|
Name |
Accession |
Description |
Interval |
E-value |
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
1-451 |
0e+00 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 902.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 1 MRLERTSFARRLEGYTEAVSLPAQPVVEGRLLRMVGLTLEAEGLQAAVGSRCNVINESGYHPVQVEAEVMGFSGSKVYLM 80
Cdd:PRK05688 1 MRLERTSFAKRLEGYAEAISLPAQPVVEGRLLRMVGLTLEAEGLRAAVGSRCLVINDDSYHPVQVEAEVMGFSGDKVFLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 81 PVGSLAGIAPGARVVPLPDTGRLPMGMSMLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSIN 160
Cdd:PRK05688 81 PVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 161 GLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTRADIIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPLMRL 240
Cdd:PRK05688 161 GLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEADIIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 241 RAAQYCTRIAEYFRDKGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAGGGSITAFYT 320
Cdd:PRK05688 241 RAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITAFYT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 321 VLSEGDDQQDPIADAARGVLDGHFVLSRRLAEEGHYPAIDIEASISRVMPQVVEAEHLRDAQRFKQLWSRYQQSRDLISV 400
Cdd:PRK05688 321 VLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQSRDLISV 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 15596301 401 GAYVAGGDPETDLAIARFPVMRQFLRQGLDESESLAESRARLASLLAGGQA 451
Cdd:PRK05688 401 GAYVAGGDPETDLAIARFPHLVQFLRQGLRENVSLAQSREQLAAIFAPAAG 451
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
10-446 |
0e+00 |
|
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: 756.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 10 RRLEGYTEAVSLPAQPVVEGRLLRMVGLTLEAEGLQAAVGSRCNVINESGyhpVQVEAEVMGFSGSKVYLMPVGSLAGIA 89
Cdd:COG1157 2 DRLARLLARLEELPPVRVSGRVTRVVGLLIEAVGPDASIGELCEIETADG---RPVLAEVVGFRGDRVLLMPLGDLEGIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 90 PGARVVPLPDTGRLPMGMSMLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQ 169
Cdd:COG1157 79 PGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 170 RLGLFAGTGVGKSVLLGMMTRFTRADIIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPLMRLRAAQYCTRI 249
Cdd:COG1157 159 RIGIFAGSGVGKSTLLGMIARNTEADVNVIALIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 250 AEYFRDKGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNaeAGGGSITAFYTVLSEGDDQQ 329
Cdd:COG1157 239 AEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN--GGKGSITAFYTVLVEGDDMN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 330 DPIADAARGVLDGHFVLSRRLAEEGHYPAIDIEASISRVMPQVVEAEHLRDAQRFKQLWSRYQQSRDLISVGAYVAGGDP 409
Cdd:COG1157 317 DPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENEDLIRIGAYQPGSDP 396
|
410 420 430
....*....|....*....|....*....|....*..
gi 15596301 410 ETDLAIARFPVMRQFLRQGLDESESLAESRARLASLL 446
Cdd:COG1157 397 ELDEAIALIPAIEAFLRQGMDERVSFEESLAQLAELL 433
|
|
| FliI_clade1 |
TIGR03496 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
29-442 |
0e+00 |
|
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: 274607 [Multi-domain] Cd Length: 411 Bit Score: 742.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 29 GRLLRMVGLTLEAEGLQAAVGSRCNVINESGYHpvqVEAEVMGFSGSKVYLMPVGSLAGIAPGARVVPLPDTGRLPMGMS 108
Cdd:TIGR03496 1 GRVTRVVGLVLEAVGLRAPVGSRCEIESSDGDP---IEAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLGGPLRLPVGDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 109 MLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMM 188
Cdd:TIGR03496 78 LLGRVIDGLGRPLDGKGPLDAGERVPLYAPPINPLKRAPIDEPLDVGVRAINGLLTVGRGQRMGIFAGSGVGKSTLLGMM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 189 TRFTRADIIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPLMRLRAAQYCTRIAEYFRDKGKNVLLLMDSLT 268
Cdd:TIGR03496 158 ARYTEADVVVVGLIGERGREVKEFIEDILGEEGLARSVVVAATADESPLMRLRAAFYATAIAEYFRDQGKDVLLLMDSLT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 269 RYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAGGGSITAFYTVLSEGDDQQDPIADAARGVLDGHFVLSR 348
Cdd:TIGR03496 238 RFAMAQREIALAIGEPPATKGYPPSVFAKLPQLVERAGNGEEGKGSITAFYTVLVEGDDQQDPIADAARAILDGHIVLSR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 349 RLAEEGHYPAIDIEASISRVMPQVVEAEHLRDAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPVMRQFLRQG 428
Cdd:TIGR03496 318 ELAEQGHYPAIDILASISRVMPDVVSPEHRQAARRFKQLLSRYQENRDLISIGAYQAGSDPELDQAIALYPRIEAFLQQG 397
|
410
....*....|....
gi 15596301 429 LDESESLAESRARL 442
Cdd:TIGR03496 398 MRERASFEESLEAL 411
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
7-450 |
0e+00 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 689.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 7 SFARRLEGYTEAVsLPAQPVVEGRLLRMVGLTLEAEGLQAAVGSRCNVINESGyhpvQVEAEVMGFSGSKVYLMPVGSLA 86
Cdd:PRK08972 6 QLLNRLKQYKVKV-PPFRAVASGKLVRVVGLTLEATGCRAPVGSLCSIETMAG----ELEAEVVGFDGDLLYLMPIEELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 87 GIAPGARVVPLPDTGRLPMGMSMLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVG 166
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 167 RGQRLGLFAGTGVGKSVLLGMMTRFTRADIIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPLMRLRAAQYC 246
Cdd:PRK08972 161 KGQRMGLFAGSGVGKSVLLGMMTRGTTADVIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCETA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 247 TRIAEYFRDKGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAGGGSITAFYTVLSEGD 326
Cdd:PRK08972 241 TTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSITAFYTVLTEGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 327 DQQDPIADAARGVLDGHFVLSRRLAEEGHYPAIDIEASISRVMPQVVEAEHLRDAQRFKQLWSRYQQSRDLISVGAYVAG 406
Cdd:PRK08972 321 DLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLYQQNRDLISIGAYKQG 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15596301 407 GDPETDLAIARFPVMRQFLRQGLDESESLAESRARLASLLAGGQ 450
Cdd:PRK08972 401 SDPRIDNAIRLQPAMNAFLQQTMKEAVPYDMSVNMLKQLAAQCK 444
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
29-448 |
0e+00 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 592.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 29 GRLLRMVGLTLEAEGLQAAVGSRCNVINESGYHPVQVEAEVMGFSGSKVYLMPVGSLAGIAPGARVVPLPDTG------- 101
Cdd:PRK07960 29 GRLTRATGLVLEATGLQLPLGATCVIERQNGSETHEVESEVVGFNGQRLFLMPLEEVEGILPGARVYARNISGeglqsgk 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 102 RLPMGMSMLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGK 181
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 182 SVLLGMMTRFTRADIIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPLMRLRAAQYCTRIAEYFRDKGKNVL 261
Cdd:PRK07960 189 SVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 262 LLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAGGGSITAFYTVLSEGDDQQDPIADAARGVLD 341
Cdd:PRK07960 269 LIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARAILD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 342 GHFVLSRRLAEEGHYPAIDIEASISRVMPQVVEAEHLRDAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPVM 421
Cdd:PRK07960 349 GHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAIALWPQL 428
|
410 420
....*....|....*....|....*..
