|
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: 933.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 1 MTTRLTRWLTTLDNFEAKMAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCVIERQNGTETHEVESEVVGFNGQRLFLM 80
Cdd:PRK07960 1 MTTRLTRWLTTLDNFEAKMAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCVIERQNGSETHEVESEVVGFNGQRLFLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 81 PLEEVEGVLPGARVYAKNISAEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLD 160
Cdd:PRK07960 81 PLEEVEGILPGARVYARNISGEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 161 TGVRPINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPAD 240
Cdd:PRK07960 161 TGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 241 VSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGG 320
Cdd:PRK07960 241 VSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 321 SITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQR 400
Cdd:PRK07960 321 SITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLLSSFQR 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446135456 401 NRDLVSVGAYAKGSDPMLDKAIALWPQLEGYLQQGIFERADWEASLQGLERIFPT 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: 737.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 29 GRLTRATGLVLEATGLQLPLGATCVIERQNGtetHEVESEVVGFNGQRLFLMPLEEVEGVLPGARVYAKNisaeglqSGK 108
Cdd:TIGR03496 1 GRVTRVVGLVLEAVGLRAPVGSRCEIESSDG---DPIEAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLG-------GPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 109 QLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGK 188
Cdd:TIGR03496 71 RLPVGDSLLGRVIDGLGRPLDGKGPLDAGERVPLYAPPINPLKRAPIDEPLDVGVRAINGLLTVGRGQRMGIFAGSGVGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 189 SVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVL 268
Cdd:TIGR03496 151 STLLGMMARYTEADVVVVGLIGERGREVKEFIEDILGEEGLARSVVVAATADESPLMRLRAAFYATAIAEYFRDQGKDVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 269 LIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARAILD 348
Cdd:TIGR03496 231 LLMDSLTRFAMAQREIALAIGEPPATKGYPPSVFAKLPQLVERAGNGEEGKGSITAFYTVLVEGDDQQDPIADAARAILD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 349 GHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAIALWPQL 428
Cdd:TIGR03496 311 GHIVLSRELAEQGHYPAIDILASISRVMPDVVSPEHRQAARRFKQLLSRYQENRDLISIGAYQAGSDPELDQAIALYPRI 390
|
410 420
....*....|....*....|.
gi 446135456 429 EGYLQQGIFERADWEASLQGL 449
Cdd:TIGR03496 391 EAFLQQGMRERASFEESLEAL 411
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
13-453 |
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: 727.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 13 DNFEAKMAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCVIERQNGtetHEVESEVVGFNGQRLFLMPLEEVEGVLPGA 92
Cdd:COG1157 5 ARLLARLEELPPVRVSGRVTRVVGLLIEAVGPDASIGELCEIETADG---RPVLAEVVGFRGDRVLLMPLGDLEGISPGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 93 RVYAknisaegLQSGKQLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTV 172
Cdd:COG1157 82 RVVP-------TGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 173 GRGQRMGLFAGSGVGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAY 252
Cdd:COG1157 155 GRGQRIGIFAGSGVGKSTLLGMIARNTEADVNVIALIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 253 ATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEG 332
Cdd:COG1157 235 ATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERA--GNGGKGSITAFYTVLVEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 333 DDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGAYAK 412
Cdd:COG1157 313 DDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENEDLIRIGAYQP 392
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 446135456 413 GSDPMLDKAIALWPQLEGYLQQGIFERADWEASLQGLERIF 453
Cdd:COG1157 393 GSDPELDEAIALIPAIEAFLRQGMDERVSFEESLAQLAELL 433
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
13-454 |
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: 686.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 13 DNFEAKMAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCVIERQNGtETHeVESEVVGFNGQRLFLMPLEEVEGVLPGA 92
Cdd:TIGR01026 9 YNRLCQEMDLRLVKRVGRVTKVKGLLIEAVGPQASVGDLCLIERRGS-EGR-LVAEVVGFNGEFVFLMPYEEVEGVRPGS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 93 RVYAKNisaEGLQsgkqLPLGPALLGRVLDGSGKPLDGLPSP-DTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLT 171
Cdd:TIGR01026 87 KVLATG---EGLS----IKVGDGLLGRVLDGLGKPIDGKGKFlDNVETEGLITAPINPLKRAPIREILSTGVRSIDGLLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 172 VGRGQRMGLFAGSGVGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAA 251
Cdd:TIGR01026 160 VGKGQRIGIFAGSGVGKSTLLGMIARNTEADVNVIALIGERGREVREFIEHDLGEEGLKRSVVVVATSDQSPLLRLKGAY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 252 YATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTE 331
Cdd:TIGR01026 240 VATAIAEYFRDQGKDVLLLMDSVTRFAMAQREIGLAAGEPPATKGYTPSVFSTLPRLLERA--GASGKGSITAFYTVLVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 332 GDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGAYA 411
Cdd:TIGR01026 318 GDDMNEPIADSVRGILDGHIVLSRALAQRGHYPAIDVLASISRLMTAIVSEEHRRAARKFRELLSKYKDNEDLIRIGAYQ 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 446135456 412 KGSDPMLDKAIALWPQLEGYLQQGIFERADWEASLQGLERIFP 454
Cdd:TIGR01026 398 RGSDRELDFAIAKYPKLERFLKQGINEKVNFEESLQQLEEIFR 440
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
29-452 |
0e+00 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 640.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 29 GRLTRATGLVLEATGLQLPLGATCVIERQNGtethEVESEVVGFNGQRLFLMPLEEVEGVLPGARVyakniSAEGLQSGk 108
Cdd:PRK08972 27 GKLVRVVGLTLEATGCRAPVGSLCSIETMAG----ELEAEVVGFDGDLLYLMPIEELRGVLPGARV-----TPLGEQSG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 109 qLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGK 188
Cdd:PRK08972 97 -LPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 189 SVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVL 268
Cdd:PRK08972 176 SVLLGMMTRGTTADVIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 269 LIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARAILD 348
Cdd:PRK08972 256 LLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSITAFYTVLTEGDDLQDPIADASRAILD 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 349 GHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAIALWPQL 428
Cdd:PRK08972 336 GHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLYQQNRDLISIGAYKQGSDPRIDNAIRLQPAM 415
|
410 420
....*....|....*....|....
