|
Name |
Accession |
Description |
Interval |
E-value |
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
1-452 |
0e+00 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 883.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 1 MSSRLDTWLGALASLERRIPTLPEARRYGKLTRATGLVLEATGLQLPIGATCRVERHDGHQVLDVEAEVVGFNGRQLFLM 80
Cdd:PRK07960 1 MTTRLTRWLTTLDNFEAKMAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCVIERQNGSETHEVESEVVGFNGQRLFLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 81 PLEEVEGIVPGARVWAP---AAALNSGKQLPLGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLD 157
Cdd:PRK07960 81 PLEEVEGILPGARVYARnisGEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 158 VGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPAD 237
Cdd:PRK07960 161 TGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 238 VSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGG 317
Cdd:PRK07960 241 VSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 318 SITAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQR 397
Cdd:PRK07960 321 SITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLLSSFQR 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 506351991 398 NRDLISVGAYARGSDPLLDQAIALYPQLEAFLQQGIFERSDYQQSCTALQTLFST 452
Cdd:PRK07960 401 NRDLVSVGAYAKGSDPMLDKAIALWPQLEAFLQQGIFERADWEDSLQALERIFPT 455
|
|
| FliI_clade1 |
TIGR03496 |
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: 274607 [Multi-domain] Cd Length: 411 Bit Score: 741.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 29 GKLTRATGLVLEATGLQLPIGATCRVERHDGHQVldvEAEVVGFNGRQLFLMPLEEVEGIVPGARVWApaaaLNSGKQLP 108
Cdd:TIGR03496 1 GRVTRVVGLVLEAVGLRAPVGSRCEIESSDGDPI---EAEVVGFRGDRVLLMPLEDVEGLRPGARVFP----LGGPLRLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 109 LGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLDVGVRAINALLTVGRGQRMGLFAGSGVGKSVL 188
Cdd:TIGR03496 74 VGDSLLGRVIDGLGRPLDGKGPLDAGERVPLYAPPINPLKRAPIDEPLDVGVRAINGLLTVGRGQRMGIFAGSGVGKSTL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 189 LGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIM 268
Cdd:TIGR03496 154 LGMMARYTEADVVVVGLIGERGREVKEFIEDILGEEGLARSVVVAATADESPLMRLRAAFYATAIAEYFRDQGKDVLLLM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 269 DSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARAILDGHV 348
Cdd:TIGR03496 234 DSLTRFAMAQREIALAIGEPPATKGYPPSVFAKLPQLVERAGNGEEGKGSITAFYTVLVEGDDQQDPIADAARAILDGHI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 349 VLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQRNRDLISVGAYARGSDPLLDQAIALYPQLEAF 428
Cdd:TIGR03496 314 VLSRELAEQGHYPAIDILASISRVMPDVVSPEHRQAARRFKQLLSRYQENRDLISIGAYQAGSDPELDQAIALYPRIEAF 393
|
410
....*....|....*...
gi 506351991 429 LQQGIFERSDYQQSCTAL 446
Cdd:TIGR03496 394 LQQGMRERASFEESLEAL 411
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
9-450 |
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: 736.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 9 LGALASLERRIPTLPEARRYGKLTRATGLVLEATGLQLPIGATCRVERHDGHqvlDVEAEVVGFNGRQLFLMPLEEVEGI 88
Cdd:COG1157 1 LDRLARLLARLEELPPVRVSGRVTRVVGLLIEAVGPDASIGELCEIETADGR---PVLAEVVGFRGDRVLLMPLGDLEGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 89 VPGARVWApaaaLNSGKQLPLGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLDVGVRAINALLT 168
Cdd:COG1157 78 SPGARVVP----TGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 169 VGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLRMQGAA 248
Cdd:COG1157 154 VGRGQRIGIFAGSGVGKSTLLGMIARNTEADVNVIALIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 249 YATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTE 328
Cdd:COG1157 234 TATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERA--GNGGKGSITAFYTVLVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 329 GDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQRNRDLISVGAYA 408
Cdd:COG1157 312 GDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENEDLIRIGAYQ 391
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 506351991 409 RGSDPLLDQAIALYPQLEAFLQQGIFERSDYQQSCTALQTLF 450
Cdd:COG1157 392 PGSDPELDEAIALIPAIEAFLRQGMDERVSFEESLAQLAELL 433
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
2-449 |
0e+00 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 656.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 2 SSRLDTWLGALASLERRI-PTLPEARryGKLTRATGLVLEATGLQLPIGATCRVERHDGhqvlDVEAEVVGFNGRQLFLM 80
Cdd:PRK08972 1 QNRQHQLLNRLKQYKVKVpPFRAVAS--GKLVRVVGLTLEATGCRAPVGSLCSIETMAG----ELEAEVVGFDGDLLYLM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 81 PLEEVEGIVPGARVwapaAALNSGKQLPLGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLDVGV 160
Cdd:PRK08972 75 PIEELRGVLPGARV----TPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 161 RAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSP 240
Cdd:PRK08972 151 RAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTTADVIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 241 LLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSIT 320
Cdd:PRK08972 231 LMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSIT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 321 AFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQRNRD 400
Cdd:PRK08972 311 AFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLYQQNRD 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 506351991 401 LISVGAYARGSDPLLDQAIALYPQLEAFLQQGIFERSDYQQSCTALQTL 449
Cdd:PRK08972 391 LISIGAYKQGSDPRIDNAIRLQPAMNAFLQQTMKEAVPYDMSVNMLKQL 439
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
5-451 |
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: 636.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 5 LDTWLGALASLERRIPTLPEARRYGKLTRATGLVLEATGLQLPIGATCRVERHDGHQvlDVEAEVVGFNGRQLFLMPLEE 84
Cdd:TIGR01026 1 MERNLTTFYNRLCQEMDLRLVKRVGRVTKVKGLLIEAVGPQASVGDLCLIERRGSEG--RLVAEVVGFNGEFVFLMPYEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 85 VEGIVPGARVWApaaaLNSGKQLPLGPALLGRVLDGSARPLDGLP-PPDESDHGGLSSQPFNPLQRTPITQVLDVGVRAI 163
Cdd:TIGR01026 79 VEGVRPGSKVLA----TGEGLSIKVGDGLLGRVLDGLGKPIDGKGkFLDNVETEGLITAPINPLKRAPIREILSTGVRSI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 164 NALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLR 243
Cdd:TIGR01026 155 DGLLTVGKGQRIGIFAGSGVGKSTLLGMIARNTEADVNVIALIGERGREVREFIEHDLGEEGLKRSVVVVATSDQSPLLR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 244 MQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFY 323
Cdd:TIGR01026 235 LKGAYVATAIAEYFRDQGKDVLLLMDSVTRFAMAQREIGLAAGEPPATKGYTPSVFSTLPRLLERA--GASGKGSITAFY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 324 TVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQRNRDLIS 403
Cdd:TIGR01026 313 TVLVEGDDMNEPIADSVRGILDGHIVLSRALAQRGHYPAIDVLASISRLMTAIVSEEHRRAARKFRELLSKYKDNEDLIR 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 506351991 404 VGAYARGSDPLLDQAIALYPQLEAFLQQGIFERSDYQQSCTALQTLFS 451
Cdd:TIGR01026 393 IGAYQRGSDRELDFAIAKYPKLERFLKQGINEKVNFEESLQQLEEIFR 440
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
1-450 |
