|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
85-557 |
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 22326673 85 AIGRVCQVIGAIVDVRFEDqEGLPPIMTSLEVQDH-PTRLVLEVSHHLGQNVVRTIAMDGTEGLVRGRKVLNTGAPITVP 163
Cdd:COG0055 4 NTGKIVQVIGPVVDVEFPE-GELPAIYNALEVENEgGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 164 VGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVL 243
Cdd:COG0055 83 VGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 244 IMELINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIKlgekqsesKCALVYGQMNEPPGARARVGLTGLTVAEYF 323
Cdd:COG0055 163 IMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD--------KTALVFGQMNEPPGARLRVALTALTMAEYF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 324 RDAEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQAIYVPADDLTDPAPA 403
Cdd:COG0055 235 RDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 404 TTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSPHILGEEHYNTARGVQKVLQNYKNLQDIIAILGMDELSEDDKLT 483
Cdd:COG0055 315 TTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLT 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22326673 484 VARARKIQRFLSQPFHVAEIFTGAPGKYVDLKENINSFQGLLDGKYDDLSEQSFYMVGGIDEVVAKAEKIAKES 557
Cdd:COG0055 395 VARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAEA 468
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
86-558 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 852.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 86 IGRVCQVIGAIVDVRFEDQEgLPPIMTSLEVQD-----HPTRLVLEVSHHLGQNVVRTIAMDGTEGLVRGRKVLNTGAPI 160
Cdd:CHL00060 16 LGRITQIIGPVLDVAFPPGK-MPNIYNALVVKGrdtagQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 161 TVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGK 240
Cdd:CHL00060 95 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 241 TVLIMELINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIKLgEKQSESKCALVYGQMNEPPGARARVGLTGLTVA 320
Cdd:CHL00060 175 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINE-QNIAESKVALVYGQMNEPPGARMRVGLTALTMA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 321 EYFRDAEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQAIYVPADDLTDP 400
Cdd:CHL00060 254 EYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 401 APATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSPHILGEEHYNTARGVQKVLQNYKNLQDIIAILGMDELSEDD 480
Cdd:CHL00060 334 APATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEED 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22326673 481 KLTVARARKIQRFLSQPFHVAEIFTGAPGKYVDLKENINSFQGLLDGKYDDLSEQSFYMVGGIDEVVAKAEKIAKESA 558
Cdd:CHL00060 414 RLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANLEVESK 491
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
85-553 |
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: 850.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 85 AIGRVCQVIGAIVDVRFEDQEgLPPIMTSLEVQ-DHPTRLVLEVSHHLGQNVVRTIAMDGTEGLVRGRKVLNTGAPITVP 163
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGE-LPRIYNALKVQnRAESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 164 VGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVL 243
Cdd:TIGR01039 80 VGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 244 IMELINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIKlgekqsesKCALVYGQMNEPPGARARVGLTGLTVAEYF 323
Cdd:TIGR01039 160 IQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID--------KTALVYGQMNEPPGARMRVALTGLTMAEYF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 324 RDAEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQAIYVPADDLTDPAPA 403
Cdd:TIGR01039 232 RDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 404 TTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSPHILGEEHYNTARGVQKVLQNYKNLQDIIAILGMDELSEDDKLT 483
Cdd:TIGR01039 312 TTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLT 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 484 VARARKIQRFLSQPFHVAEIFTGAPGKYVDLKENINSFQGLLDGKYDDLSEQSFYMVGGIDEVVAKAEKI 553
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 ... |
161-440 |
0e+00 |
|
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410877 [Multi-domain] Cd Length: 277 Bit Score: 609.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 161 TVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGK 240
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 241 TVLIMELINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIKLGekqSESKCALVYGQMNEPPGARARVGLTGLTVA 320
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLD---GLSKVALVYGQMNEPPGARARVALTGLTMA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 321 EYFRDAEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQAIYVPADDLTDP 400
Cdd:cd01133 158 EYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDP 237
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 22326673 401 APATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSP 440
Cdd:cd01133 238 APATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
87-545 |
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: 564.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 87 GRVCQVIGAIVDVRFEDQegLPPIMTSLEVQDHpTRLVLEVSHHLGQNVVRTIAMDGTEGLVRGRKVLNTGAPITVPVGR 166
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDGE--LPAIHSVLRAGRE-GEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 167 ATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIME 246
Cdd:TIGR03305 78 PTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 247 LINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIklgekqseSKCALVYGQMNEPPGARARVGLTGLTVAEYFRDA 326
Cdd:TIGR03305 158 MIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVL--------DNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 327 EGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQAIYVPADDLTDPAPATTF 406
Cdd:TIGR03305 230 EKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 407 AHLDATTVLSRQISELGIYPAVDPLDSTSRMLSPHILGEEHYNTARGVQKVLQNYKNLQDIIAILGMDELSEDDKLTVAR 486
Cdd:TIGR03305 310 SHLSASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNR 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 22326673 487 ARKIQRFLSQPFHVAEIFTGAPGKYVDLKENINSFQGLLDGKYDDLSEQSFYMVGGIDE 545
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 ... |
162-437 |
1.23e-129 |
|
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: 379.49 E-value: 1.23e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 162 VPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKT 241