gi 446135456 429 EGYLQQGIFERADWEASLQGLERI 452
Cdd:PRK08972 416 NAFLQQTMKEAVPYDMSVNMLKQL 439
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
29-454 |
0e+00 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 594.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 29 GRLTRATGLVLEATGLQLPLGATCVIERQNGTETHEVESEVVGFNGQRLFLMPLEEVEGVLPGARVYAknisaegLQSGK 108
Cdd:PRK05688 29 GRLLRMVGLTLEAEGLRAAVGSRCLVINDDSYHPVQVEAEVMGFSGDKVFLMPVGSVAGIAPGARVVP-------LADTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 109 QLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGK 188
Cdd:PRK05688 102 RLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 189 SVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVL 268
Cdd:PRK05688 182 SVLLGMMTRFTEADIIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 269 LIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARAILD 348
Cdd:PRK05688 262 LLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITAFYTVLSEGDDQQDPIADSARGVLD 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 349 GHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAIALWPQL 428
Cdd:PRK05688 342 GHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPHL 421
|
410 420
....*....|....*....|....*.
gi 446135456 429 EGYLQQGIFERADWEASLQGLERIFP 454
Cdd:PRK05688 422 VQFLRQGLRENVSLAQSREQLAAIFA 447
|
|
| 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: 529.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 29 GRLTRATGLVLEATGLQLPLGATCVIERQNGtetHEVESEVVGFNGQRLFLMPLEEVEGVLPGARVYAknisaeglqSGK 108
Cdd:TIGR03497 1 GKVTRVIGLTIESKGPKASIGELCSILTKGG---KPVLAEVVGFKEENVLLMPLGEVEGIGPGSLVIA---------TGR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 109 QL--PLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGLFAGSGV 186
Cdd:TIGR03497 69 PLaiKVGKGLLGRVLDGLGRPLDGEGPIIGEEPYPLDNPPPNPLKRPRIRDPLETGIKAIDGLLTIGKGQRVGIFAGSGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 187 GKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQH 266
Cdd:TIGR03497 149 GKSTLLGMIARNAKADINVIALIGERGREVRDFIEKDLGEEGLKRSVVVVATSDQPALMRLKAAFTATAIAEYFRDQGKD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 267 VLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQDPIADSARAI 346
Cdd:TIGR03497 229 VLLMMDSVTRFAMAQREIGLAVGEPPTTRGYTPSVFSLLPKLLERS--GNSQKGSITGFYTVLVDGDDMNEPIADAVRGI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 347 LDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAIALWP 426
Cdd:TIGR03497 307 LDGHIVLSRELAAKNHYPAIDVLASVSRVMNEIVSEEHKELAGKLRELLAVYKEAEDLINIGAYKRGSNPKIDEAIRYIE 386
|
410 420
....*....|....*....|....*..
gi 446135456 427 QLEGYLQQGIFERADWEASLQGLERIF 453
Cdd:TIGR03497 387 KINSFLKQGIDEKFTFEETVQLLKELL 413
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
22-453 |
4.91e-171 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 487.31 E-value: 4.91e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 22 LPAVRRYGRLTRATGLVLEATGLQLPLGATCVIERQNGTeTHEVESEVVGFNGQRLFLMPLEEVEGVLPGARVyaknisa 101
Cdd:PRK07721 13 LDPYKRYGKVSRVIGLMIESKGPESSIGDVCYIHTKGGG-DKAIKAEVVGFKDEHVLLMPYTEVAEIAPGCLV------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 102 EGLQSGKQLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGLF 181
Cdd:PRK07721 85 EATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 182 AGSGVGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFR 261
Cdd:PRK07721 165 AGSGVGKSTLMGMIARNTSADLNVIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 262 DRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQDPIAD 341
Cdd:PRK07721 245 DQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERT--GTNASGSITAFYTVLVDGDDMNEPIAD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 342 SARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKA 421
Cdd:PRK07721 323 TVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLINIGAYKRGSSREIDEA 402
|
410 420 430
....*....|....*....|....*....|..
gi 446135456 422 IALWPQLEGYLQQGIFERADWEASLQGLERIF 453
Cdd:PRK07721 403 IQFYPQIISFLKQGTDEKATFEESIQALLSLF 434
|
|
| FliI_clade3 |
TIGR03498 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
29-452 |
4.82e-169 |
|
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: 481.42 E-value: 4.82e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 29 GRLTRATGLVLEATGLQ--LPLGATCVIERQNGTEtheVESEVVGFNGQRLFLMPLEEVEGVLPGARVYAKNisaeglqS 106
Cdd:TIGR03498 1 GRVTAVTGLLIEVRGLSraVRLGDRCAIRARDGRP---VLAEVVGFNGDRVLLMPFEPLEGVGLGCAVFARE-------G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 107 GKQLPLGPALLGRVLDGSGKPLDGLPS-PDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGLFAGSG 185
Cdd:TIGR03498 71 PLAVRPHPSWLGRVINALGEPIDGKGPlPQGERRYPLRASPPPAMSRARVGEPLDTGVRVIDTFLPLCRGQRLGIFAGSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 186 VGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQ 265
Cdd:TIGR03498 151 VGKSTLLSMLARNTDADVVVIALVGERGREVREFLEDDLGEEGLKRSVVVVATSDESPLMRRQAAYTATAIAEYFRDQGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 266 HVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARA 345
Cdd:TIGR03498 231 DVLLLMDSVTRFAMAQREIGLAAGEPPVARGYTPSVFSELPRLLERAGPGAEGKGSITGIFTVLVDGDDHNEPVADAVRG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 346 ILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAIALW 425
Cdd:TIGR03498 311 ILDGHIVLDRAIAERGRYPAINVLASVSRLAPRVWSPEERKLVRRLRALLARYEETEDLIRLGAYRKGSDPELDEAIRLV 390
|
410 420
....*....|....*....|....*..
gi 446135456 426 PQLEGYLQQGIFERADWEASLQGLERI 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 |
1.12e-167 |
|
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: 478.35 E-value: 1.12e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 23 PAVRRYGRLTRATGLVLEATGLQLPLGATCVIERQNGTEtheVESEVVGFNGQRLFLMPLEEVEGVLPGARVyaknisaE 102
Cdd:TIGR02546 1 QPVRVRGRVTEVSGTLLKAVLPGARVGELCLIRRRDPSQ---LLAEVVGFTGDEALLSPLGELHGISPGSEV-------I 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 103 GLQSGKQLPLGPALLGRVLDGSGKPLDGLPSP--DTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGL 180
Cdd:TIGR02546 71 PTGRPLSIRVGEALLGRVLDGFGRPLDGKGELpaGEIETRPLDADPPPPMSRQPIDQPLPTGVRAIDGLLTCGEGQRIGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 181 FAGSGVGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDF 260
Cdd:TIGR02546 151 FAGAGVGKSTLLGMIARGASADVNVIALIGERGREVREFIEHHLGEEGRKRSVLVVSTSDRPSLERLKAAYTATAIAEYF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 261 RDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQDPIA 340
Cdd:TIGR02546 231 RDQGKRVLLMMDSLTRFARALREIGLAAGEPPARGGYPPSVFSSLPRLLERA--GNGEKGSITALYTVLVEGDDMNDPIA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 341 DSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGAYAKGSDPMLDK 420
Cdd:TIGR02546 309 DEVRSILDGHIVLSRALAERNHYPAIDVLASLSRVMSQVVSTEHRRAAGKLRRLLATYKEVELLIRLGEYQPGSDPETDD 388
|
410 420 430
....*....|....*....|....*....|...