0e+00 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 615.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 1 MSSRLDTWLGALAslerrIPTLPEARryGKLTRATGLVLEATGLQLPIGATCRVERHDGHQVLDVEAEVVGFNGRQLFLM 80
Cdd:PRK05688 8 FAKRLEGYAEAIS-----LPAQPVVE--GRLLRMVGLTLEAEGLRAAVGSRCLVINDDSYHPVQVEAEVMGFSGDKVFLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 81 PLEEVEGIVPGARVwapaAALNSGKQLPLGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLDVGV 160
Cdd:PRK05688 81 PVGSVAGIAPGARV----VPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 161 RAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSP 240
Cdd:PRK05688 157 RSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEADIIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 241 LLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSIT 320
Cdd:PRK05688 237 LMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSIT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 321 AFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQRNRD 400
Cdd:PRK05688 317 AFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQSRD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 506351991 401 LISVGAYARGSDPLLDQAIALYPQLEAFLQQGIFERSDYQQSCTALQTLF 450
Cdd:PRK05688 397 LISVGAYVAGGDPETDLAIARFPHLVQFLRQGLRENVSLAQSREQLAAIF 446
|
|
| FliI_clade2 |
TIGR03497 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
29-450 |
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: 547.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 29 GKLTRATGLVLEATGLQLPIGATCRVERHDGHQVLdveAEVVGFNGRQLFLMPLEEVEGIVPGARVWApaaalnSGKQL- 107
Cdd:TIGR03497 1 GKVTRVIGLTIESKGPKASIGELCSILTKGGKPVL---AEVVGFKEENVLLMPLGEVEGIGPGSLVIA------TGRPLa 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 108 -PLGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLDVGVRAINALLTVGRGQRMGLFAGSGVGKS 186
Cdd:TIGR03497 72 iKVGKGLLGRVLDGLGRPLDGEGPIIGEEPYPLDNPPPNPLKRPRIRDPLETGIKAIDGLLTIGKGQRVGIFAGSGVGKS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 187 VLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLL 266
Cdd:TIGR03497 152 TLLGMIARNAKADINVIALIGERGREVRDFIEKDLGEEGLKRSVVVVATSDQPALMRLKAAFTATAIAEYFRDQGKDVLL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 267 IMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQDPIADSARAILDG 346
Cdd:TIGR03497 232 MMDSVTRFAMAQREIGLAVGEPPTTRGYTPSVFSLLPKLLERS--GNSQKGSITGFYTVLVDGDDMNEPIADAVRGILDG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 347 HVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQRNRDLISVGAYARGSDPLLDQAIALYPQLE 426
Cdd:TIGR03497 310 HIVLSRELAAKNHYPAIDVLASVSRVMNEIVSEEHKELAGKLRELLAVYKEAEDLINIGAYKRGSNPKIDEAIRYIEKIN 389
|
410 420
....*....|....*....|....
gi 506351991 427 AFLQQGIFERSDYQQSCTALQTLF 450
Cdd:TIGR03497 390 SFLKQGIDEKFTFEETVQLLKELL 413
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
12-451 |
2.02e-178 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 506.18 E-value: 2.02e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 12 LASLERRIPTLPEARRYGKLTRATGLVLEATGLQLPIGATCRV-ERHDGHQVldVEAEVVGFNGRQLFLMPLEEVEGIVP 90
Cdd:PRK07721 3 TQQLIDCIETLDPYKRYGKVSRVIGLMIESKGPESSIGDVCYIhTKGGGDKA--IKAEVVGFKDEHVLLMPYTEVAEIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 91 GARVWAPAAALnsgkQLPLGPALLGRVLDGSARPLDGLPPPDesdhgGLSS-----QPFNPLQRTPITQVLDVGVRAINA 165
Cdd:PRK07721 81 GCLVEATGKPL----EVKVGSGLIGQVLDALGEPLDGSALPK-----GLAPvstdqDPPNPLKRPPIREPMEVGVRAIDS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 166 LLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLRMQ 245
Cdd:PRK07721 152 LLTVGKGQRVGIFAGSGVGKSTLMGMIARNTSADLNVIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 246 GAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTV 325
Cdd:PRK07721 232 GAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERT--GTNASGSITAFYTV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 326 LTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQRNRDLISVG 405
Cdd:PRK07721 310 LVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLINIG 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 506351991 406 AYARGSDPLLDQAIALYPQLEAFLQQGIFERSDYQQSCTALQTLFS 451
Cdd:PRK07721 390 AYKRGSSREIDEAIQFYPQIISFLKQGTDEKATFEESIQALLSLFG 435
|
|
| FliI_clade3 |
TIGR03498 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
29-449 |
7.64e-170 |
|
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: 483.34 E-value: 7.64e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 29 GKLTRATGLVLEATGLQ--LPIGATCRVERHDGHQVLdveAEVVGFNGRQLFLMPLEEVEGIVPGARVWApaaaLNSGKQ 106
Cdd:TIGR03498 1 GRVTAVTGLLIEVRGLSraVRLGDRCAIRARDGRPVL---AEVVGFNGDRVLLMPFEPLEGVGLGCAVFA----REGPLA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 107 LPLGPALLGRVLDGSARPLDGLPP-PDESDHGGLSSQPFNPLQRTPITQVLDVGVRAINALLTVGRGQRMGLFAGSGVGK 185
Cdd:TIGR03498 74 VRPHPSWLGRVINALGEPIDGKGPlPQGERRYPLRASPPPAMSRARVGEPLDTGVRVIDTFLPLCRGQRLGIFAGSGVGK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 186 SVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVL 265
Cdd:TIGR03498 154 STLLSMLARNTDADVVVIALVGERGREVREFLEDDLGEEGLKRSVVVVATSDESPLMRRQAAYTATAIAEYFRDQGKDVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 266 LIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARAILD 345
Cdd:TIGR03498 234 LLMDSVTRFAMAQREIGLAAGEPPVARGYTPSVFSELPRLLERAGPGAEGKGSITGIFTVLVDGDDHNEPVADAVRGILD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 346 GHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQRNRDLISVGAYARGSDPLLDQAIALYPQL 425
Cdd:TIGR03498 314 GHIVLDRAIAERGRYPAINVLASVSRLAPRVWSPEERKLVRRLRALLARYEETEDLIRLGAYRKGSDPELDEAIRLVPKI 393
|
410 420
....*....|....*....|....
gi 506351991 426 EAFLQQGIFERSDYQQSCTALQTL 449
Cdd:TIGR03498 394 YEFLTQGPDEPTSLQDPFADLAAI 417
|
|
| III_secr_ATP |
TIGR02546 |
type III secretion apparatus H+-transporting two-sector ATPase; [Protein fate, Protein and ... |
26-450 |
4.99e-168 |
|
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: 479.12 E-value: 4.99e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 26 RRYGKLTRATGLVLEATGLQLPIGATCRVERHDGhqvLDVEAEVVGFNGRQLFLMPLEEVEGIVPGARVwapaAALNSGK 105
Cdd:TIGR02546 4 RVRGRVTEVSGTLLKAVLPGARVGELCLIRRRDP---SQLLAEVVGFTGDEALLSPLGELHGISPGSEV----IPTGRPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 106 QLPLGPALLGRVLDGSARPLDG--LPPPDESDHGGLSSQPFNPLQRTPITQVLDVGVRAINALLTVGRGQRMGLFAGSGV 183
Cdd:TIGR02546 77 SIRVGEALLGRVLDGFGRPLDGkgELPAGEIETRPLDADPPPPMSRQPIDQPLPTGVRAIDGLLTCGEGQRIGIFAGAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 184 GKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQH 263
Cdd:TIGR02546 157 GKSTLLGMIARGASADVNVIALIGERGREVREFIEHHLGEEGRKRSVLVVSTSDRPSLERLKAAYTATAIAEYFRDQGKR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 264 VLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQDPIADSARAI 343
Cdd:TIGR02546 237 VLLMMDSLTRFARALREIGLAAGEPPARGGYPPSVFSSLPRLLERA--GNGEKGSITALYTVLVEGDDMNDPIADEVRSI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 344 LDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQRNRDLISVGAYARGSDPLLDQAIALYP 423
Cdd:TIGR02546 315 LDGHIVLSRALAERNHYPAIDVLASLSRVMSQVVSTEHRRAAGKLRRLLATYKEVELLIRLGEYQPGSDPETDDAIDKID 394
|
410 420
....*....|....*....|....*..
