605819 406 FLTQPFFTTEQFTGIKGKSISLSDALDGCERILNDEFKDYSEGDLYMIGTIDEAMAK 462
Cdd:COG0055 404 FLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEK 460
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
9-462 |
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: 627.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 9 NLGKVISVRGSIVDVLFEK-HLPPVYTLLRA--GRESQIAIEVLTQLDAHHVRGIALTPTEGLARGMAVEDTGGPLKAPV 85
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQgELPRIYNALKVqnRAESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 86 GREILSRMFDVFGNTIDRRKP-PSDIQWrSIHQTPPPLMRRSTTSEIFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVL 164
Cdd:TIGR01039 81 GKETLGRIFNVLGEPIDEKGPiPAKERW-PIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 165 LTEMIHNVVKQHQGVSIFCGIGERCREGEELYRDMKDAGVLPNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDERRDV 244
Cdd:TIGR01039 160 IQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 245 LLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERISTTDAGAIMSIQAVYVPADDFTDPSAVHTFSHLSA 324
Cdd:TIGR01039 240 LLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 325 SIVLSRKRASEGLYPAIDPLQSNSKMATPGIVGERHYLLAQEIRQTLAQYSELKDIISMLGLEQLSPEDRNVVARARRLE 404
Cdd:TIGR01039 320 TTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQ 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2605819 405 RFLTQPFFTTEQFTGIKGKSISLSDALDGCERILNDEFKDYSEGDLYMIGTIDEAMAK 462
Cdd:TIGR01039 400 RFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEK 457
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
9-462 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 615.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 9 NLGKVISVRGSIVDVLFEK-HLPPVYTLLR------AGRESQIAIEVLTQLDAHHVRGIALTPTEGLARGMAVEDTGGPL 81
Cdd:CHL00060 15 NLGRITQIIGPVLDVAFPPgKMPNIYNALVvkgrdtAGQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 82 KAPVGREILSRMFDVFGNTIDRRKPPSDIQWRSIHQTPPPLMRRSTTSEIFETGIKAIDVLVPLERGGKAGLFGGAGVGK 161
Cdd:CHL00060 95 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 162 TVLLTEMIHNVVKQHQGVSIFCGIGERCREGEELYRDMKDAGV-----LPNT--VMVFGQMNEPPGARFRVGHTALTMAE 234
Cdd:CHL00060 175 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVineqnIAESkvALVYGQMNEPPGARMRVGLTALTMAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 235 YFRDDERRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERISTTDAGAIMSIQAVYVPADDFTDPS 314
Cdd:CHL00060 255 YFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 315 AVHTFSHLSASIVLSRKRASEGLYPAIDPLQSNSKMATPGIVGERHYLLAQEIRQTLAQYSELKDIISMLGLEQLSPEDR 394
Cdd:CHL00060 335 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDR 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2605819 395 NVVARARRLERFLTQPFFTTEQFTGIKGKSISLSDALDGCERILNDEFKDYSEGDLYMIGTIDEAMAK 462
Cdd:CHL00060 415 LTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAK 482
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
82-353 |
7.19e-161 |
|
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: 455.91 E-value: 7.19e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 82 KAPVGREILSRMFDVFGNTIDRRKPPSDIQWRSIHQTPPPLMRRSTTSEIFETGIKAIDVLVPLERGGKAGLFGGAGVGK 161
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 162 TVLLTEMIHNVVKQHQGVSIFCGIGERCREGEELYRDMKDAGV-----LPNTVMVFGQMNEPPGARFRVGHTALTMAEYF 236
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVinldgLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 237 RDDERRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERISTTDAGAIMSIQAVYVPADDFTDPSAV 316
Cdd:cd01133 161 RDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPA 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 2605819 317 HTFSHLSASIVLSRKRASEGLYPAIDPLQSNSKMATP 353
Cdd:cd01133 241 TTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
82-350 |
3.55e-101 |
|
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: 303.61 E-value: 3.55e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 82 KAPVGREILSRMFDVFGNTIDRRKPPSDIQWRSIHQTPPPLMRRSTTSEIFETGIKAIDVLVPLERGGKAGLFGGAGVGK 161
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 162 TVLLTEMIHNVVKQHQGVSIFCGIGERCREGEELYRDMKDAGVLPNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEr 241
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNG- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 242 RDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERISTTDA--GAIMSIQAVYVPADDFTDPSAVHTF 319
Cdd:cd19476 160 QHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDggGSITAIPAVSTPGDDLTDPIPDNTF 239
|
250 260 270
....*....|....*....|....*....|.
gi 2605819 320 SHLSASIVLSRKRASEGLYPAIDPLQSNSKM 350
Cdd:cd19476 240 AILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
135-348 |
2.88e-95 |
|
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: 286.17 E-value: 2.88e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 135 GIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNVVKQhqgVSIFCGIGERCREGEELYRDMKDAGVLPNTVMVFGQ 214
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASAD---VVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 215 MNEPPGARFRVGHTALTMAEYFRdDERRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERISTTDA 294
Cdd:pfam00006 78 SDEPPLARYRAPYTALTIAEYFR-DQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2605819 295 --GAIMSIQAVYVPADDFTDPSAVHTFSHLSASIVLSRKRASEGLYPAIDPLQSNS 348
Cdd:pfam00006 157 kgGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
11-410 |
7.53e-71 |
|
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: 231.07 E-value: 7.53e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 11 GKVISVRGSIVDVlfekHLPPVYT----LLRAGRESQIAIEVLtQLDAHHVRGIALTPTEGLARGMAVEDTGGPLKAPVG 86
Cdd:COG1157 21 GRVTRVVGLLIEA----VGPDASIgelcEIETADGRPVLAEVV-GFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 87 REILSRMFDVFGNTIDRRKPPSDIQWRSIHQTPPPLMRRSTTSEIFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLT 166
Cdd:COG1157 96 DGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 167 EMIHNVVKQhqgVSIFCGIGERCRE-GEELYRDMKDAGvLPNTVMVFGQMNEPPGARFRVGHTALTMAEYFRdDERRDVL 245
Cdd:COG1157 176 MIARNTEAD---VNVIALIGERGREvREFIEDDLGEEG-LARSVVVVATSDEPPLMRLRAAYTATAIAEYFR-DQGKNVL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 246 LLIDNIFRFIQAGSEVsGL-MGQMPSRLGYQPTLGTELSELEERISTTDAGAIMSIQAVYVPADDFTDPSAVHTFSHLSA 324
Cdd:COG1157 251 LLMDSLTRFAMAQREI-GLaAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAVRGILDG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 325 SIVLSRKRASEGLYPAIDPLQSNSKMAtPGIVGERHYLLAQEIRQTLAQYSELKDIISMlGLEQ--LSPE-DRnVVARAR 401
Cdd:COG1157 330 HIVLSRKLAERGHYPAIDVLASISRVM-PDIVSPEHRALARRLRRLLARYEENEDLIRI-GAYQpgSDPElDE-AIALIP 406
|
....*....