gi 15596301 422 RQFLRQGLDESESLAESRARLASLLAG 448
Cdd:PRK07960 429 EAFLQQGIFERADWEDSLQALERIFPT 455
|
|
| FliI_clade2 |
TIGR03497 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
29-446 |
0e+00 |
|
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: 570.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 29 GRLLRMVGLTLEAEGLQAAVGSRCNVINESGyHPVQveAEVMGFSGSKVYLMPVGSLAGIAPGARVVPLPDTGRLPMGMS 108
Cdd:TIGR03497 1 GKVTRVIGLTIESKGPKASIGELCSILTKGG-KPVL--AEVVGFKEENVLLMPLGEVEGIGPGSLVIATGRPLAIKVGKG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 109 MLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMM 188
Cdd:TIGR03497 78 LLGRVLDGLGRPLDGEGPIIGEEPYPLDNPPPNPLKRPRIRDPLETGIKAIDGLLTIGKGQRVGIFAGSGVGKSTLLGMI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 189 TRFTRADIIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPLMRLRAAQYCTRIAEYFRDKGKNVLLLMDSLT 268
Cdd:TIGR03497 158 ARNAKADINVIALIGERGREVRDFIEKDLGEEGLKRSVVVVATSDQPALMRLKAAFTATAIAEYFRDQGKDVLLMMDSVT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 269 RYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEagGGSITAFYTVLSEGDDQQDPIADAARGVLDGHFVLSR 348
Cdd:TIGR03497 238 RFAMAQREIGLAVGEPPTTRGYTPSVFSLLPKLLERSGNSQ--KGSITGFYTVLVDGDDMNEPIADAVRGILDGHIVLSR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 349 RLAEEGHYPAIDIEASISRVMPQVVEAEHLRDAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPVMRQFLRQG 428
Cdd:TIGR03497 316 ELAAKNHYPAIDVLASVSRVMNEIVSEEHKELAGKLRELLAVYKEAEDLINIGAYKRGSNPKIDEAIRYIEKINSFLKQG 395
|
410
....*....|....*...
gi 15596301 429 LDESESLAESRARLASLL 446
Cdd:TIGR03497 396 IDEKFTFEETVQLLKELL 413
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
1-446 |
0e+00 |
|
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: 553.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 1 MRLERTSFARRLegyTEAVSLPAQPVVeGRLLRMVGLTLEAEGLQAAVGSRCnVINESGYHPvQVEAEVMGFSGSKVYLM 80
Cdd:TIGR01026 1 MERNLTTFYNRL---CQEMDLRLVKRV-GRVTKVKGLLIEAVGPQASVGDLC-LIERRGSEG-RLVAEVVGFNGEFVFLM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 81 PVGSLAGIAPGARVVPLPDTGRLPMGMSMLGRVLDGAGRALDGKGGMRA-EDWVPMDGPTINPLKRHPISEPLDVGIRSI 159
Cdd:TIGR01026 75 PYEEVEGVRPGSKVLATGEGLSIKVGDGLLGRVLDGLGKPIDGKGKFLDnVETEGLITAPINPLKRAPIREILSTGVRSI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 160 NGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTRADIIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPLMR 239
Cdd:TIGR01026 155 DGLLTVGKGQRIGIFAGSGVGKSTLLGMIARNTEADVNVIALIGERGREVREFIEHDLGEEGLKRSVVVVATSDQSPLLR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 240 LRAAQYCTRIAEYFRDKGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGnaEAGGGSITAFY 319
Cdd:TIGR01026 235 LKGAYVATAIAEYFRDQGKDVLLLMDSVTRFAMAQREIGLAAGEPPATKGYTPSVFSTLPRLLERAG--ASGKGSITAFY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 320 TVLSEGDDQQDPIADAARGVLDGHFVLSRRLAEEGHYPAIDIEASISRVMPQVVEAEHLRDAQRFKQLWSRYQQSRDLIS 399
Cdd:TIGR01026 313 TVLVEGDDMNEPIADSVRGILDGHIVLSRALAQRGHYPAIDVLASISRLMTAIVSEEHRRAARKFRELLSKYKDNEDLIR 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 15596301 400 VGAYVAGGDPETDLAIARFPVMRQFLRQGLDESESLAESRARLASLL 446
Cdd:TIGR01026 393 IGAYQRGSDRELDFAIAKYPKLERFLKQGINEKVNFEESLQQLEEIF 439
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
29-449 |
0e+00 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 523.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 29 GRLLRMVGLTLEAEGLQAAVGSRCNvINESGYHPVQVEAEVMGFSGSKVYLMPVGSLAGIAPGARVVPLPDTGRLPMGMS 108
Cdd:PRK07721 20 GKVSRVIGLMIESKGPESSIGDVCY-IHTKGGGDKAIKAEVVGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVGSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 109 MLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMM 188
Cdd:PRK07721 99 LIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 189 TRFTRADIIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPLMRLRAAQYCTRIAEYFRDKGKNVLLLMDSLT 268
Cdd:PRK07721 179 ARNTSADLNVIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 269 RYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAggGSITAFYTVLSEGDDQQDPIADAARGVLDGHFVLSR 348
Cdd:PRK07721 259 RVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNAS--GSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 349 RLAEEGHYPAIDIEASISRVMPQVVEAEHLRDAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPVMRQFLRQG 428
Cdd:PRK07721 337 QLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLINIGAYKRGSSREIDEAIQFYPQIISFLKQG 416
|
410 420
....*....|....*....|.
gi 15596301 429 LDESESLAESRARLASLLAGG 449
Cdd:PRK07721 417 TDEKATFEESIQALLSLFGKG 437
|
|
| III_secr_ATP |
TIGR02546 |
type III secretion apparatus H+-transporting two-sector ATPase; [Protein fate, Protein and ... |
27-447 |
0e+00 |
|
type III secretion apparatus H+-transporting two-sector ATPase; [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274191 [Multi-domain] Cd Length: 422 Bit Score: 518.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 27 VEGRLLRMVGLTLEAEGLQAAVGSRCNVINESgyhPVQVEAEVMGFSGSKVYLMPVGSLAGIAPGARVVPLPDTGRLPMG 106
Cdd:TIGR02546 5 VRGRVTEVSGTLLKAVLPGARVGELCLIRRRD---PSQLLAEVVGFTGDEALLSPLGELHGISPGSEVIPTGRPLSIRVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 107 MSMLGRVLDGAGRALDGKGGM--RAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVL 184
Cdd:TIGR02546 82 EALLGRVLDGFGRPLDGKGELpaGEIETRPLDADPPPPMSRQPIDQPLPTGVRAIDGLLTCGEGQRIGIFAGAGVGKSTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 185 LGMMTRFTRADIIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPLMRLRAAQYCTRIAEYFRDKGKNVLLLM 264
Cdd:TIGR02546 162 LGMIARGASADVNVIALIGERGREVREFIEHHLGEEGRKRSVLVVSTSDRPSLERLKAAYTATAIAEYFRDQGKRVLLMM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 265 DSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAggGSITAFYTVLSEGDDQQDPIADAARGVLDGHF 344
Cdd:TIGR02546 242 DSLTRFARALREIGLAAGEPPARGGYPPSVFSSLPRLLERAGNGEK--GSITALYTVLVEGDDMNDPIADEVRSILDGHI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 345 VLSRRLAEEGHYPAIDIEASISRVMPQVVEAEHLRDAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPVMRQF 424
Cdd:TIGR02546 320 VLSRALAERNHYPAIDVLASLSRVMSQVVSTEHRRAAGKLRRLLATYKEVELLIRLGEYQPGSDPETDDAIDKIDAIRAF 399
|
410 420
....*....|....*....|...
