|
Name |
Accession |
Description |
Interval |
E-value |
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
3-434 |
0e+00 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 892.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 3 RLLMNENEKWNKFIETPLYTKVGKVHSVQEQFFVAKGPKAKIGDVCFVGEHNVLCEVIAIEKENNMLLPFEQTEKVCYGD 82
Cdd:PRK06793 1 RLLMNENQKWNTFIETPFYTKVGKVHSVQEQFFVAKGPKAKIGDVCFVGEHNVLCEVIAIEKENNMLLPFEQTEKVCYGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 83 SVTLVSEDVVVPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIG 162
Cdd:PRK06793 81 SVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 163 IFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEY 242
Cdd:PRK06793 161 IFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 243 FRDQGNNVLLMMDSVTRFADARRSVDIAVKELPIGGKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDL 322
Cdd:PRK06793 241 FRDQGNNVLLMMDSVTRFADARRSVDIAVKELPIGGKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 323 ARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENELYFKLGTIQENEENAYIFEC 402
Cdd:PRK06793 321 ARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGTIQENAENAYIFEC 400
|
410 420 430
....*....|....*....|....*....|..
gi 1261856570 403 KNKVEGINTFLKQGRSDSFQFDDIVEAIHHIV 434
Cdd:PRK06793 401 KNKVEGINTFLKQGRSDSFQFDDIVEAMHHIV 432
|
|
| FliI_clade2 |
TIGR03497 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
25-434 |
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: 692.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 25 GKVHSVQEQFFVAKGPKAKIGDVCFV---GEHNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLVSEDVVVPRGNHLLG 101
Cdd:TIGR03497 1 GKVTRVIGLTIESKGPKASIGELCSIltkGGKPVLAEVVGFKEENVLLMPLGEVEGIGPGSLVIATGRPLAIKVGKGLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 102 KVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN 181
Cdd:TIGR03497 81 RVLDGLGRPLDGEGPIIGEEPYPLDNPPPNPLKRPRIRDPLETGIKAIDGLLTIGKGQRVGIFAGSGVGKSTLLGMIARN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 182 AKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFA 261
Cdd:TIGR03497 161 AKADINVIALIGERGREVRDFIEKDLGEEGLKRSVVVVATSDQPALMRLKAAFTATAIAEYFRDQGKDVLLMMDSVTRFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 262 DARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATL 340
Cdd:TIGR03497 241 MAQREIGLAVGEPPTTrGYTPSVFSLLPKLLERSGNSQKGSITGFYTVLVDGDDMNEPIADAVRGILDGHIVLSRELAAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 341 SHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENELYFKLGTIQENeENAYIFECKNKVEGINTFLKQGRSDS 420
Cdd:TIGR03497 321 NHYPAIDVLASVSRVMNEIVSEEHKELAGKLRELLAVYKEAEDLINIGAYKRG-SNPKIDEAIRYIEKINSFLKQGIDEK 399
|
410
....*....|....
gi 1261856570 421 FQFDDIVEAIHHIV 434
Cdd:TIGR03497 400 FTFEETVQLLKELL 413
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
17-434 |
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: 586.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 17 ETPLYTKVGKVHSVQEQFFVAKGPKAKIGDVCFV---GEHNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLVSEDVVV 93
Cdd:COG1157 13 ELPPVRVSGRVTRVVGLLIEAVGPDASIGELCEIetaDGRPVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 94 PRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST 173
Cdd:COG1157 93 PVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKST 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 174 LLGMIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLM 253
Cdd:COG1157 173 LLGMIARNTEADVNVIALIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 254 MDSVTRFADARRSVDIAVKELPI-GGKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIV 332
Cdd:COG1157 253 MDSLTRFAMAQREIGLAAGEPPAtRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAVRGILDGHIV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 333 LKRELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENELYFKLGTIQENeENAYIFECKNKVEGINTF 412
Cdd:COG1157 333 LSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENEDLIRIGAYQPG-SDPELDEAIALIPAIEAF 411
|
410 420
....*....|....*....|..