gi 2605819 402 RLERFLTQP 410
Cdd:COG1157 407 AIEAFLRQG 415
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
84-349 |
5.15e-59 |
|
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: 194.70 E-value: 5.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 84 PVGREILSRMFDVFGNTIDRRKPPSDIQWRSIHQTPPPLMRRSTTSEIFETGIKAIDVLVPLERGGKAGLFGGAGVGKTV 163
Cdd:cd01136 3 PVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 164 LLTEMIHNVVKQhqgVSIFCGIGERCREGEELYRDMKDAGVLPNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDdERRD 243
Cdd:cd01136 83 LLGMIARNTDAD---VNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRD-QGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 244 VLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERISTTDAGAIMSIQAVYVPADDFTDPSAVHTFSHLS 323
Cdd:cd01136 159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRSILD 238
|
250 260
....*....|....*....|....*.
gi 2605819 324 ASIVLSRKRASEGLYPAIDPLQSNSK 349
Cdd:cd01136 239 GHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| ATP-synt_F1_beta_C |
cd18110 |
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ... |
355-462 |
2.05e-58 |
|
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: 187.69 E-value: 2.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 355 IVGERHYLLAQEIRQTLAQYSELKDIISMLGLEQLSPEDRNVVARARRLERFLTQPFFTTEQFTGIKGKSISLSDALDGC 434
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 2605819 435 ERILNDEFKDYSEGDLYMIGTIDEAMAK 462
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
62-409 |
2.06e-55 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 190.73 E-value: 2.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 62 LTP---TEGLARGMAVEDTGGPLKAPVGREILSRMFDVFGNTIDRRKPPSDIQWRSIHQTPPPLMRRSTTSEIFETGIKA 138
Cdd:PRK06936 73 LTPlgeMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 139 IDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNVvkqHQGVSIFCGIGERCREGEE-LYRDMKDAGvLPNTVMVFGQMNE 217
Cdd:PRK06936 153 IDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSA---EVDVTVLALIGERGREVREfIESDLGEEG-LRKAVLVVATSDR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 218 PPGARFRVGHTALTMAEYFRDDERRdVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERISTTDAGAI 297
Cdd:PRK06936 229 PSMERAKAGFVATSIAEYFRDQGKR-VLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 298 MSIQAVYVPADDFTDPSAVHTFSHLSASIVLSRKRASEGLYPAIDPLQSNSKMATpGIVGERHYLLAQEIRQTLAQYSEL 377
Cdd:PRK06936 308 TALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEV 386
|
330 340 350
....*....|....*....|....*....|...
gi 2605819 378 KDIISMLGLEQLS-PEDRNVVARARRLERFLTQ 409
Cdd:PRK06936 387 ELLLQIGEYQKGQdKEADQAIERIGAIRGFLRQ 419
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
11-383 |
1.49e-52 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 183.00 E-value: 1.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 11 GKVISVRG----------SIVDVlfekhlppVYTLLRAGRESQIAIEVLTQLDAHhvrgIALTPTEGLAR---GMAVEDT 77
Cdd:PRK07721 20 GKVSRVIGlmieskgpesSIGDV--------CYIHTKGGGDKAIKAEVVGFKDEH----VLLMPYTEVAEiapGCLVEAT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 78 GGPLKAPVGREILSRMFDVFGNTIDRRKPPSDIQWRSIHQTPPPLMRRSTTSEIFETGIKAIDVLVPLERGGKAGLFGGA 157
Cdd:PRK07721 88 GKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 158 GVGKTVLLTeMIhnvVKQHQG-VSIFCGIGERCREGEE-LYRDMKDAGvLPNTVMVFGQMNEPPGARFRVGHTALTMAEY 235
Cdd:PRK07721 168 GVGKSTLMG-MI---ARNTSAdLNVIALIGERGREVREfIERDLGPEG-LKRSIVVVATSDQPALMRIKGAYTATAIAEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 236 FRdDERRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERISTTDAGAIMSIQAVYVPADDFTDPSA 315
Cdd:PRK07721 243 FR-DQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIA 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2605819 316 VHTFSHLSASIVLSRKRASEGLYPAIDPLQSNSKMaTPGIVGERHYLLAQEIRQTLAQYSELKDIISM 383
Cdd:PRK07721 322 DTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRV-MNHIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
62-378 |
1.18e-51 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 180.78 E-value: 1.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 62 LTP---TEGLARGMAVEDTGGPLKAPVGREILSRMFDVFGNTIDRrKPPSDIQWRSIHQTPPPLMRRSTTSEIFETGIKA 138
Cdd:PRK06820 75 LSPfasSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 139 IDVLVPLERGGKAGLFGGAGVGKTVLLTeMIhnVVKQHQGVSIFCGIGERCREGEELYRDMKDAGVLPNTVMVFGQMNEP 218
Cdd:PRK06820 154 IDGILSCGEGQRIGIFAAAGVGKSTLLG-ML--CADSAADVMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 219 PGARFRVGHTALTMAEYFRDdERRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERISTTDAGAIM 298
Cdd:PRK06820 231 ALERLKGLSTATTIAEYFRD-RGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSIT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 299 SIQAVYVPADDFTDPSAVHTFSHLSASIVLSRKRASEGLYPAIDPLQSNSKMaTPGIVGERHYLLAQEIRQTLAQYSELK 378
Cdd:PRK06820 310 AFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRI-MPQIVSAGQLAMAQKLRRMLACYQEIE 388
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