gi 446135456 421 AIALWPQLEGYLQQGIFERADWEASLQGLERIF 453
Cdd:TIGR02546 389 AIDKIDAIRAFLRQSTDEYSPYEETLEQLHALV 421
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
18-455 |
1.48e-158 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 455.50 E-value: 1.48e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 18 KMAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCVIERQNGTEtheVESEVVGFNGQRLFLMPLEEVEGVLPGARVYAK 97
Cdd:PRK07196 8 SIENIHLARVAGRLVRVTGLLLESVGCRLAIGQRCRIESVDETF---IEAQVVGFDRDITYLMPFKHPGGVLGGARVFPS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 98 NISAEglqsgkqLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQR 177
Cdd:PRK07196 85 EQDGE-------LLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 178 MGLFAGSGVGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIA 257
Cdd:PRK07196 158 VGLMAGSGVGKSVLLGMITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 258 EDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgNGISGGGSITAFYTVLTEGDDQQD 337
Cdd:PRK07196 238 TYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESA-GNSSGNGTMTAIYTVLAEGDDQQD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 338 PIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGAYAKGSDPM 417
Cdd:PRK07196 317 PIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVAGADPM 396
|
410 420 430
....*....|....*....|....*....|....*...
gi 446135456 418 LDKAIALWPQLEGYLQQGIFERADWEASLQGLERIFPT 455
Cdd:PRK07196 397 ADQAVHYYPAITQFLRQEVGHPALFSASVEQLTGMFPS 434
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
109-374 |
2.07e-156 |
|
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: 443.54 E-value: 2.07e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 109 QLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGK 188
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 189 SVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVL 268
Cdd:cd01136 81 STLLGMIARNTDADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 269 LIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQDPIADSARAILD 348
Cdd:cd01136 161 LLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERA--GNGEKGSITAFYTVLVEGDDFNDPIADEVRSILD 238
|
250 260
....*....|....*....|....*.
gi 446135456 349 GHIVLSRRLAEAGHYPAIDIEASISR 374
Cdd:cd01136 239 GHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
17-453 |
1.16e-155 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 448.66 E-value: 1.16e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 17 AKMAQLPAVRRYGRLTRATGLVLEATGLQ--LPLGATCVIERQNGTEtheVESEVVGFNGQRLFLMPLEEVEGVLPGARV 94
Cdd:PRK08927 7 AAIGDIDTLVIYGRVVAVRGLLVEVAGPIhaLSVGARIVVETRGGRP---VPCEVVGFRGDRALLMPFGPLEGVRRGCRA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 95 YAKNisaeglqSGKQLPLGPALLGRVLDGSGKPLDGL-PSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVG 173
Cdd:PRK08927 84 VIAN-------AAAAVRPSRAWLGRVVNALGEPIDGKgPLPQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 174 RGQRMGLFAGSGVGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQgAAYA 253
Cdd:PRK08927 157 RGQRMGIFAGSGVGKSVLLSMLARNADADVSVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQ-AAYL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 254 T-RIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEG 332
Cdd:PRK08927 236 TlAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGEGTITGLFTVLVDG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 333 DDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGAYAK 412
Cdd:PRK08927 316 DDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLGAYRA 395
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 446135456 413 GSDPMLDKAIALWPQLEGYLQQGIFERADWEASLQGLERIF 453
Cdd:PRK08927 396 GSDPEVDEAIRLNPALEAFLRQGKDEATSLAEGYARLAQIL 436
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
13-452 |
3.17e-148 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 429.11 E-value: 3.17e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 13 DNFEAKMAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCVIERQNgtETHEVESEVVGFNGQRLFLMPLEEVEGVLPGA 92
Cdd:PRK08472 4 ESLKNKLQKFNLSPRFGSITKISPTIIEADGLNPSVGDIVKIESSD--NGKECLGMVVVIEKEQFGISPFSFIEGFKIGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 93 RVYaknISAEGLQsgkqLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTV 172
Cdd:PRK08472 82 KVF---ISKEGLN----IPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 173 GRGQRMGLFAGSGVGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEgRARSVVIAAPADVSPLLRMQGAAY 252
Cdd:PRK08472 155 GKGQKLGIFAGSGVGKSTLMGMIVKGCLAPIKVVALIGERGREIPEFIEKNLGGD-LENTVIVVATSDDSPLMRKYGAFC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 253 ATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSiTAFYTVLTEG 332
Cdd:PRK08472 234 AMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGKGSI-TAFFTVLVEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 333 DDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGAYAK 412
Cdd:PRK08472 313 DDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAYQK 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 446135456 413 GSDPMLDKAIALWPQLEGYLQQGIFERADWEASLQGLERI 452
Cdd:PRK08472 393 GNDKELDEAISKKEFMEQFLKQNPNELFPFEQTFEQLEEI 432
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
16-452 |
9.59e-143 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 415.75 E-value: 9.59e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 16 EAKMAQLPA----VRRYGRLTRATGLVLEATGLQLPLGATCVIERQNgtetheVESEVVGFNGQRLFLMPLEEVEGVLPG 91
Cdd:PRK06820 14 QQQLTRPSAppegLRYRGPIVEIGPTLLRASLPGVAQGELCRIEPQG------MLAEVVSIEQEMALLSPFASSDGLRCG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 92 ARVyaknisaEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPsPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLT 171
Cdd:PRK06820 88 QWV-------TPLGHMHQVQVGADLAGRILDGLGAPIDGGP-PLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 172 VGRGQRMGLFAGSGVGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAA 251
Cdd:PRK06820 160 CGEGQRIGIFAAAGVGKSTLLGMLCADSAADVMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 252 YATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTE 331
Cdd:PRK06820 240 TATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERT--GNSDRGSITAFYTVLVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 332 GDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGAYA 411
Cdd:PRK06820 318 GDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGEYQ 397
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 446135456 412 KGSDPMLDKAIALWPQLEGYLQQGIFERADWEASLQGLERI 452
Cdd:PRK06820 398 AGEDLQADEALQRYPAICAFLQQDHSETAHLETTLEHLAQV 438
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
16-452 |
2.99e-137 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 401.44 E-value: 2.99e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 16 EAKMAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCviERQNGTETHEVESEVVGFNGQRLFLMPLEEVEGVLPGARVy 95
Cdd:PRK06936 12 RHAIVGSRLIQIRGRVTQVTGTILKAVVPGVRIGELC--YLRNPDNSLSLQAEVIGFAQHQALLTPLGEMYGISSNTEV- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 96 aknisaegLQSGK--QLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVG 173
Cdd:PRK06936 89 --------SPTGTmhQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 174 RGQRMGLFAGSGVGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYA 253
Cdd:PRK06936 161 EGQRMGIFAAAGGGKSTLLASLIRSAEVDVTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 254 TRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGD 333
Cdd:PRK06936 241 TSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERA--GQSDKGSITALYTVLVEGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 334 DQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGAYAKG 413
Cdd:PRK06936 319 DMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIGEYQKG 398
|
410 420 430
....*....|....*....|....*....|....*....
