|
Name |
Accession |
Description |
Interval |
E-value |
| T3SS_ATP_VscN2 |
NF040574 |
type III secretion system ATPase VscN2; |
1-420 |
0e+00 |
|
type III secretion system ATPase VscN2;
Pssm-ID: 468548 Cd Length: 420 Bit Score: 831.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 1 MLNHFFKVKELYQDTVVCHVSIDTFVGQECFIHTVSGDKIRGEVMKVAQPRVEIKLLQPGAVQRGGRVEITPRRFCFPLN 80
Cdd:NF040574 1 MLQHFFKVKESYQDTVVCYVDIDTFVGQECFIHTVGDERIRGEIMKIEGHRVEIKLLQPGTIQRGAKVEITPRRFCFPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 81 EKALVGKVINCYGESLYGDDYLTQPGEFVDLPIIIEPIPLQMRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKT 160
Cdd:NF040574 81 EEALIGKVINCYGESLYGEPYLIDEGEYKDLPICIEPIPLKERAPIETVFPTKLKIIDGLFTIGEGQRLGLFAPAGAGKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 161 TTVSIMANNMEADVVIFAMIGERAREVIEFLEGEIGPEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFMEQGKKVVI 240
Cdd:NF040574 161 TTVSIMANNMDADVVIFAMIGERAREVVEFLEGEIGPEVIQKSITIVSTSEANPLEKVRSGLVAVSIARYFMEQGKKVVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 241 YFDSLTRFARAQAMLDGTPIKGGIPIGVSLALSRLVESCGNSVCGSVTGIFTVLIEKEIDDDPIAHEVKSLIDGHLVYST 320
Cdd:NF040574 241 YFDSLTRFARAQAMLDGTPIQGGIPIGVSLALSRLVESCGNSIRGSVTGIFTVLIEKEIDSDPIAHEVKSLIDGHLVYST 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 321 TIASTGRYPAIDVLKSKSRLQNKVQDKKYVRLSEQIKDMVYRYFNVELLIRVGEYEKGNDLETDKAIDLFPIVMEFLKQG 400
Cdd:NF040574 321 TIASTGRYPAIDVLKSKSRLQNKIQDKRYVQLSERIKDMVYRYFDVELLIRVGEYEKGNDLLTDEAIELYPQIMEFLKQG 400
|
410 420
....*....|....*....|
gi 518110602 401 FEGVEYEETLEAMERIWSDY 420
Cdd:NF040574 401 FDGVEYEETLENMERIWSNY 420
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
83-340 |
3.13e-126 |
|
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: 365.34 E-value: 3.13e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 83 ALVGKVINCYGESLYGDDYltqPGEFVDLPIIIEPIPLQMRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKTTT 162
Cdd:cd01136 7 GLLGRVIDALGEPLDGKGL---PDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 163 VSIMANNMEADVVIFAMIGERAREVIEFLEGEIGPEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFMEQGKKVVIYF 242
Cdd:cd01136 84 LGMIARNTDADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 243 DSLTRFARAQAMLDG----TPIKGGIPIGVSLALSRLVESCGNSVCGSVTGIFTVLIEKEIDDDPIAHEVKSLIDGHLVY 318
Cdd:cd01136 164 DSLTRFAMAQREVGLaagePPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRSILDGHIVL 243
|
250 260
....*....|....*....|..
gi 518110602 319 STTIASTGRYPAIDVLKSKSRL 340
Cdd:cd01136 244 SRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
22-416 |
4.62e-125 |
|
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: 368.59 E-value: 4.62e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 22 IDTFVGQECFIHTVSGDKIRGEVMKVAQPRVEIKLLQPGA-VQRGGRVEITPRRFCFPLNEkALVGKVINCYGESLYGDD 100
Cdd:COG1157 36 PDASIGELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEgISPGARVVPTGRPLSVPVGD-GLLGRVLDGLGRPLDGKG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 101 YLtQPGEFVdlPIIIEPIPLQMRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKTTTVSIMANNMEADVVIFAMI 180
Cdd:COG1157 115 PL-PGEERR--PLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIARNTEADVNVIALI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 181 GERAREVIEFLEGEIGPEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFMEQGKKVVIYFDSLTRFARAQ---AMLDG 257
Cdd:COG1157 192 GERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQreiGLAAG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 258 -TPIKGGIPIGVSLALSRLVESCGNSVCGSVTGIFTVLIEKeiDD--DPIAHEVKSLIDGHLVYSTTIASTGRYPAIDVL 334
Cdd:COG1157 272 ePPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEG--DDmnDPIADAVRGILDGHIVLSRKLAERGHYPAIDVL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 335 KSKSRLQNKVQDKKYVRLSEQIKDMVYRYFNVELLIRVGEYEKGNDLETDKAIDLFPIVMEFLKQGF-EGVEYEETLEAM 413
Cdd:COG1157 350 ASISRVMPDIVSPEHRALARRLRRLLARYEENEDLIRIGAYQPGSDPELDEAIALIPAIEAFLRQGMdERVSFEESLAQL 429
|
...
gi 518110602 414 ERI 416
Cdd:COG1157 430 AEL 432
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
7-418 |
1.88e-108 |
|
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP synthase F1, beta subunit. It is a mixture of members with two different protein functions. The first group is exemplified by Salmonella typhimurium FliI protein. It is needed for flagellar assembly, its ATPase activity is required for flagellation, and it may be involved in a specialized protein export pathway that proceeds without signal peptide cleavage. The second group of proteins function in the export of virulence proteins; exemplified by Yersinia sp. YscN protein an ATPase involved in the type III secretory pathway for the antihost Yops proteins. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 273401 [Multi-domain] Cd Length: 440 Bit Score: 326.64 E-value: 1.88e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 7 KVKELYQDTVVCHVSIdtfvGQECFIHTVSGD-KIRGEVMKVAQPRVEIKLLQPGA-VQRGGRVEITPRRFCFPLNEkAL 84
Cdd:TIGR01026 29 KVKGLLIEAVGPQASV----GDLCLIERRGSEgRLVAEVVGFNGEFVFLMPYEEVEgVRPGSKVLATGEGLSIKVGD-GL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 85 VGKVINCYGESLygdDYLTQPGEFVDL-PIIIEPI-PLQmRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKTTT 162
Cdd:TIGR01026 104 LGRVLDGLGKPI---DGKGKFLDNVETeGLITAPInPLK-RAPIREILSTGVRSIDGLLTVGKGQRIGIFAGSGVGKSTL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 163 VSIMANNMEADVVIFAMIGERAREVIEFLEGEIGPEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFMEQGKKVVIYF 242
Cdd:TIGR01026 180 LGMIARNTEADVNVIALIGERGREVREFIEHDLGEEGLKRSVVVVATSDQSPLLRLKGAYVATAIAEYFRDQGKDVLLLM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 243 DSLTRFARAQ---AMLDGT-PIKGGIPIGVSLALSRLVESCGNSVCGSVTGIFTVLIEKEIDDDPIAHEVKSLIDGHLVY 318
Cdd:TIGR01026 260 DSVTRFAMAQreiGLAAGEpPATKGYTPSVFSTLPRLLERAGASGKGSITAFYTVLVEGDDMNEPIADSVRGILDGHIVL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 319 STTIASTGRYPAIDVLKSKSRLQNKVQDKKYVRLSEQIKDMVYRYFNVELLIRVGEYEKGNDLETDKAIDLFPIVMEFLK 398
Cdd:TIGR01026 340 SRALAQRGHYPAIDVLASISRLMTAIVSEEHRRAARKFRELLSKYKDNEDLIRIGAYQRGSDRELDFAIAKYPKLERFLK 419
|
410 420
....*....|....*....|.