63-381 |
1.67e-50 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 177.45 E-value: 1.67e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 63 TPTEGLARGMAVEDTGGPLKAPVGREILSRMFDVFGNTIDRRKPPsDIQWRSIHQTPPPLMRRSTTSEIFETGIKAIDVL 142
Cdd:PRK07594 71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRELP-DVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 143 VPLERGGKAGLFGGAGVGKTVLLTeMIHNVvkQHQGVSIFCGIGERCREGEELYRDMKDAGVLPNTVMVFGQMNEPPGAR 222
Cdd:PRK07594 150 ATCGEGQRVGIFSAPGVGKSTLLA-MLCNA--PDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALER 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 223 FRVGHTALTMAEYFRDDERRdVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERISTTDAGAIMSIQA 302
Cdd:PRK07594 227 VRALFVATTIAEFFRDNGKR-VVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFYT 305
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2605819 303 VYVPADDFTDPSAVHTFSHLSASIVLSRKRASEGLYPAIDPLQSNSKMaTPGIVGERHYLLAQEIRQTLAQYSELKDII 381
Cdd:PRK07594 306 VLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRV-FPVVTSHEHRQLAAILRRCLALYQEVELLI 383
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
62-411 |
6.52e-50 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 175.57 E-value: 6.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 62 LTPTEGLARGMAVEDTGGPLKAPVGREILSRMFDVFGNTIDRRKPP----SDIQWRSIHQTPPPLMRRSTTSEIFETGIK 137
Cdd:PRK08149 61 IGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPptvgPISEERVIDVAPPSYAERRPIREPLITGVR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 138 AIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIhnvvkQHQGVSIFC-G-IGERCREGEELYRDMKDAGVLPNTVMVFGQM 215
Cdd:PRK08149 141 AIDGLLTCGVGQRMGIFASAGCGKTSLMNMLI-----EHSEADVFViGlIGERGREVTEFVESLRASSRREKCVLVYATS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 216 NEPPGARFRVGHTALTMAEYFRDdERRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERISTTDAG 295
Cdd:PRK08149 216 DFSSVDRCNAALVATTVAEYFRD-QGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAG 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 296 AIMSIQAVYVPADDFTDPSAVHTFSHLSASIVLSRKRASEGLYPAIDPLQSNSKMATPgIVGERHYLLAQEIRQTLAQYS 375
Cdd:PRK08149 295 SITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQ-VTDPKHRQLAAAFRKLLTRLE 373
|
330 340 350
....*....|....*....|....*....|....*...
gi 2605819 376 ELKDIISmLGLEQLSPEDRNVVARARR--LERFLTQPF 411
Cdd:PRK08149 374 ELQLFID-LGEYRRGENADNDRAMDKRpaLEAFLKQDV 410
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
11-439 |
1.19e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 172.86 E-value: 1.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 11 GKVISVRGSIVDVLFEKHLPPV--YTLLRAGRESQIAIEVLTQLDAHHVRgIALTPTEGLARGMAVEDTGGPLKAPVGRE 88
Cdd:PRK08927 19 GRVVAVRGLLVEVAGPIHALSVgaRIVVETRGGRPVPCEVVGFRGDRALL-MPFGPLEGVRRGCRAVIANAAAAVRPSRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 89 ILSRMFDVFGNTIDRRKP-PSDIQWRSIHQTPPPLMRRSTTSEIFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTE 167
Cdd:PRK08927 98 WLGRVVNALGEPIDGKGPlPQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 168 MIHNVVKQhqgVSIFCGIGERCREGEE-LYRDMKDAGvLPNTVMVFGQMNEPPGARFRVGHTALTMAEYFRdDERRDVLL 246
Cdd:PRK08927 178 LARNADAD---VSVIGLIGERGREVQEfLQDDLGPEG-LARSVVVVATSDEPALMRRQAAYLTLAIAEYFR-DQGKDVLC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 247 LIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERI--STTDAGAIMSIQAVYVPADDFTDPSAVHTFSHLSA 324
Cdd:PRK08927 253 LMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 325 SIVLSRKRASEGLYPAIDPLQSNSKmATPGIVGERHYLLAQEIRQTLAQYSELKDIISmLGLEQL--SPEDRNVVARARR 402
Cdd:PRK08927 333 HIVMERAIAERGRYPAINVLKSVSR-TMPGCNDPEENPLVRRARQLMATYADMEELIR-LGAYRAgsDPEVDEAIRLNPA 410
|
410 420 430
....*....|....*....|....*....|....*..
gi 2605819 403 LERFLTQPfftteqftgiKGKSISLSDALDGCERILN 439
Cdd:PRK08927 411 LEAFLRQG----------KDEATSLAEGYARLAQILG 437
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
81-417 |
2.32e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 169.10 E-value: 2.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 81 LKAPVGREILSRMFDVFGNTIDRRKPPSDIQWRSIHQTPPPLMRRSTTSEIFETGIKAIDVLVPLERGGKAGLFGGAGVG 160
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 161 KTVLLTEMIHNVVKQHQGVSIfcgIGERCREGEE-LYRDMKdaGVLPNTVMVFGQMNEPPGARFRVGHTALTMAEYFRdD 239
Cdd:PRK08472 170 KSTLMGMIVKGCLAPIKVVAL---IGERGREIPEfIEKNLG--GDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFK-N 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 240 ERRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERISTTDA-GAIMSIQAVYVPADDFTDPSAVHT 318
Cdd:PRK08472 244 QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGkGSITAFFTVLVEGDDMSDPIADQS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 319 FSHLSASIVLSRKRASEGLYPAIDPLQSNSKMATpGIVGERHYLLAQEIRQTlaqYSELK--DIISMLGLEQ--LSPEDR 394
Cdd:PRK08472 324 RSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRL---YSLLKenEVLIRIGAYQkgNDKELD 399
|
330 340
....*....|....*....|...