gi 446135456 414 SDPMLDKAIALWPQLEGYLQQGIFERADWEASLQGLERI 452
Cdd:PRK06936 399 QDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLLETL 437
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
13-452 |
1.57e-133 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 392.21 E-value: 1.57e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 13 DNFEAKMAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCVIERQNGTETHEveSEVVGFNGQRLFLMPLEEVEGVLPGA 92
Cdd:PRK09099 10 DALERELAALPAVRRTGKVVEVIGTLLRVSGLDVTLGELCELRQRDGTLLQR--AEVVGFSRDVALLSPFGELGGLSRGT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 93 RVYaknisaeGLQSGKQLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTV 172
Cdd:PRK09099 88 RVI-------GLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 173 GRGQRMGLFAGSGVGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAY 252
Cdd:PRK09099 161 GEGQRMGIFAPAGVGKSTLMGMFARGTQCDVNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 253 ATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEG 332
Cdd:PRK09099 241 ATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERA--GMGETGSITALYTVLAED 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 333 DDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGAYAK 412
Cdd:PRK09099 319 ESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVGEYRA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 446135456 413 GSDPMLDKAIALWPQLEGYLQQGIFERADWEASLQGLERI 452
Cdd:PRK09099 399 GSDPVADEAIAKIDAIRDFLSQRTDEYSDPDATLAALAEL 438
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
109-375 |
2.29e-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: 367.55 E-value: 2.29e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 109 QLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGK 188
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 189 SVLLGMMARYT---RADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQ 265
Cdd:cd19476 81 TVLAMQLARNQakaHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 266 HVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARA 345
Cdd:cd19476 161 HVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTPGDDLTDPIPDNTFA 240
|
250 260 270
....*....|....*....|....*....|
gi 446135456 346 ILDGHIVLSRRLAEAGHYPAIDIEASISRA 375
Cdd:cd19476 241 ILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
26-452 |
6.36e-120 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 356.96 E-value: 6.36e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 26 RRYGRLTRATGLVLEATGLQLPLGATCVIERQNGTetheveSEVVGFNGQRLFLMPLEEVEGVLPGARVYAknisaegLQ 105
Cdd:PRK07594 20 CRWGRIQDVSATLLNAWLPGVFMGELCCIKPGEEL------AEVVGINGSKALLSPFTSTIGLHCGQQVMA-------LR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 106 SGKQLPLGPALLGRVLDGSGKPLDGLPSPDTTETgALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGLFAGSG 185
Cdd:PRK07594 87 RRHQVPVGEALLGRVIDGFGRPLDGRELPDVCWK-DYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 186 VGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQ 265
Cdd:PRK07594 166 VGKSTLLAMLCNAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 266 HVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQDPIADSARA 345
Cdd:PRK07594 246 RVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERT--GMGEKGSITAFYTVLVEGDDMNEPLADEVRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 346 ILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAIALW 425
Cdd:PRK07594 324 LLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEYQRGVDTDTDKAIDTY 403
|
410 420
....*....|....*....|....*..
gi 446135456 426 PQLEGYLQQGIFERADWEASLQGLERI 452
Cdd:PRK07594 404 PDICTFLRQSKDEVCGPELLIEKLHQI 430
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
162-373 |
5.22e-115 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 336.25 E-value: 5.22e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 162 GVRPINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADV 241
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLGSGALKRTVVVVATSDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 242 SPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGS 321
Cdd:pfam00006 81 PPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKGKGGS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446135456 322 ITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASIS 373
Cdd:pfam00006 161 ITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
26-452 |
7.98e-113 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 338.89 E-value: 7.98e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 26 RRYGRLTRATGLVLEATGLQLPLGATCVIERQNGTETHEVESEVVGFNGQRLFLMPLEEVEGvlpgarvyaknISAEGL- 104
Cdd:PRK08149 5 QRLAHPLRIQGPIIEAELPDVAIGEICEIRAGWHSNEVIARAQVVGFQRERTILSLIGNAQG-----------LSRQVVl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 105 -QSGKQL--PLGPALLGRVLDGSGKPLDGLPSPDTTETGALI----TPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQR 177
Cdd:PRK08149 74 kPTGKPLsvWVGEALLGAVLDPTGKIVERFDAPPTVGPISEErvidVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 178 MGLFAGSGVGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIA 257
Cdd:PRK08149 154 MGIFASAGCGKTSLMNMLIEHSEADVFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 258 EDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQD 337
Cdd:PRK08149 234 EYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERP--GATLAGSITAFYTVLLESEEEPD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 338 PIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGAYAKGSDPM 417
Cdd:PRK08149 312 PIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGEYRRGENAD 391
|
410 420 430
....*....|....*....|....*....|....*
gi 446135456 418 LDKAIALWPQLEGYLQQGIFERADWEASLQGLERI 452
Cdd:PRK08149 392 NDRAMDKRPALEAFLKQDVAEKSSFSDTLERLNEF 426
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
16-434 |
2.35e-110 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 333.12 E-value: 2.35e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 16 EAKMAQLPAVRRYGRLTRATGLVLEATGLQ--LPLGATCVIERQNGTetheVESEVVGFNGQRLFLMPLEEVEGVLPGAR 93
Cdd:PRK06002 15 ERYAAPEPLVRIGGTVSEVTASHYRVRGLSrfVRLGDFVAIRADGGT----HLGEVVRVDPDGVTVKPFEPRIEIGLGDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 94 VYAKnisaeglqSGKQLPLGPALLGRVLDGSGKPLDGL----PSPDTTETGALiTPPfnPLQRTPIEHVLDTGVRPINAL 169
Cdd:PRK06002 91 VFRK--------GPLRIRPDPSWKGRVINALGEPIDGLgplaPGTRPMSIDAT-APP--AMTRARVETGLRTGVRVIDIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 170 LTVGRGQRMGLFAGSGVGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEgRARSVVIAAPADVSPLLRMQG 249
Cdd:PRK06002 160 TPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGREVREFLEDTLADN-LKKAVAVVATSDESPMMRRLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 250 AAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVL 329
Cdd:PRK06002 239 PLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEGGGSITGIFSVL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 330 TEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGA 409
Cdd:PRK06002 319 VDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEETRDLRLIGG 398
|
410 420
....*....|....*....|....*
gi 446135456 410 YAKGSDPMLDKAIALWPQLEGYLQQ 434
Cdd:PRK06002 399 YRAGSDPDLDQAVDLVPRIYEALRQ 423
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
41-415 |
1.37e-91 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 284.56 E-value: 1.37e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 41 ATGLQLPLGATCVIERqngtetHEVESEVVGFNGQRLFLMPLEEVEGVLPGARVYaknISAEGLQsgkqLPLGPALLGRV 120
