|
Name |
Accession |
Description |
Interval |
E-value |
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
1-455 |
0e+00 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 912.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 1 MTARLTRWLTTLDNFETRMAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCIIERQDGTETQEVESEVVGFNGHRLFLM 80
Cdd:PRK07960 1 MTTRLTRWLTTLDNFEAKMAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCVIERQNGSETHEVESEVVGFNGQRLFLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 81 PLEEVEGVLPGARVYARNSTGDGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALITPPFNPLQRTAIEHVLD 160
Cdd:PRK07960 81 PLEEVEGILPGARVYARNISGEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 161 TGVRPINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPAD 240
Cdd:PRK07960 161 TGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 241 VSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGG 320
Cdd:PRK07960 241 VSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 321 SITAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQR 400
Cdd:PRK07960 321 SITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLLSSFQR 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 364568425 401 NRDLVSVGAYAKGSDPMLDKAITLWPQLEAFLQQGIFERSDWDDSLQALELIFPT 455
Cdd:PRK07960 401 NRDLVSVGAYAKGSDPMLDKAIALWPQLEAFLQQGIFERADWEDSLQALERIFPT 455
|
|
| FliI_clade1 |
TIGR03496 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
29-449 |
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: 744.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 29 GRLTRATGLVLEATGLQLPLGATCIIERQDGtetQEVESEVVGFNGHRLFLMPLEEVEGVLPGARVYARNStgdglqsGK 108
Cdd:TIGR03496 1 GRVTRVVGLVLEAVGLRAPVGSRCEIESSDG---DPIEAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLGG-------PL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALITPPFNPLQRTAIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGK 188
Cdd:TIGR03496 71 RLPVGDSLLGRVIDGLGRPLDGKGPLDAGERVPLYAPPINPLKRAPIDEPLDVGVRAINGLLTVGRGQRMGIFAGSGVGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 189 SVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVL 268
Cdd:TIGR03496 151 STLLGMMARYTEADVVVVGLIGERGREVKEFIEDILGEEGLARSVVVAATADESPLMRLRAAFYATAIAEYFRDQGKDVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 269 LIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARAILD 348
Cdd:TIGR03496 231 LLMDSLTRFAMAQREIALAIGEPPATKGYPPSVFAKLPQLVERAGNGEEGKGSITAFYTVLVEGDDQQDPIADAARAILD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 349 GHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAITLWPQL 428
Cdd:TIGR03496 311 GHIVLSRELAEQGHYPAIDILASISRVMPDVVSPEHRQAARRFKQLLSRYQENRDLISIGAYQAGSDPELDQAIALYPRI 390
|
410 420
....*....|....*....|.
gi 364568425 429 EAFLQQGIFERSDWDDSLQAL 449
Cdd:TIGR03496 391 EAFLQQGMRERASFEESLEAL 411
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
9-453 |
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: 732.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 9 LTTLDNFETRMAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCIIERQDGtetQEVESEVVGFNGHRLFLMPLEEVEGV 88
Cdd:COG1157 1 LDRLARLLARLEELPPVRVSGRVTRVVGLLIEAVGPDASIGELCEIETADG---RPVLAEVVGFRGDRVLLMPLGDLEGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 89 LPGARVYArnstgdgLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALITPPFNPLQRTAIEHVLDTGVRPINA 168
Cdd:COG1157 78 SPGARVVP-------TGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 169 LLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVSPLLRMQ 248
Cdd:COG1157 151 LLTVGRGQRIGIFAGSGVGKSTLLGMIARNTEADVNVIALIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 249 GAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTV 328
Cdd:COG1157 231 AAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERA--GNGGKGSITAFYTV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 329 LTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQRNRDLVSVG 408
Cdd:COG1157 309 LVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENEDLIRIG 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 364568425 409 AYAKGSDPMLDKAITLWPQLEAFLQQGIFERSDWDDSLQALELIF 453
Cdd:COG1157 389 AYQPGSDPELDEAIALIPAIEAFLRQGMDERVSFEESLAQLAELL 433
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
5-454 |
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: 680.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 5 LTRWLTTLDNFETRMAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCIIERQdGTETQeVESEVVGFNGHRLFLMPLEE 84
Cdd:TIGR01026 1 MERNLTTFYNRLCQEMDLRLVKRVGRVTKVKGLLIEAVGPQASVGDLCLIERR-GSEGR-LVAEVVGFNGEFVFLMPYEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 85 VEGVLPGARVYARNstgdGLQSGkqlPLGPALLGRVLDGSGKPLDGLP-APDTTETGALITPPFNPLQRTAIEHVLDTGV 163
Cdd:TIGR01026 79 VEGVRPGSKVLATG----EGLSI---KVGDGLLGRVLDGLGKPIDGKGkFLDNVETEGLITAPINPLKRAPIREILSTGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 164 RPINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVSP 243
Cdd:TIGR01026 152 RSIDGLLTVGKGQRIGIFAGSGVGKSTLLGMIARNTEADVNVIALIGERGREVREFIEHDLGEEGLKRSVVVVATSDQSP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 244 LLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSIT 323
Cdd:TIGR01026 232 LLRLKGAYVATAIAEYFRDQGKDVLLLMDSVTRFAMAQREIGLAAGEPPATKGYTPSVFSTLPRLLERA--GASGKGSIT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 324 AFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQRNRD 403
Cdd:TIGR01026 310 AFYTVLVEGDDMNEPIADSVRGILDGHIVLSRALAQRGHYPAIDVLASISRLMTAIVSEEHRRAARKFRELLSKYKDNED 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 364568425 404 LVSVGAYAKGSDPMLDKAITLWPQLEAFLQQGIFERSDWDDSLQALELIFP 454
Cdd:TIGR01026 390 LIRIGAYQRGSDRELDFAIAKYPKLERFLKQGINEKVNFEESLQQLEEIFR 440
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
3-452 |
0e+00 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 651.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 3 ARLTRWLTTLDNFETRMAQLPAVRRyGRLTRATGLVLEATGLQLPLGATCIIERQDGtetqEVESEVVGFNGHRLFLMPL 82
Cdd:PRK08972 2 NRQHQLLNRLKQYKVKVPPFRAVAS-GKLVRVVGLTLEATGCRAPVGSLCSIETMAG----ELEAEVVGFDGDLLYLMPI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 83 EEVEGVLPGARVYARNStgdglQSGkqLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALITPPFNPLQRTAIEHVLDTG 162
Cdd:PRK08972 77 EELRGVLPGARVTPLGE-----QSG--LPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 163 VRPINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVS 242
Cdd:PRK08972 150 VRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTTADVIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 243 PLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSI 322
Cdd:PRK08972 230 PLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 323 TAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQRNR 402
Cdd:PRK08972 310 TAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLYQQNR 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 364568425 403 DLVSVGAYAKGSDPMLDKAITLWPQLEAFLQQGIFERSDWDDSLQALELI 452
Cdd:PRK08972 390 DLISIGAYKQGSDPRIDNAIRLQPAMNAFLQQTMKEAVPYDMSVNMLKQL 439
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
29-456 |
0e+00 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 597.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 29 GRLTRATGLVLEATGLQLPLGATCIIERQDGTETQEVESEVVGFNGHRLFLMPLEEVEGVLPGARVYARNSTGdglqsgk 108
Cdd:PRK05688 29 GRLLRMVGLTLEAEGLRAAVGSRCLVINDDSYHPVQVEAEVMGFSGDKVFLMPVGSVAGIAPGARVVPLADTG------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 109 QLPLGPALLGRVLDGSGKPLDG---LPAPDTTEtgaLITPPFNPLQRTAIEHVLDTGVRPINALLTVGRGQRMGLFAGSG 185
Cdd:PRK05688 102 RLPMGMSMLGRVLDGAGRALDGkgpMKAEDWVP---MDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 186 VGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVSPLLRMQGAAYATRIAEDFRDRGQ 265
Cdd:PRK05688 179 VGKSVLLGMMTRFTEADIIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 266 HVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARA 345
Cdd:PRK05688 259 NVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITAFYTVLSEGDDQQDPIADSARG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 346 ILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAITLW 425
Cdd:PRK05688 339 VLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARF 418
|
410 420 430
....*....|....*....|....*....|.