gi 1261856570 413 LKQGRSDSFQFDDIVEAIHHIV 434
Cdd:COG1157 412 LRQGMDERVSFEESLAQLAELL 433
|
|
| FliI_clade1 |
TIGR03496 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
25-429 |
4.45e-168 |
|
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: 477.74 E-value: 4.45e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 25 GKVHSVQEQFFVAKGPKAKIGDVCFV---GEHNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLVSEDVVVPRGNHLLG 101
Cdd:TIGR03496 1 GRVTRVVGLVLEAVGLRAPVGSRCEIessDGDPIEAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLGGPLRLPVGDSLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 102 KVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN 181
Cdd:TIGR03496 81 RVIDGLGRPLDGKGPLDAGERVPLYAPPINPLKRAPIDEPLDVGVRAINGLLTVGRGQRMGIFAGSGVGKSTLLGMMARY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 182 AKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFA 261
Cdd:TIGR03496 161 TEADVVVVGLIGERGREVKEFIEDILGEEGLARSVVVAATADESPLMRLRAAFYATAIAEYFRDQGKDVLLLMDSLTRFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 262 DARRSVDIAVKELPIggktllMESY-------MKKLLERSGKTQ--KGSITGIYTVLVDGDDLNGPVPDLARGILDGHIV 332
Cdd:TIGR03496 241 MAQREIALAIGEPPA------TKGYppsvfakLPQLVERAGNGEegKGSITAFYTVLVEGDDQQDPIADAARAILDGHIV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 333 LKRELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENELYFKLGtiqeneenAYIF-------ECKNK 405
Cdd:TIGR03496 315 LSRELAEQGHYPAIDILASISRVMPDVVSPEHRQAARRFKQLLSRYQENRDLISIG--------AYQAgsdpeldQAIAL 386
|
410 420
....*....|....*....|....
gi 1261856570 406 VEGINTFLKQGRSDSFQFDDIVEA 429
Cdd:TIGR03496 387 YPRIEAFLQQGMRERASFEESLEA 410
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
1-433 |
1.54e-156 |
|
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: 449.90 E-value: 1.54e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 1 MSRLLMNENEKWNKFIETPLYTKVGKVHSVQEQFFVAKGPKAKIGDVCFV----GEHNVLCEVIAIEKENNMLLPFEQTE 76
Cdd:TIGR01026 1 MERNLTTFYNRLCQEMDLRLVKRVGRVTKVKGLLIEAVGPQASVGDLCLIerrgSEGRLVAEVVGFNGEFVFLMPYEEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 77 KVCYGDSVTLVSEDVVVPRGNHLLGKVLSANGEVLNEEAENI-PLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTI 155
Cdd:TIGR01026 81 GVRPGSKVLATGEGLSIKVGDGLLGRVLDGLGKPIDGKGKFLdNVETEGLITAPINPLKRAPIREILSTGVRSIDGLLTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 156 GIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKL 235
Cdd:TIGR01026 161 GKGQRIGIFAGSGVGKSTLLGMIARNTEADVNVIALIGERGREVREFIEHDLGEEGLKRSVVVVATSDQSPLLRLKGAYV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 236 ATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELPI-GGKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDD 314
Cdd:TIGR01026 241 ATAIAEYFRDQGKDVLLLMDSVTRFAMAQREIGLAAGEPPAtKGYTPSVFSTLPRLLERAGASGKGSITAFYTVLVEGDD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 315 LNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENELYFKLGTIQENe 394
Cdd:TIGR01026 321 MNEPIADSVRGILDGHIVLSRALAQRGHYPAIDVLASISRLMTAIVSEEHRRAARKFRELLSKYKDNEDLIRIGAYQRG- 399
|
410 420 430
....*....|....*....|....*....|....*....