gi 506351991 424 QLEAFLQQGIFERSDYQQSCTALQTLF 450
Cdd:TIGR02546 395 AIRAFLRQSTDEYSPYEETLEQLHALV 421
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
11-452 |
2.81e-160 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 459.74 E-value: 2.81e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 11 ALASLERRIPTLPEARRYGKLTRATGLVLEATGLQLPIGATCRVERHDGHQVldvEAEVVGFNGRQLFLMPLEEVEGIVP 90
Cdd:PRK07196 1 ALDHALKSIENIHLARVAGRLVRVTGLLLESVGCRLAIGQRCRIESVDETFI---EAQVVGFDRDITYLMPFKHPGGVLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 91 GARVWApaaALNSGkQLPLGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLDVGVRAINALLTVG 170
Cdd:PRK07196 78 GARVFP---SEQDG-ELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 171 RGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLRMQGAAYA 250
Cdd:PRK07196 154 KGQRVGLMAGSGVGKSVLLGMITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 251 TRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgNGISGGGSITAFYTVLTEGD 330
Cdd:PRK07196 234 HAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESA-GNSSGNGTMTAIYTVLAEGD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 331 DQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQRNRDLISVGAYARG 410
Cdd:PRK07196 313 DQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVAG 392
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 506351991 411 SDPLLDQAIALYPQLEAFLQQGIFERSDYQQSCTALQTLFST 452
Cdd:PRK07196 393 ADPMADQAVHYYPAITQFLRQEVGHPALFSASVEQLTGMFPS 434
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
11-452 |
7.57e-159 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 456.36 E-value: 7.57e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 11 ALASLERRIPTLPEARRYGKLTRATGLVLEATGLQ--LPIGATCRVERHDGHQVldvEAEVVGFNGRQLFLMPLEEVEGI 88
Cdd:PRK08927 1 MMAALAAAIGDIDTLVIYGRVVAVRGLLVEVAGPIhaLSVGARIVVETRGGRPV---PCEVVGFRGDRALLMPFGPLEGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 89 VPGARvwapAAALNSGKQLPLGPALLGRVLDGSARPLDGLPPPDESDHG-GLSSQPFNPLQRTPITQVLDVGVRAINALL 167
Cdd:PRK08927 78 RRGCR----AVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPyPLRAPPPPAHSRARVGEPLDLGVRALNTFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 168 TVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLRMQgA 247
Cdd:PRK08927 154 TCCRGQRMGIFAGSGVGKSVLLSMLARNADADVSVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQ-A 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 248 AYAT-RIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVL 326
Cdd:PRK08927 233 AYLTlAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGEGTITGLFTVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 327 TEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQRNRDLISVGA 406
Cdd:PRK08927 313 VDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLGA 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 506351991 407 YARGSDPLLDQAIALYPQLEAFLQQGIFERSDYQQSCTALQTLFST 452
Cdd:PRK08927 393 YRAGSDPEVDEAIRLNPALEAFLRQGKDEATSLAEGYARLAQILGG 438
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
106-371 |
1.39e-153 |
|
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: 436.22 E-value: 1.39e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 106 QLPLGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLDVGVRAINALLTVGRGQRMGLFAGSGVGK 185
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 186 SVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVL 265
Cdd:cd01136 81 STLLGMIARNTDADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 266 LIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQDPIADSARAILD 345
Cdd:cd01136 161 LLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERA--GNGEKGSITAFYTVLVEGDDFNDPIADEVRSILD 238
|
250 260
....*....|....*....|....*.
gi 506351991 346 GHVVLSRRLAEAGHYPAIDIEASISR 371
Cdd:cd01136 239 GHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
11-449 |
1.53e-147 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 427.18 E-value: 1.53e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 11 ALASLERRIPTLPEARRYGKLTRATGLVLEATGLQLPIGATCRVERHDGHQvlDVEAEVVGFNGRQLFLMPLEEVEGIVP 90
Cdd:PRK08472 2 PLESLKNKLQKFNLSPRFGSITKISPTIIEADGLNPSVGDIVKIESSDNGK--ECLGMVVVIEKEQFGISPFSFIEGFKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 91 GARVWApaaaLNSGKQLPLGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLDVGVRAINALLTVG 170
Cdd:PRK08472 80 GDKVFI----SKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 171 RGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEgRQRSVVIAAPADVSPLLRMQGAAYA 250
Cdd:PRK08472 156 KGQKLGIFAGSGVGKSTLMGMIVKGCLAPIKVVALIGERGREIPEFIEKNLGGD-LENTVIVVATSDDSPLMRKYGAFCA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 251 TRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSiTAFYTVLTEGD 330
Cdd:PRK08472 235 MSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGKGSI-TAFFTVLVEGD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 331 DQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQRNRDLISVGAYARG 410
Cdd:PRK08472 314 DMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAYQKG 393
|
410 420 430
....*....|....*....|....*....|....*....
gi 506351991 411 SDPLLDQAIALYPQLEAFLQQGIFERSDYQQSCTALQTL 449
Cdd:PRK08472 394 NDKELDEAISKKEFMEQFLKQNPNELFPFEQTFEQLEEI 432
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-449 |
1.83e-142 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 414.53 E-value: 1.83e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 29 GKLTRATGLVLEATGLQLPIGATCRVERHDghQVLDVEAEVVGFNGRQLFLMPLEEVEGIVPGARVwAPAAALNsgkQLP 108
Cdd:PRK06936 25 GRVTQVTGTILKAVVPGVRIGELCYLRNPD--NSLSLQAEVIGFAQHQALLTPLGEMYGISSNTEV-SPTGTMH---QVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 109 LGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLDVGVRAINALLTVGRGQRMGLFAGSGVGKSVL 188
Cdd:PRK06936 99 VGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 189 LGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIM 268
Cdd:PRK06936 179 LASLIRSAEVDVTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 269 DSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQDPIADSARAILDGHV 348
Cdd:PRK06936 259 DSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERA--GQSDKGSITALYTVLVEGDDMTEPVADETRSILDGHI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 349 VLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQRNRDLISVGAYARGSDPLLDQAIALYPQLEAF 428
Cdd:PRK06936 337 ILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIGEYQKGQDKEADQAIERIGAIRGF 416
|
410 420
....*....|....*....|.