gi 364568425 426 PQLEAFLQQGIFERSDWDDSLQALELIFPTA 456
Cdd:PRK05688 419 PHLVQFLRQGLRENVSLAQSREQLAAIFAPA 449
|
|
| FliI_clade2 |
TIGR03497 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
29-453 |
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: 536.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 29 GRLTRATGLVLEATGLQLPLGATCIIERQDGtetQEVESEVVGFNGHRLFLMPLEEVEGVLPGARVYArnsTGDGLQsgk 108
Cdd:TIGR03497 1 GKVTRVIGLTIESKGPKASIGELCSILTKGG---KPVLAEVVGFKEENVLLMPLGEVEGIGPGSLVIA---TGRPLA--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 109 qLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALITPPFNPLQRTAIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGK 188
Cdd:TIGR03497 72 -IKVGKGLLGRVLDGLGRPLDGEGPIIGEEPYPLDNPPPNPLKRPRIRDPLETGIKAIDGLLTIGKGQRVGIFAGSGVGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 189 SVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVL 268
Cdd:TIGR03497 151 STLLGMIARNAKADINVIALIGERGREVRDFIEKDLGEEGLKRSVVVVATSDQPALMRLKAAFTATAIAEYFRDQGKDVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 269 LIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQDPIADSARAILD 348
Cdd:TIGR03497 231 LMMDSVTRFAMAQREIGLAVGEPPTTRGYTPSVFSLLPKLLERS--GNSQKGSITGFYTVLVDGDDMNEPIADAVRGILD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 349 GHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAITLWPQL 428
Cdd:TIGR03497 309 GHIVLSRELAAKNHYPAIDVLASVSRVMNEIVSEEHKELAGKLRELLAVYKEAEDLINIGAYKRGSNPKIDEAIRYIEKI 388
|
410 420
....*....|....*....|....*
gi 364568425 429 EAFLQQGIFERSDWDDSLQALELIF 453
Cdd:TIGR03497 389 NSFLKQGIDEKFTFEETVQLLKELL 413
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
22-449 |
4.15e-172 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 490.00 E-value: 4.15e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 22 LPAVRRYGRLTRATGLVLEATGLQLPLGATCIIERQDGTeTQEVESEVVGFNGHRLFLMPLEEVEGVLPGARVYArnsTG 101
Cdd:PRK07721 13 LDPYKRYGKVSRVIGLMIESKGPESSIGDVCYIHTKGGG-DKAIKAEVVGFKDEHVLLMPYTEVAEIAPGCLVEA---TG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 102 DGLQsgkqLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALITPPFNPLQRTAIEHVLDTGVRPINALLTVGRGQRMGLF 181
Cdd:PRK07721 89 KPLE----VKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 182 AGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVSPLLRMQGAAYATRIAEDFR 261
Cdd:PRK07721 165 AGSGVGKSTLMGMIARNTSADLNVIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 262 DRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQDPIAD 341
Cdd:PRK07721 245 DQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERT--GTNASGSITAFYTVLVDGDDMNEPIAD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 342 SARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKA 421
Cdd:PRK07721 323 TVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLINIGAYKRGSSREIDEA 402
|
410 420
....*....|....*....|....*...
gi 364568425 422 ITLWPQLEAFLQQGIFERSDWDDSLQAL 449
Cdd:PRK07721 403 IQFYPQIISFLKQGTDEKATFEESIQAL 430
|
|
| FliI_clade3 |
TIGR03498 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
29-452 |
5.71e-171 |
|
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: 486.43 E-value: 5.71e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 29 GRLTRATGLVLEATGLQ--LPLGATCIIERQDGtetQEVESEVVGFNGHRLFLMPLEEVEGVLPGARVYARNStgdglqs 106
Cdd:TIGR03498 1 GRVTAVTGLLIEVRGLSraVRLGDRCAIRARDG---RPVLAEVVGFNGDRVLLMPFEPLEGVGLGCAVFAREG------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 107 GKQLPLGPALLGRVLDGSGKPLDGLPA-PDTTETGALITPPFNPLQRTAIEHVLDTGVRPINALLTVGRGQRMGLFAGSG 185
Cdd:TIGR03498 71 PLAVRPHPSWLGRVINALGEPIDGKGPlPQGERRYPLRASPPPAMSRARVGEPLDTGVRVIDTFLPLCRGQRLGIFAGSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 186 VGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVSPLLRMQGAAYATRIAEDFRDRGQ 265
Cdd:TIGR03498 151 VGKSTLLSMLARNTDADVVVIALVGERGREVREFLEDDLGEEGLKRSVVVVATSDESPLMRRQAAYTATAIAEYFRDQGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 266 HVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARA 345
Cdd:TIGR03498 231 DVLLLMDSVTRFAMAQREIGLAAGEPPVARGYTPSVFSELPRLLERAGPGAEGKGSITGIFTVLVDGDDHNEPVADAVRG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 346 ILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAITLW 425
Cdd:TIGR03498 311 ILDGHIVLDRAIAERGRYPAINVLASVSRLAPRVWSPEERKLVRRLRALLARYEETEDLIRLGAYRKGSDPELDEAIRLV 390
|
410 420
....*....|....*....|....*..