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 242 VLIMELINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGViklgekqsESKCALVYGQMNEPPGARARVGLTGLTVAE 321
Cdd:cd19476 82 VLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGA--------MERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 322 YFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTK--KGSITSVQAIYVPADDLTD 399
Cdd:cd19476 154 YFRD-NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTD 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 22326673 400 PAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRM 437
Cdd:cd19476 233 PIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
214-435 |
1.38e-91 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 279.63 E-value: 1.38e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 214 GIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELINNVAKahgGFSVFAGVGERTREGNDLYREMIESGVIKlgekqses 293
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALK-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 294 KCALVYGQMNEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQ 373
Cdd:pfam00006 70 RTVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22326673 374 ERITTT--KKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTS 435
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 ... |
442-549 |
2.34e-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: 223.51 E-value: 2.34e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 442 ILGEEHYNTARGVQKVLQNYKNLQDIIAILGMDELSEDDKLTVARARKIQRFLSQPFHVAEIFTGAPGKYVDLKENINSF 521
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 22326673 522 QGLLDGKYDDLSEQSFYMVGGIDEVVAK 549
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
87-499 |
1.85e-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: 224.52 E-value: 1.85e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 87 GRVCQVIGAIVDVRfedqeGLP-PIMTSLEVQDHPTRLVL-EVshhLGQNVVRTIAM--DGTEGLVRGRKVLNTGAPITV 162
Cdd:COG1157 21 GRVTRVVGLLIEAV-----GPDaSIGELCEIETADGRPVLaEV---VGFRGDRVLLMplGDLEGISPGARVVPTGRPLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 163 PVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAP-----ALVDlatgqEILATGIKVVDLLAPYQRGGKIGLFGGAG 237
Cdd:COG1157 93 PVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPnplerARIT-----EPLDTGVRAIDGLLTVGRGQRIGIFAGSG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 238 VGKTVLIMELINNvAKAHggFSVFAGVGERTREgndlYREMIESgviKLGEkqsE--SKCALVYGQMNEPPGARARVGLT 315
Cdd:COG1157 168 VGKSTLLGMIARN-TEAD--VNVIALIGERGRE----VREFIED---DLGE---EglARSVVVVATSDEPPLMRLRAAYT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 316 GLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITsvqAIY---V 392
Cdd:COG1157 235 ATAIAEYFRD-QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSIT---AFYtvlV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 393 PADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRmLSPHILGEEHYNTARGVQKVLQNYKNLQDIIAI-- 470
Cdd:COG1157 311 EGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISR-VMPDIVSPEHRALARRLRRLLARYEENEDLIRIga 389
|
410 420 430
....*....|....*....|....*....|.
gi 22326673 471 --LGMDElsEDDKlTVARARKIQRFLSQPFH 499
Cdd:COG1157 390 yqPGSDP--ELDE-AIALIPAIEAFLRQGMD 417
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
161-436 |
1.49e-62 |
|
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: 206.26 E-value: 1.49e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 161 TVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGK 240
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 241 TVLIMELINNVAKAhggFSVFAGVGERTREgndlYREMIESgviKLGEkQSESKCALVYGQMNEPPGARARVGLTGLTVA 320
Cdd:cd01136 81 STLLGMIARNTDAD---VNVIALIGERGRE----VREFIEK---DLGE-EGLKRSVLVVATSDESPLLRVRAAYTATAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 321 EYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQAIYVPADDLTDP 400
Cdd:cd01136 150 EYFRD-QGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDP 228
|
250 260 270
....*....|....*....|....*....|....*.
gi 22326673 401 APATTFAHLDATTVLSRQISELGIYPAVDPLDSTSR 436
Cdd:cd01136 229 IADEVRSILDGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
87-499 |
1.76e-53 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 187.65 E-value: 1.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 87 GRVCQVIGAIVD-----VRFEDqeglppiMTSLEVQDHPTRLVLEVshhLG--QNVVRTIAMDGTEGLVRGRKVLNTGAP 159
Cdd:PRK06936 25 GRVTQVTGTILKavvpgVRIGE-------LCYLRNPDNSLSLQAEV---IGfaQHQALLTPLGEMYGISSNTEVSPTGTM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 160 ITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVG 239
Cdd:PRK06936 95 HQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 240 KTVLIMELINNvakAHGGFSVFAGVGERTREgndlYREMIESgviKLGEkQSESKCALVYGQMNEPPGARARVGLTGLTV 319
Cdd:PRK06936 175 KSTLLASLIRS---AEVDVTVLALIGERGRE----VREFIES---DLGE-EGLRKAVLVVATSDRPSMERAKAGFVATSI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 320 AEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQAIYVPADDLTD 399
Cdd:PRK06936 244 AEYFRD-QGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 400 PAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSpHILGEEHYNTARGVQKVLQNYKNLQDIIAI----LGMDE 475
Cdd:PRK06936 323 PVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDK 401
|
410 420
....*....|....*....|....
gi 22326673 476 LSEDdklTVARARKIQRFLSQPFH 499
Cdd:PRK06936 402 EADQ---AIERIGAIRGFLRQGTH 422
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
145-496 |
2.43e-53 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 187.20 E-value: 2.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 145 EGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPY 224
Cdd:PRK08472 75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTC 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 225 QRGGKIGLFGGAGVGKTVLiMELINNVAKAHggFSVFAGVGERTREgndlYREMIESgviKLGEKQSEskCALVYGQMNE 304
Cdd:PRK08472 155 GKGQKLGIFAGSGVGKSTL-MGMIVKGCLAP--IKVVALIGERGRE----IPEFIEK---NLGGDLEN--TVIVVATSDD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 305 PPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTK-KGS 383
Cdd:PRK08472 223 SPLMRKYGAFCAMSVAEYFKN-QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGS 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 384 ITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSpHILGEEHYNTARGVQKVLQNYKN 463
Cdd:PRK08472 302 ITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKE 380
|
330 340 350
....*....|....*....|....*....|....*...
