|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
82-554 |
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: 973.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 82 AIGRVCQVIGAIVDVRFEDqEGLPPIMTSLEVQDH-PTRLVLEVSHHLGQNVVRTIAMDGTEGLVRGRKVLNTGAPITVP 160
Cdd:COG0055 4 NTGKIVQVIGPVVDVEFPE-GELPAIYNALEVENEgGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 161 VGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVL 240
Cdd:COG0055 83 VGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 241 IMELINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIKlgekqsesKCALVYGQMNEPPGARARVGLTGLTVAEYF 320
Cdd:COG0055 163 IMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD--------KTALVFGQMNEPPGARLRVALTALTMAEYF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 321 RDAEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQAIYVPADDLTDPAPA 400
Cdd:COG0055 235 RDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 401 TTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSPHILGEEHYNTARGVQKVLQNYKNLQDIIAILGMDELSEDDKLT 480
Cdd:COG0055 315 TTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLT 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18415911 481 VARARKIQRFLSQPFHVAEIFTGAPGKYVDLKENINSFQGLLDGKYDDLSEQSFYMVGGIDEVVAKAEKIAKES 554
Cdd:COG0055 395 VARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAEA 468
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
83-555 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 853.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 83 IGRVCQVIGAIVDVRFEDQEgLPPIMTSLEVQD-----HPTRLVLEVSHHLGQNVVRTIAMDGTEGLVRGRKVLNTGAPI 157
Cdd:CHL00060 16 LGRITQIIGPVLDVAFPPGK-MPNIYNALVVKGrdtagQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 158 TVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGK 237
Cdd:CHL00060 95 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 238 TVLIMELINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIKLgEKQSESKCALVYGQMNEPPGARARVGLTGLTVA 317
Cdd:CHL00060 175 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINE-QNIAESKVALVYGQMNEPPGARMRVGLTALTMA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 318 EYFRDAEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQAIYVPADDLTDP 397
Cdd:CHL00060 254 EYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 398 APATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSPHILGEEHYNTARGVQKVLQNYKNLQDIIAILGMDELSEDD 477
Cdd:CHL00060 334 APATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEED 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18415911 478 KLTVARARKIQRFLSQPFHVAEIFTGAPGKYVDLKENINSFQGLLDGKYDDLSEQSFYMVGGIDEVVAKAEKIAKESA 555
Cdd:CHL00060 414 RLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANLEVESK 491
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
82-550 |
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: 851.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 82 AIGRVCQVIGAIVDVRFEDQEgLPPIMTSLEVQ-DHPTRLVLEVSHHLGQNVVRTIAMDGTEGLVRGRKVLNTGAPITVP 160
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGE-LPRIYNALKVQnRAESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 161 VGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVL 240
Cdd:TIGR01039 80 VGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 241 IMELINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIKlgekqsesKCALVYGQMNEPPGARARVGLTGLTVAEYF 320
Cdd:TIGR01039 160 IQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID--------KTALVYGQMNEPPGARMRVALTGLTMAEYF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 321 RDAEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQAIYVPADDLTDPAPA 400
Cdd:TIGR01039 232 RDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 401 TTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSPHILGEEHYNTARGVQKVLQNYKNLQDIIAILGMDELSEDDKLT 480
Cdd:TIGR01039 312 TTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLT 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 481 VARARKIQRFLSQPFHVAEIFTGAPGKYVDLKENINSFQGLLDGKYDDLSEQSFYMVGGIDEVVAKAEKI 550
Cdd:TIGR01039 392 VERARRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
158-437 |
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: 611.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 158 TVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGK 237
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 238 TVLIMELINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIKLGekqSESKCALVYGQMNEPPGARARVGLTGLTVA 317
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLD---GLSKVALVYGQMNEPPGARARVALTGLTMA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 318 EYFRDAEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQAIYVPADDLTDP 397
Cdd:cd01133 158 EYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDP 237
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 18415911 398 APATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSP 437
Cdd:cd01133 238 APATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
84-542 |
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: 566.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 84 GRVCQVIGAIVDVRFEDQegLPPIMTSLEVQDHpTRLVLEVSHHLGQNVVRTIAMDGTEGLVRGRKVLNTGAPITVPVGR 163
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDGE--LPAIHSVLRAGRE-GEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 164 ATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIME 243
Cdd:TIGR03305 78 PTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 244 LINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIklgekqseSKCALVYGQMNEPPGARARVGLTGLTVAEYFRDA 323
Cdd:TIGR03305 158 MIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVL--------DNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 324 EGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQAIYVPADDLTDPAPATTF 403
Cdd:TIGR03305 230 EKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 404 AHLDATTVLSRQISELGIYPAVDPLDSTSRMLSPHILGEEHYNTARGVQKVLQNYKNLQDIIAILGMDELSEDDKLTVAR 483
Cdd:TIGR03305 310 SHLSASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNR 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 18415911 484 ARKIQRFLSQPFHVAEIFTGAPGKYVDLKENINSFQGLLDGKYDDLSEQSFYMVGGIDE 542
Cdd:TIGR03305 390 ARRLERFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDE 448
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
159-434 |
1.69e-130 |
|
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: 381.42 E-value: 1.69e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 159 VPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKT 238
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 239 VLIMELINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGViklgekqsESKCALVYGQMNEPPGARARVGLTGLTVAE 318
Cdd:cd19476 82 VLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGA--------MERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 319 YFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTK--KGSITSVQAIYVPADDLTD 396
Cdd:cd19476 154 YFRD-NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTD 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 18415911 397 PAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRM 434
Cdd:cd19476 233 PIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
211-432 |
5.48e-92 |
|
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: 5.48e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 211 GIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELINNVAKahgGFSVFAGVGERTREGNDLYREMIESGVIKlgekqses 290
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALK-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 291 KCALVYGQMNEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQ 370
Cdd:pfam00006 70 RTVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18415911 371 ERITTT--KKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTS 432
Cdd:pfam00006 149 ERAGRVkgKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| ATP-synt_F1_beta_C |
cd18110 |
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ... |
439-546 |
6.92e-71 |
|
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of F0F1-ATP synthase, C-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic.