gi 1261856570 395 ENAYIFECKNKVEGINTFLKQGRSDSFQFDDIVEAIHHI 433
Cdd:TIGR01026 400 SDRELDFAIAKYPKLERFLKQGINEKVNFEESLQQLEEI 438
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
11-430 |
1.59e-152 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 439.54 E-value: 1.59e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 11 KWNKFIE----TPLYTKVGKVHSVQEQFFVAKGPKAKIGDVCFV-----GEHNVLCEVIAIEKENNMLLPFEQTEKVCYG 81
Cdd:PRK07721 2 KTQQLIDcietLDPYKRYGKVSRVIGLMIESKGPESSIGDVCYIhtkggGDKAIKAEVVGFKDEHVLLMPYTEVAEIAPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 82 DSVTLVSEDVVVPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKI 161
Cdd:PRK07721 82 CLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 162 GIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAE 241
Cdd:PRK07721 162 GIFAGSGVGKSTLMGMIARNTSADLNVIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 242 YFRDQGNNVLLMMDSVTRFADARRSVDIAVKELPI-GGKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVP 320
Cdd:PRK07721 242 YFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTtKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 321 DLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENELYFKLGTIQENeENAYIF 400
Cdd:PRK07721 322 DTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLINIGAYKRG-SSREID 400
|
410 420 430
....*....|....*....|....*....|
gi 1261856570 401 ECKNKVEGINTFLKQGRSDSFQFDDIVEAI 430
Cdd:PRK07721 401 EAIQFYPQIISFLKQGTDEKATFEESIQAL 430
|
|
| III_secr_ATP |
TIGR02546 |
type III secretion apparatus H+-transporting two-sector ATPase; [Protein fate, Protein and ... |
19-434 |
3.71e-150 |
|
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: 432.90 E-value: 3.71e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 19 PLYTKVGKVHSVQEQFFVAKGPKAKIGDVCFV---GEHNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLVSEDVVVPR 95
Cdd:TIGR02546 1 QPVRVRGRVTEVSGTLLKAVLPGARVGELCLIrrrDPSQLLAEVVGFTGDEALLSPLGELHGISPGSEVIPTGRPLSIRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 96 GNHLLGKVLSANGEVLNEEAEnIPLQKIK---LDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKS 172
Cdd:TIGR02546 81 GEALLGRVLDGFGRPLDGKGE-LPAGEIEtrpLDADPPPPMSRQPIDQPLPTGVRAIDGLLTCGEGQRIGIFAGAGVGKS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 173 TLLGMIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLL 252
Cdd:TIGR02546 160 TLLGMIARGASADVNVIALIGERGREVREFIEHHLGEEGRKRSVLVVSTSDRPSLERLKAAYTATAIAEYFRDQGKRVLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 253 MMDSVTRFADARRSVDIAVKELPI-GGKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHI 331
Cdd:TIGR02546 240 MMDSLTRFARALREIGLAAGEPPArGGYPPSVFSSLPRLLERAGNGEKGSITALYTVLVEGDDMNDPIADEVRSILDGHI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 332 VLKRELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENELYFKLGTIQENeENAYIFECKNKVEGINT 411
Cdd:TIGR02546 320 VLSRALAERNHYPAIDVLASLSRVMSQVVSTEHRRAAGKLRRLLATYKEVELLIRLGEYQPG-SDPETDDAIDKIDAIRA 398
|
410 420
....*....|....*....|...
gi 1261856570 412 FLKQGRSDSFQFDDIVEAIHHIV 434
Cdd:TIGR02546 399 FLRQSTDEYSPYEETLEQLHALV 421
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
93-355 |
4.84e-147 |
|
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: 418.89 E-value: 4.84e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 93 VPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKS 172
Cdd:cd01136 2 IPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 173 TLLGMIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLL 252
Cdd:cd01136 82 TLLGMIARNTDADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 253 MMDSVTRFADARRSVDIAVKELPI-GGKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHI 331
Cdd:cd01136 162 LMDSLTRFAMAQREVGLAAGEPPTrRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRSILDGHI 241
|
250 260
....*....|....*....|....