gi 2605819 395 NVVARARRLERFLTQPffTTEQF 417
Cdd:PRK08472 400 EAISKKEFMEQFLKQN--PNELF 420
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
37-409 |
3.36e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 166.03 E-value: 3.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 37 RAGRESQIAIEVLT-QLDAHhVRGIA-----LTPTE---GLARGMAVEDTGGPLKAPVGREILSRMFDVFGNTIDRRKPP 107
Cdd:PRK08972 43 RAPVGSLCSIETMAgELEAE-VVGFDgdllyLMPIEelrGVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 108 SDIQWRSIHQTP-PPLMRRSTTsEIFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNVVKQhqgVSIFCGIG 186
Cdd:PRK08972 122 YTDQRASRHSPPiNPLSRRPIT-EPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTTAD---VIVVGLVG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 187 ERCREGEELYRDMKDAGVLPNTVMVFGQMNEPPGARFRVGHTALTMAEYFRdDERRDVLLLIDNIFRFIQAGSEVSGLMG 266
Cdd:PRK08972 198 ERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCETATTIAEYFR-DQGLNVLLLMDSLTRYAQAQREIALAVG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 267 QMPSRLGYQPTLGTELSELEERIST--TDAGAIMSIQAVYVPADDFTDPSAVHTFSHLSASIVLSRKRASEGLYPAIDPL 344
Cdd:PRK08972 277 EPPATKGYPPSVFAKLPALVERAGNggPGQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIE 356
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2605819 345 QSNSKMAtPGIVGERHYLLAQEIRQTLAQYSELKDIISMLGLEQLS-PEDRNVVARARRLERFLTQ 409
Cdd:PRK08972 357 ASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLISIGAYKQGSdPRIDNAIRLQPAMNAFLQQ 421
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
92-385 |
3.82e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 160.55 E-value: 3.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 92 RMFDVFGNTIDRRKP-PSDIQWRSIHQTPPPLMRRSTTSEIFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEM-- 168
Cdd:PRK06002 108 RVINALGEPIDGLGPlAPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLar 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 169 ---IHNVVkqhqgVSIfcgIGERCREGEELYRDMKdAGVLPNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDERRdVL 245
Cdd:PRK06002 188 adaFDTVV-----IAL---VGERGREVREFLEDTL-ADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGEN-VL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 246 LLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERI--STTDAGAIMSIQAVYVPADDFTDPSAVHTFSHLS 323
Cdd:PRK06002 258 LIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLD 337
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2605819 324 ASIVLSRKRASEGLYPAIDPLQSNSKMATPGIVGERHYLLAQeIRQTLAQYSELKDIISMLG 385
Cdd:PRK06002 338 GHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSR-LKSMIARFEETRDLRLIGG 398
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
66-410 |
4.53e-44 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 160.32 E-value: 4.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 66 EGLARGMAVEDTGGPLKAPVGREILSRMFDVFGNTIDRRKPPSDIQWRSIHQTPPPLMRRSTTSEIFETGIKAIDVLVPL 145
Cdd:PRK09099 81 GGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 146 ERGGKAGLFGGAGVGKTVLLTEMIHNVvkqHQGVSIFCGIGERCREGEELYRDMKDAGVLPNTVMVFGQMNEPPGARFRV 225
Cdd:PRK09099 161 GEGQRMGIFAPAGVGKSTLMGMFARGT---QCDVNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 226 GHTALTMAEYFRDDERRdVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERISTTDAGAIMSIQAVYV 305
Cdd:PRK09099 238 AYVATAIAEYFRDRGLR-VLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 306 PADDFTDPSAVHTFSHLSASIVLSRKRASEGLYPAIDPLQSNSKMaTPGIVGERHYLLAQEIRQTLAQYSELKDIISMLG 385
Cdd:PRK09099 317 EDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRV-MPQVVPREHVQAAGRLRQLLAKHREVETLLQVGE 395
|
330 340
....*....|....*....|....*.
gi 2605819 386 LEQLS-PEDRNVVARARRLERFLTQP 410
Cdd:PRK09099 396 YRAGSdPVADEAIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
66-409 |
5.98e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 157.58 E-value: 5.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 66 EGLARGMAVEDTGGPLKAPVGREILSRMFDVFGNTIDRRKPPSDIQWrsIHQTPPPL--MRRSTTSEIFETGIKAIDVLV 143
Cdd:PRK05688 86 AGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDW--VPMDGPTInpLNRHPISEPLDVGIRSINGLL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 144 PLERGGKAGLFGGAGVGKTVLLTEMIHNVVKQHQGVSIfcgIGERCREGEELYRDMKDAGVLPNTVMVFGQMNEPPGARF 223
Cdd:PRK05688 164 TVGRGQRLGLFAGTGVGKSVLLGMMTRFTEADIIVVGL---IGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 224 RVGHTALTMAEYFRdDERRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERISTTDAGAiMSIQAV 303
Cdd:PRK05688 241 RAAMYCTRIAEYFR-DKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGG-GSITAF 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 304 YV---PADDFTDPSAVHTFSHLSASIVLSRKRASEGLYPAIDPLQSNSKmATPGIVGERHYLLAQEIRQTLAQYSELKDI 380
Cdd:PRK05688 319 YTvlsEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISR-VMPQVVDPEHLRRAQRFKQLWSRYQQSRDL 397
|
330 340 350
....*....|....*....|....*....|
gi 2605819 381 ISMLGLEQLS-PEDRNVVARARRLERFLTQ 409
Cdd:PRK05688 398 ISVGAYVAGGdPETDLAIARFPHLVQFLRQ 427
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
60-411 |
1.47e-39 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 147.74 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 60 IALTPTEGLARGMAVEDTGGPLKAPVGREILSRMFDVFGNTIDRRKPPSDIQWRSIHQTPPPLMRRSTTSEIFETGIKAI 139