Pssm-ID: 349745 [Multi-domain] Cd Length: 108 Bit Score: 222.35 E-value: 6.92e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 439 ILGEEHYNTARGVQKVLQNYKNLQDIIAILGMDELSEDDKLTVARARKIQRFLSQPFHVAEIFTGAPGKYVDLKENINSF 518
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 18415911 519 QGLLDGKYDDLSEQSFYMVGGIDEVVAK 546
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
84-496 |
1.38e-67 |
|
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 224.91 E-value: 1.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 84 GRVCQVIGAIVDVRfedqeGLP-PIMTSLEVQDHPTRLVL-EVshhLGQNVVRTIAM--DGTEGLVRGRKVLNTGAPITV 159
Cdd:COG1157 21 GRVTRVVGLLIEAV-----GPDaSIGELCEIETADGRPVLaEV---VGFRGDRVLLMplGDLEGISPGARVVPTGRPLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 160 PVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAP-----ALVDlatgqEILATGIKVVDLLAPYQRGGKIGLFGGAG 234
Cdd:COG1157 93 PVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPnplerARIT-----EPLDTGVRAIDGLLTVGRGQRIGIFAGSG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 235 VGKTVLIMELINNvAKAHggFSVFAGVGERTREgndlYREMIESgviKLGEkqsE--SKCALVYGQMNEPPGARARVGLT 312
Cdd:COG1157 168 VGKSTLLGMIARN-TEAD--VNVIALIGERGRE----VREFIED---DLGE---EglARSVVVVATSDEPPLMRLRAAYT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 313 GLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITsvqAIY---V 389
Cdd:COG1157 235 ATAIAEYFRD-QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSIT---AFYtvlV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 390 PADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRmLSPHILGEEHYNTARGVQKVLQNYKNLQDIIAI-- 467
Cdd:COG1157 311 EGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISR-VMPDIVSPEHRALARRLRRLLARYEENEDLIRIga 389
|
410 420 430
....*....|....*....|....*....|.
gi 18415911 468 --LGMDElsEDDKlTVARARKIQRFLSQPFH 496
Cdd:COG1157 390 yqPGSDP--ELDE-AIALIPAIEAFLRQGMD 417
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
158-433 |
7.48e-63 |
|
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: 207.03 E-value: 7.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 158 TVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGK 237
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 238 TVLIMELINNVAKAhggFSVFAGVGERTREgndlYREMIESgviKLGEkQSESKCALVYGQMNEPPGARARVGLTGLTVA 317
Cdd:cd01136 81 STLLGMIARNTDAD---VNVIALIGERGRE----VREFIEK---DLGE-EGLKRSVLVVATSDESPLLRVRAAYTATAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 318 EYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQAIYVPADDLTDP 397
Cdd:cd01136 150 EYFRD-QGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDP 228
|
250 260 270
....*....|....*....|....*....|....*.
gi 18415911 398 APATTFAHLDATTVLSRQISELGIYPAVDPLDSTSR 433
Cdd:cd01136 229 IADEVRSILDGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
84-496 |
1.12e-53 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 188.04 E-value: 1.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 84 GRVCQVIGAIVD-----VRFEDqeglppiMTSLEVQDHPTRLVLEVshhLG--QNVVRTIAMDGTEGLVRGRKVLNTGAP 156
Cdd:PRK06936 25 GRVTQVTGTILKavvpgVRIGE-------LCYLRNPDNSLSLQAEV---IGfaQHQALLTPLGEMYGISSNTEVSPTGTM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 157 ITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVG 236
Cdd:PRK06936 95 HQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 237 KTVLIMELINNvakAHGGFSVFAGVGERTREgndlYREMIESgviKLGEkQSESKCALVYGQMNEPPGARARVGLTGLTV 316
Cdd:PRK06936 175 KSTLLASLIRS---AEVDVTVLALIGERGRE----VREFIES---DLGE-EGLRKAVLVVATSDRPSMERAKAGFVATSI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 317 AEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQAIYVPADDLTD 396
Cdd:PRK06936 244 AEYFRD-QGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 397 PAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSpHILGEEHYNTARGVQKVLQNYKNLQDIIAI----LGMDE 472
Cdd:PRK06936 323 PVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDK 401
|
410 420
....*....|....*....|....
gi 18415911 473 LSEDdklTVARARKIQRFLSQPFH 496
Cdd:PRK06936 402 EADQ---AIERIGAIRGFLRQGTH 422
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
142-493 |
1.67e-53 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 187.59 E-value: 1.67e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 142 EGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPY 221
Cdd:PRK08472 75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTC 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 222 QRGGKIGLFGGAGVGKTVLiMELINNVAKAHggFSVFAGVGERTREgndlYREMIESgviKLGEKQSEskCALVYGQMNE 301
Cdd:PRK08472 155 GKGQKLGIFAGSGVGKSTL-MGMIVKGCLAP--IKVVALIGERGRE----IPEFIEK---NLGGDLEN--TVIVVATSDD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 302 PPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTK-KGS 380
Cdd:PRK08472 223 SPLMRKYGAFCAMSVAEYFKN-QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGS 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 381 ITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSpHILGEEHYNTARGVQKVLQNYKN 460
Cdd:PRK08472 302 ITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKE 380
|
330 340 350
....*....|....*....|....*....|....*...