gi 1261856570 332 VLKRELATLSHYPAISVLDSVSRI 355
Cdd:cd01136 242 VLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI_clade3 |
TIGR03498 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
25-425 |
7.61e-140 |
|
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: 406.30 E-value: 7.61e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 25 GKVHSVQEQFFVAKGPKA--KIGDVCFVGEHN---VLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLVSEDVVVPRGNHL 99
Cdd:TIGR03498 1 GRVTAVTGLLIEVRGLSRavRLGDRCAIRARDgrpVLAEVVGFNGDRVLLMPFEPLEGVGLGCAVFAREGPLAVRPHPSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 100 LGKVLSANGEVL-NEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMI 178
Cdd:TIGR03498 81 LGRVINALGEPIdGKGPLPQGERRYPLRASPPPAMSRARVGEPLDTGVRVIDTFLPLCRGQRLGIFAGSGVGKSTLLSML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 179 AKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVT 258
Cdd:TIGR03498 161 ARNTDADVVVIALVGERGREVREFLEDDLGEEGLKRSVVVVATSDESPLMRRQAAYTATAIAEYFRDQGKDVLLLMDSVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 259 RFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGK--TQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKR 335
Cdd:TIGR03498 241 RFAMAQREIGLAAGEPPVArGYTPSVFSELPRLLERAGPgaEGKGSITGIFTVLVDGDDHNEPVADAVRGILDGHIVLDR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 336 ELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENELYFKLGTIQENeENAYIFECKNKVEGINTFLKQ 415
Cdd:TIGR03498 321 AIAERGRYPAINVLASVSRLAPRVWSPEERKLVRRLRALLARYEETEDLIRLGAYRKG-SDPELDEAIRLVPKIYEFLTQ 399
|
410
....*....|
gi 1261856570 416 GRSDSFQFDD 425
Cdd:TIGR03498 400 GPDEPTSLQD 409
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
25-434 |
4.07e-127 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 374.92 E-value: 4.07e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 25 GKVHSVQEQFFVAKGPKAKIGDVCFVGEHNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLVSEDVVVPRGNHLLGKVL 104
Cdd:PRK06820 31 GPIVEIGPTLLRASLPGVAQGELCRIEPQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 105 SANGEVLnEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKA 184
Cdd:PRK06820 111 DGLGAPI-DGGPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCADSAA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 185 DINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADAR 264
Cdd:PRK06820 190 DVMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 265 RSVDIAVKELPIGGktllmeSY-------MKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKREL 337
Cdd:PRK06820 270 REIGLAAGEPPAAG------SFppsvfanLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 338 ATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENELYFKLGTIQENEEnAYIFECKNKVEGINTFLKQGR 417
Cdd:PRK06820 344 AGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGEYQAGED-LQADEALQRYPAICAFLQQDH 422
|
410
....*....|....*..