gi 15596301 425 LRQGLDESESLAESRARLASLLA 447
Cdd:TIGR02546 400 LRQSTDEYSPYEETLEQLHALVA 422
|
|
| FliI_clade3 |
TIGR03498 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
29-446 |
5.55e-178 |
|
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: 504.14 E-value: 5.55e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 29 GRLLRMVGLTLEAEGLQAA--VGSRCNVINESGYhpvQVEAEVMGFSGSKVYLMPVGSLAGIAPGARVVPLPDTGRLPMG 106
Cdd:TIGR03498 1 GRVTAVTGLLIEVRGLSRAvrLGDRCAIRARDGR---PVLAEVVGFNGDRVLLMPFEPLEGVGLGCAVFAREGPLAVRPH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 107 MSMLGRVLDGAGRALDGKGGMRA-EDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLL 185
Cdd:TIGR03498 78 PSWLGRVINALGEPIDGKGPLPQgERRYPLRASPPPAMSRARVGEPLDTGVRVIDTFLPLCRGQRLGIFAGSGVGKSTLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 186 GMMTRFTRADIIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPLMRLRAAQYCTRIAEYFRDKGKNVLLLMD 265
Cdd:TIGR03498 158 SMLARNTDADVVVIALVGERGREVREFLEDDLGEEGLKRSVVVVATSDESPLMRRQAAYTATAIAEYFRDQGKDVLLLMD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 266 SLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAGGGSITAFYTVLSEGDDQQDPIADAARGVLDGHFV 345
Cdd:TIGR03498 238 SVTRFAMAQREIGLAAGEPPVARGYTPSVFSELPRLLERAGPGAEGKGSITGIFTVLVDGDDHNEPVADAVRGILDGHIV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 346 LSRRLAEEGHYPAIDIEASISRVMPQVVEAEHLRDAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPVMRQFL 425
Cdd:TIGR03498 318 LDRAIAERGRYPAINVLASVSRLAPRVWSPEERKLVRRLRALLARYEETEDLIRLGAYRKGSDPELDEAIRLVPKIYEFL 397
|
410 420
....*....|....*....|.
gi 15596301 426 RQGLDESESLAESRARLASLL 446
Cdd:TIGR03498 398 TQGPDEPTSLQDPFADLAAIL 418
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
27-447 |
5.25e-175 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 497.11 E-value: 5.25e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 27 VEGRLLRMVGLTLEAEGLQAAVGSRCNVINESGyhpVQVEAEVMGFSGSKVYLMPVGSLAGIAPGARVVPLPDTGRLPMG 106
Cdd:PRK07196 17 VAGRLVRVTGLLLESVGCRLAIGQRCRIESVDE---TFIEAQVVGFDRDITYLMPFKHPGGVLGGARVFPSEQDGELLIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 107 MSMLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLG 186
Cdd:PRK07196 94 DSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 187 MMTRFTRADIIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPLMRLRAAQYCTRIAEYFRDKGKNVLLLMDS 266
Cdd:PRK07196 174 MITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 267 LTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEaGGGSITAFYTVLSEGDDQQDPIADAARGVLDGHFVL 346
Cdd:PRK07196 254 LTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSS-GNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 347 SRRLAEEGHYPAIDIEASISRVMPQVVEAEHLRDAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPVMRQFLR 426
Cdd:PRK07196 333 SRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVAGADPMADQAVHYYPAITQFLR 412
|
410 420
....*....|....*....|.
gi 15596301 427 QGLDESESLAESRARLASLLA 447
Cdd:PRK07196 413 QEVGHPALFSASVEQLTGMFP 433
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
26-449 |
5.34e-169 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 482.17 E-value: 5.34e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 26 VVEGRLLRMVGLTLEAEGLQAA--VGSRCNVINESGYhpvQVEAEVMGFSGSKVYLMPVGSLAGIAPGARVVPLPDTGRL 103
Cdd:PRK08927 16 VIYGRVVAVRGLLVEVAGPIHAlsVGARIVVETRGGR---PVPCEVVGFRGDRALLMPFGPLEGVRRGCRAVIANAAAAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 104 PMGMSMLGRVLDGAGRALDGKGgmraedwvPM-DGPTINPLKRHP--------ISEPLDVGIRSINGLLTVGRGQRLGLF 174
Cdd:PRK08927 93 RPSRAWLGRVVNALGEPIDGKG--------PLpQGPVPYPLRAPPppahsrarVGEPLDLGVRALNTFLTCCRGQRMGIF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 175 AGTGVGKSVLLGMMTRFTRADIIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPLMRLRAAQYCTRIAEYFR 254
Cdd:PRK08927 165 AGSGVGKSVLLSMLARNADADVSVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 255 DKGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAGGGSITAFYTVLSEGDDQQDPIAD 334
Cdd:PRK08927 245 DQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGEGTITGLFTVLVDGDDHNEPVAD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 335 AARGVLDGHFVLSRRLAEEGHYPAIDIEASISRVMPQVVEAEHLRDAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLA 414
Cdd:PRK08927 325 AVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLGAYRAGSDPEVDEA 404
|
410 420 430
....*....|....*....|....*....|....*
gi 15596301 415 IARFPVMRQFLRQGLDESESLAESRARLASLLAGG 449
Cdd:PRK08927 405 IRLNPALEAFLRQGKDEATSLAEGYARLAQILGGP 439
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
62-446 |
7.99e-157 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 451.19 E-value: 7.99e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 62 PVQVEAEVMGFSGSKVYLMPVGSLAGIAPGARVVPLPDTGRLPMGMSMLGRVLDGAGRALDGkGGMRAEDWVPMDGPTIN 141
Cdd:PRK06820 58 PQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 142 PLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTRADIIVVGLIGERGREVKEFIDEILGEEG 221
Cdd:PRK06820 137 PLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCADSAADVMVLALIGERGREVREFLEQVLTPEA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 222 LKRSVVVASPADDAPLMRLRAAQYCTRIAEYFRDKGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKL 301
Cdd:PRK06820 217 RARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 302 VERAGNAEAggGSITAFYTVLSEGDDQQDPIADAARGVLDGHFVLSRRLAEEGHYPAIDIEASISRVMPQVVEAEHLRDA 381
Cdd:PRK06820 297 LERTGNSDR--GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMA 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596301 382 QRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPVMRQFLRQGLDESESLAESRARLASLL 446
Cdd:PRK06820 375 QKLRRMLACYQEIELLVRVGEYQAGEDLQADEALQRYPAICAFLQQDHSETAHLETTLEHLAQVV 439
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
102-368 |
6.64e-155 |
|
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: 439.30 E-value: 6.64e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 102 RLPMGMSMLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGK 181
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 182 SVLLGMMTRFTRADIIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPLMRLRAAQYCTRIAEYFRDKGKNVL 261
Cdd:cd01136 81 STLLGMIARNTDADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 262 LLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAggGSITAFYTVLSEGDDQQDPIADAARGVLD 341
Cdd:cd01136 161 LLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEK--GSITAFYTVLVEGDDFNDPIADEVRSILD 238
|
250 260
....*....|....*....|....*..
gi 15596301 342 GHFVLSRRLAEEGHYPAIDIEASISRV 368
Cdd:cd01136 239 GHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
27-447 |
6.19e-153 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 441.11 E-value: 6.19e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 27 VEGRLLRMVGLTLEAEGLQAAVGSRCNVINESgyHPVQVEAEVMGFSGSKVYLMPVGSLAGIAPGARVVPLPDTGRLPMG 106
Cdd:PRK06936 23 IRGRVTQVTGTILKAVVPGVRIGELCYLRNPD--NSLSLQAEVIGFAQHQALLTPLGEMYGISSNTEVSPTGTMHQVGVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 107 MSMLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLG 186
Cdd:PRK06936 101 EHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 187 MMTRFTRADIIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPLMRLRAAQYCTRIAEYFRDKGKNVLLLMDS 266
Cdd:PRK06936 181 SLIRSAEVDVTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 267 LTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAggGSITAFYTVLSEGDDQQDPIADAARGVLDGHFVL 346
Cdd:PRK06936 261 VTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDK--GSITALYTVLVEGDDMTEPVADETRSILDGHIIL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 347 SRRLAEEGHYPAIDIEASISRVMPQVVEAEHLRDAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPVMRQFLR 426
Cdd:PRK06936 339 SRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIGEYQKGQDKEADQAIERIGAIRGFLR 418
|
410 420
....*....|....*....|.