gi 22326673 464 LQDIIAI----LGMD-ELSEddklTVARARKIQRFLSQ 496
Cdd:PRK08472 381 NEVLIRIgayqKGNDkELDE----AISKKEFMEQFLKQ 414
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
150-470 |
1.30e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 179.92 E-value: 1.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 150 GRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGK 229
Cdd:PRK07721 81 GCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 230 IGLFGGAGVGKTVLiMELINNVAKAHggFSVFAGVGERTREgndlYREMIESgviKLGEkQSESKCALVYGQMNEPPGAR 309
Cdd:PRK07721 161 VGIFAGSGVGKSTL-MGMIARNTSAD--LNVIALIGERGRE----VREFIER---DLGP-EGLKRSIVVVATSDQPALMR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 310 ARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQA 389
Cdd:PRK07721 230 IKGAYTATAIAEYFRD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 390 IYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSpHILGEEHYNTARGVQKVLQNYKNLQDIIA 469
Cdd:PRK07721 309 VLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMN-HIVSPEHKEAANRFRELLSTYQNSEDLIN 387
|
.
gi 22326673 470 I 470
Cdd:PRK07721 388 I 388
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
146-470 |
1.54e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 177.20 E-value: 1.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 146 GLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHrdAPALVDLATGQ--EILATGIKVVDLLAP 223
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRH--SPPINPLSRRPitEPLDVGVRAINAMLT 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 224 YQRGGKIGLFGGAGVGKTVLI-MELINNVAKAhggfSVFAGVGERTREgndlYREMIESgviKLGEkQSESKCALVYGQM 302
Cdd:PRK08972 159 VGKGQRMGLFAGSGVGKSVLLgMMTRGTTADV----IVVGLVGERGRE----VKEFIEE---ILGE-EGRARSVVVAAPA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 303 NEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITT--TK 380
Cdd:PRK08972 227 DTSPLMRLKGCETATTIAEYFRD-QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNggPG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 381 KGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLsPHILGEEHYNTARGVQKVLQN 460
Cdd:PRK08972 306 QGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSL 384
|
330
....*....|
gi 22326673 461 YKNLQDIIAI 470
Cdd:PRK08972 385 YQQNRDLISI 394
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
170-437 |
2.42e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 174.03 E-value: 2.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 170 GRIMNVLGEPIDERGEIKT-EHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELi 248
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 249 nnvAKAHGgFS--VFAGVGERTREgndlYREMIESgviKLGEkqSESKCALVYGQMNEPPGARARVGLTGLTVAEYFRDA 326
Cdd:PRK06002 186 ---ARADA-FDtvVIALVGERGRE----VREFLED---TLAD--NLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDR 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 327 eGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERI--TTTKKGSITSVQAIYVPADDLTDPAPAT 404
Cdd:PRK06002 253 -GENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADS 331
|
250 260 270
....*....|....*....|....*....|...
gi 22326673 405 TFAHLDATTVLSRQISELGIYPAVDPLDSTSRM 437
Cdd:PRK06002 332 IRGTLDGHIVLDRAIAEQGRYPAVDPLASISRL 364
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
120-496 |
1.78e-47 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 171.54 E-value: 1.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 120 PTRLVLEVSHhLGQNVVRTIAMDGTEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDErGEIKTEHYLPIHRDAP 199
Cdd:PRK06820 58 PQGMLAEVVS-IEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 200 ALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELinnVAKAHGGFSVFAGVGERTREgndlYREMI 279
Cdd:PRK06820 136 SPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGML---CADSAADVMVLALIGERGRE----VREFL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 280 ESGViklgEKQSESKCALVYGQMNEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAV 359
Cdd:PRK06820 209 EQVL----TPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRD-RGKKVLLMADSLTRYARAAREIGLAAGEPPAAG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 360 GYQPTLASDLGALQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLs 439
Cdd:PRK06820 284 SFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM- 362
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22326673 440 PHILGEEHYNTARGVQKVLQNYKNLQDIIAI----LGMDELSEDdklTVARARKIQRFLSQ 496
Cdd:PRK06820 363 PQIVSAGQLAMAQKLRRMLACYQEIELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
87-470 |
6.88e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 164.38 E-value: 6.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 87 GRVCQVIGAIVDVRfedqeGLPPIMT-----SLEVQDHpTRLVLEVshhLGQNVVRTIAM--DGTEGLVRGRKVLNTGAP 159
Cdd:PRK08927 19 GRVVAVRGLLVEVA-----GPIHALSvgariVVETRGG-RPVPCEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 160 ITVPVGRATLGRIMNVLGEPIDERGEI-KTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGV 238
Cdd:PRK08927 90 AAVRPSRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 239 GKTVLIMELINNVAKAhggFSVFAGVGERTREgndlYREMIESgviKLGEkQSESKCALVYGQMNEPPGARARVGLTGLT 318
Cdd:PRK08927 170 GKSVLLSMLARNADAD---VSVIGLIGERGRE----VQEFLQD---DLGP-EGLARSVVVVATSDEPALMRRQAAYLTLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 319 VAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERI--TTTKKGSITSVQAIYVPADD 396
Cdd:PRK08927 239 IAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDD 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22326673 397 LTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLsPHILGEEHYNTARGVQKVLQNYKNLQDIIAI 470
Cdd:PRK08927 318 HNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
145-497 |
1.33e-44 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 163.79 E-value: 1.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 145 EGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPY 224
Cdd:PRK09099 81 GGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 225 QRGGKIGLFGGAGVGKTVLIMELINNvakAHGGFSVFAGVGERTREgndlYREMIESGVIKLGEKQSESKCALVYGQMNE 304
Cdd:PRK09099 161 GEGQRMGIFAPAGVGKSTLMGMFARG---TQCDVNVIALIGERGRE----VREFIELILGEDGMARSVVVCATSDRSSIE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 305 ppgaRARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSI 384
Cdd:PRK09099 234 ----RAKAAYVATAIAEYFRD-RGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSI 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 385 TSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLsPHILGEEHYNTARGVQKVLQNYKNL 464
Cdd:PRK09099 309 TALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREV 387
|
330 340 350
....*....|....*....|....*....|....*..