gi 364568425 426 PQLEAFLQQGIFERSDWDDSLQALELI 452
Cdd:TIGR03498 391 PKIYEFLTQGPDEPTSLQDPFADLAAI 417
|
|
| III_secr_ATP |
TIGR02546 |
type III secretion apparatus H+-transporting two-sector ATPase; [Protein fate, Protein and ... |
23-453 |
2.03e-169 |
|
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: 482.59 E-value: 2.03e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 23 PAVRRYGRLTRATGLVLEATGLQLPLGATCIIERQDGTEtqeVESEVVGFNGHRLFLMPLEEVEGVLPGARVYArnsTGD 102
Cdd:TIGR02546 1 QPVRVRGRVTEVSGTLLKAVLPGARVGELCLIRRRDPSQ---LLAEVVGFTGDEALLSPLGELHGISPGSEVIP---TGR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 103 GLQsgkqLPLGPALLGRVLDGSGKPLDG--LPAPDTTETGALITPPFNPLQRTAIEHVLDTGVRPINALLTVGRGQRMGL 180
Cdd:TIGR02546 75 PLS----IRVGEALLGRVLDGFGRPLDGkgELPAGEIETRPLDADPPPPMSRQPIDQPLPTGVRAIDGLLTCGEGQRIGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 181 FAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVSPLLRMQGAAYATRIAEDF 260
Cdd:TIGR02546 151 FAGAGVGKSTLLGMIARGASADVNVIALIGERGREVREFIEHHLGEEGRKRSVLVVSTSDRPSLERLKAAYTATAIAEYF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 261 RDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQDPIA 340
Cdd:TIGR02546 231 RDQGKRVLLMMDSLTRFARALREIGLAAGEPPARGGYPPSVFSSLPRLLERA--GNGEKGSITALYTVLVEGDDMNDPIA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 341 DSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQRNRDLVSVGAYAKGSDPMLDK 420
Cdd:TIGR02546 309 DEVRSILDGHIVLSRALAERNHYPAIDVLASLSRVMSQVVSTEHRRAAGKLRRLLATYKEVELLIRLGEYQPGSDPETDD 388
|
410 420 430
....*....|....*....|....*....|...
gi 364568425 421 AITLWPQLEAFLQQGIFERSDWDDSLQALELIF 453
Cdd:TIGR02546 389 AIDKIDAIRAFLRQSTDEYSPYEETLEQLHALV 421
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
12-455 |
5.67e-160 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 459.36 E-value: 5.67e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 12 LDNFETRMAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCIIERQDGTEtqeVESEVVGFNGHRLFLMPLEEVEGVLPG 91
Cdd:PRK07196 2 LDHALKSIENIHLARVAGRLVRVTGLLLESVGCRLAIGQRCRIESVDETF---IEAQVVGFDRDITYLMPFKHPGGVLGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 92 ARVYARNSTGdglqsgkQLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALITPPFNPLQRTAIEHVLDTGVRPINALLT 171
Cdd:PRK07196 79 ARVFPSEQDG-------ELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 172 VGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVSPLLRMQGAA 251
Cdd:PRK07196 152 IGKGQRVGLMAGSGVGKSVLLGMITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 252 YATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgNGISGGGSITAFYTVLTE 331
Cdd:PRK07196 232 LCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESA-GNSSGNGTMTAIYTVLAE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 332 GDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQRNRDLVSVGAYA 411
Cdd:PRK07196 311 GDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYV 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 364568425 412 KGSDPMLDKAITLWPQLEAFLQQGIFERSDWDDSLQALELIFPT 455
Cdd:PRK07196 391 AGADPMADQAVHYYPAITQFLRQEVGHPALFSASVEQLTGMFPS 434
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
11-453 |
1.23e-159 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 458.67 E-value: 1.23e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 11 TLDNFETRMAQLPAVRRYGRLTRATGLVLEATGLQ--LPLGATCIIERQDGTEtqeVESEVVGFNGHRLFLMPLEEVEGV 88
Cdd:PRK08927 1 MMAALAAAIGDIDTLVIYGRVVAVRGLLVEVAGPIhaLSVGARIVVETRGGRP---VPCEVVGFRGDRALLMPFGPLEGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 89 LPGARVYARNSTGdglqsgkQLPLGPALLGRVLDGSGKPLDGL-PAPDTTETGALITPPFNPLQRTAIEHVLDTGVRPIN 167
Cdd:PRK08927 78 RRGCRAVIANAAA-------AVRPSRAWLGRVVNALGEPIDGKgPLPQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 168 ALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVSPLLRM 247
Cdd:PRK08927 151 TFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADADVSVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 248 QgAAYAT-RIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFY 326
Cdd:PRK08927 231 Q-AAYLTlAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGEGTITGLF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 327 TVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQRNRDLVS 406
Cdd:PRK08927 310 TVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIR 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 364568425 407 VGAYAKGSDPMLDKAITLWPQLEAFLQQGIFERSDWDDSLQALELIF 453
Cdd:PRK08927 390 LGAYRAGSDPEVDEAIRLNPALEAFLRQGKDEATSLAEGYARLAQIL 436
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
109-374 |
2.91e-155 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 440.46 E-value: 2.91e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALITPPFNPLQRTAIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGK 188
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 189 SVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVL 268
Cdd:cd01136 81 STLLGMIARNTDADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 269 LIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQDPIADSARAILD 348
Cdd:cd01136 161 LLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERA--GNGEKGSITAFYTVLVEGDDFNDPIADEVRSILD 238
|
250 260
....*....|....*....|....*.
gi 364568425 349 GHVVLSRRLAEAGHYPAIDIEASISR 374
Cdd:cd01136 239 GHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
12-452 |
1.56e-151 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 437.58 E-value: 1.56e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 12 LDNFETRMAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCIIERQDgtETQEVESEVVGFNGHRLFLMPLEEVEGVLPG 91
Cdd:PRK08472 3 LESLKNKLQKFNLSPRFGSITKISPTIIEADGLNPSVGDIVKIESSD--NGKECLGMVVVIEKEQFGISPFSFIEGFKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 92 ARVYArnstgdgLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALITPPFNPLQRTAIEHVLDTGVRPINALLT 171
Cdd:PRK08472 81 DKVFI-------SKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 172 VGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADgRARSVVVAAPADVSPLLRMQGAA 251
Cdd:PRK08472 154 CGKGQKLGIFAGSGVGKSTLMGMIVKGCLAPIKVVALIGERGREIPEFIEKNLGGD-LENTVIVVATSDDSPLMRKYGAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 252 YATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSiTAFYTVLTE 331
Cdd:PRK08472 233 CAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGKGSI-TAFFTVLVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 332 GDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQRNRDLVSVGAYA 411
Cdd:PRK08472 312 GDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAYQ 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 364568425 412 KGSDPMLDKAITLWPQLEAFLQQGIFERSDWDDSLQALELI 452
Cdd:PRK08472 392 KGNDKELDEAISKKEFMEQFLKQNPNELFPFEQTFEQLEEI 432
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
16-452 |
3.26e-143 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 416.91 E-value: 3.26e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 16 ETRMAQLPA----VRRYGRLTRATGLVLEATGLQLPLGATCIIErqdgteTQEVESEVVGFNGHRLFLMPLEEVEGVLPG 91
Cdd:PRK06820 14 QQQLTRPSAppegLRYRGPIVEIGPTLLRASLPGVAQGELCRIE------PQGMLAEVVSIEQEMALLSPFASSDGLRCG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 92 ARVyarnstgDGLQSGKQLPLGPALLGRVLDGSGKPLDGLPaPDTTETGALITPPFNPLQRTAIEHVLDTGVRPINALLT 171
Cdd:PRK06820 88 QWV-------TPLGHMHQVQVGADLAGRILDGLGAPIDGGP-PLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 172 VGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVSPLLRMQGAA 251
Cdd:PRK06820 160 CGEGQRIGIFAAAGVGKSTLLGMLCADSAADVMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 252 YATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTE 331
Cdd:PRK06820 240 TATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERT--GNSDRGSITAFYTVLVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 332 GDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQRNRDLVSVGAYA 411
Cdd:PRK06820 318 GDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGEYQ 397
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 364568425 412 KGSDPMLDKAITLWPQLEAFLQQGIFERSDWDDSLQALELI 452
Cdd:PRK06820 398 AGEDLQADEALQRYPAICAFLQQDHSETAHLETTLEHLAQV 438
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
19-450 |
5.77e-141 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 411.07 E-value: 5.77e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 19 MAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCIIERQDgtETQEVESEVVGFNGHRLFLMPLEEVEGVLPGARVyarN 98
Cdd:PRK06936 15 IVGSRLIQIRGRVTQVTGTILKAVVPGVRIGELCYLRNPD--NSLSLQAEVIGFAQHQALLTPLGEMYGISSNTEV---S 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 99 STGDGLQsgkqLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALITPPFNPLQRTAIEHVLDTGVRPINALLTVGRGQRM 178
Cdd:PRK06936 90 PTGTMHQ----VGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 179 GLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVSPLLRMQGAAYATRIAE 258
Cdd:PRK06936 166 GIFAAAGGGKSTLLASLIRSAEVDVTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 259 DFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQDP 338
Cdd:PRK06936 246 YFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERA--GQSDKGSITALYTVLVEGDDMTEP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 339 IADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQRNRDLVSVGAYAKGSDPML 418
Cdd:PRK06936 324 VADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIGEYQKGQDKEA 403
|
410 420 430
....*....|....*....|....*....|..