gi 15596301 427 QGLDESESLAESRARLASLLA 447
Cdd:PRK06936 419 QGTHELSHFNETLNLLETLTQ 439
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
29-447 |
1.77e-151 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 437.19 E-value: 1.77e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 29 GRLLRMVGLTLEAEGLQAAVGSRCNVinESGYHPVQVEAEVMGFSGSKVYLMPVGSLAGIAPGARVVPLPDTGRLPMGMS 108
Cdd:PRK08472 20 GSITKISPTIIEADGLNPSVGDIVKI--ESSDNGKECLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 109 MLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMM 188
Cdd:PRK08472 98 LLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 189 TRFTRADIIVVGLIGERGREVKEFIDEILGEEgLKRSVVVASPADDAPLMRLRAAQYCTRIAEYFRDKGKNVLLLMDSLT 268
Cdd:PRK08472 178 VKGCLAPIKVVALIGERGREIPEFIEKNLGGD-LENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 269 RYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNaEAGGGSITAFYTVLSEGDDQQDPIADAARGVLDGHFVLSR 348
Cdd:PRK08472 257 RFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK-EEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 349 RLAEEGHYPAIDIEASISRVMPQVVEAEHLRDAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPVMRQFLRQG 428
Cdd:PRK08472 336 ELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAYQKGNDKELDEAISKKEFMEQFLKQN 415
|
410
....*....|....*....
gi 15596301 429 LDESESLAESRARLASLLA 447
Cdd:PRK08472 416 PNELFPFEQTFEQLEEILR 434
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
23-445 |
6.95e-143 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 415.71 E-value: 6.95e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 23 AQPVVEGRLLRMVGLTLEAEGLQAAVGSRCNVINESGyhPVQVEAEVMGFSGSKVYLMPVGSLAGIAPGARVVPLPDTGR 102
Cdd:PRK09099 20 PAVRRTGKVVEVIGTLLRVSGLDVTLGELCELRQRDG--TLLQRAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 103 LPMGMSMLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKS 182
Cdd:PRK09099 98 VPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 183 VLLGMMTRFTRADIIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPLMRLRAAQYCTRIAEYFRDKGKNVLL 262
Cdd:PRK09099 178 TLMGMFARGTQCDVNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 263 LMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAggGSITAFYTVLSEGDDQQDPIADAARGVLDG 342
Cdd:PRK09099 258 MMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGET--GSITALYTVLAEDESGSDPIAEEVRGILDG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 343 HFVLSRRLAEEGHYPAIDIEASISRVMPQVVEAEHLRDAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPVMR 422
Cdd:PRK09099 336 HMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVGEYRAGSDPVADEAIAKIDAIR 415
|
410 420
....*....|....*....|...
gi 15596301 423 QFLRQGLDESESLAESRARLASL 445
Cdd:PRK09099 416 DFLSQRTDEYSDPDATLAALAEL 438
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-431 |
9.34e-128 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 376.99 E-value: 9.34e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 29 GRLLRMVGLTLEAEGLQAAVGSRCNVINESGYhpvqveAEVMGFSGSKVYLMPVGSLAGIAPGARVVPLPDTGRLPMGMS 108
Cdd:PRK07594 23 GRIQDVSATLLNAWLPGVFMGELCCIKPGEEL------AEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 109 MLGRVLDGAGRALDGKggmraED----WVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVL 184
Cdd:PRK07594 97 LLGRVIDGFGRPLDGR-----ELpdvcWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 185 LGMMTRFTRADIIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPLMRLRAAQYCTRIAEYFRDKGKNVLLLM 264
Cdd:PRK07594 172 LAMLCNAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 265 DSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAggGSITAFYTVLSEGDDQQDPIADAARGVLDGHF 344
Cdd:PRK07594 252 DSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEK--GSITAFYTVLVEGDDMNEPLADEVRSLLDGHI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 345 VLSRRLAEEGHYPAIDIEASISRVMPQVVEAEHLRDAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPVMRQF 424
Cdd:PRK07594 330 VLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEYQRGVDTDTDKAIDTYPDICTF 409
|
....*..
gi 15596301 425 LRQGLDE 431
Cdd:PRK07594 410 LRQSKDE 416
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
32-447 |
5.14e-127 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 374.72 E-value: 5.14e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 32 LRMVGLTLEAEGLQAAVGSRCNVinESGYHPVQV--EAEVMGFSGSKVYLMPVGSLAGIAPGARVVPLPDTGRLPMGMSM 109
Cdd:PRK08149 11 LRIQGPIIEAELPDVAIGEICEI--RAGWHSNEViaRAQVVGFQRERTILSLIGNAQGLSRQVVLKPTGKPLSVWVGEAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 110 LGRVLDGAGRALDGKGG----MRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLL 185
Cdd:PRK08149 89 LGAVLDPTGKIVERFDApptvGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 186 GMMTRFTRADIIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPLMRLRAAQYCTRIAEYFRDKGKNVLLLMD 265
Cdd:PRK08149 169 NMLIEHSEADVFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFID 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 266 SLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAggGSITAFYTVLSEGDDQQDPIADAARGVLDGHFV 345
Cdd:PRK08149 249 SMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLA--GSITAFYTVLLESEEEPDPIGDEIRSILDGHIY 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 346 LSRRLAEEGHYPAIDIEASISRVMPQVVEAEHLRDAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPVMRQFL 425
Cdd:PRK08149 327 LSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGEYRRGENADNDRAMDKRPALEAFL 406
|
410 420
....*....|....*....|..