Cdd:PRK05922 69 MSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 140 DVLVPLERGGKAGLFGGAGVGKTVLLTEMihnVVKQHQGVSIFCGIGERCREGEELYRDMKDAGVLPNTVMVFGQMNEPP 219
Cdd:PRK05922 149 DAFLTLGKGQRIGVFSEPGSGKSSLLSTI---AKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 220 GARFRVGHTALTMAEYFRdDERRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERISTTDAGAIMS 299
Cdd:PRK05922 226 PTKVIAGRAAMTIAEYFR-DQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 300 IQAV-YVP--ADDFTDpsavHTFSHLSASIVLSRKRASEGlYPAIDPLQSNS----KMATPgivgeRHYLLAQEIRQTLA 372
Cdd:PRK05922 305 LYAIlHYPnhPDIFTD----YLKSLLDGHFFLTPQGKALA-SPPIDILTSLSrsarQLALP-----HHYAAAEELRSLLK 374
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2605819 373 QYSELKDIISmlgLEQLSPEDRNVVARARRL----ERFLTQPF 411
Cdd:PRK05922 375 AYHEALDIIQ---LGAYVPGQDAHLDRAVKLlpsiKQFLSQPL 414
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
69-418 |
6.30e-39 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 146.47 E-value: 6.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 69 ARGMAVEDTGGPLKAPVGREILSRMFDVFGNTIDRRkPPSDIQWRSIHQTPP--PLmRRSTTSEIFETGIKAIDVLVPLE 146
Cdd:PRK07960 96 ARNISGEGLQSGKQLPLGPALLGRVLDGSGKPLDGL-PAPDTGETGALITPPfnPL-QRTPIEHVLDTGVRAINALLTVG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 147 RGGKAGLFGGAGVGKTVLLTEMihnvVKQHQGVSIFCG-IGERCREGEELYRDMKDAGVLPNTVMVFGQMNEPPGARFRV 225
Cdd:PRK07960 174 RGQRMGLFAGSGVGKSVLLGMM----ARYTQADVIVVGlIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 226 GHTALTMAEYFRdDERRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERIST--TDAGAIMSIQAV 303
Cdd:PRK07960 250 AAYATRIAEDFR-DRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTV 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 304 YVPADDFTDPSAVHTFSHLSASIVLSRKRASEGLYPAIDPLQSNSKMATpGIVGERHYLLAQEIRQTLAQYSELKDIISM 383
Cdd:PRK07960 329 LTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMT-ALIDEQHYARVRQFKQLLSSFQRNRDLVSV 407
|
330 340 350
....*....|....*....|....*....|....*.
gi 2605819 384 LGLEQLS-PEDRNVVARARRLERFLTQPFFTTEQFT 418
Cdd:PRK07960 408 GAYAKGSdPMLDKAIALWPQLEAFLQQGIFERADWE 443
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
69-409 |
8.74e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 145.80 E-value: 8.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 69 ARGMAVEDTGGPLkapVGREILSRMFDVFGNTIDRRKPPSDIQwrSIHQTPPPL--MRRSTTSEIFETGIKAIDVLVPLE 146
Cdd:PRK07196 79 ARVFPSEQDGELL---IGDSWLGRVINGLGEPLDGKGQLGGST--PLQQQLPQIhpLQRRAVDTPLDVGVNAINGLLTIG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 147 RGGKAGLFGGAGVGKTVLLTeMIhnvVKQHQGVSIFCG-IGERCREGEELYRDMKDAGVLPNTVMVFGQMNEPPGARFRV 225
Cdd:PRK07196 154 KGQRVGLMAGSGVGKSVLLG-MI---TRYTQADVVVVGlIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 226 GHTALTMAEYFRdDERRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERISTTDAGAIMS-IQAVY 304
Cdd:PRK07196 230 TELCHAIATYYR-DKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSGNGTMTaIYTVL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 305 VPADDFTDPSAVHTFSHLSASIVLSRKRASEGLYPAIDPLQSNSKMATPgIVGERHYLLAQEIRQTLAQYSELKDIISML 384
Cdd:PRK07196 309 AEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQ-VIGSQQAKAASLLKQCYADYMAIKPLIPLG 387
|
330 340
....*....|....*....|....*.
gi 2605819 385 GLEQ-LSPEDRNVVARARRLERFLTQ 409
Cdd:PRK07196 388 GYVAgADPMADQAVHYYPAITQFLRQ 413
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
65-376 |
5.23e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 140.88 E-value: 5.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 65 TEGLARGMAVEDTGGPLKAPVGREILSRMFDVFGNTIDrrKPPSDIQWRSIHQTPPPL--MRRSTTSEIFETGIKAIDVL 142
Cdd:PRK06793 73 TEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLN--EEAENIPLQKIKLDAPPIhaFEREEITDVFETGIKSIDSM 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 143 VPLERGGKAGLFGGAGVGKTVLLTEMIHNVVKQHQGVSIfcgIGERCREGEELYR-DMKDAGvLPNTVMVFGQMNEPPGA 221
Cdd:PRK06793 151 LTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISL---VGERGREVKDFIRkELGEEG-MRKSVVVVATSDESHLM 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 222 RFRVGHTALTMAEYFRdDERRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRlGYQPTLGTELSELEERISTTDAGAIMSIQ 301
Cdd:PRK06793 227 QLRAAKLATSIAEYFR-DQGNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQKGSITGIY 304
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2605819 302 AVYVPADDFTDPSAVHTFSHLSASIVLSRKRASEGLYPAIDPLQSNSKMATPgIVGERHYLLAQEIRQTLAQYSE 376
Cdd:PRK06793 305 TVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEE-IVSPNHWQLANEMRKILSIYKE 378
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
52-413 |
5.30e-36 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 139.28 E-value: 5.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 52 LDAHHVRGIALTPTEGLARGMAVEDTGGPLKAPVGREILSRMFDVFGNTIDRRKPPSDIQWRSIHQTPPPLMRRSTTSEI 131
Cdd:PRK13343 66 LEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 132 FETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNvvKQHQGV-SIFCGIGERCREGEELYRDMKDAGVLPNTVM 210