gi 364568425 419 DKAITLWPQLEAFLQQGIFERSDWDDSLQALE 450
Cdd:PRK06936 404 DQAIERIGAIRGFLRQGTHELSHFNETLNLLE 435
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
2-449 |
8.74e-141 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 410.70 E-value: 8.74e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 2 TARLTRWLttldnfETRMAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCIIERQDGTETQEveSEVVGFNGHRLFLMP 81
Cdd:PRK09099 5 LSRLADAL------ERELAALPAVRRTGKVVEVIGTLLRVSGLDVTLGELCELRQRDGTLLQR--AEVVGFSRDVALLSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 82 LEEVEGVLPGARVYarnstgdGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALITPPFNPLQRTAIEHVLDT 161
Cdd:PRK09099 77 FGELGGLSRGTRVI-------GLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 162 GVRPINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADV 241
Cdd:PRK09099 150 GVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQCDVNVIALIGERGREVREFIELILGEDGMARSVVVCATSDR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 242 SPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGS 321
Cdd:PRK09099 230 SSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERA--GMGETGS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 322 ITAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQRN 401
Cdd:PRK09099 308 ITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREV 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 364568425 402 RDLVSVGAYAKGSDPMLDKAITLWPQLEAFLQQGIFERSDWDDSLQAL 449
Cdd:PRK09099 388 ETLLQVGEYRAGSDPVADEAIAKIDAIRDFLSQRTDEYSDPDATLAAL 435
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
109-375 |
5.06e-126 |
|
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: 366.40 E-value: 5.06e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALITPPFNPLQRTAIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGK 188
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 189 SVLLGMMARYTQ---ADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVSPLLRMQGAAYATRIAEDFRDRGQ 265
Cdd:cd19476 81 TVLAMQLARNQAkahAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 266 HVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARA 345
Cdd:cd19476 161 HVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTPGDDLTDPIPDNTFA 240
|
250 260 270
....*....|....*....|....*....|
gi 364568425 346 ILDGHVVLSRRLAEAGHYPAIDIEASISRA 375
Cdd:cd19476 241 ILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
26-452 |
9.82e-118 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 351.56 E-value: 9.82e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 26 RRYGRLTRATGLVLEATGLQLPLGATCIIERQDGTetqeveSEVVGFNGHRLFLMPLEEVEGVLPGARVYArnstgdgLQ 105
Cdd:PRK07594 20 CRWGRIQDVSATLLNAWLPGVFMGELCCIKPGEEL------AEVVGINGSKALLSPFTSTIGLHCGQQVMA-------LR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 106 SGKQLPLGPALLGRVLDGSGKPLDGLPAPDTTETgALITPPFNPLQRTAIEHVLDTGVRPINALLTVGRGQRMGLFAGSG 185
Cdd:PRK07594 87 RRHQVPVGEALLGRVIDGFGRPLDGRELPDVCWK-DYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 186 VGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVSPLLRMQGAAYATRIAEDFRDRGQ 265
Cdd:PRK07594 166 VGKSTLLAMLCNAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 266 HVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQDPIADSARA 345
Cdd:PRK07594 246 RVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERT--GMGEKGSITAFYTVLVEGDDMNEPLADEVRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 346 ILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAITLW 425
Cdd:PRK07594 324 LLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEYQRGVDTDTDKAIDTY 403
|
410 420
....*....|....*....|....*..
gi 364568425 426 PQLEAFLQQGIFERSDWDDSLQALELI 452
Cdd:PRK07594 404 PDICTFLRQSKDEVCGPELLIEKLHQI 430
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
26-450 |
2.73e-115 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 345.06 E-value: 2.73e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 26 RRYGRLTRATGLVLEATGLQLPLGATCIIERQDGTETQEVESEVVGFNGHRLFLMPLEEVEGVlpgARVYARNSTGDGLQ 105
Cdd:PRK08149 5 QRLAHPLRIQGPIIEAELPDVAIGEICEIRAGWHSNEVIARAQVVGFQRERTILSLIGNAQGL---SRQVVLKPTGKPLS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 106 sgkqLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALI----TPPFNPLQRTAIEHVLDTGVRPINALLTVGRGQRMGLF 181
Cdd:PRK08149 82 ----VWVGEALLGAVLDPTGKIVERFDAPPTVGPISEErvidVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 182 AGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVSPLLRMQGAAYATRIAEDFR 261
Cdd:PRK08149 158 ASAGCGKTSLMNMLIEHSEADVFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 262 DRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQDPIAD 341
Cdd:PRK08149 238 DQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERP--GATLAGSITAFYTVLLESEEEPDPIGD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 342 SARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKA 421
Cdd:PRK08149 316 EIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGEYRRGENADNDRA 395
|
410 420
....*....|....*....|....*....
gi 364568425 422 ITLWPQLEAFLQQGIFERSDWDDSLQALE 450
Cdd:PRK08149 396 MDKRPALEAFLKQDVAEKSSFSDTLERLN 424
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
162-373 |
1.08e-114 |
|
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: 335.48 E-value: 1.08e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 162 GVRPINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADV 241
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLGSGALKRTVVVVATSDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 242 SPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGS 321
Cdd:pfam00006 81 PPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKGKGGS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 364568425 322 ITAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASIS 373
Cdd:pfam00006 161 ITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
9-434 |
1.40e-111 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 336.20 E-value: 1.40e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 9 LTTLDNFETRMAQ-LPAVRRYGRLTRATGLVLEATGLQ--LPLGATCIIERQdgteTQEVESEVVGFNGHRLFLMPLEEV 85
Cdd:PRK06002 7 LARLAALVERYAApEPLVRIGGTVSEVTASHYRVRGLSrfVRLGDFVAIRAD----GGTHLGEVVRVDPDGVTVKPFEPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 86 EGVLPGARVYARNStgdglqsgKQLPLGPALLGRVLDGSGKPLDGL----PAPDTTETGALiTPPfnPLQRTAIEHVLDT 161
Cdd:PRK06002 83 IEIGLGDAVFRKGP--------LRIRPDPSWKGRVINALGEPIDGLgplaPGTRPMSIDAT-APP--AMTRARVETGLRT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 162 GVRPINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGaDGRARSVVVAAPADV 241
Cdd:PRK06002 152 GVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGREVREFLEDTLA-DNLKKAVAVVATSDE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 242 SPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGS 321
Cdd:PRK06002 231 SPMMRRLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEGGGS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 322 ITAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQRN 401
Cdd:PRK06002 311 ITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEET 390
|
410 420 430
....*....|....*....|....*....|...