Cdd:PRK06793 35 AKGPKAKIGDVCFVGE------HNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVT---LIAEDVV----IPRGNHLLGKV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 121 LDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTR 200
Cdd:PRK06793 102 LSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 201 ADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMA 280
Cdd:PRK06793 182 ADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 281 QREIALAIGEPPaTKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEA 360
Cdd:PRK06793 262 RRSVDIAVKELP-IGGKTLLMESYMKKLLERS--GKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATL 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446135456 361 GHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGAYAKGSD 415
Cdd:PRK06793 339 SHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGTIQENAE 393
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
26-452 |
9.19e-90 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 279.87 E-value: 9.19e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 26 RRYGRLTRATGLVLEATGLQLPLGATCVIerqNGTETHEVESEVVGFNGQRLFLMPLEEVEGVLPGARVYAknisaegLQ 105
Cdd:PRK05922 18 RECGLLSRVSGNLLEAQGLSACLGELCQI---SLSKSPPILAEVIGFHNRTTLLMSLSPIHYVALGAEVLP-------LR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 106 SGKQLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGLFAGSG 185
Cdd:PRK05922 88 RPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 186 VGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPA-DVSPLLRMQGAAyATRIAEDFRDRG 264
Cdd:PRK05922 168 SGKSSLLSTIAKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAhETAPTKVIAGRA-AMTIAEYFRDQG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 265 QHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGdDQQDPIADSAR 344
Cdd:PRK05922 247 HRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERA--GNNDKGSITALYAILHYP-NHPDIFTDYLK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 345 AILDGHIVLSRRlAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAIAL 424
Cdd:PRK05922 324 SLLDGHFFLTPQ-GKALASPPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGAYVPGQDAHLDRAVKL 402
|
410 420
....*....|....*....|....*...
gi 446135456 425 WPQLEGYLQQGIFERADWEASLQGLERI 452
Cdd:PRK05922 403 LPSIKQFLSQPLSSYCALHNTLKQLEAL 430
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
109-376 |
9.32e-39 |
|
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: 141.59 E-value: 9.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 109 QLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGK 188
Cdd:cd01135 3 KLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLPH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 189 SVLLGMMARYTR------ADVIVVGLIGERGRE----VKDFIENilGAEGraRSVVIAAPADVSPLLRMQGAAYATRIAE 258
Cdd:cd01135 83 NELAAQIARQAGvvgseeNFAIVFAAMGVTMEEarffKDDFEET--GALE--RVVLFLNLANDPTIERIITPRMALTTAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 259 DFR-DRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFyTVLT-EGDDQQ 336
Cdd:cd01135 159 YLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQI-PILTmPNDDIT 237
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446135456 337 DPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAM 376
Cdd:cd01135 238 HPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLM 277
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
28-407 |
3.98e-36 |
|
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: 138.70 E-value: 3.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 28 YGRLTRATGLVLEA--TGLQLP--LGATCVIERQNGTETHEVeSEVVGFNGQRLFLMplEEVEGVLPGARVYAKNISAEg 103
Cdd:TIGR01039 2 KGKVVQVIGPVVDVefEQGELPriYNALKVQNRAESELTLEV-AQHLGDDTVRTIAM--GSTDGLVRGLEVIDTGAPIS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 104 lqsgkqLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGLFAG 183
Cdd:TIGR01039 78 ------VPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 184 SGVGKSVLLGMMAR---YTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDF 260
Cdd:TIGR01039 152 AGVGKTVLIQELINniaKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 261 RD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERagNGISGGGSITAFYTVLTEGDDQQDPI 339
Cdd:TIGR01039 232 RDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQER--ITSTKTGSITSVQAVYVPADDLTDPA 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446135456 340 ADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALI-SEQHYARVRTFKQLLSSFQRNRDLVSV 407
Cdd:TIGR01039 310 PATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVvGEEHYDVARGVQQILQRYKELQDIIAI 378
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
109-374 |
7.45e-36 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 138.51 E-value: 7.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 109 QLPLGPALLGRVLDGSGKPLDGLPSPDTTETGAL--ITPPFnpLQRTPIEHVLDTGVRPINALLTVGRGQRMGLFAGSGV 186
Cdd:PRK13343 96 EVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLerPAPAI--IERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 187 GKSVL-LGMMARYTRADVIVVG-LIGERGREVKDFIENILGAEGRARSVVIAAPADVSPllrmqGAAY-----ATRIAED 259
Cdd:PRK13343 174 GKTAIaIDAIINQKDSDVICVYvAIGQKASAVARVIETLREHGALEYTTVVVAEASDPP-----GLQYlapfaGCAIAEY 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 260 FRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGG--SITAFYTVLTEGDDQQD 337
Cdd:PRK13343 249 FRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGggSLTALPIIETLAGELSA 328
|
250 260 270
....*....|....*....|....*....|....*..
gi 446135456 338 PIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISR 374
Cdd:PRK13343 329 YIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
109-376 |
7.70e-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: 130.80 E-value: 7.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 109 QLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALIT--PPFNPLQRTPieHVLDTGVRPINALLTVGRGQRMGLFAGSGV 186
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHReaPEFVELSTEQ--EILETGIKVVDLLAPYAKGGKIGLFGGAGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 187 GKSVLlgMM------ARYTRADVIVVGlIGERGREVKDFIE-----NILGAEGRARSVVIAAPADVSPLLRMQGAAYATR 255
Cdd:cd01133 79 GKTVL--IMelinniAKAHGGYSVFAG-VGERTREGNDLYHemkesGVINLDGLSKVALVYGQMNEPPGARARVALTGLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 256 IAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERagNGISGGGSITAFYTVLTEGDD 334
Cdd:cd01133 156 MAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQER--ITSTKKGSITSVQAVYVPADD 233
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446135456 335 QQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAM 376
Cdd:cd01133 234 LTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
109-374 |
3.36e-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: 129.22 E-value: 3.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 109 QLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGK 188
Cdd:cd01132 3 EVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 189 -SVLLGMMARYTRADVIVVGL-IGERGREVKDFIENILGAEGRARSVVIAAPA-DVSPLLRMqgAAYA-TRIAEDFRDRG 264
Cdd:cd01132 83 tAIAIDTIINQKGKKVYCIYVaIGQKRSTVAQIVKTLEEHGAMEYTIVVAATAsDPAPLQYL--APYAgCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 265 QHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGS--ITAFYTVLTEGDDQQDPIADS 342
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGgsLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|..