gi 18415911 461 LQDIIAI----LGMD-ELSEddklTVARARKIQRFLSQ 493
Cdd:PRK08472 381 NEVLIRIgayqKGNDkELDE----AISKKEFMEQFLKQ 414
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
147-467 |
1.06e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 180.30 E-value: 1.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 147 GRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGK 226
Cdd:PRK07721 81 GCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 227 IGLFGGAGVGKTVLiMELINNVAKAHggFSVFAGVGERTREgndlYREMIESgviKLGEkQSESKCALVYGQMNEPPGAR 306
Cdd:PRK07721 161 VGIFAGSGVGKSTL-MGMIARNTSAD--LNVIALIGERGRE----VREFIER---DLGP-EGLKRSIVVVATSDQPALMR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 307 ARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQA 386
Cdd:PRK07721 230 IKGAYTATAIAEYFRD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 387 IYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSpHILGEEHYNTARGVQKVLQNYKNLQDIIA 466
Cdd:PRK07721 309 VLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMN-HIVSPEHKEAANRFRELLSTYQNSEDLIN 387
|
.
gi 18415911 467 I 467
Cdd:PRK07721 388 I 388
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
143-467 |
9.13e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 177.58 E-value: 9.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 143 GLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHrdAPALVDLATGQ--EILATGIKVVDLLAP 220
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRH--SPPINPLSRRPitEPLDVGVRAINAMLT 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 221 YQRGGKIGLFGGAGVGKTVLI-MELINNVAKAhggfSVFAGVGERTREgndlYREMIESgviKLGEkQSESKCALVYGQM 299
Cdd:PRK08972 159 VGKGQRMGLFAGSGVGKSVLLgMMTRGTTADV----IVVGLVGERGRE----VKEFIEE---ILGE-EGRARSVVVAAPA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 300 NEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITT--TK 377
Cdd:PRK08972 227 DTSPLMRLKGCETATTIAEYFRD-QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNggPG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 378 KGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLsPHILGEEHYNTARGVQKVLQN 457
Cdd:PRK08972 306 QGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSL 384
|
330
....*....|
gi 18415911 458 YKNLQDIIAI 467
Cdd:PRK08972 385 YQQNRDLISI 394
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
167-434 |
1.10e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 174.80 E-value: 1.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 167 GRIMNVLGEPIDERGEIKT-EHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELi 245
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 246 nnvAKAHGgFS--VFAGVGERTREgndlYREMIESgviKLGEkqSESKCALVYGQMNEPPGARARVGLTGLTVAEYFRDA 323
Cdd:PRK06002 186 ---ARADA-FDtvVIALVGERGRE----VREFLED---TLAD--NLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDR 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 324 eGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERI--TTTKKGSITSVQAIYVPADDLTDPAPAT 401
Cdd:PRK06002 253 -GENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADS 331
|
250 260 270
....*....|....*....|....*....|...
gi 18415911 402 TFAHLDATTVLSRQISELGIYPAVDPLDSTSRM 434
Cdd:PRK06002 332 IRGTLDGHIVLDRAIAEQGRYPAVDPLASISRL 364
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
117-493 |
8.21e-48 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 172.31 E-value: 8.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 117 PTRLVLEVSHhLGQNVVRTIAMDGTEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDErGEIKTEHYLPIHRDAP 196
Cdd:PRK06820 58 PQGMLAEVVS-IEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 197 ALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELinnVAKAHGGFSVFAGVGERTREgndlYREMI 276
Cdd:PRK06820 136 SPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGML---CADSAADVMVLALIGERGRE----VREFL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 277 ESGViklgEKQSESKCALVYGQMNEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAV 356
Cdd:PRK06820 209 EQVL----TPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRD-RGKKVLLMADSLTRYARAAREIGLAAGEPPAAG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 357 GYQPTLASDLGALQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLs 436
Cdd:PRK06820 284 SFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM- 362
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18415911 437 PHILGEEHYNTARGVQKVLQNYKNLQDIIAI----LGMDELSEDdklTVARARKIQRFLSQ 493
Cdd:PRK06820 363 PQIVSAGQLAMAQKLRRMLACYQEIELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
84-467 |
3.23e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 165.15 E-value: 3.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 84 GRVCQVIGAIVDVRfedqeGLPPIMT-----SLEVQDHpTRLVLEVshhLGQNVVRTIAM--DGTEGLVRGRKVLNTGAP 156
Cdd:PRK08927 19 GRVVAVRGLLVEVA-----GPIHALSvgariVVETRGG-RPVPCEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 157 ITVPVGRATLGRIMNVLGEPIDERGEI-KTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGV 235
Cdd:PRK08927 90 AAVRPSRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 236 GKTVLIMELINNVAKAhggFSVFAGVGERTREgndlYREMIESgviKLGEkQSESKCALVYGQMNEPPGARARVGLTGLT 315
Cdd:PRK08927 170 GKSVLLSMLARNADAD---VSVIGLIGERGRE----VQEFLQD---DLGP-EGLARSVVVVATSDEPALMRRQAAYLTLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 316 VAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERI--TTTKKGSITSVQAIYVPADD 393
Cdd:PRK08927 239 IAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDD 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18415911 394 LTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLsPHILGEEHYNTARGVQKVLQNYKNLQDIIAI 467
Cdd:PRK08927 318 HNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
142-494 |
7.80e-45 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 164.17 E-value: 7.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 142 EGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPY 221
Cdd:PRK09099 81 GGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 222 QRGGKIGLFGGAGVGKTVLIMELINNvakAHGGFSVFAGVGERTREgndlYREMIESGVIKLGEKQSESKCALVYGQMNE 301
Cdd:PRK09099 161 GEGQRMGIFAPAGVGKSTLMGMFARG---TQCDVNVIALIGERGRE----VREFIELILGEDGMARSVVVCATSDRSSIE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 302 ppgaRARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSI 381
Cdd:PRK09099 234 ----RAKAAYVATAIAEYFRD-RGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSI 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 382 TSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLsPHILGEEHYNTARGVQKVLQNYKNL 461
Cdd:PRK09099 309 TALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREV 387
|
330 340 350
....*....|....*....|....*....|....*..
