|
Name |
Accession |
Description |
Interval |
E-value |
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
7-439 |
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: 764.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 7 RLKRYLQCEYEPPRPDVEGRVTRLIGLTLEAVGLKAALGDYCLVSLQEEGSVEAEVVGFSGDRIYLMPLDSVDGLAPGAA 86
Cdd:COG1157 3 RLARLLARLEELPPVRVSGRVTRVVGLLIEAVGPDASIGELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGISPGAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 87 VRPKVGASLVPVGFGLLGRVIDGIGRPLDGKGPLRPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQRLGL 166
Cdd:COG1157 83 VVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 167 FAGSGVGKSVLLGMMTRFTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRIAEYF 246
Cdd:COG1157 163 FAGSGVGKSTLLGMIARNTEADVNVIALIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEYF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 247 RAQGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGstGGGSITAFYTVLTEGDDQQDPVA 326
Cdd:COG1157 243 RDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNG--GKGSITAFYTVLVEGDDMNDPIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 327 DSARAILDGHFVLSRSLAEQGHYPAIDIEASISRAMPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYARGSDPETDR 406
Cdd:COG1157 321 DAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENEDLIRIGAYQPGSDPELDE 400
|
410 420 430
....*....|....*....|....*....|...
gi 2197018873 407 AIDMLPAIRAYLLQGMNEPMPMQRCVQELAMVM 439
Cdd:COG1157 401 AIALIPAIEAFLRQGMDERVSFEESLAQLAELL 433
|
|
| FliI_clade1 |
TIGR03496 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
25-435 |
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: 750.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 25 GRVTRLIGLTLEAVGLKAALGDYCLVSLQEEGSVEAEVVGFSGDRIYLMPLDSVDGLAPGAAVRPKVGASLVPVGFGLLG 104
Cdd:TIGR03496 1 GRVTRVVGLVLEAVGLRAPVGSRCEIESSDGDPIEAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLGGPLRLPVGDSLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 105 RVIDGIGRPLDGKGPLRPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGKSVLLGMMTRF 184
Cdd:TIGR03496 81 RVIDGLGRPLDGKGPLDAGERVPLYAPPINPLKRAPIDEPLDVGVRAINGLLTVGRGQRMGIFAGSGVGKSTLLGMMARY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 185 TEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQGKNVLLLMDSLTRYA 264
Cdd:TIGR03496 161 TEADVVVVGLIGERGREVKEFIEDILGEEGLARSVVVAATADESPLMRLRAAFYATAIAEYFRDQGKDVLLLMDSLTRFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 265 QAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGSTGGGSITAFYTVLTEGDDQQDPVADSARAILDGHFVLSRSLA 344
Cdd:TIGR03496 241 MAQREIALAIGEPPATKGYPPSVFAKLPQLVERAGNGEEGKGSITAFYTVLVEGDDQQDPIADAARAILDGHIVLSRELA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 345 EQGHYPAIDIEASISRAMPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYARGSDPETDRAIDMLPAIRAYLLQGMNE 424
Cdd:TIGR03496 321 EQGHYPAIDILASISRVMPDVVSPEHRQAARRFKQLLSRYQENRDLISIGAYQAGSDPELDQAIALYPRIEAFLQQGMRE 400
|
410
....*....|.
gi 2197018873 425 PMPMQRCVQEL 435
Cdd:TIGR03496 401 RASFEESLEAL 411
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
6-439 |
0e+00 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 719.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 6 QRLKRYLQCEYEPPRPDVEGRVTRLIGLTLEAVGLKAALGDYCLVSLQE---EGSVEAEVVGFSGDRIYLMPLDSVDGLA 82
Cdd:PRK05688 10 KRLEGYAEAISLPAQPVVEGRLLRMVGLTLEAEGLRAAVGSRCLVINDDsyhPVQVEAEVMGFSGDKVFLMPVGSVAGIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 83 PGAAVRPKVGASLVPVGFGLLGRVIDGIGRPLDGKGPLRPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQ 162
Cdd:PRK05688 90 PGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 163 RLGLFAGSGVGKSVLLGMMTRFTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRI 242
Cdd:PRK05688 170 RLGLFAGTGVGKSVLLGMMTRFTEADIIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 243 AEYFRAQGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGSTGGGSITAFYTVLTEGDDQQ 322
Cdd:PRK05688 250 AEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITAFYTVLSEGDDQQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 323 DPVADSARAILDGHFVLSRSLAEQGHYPAIDIEASISRAMPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYARGSDP 402
Cdd:PRK05688 330 DPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQSRDLISVGAYVAGGDP 409
|
410 420 430
....*....|....*....|....*....|....*..
gi 2197018873 403 ETDRAIDMLPAIRAYLLQGMNEPMPMQRCVQELAMVM 439
Cdd:PRK05688 410 ETDLAIARFPHLVQFLRQGLRENVSLAQSREQLAAIF 446
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
1-440 |
0e+00 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 688.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 1 MPDLDQRLKRYLQcEYEPPRPDVEGRVTRLIGLTLEAVGLKAALGDYCLVSLQEeGSVEAEVVGFSGDRIYLMPLDSVDG 80
Cdd:PRK08972 4 QHQLLNRLKQYKV-KVPPFRAVASGKLVRVVGLTLEATGCRAPVGSLCSIETMA-GELEAEVVGFDGDLLYLMPIEELRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 81 LAPGAAVRPKVGASLVPVGFGLLGRVIDGIGRPLDGKGPLRPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGR 160
Cdd:PRK08972 82 VLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 161 GQRLGLFAGSGVGKSVLLGMMTRFTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTT 240
Cdd:PRK08972 162 GQRMGLFAGSGVGKSVLLGMMTRGTTADVIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCETAT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 241 RIAEYFRAQGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGSTGGGSITAFYTVLTEGDD 320
Cdd:PRK08972 242 TIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSITAFYTVLTEGDD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 321 QQDPVADSARAILDGHFVLSRSLAEQGHYPAIDIEASISRAMPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYARGS 400
Cdd:PRK08972 322 LQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLYQQNRDLISIGAYKQGS 401
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2197018873 401 DPETDRAIDMLPAIRAYLLQGMNEPMPMQRCVQELAMVMS 440
Cdd:PRK08972 402 DPRIDNAIRLQPAMNAFLQQTMKEAVPYDMSVNMLKQLAA 441
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
1-440 |
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: 585.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 1 MPDLDQRLKRYLQCEYEPPRPDVEGRVTRLIGLTLEAVGLKAALGDYCLVSLQ-EEGSVEAEVVGFSGDRIYLMPLDSVD 79
Cdd:TIGR01026 1 MERNLTTFYNRLCQEMDLRLVKRVGRVTKVKGLLIEAVGPQASVGDLCLIERRgSEGRLVAEVVGFNGEFVFLMPYEEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 80 GLAPGAAVRPKVGASLVPVGFGLLGRVIDGIGRPLDGKG-PLRPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTV 158
Cdd:TIGR01026 81 GVRPGSKVLATGEGLSIKVGDGLLGRVLDGLGKPIDGKGkFLDNVETEGLITAPINPLKRAPIREILSTGVRSIDGLLTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 159 GRGQRLGLFAGSGVGKSVLLGMMTRFTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQL 238
Cdd:TIGR01026 161 GKGQRIGIFAGSGVGKSTLLGMIARNTEADVNVIALIGERGREVREFIEHDLGEEGLKRSVVVVATSDQSPLLRLKGAYV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 239 TTRIAEYFRAQGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAgnGSTGGGSITAFYTVLTEG 318
Cdd:TIGR01026 241 ATAIAEYFRDQGKDVLLLMDSVTRFAMAQREIGLAAGEPPATKGYTPSVFSTLPRLLERA--GASGKGSITAFYTVLVEG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 319 DDQQDPVADSARAILDGHFVLSRSLAEQGHYPAIDIEASISRAMPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYAR 398
Cdd:TIGR01026 319 DDMNEPIADSVRGILDGHIVLSRALAQRGHYPAIDVLASISRLMTAIVSEEHRRAARKFRELLSKYKDNEDLIRIGAYQR 398
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2197018873 399 GSDPETDRAIDMLPAIRAYLLQGMNEPMPMQRCVQELAMVMS 440
Cdd:TIGR01026 399 GSDRELDFAIAKYPKLERFLKQGINEKVNFEESLQQLEEIFR 440
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
25-435 |
0e+00 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 584.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 25 GRVTRLIGLTLEAVGLKAALGDYCLVSLQEEGS---VEAEVVGFSGDRIYLMPLDSVDGLAPGAAV-------RPKVGAS 94
Cdd:PRK07960 29 GRLTRATGLVLEATGLQLPLGATCVIERQNGSEtheVESEVVGFNGQRLFLMPLEEVEGILPGARVyarnisgEGLQSGK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 95 LVPVGFGLLGRVIDGIGRPLDGKGPLRPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGK 174
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 175 SVLLGMMTRFTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQGKNVL 254
Cdd:PRK07960 189 SVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 255 LLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGSTGGGSITAFYTVLTEGDDQQDPVADSARAILD 334
Cdd:PRK07960 269 LIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARAILD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 335 GHFVLSRSLAEQGHYPAIDIEASISRAMPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYARGSDPETDRAIDMLPAI 414
Cdd:PRK07960 349 GHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAIALWPQL 428
|
410 420
....*....|....*....|.