gi 22326673 465 QDIIAI----LGMDELSEDdklTVARARKIQRFLSQP 497
Cdd:PRK09099 388 ETLLQVgeyrAGSDPVADE---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
144-496 |
1.32e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 160.91 E-value: 1.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 144 TEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIhrDAPALVDLATGQ--EILATGIKVVDLL 221
Cdd:PRK06793 73 TEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKL--DAPPIHAFEREEitDVFETGIKSIDSM 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 222 APYQRGGKIGLFGGAGVGKTVLIMELINNvAKAHggFSVFAGVGERTREGNDLYREmiesgviKLGEkQSESKCALVYGQ 301
Cdd:PRK06793 151 LTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKAD--INVISLVGERGREVKDFIRK-------ELGE-EGMRKSVVVVAT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 302 MNEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAvGYQPTLASDLGALQERITTTKK 381
Cdd:PRK06793 220 SDESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 382 GSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSpHILGEEHYNTARGVQKVLQNY 461
Cdd:PRK06793 298 GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPNHWQLANEMRKILSIY 376
|
330 340 350
....*....|....*....|....*....|....*...
gi 22326673 462 KNlQDIIAILGMDELSEDDKLTVARARK---IQRFLSQ 496
Cdd:PRK06793 377 KE-NELYFKLGTIQENAENAYIFECKNKvegINTFLKQ 413
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
144-470 |
2.81e-43 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 159.73 E-value: 2.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 144 TEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDER----GEIKTEHYLPihrdAPALVDLATGQEILaTGIKVVD 219
Cdd:PRK07594 73 TIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRelpdVCWKDYDAMP----PPAMVRQPITQPLM-TGIRAID 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 220 LLAPYQRGGKIGLFGGAGVGKTVLIMELINnvaKAHGGFSVFAGVGERTREgndlYREMIESGViklgEKQSESKCALVY 299
Cdd:PRK07594 148 SVATCGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGRE----VREFIDFTL----SEETRKRCVIVV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 300 GQMNEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTT 379
Cdd:PRK07594 217 ATSDRPALERVRALFVATTIAEFFRD-NGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMG 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 380 KKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLsPHILGEEHYNTARGVQKVLQ 459
Cdd:PRK07594 296 EKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLA 374
|
330
....*....|.
gi 22326673 460 NYKNLQDIIAI 470
Cdd:PRK07594 375 LYQEVELLIRI 385
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
145-496 |
6.11e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 159.13 E-value: 6.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 145 EGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIhrDAPALVDL--ATGQEILATGIKVVDLLA 222
Cdd:PRK05688 86 AGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPM--DGPTINPLnrHPISEPLDVGIRSINGLL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 223 PYQRGGKIGLFGGAGVGKTVLiMELINNVAKAHggFSVFAGVGERTREgndlYREMIESgviKLGEkQSESKCALVYGQM 302
Cdd:PRK05688 164 TVGRGQRLGLFAGTGVGKSVL-LGMMTRFTEAD--IIVVGLIGERGRE----VKEFIEH---ILGE-EGLKRSVVVASPA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 303 NEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKG 382
Cdd:PRK05688 233 DDAPLMRLRAAMYCTRIAEYFRD-KGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 383 --SITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLsPHILGEEHYNTARGVQKVLQN 460
Cdd:PRK05688 312 ggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSR 390
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 22326673 461 YKNLQDIIAI----LGMDelsEDDKLTVARARKIQRFLSQ 496
Cdd:PRK05688 391 YQQSRDLISVgayvAGGD---PETDLAIARFPHLVQFLRQ 427
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
144-498 |
3.05e-41 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 154.00 E-value: 3.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 144 TEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGE-------PIDERGEIKtehYLPIHRDAPALVDLATGQEILATGIK 216
Cdd:PRK08149 64 AQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKiverfdaPPTVGPISE---ERVIDVAPPSYAERRPIREPLITGVR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 217 VVDLLAPYQRGGKIGLFGGAGVGKTVLIMELINNvakAHGGFSVFAGVGERTREGNDLYREMIESGviklgekqSESKCA 296
Cdd:PRK08149 141 AIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGERGREVTEFVESLRASS--------RREKCV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 297 LVYGQMNEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERI 376
Cdd:PRK08149 210 LVYATSDFSSVDRCNAALVATTVAEYFRD-QGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 377 TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSpHILGEEHYNTARGVQK 456
Cdd:PRK08149 289 GATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFG-QVTDPKHRQLAAAFRK 367
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 22326673 457 VLQNYKNLQDIIAiLGMDELSE--DDKLTVARARKIQRFLSQPF 498