gi 506351991 429 LQQGIFERSDYQQSCTALQTL 449
Cdd:PRK06936 417 LRQGTHELSHFNETLNLLETL 437
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
15-451 |
1.05e-140 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 410.36 E-value: 1.05e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 15 LERRIPTLPEARRYGKLTRATGLVLEATGLQLPIGATCRVErHDGhqvldVEAEVVGFNGRQLFLMPLEEVEGIVPGARV 94
Cdd:PRK06820 17 LTRPSAPPEGLRYRGPIVEIGPTLLRASLPGVAQGELCRIE-PQG-----MLAEVVSIEQEMALLSPFASSDGLRCGQWV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 95 wapaAALNSGKQLPLGPALLGRVLDGSARPLDGlPPPDESDHGGLSSQPFNPLQRTPITQVLDVGVRAINALLTVGRGQR 174
Cdd:PRK06820 91 ----TPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 175 MGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLRMQGAAYATRIA 254
Cdd:PRK06820 166 IGIFAAAGVGKSTLLGMLCADSAADVMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 255 EDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQD 334
Cdd:PRK06820 246 EYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERT--GNSDRGSITAFYTVLVEGDDMNE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 335 PIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQRNRDLISVGAYARGSDPL 414
Cdd:PRK06820 324 PVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGEYQAGEDLQ 403
|
410 420 430
....*....|....*....|....*....|....*..
gi 506351991 415 LDQAIALYPQLEAFLQQGIFERSDYQQSCTALQTLFS 451
Cdd:PRK06820 404 ADEALQRYPAICAFLQQDHSETAHLETTLEHLAQVVG 440
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
4-449 |
5.40e-134 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 392.98 E-value: 5.40e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 4 RLDTWLGALASLERRIPTLPEARRYGKLTRATGLVLEATGLQLPIGATCRVERHDGhqVLDVEAEVVGFNGRQLFLMPLE 83
Cdd:PRK09099 1 ALAELSRLADALERELAALPAVRRTGKVVEVIGTLLRVSGLDVTLGELCELRQRDG--TLLQRAEVVGFSRDVALLSPFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 84 EVEGIVPGARVWAPAAALNsgkqLPLGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLDVGVRAI 163
Cdd:PRK09099 79 ELGGLSRGTRVIGLGRPLS----VPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 164 NALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLR 243
Cdd:PRK09099 155 DGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQCDVNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIER 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 244 MQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFY 323
Cdd:PRK09099 235 AKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERA--GMGETGSITALY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 324 TVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQRNRDLIS 403
Cdd:PRK09099 313 TVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQ 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 506351991 404 VGAYARGSDPLLDQAIALYPQLEAFLQQGIFERSDYQQSCTALQTL 449
Cdd:PRK09099 393 VGEYRAGSDPVADEAIAKIDAIRDFLSQRTDEYSDPDATLAALAEL 438
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
26-431 |
7.24e-122 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 361.96 E-value: 7.24e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 26 RRYGKLTRATGLVLEATGLQLPIGATCRVERHDGHqvldveAEVVGFNGRQLFLMPLEEVEGIVPGARVwapaAALNSGK 105
Cdd:PRK07594 20 CRWGRIQDVSATLLNAWLPGVFMGELCCIKPGEEL------AEVVGINGSKALLSPFTSTIGLHCGQQV----MALRRRH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 106 QLPLGPALLGRVLDGSARPLDGLPPPDESdHGGLSSQPFNPLQRTPITQVLDVGVRAINALLTVGRGQRMGLFAGSGVGK 185
Cdd:PRK07594 90 QVPVGEALLGRVIDGFGRPLDGRELPDVC-WKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 186 SVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVL 265
Cdd:PRK07594 169 STLLAMLCNAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 266 LIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQDPIADSARAILD 345
Cdd:PRK07594 249 LLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERT--GMGEKGSITAFYTVLVEGDDMNEPLADEVRSLLD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 346 GHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQRNRDLISVGAYARGSDPLLDQAIALYPQL 425
Cdd:PRK07594 327 GHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEYQRGVDTDTDKAIDTYPDI 406
|
....*.
gi 506351991 426 EAFLQQ 431
Cdd:PRK07594 407 CTFLRQ 412
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
106-372 |
1.24e-118 |
|
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: 347.52 E-value: 1.24e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 106 QLPLGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLDVGVRAINALLTVGRGQRMGLFAGSGVGK 185
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 186 SVLLGMMARYTQ---ADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQ 262
Cdd:cd19476 81 TVLAMQLARNQAkahAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 263 HVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARA 342
Cdd:cd19476 161 HVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTPGDDLTDPIPDNTFA 240
|
250 260 270
....*....|....*....|....*....|
gi 506351991 343 ILDGHVVLSRRLAEAGHYPAIDIEASISRA 372
Cdd:cd19476 241 ILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
26-441 |
2.92e-116 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 347.37 E-value: 2.92e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 26 RRYGKLTRATGLVLEATGLQLPIGATCRVERHDGHQVLDVEAEVVGFNGRQLFLMPLEEVEG------IVPgarvwapaa 99
Cdd:PRK08149 5 QRLAHPLRIQGPIIEAELPDVAIGEICEIRAGWHSNEVIARAQVVGFQRERTILSLIGNAQGlsrqvvLKP--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 100 alnSGKQL--PLGPALLGRVLDGSARPLDGLPPPDESDHGGLS----SQPFNPLQRTPITQVLDVGVRAINALLTVGRGQ 173
Cdd:PRK08149 76 ---TGKPLsvWVGEALLGAVLDPTGKIVERFDAPPTVGPISEErvidVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 174 RMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLRMQGAAYATRI 253
Cdd:PRK08149 153 RMGIFASAGCGKTSLMNMLIEHSEADVFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 254 AEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQ 333
Cdd:PRK08149 233 AEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERP--GATLAGSITAFYTVLLESEEEP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 334 DPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQRNRDLISVGAYARGSDP 413
Cdd:PRK08149 311 DPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGEYRRGENA 390
|
410 420
....*....|....*....|....*...
gi 506351991 414 LLDQAIALYPQLEAFLQQGIFERSDYQQ 441
Cdd:PRK08149 391 DNDRAMDKRPALEAFLKQDVAEKSSFSD 418
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
159-370 |
1.64e-115 |
|
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: 337.41 E-value: 1.64e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 159 GVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADV 238
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLGSGALKRTVVVVATSDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 239 SPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGS 318
Cdd:pfam00006 81 PPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKGKGGS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 506351991 319 ITAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASIS 370
Cdd:pfam00006 161 ITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
5-431 |
4.59e-109 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 329.65 E-value: 4.59e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 5 LDTWLGALAS-LERRIPTLPEARRYGKLTRATGLVLEATGLQ--LPIGATCRVERHDGHQVldveAEVVGFNGRQLFLMP 81
Cdd:PRK06002 3 PDNALARLAAlVERYAAPEPLVRIGGTVSEVTASHYRVRGLSrfVRLGDFVAIRADGGTHL----GEVVRVDPDGVTVKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 82 LEEVEGIVPGARVWAPAAalnsgKQLPLGPALLGRVLDGSARPLDGLPPPDESDHG-GLSSQPFNPLQRTPITQVLDVGV 160
Cdd:PRK06002 79 FEPRIEIGLGDAVFRKGP-----LRIRPDPSWKGRVINALGEPIDGLGPLAPGTRPmSIDATAPPAMTRARVETGLRTGV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 161 RAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEgRQRSVVIAAPADVSP 240
Cdd:PRK06002 154 RVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGREVREFLEDTLADN-LKKAVAVVATSDESP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 241 LLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSIT 320
Cdd:PRK06002 233 MMRRLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEGGGSIT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 321 AFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQRNRD 400
Cdd:PRK06002 313 GIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEETRD 392
|
410 420 430
....*....|....*....|....*....|.