gi 2197018873 415 RAYLLQGMNEPMPMQRCVQEL 435
Cdd:PRK07960 429 EAFLQQGIFERADWEDSLQAL 449
|
|
| FliI_clade2 |
TIGR03497 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
25-436 |
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: 578.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 25 GRVTRLIGLTLEAVGLKAALGDYCLVSLQEEGSVEAEVVGFSGDRIYLMPLDSVDGLAPGAAVRPkVGASL-VPVGFGLL 103
Cdd:TIGR03497 1 GKVTRVIGLTIESKGPKASIGELCSILTKGGKPVLAEVVGFKEENVLLMPLGEVEGIGPGSLVIA-TGRPLaIKVGKGLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 104 GRVIDGIGRPLDGKGPLRPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGKSVLLGMMTR 183
Cdd:TIGR03497 80 GRVLDGLGRPLDGEGPIIGEEPYPLDNPPPNPLKRPRIRDPLETGIKAIDGLLTIGKGQRVGIFAGSGVGKSTLLGMIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 184 FTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQGKNVLLLMDSLTRY 263
Cdd:TIGR03497 160 NAKADINVIALIGERGREVRDFIEKDLGEEGLKRSVVVVATSDQPALMRLKAAFTATAIAEYFRDQGKDVLLMMDSVTRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 264 AQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNgsTGGGSITAFYTVLTEGDDQQDPVADSARAILDGHFVLSRSL 343
Cdd:TIGR03497 240 AMAQREIGLAVGEPPTTRGYTPSVFSLLPKLLERSGN--SQKGSITGFYTVLVDGDDMNEPIADAVRGILDGHIVLSREL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 344 AEQGHYPAIDIEASISRAMPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYARGSDPETDRAIDMLPAIRAYLLQGMN 423
Cdd:TIGR03497 318 AAKNHYPAIDVLASVSRVMNEIVSEEHKELAGKLRELLAVYKEAEDLINIGAYKRGSNPKIDEAIRYIEKINSFLKQGID 397
|
410
....*....|...
gi 2197018873 424 EPMPMQRCVQELA 436
Cdd:TIGR03497 398 EKFTFEETVQLLK 410
|
|
| FliI_clade3 |
TIGR03498 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
25-439 |
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.
Pssm-ID: 163293 [Multi-domain] Cd Length: 418 Bit Score: 539.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 25 GRVTRLIGLTLEAVGLKAA--LGDYCLVSLQEEGSVEAEVVGFSGDRIYLMPLDSVDGLAPGAAVRPKVGASLVPVGFGL 102
Cdd:TIGR03498 1 GRVTAVTGLLIEVRGLSRAvrLGDRCAIRARDGRPVLAEVVGFNGDRVLLMPFEPLEGVGLGCAVFAREGPLAVRPHPSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 103 LGRVIDGIGRPLDGKGPL-RPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGKSVLLGMM 181
Cdd:TIGR03498 81 LGRVINALGEPIDGKGPLpQGERRYPLRASPPPAMSRARVGEPLDTGVRVIDTFLPLCRGQRLGIFAGSGVGKSTLLSML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 182 TRFTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQGKNVLLLMDSLT 261
Cdd:TIGR03498 161 ARNTDADVVVIALVGERGREVREFLEDDLGEEGLKRSVVVVATSDESPLMRRQAAYTATAIAEYFRDQGKDVLLLMDSVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 262 RYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGSTGGGSITAFYTVLTEGDDQQDPVADSARAILDGHFVLSR 341
Cdd:TIGR03498 241 RFAMAQREIGLAAGEPPVARGYTPSVFSELPRLLERAGPGAEGKGSITGIFTVLVDGDDHNEPVADAVRGILDGHIVLDR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 342 SLAEQGHYPAIDIEASISRAMPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYARGSDPETDRAIDMLPAIRAYLLQG 421
Cdd:TIGR03498 321 AIAERGRYPAINVLASVSRLAPRVWSPEERKLVRRLRALLARYEETEDLIRLGAYRKGSDPELDEAIRLVPKIYEFLTQG 400
|
410
....*....|....*...
gi 2197018873 422 MNEPMPMQRCVQELAMVM 439
Cdd:TIGR03498 401 PDEPTSLQDPFADLAAIL 418
|
|
| III_secr_ATP |
TIGR02546 |
type III secretion apparatus H+-transporting two-sector ATPase; [Protein fate, Protein and ... |
23-436 |
0e+00 |
|
type III secretion apparatus H+-transporting two-sector ATPase; [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274191 [Multi-domain] Cd Length: 422 Bit Score: 536.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 23 VEGRVTRLIGLTLEAVGLKAALGDYCLVSLQEEGSVEAEVVGFSGDRIYLMPLDSVDGLAPGAAVRPKVGASLVPVGFGL 102
Cdd:TIGR02546 5 VRGRVTEVSGTLLKAVLPGARVGELCLIRRRDPSQLLAEVVGFTGDEALLSPLGELHGISPGSEVIPTGRPLSIRVGEAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 103 LGRVIDGIGRPLDGKGPLRPD--DMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGKSVLLGM 180
Cdd:TIGR02546 85 LGRVLDGFGRPLDGKGELPAGeiETRPLDADPPPPMSRQPIDQPLPTGVRAIDGLLTCGEGQRIGIFAGAGVGKSTLLGM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 181 MTRFTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQGKNVLLLMDSL 260
Cdd:TIGR02546 165 IARGASADVNVIALIGERGREVREFIEHHLGEEGRKRSVLVVSTSDRPSLERLKAAYTATAIAEYFRDQGKRVLLMMDSL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 261 TRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGSTggGSITAFYTVLTEGDDQQDPVADSARAILDGHFVLS 340
Cdd:TIGR02546 245 TRFARALREIGLAAGEPPARGGYPPSVFSSLPRLLERAGNGEK--GSITALYTVLVEGDDMNDPIADEVRSILDGHIVLS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 341 RSLAEQGHYPAIDIEASISRAMPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYARGSDPETDRAIDMLPAIRAYLLQ 420
Cdd:TIGR02546 323 RALAERNHYPAIDVLASLSRVMSQVVSTEHRRAAGKLRRLLATYKEVELLIRLGEYQPGSDPETDDAIDKIDAIRAFLRQ 402
|
410
....*....|....*.
gi 2197018873 421 GMNEPMPMQRCVQELA 436
Cdd:TIGR02546 403 STDEYSPYEETLEQLH 418
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
25-435 |
0e+00 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 514.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 25 GRVTRLIGLTLEAVGLKAALGDYCLVSLQEEG--SVEAEVVGFSGDRIYLMPLDSVDGLAPGAAVRpKVGASL-VPVGFG 101
Cdd:PRK07721 20 GKVSRVIGLMIESKGPESSIGDVCYIHTKGGGdkAIKAEVVGFKDEHVLLMPYTEVAEIAPGCLVE-ATGKPLeVKVGSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 102 LLGRVIDGIGRPLDGKgPLRPDDM-VTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGKSVLLGM 180
Cdd:PRK07721 99 LIGQVLDALGEPLDGS-ALPKGLApVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 181 MTRFTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQGKNVLLLMDSL 260
Cdd:PRK07721 178 IARNTSADLNVIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 261 TRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAgnGSTGGGSITAFYTVLTEGDDQQDPVADSARAILDGHFVLS 340
Cdd:PRK07721 258 TRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERT--GTNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLD 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 341 RSLAEQGHYPAIDIEASISRAMPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYARGSDPETDRAIDMLPAIRAYLLQ 420
Cdd:PRK07721 336 RQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLINIGAYKRGSSREIDEAIQFYPQIISFLKQ 415
|
410
....*....|....*
gi 2197018873 421 GMNEPMPMQRCVQEL 435
Cdd:PRK07721 416 GTDEKATFEESIQAL 430
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
19-435 |
8.02e-179 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 507.12 E-value: 8.02e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 19 PRPDVEGRVTRLIGLTLEAVGLKAALGDYCLVSLQEEGSVEAEVVGFSGDRIYLMPLDSVDGLAPGAAVRPKVGASLVPV 98
Cdd:PRK07196 13 HLARVAGRLVRVTGLLLESVGCRLAIGQRCRIESVDETFIEAQVVGFDRDITYLMPFKHPGGVLGGARVFPSEQDGELLI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 99 GFGLLGRVIDGIGRPLDGKGPLRPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGKSVLL 178
Cdd:PRK07196 93 GDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 179 GMMTRFTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQGKNVLLLMD 258
Cdd:PRK07196 173 GMITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 259 SLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGStGGGSITAFYTVLTEGDDQQDPVADSARAILDGHFV 338
Cdd:PRK07196 253 SLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSS-GNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 339 LSRSLAEQGHYPAIDIEASISRAMPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYARGSDPETDRAIDMLPAIRAYL 418
Cdd:PRK07196 332 LSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVAGADPMADQAVHYYPAITQFL 411
|
410
....*....|....*..
