|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-309 |
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: 713.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 1 ELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINlkdatsKVALVYGQMNEPPGARARVALTGLTVAEYFRDQE 80
Cdd:COG0055 165 ELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD------KTALVFGQMNEPPGARLRVALTALTMAEYFRDEE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 81 GQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFA 160
Cdd:COG0055 239 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFA 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 161 HLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRA 240
Cdd:COG0055 319 HLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARA 398
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28931 241 RKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEE 309
Cdd:COG0055 399 RKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAE 467
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
1-309 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 634.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 1 ELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKD-ATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQ 79
Cdd:CHL00060 180 ELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNiAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDV 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 80 EGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTF 159
Cdd:CHL00060 260 NKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTF 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 160 AHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSR 239
Cdd:CHL00060 340 AHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVAR 419
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 240 ARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEE 309
Cdd:CHL00060 420 ARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANLEVE 489
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
1-306 |
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: 630.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 1 ELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINlkdatsKVALVYGQMNEPPGARARVALTGLTVAEYFRDQE 80
Cdd:TIGR01039 162 ELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID------KTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQ 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 81 GQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFA 160
Cdd:TIGR01039 236 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 161 HLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRA 240
Cdd:TIGR01039 316 HLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERA 395
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28931 241 RKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKL 306
Cdd:TIGR01039 396 RRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
1-193 |
7.01e-164 |
|
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: 457.07 E-value: 7.01e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 1 ELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLkDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQE 80
Cdd:cd01133 86 ELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINL-DGLSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 81 GQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFA 160
Cdd:cd01133 165 GQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPATTFA 244
|
170 180 190
....*....|....*....|....*....|...
gi 28931 161 HLDATTVLSRAIAELGIYPAVDPLDSTSRIMDP 193
Cdd:cd01133 245 HLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
1-299 |
2.00e-145 |
|
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: 416.92 E-value: 2.00e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 1 ELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINlkdatsKVALVYGQMNEPPGARARVALTGLTVAEYFRDQE 80
Cdd:TIGR03305 157 EMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLD------NTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 81 GQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFA 160
Cdd:TIGR03305 231 KQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFS 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 161 HLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRA 240
Cdd:TIGR03305 311 HLSASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRA 390
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 28931 241 RKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEA 299
Cdd:TIGR03305 391 RRLERFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDEA 449
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
1-190 |
9.92e-96 |
|
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: 283.96 E-value: 9.92e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 1 ELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGvinlkdATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQe 80
Cdd:cd19476 86 QLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSG------AMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDN- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 81 GQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTK--KGSITSVQAIYVPADDLTDPAPATT 158
Cdd:cd19476 159 GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDPIPDNT 238
|
170 180 190
....*....|....*....|....*....|..
gi 28931 159 FAHLDATTVLSRAIAELGIYPAVDPLDSTSRI 190
Cdd:cd19476 239 FAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_F1_beta_C |
cd18110 |
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ... |
195-302 |
6.38e-80 |
|
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: 237.76 E-value: 6.38e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 195 IVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGF 274
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 28931 275 QQILAGEYDHLPEQAFYMVGPIEEAVAK 302
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
1-188 |
3.06e-78 |
|
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: 237.25 E-value: 3.06e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 1 ELINNVAK-AHGGYSVFAGVGERTREGNDLYHEMIESGVInlkdatSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQ 79
Cdd:pfam00006 29 VLAGMIARqASADVVVYALIGERGREVREFIEELLGSGAL------KRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 80 eGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTT--KKGSITSVQAIYVPADDLTDPAPAT 157
Cdd:pfam00006 103 -GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVkgKGGSITALPTVLVPGDDITDPIPDN 181
|
170 180 190
....*....|....*....|....*....|.
gi 28931 158 TFAHLDATTVLSRAIAELGIYPAVDPLDSTS 188
Cdd:pfam00006 182 TRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
15-278 |
1.56e-38 |
|
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: 140.94 E-value: 1.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 15 VFAGVGERTREGNdlyhEMIES--GVINLKD-----ATSkvalvygqmNEPPGARARVALTGLTVAEYFRDQeGQDVLLF 87
Cdd:COG1157 187 VIALIGERGREVR----EFIEDdlGEEGLARsvvvvATS---------DEPPLMRLRAAYTATAIAEYFRDQ-GKNVLLL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 88 IDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITsvqAIY---VPADDLTDPAPATTFAHLDA 164
Cdd:COG1157 253 MDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSIT---AFYtvlVEGDDMNDPIADAVRGILDG 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 165 TTVLSRAIAELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQDIIAI----LGMDELSEEdklTVSRA 240
Cdd:COG1157 330 HIVLSRKLAERGHYPAIDVLASISRVM-PDIVSPEHRALARRLRRLLARYEENEDLIRIgayqPGSDPELDE---AIALI 405
|
250 260 270
....*....|....*....|....*....|....*...