gi 518110602 399 QG-FEGVEYEETLEAMERIWS 418
Cdd:TIGR01026 420 QGiNEKVNFEESLQQLEEIFR 440
|
|
| FliI_clade2 |
TIGR03497 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
23-416 |
2.58e-104 |
|
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of bacterial flagellum systems. This protein acts to drive protein export for flagellar biosynthesis. The most closely related family is the YscN family of bacterial type III secretion systems. This model represents one (of three) segment of the FliI family tree. These have been modeled separately in order to exclude the type III secretion ATPases more effectively. [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274608 [Multi-domain] Cd Length: 413 Bit Score: 315.01 E-value: 2.58e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 23 DTFVGQECFIHTVSGDKIRGEVMKVAQPRVeikLLQP-GAVQR---GGRVEITPRRFCFPLNeKALVGKVINCYGESLYG 98
Cdd:TIGR03497 17 KASIGELCSILTKGGKPVLAEVVGFKEENV---LLMPlGEVEGigpGSLVIATGRPLAIKVG-KGLLGRVLDGLGRPLDG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 99 DDYLTQPGEFvdlPIIIEPI-PLQmRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKTTTVSIMANNMEADVVIF 177
Cdd:TIGR03497 93 EGPIIGEEPY---PLDNPPPnPLK-RPRIRDPLETGIKAIDGLLTIGKGQRVGIFAGSGVGKSTLLGMIARNAKADINVI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 178 AMIGERAREVIEFLEGEIGPEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFMEQGKKVVIYFDSLTRFARAQAMLDG 257
Cdd:TIGR03497 169 ALIGERGREVRDFIEKDLGEEGLKRSVVVVATSDQPALMRLKAAFTATAIAEYFRDQGKDVLLMMDSVTRFAMAQREIGL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 258 T----PIKGGIPIGVSLALSRLVESCGNSVCGSVTGIFTVLIEKEIDDDPIAHEVKSLIDGHLVYSTTIASTGRYPAIDV 333
Cdd:TIGR03497 249 AvgepPTTRGYTPSVFSLLPKLLERSGNSQKGSITGFYTVLVDGDDMNEPIADAVRGILDGHIVLSRELAAKNHYPAIDV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 334 LKSKSRLQNKVQDKKYVRLSEQIKDMVYRYFNVELLIRVGEYEKGNDLETDKAIDLFPIVMEFLKQGF-EGVEYEETLEA 412
Cdd:TIGR03497 329 LASVSRVMNEIVSEEHKELAGKLRELLAVYKEAEDLINIGAYKRGSNPKIDEAIRYIEKINSFLKQGIdEKFTFEETVQL 408
|
....
gi 518110602 413 MERI 416
Cdd:TIGR03497 409 LKEL 412
|
|
| FliI_clade3 |
TIGR03498 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
26-416 |
1.83e-101 |
|
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of bacterial flagellum systems. This protein acts to drive protein export for flagellar biosynthesis. The most closely related family is the YscN family of bacterial type III secretion systems. This model represents one (of three) segment of the FliI family tree. These have been modeled separately in order to exclude the type III secretion ATPases more effectively.
Pssm-ID: 163293 [Multi-domain] Cd Length: 418 Bit Score: 308.08 E-value: 1.83e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 26 VGQECFIHTVSGDKIRGEVMKVAQPRVEIKLLQPGA-VQRGGRVEITPRRFCFPLNEkALVGKVINCYGESLYGDDYLTQ 104
Cdd:TIGR03498 22 LGDRCAIRARDGRPVLAEVVGFNGDRVLLMPFEPLEgVGLGCAVFAREGPLAVRPHP-SWLGRVINALGEPIDGKGPLPQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 105 PgeFVDLPIIIEPIPLQMRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKTTTVSIMANNMEADVVIFAMIGERA 184
Cdd:TIGR03498 101 G--ERRYPLRASPPPAMSRARVGEPLDTGVRVIDTFLPLCRGQRLGIFAGSGVGKSTLLSMLARNTDADVVVIALVGERG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 185 REVIEFLEGEIGPEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFMEQGKKVVIYFDSLTRFARAQ---AMLDGTP-I 260
Cdd:TIGR03498 179 REVREFLEDDLGEEGLKRSVVVVATSDESPLMRRQAAYTATAIAEYFRDQGKDVLLLMDSVTRFAMAQreiGLAAGEPpV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 261 KGGIPIGVSLALSRLVESCGNSVC--GSVTGIFTVLIEKEIDDDPIAHEVKSLIDGHLVYSTTIASTGRYPAIDVLKSKS 338
Cdd:TIGR03498 259 ARGYTPSVFSELPRLLERAGPGAEgkGSITGIFTVLVDGDDHNEPVADAVRGILDGHIVLDRAIAERGRYPAINVLASVS 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518110602 339 RLQNKVQDKKYVRLSEQIKDMVYRYFNVELLIRVGEYEKGNDLETDKAIDLFPIVMEFLKQGF-EGVEYEETLEAMERI 416
Cdd:TIGR03498 339 RLAPRVWSPEERKLVRRLRALLARYEETEDLIRLGAYRKGSDPELDEAIRLVPKIYEFLTQGPdEPTSLQDPFADLAAI 417
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
40-416 |
1.54e-100 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 306.36 E-value: 1.54e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 40 IRGEVMKVAQPRVeikLLQPGAV----QRGGRVEITPRRFCFPLNEkALVGKVINCYGESLYGDDYLTQPGEFVDLPiii 115
Cdd:PRK06820 61 MLAEVVSIEQEMA---LLSPFASsdglRCGQWVTPLGHMHQVQVGA-DLAGRILDGLGAPIDGGPPLTGQWRELDCP--- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 116 EPIPLQmRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKTTTVSIMANNMEADVVIFAMIGERAREVIEFLEGEI 195
Cdd:PRK06820 134 PPSPLT-RQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCADSAADVMVLALIGERGREVREFLEQVL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 196 GPEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFMEQGKKVVIYFDSLTRFARAQ---AMLDG-TPIKGGIPIGVSLA 271
Cdd:PRK06820 213 TPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAreiGLAAGePPAAGSFPPSVFAN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 272 LSRLVESCGNSVCGSVTGIFTVLIEKEIDDDPIAHEVKSLIDGHLVYSTTIASTGRYPAIDVLKSKSRLQNKVQDKKYVR 351
Cdd:PRK06820 293 LPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLA 372
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518110602 352 LSEQIKDMVYRYFNVELLIRVGEYEKGNDLETDKAIDLFPIVMEFLKQ-GFEGVEYEETLEAMERI 416
Cdd:PRK06820 373 MAQKLRRMLACYQEIELLVRVGEYQAGEDLQADEALQRYPAICAFLQQdHSETAHLETTLEHLAQV 438
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
84-416 |
2.75e-93 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 287.80 E-value: 2.75e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 84 LVGKVINCYGESLYGDDYLTqPGEFvdLPIIIEPIPLQMRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKTTTV 163
Cdd:PRK06936 103 LLGRVLDGLGQPFDGGHPPE-PAAW--YPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 164 SIMANNMEADVVIFAMIGERAREVIEFLEGEIGPEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFMEQGKKVVIYFD 243
Cdd:PRK06936 180 ASLIRSAEVDVTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMD 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 244 SLTRFARAQ---AMLDGT-PIKGGIPIGVSLALSRLVESCGNSVCGSVTGIFTVLIEKEIDDDPIAHEVKSLIDGHLVYS 319
Cdd:PRK06936 260 SVTRFARAQreiGLAAGEpPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILS 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 320 TTIASTGRYPAIDVLKSKSRLQNKVQDKKYVRLSEQIKDMVYRYFNVELLIRVGEYEKGNDLETDKAIDLFPIVMEFLKQ 399
Cdd:PRK06936 340 RKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIGEYQKGQDKEADQAIERIGAIRGFLRQ 419
|
330
....*....|....*...
gi 518110602 400 GF-EGVEYEETLEAMERI 416
Cdd:PRK06936 420 GThELSHFNETLNLLETL 437
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
71-416 |
1.30e-89 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 277.65 E-value: 1.30e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 71 TPRRFCFPLNEkALVGKVINCYGESLYGDDYLTQPGEFVDL-PIIIEPIPLQMRAPIETVFPTKLKIIDGLFTIGEGQRV 149
Cdd:PRK08149 76 TGKPLSVWVGE-ALLGAVLDPTGKIVERFDAPPTVGPISEErVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 150 GLFAPAGAGKTTTVSIMANNMEADVVIFAMIGERAREVIEFLEgeigpeVIRKS------ITVVSTSEANPLEKVRSGLV 223
Cdd:PRK08149 155 GIFASAGCGKTSLMNMLIEHSEADVFVIGLIGERGREVTEFVE------SLRASsrrekcVLVYATSDFSSVDRCNAALV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 224 AVSIARHFMEQGKKVVIYFDSLTRFARA---QAMLDG-TPIKGGIPIGVSLALSRLVESCGNSVCGSVTGIFTVLIEKEI 299
Cdd:PRK08149 229 ATTVAEYFRDQGKRVVLFIDSMTRYARAlrdVALAAGeLPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEE 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 300 DDDPIAHEVKSLIDGHLVYSTTIASTGRYPAIDVLKSKSRLQNKVQDKKYVRLSEQIKDMVYRYFNVELLIRVGEYEKGN 379
Cdd:PRK08149 309 EPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGEYRRGE 388
|
330 340 350
....*....|....*....|....*....|....*...