gi 2197018873 419 LQGMNEPMPMQRCVQEL 435
Cdd:PRK07196 412 RQEVGHPALFSASVEQL 428
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
19-440 |
2.11e-177 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 503.74 E-value: 2.11e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 19 PRPDVEGRVTRLIGLTLEAVGLKAAL--GDYCLVSLQEEGSVEAEVVGFSGDRIYLMPLDSVDGLAPGAAVRPKVGASLV 96
Cdd:PRK08927 13 DTLVIYGRVVAVRGLLVEVAGPIHALsvGARIVVETRGGRPVPCEVVGFRGDRALLMPFGPLEGVRRGCRAVIANAAAAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 97 PVGFGLLGRVIDGIGRPLDGKGPLRPddmvtlhGETINPLHRHP--------IEQTLDVGVRAINGLLTVGRGQRLGLFA 168
Cdd:PRK08927 93 RPSRAWLGRVVNALGEPIDGKGPLPQ-------GPVPYPLRAPPppahsrarVGEPLDLGVRALNTFLTCCRGQRMGIFA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 169 GSGVGKSVLLGMMTRFTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFRA 248
Cdd:PRK08927 166 GSGVGKSVLLSMLARNADADVSVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 249 QGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGSTGGGSITAFYTVLTEGDDQQDPVADS 328
Cdd:PRK08927 246 QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGEGTITGLFTVLVDGDDHNEPVADA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 329 ARAILDGHFVLSRSLAEQGHYPAIDIEASISRAMPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYARGSDPETDRAI 408
Cdd:PRK08927 326 VRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLGAYRAGSDPEVDEAI 405
|
410 420 430
....*....|....*....|....*....|..
gi 2197018873 409 DMLPAIRAYLLQGMNEPMPMQRCVQELAMVMS 440
Cdd:PRK08927 406 RLNPALEAFLRQGKDEATSLAEGYARLAQILG 437
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
25-439 |
5.36e-159 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 456.84 E-value: 5.36e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 25 GRVTRLIGLTLEAVGLKAALGD-YCLVSLQEEGSVEAEVVGFSGDRIYLMPLDSVDGLAPGAAVRPKVGASLVPVGFGLL 103
Cdd:PRK08472 20 GSITKISPTIIEADGLNPSVGDiVKIESSDNGKECLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 104 GRVIDGIGRPLDGKGPLRPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGKSVLLGMMTR 183
Cdd:PRK08472 100 GRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 184 FTEAEITVVGLIGERGREVREFIDHSLGAEgMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQGKNVLLLMDSLTRY 263
Cdd:PRK08472 180 GCLAPIKVVALIGERGREIPEFIEKNLGGD-LENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 264 AQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNgSTGGGSITAFYTVLTEGDDQQDPVADSARAILDGHFVLSRSL 343
Cdd:PRK08472 259 AMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK-EEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSREL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 344 AEQGHYPAIDIEASISRAMPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYARGSDPETDRAIDMLPAIRAYLLQGMN 423
Cdd:PRK08472 338 TDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAYQKGNDKELDEAISKKEFMEQFLKQNPN 417
|
410
....*....|....*.
gi 2197018873 424 EPMPMQRCVQELAMVM 439
Cdd:PRK08472 418 ELFPFEQTFEQLEEIL 433
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
96-360 |
1.16e-158 |
|
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: 449.32 E-value: 1.16e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 96 VPVGFGLLGRVIDGIGRPLDGKGPLRPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGKS 175
Cdd:cd01136 2 IPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 176 VLLGMMTRFTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQGKNVLL 255
Cdd:cd01136 82 TLLGMIARNTDADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 256 LMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGSTggGSITAFYTVLTEGDDQQDPVADSARAILDG 335
Cdd:cd01136 162 LMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEK--GSITAFYTVLVEGDDFNDPIADEVRSILDG 239
|
250 260
....*....|....*....|....*
gi 2197018873 336 HFVLSRSLAEQGHYPAIDIEASISR 360
Cdd:cd01136 240 HIVLSRRLAERGHYPAIDVLASISR 264
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
23-436 |
7.61e-158 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 454.21 E-value: 7.61e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 23 VEGRVTRLIGLTLEAVGLKAALGDYC-LVSLQEEGSVEAEVVGFSGDRIYLMPLDSVDGLAPGAAVRPKVGASLVPVGFG 101
Cdd:PRK06936 23 IRGRVTQVTGTILKAVVPGVRIGELCyLRNPDNSLSLQAEVIGFAQHQALLTPLGEMYGISSNTEVSPTGTMHQVGVGEH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 102 LLGRVIDGIGRPLDGKGPLRPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGKSVLLGMM 181
Cdd:PRK06936 103 LLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 182 TRFTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQGKNVLLLMDSLT 261
Cdd:PRK06936 183 IRSAEVDVTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 262 RYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGSTggGSITAFYTVLTEGDDQQDPVADSARAILDGHFVLSR 341
Cdd:PRK06936 263 RFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDK--GSITALYTVLVEGDDMTEPVADETRSILDGHIILSR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 342 SLAEQGHYPAIDIEASISRAMPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYARGSDPETDRAIDMLPAIRAYLLQG 421
Cdd:PRK06936 341 KLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIGEYQKGQDKEADQAIERIGAIRGFLRQG 420
|
410
....*....|....*
gi 2197018873 422 MNEPMPMQRCVQELA 436
Cdd:PRK06936 421 THELSHFNETLNLLE 435
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
3-440 |
2.93e-155 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 447.34 E-value: 2.93e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 3 DLDQRLKRYLQCEYEPPRPDV-EGRVTRlIGLTLEAVGLK-AALGDYCLVslqEEGSVEAEVVGFSGDRIYLMPLDSVDG 80
Cdd:PRK06820 8 RLTPRLQQQLTRPSAPPEGLRyRGPIVE-IGPTLLRASLPgVAQGELCRI---EPQGMLAEVVSIEQEMALLSPFASSDG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 81 LAPGAAVRPKVGASLVPVGFGLLGRVIDGIGRPLDGkGPLRPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGR 160
Cdd:PRK06820 84 LRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 161 GQRLGLFAGSGVGKSVLLGMMTRFTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTT 240
Cdd:PRK06820 163 GQRIGIFAAAGVGKSTLLGMLCADSAADVMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 241 RIAEYFRAQGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGSTggGSITAFYTVLTEGDD 320
Cdd:PRK06820 243 TIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDR--GSITAFYTVLVEGDD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 321 QQDPVADSARAILDGHFVLSRSLAEQGHYPAIDIEASISRAMPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYARGS 400
Cdd:PRK06820 321 MNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGEYQAGE 400
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2197018873 401 DPETDRAIDMLPAIRAYLLQGMNEPMPMQRCVQELAMVMS 440
Cdd:PRK06820 401 DLQADEALQRYPAICAFLQQDHSETAHLETTLEHLAQVVG 440
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
25-436 |
9.89e-142 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 413.01 E-value: 9.89e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 25 GRVTRLIGLTLEAVGLKAALGDYCLVsLQEEGSV--EAEVVGFSGDRIYLMPLDSVDGLAPGAAVRPKVGASLVPVGFGL 102
Cdd:PRK09099 26 GKVVEVIGTLLRVSGLDVTLGELCEL-RQRDGTLlqRAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVGPAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 103 LGRVIDGIGRPLDGKGPLRPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGKSVLLGMMT 182
Cdd:PRK09099 105 LGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 183 RFTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQGKNVLLLMDSLTR 262
Cdd:PRK09099 185 RGTQCDVNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 263 YAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGSTggGSITAFYTVLTEGDDQQDPVADSARAILDGHFVLSRS 342
Cdd:PRK09099 265 FARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGET--GSITALYTVLAEDESGSDPIAEEVRGILDGHMILSRE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 343 LAEQGHYPAIDIEASISRAMPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYARGSDPETDRAIDMLPAIRAYLLQGM 422
Cdd:PRK09099 343 IAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVGEYRAGSDPVADEAIAKIDAIRDFLSQRT 422
|
410
....*....|....