Cdd:PRK08149 368 LLTRLEELQLFID-LGEYRRGEnaDNDRAMDKRPALEAFLKQDV 410
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
146-496 |
9.38e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 144.65 E-value: 9.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 146 GLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIK-----TEHYLPIHRDAPALVDlatgqEILATGIKVVDL 220
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGgstplQQQLPQIHPLQRRAVD-----TPLDVGVNAING 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 221 LAPYQRGGKIGLFGGAGVGKTVLiMELINNVAKAHggFSVFAGVGERTREgndlYREMIESGvikLGEkQSESKCALVYG 300
Cdd:PRK07196 149 LLTIGKGQRVGLMAGSGVGKSVL-LGMITRYTQAD--VVVVGLIGERGRE----VKEFIEHS---LQA-AGMAKSVVVAA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 301 QMNEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTK 380
Cdd:PRK07196 218 PADESPLMRIKATELCHAIATYYRD-KGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSS 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 381 -KGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSpHILGEEHYNTARGVQKVLQ 459
Cdd:PRK07196 297 gNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYA 375
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 22326673 460 NYKNLQDIIA----ILGMDELSEDdklTVARARKIQRFLSQ 496
Cdd:PRK07196 376 DYMAIKPLIPlggyVAGADPMADQ---AVHYYPAITQFLRQ 413
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
105-499 |
1.08e-35 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 139.19 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 105 EGLPPI----MTSLEVQDHPTRL--VLEVShhlGQNVVRTIaMDGTEGL-VRGRKVLNTGAPITVPVGRATLGRIMNVLG 177
Cdd:PRK04196 18 EGVEGVaygeIVEIELPNGEKRRgqVLEVS---EDKAVVQV-FEGTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 178 EPIDERGEIKTEHYLPIH--------RDAPalvdlatgQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELIN 249
Cdd:PRK04196 94 RPIDGGPEIIPEKRLDINgapinpvaREYP--------EEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 250 NvAKAHGGFS----VFAGVGERTREGNDLYREMIESGVIklgekqseSKCALVYGQMNEPPGARARVGLTGLTVAEYFRD 325
Cdd:PRK04196 166 Q-AKVLGEEEnfavVFAAMGITFEEANFFMEDFEETGAL--------ERSVVFLNLADDPAIERILTPRMALTAAEYLAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 326 AEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQER--ITTTKKGSITSVQAIYVPADDLTDPAPa 403
Cdd:PRK04196 237 EKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIP- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 404 ttfahlDAT-------TVLSRQISELGIYPAVDPLDSTSRMLSPHIlG-----EEHYNTARGVQKVLQNYKNLQDIIAIL 471
Cdd:PRK04196 316 ------DLTgyitegqIVLSRELHRKGIYPPIDVLPSLSRLMKDGI-GegktrEDHKDVANQLYAAYARGKDLRELAAIV 388
|
410 420
....*....|....*....|....*....
gi 22326673 472 GMDELSEDDKLTVARARKI-QRFLSQPFH 499
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 ... |
159-437 |
1.89e-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: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 159 PITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIH--------RDAPalvdlatgQEILATGIKVVDLLAPYQRGGKI 230
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINgppinpvaRIYP--------EEMIQTGISAIDVMNTLVRGQKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 231 GLFGGAGVGKTVLIMELINN--VAKAHGGFS-VFAGVGERTREGNDLYREMIESGVIklgekqseSKCALVYGQMNEPPG 307
Cdd:cd01135 73 PIFSGSGLPHNELAAQIARQagVVGSEENFAiVFAAMGVTMEEARFFKDDFEETGAL--------ERVVLFLNLANDPTI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 308 ARARVGLTGLTVAEYFRDAEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQER--ITTTKKGSIT 385
Cdd:cd01135 145 ERIITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSIT 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 22326673 386 SVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRM 437
Cdd:cd01135 225 QIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRL 276
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
141-470 |
2.91e-32 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 129.13 E-value: 2.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 141 MDGTEGLVRGRKVL-------NTGAPITVPVGRATLGRIMNVLGEPID--------ERGEIKTEHYLPIHRDAPalvdla 205
Cdd:PRK07960 82 LEEVEGILPGARVYarnisgeGLQSGKQLPLGPALLGRVLDGSGKPLDglpapdtgETGALITPPFNPLQRTPI------ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 206 tgQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLiMELINNVAKAHggFSVFAGVGERTREGNDLyremIESgviK 285
Cdd:PRK07960 156 --EHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVL-LGMMARYTQAD--VIVVGLIGERGREVKDF----IEN---I 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 286 LGEkQSESKCALVYGQMNEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTL 365
Cdd:PRK07960 224 LGA-EGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 366 ASDLGALQERITT--TKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSpHIL 443
Cdd:PRK07960 302 FAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMT-ALI 380
|
330 340
....*....|....*....|....*..