Cdd:PRK13343 146 LQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN--QKDSDViCVYVAIGQKASAVARVIETLREHGALEYTTV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 211 VFGQMNEPPGARFRVGHTALTMAEYFRdDERRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEER-- 288
Cdd:PRK13343 224 VVAEASDPPGLQYLAPFAGCAIAEYFR-DQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERaa 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 289 ---------------ISTTDAGAImsiqAVYVPAD--DFTDpsavhtfshlsASIVLSRKRASEGLYPAIDPLQSNS--- 348
Cdd:PRK13343 303 klspelgggsltalpIIETLAGEL----SAYIPTNliSITD-----------GQIYLDSDLFAAGQRPAVDVGLSVSrvg 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2605819 349 -KMATPGIvgeRHylLAQEIRQTLAQYSELKdIISMLGlEQLSPEDRNVVARARRLERFLTQPFFT 413
Cdd:PRK13343 368 gKAQHPAI---RK--ESGRLRLDYAQFLELE-AFTRFG-GLLDAGTQKQITRGRRLRELLKQPRFS 426
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
80-355 |
5.86e-35 |
|
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: 131.58 E-value: 5.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 80 PLKAPVGREILSRMFDVFGNTIDRRKPPSDIQWRSIHQTPPPLMRRSTTSEIFETGIKAIDVLVPLERGGKAGLFGGAGV 159
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 160 GKTVLLTEMIHN--VVKQHQGVSI-FCGIGERCREGEELYRDMKDAGVLPNTVMVFGQMNEPPGARFRVGHTALTMAEYF 236
Cdd:cd01135 81 PHNELAAQIARQagVVGSEENFAIvFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 237 RDDERRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERISTTD--AGAIMSIQAVYVPADDFTDPS 314
Cdd:cd01135 161 AYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEgrKGSITQIPILTMPNDDITHPI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2605819 315 AVHTFSHLSASIVLSRKRASEGLYPAIDPLQSNSKMATPGI 355
Cdd:cd01135 241 PDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGI 281
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
65-413 |
1.15e-33 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 131.87 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 65 TEGLA-RGMAVEDTGGPLKAPVGREILSRMFDVFGNTIDRRKPPSDIQWRSIHQTPPPLMRRSTTSEIFETGIKAIDVLV 143
Cdd:PRK04196 59 TTGLDlKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 144 PLERGGKAGLFGGAGvgktvllteMIHN-----VVKQ-------HQGVSIFCGIGERCREGEELYRDMKDAGVLPNTVMV 211
Cdd:PRK04196 139 TLVRGQKLPIFSGSG---------LPHNelaaqIARQakvlgeeENFAVVFAAMGITFEEANFFMEDFEETGALERSVVF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 212 FGQMNEPPGARFRVGHTALTMAEYFRDDERRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEER--I 289
Cdd:PRK04196 210 LNLADDPAIERILTPRMALTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 290 STTDAGAIMSIQAVYVPADDFTDPSAVHTFSHLSASIVLSRKRASEGLYPAIDPLQSNSKMATPGIvG-----ERHYLLA 364
Cdd:PRK04196 290 IKGKKGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGI-GegktrEDHKDVA 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2605819 365 QEIRQTLAQYSELKDIISMLGLEQLSPEDRNVVARARRLE-RFLTQPFFT 413
Cdd:PRK04196 369 NQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFErEFVNQGFDE 418
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
80-349 |
5.89e-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: 118.06 E-value: 5.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 80 PLKAPVGREILSRMFDVFGNTIDRRKPPSDI---QWRSIHQ----TPPPLMRRSTTSEIFETGIKAIDVLVPLERGGKAG 152
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAETGSIfipRGVNVQRwpvrQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGTAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 153 LFGGAGVGKTVLLtemiHNVVKQHQG-VSIFCGIGERCREGEELYRD-------MKDAGVLPNTVMVFGQMNEPPGARFR 224
Cdd:cd01134 81 IPGPFGCGKTVIS----QSLSKWSNSdVVIYVGCGERGNEMAEVLEEfpelkdpITGESLMERTVLIANTSNMPVAAREA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 225 VGHTALTMAEYFRdDERRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERI-------STTDAGAI 297
Cdd:cd01134 157 SIYTGITIAEYFR-DMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrclgSPGREGSV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2605819 298 MSIQAVYVPADDFTDPSAVHTFSHLSASIVLSRKRASEGLYPAIDPLQSNSK 349
Cdd:cd01134 236 TIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
119-409 |
8.95e-29 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 119.12 E-value: 8.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 119 PPPLMRRSTTSEIFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLltemihnvvkQHQ-------GVSIFCGIGERCRE 191
Cdd:PRK04192 198 PRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVT----------QHQlakwadaDIVIYVGCGERGNE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 192 GEELYRD---MKDagvlPN--------TVMVFGQMNEPPGARFRVGHTALTMAEYFRDdERRDVLLLIDNIFRFIQAGSE 260
Cdd:PRK04192 268 MTEVLEEfpeLID----PKtgrplmerTVLIANTSNMPVAAREASIYTGITIAEYYRD-MGYDVLLMADSTSRWAEALRE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 261 VSGLMGQMPSRLGYQPTLGTELSELEER---IST--TDAGAIMSIQAVYVPADDFTDP------SAVHTFSHLSASivLS 329
Cdd:PRK04192 343 ISGRLEEMPGEEGYPAYLASRLAEFYERagrVKTlgGEEGSVTIIGAVSPPGGDFSEPvtqntlRIVKVFWALDAE--LA 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 330 RKRAseglYPAIDPLQSNSK---MATPGI---VGERHYLLAQEIRQTLAQYSELKDIISMLGLEQLSPEDRNVVARARRL 403
Cdd:PRK04192 421 DRRH----FPAINWLTSYSLyldQVAPWWeenVDPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARLI 496
|
....*..