gi 2197018873 423 NEPMPMQRCVQELA 436
Cdd:PRK09099 423 DEYSDPDATLAALA 436
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
28-435 |
6.46e-132 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 387.43 E-value: 6.46e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 28 TRLIGLTLEAVGLKAALGDYCLV--SLQEEGSV-EAEVVGFSGDRIYLMPLDSVDGLAPGAAVRPKVGASLVPVGFGLLG 104
Cdd:PRK08149 11 LRIQGPIIEAELPDVAIGEICEIraGWHSNEVIaRAQVVGFQRERTILSLIGNAQGLSRQVVLKPTGKPLSVWVGEALLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 105 RVIDGIGRPLDGKGPLRPDDMVTLHGETINP----LHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGKSVLLGM 180
Cdd:PRK08149 91 AVLDPTGKIVERFDAPPTVGPISEERVIDVAppsyAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 181 MTRFTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQGKNVLLLMDSL 260
Cdd:PRK08149 171 LIEHSEADVFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 261 TRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNgsTGGGSITAFYTVLTEGDDQQDPVADSARAILDGHFVLS 340
Cdd:PRK08149 251 TRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGA--TLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 341 RSLAEQGHYPAIDIEASISRAMPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYARGSDPETDRAIDMLPAIRAYLLQ 420
Cdd:PRK08149 329 RKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGEYRRGENADNDRAMDKRPALEAFLKQ 408
|
410
....*....|....*
gi 2197018873 421 GMNEPMPMQRCVQEL 435
Cdd:PRK08149 409 DVAEKSSFSDTLERL 423
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
4-440 |
9.38e-130 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 382.38 E-value: 9.38e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 4 LDQRLKRYLQCEYEPPrpDVEGRVTRL--IGLTLEAVGLKAA-LGDYCLVSLQEEgsvEAEVVGFSGDRIYLMPLDSVDG 80
Cdd:PRK07594 1 MKNELMQRLRLKYPPP--DGYCRWGRIqdVSATLLNAWLPGVfMGELCCIKPGEE---LAEVVGINGSKALLSPFTSTIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 81 LAPGAAVRPKVGASLVPVGFGLLGRVIDGIGRPLDGkgplRPDDMVT---LHGETINPLHRHPIEQTLDVGVRAINGLLT 157
Cdd:PRK07594 76 LHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDG----RELPDVCwkdYDAMPPPAMVRQPITQPLMTGIRAIDSVAT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 158 VGRGQRLGLFAGSGVGKSVLLGMMTRFTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQ 237
Cdd:PRK07594 152 CGEGQRVGIFSAPGVGKSTLLAMLCNAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 238 LTTRIAEYFRAQGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGSTggGSITAFYTVLTE 317
Cdd:PRK07594 232 VATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEK--GSITAFYTVLVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 318 GDDQQDPVADSARAILDGHFVLSRSLAEQGHYPAIDIEASISRAMPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYA 397
Cdd:PRK07594 310 GDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEYQ 389
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2197018873 398 RGSDPETDRAIDMLPAIRAYLLQGMNEPMPMQRCVQELAMVMS 440
Cdd:PRK07594 390 RGVDTDTDKAIDTYPDICTFLRQSKDEVCGPELLIEKLHQILT 432
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
44-436 |
5.25e-128 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 378.57 E-value: 5.25e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 44 LGDycLVSLQEEGSVE-AEVVGFSGDRIYLMPLDSVDGLAPGAAVRPKVGASLVPVGfGLLGRVIDGIGRPLDGKGPLRP 122
Cdd:PRK06002 49 LGD--FVAIRADGGTHlGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKGPLRIRPDP-SWKGRVINALGEPIDGLGPLAP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 123 -DDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGKSVLLGMMTRFTEAEITVVGLIGERGRE 201
Cdd:PRK06002 126 gTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGRE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 202 VREFIDHSLGAEgMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQGKNVLLLMDSLTRYAQAQREIALAVGEPPATK 281
Cdd:PRK06002 206 VREFLEDTLADN-LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVAR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 282 GYPPSVFAKLPKLVERAGNGSTGGGSITAFYTVLTEGDDQQDPVADSARAILDGHFVLSRSLAEQGHYPAIDIEASISRA 361
Cdd:PRK06002 285 GYPPSVFSELPRLLERAGPGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRL 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2197018873 362 MPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYARGSDPETDRAIDMLPAIRAYLLQGMNEPmPMQRCVQELA 436
Cdd:PRK06002 365 ARHAWTPEQRKLVSRLKSMIARFEETRDLRLIGGYRAGSDPDLDQAVDLVPRIYEALRQSPGDP-PSDDAFADLA 438
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
148-359 |
6.25e-125 |
|
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: 361.67 E-value: 6.25e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 148 GVRAINGLLTVGRGQRLGLFAGSGVGKSVLLGMMTRFTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADD 227
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLGSGALKRTVVVVATSDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 228 SPLMRLRAAQLTTRIAEYFRAQGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGSTGGGS 307
Cdd:pfam00006 81 PPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKGKGGS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2197018873 308 ITAFYTVLTEGDDQQDPVADSARAILDGHFVLSRSLAEQGHYPAIDIEASIS 359
Cdd:pfam00006 161 ITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
96-361 |
2.74e-110 |
|
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: 326.72 E-value: 2.74e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 96 VPVGFGLLGRVIDGIGRPLDGKGPLRPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGKS 175
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 176 VLLGMMTRFT---EAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQGKN 252
Cdd:cd19476 82 VLAMQLARNQakaHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 253 VLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGSTGGGSITAFYTVLTEGDDQQDPVADSARAI 332
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTPGDDLTDPIPDNTFAI 241
|
250 260
....*....|....*....|....*....
gi 2197018873 333 LDGHFVLSRSLAEQGHYPAIDIEASISRA 361
Cdd:cd19476 242 LDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
39-435 |
3.59e-106 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 321.93 E-value: 3.59e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 39 GLKAALGDYCLVSlqeEGSVEAEVVGFSGDRIYLMPLDSVDGLAPGAAVRPKVGASLVPVGFGLLGRVIDGIGRPLDGKG 118
Cdd:PRK06793 37 GPKAKIGDVCFVG---EHNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 119 PLRPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGKSVLLGMMTRFTEAEITVVGLIGER 198
Cdd:PRK06793 114 ENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGER 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 199 GREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQGKNVLLLMDSLTRYAQAQREIALAVGEPP 278
Cdd:PRK06793 194 GREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 279 aTKGYPPSVFAKLPKLVERAGNgsTGGGSITAFYTVLTEGDDQQDPVADSARAILDGHFVLSRSLAEQGHYPAIDIEASI 358
Cdd:PRK06793 274 -IGGKTLLMESYMKKLLERSGK--TQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 359 SRAMPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYARGSDP----ETDRAIDmlpAIRAYLLQGMNEPMPMQRCVQE 434
Cdd:PRK06793 351 SRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGTIQENAENayifECKNKVE---GINTFLKQGRSDSFQFDDIVEA 427
|
.
gi 2197018873 435 L 435
Cdd:PRK06793 428 M 428
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
25-435 |
2.85e-97 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 299.13 E-value: 2.85e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 25 GRVTRLIGLTLEAVGLKAALGDYCLVSLQEEGSVEAEVVGFSGDRIYLMPLDSVDGLAPGAAVRPKVGASLVPVGFGLLG 104
Cdd:PRK05922 21 GLLSRVSGNLLEAQGLSACLGELCQISLSKSPPILAEVIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDHLLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 105 RVIDGIGRPLDGKGPLRPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGKSVLLGMMTRF 184
Cdd:PRK05922 101 RVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 185 TEAEITVVGLIGERGREVREFIDHSlgAEGMA--RSVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQGKNVLLLMDSLTR 262
Cdd:PRK05922 181 SKSTINVIALIGERGREVREYIEQH--KEGLAaqRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 263 YAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGSTggGSITAFYTVLTEGdDQQDPVADSARAILDGHFVLS-- 340
Cdd:PRK05922 259 WIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDK--GSITALYAILHYP-NHPDIFTDYLKSLLDGHFFLTpq 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 341 -RSLAEqghyPAIDIEASISRAMPQIVDPQRLNLALQFKRLYSRYQQNADLIAVGAYARGSDPETDRAIDMLPAIRAYLL 419
Cdd:PRK05922 336 gKALAS----PPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGAYVPGQDAHLDRAVKLLPSIKQFLS 411
|
410
....*....|....*.