gi 518110602 380 DLETDKAIDLFPIVMEFLKQGF-EGVEYEETLEAMERI 416
Cdd:PRK08149 389 NADNDRAMDKRPALEAFLKQDVaEKSSFSDTLERLNEF 426
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
23-413 |
2.42e-88 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 275.06 E-value: 2.42e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 23 DTFVGQECFIHTVSG--DKIRGEVMKVAQPRVeikLLQP-GAVQR---GGRVEITPRrfcfPLNEK---ALVGKVINCYG 93
Cdd:PRK07721 36 ESSIGDVCYIHTKGGgdKAIKAEVVGFKDEHV---LLMPyTEVAEiapGCLVEATGK----PLEVKvgsGLIGQVLDALG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 94 ESLygDDYLTQPGefvDLPIIIE---PIPLQmRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKTTTVSIMANNM 170
Cdd:PRK07721 109 EPL--DGSALPKG---LAPVSTDqdpPNPLK-RPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIARNT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 171 EADVVIFAMIGERAREVIEFLEGEIGPEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFMEQGKKVVIYFDSLTRFAR 250
Cdd:PRK07721 183 SADLNVIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAM 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 251 AQ---AMLDGTP--IKGGIPiGVSLALSRLVESCGNSVCGSVTGIFTVLIEKEIDDDPIAHEVKSLIDGHLVYSTTIAST 325
Cdd:PRK07721 263 AQreiGLAVGEPptTKGYTP-SVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 326 GRYPAIDVLKSKSRLQNKVQDKKYVRLSEQIKDMVYRYFNVELLIRVGEYEKGNDLETDKAIDLFPIVMEFLKQGF-EGV 404
Cdd:PRK07721 342 GQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLINIGAYKRGSSREIDEAIQFYPQIISFLKQGTdEKA 421
|
....*....
gi 518110602 405 EYEETLEAM 413
Cdd:PRK07721 422 TFEESIQAL 430
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
25-399 |
1.19e-87 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 272.98 E-value: 1.19e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 25 FVGQECFIhtvsgdKIRGEVMKVAQPRVEIKLLQP----GAVQRGGRVEITPRRFCFPLNEkALVGKVINCYGESLYGDD 100
Cdd:PRK07594 41 FMGELCCI------KPGEELAEVVGINGSKALLSPftstIGLHCGQQVMALRRRHQVPVGE-ALLGRVIDGFGRPLDGRE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 101 YLTQPGEFVDLPiiiePIPLQMRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKTTTVSIMANNMEADVVIFAMI 180
Cdd:PRK07594 114 LPDVCWKDYDAM----PPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDADSNVLVLI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 181 GERAREVIEFLEGEIGPEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFMEQGKKVVIYFDSLTRFARAQ---AMLDG 257
Cdd:PRK07594 190 GERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAreiALAAG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 258 -TPIKGGIPIGVSLALSRLVESCGNSVCGSVTGIFTVLIEKEIDDDPIAHEVKSLIDGHLVYSTTIASTGRYPAIDVLKS 336
Cdd:PRK07594 270 eTAVSGEYPPGVFSALPRLLERTGMGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLAT 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518110602 337 KSRLQNKVQDKKYVRLSEQIKDMVYRYFNVELLIRVGEYEKGNDLETDKAIDLFPIVMEFLKQ 399
Cdd:PRK07594 350 LSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEYQRGVDTDTDKAIDTYPDICTFLRQ 412
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
15-416 |
2.51e-85 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 267.40 E-value: 2.51e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 15 TVVCHVSIDTFVGQECFIHTVSGDKI-RGEVMKVAQprvEIKLLQP----GAVQRGGRVEITPRRFCFPLNEkALVGKVI 89
Cdd:PRK09099 34 TLLRVSGLDVTLGELCELRQRDGTLLqRAEVVGFSR---DVALLSPfgelGGLSRGTRVIGLGRPLSVPVGP-ALLGRVI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 90 NCYGESLYGDDyltqPGEFVDL-PIIIEPiPLQMRAP-IETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKTTTVSIMA 167
Cdd:PRK09099 110 DGLGEPIDGGG----PLDCDELvPVIAAP-PDPMSRRmVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 168 NNMEADVVIFAMIGERAREVIEFLEGEIGPEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFMEQGKKVVIYFDSLTR 247
Cdd:PRK09099 185 RGTQCDVNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 248 FARAQ---AMLDGT-PIKGGIPIGVSLALSRLVESCGNSVCGSVTGIFTVLIEKEIDDDPIAHEVKSLIDGHLVYSTTIA 323
Cdd:PRK09099 265 FARAQreiGLAAGEpPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 324 STGRYPAIDVLKSKSRLQNKVQDKKYVRLSEQIKDMVYRYFNVELLIRVGEYEKGNDLETDKAIDLFPIVMEFLKQGF-E 402
Cdd:PRK09099 345 ARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVGEYRAGSDPVADEAIAKIDAIRDFLSQRTdE 424
|
410
....*....|....
gi 518110602 403 GVEYEETLEAMERI 416
Cdd:PRK09099 425 YSDPDATLAALAEL 438
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
29-399 |
3.58e-77 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 246.45 E-value: 3.58e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 29 ECFIHTVSGDKIRGEVMKVAQPRVEIKLLQPG-------AVQRGGRVEITP-RRFCfplnekalvGKVINCYGESLYGDD 100
Cdd:PRK06002 51 DFVAIRADGGTHLGEVVRVDPDGVTVKPFEPRieiglgdAVFRKGPLRIRPdPSWK---------GRVINALGEPIDGLG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 101 YLtQPGEfVDLPIIIEPIPLQMRAPIETVFPTKLKIIDgLFT-IGEGQRVGLFAPAGAGKTTTVSIMANNMEADVVIFAM 179
Cdd:PRK06002 122 PL-APGT-RPMSIDATAPPAMTRARVETGLRTGVRVID-IFTpLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIAL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 180 IGERAREVIEFLEGEIGpEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFMEQGKKVVIYFDSLTRFARAQ---AMLD 256
Cdd:PRK06002 199 VGERGREVREFLEDTLA-DNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAArevALAA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 257 GTP-IKGGIPIGVSLALSRLVESCGNSV--CGSVTGIFTVLIEKEIDDDPIAHEVKSLIDGHLVYSTTIASTGRYPAIDV 333
Cdd:PRK06002 278 GEPpVARGYPPSVFSELPRLLERAGPGAegGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDP 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518110602 334 LKSKSRLQNKVQDKKYVRLSEQIKDMVYRYFNVELLIRVGEYEKGNDLETDKAIDLFPIVMEFLKQ 399
Cdd:PRK06002 358 LASISRLARHAWTPEQRKLVSRLKSMIARFEETRDLRLIGGYRAGSDPDLDQAVDLVPRIYEALRQ 423
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
134-338 |
1.30e-75 |
|
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: 234.17 E-value: 1.30e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 134 LKIIDGLFTIGEGQRVGLFAPAGAGKTTTVSIMANNMEADVVIFAMIGERAREVIEFLEGEIGPEVIRKSITVVSTSEAN 213
Cdd:pfam00006 2 IRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLGSGALKRTVVVVATSDEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 214 PLEKVRSGLVAVSIARHFMEQGKKVVIYFDSLTRFARAQ----AMLDGTPIKGGIPIGVSLALSRLVESCGNSVC--GSV 287
Cdd:pfam00006 82 PLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALreisLALGEPPGREGYPPSVFSLLARLLERAGRVKGkgGSI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518110602 288 TGIFTVLIEKEIDDDPIAHEVKSLIDGHLVYSTTIASTGRYPAIDVLKSKS 338
Cdd:pfam00006 162 TALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
26-400 |
1.58e-75 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 241.81 E-value: 1.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 26 VGQECFIHTVSGDKIRGEVMKVAQPRVeikLLQPGA----VQRGGRVEITPRRFCFPLNeKALVGKVINCYGESLYGDDY 101
Cdd:PRK08927 40 VGARIVVETRGGRPVPCEVVGFRGDRA---LLMPFGplegVRRGCRAVIANAAAAVRPS-RAWLGRVVNALGEPIDGKGP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 102 LTQpGEfVDLPIIIEPIPLQMRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKTTTVSIMANNMEADVVIFAMIG 181
Cdd:PRK08927 116 LPQ-GP-VPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADADVSVIGLIG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 182 ERAREVIEFLEGEIGPEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFMEQGKKVVIYFDSLTRFARAQ---AMLDGT 258
Cdd:PRK08927 194 ERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQreiGLSAGE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 259 P--IKGGIPIgVSLALSRLVESC--GNSVCGSVTGIFTVLIEKEIDDDPIAHEVKSLIDGHLVYSTTIASTGRYPAIDVL 334
Cdd:PRK08927 274 PptTKGYTPT-VFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVL 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518110602 335 KSKSRLQNKVQDKKYVRLSEQIKDMVYRYFNVELLIRVGEYEKGNDLETDKAIDLFPIVMEFLKQG 400
Cdd:PRK08927 353 KSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLGAYRAGSDPEVDEAIRLNPALEAFLRQG 418
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
26-416 |
4.36e-75 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 240.76 E-value: 4.36e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 26 VGQECFIHTVSGDkIRGEVMKVAQ------PRVEIKLLQPGAvqrggRVEitprrfcfPLNEKA-------LVGKVINCY 92
Cdd:PRK08972 46 VGSLCSIETMAGE-LEAEVVGFDGdllylmPIEELRGVLPGA-----RVT--------PLGEQSglpvgmsLLGRVIDGV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 93 GESL--YGDDYLTQPGEFVDLPIIiepiPLQmRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKTTTVSIMANNM 170
Cdd:PRK08972 112 GNPLdgLGPIYTDQRASRHSPPIN----PLS-RRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 171 EADVVIFAMIGERAREVIEFLEGEIGPEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFMEQGKKVVIYFDSLTRFAR 250
Cdd:PRK08972 187 TADVIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 251 AQ---AMLDGT-PIKGGIPIGVSLALSRLVESCGN--SVCGSVTGIFTVLIEKEIDDDPIAHEVKSLIDGHLVYSTTIAS 324
Cdd:PRK08972 267 AQreiALAVGEpPATKGYPPSVFAKLPALVERAGNggPGQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELAD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 325 TGRYPAIDVLKSKSRLQNKVQDKKYVRLSEQIKDMVYRYFNVELLIRVGEYEKGNDLETDKAIDLFPIVMEFLKQGF-EG 403
Cdd:PRK08972 347 SGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLYQQNRDLISIGAYKQGSDPRIDNAIRLQPAMNAFLQQTMkEA 426
|
410
....*....|...