gi 1261856570 418 SDSFQFDDIVEAIHHIV 434
Cdd:PRK06820 423 SETAHLETTLEHLAQVV 439
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
1-434 |
7.83e-127 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 374.42 E-value: 7.83e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 1 MSRLLMNENEKWNKFIETPLYTKVGKVHSVQEQFFVAKGPKAKIGDVCFV----GEhnVLCEVIAIEKENNMLLPFEQTE 76
Cdd:PRK08972 3 RQHQLLNRLKQYKVKVPPFRAVASGKLVRVVGLTLEATGCRAPVGSLCSIetmaGE--LEAEVVGFDGDLLYLMPIEELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 77 KVCYGDSVTLVSEDVVVPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIG 156
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 157 IGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLA 236
Cdd:PRK08972 161 KGQRMGLFAGSGVGKSVLLGMMTRGTTADVIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCETA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 237 TSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP-IGGKTLLMESYMKKLLERSGK--TQKGSITGIYTVLVDGD 313
Cdd:PRK08972 241 TTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPaTKGYPPSVFAKLPALVERAGNggPGQGSITAFYTVLTEGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 314 DLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENELYFKLGTIQEN 393
Cdd:PRK08972 321 DLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLYQQNRDLISIGAYKQG 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1261856570 394 E----ENAYIFECKnkvegINTFLKQGRSDSFQFDDIVEAIHHIV 434
Cdd:PRK08972 401 SdpriDNAIRLQPA-----MNAFLQQTMKEAVPYDMSVNMLKQLA 440
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
13-434 |
8.28e-127 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 373.64 E-value: 8.28e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 13 NKFIETPLYTKVGKVHSVQEQFFVAKGPKAKIGD-VCFVGE---HNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLVS 88
Cdd:PRK08472 8 NKLQKFNLSPRFGSITKISPTIIEADGLNPSVGDiVKIESSdngKECLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 89 EDVVVPRGNHLLGKVLSANGEVLN-----EEAENIPLQKikldaPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGI 163
Cdd:PRK08472 88 EGLNIPVGRNLLGRVVDPLGRPIDgkgaiDYERYAPIMK-----APIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 164 FAGSGVGKSTLLGMIAKNAKADINVISLVGERGREVKDFIRKELGEEgMRKSVVVVATSDESHLMQLRAAKLATSIAEYF 243
Cdd:PRK08472 163 FAGSGVGKSTLMGMIVKGCLAPIKVVALIGERGREIPEFIEKNLGGD-LENTVIVVATSDDSPLMRKYGAFCAMSVAEYF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 244 RDQGNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQ-KGSITGIYTVLVDGDDLNGPVPD 321
Cdd:PRK08472 242 KNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSkGYPPSVLSLLPQLMERAGKEEgKGSITAFFTVLVEGDDMSDPIAD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 322 LARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENELYFKLGTIQENEENAyIFE 401
Cdd:PRK08472 322 QSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAYQKGNDKE-LDE 400
|
410 420 430
....*....|....*....|....*....|...
gi 1261856570 402 CKNKVEGINTFLKQGRSDSFQFDDIVEAIHHIV 434
Cdd:PRK08472 401 AISKKEFMEQFLKQNPNELFPFEQTFEQLEEIL 433
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
25-434 |
1.00e-122 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 363.69 E-value: 1.00e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 25 GKVHSVQEQFFVAKGPKAKIGDVCFV----GEHNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLVSEDVVVPRGNHLL 100
Cdd:PRK06936 25 GRVTQVTGTILKAVVPGVRIGELCYLrnpdNSLSLQAEVIGFAQHQALLTPLGEMYGISSNTEVSPTGTMHQVGVGEHLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 101 GKVLSANGEVLNEEAENIPLQK--IKLDAPPihAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMI 178
Cdd:PRK06936 105 GRVLDGLGQPFDGGHPPEPAAWypVYADAPA--PMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 179 AKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVT 258
Cdd:PRK06936 183 IRSAEVDVTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 259 RFADARRSVDIAVKELPI-GGKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKREL 337
Cdd:PRK06936 263 RFARAQREIGLAAGEPPTrRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 338 ATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENELYFKLGTIQENEENAyIFECKNKVEGINTFLKQGR 417
Cdd:PRK06936 343 AAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIGEYQKGQDKE-ADQAIERIGAIRGFLRQGT 421
|
410
....*....|....*..
gi 1261856570 418 SDSFQFDDIVEAIHHIV 434
Cdd:PRK06936 422 HELSHFNETLNLLETLT 438
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
25-419 |
1.13e-117 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 350.82 E-value: 1.13e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 25 GKVHSVQEQFFVAKGPKA--KIGDVCFV---GEHNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLVSEDVVVPRGNHL 99
Cdd:PRK08927 19 GRVVAVRGLLVEVAGPIHalSVGARIVVetrGGRPVPCEVVGFRGDRALLMPFGPLEGVRRGCRAVIANAAAAVRPSRAW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 100 LGKVLSANGE------VLNEEAENIPLQkikldAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST 173
Cdd:PRK08927 99 LGRVVNALGEpidgkgPLPQGPVPYPLR-----APPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 174 LLGMIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLM 253
Cdd:PRK08927 174 LLSMLARNADADVSVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 254 MDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERS--GKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGH 330
Cdd:PRK08927 254 MDSVTRFAMAQREIGLSAGEPPTTkGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGH 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 331 IVLKRELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENELYFKLGtiqeneenAYIFECKNKV---- 406
Cdd:PRK08927 334 IVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLG--------AYRAGSDPEVdeai 405
|
410
....*....|....*.