gi 28931 241 RKIQRFLSQPfqvaevftghMGKLVPLKETIKGFQQIL 278
Cdd:COG1157 406 PAIEAFLRQG----------MDERVSFEESLAQLAELL 433
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
15-278 |
4.29e-37 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 137.25 E-value: 4.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 15 VFAGVGERTREgndlYHEMIESgviNL-KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFR 93
Cdd:PRK06820 193 VLALIGERGRE----VREFLEQ---VLtPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDR-GKKVLLMADSLTR 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 94 FTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIA 173
Cdd:PRK06820 265 YARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 174 ELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQDIIAI----LGMDELSEEdklTVSRARKIQRFLSQ 249
Cdd:PRK06820 345 GAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQEIELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
250 260
....*....|....*....|....*....
gi 28931 250 pfqvaevftgHMGKLVPLKETIKGFQQIL 278
Cdd:PRK06820 421 ----------DHSETAHLETTLEHLAQVV 439
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
15-190 |
2.65e-35 |
|
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: 128.45 E-value: 2.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 15 VFAGVGERTREGNdlyhEMIEsGVINlKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRF 94
Cdd:cd01136 97 VIALIGERGREVR----EFIE-KDLG-EEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQ-GKKVLLLMDSLTRF 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 95 TQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAE 174
Cdd:cd01136 170 AMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAE 249
|
170
....*....|....*.
gi 28931 175 LGIYPAVDPLDSTSRI 190
Cdd:cd01136 250 RGHYPAIDVLASISRV 265
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
15-279 |
1.11e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 130.58 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 15 VFAGVGERTREgndlYHEMIESgviNLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRF 94
Cdd:PRK08472 187 VVALIGERGRE----IPEFIEK---NLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQ-GLDVLFIMDSVTRF 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 95 TQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTK-KGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIA 173
Cdd:PRK08472 259 AMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELT 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 174 ELGIYPAVDPLDSTSRIMDpNIVGSEHYDVARGVQKILQDYKSLQDIIAI----LGMD-ELSEedklTVSRARKIQRFLS 248
Cdd:PRK08472 339 DFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENEVLIRIgayqKGNDkELDE----AISKKEFMEQFLK 413
|
250 260 270
....*....|....*....|....*....|.
gi 28931 249 QPFQvaevftghmgKLVPLKETIKGFQQILA 279
Cdd:PRK08472 414 QNPN----------ELFPFEQTFEQLEEILR 434
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
15-192 |
8.07e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 128.58 E-value: 8.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 15 VFAGVGERTREgndlYHEMIESgviNLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRF 94
Cdd:PRK06002 195 VIALVGERGRE----VREFLED---TLADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDR-GENVLLIVDSVTRF 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 95 TQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI--TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAI 172
Cdd:PRK06002 267 AHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAI 346
|
170 180
....*....|....*....|
gi 28931 173 AELGIYPAVDPLDSTSRIMD 192
Cdd:PRK06002 347 AEQGRYPAVDPLASISRLAR 366
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
15-249 |
2.54e-33 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 127.18 E-value: 2.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 15 VFAGVGERTREgndlYHEMIESgviNL-KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFR 93
Cdd:PRK06936 192 VLALIGERGRE----VREFIES---DLgEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQ-GKRVLLLMDSVTR 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 94 FTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIA 173
Cdd:PRK06936 264 FARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 174 ELGIYPAVDPLDSTSRIMDpNIVGSEHYDVARGVQKILQDYKSLQDIIAI----LGMDELSEEdklTVSRARKIQRFLSQ 249
Cdd:PRK06936 344 AANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
15-223 |
1.73e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 124.83 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 15 VFAGVGERTREgndlYHEMIES--GVINLKdatsKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIF 92
Cdd:PRK07721 188 VIALIGERGRE----VREFIERdlGPEGLK----RSIVVVATSDQPALMRIKGAYTATAIAEYFRDQ-GLNVMLMMDSVT 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 93 RFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAI 172
Cdd:PRK07721 259 RVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQL 338
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 28931 173 AELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQDIIAI 223
Cdd:PRK07721 339 ANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
19-223 |
5.44e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 123.27 E-value: 5.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 19 VGERTREgndlYHEMIESgvINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAG 98
Cdd:PRK08972 196 VGERGRE----VKEFIEE--ILGEEGRARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQ-GLNVLLLMDSLTRYAQAQ 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 99 SEVSALLGRIPSAVGYQPTLATDMGTMQERITT--TKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELG 176
Cdd:PRK08972 269 REIALAVGEPPATKGYPPSVFAKLPALVERAGNggPGQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSG 348
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 28931 177 IYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQDIIAI 223
Cdd:PRK08972 349 HYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLISI 394
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
2-249 |
5.27e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 117.77 E-value: 5.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 2 LINNVAK-AHGGYSVFAGVGERTREGND-LYHEMIESGVinlkdatSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQ 79
Cdd:PRK06793 172 LLGMIAKnAKADINVISLVGERGREVKDfIRKELGEEGM-------RKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQ 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 80 eGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAvGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTF 159
Cdd:PRK06793 245 -GNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLAR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 160 AHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDpNIVGSEHYDVARGVQKILQDYKSlQDIIAILGMDELSEEDKLTVSR 239
Cdd:PRK06793 323 GILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPNHWQLANEMRKILSIYKE-NELYFKLGTIQENAENAYIFEC 400
|
250
....*....|...