gi 22326673 444 GEEHYNTARGVQKVLQNYKNLQDIIAI 470
Cdd:PRK07960 381 DEQHYARVRQFKQLLSSFQRNRDLVSV 407
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
150-526 |
1.65e-31 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 126.94 E-value: 1.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 150 GRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGK 229
Cdd:PRK05922 80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 230 IGLFGGAGVGKTvlimELINNVAK-AHGGFSVFAGVGERTREgndlYREMIEsgviKLGEKQSESKCALVYGQMNEPPGA 308
Cdd:PRK05922 160 IGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGRE----VREYIE----QHKEGLAAQRTIIIASPAHETAPT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 309 RARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQ 388
Cdd:PRK05922 228 KVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALY 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 389 AI-YVP--ADDLTDPAPATtfahLDATTVLSRQISELGiYPAVDPLDSTSR----MLSPHilgeeHYNTARGVQKVLQNY 461
Cdd:PRK05922 307 AIlHYPnhPDIFTDYLKSL----LDGHFFLTPQGKALA-SPPIDILTSLSRsarqLALPH-----HYAAAEELRSLLKAY 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22326673 462 KNLQDIIAiLGMDELSEDDKL--TVARARKIQRFLSQPFhvaeiftgapGKYVDLKENINSFQGLLD 526
Cdd:PRK05922 377 HEALDIIQ-LGAYVPGQDAHLdrAVKLLPSIKQFLSQPL----------SSYCALHNTLKQLEALLK 432
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
127-436 |
1.06e-30 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 125.41 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 127 VSHHLGQNVVRTIAMDGTEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLAT 206
Cdd:PRK13343 62 FAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 207 GQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELINNvAKAHGGFSVFAGVGERtregndlyREMIESGVIKL 286
Cdd:PRK13343 142 VTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN-QKDSDVICVYVAIGQK--------ASAVARVIETL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 287 GEKQSESKCALVYGQMNEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLA 366
Cdd:PRK13343 213 REHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIF 291
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22326673 367 SDLGALQERITTTKK----GSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSR 436
Cdd:PRK13343 292 YLHSRLLERAAKLSPelggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
86-436 |
2.44e-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: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 86 IGRVCQVIGAIVDVrfedqEGLPPIMTSlEVQDHPTRlVLEVSHHLGQNVVRTIAMDGTEGLVRGRKVLNTGAPITVPVG 165
Cdd:TIGR00962 27 VGTVVSVGDGIARV-----YGLENVMSG-ELIEFEGG-VQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 166 RATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIM 245
Cdd:TIGR00962 100 DGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 246 ELINNvAKAHGGFSVFAGVGERtregndlyREMIESGVIKLGEKQSESKCALVYGQMNEPPGARARVGLTGLTVAEYFRD 325
Cdd:TIGR00962 180 DTIIN-QKDSDVYCIYVAIGQK--------ASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 326 aEGQDVLLFIDNIFRFTQANSEVSALLGR------IPSAVGYqptLASDLGALQERITTTK-KGSITSVQAIYVPADDLT 398
Cdd:TIGR00962 251 -NGKHALIIYDDLSKQAVAYRQISLLLRRppgreaFPGDVFY---LHSRLLERAAKLNDEKgGGSLTALPIIETQAGDVS 326
|
330 340 350
....*....|....*....|....*....|....*...
gi 22326673 399 DPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSR 436
Cdd:TIGR00962 327 AYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSR 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 ... |
85-160 |
3.87e-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: 3.87e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22326673 85 AIGRVCQVIGAIVDVRFEDQEgLPPIMTSLEVQDH-PTRLVLEVSHHLGQNVVRTIAMDGTEGLVRGRKVLNTGAPI 160
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 ... |
159-436 |
6.14e-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: 98.80 E-value: 6.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 159 PITVPVGRATLGRIMNVLGEPIDE----------RGeIKTeHYLPIHRDAPALVDLAtGQEILATGIKVVDLLAPYQRGG 228
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEViaetgsifipRG-VNV-QRWPVRQPRPVKEKLP-PNVPLLTGQRVLDTLFPVAKGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 229 KIGLFGGAGVGKTVLIMELinnvAK-AHGGFSVFAGVGERTREGNDLYREMIESGVIKLGEKQSESKCaLVYGQMNEPPG 307
Cdd:cd01134 78 TAAIPGPFGCGKTVISQSL----SKwSNSDVVIYVGCGERGNEMAEVLEEFPELKDPITGESLMERTV-LIANTSNMPVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 308 ARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERI-------TTTK 380
Cdd:cd01134 153 AREASIYTGITIAEYFRD-MGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrclgSPGR 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 22326673 381 KGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSR 436
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 ... |
124-499 |
1.22e-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: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 124 VLEVSHHlgQNVVRTiaMDGTEGL-VRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYL--------PI 194
Cdd:TIGR01040 41 VLEVSGN--KAVVQV--FEGTSGIdAKKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLdingqpinPY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 195 HRDAPalvdlatgQEILATGIKVVDLLAPYQRGGKIGLFGGAG----------VGKTVLIMELINNVAKAH-GGFS-VFA 262
Cdd:TIGR01040 117 ARIYP--------EEMIQTGISAIDVMNSIARGQKIPIFSAAGlphneiaaqiCRQAGLVKLPTKDVHDGHeDNFAiVFA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 263 GVGERTREGNDLYREMIESGviklgekqSESKCALVYGQMNEPPGARARVGLTGLTVAEYFRDAEGQDVLLFIDNIFRFT 342