gi 446135456 343 ARAILDGHIVLSRRLAEAGHYPAIDIEASISR 374
Cdd:cd01132 241 VISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
97-404 |
9.36e-34 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 131.87 E-value: 9.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 97 KNISAEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQ 176
Cdd:PRK04196 65 KDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 177 RMGLFAGSGVGKSVLLGMMARytRADV--------IVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQ 248
Cdd:PRK04196 145 KLPIFSGSGLPHNELAAQIAR--QAKVlgeeenfaVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERIL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 249 GAAYATRIAE--DFrDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFy 326
Cdd:PRK04196 223 TPRMALTAAEylAF-EKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQI- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 327 TVLT-EGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQH----YARVrtFKQLLSSFQRN 401
Cdd:PRK04196 301 PILTmPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKtredHKDV--ANQLYAAYARG 378
|
...
gi 446135456 402 RDL 404
Cdd:PRK04196 379 KDL 381
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
84-407 |
3.72e-31 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 125.15 E-value: 3.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 84 EVEGVLPGARVYAKNISA-EGLQSGKQ---------LPLGPALLGRVLDGSGKPLDGLPSPDTTETGAL--ITPPFNPLQ 151
Cdd:CHL00060 60 EVQQLLGNNRVRAVAMSAtDGLMRGMEvidtgaplsVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIhrSAPAFIQLD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 152 RTPieHVLDTGVRPINALLTVGRGQRMGLFAGSGVGKSVLLgM-----MARyTRADVIVVGLIGERGREVKDfieniLGA 226
Cdd:CHL00060 140 TKL--SIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLI-MelinnIAK-AHGGVSVFGGVGERTREGND-----LYM 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 227 EGRARSVVIAAPADVS------------PLLRMQGAAYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPA 293
Cdd:CHL00060 211 EMKESGVINEQNIAESkvalvygqmnepPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 294 TKGYPPSVFAKLPALVERagNGISGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASIS 373
Cdd:CHL00060 291 AVGYQPTLSTEMGSLQER--ITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 368
|
330 340 350
....*....|....*....|....*....|....*
gi 446135456 374 RAMTALI-SEQHYARVRTFKQLLSSFQRNRDLVSV 407
Cdd:CHL00060 369 TMLQPRIvGEEHYETAQRVKQTLQRYKELQDIIAI 403
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
111-404 |
1.07e-28 |
|
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: 117.88 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 111 PLGPALLGRVLDGSGKPLDGLPSPDTTETGAlI---TPPFNplQRTPIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVG 187
Cdd:COG0055 82 PVGEATLGRIFNVLGEPIDGKGPIEAKERRP-IhrpAPPFE--EQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 188 KSVLLgM-----MARYTRADVIVVGlIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRD 262
Cdd:COG0055 159 KTVLI-MelihnIAKEHGGVSVFAG-VGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRD 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 263 -RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERagNGISGGGSITAFYTVLTEGDDQQDPIAD 341
Cdd:COG0055 237 eEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQER--ITSTKKGSITSVQAVYVPADDLTDPAPA 314
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446135456 342 SARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALI-SEQHYARVRTFKQLLssfQRNRDL 404
Cdd:COG0055 315 TTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIvGEEHYRVAREVQRIL---QRYKEL 375
|
|
| ATP-synt_flagellum-secretory_path_III_C |
cd18114 |
Flagellum-specific ATP synthase, C-terminal domain; The C-terminal domain of the ... |
384-454 |
1.74e-28 |
|
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: 106.92 E-value: 1.74e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446135456 384 HYARVRTFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAIALWPQLEGYLQQGIFERADWEASLQGLERIFP 454
Cdd:cd18114 1 HYLAARKFRELMSTYQENEDLIRIGAYKKGSDPEVDEAIRLKPQIEAFLKQGLNEKAPLEESLQQLEEIFG 71
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
380-449 |
1.08e-25 |
|
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: 99.43 E-value: 1.08e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 380 ISEQHYARVRTFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAIALWPQLEGYLQQGIFERADWEASLQGL 449
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIGAYQAGSDPEIDEAIAKRPAINAFLRQGVDEPVSFEETLAQL 70
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
109-394 |
1.94e-25 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 108.51 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 109 QLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGK 188
Cdd:CHL00059 75 QIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 189 -SVLLGMMARYTRADVIVVGL-IGERGREVKDfIENILGAEGR-ARSVVIAAPADVSPLLR----MQGAAyatrIAEDFR 261
Cdd:CHL00059 155 tAVATDTILNQKGQNVICVYVaIGQKASSVAQ-VVTTLQERGAmEYTIVVAETADSPATLQylapYTGAA----LAEYFM 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 262 DRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISG--GGSITAFYTVLTEGDDQQDPI 339
Cdd:CHL00059 230 YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQlgEGSMTALPIVETQAGDVSAYI 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446135456 340 ADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAliseqhyARVRTFKQL 394
Cdd:CHL00059 310 PTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSA-------AQIKAMKQV 357
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
112-367 |
6.01e-25 |
|
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: 103.81 E-value: 6.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 112 LGPALLGRVLDGSGKPLDGLpspdtTETGALITPPFNPLQRTPI------------EHVLDTGVRPINALLTVGRGqrmG 179
Cdd:cd01134 6 LGPGLLGSIFDGIQRPLEVI-----AETGSIFIPRGVNVQRWPVrqprpvkeklppNVPLLTGQRVLDTLFPVAKG---G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 180 LFA---GSGVGKSVLLGMMARYTRADVIVVGLIGERGREV----KDFIENILGAEGRA---RSVVIAAPADvspllrMQG 249
Cdd:cd01134 78 TAAipgPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMaevlEEFPELKDPITGESlmeRTVLIANTSN------MPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 250 AA-----Y-ATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERA-----GNGISG 318
Cdd:cd01134 152 AAreasiYtGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrcLGSPGR 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446135456 319 GGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAID 367
Cdd:cd01134 232 EGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSIN 280
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
26-374 |
1.02e-24 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 105.89 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 26 RRYGRLTRATG--LVLEATGLQLplGATCVIERQNGTETheveSEVVGFNGQRLFLMPLEEVEGVLPGARVyaknisaEG 103
Cdd:PRK02118 3 KIYTKITDITGnvITVEAEGVGY--GELATVERKDGSSL----AQVIRLDGDKVTLQVFGGTRGISTGDEV-------VF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 104 LQSGKQLPLGPALLGRVLDGSGKPLDGLPSPDTTETgALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGLFAG 183
Cdd:PRK02118 70 LGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGEPI-EIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 184 SGVGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFR-D 262
Cdd:PRK02118 149 SGEPYNALLARIALQAEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 263 RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSitafyTVLT----EGDDQQDP 338
Cdd:PRK02118 229 GKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEDGGSI-----TIIAvttmPGDDVTHP 303
|
330 340 350
....*....|....*....|....*....|....*.