gi 518110602 404 VEYEETLEAMERI 416
Cdd:PRK08972 427 VPYDMSVNMLKQL 439
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
83-416 |
1.19e-73 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 237.37 E-value: 1.19e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 83 ALVGKVINCYGESLygdDYLTQPGEFVDLPIIIEPI-PLQmRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKTT 161
Cdd:PRK07960 115 ALLGRVLDGSGKPL---DGLPAPDTGETGALITPPFnPLQ-RTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 162 TVSIMANNMEADVVIFAMIGERAREVIEFLEGEIGPEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFMEQGKKVVIY 241
Cdd:PRK07960 191 LLGMMARYTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 242 FDSLTRFARAQ---AMLDGT-PIKGGIPIGVSLALSRLVESCGNSVC--GSVTGIFTVLIEKEIDDDPIAHEVKSLIDGH 315
Cdd:PRK07960 271 MDSLTRYAMAQreiALAIGEpPATKGYPPSVFAKLPALVERAGNGISggGSITAFYTVLTEGDDQQDPIADSARAILDGH 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 316 LVYSTTIASTGRYPAIDVLKSKSRLQNKVQDKKYVRLSEQIKDMVYRYFNVELLIRVGEYEKGNDLETDKAIDLFPIVME 395
Cdd:PRK07960 351 IVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAIALWPQLEA 430
|
330 340
....*....|....*....|..
gi 518110602 396 FLKQG-FEGVEYEETLEAMERI 416
Cdd:PRK07960 431 FLQQGiFERADWEDSLQALERI 452
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
26-416 |
1.58e-73 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 236.94 E-value: 1.58e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 26 VGQECFI---HTVSGDKIRGEVMKVAQPRV------EIKLLQPGA----VQRGGRVEITPrrfcfplnekALVGKVINCY 92
Cdd:PRK05688 48 VGSRCLVindDSYHPVQVEAEVMGFSGDKVflmpvgSVAGIAPGArvvpLADTGRLPMGM----------SMLGRVLDGA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 93 GESLYGDDYLtQPGEFVDL-PIIIEPIPlqmRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKTTTVSIMANNME 171
Cdd:PRK05688 118 GRALDGKGPM-KAEDWVPMdGPTINPLN---RHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 172 ADVVIFAMIGERAREVIEFLEGEIGPEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFMEQGKKVVIYFDSLTRFARA 251
Cdd:PRK05688 194 ADIIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 252 Q---AMLDGT-PIKGGIPIGVSLALSRLVESCGNSVC--GSVTGIFTVLIEKEIDDDPIAHEVKSLIDGHLVYSTTIAST 325
Cdd:PRK05688 274 QreiALAIGEpPATKGYPPSVFAKLPKLVERAGNAEPggGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 326 GRYPAIDVLKSKSRLQNKVQDKKYVRLSEQIKDMVYRYFNVELLIRVGEYEKGNDLETDKAIDLFPIVMEFLKQGF-EGV 404
Cdd:PRK05688 354 GHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPHLVQFLRQGLrENV 433
|
410
....*....|..
gi 518110602 405 EYEETLEAMERI 416
Cdd:PRK05688 434 SLAQSREQLAAI 445
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
26-418 |
7.73e-72 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 232.09 E-value: 7.73e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 26 VGQECFIHTVSGDKIRGEVMKVaqpRVEIKLL----QPGAVQRGGRVEITPRRFCFPLNEKALvGKVINCYGESLYGDDY 101
Cdd:PRK07196 38 IGQRCRIESVDETFIEAQVVGF---DRDITYLmpfkHPGGVLGGARVFPSEQDGELLIGDSWL-GRVINGLGEPLDGKGQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 102 LTQPGEFVDLPIIIEPIplqMRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKTTTVSIMANNMEADVVIFAMIG 181
Cdd:PRK07196 114 LGGSTPLQQQLPQIHPL---QRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQADVVVVGLIG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 182 ERAREVIEFLEGEIGPEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFMEQGKKVVIYFDSLTRFARAQA----MLDG 257
Cdd:PRK07196 191 ERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQReialSLGE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 258 TPIKGGIPIGVSLALSRLVESCGNSV-CGSVTGIFTVLIEKEIDDDPIAHEVKSLIDGHLVYSTTIASTGRYPAIDVLKS 336
Cdd:PRK07196 271 PPATKGYPPSAFSIIPRLAESAGNSSgNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQS 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 337 KSRLQNKVQDKKYVRLSEQIKDMVYRYFNVELLIRVGEYEKGNDLETDKAIDLFPIVMEFLKQGF-EGVEYEETLEAMER 415
Cdd:PRK07196 351 ISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVAGADPMADQAVHYYPAITQFLRQEVgHPALFSASVEQLTG 430
|
...