gi 506351991 401 LISVGAYARGSDPLLDQAIALYPQLEAFLQQ 431
Cdd:PRK06002 393 LRLIGGYRAGSDPDLDQAVDLVPRIYEALRQ 423
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
29-449 |
6.01e-91 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 282.64 E-value: 6.01e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 29 GKLTRATGLVLEATGLQLPIGATCRVERHDghqvldVEAEVVGFNGRQLFLMPLEEVEGIVPGARVWAPAAALnsgkQLP 108
Cdd:PRK06793 23 GKVHSVQEQFFVAKGPKAKIGDVCFVGEHN------VLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLIAEDV----VIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 109 LGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLDVGVRAINALLTVGRGQRMGLFAGSGVGKSVL 188
Cdd:PRK06793 93 RGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 189 LGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIM 268
Cdd:PRK06793 173 LGMIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 269 DSLTRYAMAQREIALAIGEPPaTKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQDPIADSARAILDGHV 348
Cdd:PRK06793 253 DSVTRFADARRSVDIAVKELP-IGGKTLLMESYMKKLLERS--GKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 349 VLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQRNRDLISVGAYARGSD-PLLDQAIALYPQLEA 427
Cdd:PRK06793 330 VLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGTIQENAEnAYIFECKNKVEGINT 409
|
410 420
....*....|....*....|..
gi 506351991 428 FLQQGIFERSDYQQSCTALQTL 449
Cdd:PRK06793 410 FLKQGRSDSFQFDDIVEAMHHI 431
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
26-449 |
3.69e-88 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 275.63 E-value: 3.69e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 26 RRYGKLTRATGLVLEATGLQLPIGATCRVERHDGHQVLdveAEVVGFNGRQLFLMPLEEVEGIVPGARVwapaAALNSGK 105
Cdd:PRK05922 18 RECGLLSRVSGNLLEAQGLSACLGELCQISLSKSPPIL---AEVIGFHNRTTLLMSLSPIHYVALGAEV----LPLRRPP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 106 QLPLGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLDVGVRAINALLTVGRGQRMGLFAGSGVGK 185
Cdd:PRK05922 91 SLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 186 SVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPA-DVSPLLRMQGAAyATRIAEDFRDRGQHV 264
Cdd:PRK05922 171 SSLLSTIAKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAhETAPTKVIAGRA-AMTIAEYFRDQGHRV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 265 LLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGdDQQDPIADSARAIL 344
Cdd:PRK05922 250 LFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERA--GNNDKGSITALYAILHYP-NHPDIFTDYLKSLL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 345 DGHVVLSRRlAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSYQRNRDLISVGAYARGSDPLLDQAIALYPQ 424
Cdd:PRK05922 327 DGHFFLTPQ-GKALASPPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGAYVPGQDAHLDRAVKLLPS 405
|
410 420
....*....|....*....|....*
gi 506351991 425 LEAFLQQGIFERSDYQQSCTALQTL 449
Cdd:PRK05922 406 IKQFLSQPLSSYCALHNTLKQLEAL 430
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
53-401 |
4.30e-38 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 143.81 E-value: 4.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 53 RVERHDGH----QVLDVEAEVVGFngrQLFlmplEEVEGIVP-GARVWApaaaLNSGKQLPLGPALLGRVLDGSARPLDG 127
Cdd:PRK04196 30 EIELPNGEkrrgQVLEVSEDKAVV---QVF----EGTTGLDLkDTKVRF----TGEPLKLPVSEDMLGRIFDGLGRPIDG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 128 LPPP---DESDHGGlssQPFNPLQRTPITQVLDVGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARytQADV---- 200
Cdd:PRK04196 99 GPEIipeKRLDING---APINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIAR--QAKVlgee 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 201 ----IVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLRMQGAAYATRIAE--DFrDRGQHVLLIMDSLTRY 274
Cdd:PRK04196 174 enfaVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEylAF-EKGMHVLVILTDMTNY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 275 AMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFyTVLT-EGDDQQDPIADSARAILDGHVVLSRR 353
Cdd:PRK04196 253 CEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQI-PILTmPDDDITHPIPDLTGYITEGQIVLSRE 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 506351991 354 LAEAGHYPAIDIEASISRAMTSLIDEAH----YARVRSfkQLLSSYQRNRDL 401
Cdd:PRK04196 332 LHRKGIYPPIDVLPSLSRLMKDGIGEGKtredHKDVAN--QLYAAYARGKDL 381
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
28-434 |
2.68e-37 |
|
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: 141.78 E-value: 2.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 28 YGKLTRATGLVLEA--TGLQLP-IGATCRVE-RHDGHQVLDVEAEVVGFNGRQLFLMPleeVEGIVPGARVwapaaaLNS 103
Cdd:TIGR01039 2 KGKVVQVIGPVVDVefEQGELPrIYNALKVQnRAESELTLEVAQHLGDDTVRTIAMGS---TDGLVRGLEV------IDT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 104 GK--QLPLGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLDVGVRAINALLTVGRGQRMGLFAGS 181
Cdd:TIGR01039 73 GApiSVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 182 GVGKSVLLGMMAR---YTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLRMQGAAYATRIAEDFR 258
Cdd:TIGR01039 153 GVGKTVLIQELINniaKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 259 D-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERagNGISGGGSITAFYTVLTEGDDQQDPIA 337
Cdd:TIGR01039 233 DeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQER--ITSTKTGSITSVQAVYVPADDLTDPAP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 338 DSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMT-SLIDEAHYARVRSFKQLLSSYQRNRDLISVgayaRGSDPLLD 416
Cdd:TIGR01039 311 ATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVGEEHYDVARGVQQILQRYKELQDIIAI----LGMDELSE 386
|
410 420
....*....|....*....|.
gi 506351991 417 Q---AIALYPQLEAFLQQGIF 434
Cdd:TIGR01039 387 EdklTVERARRIQRFLSQPFF 407
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
106-377 |
7.20e-37 |
|
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: 136.58 E-value: 7.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 106 QLPLGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLDVGVRAINALLTVGRGQRMGLFAGSGVGK 185
Cdd:cd01135 3 KLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLPH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 186 SVLLGMMARytQADV--------IVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLRMQGAAYATRIAEDF 257
Cdd:cd01135 83 NELAAQIAR--QAGVvgseenfaIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 258 R-DRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFyTVLT-EGDDQQDP 335
Cdd:cd01135 161 AyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQI-PILTmPNDDITHP 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 506351991 336 IADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLI 377
Cdd:cd01135 240 IPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGI 281
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
106-371 |
6.54e-33 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 130.04 E-value: 6.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 106 QLPLGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLDVGVRAINALLTVGRGQRMGLFAGSGVGK 185
Cdd:PRK13343 96 EVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 186 SVLlGMMARYTQ--ADVIVVG-LIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPllrmqGAAY-----ATRIAEDF 257
Cdd:PRK13343 176 TAI-AIDAIINQkdSDVICVYvAIGQKASAVARVIETLREHGALEYTTVVVAEASDPP-----GLQYlapfaGCAIAEYF 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 258 RDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGG--SITAFYTVLTEGDDQQDP 335
Cdd:PRK13343 250 RDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGggSLTALPIIETLAGELSAY 329
|
250 260 270
....*....|....*....|....*....|....*.