gi 15596301 426 RQGLDESESLAESRARLASLLA 447
Cdd:PRK08149 407 KQDVAEKSSFSDTLERLNEFAA 428
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
155-366 |
2.24e-123 |
|
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: 357.44 E-value: 2.24e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 155 GIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTRADIIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADD 234
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLGSGALKRTVVVVATSDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 235 APLMRLRAAQYCTRIAEYFRDKGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAGGGS 314
Cdd:pfam00006 81 PPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKGKGGS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15596301 315 ITAFYTVLSEGDDQQDPIADAARGVLDGHFVLSRRLAEEGHYPAIDIEASIS 366
Cdd:pfam00006 161 ITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
67-451 |
1.58e-119 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 356.62 E-value: 1.58e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 67 AEVMGFSGSKVYLMPVGSLAGIAPGARVVPLPdTGRLPMGMSMLGRVLDGAGRALDGKGG-MRAEDWVPMDGPTINPLKR 145
Cdd:PRK06002 64 GEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKG-PLRIRPDPSWKGRVINALGEPIDGLGPlAPGTRPMSIDATAPPAMTR 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 146 HPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTRADIIVVGLIGERGREVKEFIDEILGEEgLKRS 225
Cdd:PRK06002 143 ARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGREVREFLEDTLADN-LKKA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 226 VVVASPADDAPLMRLRAAQYCTRIAEYFRDKGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERA 305
Cdd:PRK06002 222 VAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 306 GNAEAGGGSITAFYTVLSEGDDQQDPIADAARGVLDGHFVLSRRLAEEGHYPAIDIEASISRVMPQVVEAEHLRDAQRFK 385
Cdd:PRK06002 302 GPGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLK 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596301 386 QLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPVMRQFLRQGLDESESlAESRARLASLLAGGQA 451
Cdd:PRK06002 382 SMIARFEETRDLRLIGGYRAGSDPDLDQAVDLVPRIYEALRQSPGDPPS-DDAFADLAAALKGAAQ 446
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
102-368 |
1.13e-106 |
|
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: 317.09 E-value: 1.13e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 102 RLPMGMSMLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGK 181
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 182 SVLLGMMTRFT---RADIIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPLMRLRAAQYCTRIAEYFRDKGK 258
Cdd:cd19476 81 TVLAMQLARNQakaHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 259 NVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAGGGSITAFYTVLSEGDDQQDPIADAARG 338
Cdd:cd19476 161 HVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTPGDDLTDPIPDNTFA 240
|
250 260 270
....*....|....*....|....*....|
gi 15596301 339 VLDGHFVLSRRLAEEGHYPAIDIEASISRV 368
Cdd:cd19476 241 ILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
41-437 |
1.67e-105 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 320.00 E-value: 1.67e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 41 AEGLQAAVGSRCNVinesGYHpvQVEAEVMGFSGSKVYLMPVGSLAGIAPGARVVPLPDTGRLPMGMSMLGRVLDGAGRA 120
Cdd:PRK06793 35 AKGPKAKIGDVCFV----GEH--NVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 121 LDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTRADIIVVG 200
Cdd:PRK06793 109 LNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVIS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 201 LIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPLMRLRAAQYCTRIAEYFRDKGKNVLLLMDSLTRYAQAQREIALA 280
Cdd:PRK06793 189 LVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 281 IGEPPaTKGYPPSVFAKLPKLVERAGNAEAggGSITAFYTVLSEGDDQQDPIADAARGVLDGHFVLSRRLAEEGHYPAID 360
Cdd:PRK06793 269 VKELP-IGGKTLLMESYMKKLLERSGKTQK--GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAIS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 361 IEASISRVMPQVVEAEHLRDAQRFKQLWSRYQQSRDLISVG--------AYVAGGDPETDLaiarfpvMRQFLRQGLDES 432
Cdd:PRK06793 346 VLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGtiqenaenAYIFECKNKVEG-------INTFLKQGRSDS 418
|
....*
gi 15596301 433 ESLAE 437
Cdd:PRK06793 419 FQFDD 423
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
24-446 |
8.66e-95 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 292.58 E-value: 8.66e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 24 QPVVE-GRLLRMVGLTLEAEGLQAAVGSRCNvINESGYHPVQveAEVMGFSGSKVYLMPVGSLAGIAPGARVVPLPDTGR 102
Cdd:PRK05922 15 QPYREcGLLSRVSGNLLEAQGLSACLGELCQ-ISLSKSPPIL--AEVIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPPS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 103 LPMGMSMLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKS 182
Cdd:PRK05922 92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 183 VLLGMMTRFTRADIIVVGLIGERGREVKEFIDEilGEEGLK--RSVVVASPADDAPLMRLRAAQYCTRIAEYFRDKGKNV 260
Cdd:PRK05922 172 SLLSTIAKGSKSTINVIALIGERGREVREYIEQ--HKEGLAaqRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 261 LLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAggGSITAFYTVLSEGdDQQDPIADAARGVL 340
Cdd:PRK05922 250 LFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDK--GSITALYAILHYP-NHPDIFTDYLKSLL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 341 DGHFVLS---RRLAEeghyPAIDIEASISRVMPQVVEAEHLRDAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIAR 417
Cdd:PRK05922 327 DGHFFLTpqgKALAS----PPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGAYVPGQDAHLDRAVKL 402
|
410 420
....*....|....*....|....*....
gi 15596301 418 FPVMRQFLRQGLDESESLAESRARLASLL 446
Cdd:PRK05922 403 LPSIKQFLSQPLSSYCALHNTLKQLEALL 431
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
102-369 |
1.31e-51 |
|
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: 175.49 E-value: 1.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 102 RLPMGMSMLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGK 181
Cdd:cd01135 3 KLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLPH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 182 SVLLGMMTRFTR------ADIIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPLMRLRAAQYCTRIAEYFR- 254
Cdd:cd01135 83 NELAAQIARQAGvvgseeNFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYLAy 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 255 DKGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAGGGSITAFYTVLSEGDDQQDPIAD 334
Cdd:cd01135 163 EKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPILTMPNDDITHPIPD 242
|
250 260 270
....*....|....*....|....*....|....*
gi 15596301 335 AARGVLDGHFVLSRRLAEEGHYPAIDIEASISRVM 369
Cdd:cd01135 243 LTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLM 277
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
87-438 |
2.49e-50 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 176.94 E-value: 2.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 87 GIAP-GARVVPLPDTGRLPMGMSMLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTV 165
Cdd:PRK04196 61 GLDLkDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 166 GRGQRLGLFAGTG----------VGKSVLLGMMTRFTradiIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDA 235
Cdd:PRK04196 141 VRGQKLPIFSGSGlphnelaaqiARQAKVLGEEENFA----VVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDP 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 236 PLMRL---RAAQYCtriAEYFR-DKGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAG 311
Cdd:PRK04196 217 AIERIltpRMALTA---AEYLAfEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 312 GGSITAFYTVLSEGDDQQDPIADAARGVLDGHFVLSRRLAEEGHYPAIDIEASISRVMPQVVEAEHLRD--AQRFKQLWS 389
Cdd:PRK04196 294 KGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKTREdhKDVANQLYA 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 15596301 390 RYQQSRDLISVGAYVaGGD--PETDLAIARFPVM--RQFLRQGLDESESLAES 438
Cdd:PRK04196 374 AYARGKDLRELAAIV-GEEalSERDRKYLKFADAfeREFVNQGFDENRSIEET 425
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
74-427 |
1.09e-45 |
|
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: 164.89 E-value: 1.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 74 GSKVYLMPVGSLAGIAPGARVVplpDTGR---LPMGMSMLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISE 150
Cdd:TIGR01039 49 DDTVRTIAMGSTDGLVRGLEVI---DTGApisVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 151 PLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTR---FTRADIIVVGLIGERGREVKEFIDEILGEEGLKRSVV 227
Cdd:TIGR01039 126 ILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINniaKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTAL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 228 VASPADDAPLMRLRAAQYCTRIAEYFRD-KGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAg 306
Cdd:TIGR01039 206 VYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERI- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 307 nAEAGGGSITAFYTVLSEGDDQQDPIADAARGVLDGHFVLSRRLAEEGHYPAIDIEASISRVM-PQVVEAEHLRDAQRFK 385
Cdd:TIGR01039 285 -TSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLdPSVVGEEHYDVARGVQ 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15596301 386 QLWSRYQQSRDLISvgayVAGGDP---ETDLAIARFPVMRQFLRQ 427
Cdd:TIGR01039 364 QILQRYKELQDIIA----ILGMDElseEDKLTVERARRIQRFLSQ 404
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
86-448 |
5.22e-43 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 158.15 E-value: 5.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 86 AGIAPGARVVPLPDTGRLPMGMSMLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTV 165
Cdd:PRK13343 80 ADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 166 GRGQRLGLFAGTGVGKSVlLGMMTRFTRAD---IIVVGLIGERGREVKEFIDEILGEEGLKRSVVVASPADDAPlmrlrA 242
Cdd:PRK13343 160 GRGQRELIIGDRQTGKTA-IAIDAIINQKDsdvICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPP-----G 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 243 AQY------CTrIAEYFRDKGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEAGGGS 314
Cdd:PRK13343 234 LQYlapfagCA-IAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAklSPELGGGS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 315 ITAFYTVLSEGDDQQDPIADAARGVLDGHFVLSRRLAEEGHYPAIDIEASISRVMPQvveAEHlrdaQRFKQLWSR---- 390
Cdd:PRK13343 313 LTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGK---AQH----PAIRKESGRlrld 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 15596301 391 YQQSRDLISVGAYVAGGDPETDLAIARFPVMRQFLRQGLDESESLAESRARLASLLAG 448
Cdd:PRK13343 386 YAQFLELEAFTRFGGLLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEG 443
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
104-368 |
5.37e-43 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 152.71 E-value: 5.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 104 PMGMSMLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGK-S 182
Cdd:cd01132 5 PVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKtA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 183 VLLGMMTRFTRADIIVVGL-IGERGREVKEFIdEILGEEG-LKRSVVVASPADD-APLMRLraAQY--CTrIAEYFRDKG 257
Cdd:cd01132 85 IAIDTIINQKGKKVYCIYVaIGQKRSTVAQIV-KTLEEHGaMEYTIVVAATASDpAPLQYL--APYagCA-MGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 258 KNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEAGGGSITAFYTVLSEGDDQQDPIADA 335
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklSDELGGGSLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|...