gi 518110602 416 IWS 418
Cdd:PRK07196 431 MFP 433
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
65-416 |
9.28e-69 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 224.18 E-value: 9.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 65 GGRVEITPRRFCFPLNEKaLVGKVINCYGESL--YGDDYLTQpgefvDLPIIIEPIPLQMRAPIETVFPTKLKIIDGLFT 142
Cdd:PRK08472 80 GDKVFISKEGLNIPVGRN-LLGRVVDPLGRPIdgKGAIDYER-----YAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLT 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 143 IGEGQRVGLFAPAGAGKTTTVSIMANNMEADVVIFAMIGERAREVIEFLEGEIGPEvIRKSITVVSTSEANPLEKVRSGL 222
Cdd:PRK08472 154 CGKGQKLGIFAGSGVGKSTLMGMIVKGCLAPIKVVALIGERGREIPEFIEKNLGGD-LENTVIVVATSDDSPLMRKYGAF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 223 VAVSIARHFMEQGKKVVIYFDSLTRFARAQA----MLDGTPIKGGIPIGVSLALSRLVESCGNSVC-GSVTGIFTVLIEK 297
Cdd:PRK08472 233 CAMSVAEYFKNQGLDVLFIMDSVTRFAMAQReiglALGEPPTSKGYPPSVLSLLPQLMERAGKEEGkGSITAFFTVLVEG 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 298 EIDDDPIAHEVKSLIDGHLVYSTTIASTGRYPAIDVLKSKSRLQNKVQDK-------KYVRLSEQIKDMvyryfnvELLI 370
Cdd:PRK08472 313 DDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPehklaarKFKRLYSLLKEN-------EVLI 385
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 518110602 371 RVGEYEKGNDLETDKAIDLFPIVMEFLKQGF-EGVEYEETLEAMERI 416
Cdd:PRK08472 386 RIGAYQKGNDKELDEAISKKEFMEQFLKQNPnELFPFEQTFEQLEEI 432
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
58-416 |
9.63e-66 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 216.38 E-value: 9.63e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 58 QPGAVQRGGRVEITPRRFCFPLNEKaLVGKVINCYGEslygddYLTQPGEFVDL---PIIIEPIPLQMRAPIETVFPTKL 134
Cdd:PRK06793 72 QTEKVCYGDSVTLIAEDVVIPRGNH-LLGKVLSANGE------VLNEEAENIPLqkiKLDAPPIHAFEREEITDVFETGI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 135 KIIDGLFTIGEGQRVGLFAPAGAGKTTTVSIMANNMEADVVIFAMIGERAREVIEFLEGEIGPEVIRKSITVVSTSEANP 214
Cdd:PRK06793 145 KSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESH 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 215 LEKVRSGLVAVSIARHFMEQGKKVVIYFDSLTRFARAQAMLD----GTPIkGGIPIGVSLALSRLVESCGNSVCGSVTGI 290
Cdd:PRK06793 225 LMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDiavkELPI-GGKTLLMESYMKKLLERSGKTQKGSITGI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 291 FTVLIEKEIDDDPIAHEVKSLIDGHLVYSTTIASTGRYPAIDVLKSKSRLQNKVQDKKYVRLSEQIKDMVYRYFNVELLI 370
Cdd:PRK06793 304 YTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYF 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 518110602 371 RVGEYEKGND----LETDKAIDLfpiVMEFLKQG-FEGVEYEETLEAMERI 416
Cdd:PRK06793 384 KLGTIQENAEnayiFECKNKVEG---INTFLKQGrSDSFQFDDIVEAMHHI 431
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
83-340 |
3.57e-50 |
|
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: 170.71 E-value: 3.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 83 ALVGKVINCYGESLygdDYLTQPGEFVDLPIIIEPIPLQMRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKTTT 162
Cdd:cd19476 7 ELLGRILDGLGEPL---DGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 163 VSIMANNM---EADVVIFAMIGERAREVIEFLEGEIGPEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFMEQGKKVV 239
Cdd:cd19476 84 AMQLARNQakaHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 240 IYFDSLTRFARAQ----AMLDGTPIKGGIPIGVSLALSRLVESCGNSVC--GSVTGIFTVLIEKEIDDDPIAHEVKSLID 313
Cdd:cd19476 164 LIIDDISRYAEALremsALLGEPPGREGYPPYLFTKLATLYERAGKVKDggGSITAIPAVSTPGDDLTDPIPDNTFAILD 243
|
250 260
....*....|....*....|....*..
gi 518110602 314 GHLVYSTTIASTGRYPAIDVLKSKSRL 340
Cdd:cd19476 244 GQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
26-416 |
5.81e-50 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 174.71 E-value: 5.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 26 VGQECFIHTVSGDKIRGEVMKVAQPRVEIKLLQP-GAVQRGGRVEITPRRFCFPLNEKaLVGKVINCYGESLYGDDYLTQ 104
Cdd:PRK05922 40 LGELCQISLSKSPPILAEVIGFHNRTTLLMSLSPiHYVALGAEVLPLRRPPSLHLSDH-LLGRVLDGFGNPLDGKEQLPK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 105 pgefVDLPIIIEPIPLQM-RAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKTTTVSIMANNMEADVVIFAMIGER 183
Cdd:PRK05922 119 ----THLKPLFSSPPSPMsRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKGSKSTINVIALIGER 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 184 AREVIEFLEGEIGPEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFMEQGKKVVIYFDSLTRFARAQ---AMLDGTPI 260
Cdd:PRK05922 195 GREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALqevALARGETL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 261 KG-GIPIGVSLALSRLVESCGNSVCGSVTGIFTVLIEKEiDDDPIAHEVKSLIDGHLvYSTTIASTGRYPAIDVLKSKSR 339
Cdd:PRK05922 275 SAhHYAASVFHHVSEFTERAGNNDKGSITALYAILHYPN-HPDIFTDYLKSLLDGHF-FLTPQGKALASPPIDILTSLSR 352
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518110602 340 LQNKVQDKKYVRLSEQIKDMVYRYFNVELLIRVGEYEKGNDLETDKAIDLFPIVMEFLKQGFEGVEY-EETLEAMERI 416
Cdd:PRK05922 353 SARQLALPHHYAAAEELRSLLKAYHEALDIIQLGAYVPGQDAHLDRAVKLLPSIKQFLSQPLSSYCAlHNTLKQLEAL 430
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
35-363 |
2.82e-23 |
|
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: 101.33 E-value: 2.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 35 VSGDKIRGEVMKVAQ----PRVEIKLLQPG-AVQRGGRVEITPRRFCFPLNEKALvGKVINCYGESLYGDDYLtqpGEFV 109
Cdd:TIGR01039 31 VQNRAESELTLEVAQhlgdDTVRTIAMGSTdGLVRGLEVIDTGAPISVPVGKETL-GRIFNVLGEPIDEKGPI---PAKE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 110 DLPIIIEPIPLQMRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKTTTVSIMANNM---EADVVIFAMIGERARE 186
Cdd:TIGR01039 107 RWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIakeHGGYSVFAGVGERTRE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 187 VIEFLEGEIGPEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFM-EQGKKVVIYFDSLTRFarAQAMLDGTPIKGGIP 265
Cdd:TIGR01039 187 GNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRdEQGQDVLLFIDNIFRF--TQAGSEVSALLGRMP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 266 IGV----SLA--LSRLVESCGNSVCGSVTGIFTVLIEKEIDDDPIAHEVKSLIDGHLVYSTTIASTGRYPAIDVLKSKSR 339
Cdd:TIGR01039 265 SAVgyqpTLAteMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSR 344
|
330 340
....*....|....*....|....*
gi 518110602 340 -LQNKVQDKKYVRLSEQIKDMVYRY 363
Cdd:TIGR01039 345 lLDPSVVGEEHYDVARGVQQILQRY 369
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
38-399 |
3.71e-21 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 95.37 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 38 DKIRGEVMKVAQPRVEIKLLQP-GAVQRGGRVEITPRRFCFPLNEkALVGKVINCYGESLYGDdyltqpgefvdlpiiiE 116
Cdd:PRK13343 57 GGSRGFAFNLEEELVGAVLLDDtADILAGTEVRRTGRVLEVPVGD-GLLGRVIDPLGRPLDGG----------------G 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 117 PIPLQMRAPIETVFP-------------TKLKIIDGLFTIGEGQRVGLFAPAGAGKTT-TVSIMANNMEADVV-IFAMIG 181
Cdd:PRK13343 120 PLQATARRPLERPAPaiierdfvteplqTGIKVVDALIPIGRGQRELIIGDRQTGKTAiAIDAIINQKDSDVIcVYVAIG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 182 ERA---REVIEFLEGEIGPEvirKSITVVSTSEANPlekvrsGL------VAVSIARHFMEQGKKVVIYFDSLTRFARA- 251
Cdd:PRK13343 200 QKAsavARVIETLREHGALE---YTTVVVAEASDPP------GLqylapfAGCAIAEYFRDQGQDALIVYDDLSKHAAAy 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 252 ---QAMLDGTPIKGGIPIGVSLALSRLVEscgNSVC-------GSVTGIftVLIEKEIDDDP--IAHEVKSLIDGHLVYS 319
Cdd:PRK13343 271 relSLLLRRPPGREAYPGDIFYLHSRLLE---RAAKlspelggGSLTAL--PIIETLAGELSayIPTNLISITDGQIYLD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 320 TTIASTGRYPAIDVLKSKSRLQNKVQDKKYVRLSEQIKDMVYRYFNVELLIRVgeyekGNDLE--TDKAIDLFPIVMEFL 397
Cdd:PRK13343 346 SDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRF-----GGLLDagTQKQITRGRRLRELL 420
|
..