gi 18415911 462 QDIIAI----LGMDELSEDdklTVARARKIQRFLSQP 494
Cdd:PRK09099 388 ETLLQVgeyrAGSDPVADE---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
141-493 |
1.39e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 160.53 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 141 TEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIhrDAPALVDLATGQ--EILATGIKVVDLL 218
Cdd:PRK06793 73 TEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKL--DAPPIHAFEREEitDVFETGIKSIDSM 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 219 APYQRGGKIGLFGGAGVGKTVLIMELINNvAKAHggFSVFAGVGERTREGNDLYREmiesgviKLGEkQSESKCALVYGQ 298
Cdd:PRK06793 151 LTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKAD--INVISLVGERGREVKDFIRK-------ELGE-EGMRKSVVVVAT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 299 MNEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAvGYQPTLASDLGALQERITTTKK 378
Cdd:PRK06793 220 SDESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 379 GSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSpHILGEEHYNTARGVQKVLQNY 458
Cdd:PRK06793 298 GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPNHWQLANEMRKILSIY 376
|
330 340 350
....*....|....*....|....*....|....*...
gi 18415911 459 KNlQDIIAILGMDELSEDDKLTVARARK---IQRFLSQ 493
Cdd:PRK06793 377 KE-NELYFKLGTIQENAENAYIFECKNKvegINTFLKQ 413
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
141-467 |
2.28e-43 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 160.12 E-value: 2.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 141 TEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDER----GEIKTEHYLPihrdAPALVDLATGQEILaTGIKVVD 216
Cdd:PRK07594 73 TIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRelpdVCWKDYDAMP----PPAMVRQPITQPLM-TGIRAID 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 217 LLAPYQRGGKIGLFGGAGVGKTVLIMELINnvaKAHGGFSVFAGVGERTREgndlYREMIESGViklgEKQSESKCALVY 296
Cdd:PRK07594 148 SVATCGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGRE----VREFIDFTL----SEETRKRCVIVV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 297 GQMNEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTT 376
Cdd:PRK07594 217 ATSDRPALERVRALFVATTIAEFFRD-NGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMG 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 377 KKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLsPHILGEEHYNTARGVQKVLQ 456
Cdd:PRK07594 296 EKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLA 374
|
330
....*....|.
gi 18415911 457 NYKNLQDIIAI 467
Cdd:PRK07594 375 LYQEVELLIRI 385
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
142-493 |
3.04e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 160.28 E-value: 3.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 142 EGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIhrDAPALVDL--ATGQEILATGIKVVDLLA 219
Cdd:PRK05688 86 AGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPM--DGPTINPLnrHPISEPLDVGIRSINGLL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 220 PYQRGGKIGLFGGAGVGKTVLiMELINNVAKAHggFSVFAGVGERTREgndlYREMIESgviKLGEkQSESKCALVYGQM 299
Cdd:PRK05688 164 TVGRGQRLGLFAGTGVGKSVL-LGMMTRFTEAD--IIVVGLIGERGRE----VKEFIEH---ILGE-EGLKRSVVVASPA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 300 NEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKG 379
Cdd:PRK05688 233 DDAPLMRLRAAMYCTRIAEYFRD-KGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 380 --SITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLsPHILGEEHYNTARGVQKVLQN 457
Cdd:PRK05688 312 ggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSR 390
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 18415911 458 YKNLQDIIAI----LGMDelsEDDKLTVARARKIQRFLSQ 493
Cdd:PRK05688 391 YQQSRDLISVgayvAGGD---PETDLAIARFPHLVQFLRQ 427
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
141-495 |
2.52e-41 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 154.38 E-value: 2.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 141 TEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGE-------PIDERGEIKtehYLPIHRDAPALVDLATGQEILATGIK 213
Cdd:PRK08149 64 AQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKiverfdaPPTVGPISE---ERVIDVAPPSYAERRPIREPLITGVR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 214 VVDLLAPYQRGGKIGLFGGAGVGKTVLIMELINNvakAHGGFSVFAGVGERTREGNDLYREMIESGviklgekqSESKCA 293
Cdd:PRK08149 141 AIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGERGREVTEFVESLRASS--------RREKCV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 294 LVYGQMNEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERI 373
Cdd:PRK08149 210 LVYATSDFSSVDRCNAALVATTVAEYFRD-QGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 374 TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSpHILGEEHYNTARGVQK 453
Cdd:PRK08149 289 GATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFG-QVTDPKHRQLAAAFRK 367
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 18415911 454 VLQNYKNLQDIIAiLGMDELSE--DDKLTVARARKIQRFLSQPF 495