gi 15596301 336 ARGVLDGHFVLSRRLAEEGHYPAIDIEASISRV 368
Cdd:cd01132 241 VISITDGQIFLESELFNKGIRPAINVGLSVSRV 273
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
104-369 |
1.31e-41 |
|
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: 148.91 E-value: 1.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 104 PMGMSMLGRVLDGAGRALDGKGGMRAEDWVPM--DGPTINPLKrhPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGK 181
Cdd:cd01133 3 PVGEETLGRIFNVLGEPIDERGPIKAKERWPIhrEAPEFVELS--TEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 182 SVLL-GMMTRFTRAD--IIVVGLIGERGREVKEFIDE-----ILGEEGLKRSVVVASPADDAPLMRLRAAQYCTRIAEYF 253
Cdd:cd01133 81 TVLImELINNIAKAHggYSVFAGVGERTREGNDLYHEmkesgVINLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 254 RD-KGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAgnAEAGGGSITAFYTVLSEGDDQQDPI 332
Cdd:cd01133 161 RDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERI--TSTKKGSITSVQAVYVPADDLTDPA 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 15596301 333 ADAARGVLDGHFVLSRRLAEEGHYPAIDIEASISRVM 369
Cdd:cd01133 239 PATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
83-399 |
2.08e-39 |
|
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: 147.54 E-value: 2.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 83 GSLAGIAPGARVVplpDTGR---LPMGMSMLGRVLDGAGRALDGKGGMRAEDWVPM--DGPTINPLKrhPISEPLDVGIR 157
Cdd:COG0055 61 DSTDGLVRGMEVI---DTGApisVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIhrPAPPFEEQS--TKTEILETGIK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 158 SINGLLTVGRGQRLGLFAGTGVGKSVLL-GMMTRFTRAD--IIVVGLIGERGREVKEFIDEiLGEEG-LKRSVVVASPAD 233
Cdd:COG0055 136 VIDLLAPYAKGGKIGLFGGAGVGKTVLImELIHNIAKEHggVSVFAGVGERTREGNDLYRE-MKESGvLDKTALVFGQMN 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 234 DAPLMRLRAAQYCTRIAEYFRD-KGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAgnAEAGG 312
Cdd:COG0055 215 EPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERI--TSTKK 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 313 GSITAFYTVLSEGDDQQDPIADAARGVLDGHFVLSRRLAEEGHYPAIDIEASISRVM-PQVVEAEHLRDAQRFKQLWSRY 391
Cdd:COG0055 293 GSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILdPLIVGEEHYRVAREVQRILQRY 372
|
....*...
gi 15596301 392 QQSRDLIS 399
Cdd:COG0055 373 KELQDIIA 380
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
62-427 |
2.74e-37 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 142.49 E-value: 2.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 62 PVQVEAEVMGFSG-SKVYLMPVGSLAGIAPGARVVplpDTGR---LPMGMSMLGRVLDGAGRALDGKGgmraedwvPMDG 137
Cdd:CHL00060 54 EINVTCEVQQLLGnNRVRAVAMSATDGLMRGMEVI---DTGAplsVPVGGATLGRIFNVLGEPVDNLG--------PVDT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 138 PTINPLKRH-PISEPLDV-------GIRSINGLLTVGRGQRLGLFAGTGVGKSVL-LGMMTRFTRAD--IIVVGLIGERG 206
Cdd:CHL00060 123 RTTSPIHRSaPAFIQLDTklsifetGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLiMELINNIAKAHggVSVFGGVGERT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 207 REVKEFIDE-----ILGEEGLKRSVV--VASPADDAPLMRLRAAQYCTRIAEYFRDKGK-NVLLLMDSLTRYAQAQREIA 278
Cdd:CHL00060 203 REGNDLYMEmkesgVINEQNIAESKValVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 279 LAIGEPPATKGYPPSVFAKLPKLVERAgnAEAGGGSITAFYTVLSEGDDQQDPIADAARGVLDGHFVLSRRLAEEGHYPA 358
Cdd:CHL00060 283 ALLGRMPSAVGYQPTLSTEMGSLQERI--TSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPA 360
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596301 359 IDIEASISRVM-PQVVEAEHLRDAQRFKQLWSRYQQSRDLISvgayVAGGDP---ETDLAIARFPVMRQFLRQ 427
Cdd:CHL00060 361 VDPLDSTSTMLqPRIVGEEHYETAQRVKQTLQRYKELQDIIA----ILGLDElseEDRLTVARARKIERFLSQ 429
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
67-401 |
2.14e-34 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 133.24 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 67 AEVMGFSGSKVYLMPVGSLAGIAPGARVVPLPDTGRLPMGMSMLGRVLDGAGRALDGkGGMRAEDWVPMDGPTINPLKRH 146
Cdd:PRK02118 40 AQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GPELEGEPIEIGGPSVNPVKRI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 147 PISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTRADIIVVGLIGERGREVKEFIDEILGEEGLKRSV 226
Cdd:PRK02118 119 VPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLARIALQAEADIIILGGMGLTFDDYLFFKDTFENAGALDRTV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 227 VVASPADDAPLMRLRAAQYCTRIAEYFR-DKGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERA 305
Cdd:PRK02118 199 MFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 306 GNAEaGGGSITAFYTVLSEGDDQQDPIADAARGVLDGHFVLsrrlaeegHYPAIDIEASISRvMPQVVEAEHLRDAQR-- 383
Cdd:PRK02118 279 VDFE-DGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYL--------RRGRIDPFGSLSR-LKQLVIGKKTREDHGdl 348
|
330 340
....*....|....*....|.
gi 15596301 384 ---FKQLWSRYQQSRDLISVG 401
Cdd:PRK02118 349 mnaMIRLYADSREAKEKMAMG 369
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
105-360 |
2.74e-33 |
|
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: 126.92 E-value: 2.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 105 MGMSMLGRVLDGAGRALDG---------KGGMRAEDWvPMDGPTINpLKRHPISEPLDVGIRSINGLLTVGRGqrlGLFA 175
Cdd:cd01134 6 LGPGLLGSIFDGIQRPLEViaetgsifiPRGVNVQRW-PVRQPRPV-KEKLPPNVPLLTGQRVLDTLFPVAKG---GTAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 176 ---GTGVGKSVLLGMMTRFTRADIIVVGLIGERGREV----KEF---IDEILGEEGLKRSVVVASPADdAPLMRLRAAQY 245
Cdd:cd01134 81 ipgPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMaevlEEFpelKDPITGESLMERTVLIANTSN-MPVAAREASIY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 246 --CTrIAEYFRDKGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAGG-----GSITAF 318
Cdd:cd01134 160 tgIT-IAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRCLGspgreGSVTIV 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15596301 319 YTVLSEGDDQQDPIADAARGVLDGHFVLSRRLAEEGHYPAID 360
Cdd:cd01134 239 GAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSIN 280
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
100-442 |
6.25e-33 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 130.08 E-value: 6.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 100 TGRL---PMGMSMLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAG 176
Cdd:CHL00059 70 TGKIaqiPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 177 TGVGK-SVLLGMMTRFTRADIIVVGL-IGERGREVKEfIDEILGEEG-LKRSVVVASPADDAPLMRLRAAQYCTRIAEYF 253
Cdd:CHL00059 150 RQTGKtAVATDTILNQKGQNVICVYVaIGQKASSVAQ-VVTTLQERGaMEYTIVVAETADSPATLQYLAPYTGAALAEYF 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 254 RDKGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEAGGGSITAFYTVLSEGDDQQDP 331
Cdd:CHL00059 229 MYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklSSQLGEGSMTALPIVETQAGDVSAY 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 332 IADAARGVLDGHFVLSRRLAEEGHYPAIDIEASISRV--------MPQVVEAEHLRDAQrFKQLWSRYQQSRDLisvgay 403
Cdd:CHL00059 309 IPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVgsaaqikaMKQVAGKLKLELAQ-FAELEAFAQFASDL------ 381
|
330 340 350
....*....|....*....|....*....|....*....