gi 518110602 398 KQ 399
Cdd:PRK13343 421 KQ 422
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
82-340 |
5.89e-21 |
|
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: 91.90 E-value: 5.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 82 KALVGKVINCYGESLygdDYLTQPGEFVDLPIIIEPIPLQMRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKTT 161
Cdd:cd01133 6 EETLGRIFNVLGEPI---DERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 162 TVSIMANN---MEADVVIFAMIGERAREVIEFLE-----GEIGPEVIRKSITVVSTSEANPLEKVRSGLVAVSIARHFM- 232
Cdd:cd01133 83 LIMELINNiakAHGGYSVFAGVGERTREGNDLYHemkesGVINLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYFRd 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 233 EQGKKVVIYFDSLTRFARA----QAMLdgtpikGGIPIGV----SLA--LSRLVESCGNSVCGSVTGIFTVLIEKeiDD- 301
Cdd:cd01133 163 EEGQDVLLFIDNIFRFTQAgsevSALL------GRIPSAVgyqpTLAteMGSLQERITSTKKGSITSVQAVYVPA--DDl 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 518110602 302 -DPIAHEVKSLIDGHLVYSTTIASTGRYPAIDVLKSKSRL 340
Cdd:cd01133 235 tDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
57-339 |
2.34e-20 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 92.07 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 57 LQPGAVQRGgrvEITPRRFCFPLNEKalvgkvincygESLYGDDyltqPGEFVDLPIIIEPIPLQMRAPIETVFPTK--- 133
Cdd:PRK12608 59 LRTGDVVEG---VARPRERYRVLVRV-----------DSVNGTD----PEKLARRPHFDDLTPLHPRERLRLETGSDdls 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 134 LKIIDGLFTIGEGQRVGLFAPAGAGKTTTV-----SIMANNMEADVVIFaMIGERAREVIEFlEGEIGPEVIrksitvVS 208
Cdd:PRK12608 121 MRVVDLVAPIGKGQRGLIVAPPRAGKTVLLqqiaaAVAANHPEVHLMVL-LIDERPEEVTDM-RRSVKGEVY------AS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 209 TSEANPLEKVRSGLVAVSIARHFMEQGKKVVIYFDSLTRFARA---QAMLDGTPIKGGIPIGVSLALSRLVESCGN-SVC 284
Cdd:PRK12608 193 TFDRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAynnEVESSGRTLSGGVDARALQRPKRLFGAARNiEEG 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 518110602 285 GSVTGIFTVLIEK-EIDDDPIAHEVKSLIDGHLVYSTTIASTGRYPAIDVLKSKSR 339
Cdd:PRK12608 273 GSLTIIATALVDTgSRMDEVIFEEFKGTGNMEIVLDRELADKRVFPAIDIAKSGTR 328
|
|
| ATP-synt_flagellum-secretory_path_III_C |
cd18114 |
Flagellum-specific ATP synthase, C-terminal domain; The C-terminal domain of the ... |
351-418 |
7.64e-20 |
|
Flagellum-specific ATP synthase, C-terminal domain; The C-terminal domain of the 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 flagellum-specific ATPase FliI is the soluble export component that drives flagellar protein export, and it shows extensive similarity to the alpha and beta subunits of FoF1-ATP synthase. Although they both are proton driven rotary molecular devices, 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: 349749 [Multi-domain] Cd Length: 71 Bit Score: 83.04 E-value: 7.64e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 351 RLSEQIKDMVYRYFN-VELLIRVGEYEKGNDLETDKAIDLFPIVMEFLKQG-FEGVEYEETLEAMERIWS 418
Cdd:cd18114 2 YLAARKFRELMSTYQeNEDLIRIGAYKKGSDPEVDEAIRLKPQIEAFLKQGlNEKAPLEESLQQLEEIFG 71
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
346-413 |
8.74e-18 |
|
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family of ATPases that form part of the Type III secretion system (T3SS) present in Escherichia coli. T3SS is a macromolecular complex that creates a syringe-like apparatus extending from the bacterial cytosol across three membranes to the eukaryotic cytosol. This process is essential for pathogenicity. EscN is a functionally unique ATPase that provides an inner-membrane recognition gate for the T3SS chaperone-virulence effector complexes as well as a potential source of energy for their subsequent secretion.The C-terminal domain of T3SS ATPases mediates binding with multiple contact points along the chaperone.
Pssm-ID: 465691 [Multi-domain] Cd Length: 70 Bit Score: 77.09 E-value: 8.74e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518110602 346 DKKYVRLSEQIKDMVYRYFNVELLIRVGEYEKGNDLETDKAIDLFPIVMEFLKQGF-EGVEYEETLEAM 413
Cdd:pfam18269 2 SPEHLQAARRLRELLATYQENEDLIRIGAYQAGSDPEIDEAIAKRPAINAFLRQGVdEPVSFEETLAQL 70
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
135-339 |
9.48e-18 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 82.25 E-value: 9.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 135 KIIDGLFTIGEGQRVGLFAPAGAGKTT-----TVSIMANNMEADVVIFaMIGERAREVIEFLEgEIGPEVIrksitvVST 209
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTllqniANAIAKNHPEVELIVL-LIDERPEEVTDMRR-SVKGEVV------AST 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 210 SEANPLEKVRSGLVAVSIARHFMEQGKKVVIYFDSLTRFARAQAMLD---GTPIKGGIPIGvslAL---------SRLVE 277
Cdd:cd01128 77 FDEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVpssGKTLSGGVDAN---ALhkpkrffgaARNIE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518110602 278 ScgnsvCGSVTGIFTVLIEKEID-DDPIAHEVKSLIDGHLVYSTTIASTGRYPAIDVLKSKSR 339
Cdd:cd01128 154 E-----GGSLTIIATALVDTGSRmDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTR 211
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
135-339 |
3.37e-16 |
|
transcription termination factor Rho; This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding. [Transcription, Transcription factors]
Pssm-ID: 162030 [Multi-domain] Cd Length: 415 Bit Score: 79.73 E-value: 3.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 135 KIIDGLFTIGEGQRVGLFAPAGAGKTTTV-----SIMANNMEADVVIFaMIGERAREVIEfLEGEIGPEVirksitVVST 209
Cdd:TIGR00767 157 RVLDLFAPIGKGQRGLIVAPPKAGKTVLLqkiaqAITRNHPEVELIVL-LIDERPEEVTD-MQRSVKGEV------VAST 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 210 SEANPLEKVRSGLVAVSIARHFMEQGKKVVIYFDSLTRFARA--QAM-LDGTPIKGGIPigvSLAL---------SRLVE 277
Cdd:TIGR00767 229 FDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAynTVTpASGKVLSGGVD---ANALhrpkrffgaARNIE 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518110602 278 ScgnsvCGSVTGIFTVLIEK-EIDDDPIAHEVKSLIDGHLVYSTTIASTGRYPAIDVLKSKSR 339
Cdd:TIGR00767 306 E-----GGSLTIIATALIDTgSRMDEVIFEEFKGTGNMELHLDRKLADRRIFPAIDIKKSGTR 363
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
62-340 |
2.34e-14 |
|
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: 74.36 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 62 VQRGGRVEITPRRFCFPLNEKALvGKVINCYGESLygdDYLTQPGEFVDLPIIIEPIPLQMRAPIETVFPTKLKIIDGLF 141
Cdd:COG0055 66 LVRGMEVIDTGAPISVPVGEATL-GRIFNVLGEPI---DGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 142 TIGEGQRVGLFAPAGAGKTTTVSIMANNMEAD---VVIFAMIGERAREVIEFLEGEIGPEVIRKSITVVSTSEANPLEKV 218
Cdd:COG0055 142 PYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEhggVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 219 RSGLVAVSIARHFM-EQGKKVVIYFDSLTRFARA----QAMLdgtpikGGIPIGV----SLA--LSRLVESCGNSVCGSV 287
Cdd:COG0055 222 RVALTALTMAEYFRdEEGQDVLLFIDNIFRFTQAgsevSALL------GRMPSAVgyqpTLAteMGALQERITSTKKGSI 295
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 518110602 288 TGIFTVLIEKeiDD--DPIAHEVKSLIDGHLVYSTTIASTGRYPAIDVLKSKSRL 340
Cdd:COG0055 296 TSVQAVYVPA--DDltDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRI 348
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
86-363 |
4.38e-14 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 73.85 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 86 GKVINCYGESLYGDDYLTQPGEFVDL--PIIIEPIPLQMRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAGAGKT-TT 162
Cdd:PRK07165 81 GKIIDIDGNIIYPEAQNPLSKKFLPNtsSIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKThIA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 163 VSIMANNMEADV-VIFAMIGERAREVIEFLEGEIGPEVIRKSItVVSTSEANPLEKVRSGLVAVSIARHFMeQGKKVVIY 241