Cdd:TIGR01040 189 AMGVNMETARFFKQDFEENG--------SMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 343 QANSEVSALLGRIPSAVGYQPTLASDLGALQERI--TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQIS 420
Cdd:TIGR01040 261 DALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLH 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 421 ELGIYPAVDPLDSTSRMLSPHIlGE-----EHYNTARGVQKVLQNYKNLQDIIAILGMDELSEDDKLTVARARKIQR-FL 494
Cdd:TIGR01040 341 NRQIYPPINVLPSLSRLMKSAI-GEgmtrkDHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFI 419
|
....*
gi 22326673 495 SQPFH 499
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 ... |
162-436 |
2.95e-21 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 93.78 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 162 VPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKT 241
Cdd:cd01132 4 VPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 242 VLIMELINNvAKAHGGFSVFAGVGERtregndlyREMIESGVIKLGEKQSESKCALVYGQMNEPPGARARVGLTGLTVAE 321
Cdd:cd01132 84 AIAIDTIIN-QKGKKVYCIYVAIGQK--------RSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 322 YFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYqPtlaSDLGALQERI--------TTTKKGSITSVQAIYVP 393
Cdd:cd01132 155 YFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAY-P---GDVFYLHSRLleraaklsDELGGGSLTALPIIETQ 229
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 22326673 394 ADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSR 436
Cdd:cd01132 230 AGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
209-496 |
3.73e-21 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 97.16 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 209 EILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELinnvAK-AHGGFSVFAGVGERtreGNdlyrEMIEsgVI--- 284
Cdd:PRK04192 209 EPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQL----AKwADADIVIYVGCGER---GN----EMTE--VLeef 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 285 ------KLGEKQSESKCaLVYGQMNEPPGAR-ARVgLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIPS 357
Cdd:PRK04192 276 pelidpKTGRPLMERTV-LIANTSNMPVAAReASI-YTGITIAEYYRD-MGYDVLLMADSTSRWAEALREISGRLEEMPG 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 358 AVGYQPTLASDLGALQER---ITT--TKKGSITSVQAIYVPADDLTDPapaTTFAHLDATTV---LSRQISELGIYPAVD 429
Cdd:PRK04192 353 EEGYPAYLASRLAEFYERagrVKTlgGEEGSVTIIGAVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADRRHFPAIN 429
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22326673 430 PLDSTSR---MLSP--HILGEEHYNTARG-VQKVLQNYKNLQDIIAILGMDELSEDDKLTVARARKI-QRFLSQ 496
Cdd:PRK04192 430 WLTSYSLyldQVAPwwEENVDPDWRELRDeAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQ 503
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
141-356 |
6.50e-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: 6.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 141 MDGTEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDL 220
Cdd:COG0056 76 LGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 221 LAPYQRGGKIGLFGGAGVGKTVLIMELINNvAKAHGGFSVFAGVGERtregndlyremiESGVIKLGEKQSEskcalvYG 300
Cdd:COG0056 156 MIPIGRGQRELIIGDRQTGKTAIAIDTIIN-QKGKDVICIYVAIGQK------------ASTVAQVVETLEE------HG 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22326673 301 QM----------NEPPgararvGL------TGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIP 356
Cdd:COG0056 217 AMeytivvaataSDPA------PLqyiapyAGCAMGEYFMD-QGKDVLIVYDDLSKHAVAYRELSLLLRRPP 281
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
143-405 |
7.86e-19 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 88.94 E-value: 7.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 143 GTEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPID-------ERGEIKTEHYLPIHRDAPalvdlatgQEILATGI 215
Cdd:PRK02118 57 GTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDggpelegEPIEIGGPSVNPVKRIVP--------REMIRTGI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 216 KVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELinnVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIklgekqseSKC 295
Cdd:PRK02118 129 PMIDVFNTLVESQKIPIFSVSGEPYNALLARI---ALQAEADIIILGGMGLTFDDYLFFKDTFENAGAL--------DRT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 296 ALVYGQMNEPPGARARVGLTGLTVAEYFRDAEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQER 375
Cdd:PRK02118 198 VMFIHTASDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEK 277
|
250 260 270
....*....|....*....|....*....|.
gi 22326673 376 -ITTTKKGSITSVQAIYVPADDLTDPAPATT 405
Cdd:PRK02118 278 aVDFEDGGSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
260-508 |
1.12e-17 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 87.00 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 260 VFAGVGERTREGNDLYREMIESGVIKLGEKQSEsKCALVYGQMNEPPGARARVGLTGLTVAEYFRDAeGQDVLLFIDNIF 339
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFPKLKDPKTGKPLME-RTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYDVALMADSTS 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 340 RFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERI-------TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDAT 412
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVF 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 413 TVLSRQISELGIYPAVDPLDSTSRMLSP-----HILGEEHYNTARG-VQKVLQNYKNLQDIIAILGMDELSEDDKLTVAR 486
Cdd:PRK14698 844 WALDADLARRRHFPAINWLTSYSLYVDAvkdwwHKNVDPEWKAMRDkAMELLQKEAELQEIVRIVGPDALPERERAILLV 923
|
250 260
....*....|....*....|..