gi 506351991 336 IADSARAILDGHVVLSRRLAEAGHYPAIDIEASISR 371
Cdd:PRK13343 330 IPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
106-371 |
6.36e-32 |
|
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: 122.67 E-value: 6.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 106 QLPLGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLDVGVRAINALLTVGRGQRMGLFAGSGVGK 185
Cdd:cd01132 3 EVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 186 -SVLLGMMARYTQADVIVVGL-IGERGREVKDfIENILGDEG--RQRSVVIAAPADVSPLLRMqgAAYA-TRIAEDFRDR 260
Cdd:cd01132 83 tAIAIDTIINQKGKKVYCIYVaIGQKRSTVAQ-IVKTLEEHGamEYTIVVAATASDPAPLQYL--APYAgCAMGEYFRDN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 261 GQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGS--ITAFYTVLTEGDDQQDPIAD 338
Cdd:cd01132 160 GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGgsLTALPIIETQAGDVSAYIPT 239
|
250 260 270
....*....|....*....|....*....|...
gi 506351991 339 SARAILDGHVVLSRRLAEAGHYPAIDIEASISR 371
Cdd:cd01132 240 NVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
106-373 |
1.47e-31 |
|
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: 121.94 E-value: 1.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 106 QLPLGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQP--FNPLqrTPITQVLDVGVRAINALLTVGRGQRMGLFAGSGV 183
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREApeFVEL--STEQEILETGIKVVDLLAPYAKGGKIGLFGGAGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 184 GKSVLlgMM------ARYTQADVIVVGlIGERGREVKDFIE-----NILGDEGRQRSVVIAAPADVSPLLRMQGAAYATR 252
Cdd:cd01133 79 GKTVL--IMelinniAKAHGGYSVFAG-VGERTREGNDLYHemkesGVINLDGLSKVALVYGQMNEPPGARARVALTGLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 253 IAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERagNGISGGGSITAFYTVLTEGDD 331
Cdd:cd01133 156 MAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQER--ITSTKKGSITSVQAVYVPADD 233
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 506351991 332 QQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAM 373
Cdd:cd01133 234 LTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
82-401 |
2.21e-29 |
|
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: 119.42 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 82 LEEVEGIVPGARVwapaaaLNSGKQL--PLGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLDVG 159
Cdd:COG0055 60 MDSTDGLVRGMEV------IDTGAPIsvPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 160 VRAINALLTVGRGQRMGLFAGSGVGKSVLLgM-----MARYTQADVIVVGlIGERGREVKDFIENIlgdegrQRSVVIAA 234
Cdd:COG0055 134 IKVIDLLAPYAKGGKIGLFGGAGVGKTVLI-MelihnIAKEHGGVSVFAG-VGERTREGNDLYREM------KESGVLDK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 235 PADV------SPLLRMQGAAYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVE 307
Cdd:COG0055 206 TALVfgqmnePPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 308 RagNGISGGGSITAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLI-DEAHYARVR 386
Cdd:COG0055 286 R--ITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIvGEEHYRVAR 363
|
330
....*....|....*
gi 506351991 387 SFKQLLssyQRNRDL 401
Cdd:COG0055 364 EVQRIL---QRYKEL 375
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
86-434 |
7.92e-29 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 118.22 E-value: 7.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 86 EGIVPGARVWAPAAALNsgkqLPLGPALLGRVLDGSARPLDGLPPPDESDHGGL--SSQPFNPLQRTPitQVLDVGVRAI 163
Cdd:CHL00060 79 DGLMRGMEVIDTGAPLS----VPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIhrSAPAFIQLDTKL--SIFETGIKVV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 164 NALLTVGRGQRMGLFAGSGVGKSVLLgM-----MARyTQADVIVVGLIGERGREVKDfieniLGDEGRQRSVVIAAPADV 238
Cdd:CHL00060 153 DLLAPYRRGGKIGLFGGAGVGKTVLI-MelinnIAK-AHGGVSVFGGVGERTREGND-----LYMEMKESGVINEQNIAE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 239 S------------PLLRMQGAAYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPAL 305
Cdd:CHL00060 226 SkvalvygqmnepPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 306 VERagNGISGGGSITAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLI-DEAHYAR 384
Cdd:CHL00060 306 QER--ITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIvGEEHYET 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 506351991 385 VRSFKQLLSSYQRNRDLISVgayaRGSDPLLDQ---AIALYPQLEAFLQQGIF 434
Cdd:CHL00060 384 AQRVKQTLQRYKELQDIIAI----LGLDELSEEdrlTVARARKIERFLSQPFF 432
|
|
| ATP-synt_flagellum-secretory_path_III_C |
cd18114 |
Flagellum-specific ATP synthase, C-terminal domain; The C-terminal domain of the ... |
381-451 |
9.73e-29 |
|
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: 107.69 E-value: 9.73e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506351991 381 HYARVRSFKQLLSSYQRNRDLISVGAYARGSDPLLDQAIALYPQLEAFLQQGIFERSDYQQSCTALQTLFS 451
Cdd:cd18114 1 HYLAARKFRELMSTYQENEDLIRIGAYKKGSDPEVDEAIRLKPQIEAFLKQGLNEKAPLEESLQQLEEIFG 71
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
377-446 |
8.20e-28 |
|
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: 105.21 E-value: 8.20e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 377 IDEAHYARVRSFKQLLSSYQRNRDLISVGAYARGSDPLLDQAIALYPQLEAFLQQGIFERSDYQQSCTAL 446
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIGAYQAGSDPEIDEAIAKRPAINAFLRQGVDEPVSFEETLAQL 70
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
109-364 |
6.71e-26 |
|
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: 106.50 E-value: 6.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 109 LGPALLGRVLDGSARPLDGLPppDESDH---GGLSSQ------PFNPLQRTPITQVLDVGVRAINALLTVGRGqrmGLFA 179
Cdd:cd01134 6 LGPGLLGSIFDGIQRPLEVIA--ETGSIfipRGVNVQrwpvrqPRPVKEKLPPNVPLLTGQRVLDTLFPVAKG---GTAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 180 ---GSGVGKSVLLGMMARYTQADVIVVGLIGERGREV----KDFIENILGDEGR---QRSVVIAAPADvspllrMQGAA- 248
Cdd:cd01134 81 ipgPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMaevlEEFPELKDPITGEslmERTVLIANTSN------MPVAAr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 249 ----Y-ATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERA-----GNGISGGGS 318
Cdd:cd01134 155 easiYtGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrcLGSPGREGS 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 506351991 319 ITAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAID 364
Cdd:cd01134 235 VTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSIN 280
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
106-442 |
3.44e-25 |
|
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: 107.50 E-value: 3.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 106 QLPLGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLDVGVRAINALLTVGRGQRMGLFAGSGVGK 185
Cdd:TIGR01040 75 RTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 186 SVLLGMMAR------YTQADV---------IVVGLIG---ERGREVK-DFIENilgdEGRQRSVVIAAPADVSPLLRMQG 246
Cdd:TIGR01040 155 NEIAAQICRqaglvkLPTKDVhdghednfaIVFAAMGvnmETARFFKqDFEEN----GSMERVCLFLNLANDPTIERIIT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 247 AAYATRIAEDFR-DRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTV 325