gi 446135456 339 IADSARAILDGHIVLsrrlaeagHYPAIDIEASISR 374
Cdd:PRK02118 304 VPDNTGYITEGQFYL--------RRGRIDPFGSLSR 331
|
|
| ATP-synt_flagellum-secretory_path_III_N |
cd18117 |
Flagellum-specific ATP synthase, N-terminal domain; The N-terminal domain of the ... |
27-98 |
4.86e-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: 92.21 E-value: 4.86e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446135456 27 RYGRLTRATGLVLEATGLQLPLGATCVIERQNGtetHEVESEVVGFNGQRLFLMPLEEVEGVLPGARVYAKN 98
Cdd:cd18117 1 VYGRVVRVVGLLLEAVGPQAPIGELCLIETADG---LSILAEVVGFSGEKVLLMPLGELSGLSPGARVVPLG 69
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
109-454 |
6.85e-23 |
|
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: 100.95 E-value: 6.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 109 QLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGK 188
Cdd:TIGR01040 75 RTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 189 SVLLGMMAR------YTRADV---------IVVGLIG---ERGREVK-DFIENilGAEGRArsVVIAAPADVSPLLRMQG 249
Cdd:TIGR01040 155 NEIAAQICRqaglvkLPTKDVhdghednfaIVFAAMGvnmETARFFKqDFEEN--GSMERV--CLFLNLANDPTIERIIT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 250 AAYATRIAEDFR-DRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTV 328
Cdd:TIGR01040 231 PRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPIL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 329 LTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISE----QHYARVRTfkQLLSSFQRNRDL 404
Cdd:TIGR01040 311 TMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrKDHSDVSN--QLYACYAIGKDV 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446135456 405 VS----VGAYAKGSDPMLdkAIALWPQLE-GYLQQGIFERADWEASLQ---GLERIFP 454
Cdd:TIGR01040 389 QAmkavVGEEALSSEDLL--YLEFLDKFEkNFIAQGPYENRTIFESLDiawQLLRIFP 444
|
|
| 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 |
6.18e-20 |
|
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: 83.26 E-value: 6.18e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446135456 384 HYARVRTFKQLLSSFQRNRDLVSVGAYAKgSDPMLDKAIALWPQLEGYLQQGIFERADWEASLQGLERIFP 454
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDA-LSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
110-427 |
6.81e-19 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 89.33 E-value: 6.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 110 LPLGPALLGRVLDGSGKPLD-GLPSP-----DTTET-GALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGLFA 182
Cdd:PTZ00185 117 IPVGAGVLGKVVNPLGHEVPvGLLTRsrallESEQTlGKVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVG 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 183 GSGVGK-SVLLGMMARYTRAD---------VIVVGLIGERGREVKDfIENILGAEGRARSVVIAAPADVSPLLRMQGAAY 252
Cdd:PTZ00185 197 DRQTGKtSIAVSTIINQVRINqqilsknavISIYVSIGQRCSNVAR-IHRLLRSYGALRYTTVMAATAAEPAGLQYLAPY 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 253 A-TRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGI--SGGGSITAFYTVL 329
Cdd:PTZ00185 276 SgVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSpgKGGGSVTALPIVE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 330 TEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFqRNRDLVSVGA 409
Cdd:PTZ00185 356 TLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAMKAVAGKLKGILAEY-RKLAADSVGG 434
|
330 340
....*....|....*....|
gi 446135456 410 YAKGSDPMLDKA--IALWPQ 427
Cdd:PTZ00185 435 SQVQTVPMIRGArfVALFNQ 454
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
111-374 |
1.62e-18 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 87.81 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 111 PLGPALLGRVLDGSGKPLDGLPSPDTTETGAL--ITPPFnpLQRTPIEHVLDTGVRPINALLTVGRGQRMgLFAGS-GVG 187
Cdd:PRK09281 98 PVGEALLGRVVNPLGQPIDGKGPIEATETRPVerKAPGV--IDRKSVHEPLQTGIKAIDAMIPIGRGQRE-LIIGDrQTG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 188 KSVLlgmmarytrA----------DVIVVGL-IGERGREVKDFIENI--LGAegRARSVVIAAPA-DVSPLLRMqgAAYA 253
Cdd:PRK09281 175 KTAI---------AidtiinqkgkDVICIYVaIGQKASTVAQVVRKLeeHGA--MEYTIVVAATAsDPAPLQYL--APYA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 254 -TRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGS--ITAFYTVLT 330
Cdd:PRK09281 242 gCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGgsLTALPIIET 321
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446135456 331 EGDDQqdpiadSAR------AILDGHIVLSRRLAEAGHYPAIDIEASISR 374
Cdd:PRK09281 322 QAGDV------SAYiptnviSITDGQIFLESDLFNAGIRPAINVGISVSR 365
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
159-367 |
3.47e-17 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 84.06 E-value: 3.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 159 LDTGVRPINALLTVGRGqrmGLFA---GSGVGKSVLLGMMARYTRADVIVVGLIGERGREV----KDFIENILGAEGRA- 230
Cdd:PRK04192 211 LITGQRVIDTFFPVAKG---GTAAipgPFGSGKTVTQHQLAKWADADIVIYVGCGERGNEMtevlEEFPELIDPKTGRPl 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 231 --RSVVIAAPADvspllrMQGAA-----Y-ATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVF 302
Cdd:PRK04192 288 meRTVLIANTSN------MPVAAreasiYtGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLA 361
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446135456 303 AKLPALVERAGNGISGGGSI---TAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAID 367
Cdd:PRK04192 362 SRLAEFYERAGRVKTLGGEEgsvTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAIN 429
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
118-374 |
5.53e-17 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 83.10 E-value: 5.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 118 GRVLDGSGKPL-----DGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGK-SVL 191
Cdd:PRK07165 81 GKIIDIDGNIIypeaqNPLSKKFLPNTSSIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKtHIA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 192 LGMMARYTRADV--IVVGlIGERGREVKDFIENILGAEGRARSVVIAAPADVS------PLLRMqgaAYATRIAEDfrdr 263
Cdd:PRK07165 161 LNTIINQKNTNVkcIYVA-IGQKRENLSRIYETLKEHDALKNTIIIDAPSTSPyeqylaPYVAM---AHAENISYN---- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 264 gQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSiTAFYTVLTEGDDQQDPIADSA 343
Cdd:PRK07165 233 -DDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNRKTI-TALPILQTVDNDITSLISSNI 310
|
250 260 270
....*....|....*....|....*....|.