gi 2605819 404 -ERFLTQ 409
Cdd:PRK04192 497 rEDFLQQ 503
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
9-81 |
2.01e-27 |
|
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: 104.52 E-value: 2.01e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2605819 9 NLGKVISVRGSIVDVLF-EKHLPPVYTLLRAGRE--SQIAIEVLTQLDAHHVRGIALTPTEGLARGMAVEDTGGPL 81
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFpEGELPPIYNALEVKGDdgKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
65-409 |
8.40e-23 |
|
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: 100.57 E-value: 8.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 65 TEGL-ARGMAVEDTGGPLKAPVGREILSRMFDVFGNTIDRRKPPSDIQWRSIHQTPPPLMRRSTTSEIFETGIKAIDVLV 143
Cdd:TIGR01040 57 TSGIdAKKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 144 PLERGGKAGLFGGAG-------------VGKTVLLTEMIHNVVKQHQGVsIFCGIGERCREGEELYRDMKDAGVLPNTVM 210
Cdd:TIGR01040 137 SIARGQKIPIFSAAGlphneiaaqicrqAGLVKLPTKDVHDGHEDNFAI-VFAAMGVNMETARFFKQDFEENGSMERVCL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 211 VFGQMNEPPGARFRVGHTALTMAEYFRDDERRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERIS 290
Cdd:TIGR01040 216 FLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAG 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 291 TTD--AGAIMSIQAVYVPADDFTDPSAVHTFSHLSASIVLSRKRASEGLYPAIDPLQSNSKMATPGIvGE-----RHYLL 363
Cdd:TIGR01040 296 RVEgrNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAI-GEgmtrkDHSDV 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2605819 364 AQeirQTLAQYSELKDIISM---LGLEQLSPEDRNVVARARRLER-FLTQ 409
Cdd:TIGR01040 375 SN---QLYACYAIGKDVQAMkavVGEEALSSEDLLYLEFLDKFEKnFIAQ 421
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
81-274 |
4.30e-22 |
|
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: 95.70 E-value: 4.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 81 LKAPVGREILSRMFDVFGNTIDRRKPPSDIQWRSIHQTPPPLMRRSTTSEIFETGIKAIDVLVPLERGGKAGLFGGAGVG 160
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 161 KTVLLTEMIHNvvKQHQGV-SIFCGIGERCREGEELYRDMKDAGVLPNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDD 239
Cdd:cd01132 82 KTAIAIDTIIN--QKGKKVyCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDN 159
|
170 180 190
....*....|....*....|....*....|....*
gi 2605819 240 ErRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGY 274
Cdd:cd01132 160 G-KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAY 193
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
168-412 |
1.36e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 95.09 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 168 MIHNVVKQHQ-------GVSIFCGIGERCREGEELYRD---MKDAG----VLPNTVMVFGQMNEPPGARFRVGHTALTMA 233
Cdd:PRK14698 666 LLHNTVTQHQlakwsdaQVVIYIGCGERGNEMTDVLEEfpkLKDPKtgkpLMERTVLIANTSNMPVAAREASIYTGITIA 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 234 EYFRDdERRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERI-------STTDAGAIMSIQAVYVP 306
Cdd:PRK14698 746 EYFRD-MGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPP 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 307 ADDFTDPSAVHTFSHLSASIVLSRKRASEGLYPAIDPLQSNSkMATPGIVGERHYLLAQEIR-------QTLAQYSELKD 379
Cdd:PRK14698 825 GGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS-LYVDAVKDWWHKNVDPEWKamrdkamELLQKEAELQE 903
|
250 260 270
....*....|....*....|....*....|....
gi 2605819 380 IISMLGLEQLSPEDRNVVARARRL-ERFLTQPFF 412
Cdd:PRK14698 904 IVRIVGPDALPERERAILLVARMLrEDYLQQDAF 937
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
65-443 |
1.41e-18 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 87.78 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 65 TEGLARGMAVEDTGGPLKAPVGREILSRMFDVFGNTIDRRKPPSDiqwRSIHQTPPPL--MRRSTTSEIFETGIKAIDVL 142
Cdd:PRK02118 58 TRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEG---EPIEIGGPSVnpVKRIVPREMIRTGIPMIDVF 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 143 VPLERGGKAGLFGGAGVGKTVLLTEMihnVVKQHQGVSIFCGIGERCREGEELYRDMKDAGVLPNTVMVFGQMNEPPGAR 222
Cdd:PRK02118 135 NTLVESQKIPIFSVSGEPYNALLARI---ALQAEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVEC 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 223 FRVGHTALTMAEYFRDDERRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTEL-SELEERISTTDAGAIMSIQ 301
Cdd:PRK02118 212 LLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLaSRYEKAVDFEDGGSITIIA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 302 AVYVPADDFTDPSAVHTFSHLSASIVLSRKRaseglypaIDPLQSNSK---MATPGIVGERHYLLAQEIRQTLAQYSELK 378
Cdd:PRK02118 292 VTTMPGDDVTHPVPDNTGYITEGQFYLRRGR--------IDPFGSLSRlkqLVIGKKTREDHGDLMNAMIRLYADSREAK 363
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2605819 379 DIISMlGLEqLSPEDRNVVARARRLErfltqpffttEQFTGIKgKSISLSDALDGCERILNDEFK 443
Cdd:PRK02118 364 EKMAM-GFK-LSNWDEKLLKFSELFE----------SRLMDLE-VNIPLEEALDLGWKILAQCFH 415
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
71-365 |
1.07e-17 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 85.86 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 71 GMAVEDTGGPLKAPVGREILSRMFDVFGN-------TIDRRKPPSDIQWRSIHQTPPPLMRRSTTSEIFETGIKAIDVLV 143
Cdd:PTZ00185 105 GQKVMATGKLLYIPVGAGVLGKVVNPLGHevpvgllTRSRALLESEQTLGKVDAGAPNIVSRSPVNYNLLTGFKAVDTMI 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 144 PLERGGKAGLFGGAGVGKTVLLTEMIHNVVKQHQGV-------SIFCGIGERCREGEELYRDMKDAGVLPNTVMVFGQMN 216