gi 2197018873 420 QGMNEPMPMQRCVQEL 435
Cdd:PRK05922 412 QPLSSYCALHNTLKQL 427
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
24-393 |
3.56e-52 |
|
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: 182.23 E-value: 3.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 24 EGRVTRLIGLTLEAV---GLKAALGDYCLVSLQEEGSVEAEVVGFSGD-RIYLMPLDSVDGLAPGAAVRPKVGASLVPVG 99
Cdd:TIGR01039 2 KGKVVQVIGPVVDVEfeqGELPRIYNALKVQNRAESELTLEVAQHLGDdTVRTIAMGSTDGLVRGLEVIDTGAPISVPVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 100 FGLLGRVIDGIGRPLDGKGPLRPDdmvtlhgeTINPLHRHP---IEQT-----LDVGVRAINGLLTVGRGQRLGLFAGSG 171
Cdd:TIGR01039 82 KETLGRIFNVLGEPIDEKGPIPAK--------ERWPIHRKApsfEEQStkveiLETGIKVIDLLAPYAKGGKIGLFGGAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 172 VGKSVLLGMMTRFTEAE---ITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFR- 247
Cdd:TIGR01039 154 VGKTVLIQELINNIAKEhggYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRd 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 248 AQGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAgnGSTGGGSITAFYTVLTEGDDQQDPVAD 327
Cdd:TIGR01039 234 EQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERI--TSTKTGSITSVQAVYVPADDLTDPAPA 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2197018873 328 SARAILDGHFVLSRSLAEQGHYPAIDIEASISRAM-PQIVDPQRLNLALQFKRLYSRYQQNADLIAV 393
Cdd:TIGR01039 312 TTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLdPSVVGEEHYDVARGVQQILQRYKELQDIIAI 378
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
96-362 |
5.76e-48 |
|
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: 166.24 E-value: 5.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 96 VPVGFGLLGRVIDGIGRPLDGKGPLRPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGKS 175
Cdd:cd01135 4 LPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLPHN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 176 VLLGMMTR------FTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFR-A 248
Cdd:cd01135 84 ELAAQIARqagvvgSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYLAyE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 249 QGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGSTGGGSITAFyTVLT-EGDDQQDPVAD 327
Cdd:cd01135 164 KGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQI-PILTmPNDDITHPIPD 242
|
250 260 270
....*....|....*....|....*....|....*
gi 2197018873 328 SARAILDGHFVLSRSLAEQGHYPAIDIEASISRAM 362
Cdd:cd01135 243 LTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLM 277
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
4-438 |
6.93e-47 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 168.94 E-value: 6.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 4 LDQRLKRYlqceyePPRPDVE--GRVTRlIGLTLEAV-GL-KAALGDyclvSLQEEGSVEAEVVGFSGDRIYLMPLDSVD 79
Cdd:PRK13343 12 IRQRIARY------EPQPDAReiGRVES-VGDGIAFVsGLpDAALDE----LLRFEGGSRGFAFNLEEELVGAVLLDDTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 80 GLAPGAAVRPkVGASL-VPVGFGLLGRVIDGIGRPLDGKGPLRPDDMVTLhgETINP--LHRHPIEQTLDVGVRAINGLL 156
Cdd:PRK13343 81 DILAGTEVRR-TGRVLeVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPL--ERPAPaiIERDFVTEPLQTGIKVVDALI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 157 TVGRGQRLGLFAGSGVGKSVLL--GMMTRFTEAEITVVGLIGERGREVREFID--HSLGAegMARSVVVAAPADDSPLMR 232
Cdd:PRK13343 158 PIGRGQRELIIGDRQTGKTAIAidAIINQKDSDVICVYVAIGQKASAVARVIEtlREHGA--LEYTTVVVAEASDPPGLQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 233 LRAAQLTTRIAEYFRAQGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAG--NGSTGGGSITA 310
Cdd:PRK13343 236 YLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAklSPELGGGSLTA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 311 FYTVLTEGDDQQDPVADSARAILDGHFVLSRSLAEQGHYPAIDIEASISR--------AMPQIVDPQRLNLAlQFKRLYS 382
Cdd:PRK13343 316 LPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRvggkaqhpAIRKESGRLRLDYA-QFLELEA 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2197018873 383 RYQQNADLiavgayargsDPETDRAIDMLPAIRAYLLQGMNEPMPMqrcVQELAMV 438
Cdd:PRK13343 395 FTRFGGLL----------DAGTQKQITRGRRLRELLKQPRFSPLSV---EEQIALL 437
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
96-362 |
1.36e-44 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 161.92 E-value: 1.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 96 VPVGFGLLGRVIDGIGRPLDGKGPLRPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGKS 175
Cdd:PRK04196 78 LPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 176 VLLGMMTR-----FTEAEITVV-GLIGERGREVREFID--HSLGAegMARSVVVAAPADDSPLMRL---RAAqLTTriAE 244
Cdd:PRK04196 158 ELAAQIARqakvlGEEENFAVVfAAMGITFEEANFFMEdfEETGA--LERSVVFLNLADDPAIERIltpRMA-LTA--AE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 245 Y--FRaQGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGSTGGGSITAFyTVLT-EGDDQ 321
Cdd:PRK04196 233 YlaFE-KGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQI-PILTmPDDDI 310
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2197018873 322 QDPVADSARAILDGHFVLSRSLAEQGHYPAIDIEASISRAM 362
Cdd:PRK04196 311 THPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLM 351
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
25-392 |
1.69e-44 |
|
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: 161.80 E-value: 1.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 25 GRVTRLIGLTLEAV-------GLKAALgdycLVSLQEEGSVEAEVVGFSGDRIY-LMPLDSVDGLAPGAAVRPKVGASLV 96
Cdd:COG0055 6 GKIVQVIGPVVDVEfpegelpAIYNAL----EVENEGGGELVLEVAQHLGDNTVrCIAMDSTDGLVRGMEVIDTGAPISV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 97 PVGFGLLGRVIDGIGRPLDGKGPLRPDDMvtlhgetiNPLHRHP---IEQT-----LDVGVRAINGLLTVGRGQRLGLFA 168
Cdd:COG0055 82 PVGEATLGRIFNVLGEPIDGKGPIEAKER--------RPIHRPAppfEEQStkteiLETGIKVIDLLAPYAKGGKIGLFG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 169 GSGVGKSVLLGMMTRFTEAE---ITVVGLIGERGRE----VREFIDhslgAEGMARSVVVAAPADDSPLMRLRAA--QLT 239
Cdd:COG0055 154 GAGVGKTVLIMELIHNIAKEhggVSVFAGVGERTREgndlYREMKE----SGVLDKTALVFGQMNEPPGARLRVAltALT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 240 trIAEYFR-AQGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGngSTGGGSITAFYTVLTEG 318
Cdd:COG0055 230 --MAEYFRdEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERIT--STKKGSITSVQAVYVPA 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2197018873 319 DDQQDPVADSARAILDGHFVLSRSLAEQGHYPAIDIEASISRAM-PQIVDPQRLNLALQFKRLYSRYQQNADLIA 392
Cdd:COG0055 306 DDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILdPLIVGEEHYRVAREVQRILQRYKELQDIIA 380
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
96-362 |
2.49e-43 |
|
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: 153.53 E-value: 2.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 96 VPVGFGLLGRVIDGIGRPLDGKGPLRPDDmvtlhgetINPLHRHP---IEQT-----LDVGVRAINGLLTVGRGQRLGLF 167
Cdd:cd01133 2 VPVGEETLGRIFNVLGEPIDERGPIKAKE--------RWPIHREApefVELSteqeiLETGIKVVDLLAPYAKGGKIGLF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 168 AGSGVGKSVLLgMMTRFTEAE----ITVVGLIGERGRE----VREFIDHSL-GAEGMARSVVVAAPADDSPLMRLRAAQL 238
Cdd:cd01133 74 GGAGVGKTVLI-MELINNIAKahggYSVFAGVGERTREgndlYHEMKESGViNLDGLSKVALVYGQMNEPPGARARVALT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 239 TTRIAEYFR-AQGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGngSTGGGSITAFYTVLTE 317
Cdd:cd01133 153 GLTMAEYFRdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERIT--STKKGSITSVQAVYVP 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2197018873 318 GDDQQDPVADSARAILDGHFVLSRSLAEQGHYPAIDIEASISRAM 362
Cdd:cd01133 231 ADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
96-360 |
3.92e-42 |
|
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: 150.40 E-value: 3.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 96 VPVGFGLLGRVIDGIGRPLDGKGPLRPDDMVTLhgETINP--LHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVG 173
Cdd:cd01132 4 VPVGEALLGRVVDALGNPIDGKGPIQTKERRRV--ESKAPgiIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 174 KSVLL--GMMTRFTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQGK 251
Cdd:cd01132 82 KTAIAidTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 252 NVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAG--NGSTGGGSITAFYTVLTEGDDQQDPVADSA 329
Cdd:cd01132 162 HALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklSDELGGGSLTALPIIETQAGDVSAYIPTNV 241
|
250 260 270
....*....|....*....|....*....|.