gi 22326673 487 ARKIQRFLSQPFHVAEIFTGAP 508
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, ... |
447-516 |
2.28e-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: 76.71 E-value: 2.28e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 447 HYNTARGVQKVLQNYKNLQDIIAILGMDELSEDDKLTVARARKIQRFLSQPFHVAEIFTGAPGKYVDLKE 516
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
131-356 |
4.45e-17 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 83.96 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 131 LGQNVVRTIAMDGTEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEI 210
Cdd:PRK09281 66 LEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 211 LATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELINNvAKAHGGFSVFAGVGERtregndlyremiESGVIKLGEKQ 290
Cdd:PRK09281 146 LQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIIN-QKGKDVICIYVAIGQK------------ASTVAQVVRKL 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22326673 291 SEskcalvYGQM----------NEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFTQANSEVSALLGRIP 356
Cdd:PRK09281 213 EE------HGAMeytivvaataSDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQLSLLLRRPP 281
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
86-439 |
3.93e-15 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 78.08 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 86 IGRVCQVIGAIVDVRfedqeGLPPIMTS--LEVQDHPTRLVLevshHLGQNVVRTIAMDGTEGLVRGRKVLNTGAPITVP 163
Cdd:CHL00059 7 TGTVLQVGDGIARIY-----GLDEVMAGelVEFEDGTIGIAL----NLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 164 VGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVL 243
Cdd:CHL00059 78 VSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 244 IMELINNvAKAHGGFSVFAGVGERTREgndlyremIESGVIKLGEKQSESKCALVYGQMNEPPGARARVGLTGLTVAEYF 323
Cdd:CHL00059 158 ATDTILN-QKGQNVICVYVAIGQKASS--------VAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 324 RdAEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGY--------------QPTLASDLGAlqeritttkkGSITSVQA 389
Cdd:CHL00059 229 M-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYpgdvfylhsrllerAAKLSSQLGE----------GSMTALPI 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 22326673 390 IYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLS 439
Cdd:CHL00059 298 VETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGS 347
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
40-439 |
5.08e-13 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 71.61 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 40 GAAPCGTLLGRVAeySTSSPANSAAPssapakdeGKKTYdYGGKGAIGRVCQVIGAIVDVRfeDQEGLPPIM--TSLEVQ 117
Cdd:PTZ00185 5 VAQYVAPAMGRLA--STAAAGKSAAP--------GQKSF-FKATEMIGYVHSIDGTIATLI--PAPGNPGVAynTIIMIQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 118 DHPTRLVLEVSHHLGQN-VVRTIAMDGTEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPID------ERGEIKTEH 190
Cdd:PTZ00185 72 VSPTTFAAGLVFNLEKDgRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrSRALLESEQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 191 YL-PIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELINN-------VAKAHGGFSVFA 262
Cdd:PTZ00185 152 TLgKVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINqvrinqqILSKNAVISIYV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 263 GVGERTREGNDLYREMIESGVIKLgekqseskCALVYGQMNEPPGARARVGLTGLTVAEYFRDaEGQDVLLFIDNIFRFT 342
Cdd:PTZ00185 232 SIGQRCSNVARIHRLLRSYGALRY--------TTVMAATAAEPAGLQYLAPYSGVTMGEYFMN-RGRHCLCVYDDLSKQA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 343 QANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKK----GSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQ 418
Cdd:PTZ00185 303 VAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTK 382
|
410 420
....*....|....*....|.
gi 22326673 419 ISELGIYPAVDPLDSTSRMLS 439
Cdd:PTZ00185 383 LFTGGQRPAVNIGLSVSRVGS 403
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
89-157 |
1.60e-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: 1.60e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 89 VCQVIGAIVDVRFEDQEgLPPIMTSLEVQD-HPTRLVLEVSHHLGQNVVRTIAMDGTEGLVRGRKVLNTG 157
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGR-LPGLLNALEVELvEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
160-478 |
3.14e-09 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 58.94 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 160 ITVPVGRATLGRIMNVLGEPIDERGeiKTEHYL---PIHRDAPalVDLATGQEILATgiKVVDLLAPYQRGGKIGLFGGA 236
Cdd:PRK12608 69 ARPRERYRVLVRVDSVNGTDPEKLA--RRPHFDdltPLHPRER--LRLETGSDDLSM--RVVDLVAPIGKGQRGLIVAPP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 237 GVGKTVLIMELINNVAKAHGGFSVFAG-VGERTREGNDLYREMiesgviklgekQSEskcalVYGQMNEPPGARaRVGLT 315
Cdd:PRK12608 143 RAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDMRRSV-----------KGE-----VYASTFDRPPDE-HIRVA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 316 GLTVAEYFRDAE-GQDVLLFIDNIFRFTQA-NSEVSALlGRipsavgyqpTLAS--DLGALQ--ERITTTKK-----GSI 384
Cdd:PRK12608 206 ELVLERAKRLVEqGKDVVILLDSLTRLARAyNNEVESS-GR---------TLSGgvDARALQrpKRLFGAARnieegGSL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 385 TSVQAIYVP----ADDLTdpapattFAHLDAT----TVLSRQISELGIYPAVDPLDSTSR---MLsphiLGEEHYNTARG 453
Cdd:PRK12608 276 TIIATALVDtgsrMDEVI-------FEEFKGTgnmeIVLDRELADKRVFPAIDIAKSGTRreeLL----LDSKELEKVRR 344
|
330 340
....*....|....*....|....*
gi 22326673 454 VQKVLQNYKNLQdiiailGMDELSE 478
Cdd:PRK12608 345 LRRALASRKPVE------AMEALLE 363
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
226-354 |
9.67e-05 |
|
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: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326673 226 RGGKIGLFGGAGVGKTVLIMELINNVAKAHGGFSVFAgvGERTREGNDLYREMIESGVIKLGEKQseskcalvygqmnep 305
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID--GEDILEEVLDQLLLIIVGGKKASGSG--------------- 63
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 22326673 306 pGARARVgltGLTVAEYFRdaegqDVLLFIDNIFRFTQANSEVSALLGR 354
Cdd:smart00382 64 -ELRLRL---ALALARKLK-----PDVLILDEITSLLDAEQEALLLLLE 103
|
|
| Synthase_beta |
pfam11421 |
ATP synthase F1 beta subunit; The NMR solution structure of the protein in SDS micelles was ... |
1-50 |
1.05e-03 |
|
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: 37.06 E-value: 1.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 22326673 1 MASRRIlssLLRSSSSRSTSKSSLIGSRNPRLLSPGPAHGAAPCGTLLGR 50
Cdd:pfam11421 1 MASRRL---LSSLLRSSSRRSPAKLGSSNPRLPSPSPARRASPCGYLLNR 47
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
87-158 |
7.90e-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: 7.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22326673 87 GRVCQVIGAIVDVRFEDQeglPPIMTSLEVQ----DHPTRLVLEVSHHLGQNVVrTIAMDGTEGLVRGRKVLNTGA 158
Cdd:cd01426 2 GRVIRVNGPLVEAELEGE---VAIGEVCEIErgdgNNETVLKAEVIGFRGDRAI-LQLFESTRGLSRGALVEPTGR 73
|
|
| |