gi 28931 240 ARK---IQRFLSQ 249
Cdd:PRK06793 401 KNKvegINTFLKQ 413
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
19-279 |
1.33e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 117.14 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 19 VGERTREgndlYHEMIESgvINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAG 98
Cdd:PRK05688 202 IGERGRE----VKEFIEH--ILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQ 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 99 SEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKG--SITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELG 176
Cdd:PRK05688 275 REIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEG 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 177 IYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQDIIAI----LGMDelsEEDKLTVSRARKIQRFLSQpfq 252
Cdd:PRK05688 355 HYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQQSRDLISVgayvAGGD---PETDLAIARFPHLVQFLRQ--- 427
|
250 260
....*....|....*....|....*..
gi 28931 253 vaevftgHMGKLVPLKETIKGFQQILA 279
Cdd:PRK05688 428 -------GLRENVSLAQSREQLAAIFA 447
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
14-223 |
1.71e-27 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 110.81 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 14 SVFAGVGERTREgndlYHEMIESGVInlKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFR 93
Cdd:PRK07594 184 NVLVLIGERGRE----VREFIDFTLS--EETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDN-GKRVVLLADSLTR 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 94 FTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIA 173
Cdd:PRK07594 257 YARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLA 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 28931 174 ELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQDIIAI 223
Cdd:PRK07594 337 ERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEVELLIRI 385
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
14-223 |
3.48e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 110.07 E-value: 3.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 14 SVFAGVGERTRE-----GNDLYHEMIESGVINLkdATSkvalvygqmNEPPGARARVALTGLTVAEYFRDQeGQDVLLFI 88
Cdd:PRK08927 187 SVIGLIGERGREvqeflQDDLGPEGLARSVVVV--ATS---------DEPALMRRQAAYLTLAIAEYFRDQ-GKDVLCLM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 89 DNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERIT--TTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATT 166
Cdd:PRK08927 255 DSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGpgPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHI 334
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 28931 167 VLSRAIAELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQDIIAI 223
Cdd:PRK08927 335 VMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
14-250 |
3.49e-26 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 107.16 E-value: 3.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 14 SVFAGVGERTREgndlYHEMIEsgVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFR 93
Cdd:PRK09099 192 NVIALIGERGRE----VREFIE--LILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDR-GLRVLLMMDSLTR 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 94 FTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIA 173
Cdd:PRK09099 265 FARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 174 ELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQDIIAI----LGMDELSEEdklTVSRARKIQRFLSQ 249
Cdd:PRK09099 345 ARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVADE---AIAKIDAIRDFLSQ 420
|
.