gi 2197018873 330 RAILDGHFVLSRSLAEQGHYPAIDIEASISR 360
Cdd:cd01132 242 ISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
54-393 |
9.25e-40 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 149.42 E-value: 9.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 54 EEGSVEAEVVGFSGD-RIYLMPLDSVDGLAPGAAVRPKVGASLVPVGFGLLGRVIDGIGRPLDGKGPLrpddmvtlHGET 132
Cdd:CHL00060 53 QEINVTCEVQQLLGNnRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPV--------DTRT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 133 INPLHRHP-----IEQTLDV---GVRAINGLLTVGRGQRLGLFAGSGVGKSVL-LGMMTRFTEAE--ITVVGLIGERGRE 201
Cdd:CHL00060 125 TSPIHRSApafiqLDTKLSIfetGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLiMELINNIAKAHggVSVFGGVGERTRE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 202 -------VRE--FIDhslgAEGMARSVV--VAAPADDSPLMRLRAAQLTTRIAEYFRAQGK-NVLLLMDSLTRYAQAQRE 269
Cdd:CHL00060 205 gndlymeMKEsgVIN----EQNIAESKValVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 270 IALAVGEPPATKGYPPSVFAKLPKLVERAGngSTGGGSITAFYTVLTEGDDQQDPVADSARAILDGHFVLSRSLAEQGHY 349
Cdd:CHL00060 281 VSALLGRMPSAVGYQPTLSTEMGSLQERIT--STKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIY 358
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2197018873 350 PAIDIEASISRAM-PQIVDPQRLNLALQFKRLYSRYQQNADLIAV 393
Cdd:CHL00060 359 PAVDPLDSTSTMLqPRIVGEEHYETAQRVKQTLQRYKELQDIIAI 403
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
75-428 |
1.77e-37 |
|
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439826 [Multi-domain] Cd Length: 504 Bit Score: 143.26 E-value: 1.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 75 LDSVDGLAPGAAVRpKVGASL-VPVGFGLLGRVIDGIGRPLDGKGPLRPDDMVTLhgETINP--LHRHPIEQTLDVGVRA 151
Cdd:COG0056 76 LGDYEGIKEGDTVK-RTGRILsVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPV--ERPAPgvIDRQPVHEPLQTGIKA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 152 INGLLTVGRGQRlGLFAGS-GVGKsvllgmmtrfteaeiTVVGL-----------------IGERG----REVREFIDHs 209
Cdd:COG0056 153 IDAMIPIGRGQR-ELIIGDrQTGK---------------TAIAIdtiinqkgkdviciyvaIGQKAstvaQVVETLEEH- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 210 lGAegMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFA 289
Cdd:COG0056 216 -GA--MEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFY 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 290 KLPKLVERAG--NGSTGGGSITAFYTVLTEGDDqqdpVadSAR------AILDGHFVLSRSLAEQGHYPAIDIEASISR- 360
Cdd:COG0056 293 LHSRLLERAAklSDELGGGSLTALPIIETQAGD----V--SAYiptnviSITDGQIFLESDLFNAGIRPAINVGLSVSRv 366
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2197018873 361 -------AMPQIVDPQRLNLAlQFKRLYsryqqnadliavgAYAR-GS--DPETDRAIDMLPAIRAYLLQGMNEPMPM 428
Cdd:COG0056 367 ggaaqikAMKKVAGTLRLDLA-QYRELE-------------AFAQfGSdlDEATRAQLERGERLVELLKQPQYSPLSV 430
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
79-390 |
8.72e-36 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 138.17 E-value: 8.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 79 DGLA--PGAAVRPKVGASLVPVGFGLLGRVIDGIGRPLDGKGPLRPDDMVTLhgETINP--LHRHPIEQTLDVGVRAING 154
Cdd:CHL00059 57 DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLI--ESPAPgiISRRSVYEPLQTGLIAIDS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 155 LLTVGRGQRLGLFAGSGVGK-SVLLG-MMTRFTEAEITVVGLIGERGREVREfIDHSLGAEG-MARSVVVAAPADDSPLM 231
Cdd:CHL00059 135 MIPIGRGQRELIIGDRQTGKtAVATDtILNQKGQNVICVYVAIGQKASSVAQ-VVTTLQERGaMEYTIVVAETADSPATL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 232 RLRAAQLTTRIAEYFRAQGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAG--NGSTGGGSIT 309
Cdd:CHL00059 214 QYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklSSQLGEGSMT 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 310 AFYTVLTEGDDQQDPVADSARAILDGHFVLSRSLAEQGHYPAIDIEASISR--------AMPQIVDPQRLNLAlQFKRLY 381
Cdd:CHL00059 294 ALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRvgsaaqikAMKQVAGKLKLELA-QFAELE 372
|
....*....
gi 2197018873 382 SRYQQNADL 390
Cdd:CHL00059 373 AFAQFASDL 381
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
26-394 |
2.20e-34 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 133.24 E-value: 2.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 26 RVTRLIG--LTLEAVGlkAALGDYCLVSLQEeGSVEAEVVGFSGDRIYLMPLDSVDGLAPGAAVRPKVGASLVPVGFGLL 103
Cdd:PRK02118 7 KITDITGnvITVEAEG--VGYGELATVERKD-GSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 104 GRVIDGIGRPLDGkGPLRPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGKSVLLGMMTR 183
Cdd:PRK02118 84 GRRFNGSGKPIDG-GPELEGEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLARIAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 184 FTEAEITVVGLIGERGREVREFIDHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQG-KNVLLLMDSLTR 262
Cdd:PRK02118 163 QAEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGkKKVLVLLTDMTN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 263 YAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGStGGGSITAFYTVLTEGDDQQDPVADSARAILDGHFVLSRS 342
Cdd:PRK02118 243 FADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFE-DGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLRRG 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 343 laeqghypAIDIEASISRaMPQIVD--------PQRLNLALqfkRLYSRYQQNADLIAVG 394
Cdd:PRK02118 322 --------RIDPFGSLSR-LKQLVIgkktredhGDLMNAMI---RLYADSREAKEKMAMG 369
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
96-428 |
4.55e-33 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 130.57 E-value: 4.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 96 VPVGFGLLGRVIDGIGRPLDGKGPLRPDDMVTLhgETINP--LHRHPIEQTLDVGVRAINGLLTVGRGQRlGLFAGS-GV 172
Cdd:PRK09281 97 VPVGEALLGRVVNPLGQPIDGKGPIEATETRPV--ERKAPgvIDRKSVHEPLQTGIKAIDAMIPIGRGQR-ELIIGDrQT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 173 GKsvllgmmtrfteaeiTVVGL-----------------IGERGREVREFI----DHslGAegMARSVVVAAPADDSPLM 231
Cdd:PRK09281 174 GK---------------TAIAIdtiinqkgkdviciyvaIGQKASTVAQVVrkleEH--GA--MEYTIVVAATASDPAPL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 232 RLRAAQLTTRIAEYFRAQGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAG--NGSTGGGSIT 309
Cdd:PRK09281 235 QYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAklSDELGGGSLT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 310 AFYTVLTEGDDqqdpVadSAR------AILDGHFVLSRSLAEQGHYPAIDIEASISR--------AMPQIVDPQRLNLAl 375
Cdd:PRK09281 315 ALPIIETQAGD----V--SAYiptnviSITDGQIFLESDLFNAGIRPAINVGISVSRvggaaqikAMKKVAGTLRLDLA- 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2197018873 376 QFKRLYSRYQQNADLiavgayargsDPETDRAIDMLPAIRAYLLQGMNEPMPM 428
Cdd:PRK09281 388 QYRELEAFAQFGSDL----------DEATRAQLERGQRLVELLKQPQYSPLPV 430
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
96-353 |
4.10e-32 |
|
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: 123.84 E-value: 4.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 96 VPVGFGLLGRVIDGIGRPLDgkgplrpdDMVTLHGETINP---LHRHPIEQ------------TLDVGVRAINGLLTVGR 160
Cdd:cd01134 4 VELGPGLLGSIFDGIQRPLE--------VIAETGSIFIPRgvnVQRWPVRQprpvkeklppnvPLLTGQRVLDTLFPVAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 161 GqrlGLFA---GSGVGKSVLLGMMTRFTEAEITVVGLIGERGREV----REF---IDHSLGAEGMARSVVVA------AP 224
Cdd:cd01134 76 G---GTAAipgPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMaevlEEFpelKDPITGESLMERTVLIAntsnmpVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 225 AddsplmrlRAAQLTT--RIAEYFRAQGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAG--- 299
Cdd:cd01134 153 A--------REASIYTgiTIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGrvr 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2197018873 300 -NGSTG-GGSITAFYTVLTEGDDQQDPVADSARAILDGHFVLSRSLAEQGHYPAID 353
Cdd:cd01134 225 cLGSPGrEGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSIN 280