gi 364568425 402 RDLVSVGAYAKGSDPMLDKAITLWPQLEAFLQQ 434
Cdd:PRK06002 391 RDLRLIGGYRAGSDPDLDQAVDLVPRIYEALRQ 423
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
41-452 |
1.06e-91 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 284.56 E-value: 1.06e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 41 ATGLQLPLGATCIIERQdgtetqEVESEVVGFNGHRLFLMPLEEVEGVLPGARVYArnstgdgLQSGKQLPLGPALLGRV 120
Cdd:PRK06793 35 AKGPKAKIGDVCFVGEH------NVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTL-------IAEDVVIPRGNHLLGKV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 121 LDGSGKPLDGLPAPDTTETGALITPPFNPLQRTAIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQ 200
Cdd:PRK06793 102 LSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 201 ADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMA 280
Cdd:PRK06793 182 ADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 281 QREIALAIGEPPaTKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEA 360
Cdd:PRK06793 262 RRSVDIAVKELP-IGGKTLLMESYMKKLLERS--GKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 361 GHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQRNRDLVSVGAYAKGSDpmlDKAITLWPQ----LEAFLQQGI 436
Cdd:PRK06793 339 SHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGTIQENAE---NAYIFECKNkvegINTFLKQGR 415
|
410
....*....|....*.
gi 364568425 437 FERSDWDDSLQALELI 452
Cdd:PRK06793 416 SDSFQFDDIVEAMHHI 431
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
9-452 |
4.25e-91 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 283.33 E-value: 4.25e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 9 LTTLDNFETRMAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCIIERqdgTETQEVESEVVGFNGHRLFLMPLEEVEGV 88
Cdd:PRK05922 1 MTHLQEEKLLIHQWQPYRECGLLSRVSGNLLEAQGLSACLGELCQISL---SKSPPILAEVIGFHNRTTLLMSLSPIHYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 89 LPGARVYArnstgdgLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALITPPFNPLQRTAIEHVLDTGVRPINA 168
Cdd:PRK05922 78 ALGAEVLP-------LRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 169 LLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPA-DVSPLLRM 247
Cdd:PRK05922 151 FLTLGKGQRIGVFSEPGSGKSSLLSTIAKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAhETAPTKVI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 248 QGAAyATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYT 327
Cdd:PRK05922 231 AGRA-AMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERA--GNNDKGSITALYA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 328 VLTEGdDQQDPIADSARAILDGHVVLSRRlAEAGHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSSFQRNRDLVSV 407
Cdd:PRK05922 308 ILHYP-NHPDIFTDYLKSLLDGHFFLTPQ-GKALASPPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 364568425 408 GAYAKGSDPMLDKAITLWPQLEAFLQQGIFERSDWDDSLQALELI 452
Cdd:PRK05922 386 GAYVPGQDAHLDRAVKLLPSIKQFLSQPLSSYCALHNTLKQLEAL 430
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
109-380 |
1.97e-38 |
|
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: 140.82 E-value: 1.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALITPPFNPLQRTAIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGK 188
Cdd:cd01135 3 KLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLPH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 189 SVLLGMMARytQADV--------IVVGLIGERGRE----VKDFIENilGADGraRSVVVAAPADVSPLLRMQGAAYATRI 256
Cdd:cd01135 83 NELAAQIAR--QAGVvgseenfaIVFAAMGVTMEEarffKDDFEET--GALE--RVVLFLNLANDPTIERIITPRMALTT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 257 AEDFR-DRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFyTVLT-EGDD 334
Cdd:cd01135 157 AEYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQI-PILTmPNDD 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 364568425 335 QQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLI 380
Cdd:cd01135 236 ITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGI 281
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
28-407 |
2.44e-38 |
|
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: 144.86 E-value: 2.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 28 YGRLTRATGLVLEA--TGLQLP--LGATCIIERQDGTETQEVESEVvgfNGHRLFLMPLEEVEGVLPGARVYARNSTgdg 103
Cdd:TIGR01039 2 KGKVVQVIGPVVDVefEQGELPriYNALKVQNRAESELTLEVAQHL---GDDTVRTIAMGSTDGLVRGLEVIDTGAP--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 104 lqsgKQLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALITPPFNPLQRTAIEHVLDTGVRPINALLTVGRGQRMGLFAG 183
Cdd:TIGR01039 76 ----ISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 184 SGVGKSVLLGMMAR---YTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVSPLLRMQGAAYATRIAEDF 260
Cdd:TIGR01039 152 AGVGKTVLIQELINniaKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 261 RD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERagNGISGGGSITAFYTVLTEGDDQQDPI 339
Cdd:TIGR01039 232 RDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQER--ITSTKTGSITSVQAVYVPADDLTDPA 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 364568425 340 ADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMT-SLITEEHYARVRHFKQLLSSFQRNRDLVSV 407
Cdd:TIGR01039 310 PATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVGEEHYDVARGVQQILQRYKELQDIIAI 378
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
68-374 |
2.21e-36 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 140.05 E-value: 2.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 68 EVVGF-NGHRLFLMPLEE--VEGVLPGArvYARNSTGDGLQ-SGKQL--PLGPALLGRVLDGSGKPLDGLPAPDTTETGA 141
Cdd:PRK13343 51 ELLRFeGGSRGFAFNLEEelVGAVLLDD--TADILAGTEVRrTGRVLevPVGDGLLGRVIDPLGRPLDGGGPLQATARRP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 142 L--ITPPFnpLQRTAIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGKSVLlGMMARYTQ--ADVIVVG-LIGERGREV 216
Cdd:PRK13343 129 LerPAPAI--IERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAI-AIDAIINQkdSDVICVYvAIGQKASAV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 217 KDFIENILGADGRARSVVVAAPADVSPllrmqGAAY-----ATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEP 291
Cdd:PRK13343 206 ARVIETLREHGALEYTTVVVAEASDPP-----GLQYlapfaGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRP 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 292 PATKGYPPSVFAKLPALVERAGNGISGGG--SITAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIE 369
Cdd:PRK13343 281 PGREAYPGDIFYLHSRLLERAAKLSPELGggSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVG 360
|
....*
gi 364568425 370 ASISR 374
Cdd:PRK13343 361 LSVSR 365
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
109-376 |
1.96e-35 |
|
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: 132.34 E-value: 1.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALIT--PPFNPLQRTAieHVLDTGVRPINALLTVGRGQRMGLFAGSGV 186
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHReaPEFVELSTEQ--EILETGIKVVDLLAPYAKGGKIGLFGGAGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 187 GKSVLlgMM------ARYTQADVIVVGlIGERGREVKDFIE-----NILGADGRARSVVVAAPADVSPLLRMQGAAYATR 255
Cdd:cd01133 79 GKTVL--IMelinniAKAHGGYSVFAG-VGERTREGNDLYHemkesGVINLDGLSKVALVYGQMNEPPGARARVALTGLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 256 IAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERagNGISGGGSITAFYTVLTEGDD 334
Cdd:cd01133 156 MAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQER--ITSTKKGSITSVQAVYVPADD 233
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 364568425 335 QQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAM 376
Cdd:cd01133 234 LTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
100-404 |