Cdd:PTZ00185 185 PIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQIlsknaviSIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 217 EPPGARFRVGHTALTMAEYFRdDERRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTELSELEERISTTD--- 293
Cdd:PTZ00185 265 EPAGLQYLAPYSGVTMGEYFM-NRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSpgk 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 294 -AGAIMSIQAVYVPADDFTDPSAVHTFSHLSASIVLSRKRASEGLYPAIDPLQSNSKM-------ATPGIVGERHYLLAQ 365
Cdd:PTZ00185 344 gGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVgssaqnvAMKAVAGKLKGILAE 423
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
52-249 |
1.37e-14 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 75.87 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 52 LDAHHVRGIALTPTEGLARGMAVEDTGGPLKAPVGREILSRMFDVFGNTIDRRKPPSDIQWRSIHQTPPPLMRRSTTSEI 131
Cdd:PRK09281 66 LEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 132 FETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNvvkQH-QGV-SIFCGIGERCREGEELYRDMKDAGVLPNTV 209
Cdd:PRK09281 146 LQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIIN---QKgKDViCIYVAIGQKASTVAQVVRKLEEHGAMEYTI 222
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2605819 210 MVFGQMNEPPGARFRVGHTALTMAEYFRdDERRDVLLLID 249
Cdd:PRK09281 223 VVAATASDPAPLQYLAPYAGCAMGEYFM-DNGKDALIVYD 261
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
58-422 |
5.59e-14 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 73.84 E-value: 5.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 58 RGIALTPT----------EGLA--RGMAVEDTGGPLKAPVGREILSRMFDVFGNTIDRRKPPSDIQWRSIhQTPPP--LM 123
Cdd:CHL00059 39 IGIALNLEsnnvgvvlmgDGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLI-ESPAPgiIS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 124 RRSTTsEIFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNvvKQHQGV-SIFCGIGERCREGEELYRDMKDA 202
Cdd:CHL00059 118 RRSVY-EPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN--QKGQNViCVYVAIGQKASSVAQVVTTLQER 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 203 GVLPNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDErRDVLLLIDNIFRFIQAGSEVSGLMGQMPSRLGYQPTLGTEL 282
Cdd:CHL00059 195 GAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRG-RHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLH 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 283 SELEERI----------STTdAGAIMSIQA----VYVPAD--DFTDpsavhtfshlsASIVLSRKRASEGLYPAIDPLQS 346
Cdd:CHL00059 274 SRLLERAaklssqlgegSMT-ALPIVETQAgdvsAYIPTNviSITD-----------GQIFLSADLFNAGIRPAINVGIS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 347 NSKM---ATPGIVGErhylLAQEIRQTLAQYSELKdiismlGLEQLSPE----DRNVVARARRLERFLTQ----PFFTTE 415
Cdd:CHL00059 342 VSRVgsaAQIKAMKQ----VAGKLKLELAQFAELE------AFAQFASDldkaTQNQLARGQRLRELLKQsqsaPLTVEE 411
|
410
....*....|.
gi 2605819 416 Q----FTGIKG 422
Cdd:CHL00059 412 QvatiYTGTNG 422
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
360-419 |
6.46e-13 |
|
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: 63.62 E-value: 6.46e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 360 HYLLAQEIRQTLAQYSELKDIISMLGLEQLSPEDRNVVARARRLERFLTQPFFTTEQFTG 419
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIED 60
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
57-426 |
1.62e-08 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 56.91 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 57 VRGIALTPTEGLARgMAVEDTGGPLKapVGREI--LSRMFDV------FGNTID--------RRKPPSDIQWR----SIH 116
Cdd:PRK07165 35 VKAFVISATEDKAY-LLINNEKGKIK--INDELieLNNTNKVktskeyFGKIIDidgniiypEAQNPLSKKFLpntsSIF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 117 QTPPPLMRRSTTSEIFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNvvKQHQGVS-IFCGIGERCREGEEL 195
Cdd:PRK07165 112 NLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIIN--QKNTNVKcIYVAIGQKRENLSRI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 196 YRDMKDAGVLPNTvMVFGQMNEPPGARFRVGHTALTMAEYFRDDErrDVLLLID------NIFRfiqagsEVSGLMGQ-- 267
Cdd:PRK07165 190 YETLKEHDALKNT-IIIDAPSTSPYEQYLAPYVAMAHAENISYND--DVLIVFDdltkhaNIYR------EIALLTNKpv 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 268 ----MPSRLGYQPtlgtelSELEERisttdAGAIM---SIQA---VYVPADDFTDPSAVHTFSHLSASIVLSRKRASEGL 337
Cdd:PRK07165 261 gkeaFPGDMFFAH------SKLLER-----AGKFKnrkTITAlpiLQTVDNDITSLISSNIISITDGQIVTSSDLFASGK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 338 YPAIDPLQSNSKmaTPGIVGERHY-LLAQEIRQTLAQY-SELKdiISMLGLEqLSPEDRNVVARARRLERFLTQPFFT-- 413
Cdd:PRK07165 330 LPAIDIDLSVSR--TGSSVQSKTItKVAGEISKIYRAYkRQLK--LSMLDYD-LNKETSDLLFKGKMIEKMFNQKGFSly 404
|
410
....*....|...
gi 2605819 414 TEQFTGIKGKSIS 426
Cdd:PRK07165 405 SYRFVLLISKLIS 417
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
13-78 |
9.92e-07 |
|
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: 46.00 E-value: 9.92e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2605819 13 VISVRGSIVDVLFEK-HLPPVYTLLRAGRESQIA--IEVLTQLDAHHVRGIALTPTEGLARGMAVEDTG 78
Cdd:pfam02874 1 IVQVIGPVVDVEFGIgRLPGLLNALEVELVEFGSlvLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
147-272 |
1.25e-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: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2605819 147 RGGKAGLFGGAGVGKTVLLTEMIHNVVKQHQGVSIFCGIGERCREGEELYRDMKDAGVLPNTVmvfgqmneppGARFRVg 226
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSG----------ELRLRL- 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2605819 227 htALTMAEYFRDDerrdvLLLIDNIFRFIQAGSEVSGLMGQMPSRL 272
Cdd:smart00382 70 --ALALARKLKPD-----VLILDEITSLLDAEQEALLLLLEELRLL 108
|
|
| |