gi 15596301 404 vaggDPETDLAIARFPVMRQFLRQGLDESESLAESRARL 442
Cdd:CHL00059 382 ----DKATQNQLARGQRLRELLKQSQSAPLTVEEQVATI 416
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
99-438 |
5.33e-32 |
|
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: 127.15 E-value: 5.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 99 DTGRLPMGMSMLGRVLDGAGRALDGKGGMRAEDWVPMDGPTINPLKRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTG 178
Cdd:TIGR01040 72 DILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 179 V-------------------GKSVLLGMMTRFTradiIVVGLIGERgREVKEFIDEILGEEG-LKRSVVVASPADDAPLM 238
Cdd:TIGR01040 152 LphneiaaqicrqaglvklpTKDVHDGHEDNFA----IVFAAMGVN-METARFFKQDFEENGsMERVCLFLNLANDPTIE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 239 RLRAAQYCTRIAEYFR-DKGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAGGGSITA 317
Cdd:TIGR01040 227 RIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 318 FYTVLSEGDDQQDPIADAARGVLDGHFVLSRRLAEEGHYPAIDIEASISRVMPQVV-EAEHLRD-AQRFKQLWSRYQQSR 395
Cdd:TIGR01040 307 IPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIgEGMTRKDhSDVSNQLYACYAIGK 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15596301 396 DLISVGAyVAGGDPET--DLAIARF--PVMRQFLRQGLDESESLAES 438
Cdd:TIGR01040 387 DVQAMKA-VVGEEALSseDLLYLEFldKFEKNFIAQGPYENRTIFES 432
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
100-368 |
7.52e-30 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 121.33 E-value: 7.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 100 TGRL---PMGMSMLGRVLDGAGRALDGKGGMRAEDWVPMD--GPTInpLKRHPISEPLDVGIRSINGLLTVGRGQRlGLF 174
Cdd:PRK09281 91 TGRIlevPVGEALLGRVVNPLGQPIDGKGPIEATETRPVErkAPGV--IDRKSVHEPLQTGIKAIDAMIPIGRGQR-ELI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 175 AG---TG------------VGKSVLlgmmtrftradIIVVGlIGERGREVKEFIdEILGEEG-LKRSVVVASPADD-APL 237
Cdd:PRK09281 168 IGdrqTGktaiaidtiinqKGKDVI-----------CIYVA-IGQKASTVAQVV-RKLEEHGaMEYTIVVAATASDpAPL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 238 mrlraaQY------CTrIAEYFRDKGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAE 309
Cdd:PRK09281 235 ------QYlapyagCA-MGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAklSDE 307
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596301 310 AGGGSITAFytvlsegddqqdPIADAARG------------VLDGHFVLSRRLAEEGHYPAIDIEASISRV 368
Cdd:PRK09281 308 LGGGSLTAL------------PIIETQAGdvsayiptnvisITDGQIFLESDLFNAGIRPAINVGISVSRV 366
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
373-442 |
1.29e-29 |
|
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: 109.83 E-value: 1.29e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 373 VEAEHLRDAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPVMRQFLRQGLDESESLAESRARL 442
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIGAYQAGSDPEIDEAIAKRPAINAFLRQGVDEPVSFEETLAQL 70
|
|
| ATP-synt_flagellum-secretory_path_III_C |
cd18114 |
Flagellum-specific ATP synthase, C-terminal domain; The C-terminal domain of the ... |
377-446 |
3.75e-26 |
|
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: 100.76 E-value: 3.75e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 377 HLRDAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPVMRQFLRQGLDESESLAESRARLASLL 446
Cdd:cd18114 1 HYLAARKFRELMSTYQENEDLIRIGAYKKGSDPEVDEAIRLKPQIEAFLKQGLNEKAPLEESLQQLEEIF 70
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
144-372 |
6.98e-26 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 110.26 E-value: 6.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 144 KRHPISEPLDVGIRSINGLLTVGRGqrlGLFA---GTGVGKSVLLGMMTRFTRADIIVVGLIGERGREVKEFIDEIL--- 217
Cdd:PRK04192 203 EKLPPVEPLITGQRVIDTFFPVAKG---GTAAipgPFGSGKTVTQHQLAKWADADIVIYVGCGERGNEMTEVLEEFPeli 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 218 ----GEEGLKRSVVVAS----PAddaplmrlrAAQ----Y--CTrIAEYFRDKGKNVLLLMDSLTRYAQAQREIALAIGE 283
Cdd:PRK04192 280 dpktGRPLMERTVLIANtsnmPV---------AAReasiYtgIT-IAEYYRDMGYDVLLMADSTSRWAEALREISGRLEE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 284 PPATKGYPPSVFAKLPKLVERAGNAEAGG---GSITAFYTVLSEGDDQQDPIADAARGVLDGHFVLSRRLAEEGHYPAID 360
Cdd:PRK04192 350 MPGEEGYPAYLASRLAEFYERAGRVKTLGgeeGSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAIN 429
|
250
....*....|..
gi 15596301 361 IEASISRVMPQV 372
Cdd:PRK04192 430 WLTSYSLYLDQV 441
|
|
| ATP-synt_flagellum-secretory_path_III_N |
cd18117 |
Flagellum-specific ATP synthase, N-terminal domain; The N-terminal domain of the ... |
27-99 |
1.88e-21 |
|
Flagellum-specific ATP synthase, N-terminal domain; The N-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 FliI ATPase is the soluble export component that drives flagellar protein export, and it shows extensive similarity to the alpha and beta subunits of F1-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: 349741 [Multi-domain] Cd Length: 70 Bit Score: 87.58 E-value: 1.88e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596301 27 VEGRLLRMVGLTLEAEGLQAAVGSRCNVINESGyhpVQVEAEVMGFSGSKVYLMPVGSLAGIAPGARVVPLPD 99
Cdd:cd18117 1 VYGRVVRVVGLLLEAVGPQAPIGELCLIETADG---LSILAEVVGFSGEKVLLMPLGELSGLSPGARVVPLGR 70
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
73-393 |
9.06e-20 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 92.03 E-value: 9.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 73 SGSKVylMPVGSLAGIAPGARV---VPLPDTGRLPMGMSMLGRVLDGAGRALdGKggmraedwvpMDGPTINPLKRHPIS 149
Cdd:PTZ00185 104 SGQKV--MATGKLLYIPVGAGVlgkVVNPLGHEVPVGLLTRSRALLESEQTL-GK----------VDAGAPNIVSRSPVN 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 150 EPLDVGIRSINGLLTVGRGQRLGLFAGTGVGK-SVLLGMMTRFTRAD---------IIVVGLIGERGREVKEFIDEILGE 219
Cdd:PTZ00185 171 YNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKtSIAVSTIINQVRINqqilsknavISIYVSIGQRCSNVARIHRLLRSY 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 220 EGLKRSVVVASPADDAPLMRLRAAQYCTRIAEYFRDKGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLP 299
Cdd:PTZ00185 251 GALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHS 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 300 KLVERAG--NAEAGGGSITAFYTVLSEGDDQQDPIADAARGVLDGHFVLSRRLAEEGHYPAIDIEASISRVMPQVVEAEH 377
Cdd:PTZ00185 331 RLLERAAmlSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAM 410
|
330
....*....|....*.