Cdd:PRK08149 368 LLTRLEELQLFID-LGEYRRGEnaDNDRAMDKRPALEAFLKQDV 410
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
143-493 |
4.47e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 145.42 E-value: 4.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 143 GLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIK-----TEHYLPIHRDAPALVDlatgqEILATGIKVVDL 217
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGgstplQQQLPQIHPLQRRAVD-----TPLDVGVNAING 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 218 LAPYQRGGKIGLFGGAGVGKTVLiMELINNVAKAHggFSVFAGVGERTREgndlYREMIESGvikLGEkQSESKCALVYG 297
Cdd:PRK07196 149 LLTIGKGQRVGLMAGSGVGKSVL-LGMITRYTQAD--VVVVGLIGERGRE----VKEFIEHS---LQA-AGMAKSVVVAA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 298 QMNEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTK 377
Cdd:PRK07196 218 PADESPLMRIKATELCHAIATYYRD-KGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSS 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 378 -KGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSpHILGEEHYNTARGVQKVLQ 456
Cdd:PRK07196 297 gNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYA 375
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 18415911 457 NYKNLQDIIA----ILGMDELSEDdklTVARARKIQRFLSQ 493
Cdd:PRK07196 376 DYMAIKPLIPlggyVAGADPMADQ---AVHYYPAITQFLRQ 413
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
102-496 |
1.32e-35 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 138.81 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 102 EGLPPI----MTSLEVQDHPTRL--VLEVShhlGQNVVRTIaMDGTEGL-VRGRKVLNTGAPITVPVGRATLGRIMNVLG 174
Cdd:PRK04196 18 EGVEGVaygeIVEIELPNGEKRRgqVLEVS---EDKAVVQV-FEGTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 175 EPIDERGEIKTEHYLPIH--------RDAPalvdlatgQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELIN 246
Cdd:PRK04196 94 RPIDGGPEIIPEKRLDINgapinpvaREYP--------EEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 247 NvAKAHGGFS----VFAGVGERTREGNDLYREMIESGVIklgekqseSKCALVYGQMNEPPGARARVGLTGLTVAEYFRD 322
Cdd:PRK04196 166 Q-AKVLGEEEnfavVFAAMGITFEEANFFMEDFEETGAL--------ERSVVFLNLADDPAIERILTPRMALTAAEYLAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 323 AEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQER--ITTTKKGSITSVQAIYVPADDLTDPAPa 400
Cdd:PRK04196 237 EKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIP- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 401 ttfahlDAT-------TVLSRQISELGIYPAVDPLDSTSRMLSPHIlG-----EEHYNTARGVQKVLQNYKNLQDIIAIL 468
Cdd:PRK04196 316 ------DLTgyitegqIVLSRELHRKGIYPPIDVLPSLSRLMKDGI-GegktrEDHKDVANQLYAAYARGKDLRELAAIV 388
|
410 420
....*....|....*....|....*....
gi 18415911 469 GMDELSEDDKLTVARARKI-QRFLSQPFH 496
Cdd:PRK04196 389 GEEALSERDRKYLKFADAFeREFVNQGFD 417
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
156-434 |
1.59e-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: 134.27 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 156 PITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIH--------RDAPalvdlatgQEILATGIKVVDLLAPYQRGGKI 227
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINgppinpvaRIYP--------EEMIQTGISAIDVMNTLVRGQKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 228 GLFGGAGVGKTVLIMELINN--VAKAHGGFS-VFAGVGERTREGNDLYREMIESGVIklgekqseSKCALVYGQMNEPPG 304
Cdd:cd01135 73 PIFSGSGLPHNELAAQIARQagVVGSEENFAiVFAAMGVTMEEARFFKDDFEETGAL--------ERVVLFLNLANDPTI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 305 ARARVGLTGLTVAEYFRDAEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQER--ITTTKKGSIT 382
Cdd:cd01135 145 ERIITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSIT 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 18415911 383 SVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRM 434
Cdd:cd01135 225 QIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRL 276
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
138-467 |
1.40e-32 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 130.29 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 138 MDGTEGLVRGRKVL-------NTGAPITVPVGRATLGRIMNVLGEPID--------ERGEIKTEHYLPIHRDAPalvdla 202
Cdd:PRK07960 82 LEEVEGILPGARVYarnisgeGLQSGKQLPLGPALLGRVLDGSGKPLDglpapdtgETGALITPPFNPLQRTPI------ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 203 tgQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLiMELINNVAKAHggFSVFAGVGERTREGNDLyremIESgviK 282
Cdd:PRK07960 156 --EHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVL-LGMMARYTQAD--VIVVGLIGERGREVKDF----IEN---I 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 283 LGEkQSESKCALVYGQMNEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTL 362
Cdd:PRK07960 224 LGA-EGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 363 ASDLGALQERITT--TKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSpHIL 440
Cdd:PRK07960 302 FAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMT-ALI 380
|
330 340
....*....|....*....|....*..