Cdd:TIGR01040 231 PRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPIL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 326 LTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSF--KQLLSSYQRNRDLIS 403
Cdd:TIGR01040 311 TMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDvsNQLYACYAIGKDVQA 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 506351991 404 ----VGAYARGSDPLLdqAIALYPQLE-AFLQQGIFERSDYQQS 442
Cdd:TIGR01040 391 mkavVGEEALSSEDLL--YLEFLDKFEkNFIAQGPYENRTIFES 432
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
88-393 |
3.89e-25 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 107.36 E-value: 3.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 88 IVPGARVWApaaalnSGK--QLPLGPALLGRVLDGSARPLDGLPPPDESDHGGLSSQPFNPLQRTPITQVLDVGVRAINA 165
Cdd:CHL00059 61 IQEGSSVKA------TGKiaQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 166 LLTVGRGQRMGLFAGSGVGK-SVLLGMMARYTQADVIVVGL-IGERGREVKDfIENILGDEGR-QRSVVIAAPADVSPLL 242
Cdd:CHL00059 135 MIPIGRGQRELIIGDRQTGKtAVATDTILNQKGQNVICVYVaIGQKASSVAQ-VVTTLQERGAmEYTIVVAETADSPATL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 243 R----MQGAAyatrIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISG--G 316
Cdd:CHL00059 214 QylapYTGAA----LAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQlgE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 317 GSITAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISR--------AMTSL-----IDEAHYA 383
Cdd:CHL00059 290 GSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRvgsaaqikAMKQVagklkLELAQFA 369
|
330
....*....|
gi 506351991 384 RVRSFKQLLS 393
Cdd:CHL00059 370 ELEAFAQFAS 379
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
26-371 |
1.06e-23 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 102.80 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 26 RRYGKLTRATG--LVLEATGLQLpiGATCRVERHDGhqvlDVEAEVVGFNGRQLFLMPLEEVEGIVPGARVwapaAALNS 103
Cdd:PRK02118 3 KIYTKITDITGnvITVEAEGVGY--GELATVERKDG----SSLAQVIRLDGDKVTLQVFGGTRGISTGDEV----VFLGR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 104 GKQLPLGPALLGRVLDGSARPLDGLPPP--DESDHGGLSsqpFNPLQRTPITQVLDVGVRAINALLTVGRGQRMGLFAGS 181
Cdd:PRK02118 73 PMQVTYSESLLGRRFNGSGKPIDGGPELegEPIEIGGPS---VNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 182 GVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGDEGRQRSVVIAAPADVSPLLRMQGAAYATRIAEDFR-DR 260
Cdd:PRK02118 150 GEPYNALLARIALQAEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 261 GQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSitafyTVLT----EGDDQQDPI 336
Cdd:PRK02118 230 KKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEDGGSI-----TIIAvttmPGDDVTHPV 304
|
330 340 350
....*....|....*....|....*....|....*
gi 506351991 337 ADSARAILDGHVVLsrrlaeagHYPAIDIEASISR 371
Cdd:PRK02118 305 PDNTGYITEGQFYL--------RRGRIDPFGSLSR 331
|
|
| ATP-synt_flagellum-secretory_path_III_N |
cd18117 |
Flagellum-specific ATP synthase, N-terminal domain; The N-terminal domain of the ... |
27-94 |
1.24e-22 |
|
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: 91.05 E-value: 1.24e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506351991 27 RYGKLTRATGLVLEATGLQLPIGATCRVERHDGHQvldVEAEVVGFNGRQLFLMPLEEVEGIVPGARV 94
Cdd:cd18117 1 VYGRVVRVVGLLLEAVGPQAPIGELCLIETADGLS---ILAEVVGFSGEKVLLMPLGELSGLSPGARV 65
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
82-424 |
4.24e-19 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 89.71 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 82 LEEVEGIVPGARVWAPAAALnsgkQLPLGPALLGRVLD--GSARPLDGLPPP-----DESDHGGLSSQPFNPLQRTPITQ 154
Cdd:PTZ00185 96 MDNITEVQSGQKVMATGKLL----YIPVGAGVLGKVVNplGHEVPVGLLTRSralleSEQTLGKVDAGAPNIVSRSPVNY 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 155 VLDVGVRAINALLTVGRGQRMGLFAGSGVGKS----------VLLGMMARYTQADVIVVGLIGERGREVKDfIENILGDE 224
Cdd:PTZ00185 172 NLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTsiavstiinqVRINQQILSKNAVISIYVSIGQRCSNVAR-IHRLLRSY 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 225 GRQRSVVIAAPADVSPLLRMQGAAYA-TRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLP 303
Cdd:PTZ00185 251 GALRYTTVMAATAAEPAGLQYLAPYSgVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHS 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 304 ALVERAGNGI--SGGGSITAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAH 381
Cdd:PTZ00185 331 RLLERAAMLSpgKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAM 410
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 506351991 382 YARVRSFKQLLSSYqRNRDLISVGAYARGSDPLLDQA--IALYPQ 424
Cdd:PTZ00185 411 KAVAGKLKGILAEY-RKLAADSVGGSQVQTVPMIRGArfVALFNQ 454
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
29-364 |
4.91e-19 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 89.46 E-value: 4.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 29 GKLTRATGLVLEATGLQL-PIGATCRVerhdGHQVLdvEAEVVGFNGRQLFLMPLEEVEGIVPGARVwapaaaLNSGKQL 107
Cdd:PRK04192 5 GKIVRVSGPLVVAEGMGGaRMYEVVRV----GEEGL--IGEIIRIEGDKATIQVYEETSGIKPGEPV------EFTGEPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 108 P--LGPALLGRVLDGSARPLD-----------------GLP--------------------------------------P 130
Cdd:PRK04192 73 SveLGPGLLGSIFDGIQRPLDelaeksgdflergvyvpALDrekkweftptvkvgdkveagdilgtvqetpsiehkimvP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 131 PDES----------------------DHGGlSSQPFNPLQRTPI------------TQVLDVGVRAINALLTVGRGqrmG 176
Cdd:PRK04192 153 PGVSgtvkeivsegdytvddtiavleDEDG-EGVELTMMQKWPVrrprpykeklppVEPLITGQRVIDTFFPVAKG---G 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 177 LFA---GSGVGKSVLLGMMARYTQADVIVVGLIGERGREV----KDFIEniLGD--EGR---QRSVVIAAPADvspllrM 244
Cdd:PRK04192 229 TAAipgPFGSGKTVTQHQLAKWADADIVIYVGCGERGNEMtevlEEFPE--LIDpkTGRplmERTVLIANTSN------M 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 245 QGAA-----Y-ATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGS 318
Cdd:PRK04192 301 PVAAreasiYtGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGE 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 506351991 319 I---TAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAID 364
Cdd:PRK04192 381 EgsvTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAIN 429
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
108-309 |
1.29e-16 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 82.04 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 108 PLGPALLGRVLDGSARPLDGLpppdesdhGGLSSQPFNPL--------QRTPITQVLDVGVRAINALLTVGRGQRMgLFA 179
Cdd:PRK09281 98 PVGEALLGRVVNPLGQPIDGK--------GPIEATETRPVerkapgviDRKSVHEPLQTGIKAIDAMIPIGRGQRE-LII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 180 GS-GVGKSVLlgmmARYT-----QADVIVVGL-IGERGREVKDFIEnILGDEGR-QRSVVIAAPA-DVSPLLRMqgAAYA 250
Cdd:PRK09281 169 GDrQTGKTAI----AIDTiinqkGKDVICIYVaIGQKASTVAQVVR-KLEEHGAmEYTIVVAATAsDPAPLQYL--APYA 241
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 251 -TRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERA 309
Cdd:PRK09281 242 gCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERA 301
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
192-451 |
1.01e-15 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 80.07 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 192 MARYTQADVIVVGLIGERGREVKDFIENI-------LGDEGRQRSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHV 264