9.07e-35 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 134.95 E-value: 9.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 100 TGDGLQsgkqLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALITPPFNPLQRTAIEHVLDTGVRPINALLTVGRGQRMG 179
Cdd:PRK04196 72 TGEPLK----LPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 180 LFAGSGVGKSVLLGMMARytQADV--------IVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVSPLLRMQGAA 251
Cdd:PRK04196 148 IFSGSGLPHNELAAQIAR--QAKVlgeeenfaVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPR 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 252 YATRIAE--DFrDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFyTVL 329
Cdd:PRK04196 226 MALTAAEylAF-EKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQI-PIL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 330 T-EGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLI----TEEHYARVrhFKQLLSSFQRNRDL 404
Cdd:PRK04196 304 TmPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIgegkTREDHKDV--ANQLYAAYARGKDL 381
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
109-374 |
6.56e-34 |
|
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: 128.45 E-value: 6.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALITPPFNPLQRTAIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGK 188
Cdd:cd01132 3 EVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 189 -SVLLGMMARYTQADVIVVGL-IGERGREVKDFIENILGADGRARSVVVAAPA-DVSPLLRMqgAAYA-TRIAEDFRDRG 264
Cdd:cd01132 83 tAIAIDTIINQKGKKVYCIYVaIGQKRSTVAQIVKTLEEHGAMEYTIVVAATAsDPAPLQYL--APYAgCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 265 QHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGS--ITAFYTVLTEGDDQQDPIADS 342
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGgsLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|..
gi 364568425 343 ARAILDGHVVLSRRLAEAGHYPAIDIEASISR 374
Cdd:cd01132 241 VISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| ATP-synt_flagellum-secretory_path_III_C |
cd18114 |
Flagellum-specific ATP synthase, C-terminal domain; The C-terminal domain of the ... |
384-454 |
9.22e-32 |
|
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: 115.78 E-value: 9.22e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 364568425 384 HYARVRHFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAITLWPQLEAFLQQGIFERSDWDDSLQALELIFP 454
Cdd:cd18114 1 HYLAARKFRELMSTYQENEDLIRIGAYKKGSDPEVDEAIRLKPQIEAFLKQGLNEKAPLEESLQQLEEIFG 71
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
92-404 |
1.95e-31 |
|
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: 125.59 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 92 ARVYARNSTgDGLQSGK---------QLPLGPALLGRVLDGSGKPLDGLPAPDTTETGAlI---TPPFNPlQRTAIEhVL 159
Cdd:COG0055 55 VRCIAMDST-DGLVRGMevidtgapiSVPVGEATLGRIFNVLGEPIDGKGPIEAKERRP-IhrpAPPFEE-QSTKTE-IL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 160 DTGVRPINALLTVGRGQRMGLFAGSGVGKSVLLgM-----MARYTQADVIVVGlIGERGREVKDFIENILGADGRARSVV 234
Cdd:COG0055 131 ETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLI-MelihnIAKEHGGVSVFAG-VGERTREGNDLYREMKESGVLDKTAL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 235 VAAPADVSPLLRMQGAAYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERag 313
Cdd:COG0055 209 VFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQER-- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 314 NGISGGGSITAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLIT-EEHYARVRHFK 392
Cdd:COG0055 287 ITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVgEEHYRVAREVQ 366
|
330
....*....|..
gi 364568425 393 QLLssfQRNRDL 404
Cdd:COG0055 367 RIL---QRYKEL 375
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
84-407 |
4.28e-30 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 122.07 E-value: 4.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 84 EVEGVLPGARVYARN-STGDGLQSGKQ---------LPLGPALLGRVLDGSGKPLDGLPAPDTTETGAL--ITPPFNPLQ 151
Cdd:CHL00060 60 EVQQLLGNNRVRAVAmSATDGLMRGMEvidtgaplsVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIhrSAPAFIQLD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 152 RTAieHVLDTGVRPINALLTVGRGQRMGLFAGSGVGKSVLLgM-----MARyTQADVIVVGLIGERGREVKDFIEN---- 222
Cdd:CHL00060 140 TKL--SIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLI-MelinnIAK-AHGGVSVFGGVGERTREGNDLYMEmkes 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 223 -ILGADGRARSVV--VAAPADVSPLLRMQGAAYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYP 298
Cdd:CHL00060 216 gVINEQNIAESKValVYGQMNEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQ 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 299 PSVFAKLPALVERagNGISGGGSITAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTS 378
Cdd:CHL00060 296 PTLSTEMGSLQER--ITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQP 373
|
330 340 350
....*....|....*....|....*....|
gi 364568425 379 LIT-EEHYARVRHFKQLLSSFQRNRDLVSV 407
Cdd:CHL00060 374 RIVgEEHYETAQRVKQTLQRYKELQDIIAI 403
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
380-449 |
1.18e-27 |
|
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: 104.82 E-value: 1.18e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 380 ITEEHYARVRHFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAITLWPQLEAFLQQGIFERSDWDDSLQAL 449
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIGAYQAGSDPEIDEAIAKRPAINAFLRQGVDEPVSFEETLAQL 70
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
101-374 |
4.35e-26 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 110.44 E-value: 4.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 101 GDGLQ---------SGK--QLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALITPPFNPLQRTAIEHVLDTGVRPINAL 169
Cdd:CHL00059 56 GDGLMiqegssvkaTGKiaQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSM 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 170 LTVGRGQRMGLFAGSGVGK-SVLLGMMARYTQADVIVVGL-IGERGREVKDFIENILGADGRARSVVVAAPADVSPLLR- 246
Cdd:CHL00059 136 IPIGRGQRELIIGDRQTGKtAVATDTILNQKGQNVICVYVaIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQy 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 247 ---MQGAAyatrIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISG--GGS 321
Cdd:CHL00059 216 lapYTGAA----LAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQlgEGS 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 364568425 322 ITAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISR 374
Cdd:CHL00059 292 MTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSR 344
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
26-374 |
5.67e-25 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 106.66 E-value: 5.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 26 RRYGRLTRATG--LVLEATGLQLplGATCIIERQDGTETqeveSEVVGFNGHRLFLMPLEEVEGVlpgarvyarnSTGDG 103
Cdd:PRK02118 3 KIYTKITDITGnvITVEAEGVGY--GELATVERKDGSSL----AQVIRLDGDKVTLQVFGGTRGI----------STGDE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 104 ---LQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTTETgALITPPFNPLQRTAIEHVLDTGVRPINALLTVGRGQRMGL 180
Cdd:PRK02118 67 vvfLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGEPI-EIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 181 FAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGADGRARSVVVAAPADVSPLLRMQGAAYATRIAEDF 260
Cdd:PRK02118 146 FSVSGEPYNALLARIALQAEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 261 R-DRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSitafyTVLT----EGDDQ 335
Cdd:PRK02118 226 AlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEDGGSI-----TIIAvttmPGDDV 300
|
330 340 350
....*....|....*....|....*....|....*....