gi 18415911 441 GEEHYNTARGVQKVLQNYKNLQDIIAI 467
Cdd:PRK07960 381 DEQHYARVRQFKQLLSSFQRNRDLVSV 407
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
147-523 |
8.90e-32 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 127.71 E-value: 8.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 147 GRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGK 226
Cdd:PRK05922 80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 227 IGLFGGAGVGKTvlimELINNVAK-AHGGFSVFAGVGERTREgndlYREMIEsgviKLGEKQSESKCALVYGQMNEPPGA 305
Cdd:PRK05922 160 IGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGRE----VREYIE----QHKEGLAAQRTIIIASPAHETAPT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 306 RARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQ 385
Cdd:PRK05922 228 KVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALY 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 386 AI-YVP--ADDLTDPAPATtfahLDATTVLSRQISELGiYPAVDPLDSTSR----MLSPHilgeeHYNTARGVQKVLQNY 458
Cdd:PRK05922 307 AIlHYPnhPDIFTDYLKSL----LDGHFFLTPQGKALA-SPPIDILTSLSRsarqLALPH-----HYAAAEELRSLLKAY 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18415911 459 KNLQDIIAiLGMDELSEDDKLTvaRARK----IQRFLSQPFhvaeiftgapGKYVDLKENINSFQGLLD 523
Cdd:PRK05922 377 HEALDIIQ-LGAYVPGQDAHLD--RAVKllpsIKQFLSQPL----------SSYCALHNTLKQLEALLK 432
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
124-433 |
7.88e-31 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 125.80 E-value: 7.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 124 VSHHLGQNVVRTIAMDGTEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLAT 203
Cdd:PRK13343 62 FAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 204 GQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELINNvAKAHGGFSVFAGVGERtregndlyREMIESGVIKL 283
Cdd:PRK13343 142 VTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN-QKDSDVICVYVAIGQK--------ASAVARVIETL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 284 GEKQSESKCALVYGQMNEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLA 363
Cdd:PRK13343 213 REHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIF 291
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18415911 364 SDLGALQERITTTKK----GSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSR 433
Cdd:PRK13343 292 YLHSRLLERAAKLSPelggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
83-433 |
2.18e-30 |
|
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. The alpha-subunit contains a highly conserved adenine-specific noncatalytic nucleotide-binding domain. The conserved amino acid sequence is Gly-X-X-X-X-Gly-Lys. Proton translocating ATP synthase F1, alpha subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), B subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 273365 [Multi-domain] Cd Length: 501 Bit Score: 124.42 E-value: 2.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 83 IGRVCQVIGAIVDVrfedqEGLPPIMTSlEVQDHPTRlVLEVSHHLGQNVVRTIAMDGTEGLVRGRKVLNTGAPITVPVG 162
Cdd:TIGR00962 27 VGTVVSVGDGIARV-----YGLENVMSG-ELIEFEGG-VQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 163 RATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIM 242
Cdd:TIGR00962 100 DGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 243 ELINNvAKAHGGFSVFAGVGERtregndlyREMIESGVIKLGEKQSESKCALVYGQMNEPPGARARVGLTGLTVAEYFRD 322
Cdd:TIGR00962 180 DTIIN-QKDSDVYCIYVAIGQK--------ASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 323 aEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYqPT----LASDLGALQERITTTK-KGSITSVQAIYVPADDLTDP 397
Cdd:TIGR00962 251 -NGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAF-PGdvfyLHSRLLERAAKLNDEKgGGSLTALPIIETQAGDVSAY 328
|
330 340 350
....*....|....*....|....*....|....*.
gi 18415911 398 APATTFAHLDATTVLSRQISELGIYPAVDPLDSTSR 433
Cdd:TIGR00962 329 IPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSR 364
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
82-157 |
3.72e-30 |
|
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: 112.61 E-value: 3.72e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18415911 82 AIGRVCQVIGAIVDVRFEDQEgLPPIMTSLEVQDH-PTRLVLEVSHHLGQNVVRTIAMDGTEGLVRGRKVLNTGAPI 157
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFPEGE-LPPIYNALEVKGDdGKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
156-433 |
3.87e-23 |
|
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: 99.57 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 156 PITVPVGRATLGRIMNVLGEPIDE----------RGeIKTeHYLPIHRDAPALVDLAtGQEILATGIKVVDLLAPYQRGG 225
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEViaetgsifipRG-VNV-QRWPVRQPRPVKEKLP-PNVPLLTGQRVLDTLFPVAKGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 226 KIGLFGGAGVGKTVLIMELinnvAK-AHGGFSVFAGVGERTREGNDLYREMIESGVIKLGEKQSESKCaLVYGQMNEPPG 304
Cdd:cd01134 78 TAAIPGPFGCGKTVISQSL----SKwSNSDVVIYVGCGERGNEMAEVLEEFPELKDPITGESLMERTV-LIANTSNMPVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 305 ARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERI-------TTTK 377
Cdd:cd01134 153 AREASIYTGITIAEYFRD-MGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrclgSPGR 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 18415911 378 KGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSR 433
Cdd:cd01134 232 EGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSK 287
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
121-496 |
1.21e-22 |
|
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: 100.95 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 121 VLEVSHHlgQNVVRTiaMDGTEGL-VRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYL--------PI 191
Cdd:TIGR01040 41 VLEVSGN--KAVVQV--FEGTSGIdAKKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLdingqpinPY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 192 HRDAPalvdlatgQEILATGIKVVDLLAPYQRGGKIGLFGGAG----------VGKTVLIMELINNVAKAH-GGFS-VFA 259
Cdd:TIGR01040 117 ARIYP--------EEMIQTGISAIDVMNSIARGQKIPIFSAAGlphneiaaqiCRQAGLVKLPTKDVHDGHeDNFAiVFA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 260 GVGERTREGNDLYREMIESGviklgekqSESKCALVYGQMNEPPGARARVGLTGLTVAEYFRDAEGQDVLLFIDNIFRFT 339
Cdd:TIGR01040 189 AMGVNMETARFFKQDFEENG--------SMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 340 QANSEVSALLGRIPSAVGYQPTLASDLGALQERI--TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQIS 417
Cdd:TIGR01040 261 DALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLH 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 418 ELGIYPAVDPLDSTSRMLSPHIlGE-----EHYNTARGVQKVLQNYKNLQDIIAILGMDELSEDDKLTVARARKIQR-FL 491
Cdd:TIGR01040 341 NRQIYPPINVLPSLSRLMKSAI-GEgmtrkDHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFI 419
|
....*
gi 18415911 492 SQPFH 496
Cdd:TIGR01040 420 AQGPY 424
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
159-433 |
2.73e-21 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 93.78 E-value: 2.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 159 VPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKT 238
Cdd:cd01132 4 VPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 239 VLIMELINNvAKAHGGFSVFAGVGERtregndlyREMIESGVIKLGEKQSESKCALVYGQMNEPPGARARVGLTGLTVAE 318
Cdd:cd01132 84 AIAIDTIIN-QKGKKVYCIYVAIGQK--------RSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 319 YFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYqPtlaSDLGALQERI--------TTTKKGSITSVQAIYVP 390
Cdd:cd01132 155 YFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAY-P---GDVFYLHSRLleraaklsDELGGGSLTALPIIETQ 229
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 18415911 391 ADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSR 433