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
23-365 |
3.08e-29 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 120.66 E-value: 3.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 23 VEGRVTRLIGLTLEAVGLK-AALGDYCLVSlqEEGSVeAEVVGFSGDRIYLMPLDSVDGLAPGAAVRPkVGASL-VPVGF 100
Cdd:PRK04192 3 TKGKIVRVSGPLVVAEGMGgARMYEVVRVG--EEGLI-GEIIRIEGDKATIQVYEETSGIKPGEPVEF-TGEPLsVELGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 101 GLLGRVIDGIGRPLD----------GKG----PL------------RPDDMVT--------------------------- 127
Cdd:PRK04192 79 GLLGSIFDGIQRPLDelaeksgdflERGvyvpALdrekkweftptvKVGDKVEagdilgtvqetpsiehkimvppgvsgt 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 128 -----------------------LHGETINPLHRHPI------------EQTLDVGVRAINGLLTVGRGqrlGLFA---G 169
Cdd:PRK04192 159 vkeivsegdytvddtiavlededGEGVELTMMQKWPVrrprpykeklppVEPLITGQRVIDTFFPVAKG---GTAAipgP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 170 SGVGKSVLLGMMTRFTEAEITVVGLIGERGREV----REF---IDHSLGAEGMARSVV--------VAApaddsplmrlR 234
Cdd:PRK04192 236 FGSGKTVTQHQLAKWADADIVIYVGCGERGNEMtevlEEFpelIDPKTGRPLMERTVLiantsnmpVAA----------R 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 235 AAQLTT--RIAEYFRAQGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAG-----NGSTggGS 307
Cdd:PRK04192 306 EASIYTgiTIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGrvktlGGEE--GS 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2197018873 308 ITAFYTVLTEGDDQQDPVADSARAILDGHFVLSRSLAEQGHYPAIDIEASISRAMPQI 365
Cdd:PRK04192 384 VTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYSLYLDQV 441
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
96-362 |
2.58e-28 |
|
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: 116.75 E-value: 2.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 96 VPVGFGLLGRVIDGIGRPLDGKGPLRPDDMVTLHGETINPLHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGKS 175
Cdd:TIGR01040 76 TPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHN 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 176 VLLGMMTRfteaeitVVGLIGERGREVREfiDHS------LGAEG------------------MARSVVVAAPADDSPLM 231
Cdd:TIGR01040 156 EIAAQICR-------QAGLVKLPTKDVHD--GHEdnfaivFAAMGvnmetarffkqdfeengsMERVCLFLNLANDPTIE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 232 RLRAAQLTTRIAEYFRAQ-GKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGSTGGGSITA 310
Cdd:TIGR01040 227 RIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQ 306
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2197018873 311 FYTVLTEGDDQQDPVADSARAILDGHFVLSRSLAEQGHYPAIDIEASISRAM 362
Cdd:TIGR01040 307 IPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 358
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
366-435 |
1.64e-26 |
|
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: 101.74 E-value: 1.64e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 366 VDPQRLNLALQFKRLYSRYQQNADLIAVGAYARGSDPETDRAIDMLPAIRAYLLQGMNEPMPMQRCVQEL 435
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIGAYQAGSDPEIDEAIAKRPAINAFLRQGVDEPVSFEETLAQL 70
|
|
| ATP-synt_flagellum-secretory_path_III_N |
cd18117 |
Flagellum-specific ATP synthase, N-terminal domain; The N-terminal domain of the ... |
23-90 |
1.02e-22 |
|
Flagellum-specific ATP synthase, N-terminal domain; The N-terminal domain of the flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The FliI ATPase is the soluble export component that drives flagellar protein export, and it shows extensive similarity to the alpha and beta subunits of F1-ATP synthase. Although they both are proton driven rotary molecular devices, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens, such as Salmonella and Chlamydia, also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 349741 [Multi-domain] Cd Length: 70 Bit Score: 91.05 E-value: 1.02e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2197018873 23 VEGRVTRLIGLTLEAVGLKAALGDYCLVSLQEEGSVEAEVVGFSGDRIYLMPLDSVDGLAPGAAVRPK 90
Cdd:cd18117 1 VYGRVVRVVGLLLEAVGPQAPIGELCLIETADGLSILAEVVGFSGEKVLLMPLGELSGLSPGARVVPL 68
|
|
| ATP-synt_flagellum-secretory_path_III_C |
cd18114 |
Flagellum-specific ATP synthase, C-terminal domain; The C-terminal domain of the ... |
373-440 |
8.87e-22 |
|
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: 88.43 E-value: 8.87e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2197018873 373 LALQFKRLYSRYQQNADLIAVGAYARGSDPETDRAIDMLPAIRAYLLQGMNEPMPMQRCVQELAMVMS 440
Cdd:cd18114 4 AARKFRELMSTYQENEDLIRIGAYKKGSDPEVDEAIRLKPQIEAFLKQGLNEKAPLEESLQQLEEIFG 71
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
69-388 |
2.51e-21 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 96.65 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 69 RIYLMPLDSVDGLAPGAAVRPKVGASLVPVGFGLLGRVIDGIG------------RPLDGKGPLRPDDmvtlhGETINPL 136
Cdd:PTZ00185 90 RIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGhevpvglltrsrALLESEQTLGKVD-----AGAPNIV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 137 HRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGKS----------VLLGMMTRFTEAEITVVGLIGERGREVREfI 206
Cdd:PTZ00185 165 SRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTsiavstiinqVRINQQILSKNAVISIYVSIGQRCSNVAR-I 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 207 DHSLGAEGMAR-SVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPP 285
Cdd:PTZ00185 244 HRLLRSYGALRyTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPG 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 286 SVFAKLPKLVERAGNGS--TGGGSITAFYTVLTEGDDQQDPVADSARAILDGHFVLSRSLAEQGHYPAIDIEASISRAMP 363
Cdd:PTZ00185 324 DVFYLHSRLLERAAMLSpgKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGS 403
|
330 340
....*....|....*....|....*
gi 2197018873 364 QIVDPQRLNLALQFKRLYSRYQQNA 388
Cdd:PTZ00185 404 SAQNVAMKAVAGKLKGILAEYRKLA 428
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
181-408 |
2.78e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 94.32 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 181 MTRFTEAEITVVGLIGERGREVREFI-------DHSLGAEGMARSVVVAAPADDSPLMRLRAAQLTTRIAEYFRAQGKNV 253
Cdd:PRK14698 676 LAKWSDAQVVIYIGCGERGNEMTDVLeefpklkDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDV 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 254 LLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPKLVERAGNGSTGG-----GSITAFYTVLTEGDDQQDPVADS 328
Cdd:PRK14698 756 ALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGsdyrvGSVSVIGAVSPPGGDFSEPVVQN 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 329 ARAILDGHFVLSRSLAEQGHYPAIDIEASISRAMPQIVDPQRLNLALQFKRLYSR----YQQNADLIAVgAYARGSD--P 402
Cdd:PRK14698 836 TLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNVDPEWKAMRDKamelLQKEAELQEI-VRIVGPDalP 914
|
....*.
gi 2197018873 403 ETDRAI 408
Cdd:PRK14698 915 ERERAI 920
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
136-390 |
1.66e-17 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 84.64 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 136 LHRHPIEQTLDVGVRAINGLLTVGRGQRLGLFAGSGVGK-SVLLGMMTRFTEAEITVVGL-IGERgREVREFIDHSLGAE 213
Cdd:PRK07165 118 MTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKtHIALNTIINQKNTNVKCIYVaIGQK-RENLSRIYETLKEH 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 214 G-MARSVVVAAPADdSPLMRLRAAQLTTRIAEYFrAQGKNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLP 292
Cdd:PRK07165 197 DaLKNTIIIDAPST-SPYEQYLAPYVAMAHAENI-SYNDDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHS 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 293 KLVERAGNgSTGGGSITAFYTVLTEGDDQQDPVADSARAILDGHFVLSRSLAEQGHYPAIDIEASISRAMPQIVDPQRLN 372
Cdd:PRK07165 275 KLLERAGK-FKNRKTITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITK 353
|
250
....*....|....*...