gi 28931 250 P 250
Cdd:PRK09099 421 R 421
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
15-257 |
4.73e-26 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 106.62 E-value: 4.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 15 VFAGVGERTREGNDLYHEMIESGvinlkdATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRF 94
Cdd:PRK08149 181 VIGLIGERGREVTEFVESLRASS------RREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQ-GKRVVLFIDSMTRY 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 95 TQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAE 174
Cdd:PRK08149 254 ARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAA 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 175 LGIYPAVDPLDSTSRIMDpNIVGSEHYDVARGVQKILQDYKSLQDIIAiLGMDELSE--EDKLTVSRARKIQRFLSQPFQ 252
Cdd:PRK08149 334 KGHYPAIDVLKSVSRVFG-QVTDPKHRQLAAAFRKLLTRLEELQLFID-LGEYRRGEnaDNDRAMDKRPALEAFLKQDVA 411
|
....*
gi 28931 253 VAEVF 257
Cdd:PRK08149 412 EKSSF 416
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
19-279 |
8.00e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 106.13 E-value: 8.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 19 VGERTREGNDLY-HEMIESGVinlkdatSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQA 97
Cdd:PRK07196 189 IGERGREVKEFIeHSLQAAGM-------AKSVVVAAPADESPLMRIKATELCHAIATYYRDK-GHDVLLLVDSLTRYAMA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 98 GSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTK-KGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELG 176
Cdd:PRK07196 261 QREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSgNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAG 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 177 IYPAVDPLDSTSRIMDpNIVGSEHYDVARGVQKILQDYKSLQDIIA----ILGMDELSEEdklTVSRARKIQRFLSQpfq 252
Cdd:PRK07196 341 HYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMAIKPLIPlggyVAGADPMADQ---AVHYYPAITQFLRQ--- 413
|
250 260
....*....|....*....|....*..
gi 28931 253 vaevftgHMGKLVPLKETIKGFQQILA 279
Cdd:PRK07196 414 -------EVGHPALFSASVEQLTGMFP 433
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
200-269 |
5.56e-25 |
|
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: 95.20 E-value: 5.56e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 200 HYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLKE 269
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
15-251 |
2.47e-23 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 99.52 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 15 VFAGVGERTREGNDLYHEMIESGVINlkdatsKVALVYGQMNEPPGAR---ARVALTgltVAEYFRDQEGQDVLLFIDNI 91
Cdd:PRK04196 179 VFAAMGITFEEANFFMEDFEETGALE------RSVVFLNLADDPAIERiltPRMALT---AAEYLAFEKGMHVLVILTDM 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 92 FRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQER--ITTTKKGSITSVQAIYVPADDLTDPAPattfahlDAT---- 165
Cdd:PRK04196 250 TNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyit 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 166 ---TVLSRAIAELGIYPAVDPLDSTSRIMDPNIvG-----SEHYDV--------ARGVQkilqdyksLQDIIAILGMDEL 229
Cdd:PRK04196 323 egqIVLSRELHRKGIYPPIDVLPSLSRLMKDGI-GegktrEDHKDVanqlyaayARGKD--------LRELAAIVGEEAL 393
|
250 260
....*....|....*....|...
gi 28931 230 SEEDKLTVSRARKI-QRFLSQPF 251
Cdd:PRK04196 394 SERDRKYLKFADAFeREFVNQGF 416
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
15-195 |
3.67e-22 |
|
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: 93.83 E-value: 3.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 15 VFAGVGERTREGNDLYHEMIESGVINlkdatsKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRF 94
Cdd:cd01135 105 VFAAMGVTMEEARFFKDDFEETGALE------RVVLFLNLANDPTIERIITPRMALTTAEYLAYEKGKHVLVILTDMTNY 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 95 TQAGSEVSALLGRIPSAVGYQPTLATDMGTMQER--ITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAI 172
Cdd:cd01135 179 AEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDL 258
|
170 180
....*....|....*....|...