Cdd:cd01132 230 AGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
206-493 |
4.50e-21 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 96.77 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 206 EILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELinnvAK-AHGGFSVFAGVGERtreGNdlyrEMIEsgVI--- 281
Cdd:PRK04192 209 EPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQL----AKwADADIVIYVGCGER---GN----EMTE--VLeef 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 282 ------KLGEKQSESKCaLVYGQMNEPPGAR-ARVgLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPS 354
Cdd:PRK04192 276 pelidpKTGRPLMERTV-LIANTSNMPVAAReASI-YTGITIAEYYRD-MGYDVLLMADSTSRWAEALREISGRLEEMPG 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 355 AVGYQPTLASDLGALQER---ITT--TKKGSITSVQAIYVPADDLTDPapaTTFAHLDATTV---LSRQISELGIYPAVD 426
Cdd:PRK04192 353 EEGYPAYLASRLAEFYERagrVKTlgGEEGSVTIIGAVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADRRHFPAIN 429
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18415911 427 PLDSTSR---MLSP--HILGEEHYNTARG-VQKVLQNYKNLQDIIAILGMDELSEDDKLTVARARKI-QRFLSQ 493
Cdd:PRK04192 430 WLTSYSLyldQVAPwwEENVDPDWRELRDeAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQ 503
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
138-353 |
6.70e-19 |
|
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439826 [Multi-domain] Cd Length: 504 Bit Score: 89.71 E-value: 6.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 138 MDGTEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDL 217
Cdd:COG0056 76 LGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 218 LAPYQRGGKIGLFGGAGVGKTVLIMELINNvAKAHGGFSVFAGVGERtregndlyremiESGVIKLGEKQSEskcalvYG 297
Cdd:COG0056 156 MIPIGRGQRELIIGDRQTGKTAIAIDTIIN-QKGKDVICIYVAIGQK------------ASTVAQVVETLEE------HG 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18415911 298 QM----------NEPPgararvGL------TGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIP 353
Cdd:COG0056 217 AMeytivvaataSDPA------PLqyiapyAGCAMGEYFMD-QGKDVLIVYDDLSKHAVAYRELSLLLRRPP 281
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
140-402 |
7.56e-19 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 88.94 E-value: 7.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 140 GTEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPID-------ERGEIKTEHYLPIHRDAPalvdlatgQEILATGI 212
Cdd:PRK02118 57 GTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDggpelegEPIEIGGPSVNPVKRIVP--------REMIRTGI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 213 KVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELinnVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIklgekqseSKC 292
Cdd:PRK02118 129 PMIDVFNTLVESQKIPIFSVSGEPYNALLARI---ALQAEADIIILGGMGLTFDDYLFFKDTFENAGAL--------DRT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 293 ALVYGQMNEPPGARARVGLTGLTVAEYFRDAEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQER 372
Cdd:PRK02118 198 VMFIHTASDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEK 277
|
250 260 270
....*....|....*....|....*....|.
gi 18415911 373 -ITTTKKGSITSVQAIYVPADDLTDPAPATT 402
Cdd:PRK02118 278 aVDFEDGGSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
257-505 |
1.10e-17 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 87.00 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 257 VFAGVGERTREGNDLYREMIESGVIKLGEKQSEsKCALVYGQMNEPPGARARVGLTGLTVAEYFRDAeGQDVLLFIDNIF 336
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFPKLKDPKTGKPLME-RTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYDVALMADSTS 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 337 RFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERI-------TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDAT 409
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVF 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 410 TVLSRQISELGIYPAVDPLDSTSRMLSP-----HILGEEHYNTARG-VQKVLQNYKNLQDIIAILGMDELSEDDKLTVAR 483
Cdd:PRK14698 844 WALDADLARRRHFPAINWLTSYSLYVDAvkdwwHKNVDPEWKAMRDkAMELLQKEAELQEIVRIVGPDALPERERAILLV 923
|
250 260
....*....|....*....|..
gi 18415911 484 ARKIQRFLSQPFHVAEIFTGAP 505
Cdd:PRK14698 924 ARMLREDYLQQDAFDEVDTYCP 945
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
444-513 |
3.98e-17 |
|
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: 75.94 E-value: 3.98e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 444 HYNTARGVQKVLQNYKNLQDIIAILGMDELSEDDKLTVARARKIQRFLSQPFHVAEIFTGAPGKYVDLKE 513
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
128-353 |
4.51e-17 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 83.96 E-value: 4.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 128 LGQNVVRTIAMDGTEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEI 207
Cdd:PRK09281 66 LEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 208 LATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELINNvAKAHGGFSVFAGVGERtregndlyremiESGVIKLGEKQ 287
Cdd:PRK09281 146 LQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIIN-QKGKDVICIYVAIGQK------------ASTVAQVVRKL 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18415911 288 SEskcalvYGQM----------NEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIP 353
Cdd:PRK09281 213 EE------HGAMeytivvaataSDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQLSLLLRRPP 281
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
83-436 |
3.59e-15 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 78.08 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 83 IGRVCQVIGAIVDVRfedqeGLPPIMTS--LEVQDHPTRLVLevshHLGQNVVRTIAMDGTEGLVRGRKVLNTGAPITVP 160
Cdd:CHL00059 7 TGTVLQVGDGIARIY-----GLDEVMAGelVEFEDGTIGIAL----NLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 161 VGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVL 240
Cdd:CHL00059 78 VSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 241 IMELINNvAKAHGGFSVFAGVGERTREgndlyremIESGVIKLGEKQSESKCALVYGQMNEPPGARARVGLTGLTVAEYF 320
Cdd:CHL00059 158 ATDTILN-QKGQNVICVYVAIGQKASS--------VAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 321 RdAEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYqP---------------TLASDLGAlqeritttkkGSITSVQ 385
Cdd:CHL00059 229 M-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAY-PgdvfylhsrlleraaKLSSQLGE----------GSMTALP 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 18415911 386 AIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLS 436
Cdd:CHL00059 297 IVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGS 347
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
109-436 |
8.72e-13 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 70.84 E-value: 8.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 109 TSLEVQDHPTRLVLEVSHHLGQN-VVRTIAMDGTEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPID------ERG 181
Cdd:PTZ00185 66 TIIMIQVSPTTFAAGLVFNLEKDgRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrSRA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 182 EIKTEHYL-PIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELINN-------VAKAHG 253
Cdd:PTZ00185 146 LLESEQTLgKVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINqvrinqqILSKNA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 254 GFSVFAGVGERTREGNDLYREMIESGVIKLgekqseskCALVYGQMNEPPGARARVGLTGLTVAEYFRDaEGQDVLLFID 333
Cdd:PTZ00185 226 VISIYVSIGQRCSNVARIHRLLRSYGALRY--------TTVMAATAAEPAGLQYLAPYSGVTMGEYFMN-RGRHCLCVYD 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 334 NIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKK----GSITSVQAIYVPADDLTDPAPATTFAHLDAT 409
Cdd:PTZ00185 297 DLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQ 376
|
330 340
....*....|....*....|....*..