Cdd:PRK14698 676 LAKWSDAQVVIYIGCGERGNEMTDVLEEFpklkdpkTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDV 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 265 LLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGG-----SITAFYTVLTEGDDQQDPIADS 339
Cdd:PRK14698 756 ALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSdyrvgSVSVIGAVSPPGGDFSEPVVQN 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 340 ARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAH------YARVR-SFKQLLSSYQRNRDLISVgayaRGSD 412
Cdd:PRK14698 836 TLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHknvdpeWKAMRdKAMELLQKEAELQEIVRI----VGPD 911
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 506351991 413 --PLLDQAIALYPQL--EAFLQQGIFERSDY----QQSCTALQTLFS 451
Cdd:PRK14698 912 alPERERAILLVARMlrEDYLQQDAFDEVDTycppEKQVTMMRVLLN 958
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
140-371 |
3.45e-15 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 77.71 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 140 SSQPFNP----LQRTPITQVLDVGVRAINALLTVGRGQRMGLFAGSGVGK-SVLLGMMARYTQADV--IVVGlIGERGRE 212
Cdd:PRK07165 107 TSSIFNLahglMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKtHIALNTIINQKNTNVkcIYVA-IGQKREN 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 213 VKDFIENILGDEGRQRSVVIAAPADVS------PLLRMqgaAYATRIAEDfrdrgQHVLLIMDSLTRYAMAQREIALAIG 286
Cdd:PRK07165 186 LSRIYETLKEHDALKNTIIIDAPSTSPyeqylaPYVAM---AHAENISYN-----DDVLIVFDDLTKHANIYREIALLTN 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 287 EPPATKGYPPSVFAKLPALVERAGNGISGGGSiTAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIE 366
Cdd:PRK07165 258 KPVGKEAFPGDMFFAHSKLLERAGKFKNRKTI-TALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDID 336
|
....*
gi 506351991 367 ASISR 371
Cdd:PRK07165 337 LSVSR 341
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
381-450 |
5.04e-15 |
|
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: 69.40 E-value: 5.04e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 381 HYARVRSFKQLLSSYQRNRDLISVGAYARgSDPLLDQAIALYPQLEAFLQQGIFERSDYQQSCTALQTLF 450
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDA-LSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIK 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
28-94 |
2.00e-13 |
|
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: 65.03 E-value: 2.00e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506351991 28 YGKLTRATGLVLEATGL-QLPIGATCRVERHDGHQVLDVEAEVVGFNGRQLFLMPLEEVEGIVPGARV 94
Cdd:cd01426 1 KGRVIRVNGPLVEAELEgEVAIGEVCEIERGDGNNETVLKAEVIGFRGDRAILQLFESTRGLSRGALV 68
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
157-395 |
7.38e-13 |
|
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: 68.00 E-value: 7.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 157 DVGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMAR-----YTQADVIVVgLIGERGREVKDFIENILGDegrqrsvV 231
Cdd:cd01128 1 ELSTRVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANaiaknHPEVELIVL-LIDERPEEVTDMRRSVKGE-------V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 232 IAAPADVSPLLRMQGAAY----ATRIAEDfrdrGQHVLLIMDSLTRYAMAQREIAlaigePPATKGYPPSVFAK---LPA 304
Cdd:cd01128 73 VASTFDEPPERHVQVAEMviekAKRLVEH----GKDVVILLDSITRLARAYNTVV-----PSSGKTLSGGVDANalhKPK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 305 LVERAGNGISGGGSITAFYTVLTE-GDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYA 383
Cdd:cd01128 144 RFFGAARNIEEGGSLTIIATALVDtGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTRKEELLLTPEELQ 223
|
250
....*....|..
gi 506351991 384 RVRSFKQLLSSY 395
Cdd:cd01128 224 KIWLLRRILSPM 235
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
157-393 |
7.17e-12 |
|
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: 67.02 E-value: 7.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 157 DVGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMAR-----YTQADVIVVgLIGERGREVKDFIENILGDegrqrsvV 231
Cdd:TIGR00767 153 DLSTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQaitrnHPEVELIVL-LIDERPEEVTDMQRSVKGE-------V 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 232 IAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPpATKGYPPSVFAKlPALVERAGN 311
Cdd:TIGR00767 225 VASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKV-LSGGVDANALHR-PKRFFGAAR 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 312 GISGGGSITAFYTVLTE-GDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQ 390
Cdd:TIGR00767 303 NIEEGGSLTIIATALIDtGSRMDEVIFEEFKGTGNMELHLDRKLADRRIFPAIDIKKSGTRKEELLLTPEELQKIWVLRK 382
|
...
gi 506351991 391 LLS 393
Cdd:TIGR00767 383 IIS 385
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
157-394 |
1.43e-11 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 65.88 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 157 DVGVRAINALLTVGRGQRMGLFAGSGVGKSVLL-----GMMARYTQADVIVVgLIGERGREVKDFIENIlgdegrqRSVV 231
Cdd:PRK12608 118 DLSMRVVDLVAPIGKGQRGLIVAPPRAGKTVLLqqiaaAVAANHPEVHLMVL-LIDERPEEVTDMRRSV-------KGEV 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 232 IAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIG-------EPPATKGyPPSVFAklpa 304
Cdd:PRK12608 190 YASTFDRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAYNNEVESSGrtlsggvDARALQR-PKRLFG---- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 305 lverAGNGISGGGSITAFYTVLTE-GDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYA 383
Cdd:PRK12608 265 ----AARNIEEGGSLTIIATALVDtGSRMDEVIFEEFKGTGNMEIVLDRELADKRVFPAIDIAKSGTRREELLLDSKELE 340
|
250
....*....|.
gi 506351991 384 RVRSFKQLLSS 394
Cdd:PRK12608 341 KVRRLRRALAS 351
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
157-395 |
4.77e-07 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 51.68 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 157 DVGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMAR-----YTQADVIVVgLIGERGREVKDFienilgdegrQRSV- 230
Cdd:PRK09376 154 DLSTRIIDLIAPIGKGQRGLIVAPPKAGKTVLLQNIANsittnHPEVHLIVL-LIDERPEEVTDM----------QRSVk 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 231 --VIAAPADVSPLLRMQGAAY----ATRIAEdfrdRGQHVLLIMDSLTRYAmaqREIALAIgePPATKgyppsvfaklpa 304
Cdd:PRK09376 223 geVVASTFDEPAERHVQVAEMviekAKRLVE----HGKDVVILLDSITRLA---RAYNTVV--PSSGK------------ 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 305 lveragngisgggsitafytVLTEGddqQDPIA--------DSARAILDG------------------------------ 346
Cdd:PRK09376 282 --------------------VLSGG---VDANAlhrpkrffGAARNIEEGgsltiiatalidtgsrmdevifeefkgtgn 338
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 506351991 347 -HVVLSRRLAEAGHYPAIDIEASISRAMTSLIDEAHYARVRSFKQLLSSY 395
Cdd:PRK09376 339 mELHLDRKLAEKRIFPAIDINRSGTRKEELLLSPEELQKVWILRKILSPM 388
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
29-126 |
9.58e-03 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 38.46 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351991 29 GKLTRATGLVLEATGLQlpiGATCRVERHDGHqvLDVEAEVVGFNGRQLFLMPLEEVEGIVPGArvwaPAAALNSGKQLP 108
Cdd:PRK14698 5 GRIIRVTGPLVIADGMK---GAKMYEVVRVGE--LGLIGEIIRLEGDKAVIQVYEETAGLKPGE----PVEGTGSSLSVE 75
|
90
....*....|....*...
gi 506351991 109 LGPALLGRVLDGSARPLD 126
Cdd:PRK14698 76 LGPGLLTSIYDGIQRPLE 93
|
|
| |