gi 28931 173 AELGIYPAVDPLDSTSRIMDPNI 195
Cdd:cd01135 259 HNKGIYPPIDVLPSLSRLMKSGI 281
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
19-223 |
3.52e-21 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 93.31 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 19 VGERTREGNDLyhemIESgvINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAG 98
Cdd:PRK07960 209 IGERGREVKDF----IEN--ILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDR-GQHVLLIMDSLTRYAMAQ 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 99 SEVSALLGRIPSAVGYQPTLATDMGTMQERITT--TKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELG 176
Cdd:PRK07960 282 REIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAG 361
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 28931 177 IYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQDIIAI 223
Cdd:PRK07960 362 HYPAIDIEASISRAM-TALIDEQHYARVRQFKQLLSSFQRNRDLVSV 407
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
15-249 |
2.62e-19 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 88.54 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 15 VFAGVGERTREGNDLYHEMIEsgvinLKDATS------KVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFI 88
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFPK-----LKDPKTgkplmeRTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYDVALMA 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 89 DNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI-------TTTKKGSITSVQAIYVPADDLTDPAPATTFAH 161
Cdd:PRK14698 760 DSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRV 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 162 LDATTVLSRAIAELGIYPAVDPLDSTSRIMDP------NIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKL 235
Cdd:PRK14698 840 VKVFWALDADLARRRHFPAINWLTSYSLYVDAvkdwwhKNVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERA 919
|
250
....*....|....*
gi 28931 236 TVSRARKIQR-FLSQ 249
Cdd:PRK14698 920 ILLVARMLREdYLQQ 934
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
15-249 |
3.69e-17 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 81.75 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 15 VFAGVGERtreGNdlyhEMIEsgVIN----LKDATSKVALvygqM----------NEPPGAR-ARVaLTGLTVAEYFRDQ 79
Cdd:PRK04192 257 IYVGCGER---GN----EMTE--VLEefpeLIDPKTGRPL----MertvliantsNMPVAAReASI-YTGITIAEYYRDM 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 80 eGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQER---ITT--TKKGSITSVQAIYVPADDLTDPa 154
Cdd:PRK04192 323 -GYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrVKTlgGEEGSVTIIGAVSPPGGDFSEP- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 155 paTTFAHLDATTV---LSRAIAELGIYPAVDPLDSTSR-------IMDPNIVG--SEHYDVARgvqKILQDYKSLQDIIA 222
Cdd:PRK04192 401 --VTQNTLRIVKVfwaLDAELADRRHFPAINWLTSYSLyldqvapWWEENVDPdwRELRDEAM---DLLQREAELQEIVR 475
|
250 260
....*....|....*....|....*...
gi 28931 223 ILGMDELSEEDKLTVSRARKI-QRFLSQ 249
Cdd:PRK04192 476 LVGPDALPEEDRLILEVARLIrEDFLQQ 503
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
15-189 |
6.49e-17 |
|
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: 79.16 E-value: 6.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 15 VFAGVGERtreGNdlyhEMIEsgVIN----LKDATS------KVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDV 84
Cdd:cd01134 106 IYVGCGER---GN----EMAE--VLEefpeLKDPITgeslmeRTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYNV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 85 LLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI-------TTTKKGSITSVQAIYVPADDLTDPAPAT 157
Cdd:cd01134 176 SLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrclgSPGREGSVTIVGAVSPPGGDFSEPVTQA 255
|
170 180 190
....*....|....*....|....*....|..
gi 28931 158 TFAHLDATTVLSRAIAELGIYPAVDPLDSTSR 189
Cdd:cd01134 256 TLRIVQVFWGLDKKLAQRRHFPSINWLISYSK 287
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
47-258 |
5.52e-16 |
|
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: 77.84 E-value: 5.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 47 KVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQ 126
Cdd:TIGR01040 212 RVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 127 ERI--TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNI----VGSEH 200
Cdd:TIGR01040 292 ERAgrVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIgegmTRKDH 371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 201 YDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQR-FLSQ-PFQVAEVFT 258
Cdd:TIGR01040 372 SDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQgPYENRTIFE 431
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
14-251 |
2.26e-14 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 73.01 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 14 SVFAGVGERTREGNDlYHEMIESGVinlkdATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFR 93
Cdd:PRK05922 186 NVIALIGERGREVRE-YIEQHKEGL-----AAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQ-GHRVLFIMDSLSR 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 94 FTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAI-YVP--ADDLTDPAPATTFAHLDATTVlSR 170
Cdd:PRK05922 259 WIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIlHYPnhPDIFTDYLKSLLDGHFFLTPQ-GK 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 171 AIAElgiyPAVDPLDSTSRiMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAiLGMDELSEEDKLtvSRARK----IQRF 246
Cdd:PRK05922 338 ALAS----PPIDILTSLSR-SARQLALPHHYAAAEELRSLLKAYHEALDIIQ-LGAYVPGQDAHL--DRAVKllpsIKQF 409
|
....*
gi 28931 247 LSQPF 251
Cdd:PRK05922 410 LSQPL 414
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
44-158 |
7.07e-08 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 53.50 E-value: 7.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 44 ATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMG 123
Cdd:PRK02118 193 ALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLA 272
|
90 100 110
....*....|....*....|....*....|....*.
gi 28931 124 TMQER-ITTTKKGSITSVQAIYVPADDLTDPAPATT 158
Cdd:PRK02118 273 SRYEKaVDFEDGGSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
51-190 |
3.35e-07 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 51.45 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28931 51 VYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERIT 130
Cdd:PRK13343 224 VVAEASDPPGLQYLAPFAGCAIAEYFRDQ-GQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAA 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28931 131 TTKK----GSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRI 190
Cdd:PRK13343 303 KLSPelggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRV 366
|
|
| |