gi 18415911 410 TVLSRQISELGIYPAVDPLDSTSRMLS 436
Cdd:PTZ00185 377 IYLDTKLFTGGQRPAVNIGLSVSRVGS 403
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
86-154 |
1.70e-11 |
|
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: 59.87 E-value: 1.70e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 86 VCQVIGAIVDVRFEDQEgLPPIMTSLEVQD-HPTRLVLEVSHHLGQNVVRTIAMDGTEGLVRGRKVLNTG 154
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGR-LPGLLNALEVELvEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
157-475 |
3.11e-09 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 58.94 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 157 ITVPVGRATLGRIMNVLGEPIDERGeiKTEHYL---PIHRDAPalVDLATGQEILATgiKVVDLLAPYQRGGKIGLFGGA 233
Cdd:PRK12608 69 ARPRERYRVLVRVDSVNGTDPEKLA--RRPHFDdltPLHPRER--LRLETGSDDLSM--RVVDLVAPIGKGQRGLIVAPP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 234 GVGKTVLIMELINNVAKAHGGFSVFAG-VGERTREGNDLYREMiesgviklgekQSEskcalVYGQMNEPPGARaRVGLT 312
Cdd:PRK12608 143 RAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDMRRSV-----------KGE-----VYASTFDRPPDE-HIRVA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 313 GLTVAEYFRDAE-GQDVLLFIDNIFRFTQA-NSEVSALlGRipsavgyqpTLAS--DLGALQ--ERITTTKK-----GSI 381
Cdd:PRK12608 206 ELVLERAKRLVEqGKDVVILLDSLTRLARAyNNEVESS-GR---------TLSGgvDARALQrpKRLFGAARnieegGSL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 382 TSVQAIYVP----ADDLTdpapattFAHLDAT----TVLSRQISELGIYPAVDPLDSTSR---MLsphiLGEEHYNTARG 450
Cdd:PRK12608 276 TIIATALVDtgsrMDEVI-------FEEFKGTgnmeIVLDRELADKRVFPAIDIAKSGTRreeLL----LDSKELEKVRR 344
|
330 340
....*....|....*....|....*
gi 18415911 451 VQKVLQNYKNLQdiiailGMDELSE 475
Cdd:PRK12608 345 LRRALASRKPVE------AMEALLE 363
|
|
| Synthase_beta |
pfam11421 |
ATP synthase F1 beta subunit; The NMR solution structure of the protein in SDS micelles was ... |
1-47 |
3.27e-09 |
|
ATP synthase F1 beta subunit; The NMR solution structure of the protein in SDS micelles was found to contain two helices, an N-terminal amphipathic alpha-helix and a C-terminal alpha-helix separated by a large unstructured internal domain. The N-terminal alpha-helix is the Tom20 receptor binding site whereas the C-terminal alpha-helix is located upstream of the mitochondrial processing peptidase cleavage site.
Pssm-ID: 463277 Cd Length: 47 Bit Score: 52.47 E-value: 3.27e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 18415911 1 MASRRVLSSLLRSSSGRSAAKLVNRNPRLPSPSPARHAAPCSYLLGR 47
Cdd:pfam11421 1 MASRRLLSSLLRSSSRRSPAKLGSSNPRLPSPSPARRASPCGYLLNR 47
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
223-351 |
1.15e-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: 42.75 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415911 223 RGGKIGLFGGAGVGKTVLIMELINNVAKAHGGFSVFAgvGERTREGNDLYREMIESGVIKLGEKQseskcalvygqmnep 302
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID--GEDILEEVLDQLLLIIVGGKKASGSG--------------- 63
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 18415911 303 pGARARVgltGLTVAEYFRdaegqDVLLFIDNIFRFTQANSEVSALLGR 351
Cdd:smart00382 64 -ELRLRL---ALALARKLK-----PDVLILDEITSLLDAEQEALLLLLE 103
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
84-155 |
8.01e-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: 35.37 E-value: 8.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18415911 84 GRVCQVIGAIVDVRFEDQeglPPIMTSLEVQ----DHPTRLVLEVSHHLGQNVVrTIAMDGTEGLVRGRKVLNTGA 155
Cdd:cd01426 2 GRVIRVNGPLVEAELEGE---VAIGEVCEIErgdgNNETVLKAEVIGFRGDRAI-LQLFESTRGLSRGALVEPTGR 73
|
|
| |