Cdd:PRK07165 161 LNTIINQKNTNVkCIYVAIGQKRENLSRIYETLKEHDALKNTI-IIDAPSTSPYEQYLAPYVAMAHAENIS-YNDDVLIV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 242 FDSLTRFA---RAQAMLDGTPI-KGGIPIGVSLALSRLVESCGNSVCG-SVTGIftvLIEKEIDDDP---IAHEVKSLID 313
Cdd:PRK07165 239 FDDLTKHAniyREIALLTNKPVgKEAFPGDMFFAHSKLLERAGKFKNRkTITAL---PILQTVDNDItslISSNIISITD 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 518110602 314 GHLVYSTTIASTGRYPAIDVLKSKSRLQNKVQDKKYVRLSEQIKDMVYRY 363
Cdd:PRK07165 316 GQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAY 365
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
63-370 |
8.25e-14 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 72.77 E-value: 8.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 63 QRGGRVEITPRRFCFPLNEKALvGKVINCYGESLygdDYLTQPGEFVDLPIiiepiplQMRAP----IET---VFPTKLK 135
Cdd:CHL00060 82 MRGMEVIDTGAPLSVPVGGATL-GRIFNVLGEPV---DNLGPVDTRTTSPI-------HRSAPafiqLDTklsIFETGIK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 136 IIDGLFTIGEGQRVGLFAPAGAGKttTVSIMA--NNM---EADVVIFAMIGERARE----VIEFLE-GEIGPEVIRKSIT 205
Cdd:CHL00060 151 VVDLLAPYRRGGKIGLFGGAGVGK--TVLIMEliNNIakaHGGVSVFGGVGERTREgndlYMEMKEsGVINEQNIAESKV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 206 VVSTSEAN--PLEKVRSGLVAVSIARHFMEQGKKVVIYF-DSLTRFARA----QAMLDGTPIKGGIPIGVSLALSRLVES 278
Cdd:CHL00060 229 ALVYGQMNepPGARMRVGLTALTMAEYFRDVNKQDVLLFiDNIFRFVQAgsevSALLGRMPSAVGYQPTLSTEMGSLQER 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 279 CGNSVCGSVTGIFTVLIEKeiDD--DP-----IAHevkslIDGHLVYSTTIASTGRYPAIDVLKSKSR-LQNKVQDKKYV 350
Cdd:CHL00060 309 ITSTKEGSITSIQAVYVPA--DDltDPapattFAH-----LDATTVLSRGLAAKGIYPAVDPLDSTSTmLQPRIVGEEHY 381
|
330 340
....*....|....*....|
gi 518110602 351 RLSEQIKDMVYRYFNVELLI 370
Cdd:CHL00060 382 ETAQRVKQTLQRYKELQDII 401
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
117-339 |
1.64e-11 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 65.55 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 117 PIPLQMRAPIETVFPTKL--KIIDgLFT-IGEGQRVGLFAPAGAGKTTTV-----SIMANNMEADVVIFaMIGERAREVI 188
Cdd:PRK09376 138 PLYPNERLRLETGNPEDLstRIID-LIApIGKGQRGLIVAPPKAGKTVLLqnianSITTNHPEVHLIVL-LIDERPEEVT 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 189 EF---LEGEIgpevirksitVVSTSEANPLEKVRSGLVAVSIARHFMEQGKKVVIYFDSLTRFARAQAML---DGTPIKG 262
Cdd:PRK09376 216 DMqrsVKGEV----------VASTFDEPAERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVvpsSGKVLSG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 263 GIPIGvslAL---------SRLVEScGnsvcGSVTGIFTVLIEKEID-DDPIAHEVKSLIDGHLVYSTTIASTGRYPAID 332
Cdd:PRK09376 286 GVDAN---ALhrpkrffgaARNIEE-G----GSLTIIATALIDTGSRmDEVIFEEFKGTGNMELHLDRKLAEKRIFPAID 357
|
....*..
gi 518110602 333 VLKSKSR 339
Cdd:PRK09376 358 INRSGTR 364
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
117-293 |
8.91e-10 |
|
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: 59.13 E-value: 8.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 117 PIPLQMRAPIETVFPTKLKIIDGLFTIGEGqrvGLFA---PAGAGKTTTVSIMANNMEADVVIFAMIGERAREVIEFLEG 193
Cdd:cd01134 47 PRPVKEKLPPNVPLLTGQRVLDTLFPVAKG---GTAAipgPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEVLEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 194 --EIGPEVIRKSI---TV---------VSTSEAnplekvrSGLVAVSIARHFMEQGKKVVIYFDSLTRFARA----QAML 255
Cdd:cd01134 124 fpELKDPITGESLmerTVliantsnmpVAAREA-------SIYTGITIAEYFRDMGYNVSLMADSTSRWAEAlreiSGRL 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518110602 256 DGTPIKGGIPIGVSLALSRLVESCGNSVC-------GSVTGIFTV 293
Cdd:cd01134 197 EEMPAEEGYPAYLGARLAEFYERAGRVRClgspgreGSVTIVGAV 241
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
117-254 |
3.51e-09 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 58.64 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 117 PIPLQMRAPIETVFPTKLKIIDGLFTIGEGqrvGLFA---PAGAGKTTTVSIMANNMEADVVIFAMIGERAREVIEFLEG 193
Cdd:PRK04192 198 PRPYKEKLPPVEPLITGQRVIDTFFPVAKG---GTAAipgPFGSGKTVTQHQLAKWADADIVIYVGCGERGNEMTEVLEE 274
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518110602 194 eiGPEVI---------RKSITVVSTS-------EAnplekvrSGLVAVSIARHFMEQGKKVVIYFDSLTRFarAQAM 254
Cdd:PRK04192 275 --FPELIdpktgrplmERTVLIANTSnmpvaarEA-------SIYTGITIAEYYRDMGYDVLLMADSTSRW--AEAL 340
|
|
| Rho |
COG1158 |
Transcription termination factor Rho [Transcription]; |
136-251 |
3.63e-09 |
|
Transcription termination factor Rho [Transcription];
Pssm-ID: 440772 [Multi-domain] Cd Length: 373 Bit Score: 58.12 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 136 IIDgLFT-IGEGQRvGLF-APAGAGKTTTV-----SIMANNMEAdVVIFAMIGERAREVIEF---LEGEIgpevirksit 205
Cdd:COG1158 114 VID-LVApIGKGQR-GLIvAPPKAGKTTLLqdianAITANHPEV-HLIVLLIDERPEEVTDMqrsVKGEV---------- 180
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 518110602 206 VVSTSEANPLEKVR-SGLVavsI--ARHFMEQGKKVVIYFDSLTRFARA 251
Cdd:COG1158 181 IASTFDEPAERHVQvAELV---IerAKRLVELGKDVVILLDSITRLARA 226
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
62-363 |
8.75e-09 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 57.36 E-value: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 62 VQRGGRVEITPRRFCFPLNEKALvGKVINCYGESLyGDDYLTQPGEFVDLPIIIEPIP-----LQMRAPIETVFPTKLKI 136
Cdd:PTZ00185 102 VQSGQKVMATGKLLYIPVGAGVL-GKVVNPLGHEV-PVGLLTRSRALLESEQTLGKVDagapnIVSRSPVNYNLLTGFKA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 137 IDGLFTIGEGQRVGLFAPAGAGKTT-TVSIMANNMEAD---------VVIFAMIGERAREVIEFLEGEIGPEVIRKSITV 206
Cdd:PTZ00185 180 VDTMIPIGRGQRELIVGDRQTGKTSiAVSTIINQVRINqqilsknavISIYVSIGQRCSNVARIHRLLRSYGALRYTTVM 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 207 VSTSEANPLEKVRSGLVAVSIARHFMEQGKKVVIYFDSLTRFARA----QAMLDGTPIKGGIPIGVSLALSRLVESCGNS 282
Cdd:PTZ00185 260 AATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAyrqiSLLLRRPPGREAYPGDVFYLHSRLLERAAML 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 283 VCGSVTGIFTVL-IEKEIDDDPIAH---EVKSLIDGHLVYSTTIASTGRYPAIDVLKSKSRLQNKVQDKKYVRLSEQIKD 358
Cdd:PTZ00185 340 SPGKGGGSVTALpIVETLSNDVTAYivtNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAMKAVAGKLKG 419
|
....*
gi 518110602 359 MVYRY 363
Cdd:PTZ00185 420 ILAEY 424
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
84-344 |
9.06e-09 |
|
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: 56.08 E-value: 9.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 84 LVGKVINCYGESL-YGDDYLtqPGEFVDlpIIIEPIPLQMRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAG------ 156
Cdd:cd01135 10 MLGRIFNGSGKPIdGGPPIL--PEDYLD--INGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGlphnel 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 157 ----AGKTTTVsimaNNMEADVVIFAMIG---ERAREVIEFLEgEIGpeVIRKSITVVSTSEANPLEKVRSGLVAVSIAR 229
Cdd:cd01135 86 aaqiARQAGVV----GSEENFAIVFAAMGvtmEEARFFKDDFE-ETG--ALERVVLFLNLANDPTIERIITPRMALTTAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 230 HF-MEQGKKVVIYFDSLTRFARA----QAMLDGTPIKGGIPIGVSLALSRLVESCGN--SVCGSVTgIFTVLIekeIDDD 302
Cdd:cd01135 159 YLaYEKGKHVLVILTDMTNYAEAlrevSAAREEVPGRRGYPGYMYTDLATIYERAGRveGRKGSIT-QIPILT---MPND 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 518110602 303 PIAHEVKSL----IDGHLVYSTTIASTGRYPAIDVLKSKSRLQNKV 344
Cdd:cd01135 235 DITHPIPDLtgyiTEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSG 280
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
149-415 |
5.17e-07 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 51.95 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 149 VGLFAPAGAGKTTTVSIMANNMEADVVIFAMIGERAREVIEFLEG-------EIGPEVIRKSITVVSTSEANPLEKVRSG 221