gi 446135456 344 RAILDGHIVLSRRLAEAGHYPAIDIEASISR 374
Cdd:PRK07165 311 ISITDGQIVTSSDLFASGKLPAIDIDLSVSR 341
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
195-441 |
2.08e-15 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 78.91 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 195 MARYTRADVIVVGLIGERGREVKDFIENI-------LGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHV 267
Cdd:PRK14698 676 LAKWSDAQVVIYIGCGERGNEMTDVLEEFpklkdpkTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDV 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 268 LLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGG-----SITAFYTVLTEGDDQQDPIADS 342
Cdd:PRK14698 756 ALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSdyrvgSVSVIGAVSPPGGDFSEPVVQN 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 343 ARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQH------YARVRtfKQLLSSFQRNRDLVSVgAYAKGSD- 415
Cdd:PRK14698 836 TLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHknvdpeWKAMR--DKAMELLQKEAELQEI-VRIVGPDa 912
|
250 260
....*....|....*....|....*....
gi 446135456 416 -PMLDKAIALWPQL--EGYLQQGIFERAD 441
Cdd:PRK14698 913 lPERERAILLVARMlrEDYLQQDAFDEVD 941
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
28-96 |
7.38e-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: 69.26 E-value: 7.38e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 28 YGRLTRATGLVLEATGL-QLPLGATCVIERQNGTETHEVESEVVGFNGQRLFLMPLEEVEGVLPGARVYA 96
Cdd:cd01426 1 KGRVIRVNGPLVEAELEgEVAIGEVCEIERGDGNNETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEP 70
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
164-397 |
4.14e-12 |
|
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: 66.07 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 164 RPINALLTVGRGQRMGLFAGSGVGKSVLLGMMAR-----YTRADVIVVgLIGERGREVKDFIENIlGAEgrarsvVIAAP 238
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANaiaknHPEVELIVL-LIDERPEEVTDMRRSV-KGE------VVAST 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 239 ADVSPLLRMQGAAY----ATRIAEDfrdrGQHVLLIMDSLTRYAMAQREIAlaigePPATKGYPPSVFAK---LPALVER 311
Cdd:cd01128 77 FDEPPERHVQVAEMviekAKRLVEH----GKDVVILLDSITRLARAYNTVV-----PSSGKTLSGGVDANalhKPKRFFG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 312 AGNGISGGGSITAFYTVLTE-GDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRT 390
Cdd:cd01128 148 AARNIEEGGSLTIIATALVDtGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTRKEELLLTPEELQKIWL 227
|
....*..
gi 446135456 391 FKQLLSS 397
Cdd:cd01128 228 LRRILSP 234
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
146-397 |
3.08e-11 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 64.72 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 146 PFNPLQRTPIEH-VLDTGVRPINALLTVGRGQRMGLFAGSGVGKSVLL-----GMMARYTRADVIVVgLIGERGREVKDF 219
Cdd:PRK12608 103 PLHPRERLRLETgSDDLSMRVVDLVAPIGKGQRGLIVAPPRAGKTVLLqqiaaAVAANHPEVHLMVL-LIDERPEEVTDM 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 220 IENIlgaegraRSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIG-------EPP 292
Cdd:PRK12608 182 RRSV-------KGEVYASTFDRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAYNNEVESSGrtlsggvDAR 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 293 ATKGyPPSVFAklpalverAGNGISGGGSITAFYTVLTE-GDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEAS 371
Cdd:PRK12608 255 ALQR-PKRLFG--------AARNIEEGGSLTIIATALVDtGSRMDEVIFEEFKGTGNMEIVLDRELADKRVFPAIDIAKS 325
|
250 260
....*....|....*....|....*.
gi 446135456 372 ISRAMTALISEQHYARVRTFKQLLSS 397
Cdd:PRK12608 326 GTRREELLLDSKELEKVRRLRRALAS 351
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
146-396 |
4.03e-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: 64.71 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 146 PFNPLQRTPIEH-VLDTGVRPINALLTVGRGQRMGLFAGSGVGKSVLLGMMAR-----YTRADVIVVgLIGERGREVKDF 219
Cdd:TIGR00767 138 PLYPNERLRLETsTEDLSTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQaitrnHPEVELIVL-LIDERPEEVTDM 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 220 IenilgaegraRSV---VIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPpATKG 296
Cdd:TIGR00767 217 Q----------RSVkgeVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKV-LSGG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 297 YPPSVFAKlPALVERAGNGISGGGSITAFYTVLTE-GDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRA 375
Cdd:TIGR00767 286 VDANALHR-PKRFFGAARNIEEGGSLTIIATALIDtGSRMDEVIFEEFKGTGNMELHLDRKLADRRIFPAIDIKKSGTRK 364
|
250 260
....*....|....*....|.
gi 446135456 376 MTALISEQHYARVRTFKQLLS 396
Cdd:TIGR00767 365 EELLLTPEELQKIWVLRKIIS 385
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
172-397 |
4.01e-06 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 48.98 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 172 VGRGQRMGLFAGSGVGKSVLLGMMAR-----YTRADVIVVgLIGERGREVKDFienilgaegrARSV---VIAAPADVSP 243
Cdd:PRK09376 166 IGKGQRGLIVAPPKAGKTVLLQNIANsittnHPEVHLIVL-LIDERPEEVTDM----------QRSVkgeVVASTFDEPA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 244 LLRMQGAAY----ATRIAEDfrdrGQHVLLIMDSLTRYAmaqREIALAIgePPATKgyppsvfaklpalveragngisgg 319
Cdd:PRK09376 235 ERHVQVAEMviekAKRLVEH----GKDVVILLDSITRLA---RAYNTVV--PSSGK------------------------ 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135456 320 gsitafytVLTEGddqQDPIA--------DSARAILDG-------------------------------HIVLSRRLAEA 360
Cdd:PRK09376 282 --------VLSGG---VDANAlhrpkrffGAARNIEEGgsltiiatalidtgsrmdevifeefkgtgnmELHLDRKLAEK 350
|
250 260 270
....*....|....*....|....*....|....*..
gi 446135456 361 GHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSS 397
Cdd:PRK09376 351 RIFPAIDINRSGTRKEELLLSPEELQKVWILRKILSP 387
|
|
| |