gi 364568425 336 QDPIADSARAILDGHVVLsrrlaeagHYPAIDIEASISR 374
Cdd:PRK02118 301 THPVPDNTGYITEGQFYL--------RRGRIDPFGSLSR 331
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
112-367 |
2.38e-24 |
|
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: 102.27 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 112 LGPALLGRVLDGSGKPLDGLpapdtTETGALITP------------PFNPLQRTAIEHVLDTGVRPINALLTVGRGqrmG 179
Cdd:cd01134 6 LGPGLLGSIFDGIQRPLEVI-----AETGSIFIPrgvnvqrwpvrqPRPVKEKLPPNVPLLTGQRVLDTLFPVAKG---G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 180 LFA---GSGVGKSVLLGMMARYTQADVIVVGLIGERGREV----KDFIENILGADGRA---RSVVVAAPADvspllrMQG 249
Cdd:cd01134 78 TAAipgPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMaevlEEFPELKDPITGESlmeRTVLIANTSN------MPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 250 AA-----Y-ATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERA-----GNGISG 318
Cdd:cd01134 152 AAreasiYtGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrcLGSPGR 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 364568425 319 GGSITAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAID 367
Cdd:cd01134 232 EGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSIN 280
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
100-454 |
5.08e-24 |
|
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: 104.03 E-value: 5.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 100 TGDGLQsgkqLPLGPALLGRVLDGSGKPLDGLPAPDTTETGALITPPFNPLQRTAIEHVLDTGVRPINALLTVGRGQRMG 179
Cdd:TIGR01040 70 TGDILR----TPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 180 LFAGSGVGKSVLLGMMAR------YTQADV---------IVVGLIG---ERGREVK-DFIENilGADGRArsVVVAAPAD 240
Cdd:TIGR01040 146 IFSAAGLPHNEIAAQICRqaglvkLPTKDVhdghednfaIVFAAMGvnmETARFFKqDFEEN--GSMERV--CLFLNLAN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 241 VSPLLRMQGAAYATRIAEDFR-DRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGG 319
Cdd:TIGR01040 222 DPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRN 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 320 GSITAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLI----TEEHYARVRHfkQLL 395
Cdd:TIGR01040 302 GSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIgegmTRKDHSDVSN--QLY 379
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 364568425 396 SSFQRNRDLVS----VGAYAKGSDPMLdkAITLWPQLE-AFLQQGIFERSDWDDSL-QALEL--IFP 454
Cdd:TIGR01040 380 ACYAIGKDVQAmkavVGEEALSSEDLL--YLEFLDKFEkNFIAQGPYENRTIFESLdIAWQLlrIFP 444
|
|
| ATP-synt_flagellum-secretory_path_III_N |
cd18117 |
Flagellum-specific ATP synthase, N-terminal domain; The N-terminal domain of the ... |
27-98 |
1.94e-23 |
|
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: 92.98 E-value: 1.94e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 364568425 27 RYGRLTRATGLVLEATGLQLPLGATCIIERQDGtetQEVESEVVGFNGHRLFLMPLEEVEGVLPGARVYARN 98
Cdd:cd18117 1 VYGRVVRVVGLLLEAVGPQAPIGELCLIETADG---LSILAEVVGFSGEKVLLMPLGELSGLSPGARVVPLG 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
384-454 |
2.97e-22 |
|
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: 89.81 E-value: 2.97e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 364568425 384 HYARVRHFKQLLSSFQRNRDLVSVGAYAKgSDPMLDKAITLWPQLEAFLQQGIFERSDWDDSLQALELIFP 454
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDA-LSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
109-312 |
1.46e-18 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 87.81 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTTETGAL--ITPPFnpLQRTAIEHVLDTGVRPINALLTVGRGQRMgLFAGS-G 185
Cdd:PRK09281 96 EVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVerKAPGV--IDRKSVHEPLQTGIKAIDAMIPIGRGQRE-LIIGDrQ 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 186 VGKSVLlgmmARYT-----QADVIVVGL-IGERGREVKDFIENILGADGRARSVVVAAPA-DVSPLLRMqgAAYA-TRIA 257
Cdd:PRK09281 173 TGKTAI----AIDTiinqkGKDVICIYVaIGQKASTVAQVVRKLEEHGAMEYTIVVAATAsDPAPLQYL--APYAgCAMG 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 364568425 258 EDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERA 312
Cdd:PRK09281 247 EYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERA 301
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
76-421 |
7.63e-18 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 85.86 E-value: 7.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 76 RLFLMPLEEVEGVLPGARVYArnsTGDGLQsgkqLPLGPALLGRVLDGSGKPLdglPAPDTTETGALITPPF-------- 147
Cdd:PTZ00185 90 RIGIILMDNITEVQSGQKVMA---TGKLLY----IPVGAGVLGKVVNPLGHEV---PVGLLTRSRALLESEQtlgkvdag 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 148 --NPLQRTAIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGKS----------VLLGMMARYTQADVIVVGLIGERGRE 215
Cdd:PTZ00185 160 apNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTsiavstiinqVRINQQILSKNAVISIYVSIGQRCSN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 216 VKDfIENILGADGRARSVVVAAPADVSPLLRMQGAAYA-TRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPAT 294
Cdd:PTZ00185 240 VAR-IHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSgVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 295 KGYPPSVFAKLPALVERAGNGI--SGGGSITAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASI 372
Cdd:PTZ00185 319 EAYPGDVFYLHSRLLERAAMLSpgKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSV 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 364568425 373 SRAMTSLITEEHYARVRHFKQLLSSFqRNRDLVSVGAYAKGSDPMLDKA 421
Cdd:PTZ00185 399 SRVGSSAQNVAMKAVAGKLKGILAEY-RKLAADSVGGSQVQTVPMIRGA 446
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
159-367 |
3.48e-17 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 84.06 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 159 LDTGVRPINALLTVGRGqrmGLFA---GSGVGKSVLLGMMARYTQADVIVVGLIGERGREV----KDFIENILGADGRA- 230
Cdd:PRK04192 211 LITGQRVIDTFFPVAKG---GTAAipgPFGSGKTVTQHQLAKWADADIVIYVGCGERGNEMtevlEEFPELIDPKTGRPl 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 231 --RSVVVAAPADvspllrMQGAA-----Y-ATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVF 302
Cdd:PRK04192 288 meRTVLIANTSN------MPVAAreasiYtGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLA 361
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 364568425 303 AKLPALVERAGNGISGGGSI---TAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAID 367
Cdd:PRK04192 362 SRLAEFYERAGRVKTLGGEEgsvTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAIN 429
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
159-374 |
8.47e-16 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 79.63 E-value: 8.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 159 LDTGVRPINALLTVGRGQRMGLFAGSGVGK-SVLLGMMARYTQADV--IVVGlIGERGREVKDFIENILGADGRARSVVV 235
Cdd:PRK07165 127 LYTGIIAIDLLIPIGKGQRELIIGDRQTGKtHIALNTIINQKNTNVkcIYVA-IGQKRENLSRIYETLKEHDALKNTIII 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 236 AAPADVS------PLLRMqgaAYATRIAEDfrdrgQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALV 309
Cdd:PRK07165 206 DAPSTSPyeqylaPYVAM---AHAENISYN-----DDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLL 277
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 364568425 310 ERAGNGISGGGSiTAFYTVLTEGDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISR 374
Cdd:PRK07165 278 ERAGKFKNRKTI-TALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSR 341
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
28-99 |
2.06e-15 |
|
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: 70.80 E-value: 2.06e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 364568425 28 YGRLTRATGLVLEATGL-QLPLGATCIIERQDGTETQEVESEVVGFNGHRLFLMPLEEVEGVLPGARVYARNS 99
Cdd:cd01426 1 KGRVIRVNGPLVEAELEgEVAIGEVCEIERGDGNNETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
195-441 |
3.39e-14 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 75.06 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 195 MARYTQADVIVVGLIGERGREVKDFIENI-------LGADGRARSVVVAAPADVSPLLRMQGAAYATRIAEDFRDRGQHV 267
Cdd:PRK14698 676 LAKWSDAQVVIYIGCGERGNEMTDVLEEFpklkdpkTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDV 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 268 LLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGG-----SITAFYTVLTEGDDQQDPIADS 342
Cdd:PRK14698 756 ALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSdyrvgSVSVIGAVSPPGGDFSEPVVQN 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 343 ARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEH------YARVRhfKQLLSSFQRNRDLVSVgAYAKGSD- 415
Cdd:PRK14698 836 TLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHknvdpeWKAMR--DKAMELLQKEAELQEI-VRIVGPDa 912
|
250 260
....*....|....*....|....*....