gi 15596301 378 LRDAQRFKQLWSRYQQ 393
Cdd:PTZ00185 411 KAVAGKLKGILAEYRK 426
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
76-367 |
1.58e-19 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 90.80 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 76 KVYLMPVGSLAGIAPGARVVPLPDTGRLPMGMSMLGRVLDGAGRALDGKG-GMRAEDWVPMDGPTINP----LKRHPISE 150
Cdd:PRK07165 46 KAYLLINNEKGKIKINDELIELNNTNKVKTSKEYFGKIIDIDGNIIYPEAqNPLSKKFLPNTSSIFNLahglMTVKTLNE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 151 PLDVGIRSINGLLTVGRGQRLGLFAGTGVGK-SVLLGMMTRFTRADI--IVVGlIGERGREVKeFIDEILGEEG-LKRSV 226
Cdd:PRK07165 126 QLYTGIIAIDLLIPIGKGQRELIIGDRQTGKtHIALNTIINQKNTNVkcIYVA-IGQKRENLS-RIYETLKEHDaLKNTI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 227 VVASPADDAplmrlrAAQYctrIAEYFR-------DKGKNVLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLP 299
Cdd:PRK07165 204 IIDAPSTSP------YEQY---LAPYVAmahaeniSYNDDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHS 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596301 300 KLVERAGNAeAGGGSITAFYTVLSEGDDQQDPIADAARGVLDGHFVLSRRLAEEGHYPAIDIEASISR 367
Cdd:PRK07165 275 KLLERAGKF-KNRKTITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSR 341
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
188-366 |
9.68e-19 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 89.31 E-value: 9.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 188 MTRFTRADIIVVGLIGERGREVKEFIDEI-------LGEEGLKRSVVVASPADdAPLMRLRAAQYC-TRIAEYFRDKGKN 259
Cdd:PRK14698 676 LAKWSDAQVVIYIGCGERGNEMTDVLEEFpklkdpkTGKPLMERTVLIANTSN-MPVAAREASIYTgITIAEYFRDMGYD 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 260 VLLLMDSLTRYAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEAGG-----GSITAFYTVLSEGDDQQDPIAD 334
Cdd:PRK14698 755 VALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGsdyrvGSVSVIGAVSPPGGDFSEPVVQ 834
|
170 180 190
....*....|....*....|....*....|..
gi 15596301 335 AARGVLDGHFVLSRRLAEEGHYPAIDIEASIS 366
Cdd:PRK14698 835 NTLRVVKVFWALDADLARRRHFPAINWLTSYS 866
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
150-378 |
5.14e-17 |
|
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: 82.81 E-value: 5.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 150 EPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLL-----GMMTRFTRADIIVVgLIGERGREVKEFIDEILGEeglkr 224
Cdd:TIGR00767 150 STEDLSTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLqkiaqAITRNHPEVELIVL-LIDERPEEVTDMQRSVKGE----- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 225 svVVASPADDAPLMRLRAAQYCTRIAEYFRDKGKNVLLLMDSLTRYAQAQREIALAIGEpPATKGYPPSVFAKLPKLVER 304
Cdd:TIGR00767 224 --VVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGK-VLSGGVDANALHRPKRFFGA 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596301 305 AGNAEaGGGSITAFYTVLSE-GDDQQDPIADAARGVLDGHFVLSRRLAEEGHYPAIDIEASISRVMPQVVEAEHL 378
Cdd:TIGR00767 301 ARNIE-EGGSLTIIATALIDtGSRMDEVIFEEFKGTGNMELHLDRKLADRRIFPAIDIKKSGTRKEELLLTPEEL 374
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
165-388 |
1.45e-16 |
|
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: 79.17 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 165 VGRGQRLGLFAGTGVGKSVLLGMMTRFTRAD----IIVVGLIGERGREVKEFIDEILGEeglkrsvVVASPADDAPLMRL 240
Cdd:cd01128 13 IGKGQRGLIVAPPKAGKTTLLQNIANAIAKNhpevELIVLLIDERPEEVTDMRRSVKGE-------VVASTFDEPPERHV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 241 RAAQYCTRIAEYFRDKGKNVLLLMDSLTRYAQAQREIAlaigePPATKGYPPSVFAK---LPKLVERAGNAEAGGGSITA 317
Cdd:cd01128 86 QVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVV-----PSSGKTLSGGVDANalhKPKRFFGAARNIEEGGSLTI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596301 318 FYTVLSE-GDDQQDPIADAARGVLDGHFVLSRRLAEEGHYPAIDIEASISRvmpqvvEAEHLRDAQRFKQLW 388
Cdd:cd01128 161 IATALVDtGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTR------KEELLLTPEELQKIW 226
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
136-367 |
1.16e-14 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 75.12 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 136 DGPTINPLKR-HPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLL-----GMMTRFTRADIIVVgLIGERGREV 209
Cdd:PRK12608 100 DLTPLHPRERlRLETGSDDLSMRVVDLVAPIGKGQRGLIVAPPRAGKTVLLqqiaaAVAANHPEVHLMVL-LIDERPEEV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 210 KEFIDEILGEeglkrsvVVASPADDAPLMRLRAAQYCTRIAEYFRDKGKNVLLLMDSLTRYAQAQREIALAIGEPpATKG 289
Cdd:PRK12608 179 TDMRRSVKGE-------VYASTFDRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAYNNEVESSGRT-LSGG 250
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596301 290 YPPSVFAKLPKLVERAGNAEaGGGSITAFYTVLSE-GDDQQDPIADAARGVLDGHFVLSRRLAEEGHYPAIDIEASISR 367
Cdd:PRK12608 251 VDARALQRPKRLFGAARNIE-EGGSLTIIATALVDtGSRMDEVIFEEFKGTGNMEIVLDRELADKRVFPAIDIAKSGTR 328
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
165-367 |
8.30e-10 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 60.54 E-value: 8.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 165 VGRGQRlGLF-AGTGVGKSVLL-----GMMTRFTRADIIVVgLIGERGREVKEFideilgeeglKRSV---VVASPADDA 235
Cdd:PRK09376 166 IGKGQR-GLIvAPPKAGKTVLLqnianSITTNHPEVHLIVL-LIDERPEEVTDM----------QRSVkgeVVASTFDEP 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596301 236 PLMRLRAAQY----CTRIAEYfrdkGKNVLLLMDSLTRYAqaqREIALAIgePPATK----GYPPSVFAKLPKLVERAGN 307
Cdd:PRK09376 234 AERHVQVAEMviekAKRLVEH----GKDVVILLDSITRLA---RAYNTVV--PSSGKvlsgGVDANALHRPKRFFGAARN 304
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596301 308 AEaGGGSITAFYTVLSE-GDDQQDPIADAARGVLDGHFVLSRRLAEEGHYPAIDIEASISR 367
Cdd:PRK09376 305 IE-EGGSLTIIATALIDtGSRMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINRSGTR 364
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
29-102 |
5.64e-07 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 46.92 E-value: 5.64e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596301 29 GRLLRMVGLTLEAEGL-QAAVGSRCNVINESGYHPVQVEAEVMGFSGSKVYLMPVGSLAGIAPGARVVPlpdTGR 102
Cdd:cd01426 2 GRVIRVNGPLVEAELEgEVAIGEVCEIERGDGNNETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEP---TGR 73
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
377-438 |
6.40e-07 |
|
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: 46.67 E-value: 6.40e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596301 377 HLRDAQRFKQLWSRYQQSRDLISVGAYVAGgDPETDLAIARFPVMRQFLRQGLDESESLAES 438
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDAL-SEADKKTLSRGRRLEEFLQQGQFEPETIEDT 61
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