Cdd:PRK14698 659 IGGNMPTLLHNTVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEfpklkdpKTGKPLMERTVLIANTSNMPVAAREASI 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 222 LVAVSIARHFMEQGKKVVIYFDSLTRFARA----QAMLDGTPIKGGIPIGVSLALSRLVESCGNSV-------CGSVTGI 290
Cdd:PRK14698 739 YTGITIAEYFRDMGYDVALMADSTSRWAEAlreiSGRLEEMPGEEGYPAYLASKLAEFYERAGRVVtlgsdyrVGSVSVI 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 291 FTVLIEKEIDDDPIAHEVKSLIDGHLVYSTTIASTGRYPAIDVLKSKSRLQNKVQDKKYVRLSEQIKDMvyRYFNVELLI 370
Cdd:PRK14698 819 GAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNVDPEWKAM--RDKAMELLQ 896
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518110602 371 RVGEYEK-----GNDL--ETDKAIDLFPIVM--EFLKQ-GFEGVE------------------YEETLEAMER 415
Cdd:PRK14698 897 KEAELQEivrivGPDAlpERERAILLVARMLreDYLQQdAFDEVDtycppekqvtmmrvllnfYDKTMDAISR 969
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
133-173 |
7.02e-06 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 46.24 E-value: 7.02e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 518110602 133 KLKIIDGL-FTIGEGQRVGLFAPAGAGKTTTVSIMANNMEAD 173
Cdd:cd03230 12 KKTALDDIsLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD 53
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
32-411 |
8.77e-06 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 47.90 E-value: 8.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 32 IHTVSGDKIRGEVMKVAQPRVEIKLLQ--PGAVQRGGRVEITPRRFCFPLNEKaLVGKVINCYGESLYGDDYLTqPGEFV 109
Cdd:PRK04196 31 IELPNGEKRRGQVLEVSEDKAVVQVFEgtTGLDLKDTKVRFTGEPLKLPVSED-MLGRIFDGLGRPIDGGPEII-PEKRL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 110 DlpIIIEPIPLQMRAPIETVFPTKLKIIDGLFTIGEGQRVGLFAPAG------AGKTTTVSIMANNMEADVVIFAMIG-- 181
Cdd:PRK04196 109 D--INGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGlphnelAAQIARQAKVLGEEENFAVVFAAMGit 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 182 -ERAREVIEFLEgEIGpeVIRKSITVVSTSEANPLEKVRSGLVAVSIARHF-MEQGKKV-VIYFDsLTRFARA----QAM 254
Cdd:PRK04196 187 fEEANFFMEDFE-ETG--ALERSVVFLNLADDPAIERILTPRMALTAAEYLaFEKGMHVlVILTD-MTNYCEAlreiSAA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 255 LDGTPIKGGIPIGVSLALSRLVESCG--NSVCGSVTGIfTVLIekeIDDDPIAHEVKSL----IDGHLVYSTTIASTGRY 328
Cdd:PRK04196 263 REEVPGRRGYPGYMYTDLATIYERAGriKGKKGSITQI-PILT---MPDDDITHPIPDLtgyiTEGQIVLSRELHRKGIY 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 329 PAIDVLKSKSRLQNKVQDKKYVR-LSEQIKDMVYR-YFNV----ELLIRVGEYEKGndlETDKAI----DLFPivMEFLK 398
Cdd:PRK04196 339 PPIDVLPSLSRLMKDGIGEGKTReDHKDVANQLYAaYARGkdlrELAAIVGEEALS---ERDRKYlkfaDAFE--REFVN 413
|
410
....*....|....
gi 518110602 399 QGF-EGVEYEETLE 411
Cdd:PRK04196 414 QGFdENRSIEETLD 427
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
146-313 |
3.47e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.82 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 146 GQRVGLFAPAGAGKTTTVSIMANNMEADVVIFAMI-GERAREVIEFLEGEIGpevirksitvvstseANPLEKVRSGLVA 224
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIdGEDILEEVLDQLLLII---------------VGGKKASGSGELR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 225 VSIARHFMEQGKKVVIYFDSLTRFARAQAMLDGtpikggipigvsLALSRLVESCGNSVCGSVTGIFTVLIEKEIDDDPI 304
Cdd:smart00382 67 LRLALALARKLKPDVLILDEITSLLDAEQEALL------------LLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALL 134
|
....*....
gi 518110602 305 AHEVKSLID 313
Cdd:smart00382 135 RRRFDRRIV 143
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
133-196 |
3.47e-04 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 41.77 E-value: 3.47e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518110602 133 KLKIIDGL-FTIGEGQRVGLFAPAGAGKTTTVSIMANNMEADVVIFAMIGE-------RAREVIEFLEGEIG 196
Cdd:COG4555 13 KVPALKDVsFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdvrkeprEARRQIGVLPDERG 84
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
133-173 |
7.44e-04 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 40.82 E-value: 7.44e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 518110602 133 KLKIIDGL-FTIGEGQRVGLFAPAGAGKTTTVSIMANNMEAD 173
Cdd:COG1131 12 DKTALDGVsLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT 53
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
137-167 |
1.15e-03 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 40.39 E-value: 1.15e-03
10 20 30
....*....|....*....|....*....|..
gi 518110602 137 IDGL-FTIGEGQRVGLFAPAGAGKTTTVSIMA 167
Cdd:cd03267 37 LKGIsFTIEKGEIVGFIGPNGAGKTTTLKILS 68
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
135-173 |
1.50e-03 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 39.66 E-value: 1.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 518110602 135 KIIDGL-FTIGEGQRVGLFAPAGAGKTTTVSIMANNMEAD 173
Cdd:cd03266 19 QAVDGVsFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD 58
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
130-173 |
1.80e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 40.43 E-value: 1.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 518110602 130 FPTKlKIIDGL-FTIGEGQRVGLFAPAGAGKTTTVSIMANNMEAD 173
Cdd:COG0488 8 FGGR-PLLDDVsLSINPGDRIGLVGRNGAGKSTLLKILAGELEPD 51
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
141-167 |
1.86e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 40.07 E-value: 1.86e-03
10 20
....*....|....*....|....*..
gi 518110602 141 FTIGEGQRVGLFAPAGAGKTTTVSIMA 167
Cdd:COG4586 43 FTIEPGEIVGFIGPNGAGKSTTIKMLT 69
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
136-271 |
2.42e-03 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 39.81 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518110602 136 IIDGL-FTIGEGQRVGLFAPAGAGKTTTVSIMANNMEADVVIFAMIGE----RARevieflegeigpeVIRKSITVVSTS 210
Cdd:PRK13536 56 VVNGLsFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvpaRAR-------------LARARIGVVPQF 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518110602 211 EANPLE-KVRSGLVAVSiaRHFMEQGKKVVIYFDSLTRFARAQAMLDG--TPIKGGIPIGVSLA 271
Cdd:PRK13536 123 DNLDLEfTVRENLLVFG--RYFGMSTREIEAVIPSLLEFARLESKADArvSDLSGGMKRRLTLA 184
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
353-416 |
3.19e-03 |
|
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: 35.88 E-value: 3.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518110602 353 SEQIKDMVYRYFNVELLIRVGEYEKGNDlETDKAIDLFPIVMEFLKQG-FEGVEYEETLEAMERI 416
Cdd:cd01429 5 ARGFKAILAQYRELRDIVAIVGDDALSE-ADKKTLSRGRRLEEFLQQGqFEPETIEDTLEKLYPI 68
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
135-173 |
5.53e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 38.89 E-value: 5.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 518110602 135 KIIDGL-FTIGEGQRVGLFAPAGAGKTTTVSIMANNMEAD 173
Cdd:COG0488 329 TLLDDLsLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPD 368
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
134-173 |
6.11e-03 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 37.24 E-value: 6.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 518110602 134 LKIIDglFTIGEGQRVGLFAPAGAGKTTTVSIMANNMEAD 173
Cdd:pfam00005 1 LKNVS--LTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT 38
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
134-173 |
9.73e-03 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 36.27 E-value: 9.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 518110602 134 LKIIDglFTIGEGQRVGLFAPAGAGKTTTVSIMANNMEAD 173
Cdd:cd03221 16 LKDIS--LTINPGDRIGLVGRNGAGKSTLLKLIAGELEPD 53
|
|
| |