gi 364568425 416 -PMLDKAITLWPQL--EAFLQQGIFERSD 441
Cdd:PRK14698 913 lPERERAILLVARMlrEDYLQQDAFDEVD 941
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
164-397 |
1.88e-11 |
|
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: 64.15 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 164 RPINALLTVGRGQRMGLFAGSGVGKSVLLGMMAR-----YTQADVIVVgLIGERGREVKDFIENILGAdgrarsvVVAAP 238
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANaiaknHPEVELIVL-LIDERPEEVTDMRRSVKGE-------VVAST 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 239 ADVSPLLRMQGAAY----ATRIAEDfrdrGQHVLLIMDSLTRYAMAQREIAlaigePPATKGYPPSVFAK---LPALVER 311
Cdd:cd01128 77 FDEPPERHVQVAEMviekAKRLVEH----GKDVVILLDSITRLARAYNTVV-----PSSGKTLSGGVDANalhKPKRFFG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 312 AGNGISGGGSITAFYTVLTE-GDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRAMTSLITEEHYARVRH 390
Cdd:cd01128 148 AARNIEEGGSLTIIATALVDtGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTRKEELLLTPEELQKIWL 227
|
....*..
gi 364568425 391 FKQLLSS 397
Cdd:cd01128 228 LRRILSP 234
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
146-396 |
2.33e-11 |
|
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: 65.48 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 146 PFNPLQRTAIEH-VLDTGVRPINALLTVGRGQRMGLFAGSGVGKSVLLGMMAR-----YTQADVIVVgLIGERGREVKDF 219
Cdd:TIGR00767 138 PLYPNERLRLETsTEDLSTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQaitrnHPEVELIVL-LIDERPEEVTDM 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 220 IenilgadgraRSV---VVAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPpATKG 296
Cdd:TIGR00767 217 Q----------RSVkgeVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKV-LSGG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 297 YPPSVFAKlPALVERAGNGISGGGSITAFYTVLTE-GDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEASISRA 375
Cdd:TIGR00767 286 VDANALHR-PKRFFGAARNIEEGGSLTIIATALIDtGSRMDEVIFEEFKGTGNMELHLDRKLADRRIFPAIDIKKSGTRK 364
|
250 260
....*....|....*....|.
gi 364568425 376 MTSLITEEHYARVRHFKQLLS 396
Cdd:TIGR00767 365 EELLLTPEELQKIWVLRKIIS 385
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
146-397 |
1.02e-10 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 63.18 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 146 PFNPLQRTAIEH-VLDTGVRPINALLTVGRGQRMGLFAGSGVGKSVLL-----GMMARYTQADVIVVgLIGERGREVKDF 219
Cdd:PRK12608 103 PLHPRERLRLETgSDDLSMRVVDLVAPIGKGQRGLIVAPPRAGKTVLLqqiaaAVAANHPEVHLMVL-LIDERPEEVTDM 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 220 IENIlgadgraRSVVVAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIG-------EPP 292
Cdd:PRK12608 182 RRSV-------KGEVYASTFDRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAYNNEVESSGrtlsggvDAR 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 293 ATKGyPPSVFAklpalverAGNGISGGGSITAFYTVLTE-GDDQQDPIADSARAILDGHVVLSRRLAEAGHYPAIDIEAS 371
Cdd:PRK12608 255 ALQR-PKRLFG--------AARNIEEGGSLTIIATALVDtGSRMDEVIFEEFKGTGNMEIVLDRELADKRVFPAIDIAKS 325
|
250 260
....*....|....*....|....*.
gi 364568425 372 ISRAMTSLITEEHYARVRHFKQLLSS 397
Cdd:PRK12608 326 GTRREELLLDSKELEKVRRLRRALAS 351
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
172-397 |
5.30e-06 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 48.60 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 172 VGRGQRMGLFAGSGVGKSVLLGMMAR-----YTQADVIVVgLIGERGREVKDFienilgadgrARSV---VVAAPADVSP 243
Cdd:PRK09376 166 IGKGQRGLIVAPPKAGKTVLLQNIANsittnHPEVHLIVL-LIDERPEEVTDM----------QRSVkgeVVASTFDEPA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 244 LLRMQGAAY----ATRIAEDfrdrGQHVLLIMDSLTRYAmaqREIALAIgePPATKgyppsvfaklpalveragngisgg 319
Cdd:PRK09376 235 ERHVQVAEMviekAKRLVEH----GKDVVILLDSITRLA---RAYNTVV--PSSGK------------------------ 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364568425 320 gsitafytVLTEGddqQDPIA--------DSARAILDG-------------------------------HVVLSRRLAEA 360
Cdd:PRK09376 282 --------VLSGG---VDANAlhrpkrffGAARNIEEGgsltiiatalidtgsrmdevifeefkgtgnmELHLDRKLAEK 350
|
250 260 270
....*....|....*....|....*....|....*..
gi 364568425 361 GHYPAIDIEASISRAMTSLITEEHYARVRHFKQLLSS 397
Cdd:PRK09376 351 RIFPAIDINRSGTRKEELLLSPEELQKVWILRKILSP 387
|
|
| |