gi 2197018873 373 LALQFKRLYSRYQQNADL 390
Cdd:PRK07165 354 VAGEISKIYRAYKRQLKL 371
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
129-382 |
2.37e-17 |
|
transcription termination factor Rho; This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding. [Transcription, Transcription factors]
Pssm-ID: 162030 [Multi-domain] Cd Length: 415 Bit Score: 83.58 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 129 HGETINPLHrhPIEQ------TLDVGVRAINGLLTVGRGQRLGLFAGSGVGKSVLL-----GMMTRFTEAEITVVgLIGE 197
Cdd:TIGR00767 132 LFENLTPLY--PNERlrletsTEDLSTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLqkiaqAITRNHPEVELIVL-LIDE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 198 RGREVREfidhslgaegMARSV---VVAAPADDSPLMRLRAAQLTTRIAEYFRAQGKNVLLLMDSLTRYAQAQREIALAV 274
Cdd:TIGR00767 209 RPEEVTD----------MQRSVkgeVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPAS 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 275 GEpPATKGYPPSVFAKlPKLVERAGNGSTGGGSITAFYTVLTEGDDQQDPVA-DSARAILDGHFVLSRSLAEQGHYPAID 353
Cdd:TIGR00767 279 GK-VLSGGVDANALHR-PKRFFGAARNIEEGGSLTIIATALIDTGSRMDEVIfEEFKGTGNMELHLDRKLADRRIFPAID 356
|
250 260
....*....|....*....|....*....
gi 2197018873 354 IEASISRAMPQIVDPQRLNLALQFKRLYS 382
Cdd:TIGR00767 357 IKKSGTRKEELLLTPEELQKIWVLRKIIS 385
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
146-379 |
2.73e-17 |
|
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: 81.10 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 146 DVGVRAINGLLTVGRGQRLGLFAGSGVGKSVLL-----GMMTRFTEAEITVVgLIGERGREVREFIDhSLGAEgmarsvV 220
Cdd:cd01128 1 ELSTRVIDLIAPIGKGQRGLIVAPPKAGKTTLLqnianAIAKNHPEVELIVL-LIDERPEEVTDMRR-SVKGE------V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 221 VAAPADDSPLMRLRAAQLTTRIAEYFRAQGKNVLLLMDSLTRYAQAQREIAlavgePPATKGYPPSVFA---KLPKLVER 297
Cdd:cd01128 73 VASTFDEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVV-----PSSGKTLSGGVDAnalHKPKRFFG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 298 AGNGSTGGGSITAFYTVLTEGDDQQDPVadsaraILDgHF--------VLSRSLAEQGHYPAIDIEASISRAMPQIVDPQ 369
Cdd:cd01128 148 AARNIEEGGSLTIIATALVDTGSRMDEV------IFE-EFkgtgnmelVLDRKLAEKRIFPAIDILKSGTRKEELLLTPE 220
|
250
....*....|
gi 2197018873 370 RLNLALQFKR 379
Cdd:cd01128 221 ELQKIWLLRR 230
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
104-371 |
5.63e-15 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 76.28 E-value: 5.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 104 GRVIDGIGRPLDGKGPLRPDDMV----------TLHGETINPLHRHP----IEQTLDVGVRAINGLLTVGRGQRLGLFAG 169
Cdd:PRK12608 62 GDVVEGVARPRERYRVLVRVDSVngtdpeklarRPHFDDLTPLHPRErlrlETGSDDLSMRVVDLVAPIGKGQRGLIVAP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 170 SGVGKSVLL-----GMMTRFTEAEITVVgLIGERGREVREfidhslgaegMARSV---VVAAPADDSPLMRLRAAQLTTR 241
Cdd:PRK12608 142 PRAGKTVLLqqiaaAVAANHPEVHLMVL-LIDERPEEVTD----------MRRSVkgeVYASTFDRPPDEHIRVAELVLE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 242 IAEYFRAQGKNVLLLMDSLTRYAQAQREIALAVGEPpATKGYPPSVFAKlPKLVERAGNGSTGGGSITAFYTVLTEGDDQ 321
Cdd:PRK12608 211 RAKRLVEQGKDVVILLDSLTRLARAYNNEVESSGRT-LSGGVDARALQR-PKRLFGAARNIEEGGSLTIIATALVDTGSR 288
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2197018873 322 QDPVA-DSARAILDGHFVLSRSLAEQGHYPAIDIEASISRAMPQIVDPQRL 371
Cdd:PRK12608 289 MDEVIfEEFKGTGNMEIVLDRELADKRVFPAIDIAKSGTRREELLLDSKEL 339
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
119-360 |
1.30e-09 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 59.77 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 119 PLRPDDMVTLhgETINPLhrhpieqtlDVGVRAINGLLTVGRGQRlGLF-AGSGVGKSVLL-----GMMTRFTEAEITVV 192
Cdd:PRK09376 138 PLYPNERLRL--ETGNPE---------DLSTRIIDLIAPIGKGQR-GLIvAPPKAGKTVLLqnianSITTNHPEVHLIVL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 193 gLIGERGREVREfidhslgaegMARSV---VVAAPADDSPLMRLRAAQLT----TRIAEyfraQGKNVLLLMDSLTRYAq 265
Cdd:PRK09376 206 -LIDERPEEVTD----------MQRSVkgeVVASTFDEPAERHVQVAEMViekaKRLVE----HGKDVVILLDSITRLA- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 266 aqREIALAVgePPATK----GYPPSVFAKlPKLVERAGNGSTGGGSITAFYTVLTEGDDQQDPVadsaraIldghF---- 337
Cdd:PRK09376 270 --RAYNTVV--PSSGKvlsgGVDANALHR-PKRFFGAARNIEEGGSLTIIATALIDTGSRMDEV------I----Feefk 334
|
250 260 270
....*....|....*....|....*....|
gi 2197018873 338 -------VLSRSLAEQGHYPAIDIEASISR 360
Cdd:PRK09376 335 gtgnmelHLDRKLAEKRIFPAIDINRSGTR 364
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
376-435 |
6.34e-08 |
|
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: 49.36 E-value: 6.34e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 376 QFKRLYSRYQQNADLIAVGAYARgSDPETDRAIDMLPAIRAYLLQGMNEPMPMQRCVQEL 435
Cdd:cd01429 7 GFKAILAQYRELRDIVAIVGDDA-LSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKL 65
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
25-89 |
1.19e-06 |
|
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: 45.77 E-value: 1.19e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2197018873 25 GRVTRLIGLTLEAVGLK-AALGDYCLVSL---QEEGSVEAEVVGFSGDRIYLMPLDSVDGLAPGAAVRP 89
Cdd:cd01426 2 GRVIRVNGPLVEAELEGeVAIGEVCEIERgdgNNETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEP 70
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
24-115 |
8.42e-05 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 45.01 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 24 EGRVTRLIGLTLEAVGLKAAlGDYCLVSLQEEGSVeAEVVGFSGDRIYLMPLDSVDGLAPGAAVRpKVGASL-VPVGFGL 102
Cdd:PRK14698 4 KGRIIRVTGPLVIADGMKGA-KMYEVVRVGELGLI-GEIIRLEGDKAVIQVYEETAGLKPGEPVE-GTGSSLsVELGPGL 80
|
90
....*....|...
gi 2197018873 103 LGRVIDGIGRPLD 115
Cdd:PRK14698 81 LTSIYDGIQRPLE 93
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
27-89 |
1.20e-04 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 40.22 E-value: 1.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2197018873 27 VTRLIGLTLEAVGLKAAL-GDYCLVSLQ---EEGSVEAEVVGFSGDRIYLMPLDSVDGLAPGAAVRP 89
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLpGLLNALEVElveFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKR 67
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
111-194 |
4.95e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 39.51 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197018873 111 GRPLDGKGPLRPDDMVTL---HGETINPLHRHPIEQTLDV----GVRAI--NGLLTVGRGQRLGLFAGSGVGKSVLLGMM 181
Cdd:TIGR01271 1186 PRPSGGGGKYQLSTVLVIenpHAQKCWPSGGQMDVQGLTAkyteAGRAVlqDLSFSVEGGQRVGLLGRTGSGKSTLLSAL 1265
|
90
....*....|....*
gi 2197018873 182 TRF--TEAEITVVGL 194
Cdd:TIGR01271 1266 LRLlsTEGEIQIDGV 1280
|
|
| |