gi 1261856570 407 ---EGINTFLKQGRSD 419
Cdd:PRK08927 406 rlnPALEAFLRQGKDE 421
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
21-434 |
1.93e-112 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 337.31 E-value: 1.93e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 21 YTKVGKVHSVQEQFFVAKGPKAKIGDVCFVGEHNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLVSEDVVVPRGNHLL 100
Cdd:PRK07594 19 YCRWGRIQDVSATLLNAWLPGVFMGELCCIKPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 101 GKVLSANGEVLNE-EAENIPLQKikLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIA 179
Cdd:PRK07594 99 GRVIDGFGRPLDGrELPDVCWKD--YDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 180 KNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTR 259
Cdd:PRK07594 177 NAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 260 FADARRSVDIAVKELPIGGK-TLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELA 338
Cdd:PRK07594 257 YARAAREIALAAGETAVSGEyPPGVFSALPRLLERTGMGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 339 TLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENELYFKLGTIQENEENAyIFECKNKVEGINTFLKQGRS 418
Cdd:PRK07594 337 ERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEYQRGVDTD-TDKAIDTYPDICTFLRQSKD 415
|
410
....*....|....*.
gi 1261856570 419 DSFQFDDIVEAIHHIV 434
Cdd:PRK07594 416 EVCGPELLIEKLHQIL 431
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
37-381 |
1.10e-110 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 333.24 E-value: 1.10e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 37 AKGPKAKIGDVCFV----GEH--NVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLVSEDVVVPRGNHLLGKVLSANGEV 110
Cdd:PRK05688 41 AEGLRAAVGSRCLVinddSYHpvQVEAEVMGFSGDKVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 111 LNEEAeniPLQ---KIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADIN 187
Cdd:PRK05688 121 LDGKG---PMKaedWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEADII 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 188 VISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSV 267
Cdd:PRK05688 198 VVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 268 DIAVKELP-IGGKTLLMESYMKKLLERSGKTQK--GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYP 344
Cdd:PRK05688 278 ALAIGEPPaTKGYPPSVFAKLPKLVERAGNAEPggGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYP 357
|
330 340 350
....*....|....*....|....*....|....*..
gi 1261856570 345 AISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKEN 381
Cdd:PRK05688 358 AIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQS 394
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
145-353 |
1.56e-109 |
|
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: 321.23 E-value: 1.56e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 145 GIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDE 224
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLGSGALKRTVVVVATSDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 225 SHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELPI-GGKTLLMESYMKKLLERSGKT--QKGS 301
Cdd:pfam00006 81 PPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGrEGYPPSVFSLLARLLERAGRVkgKGGS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1261856570 302 ITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVS 353
Cdd:pfam00006 161 ITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
18-434 |
3.69e-109 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 329.04 E-value: 3.69e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 18 TPLYTKVGKVHSVQEQFFVAKGPKAKIGDVCFV----GEHNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLVSEDVVV 93
Cdd:PRK09099 19 LPAVRRTGKVVEVIGTLLRVSGLDVTLGELCELrqrdGTLLQRAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 94 PRGNHLLGKVLSANGEVLN-----EEAENIPLQkikldAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSG 168
Cdd:PRK09099 99 PVGPALLGRVIDGLGEPIDgggplDCDELVPVI-----AAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 169 VGKSTLLGMIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGN 248
Cdd:PRK09099 174 VGKSTLMGMFARGTQCDVNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 249 NVLLMMDSVTRFADARRSVDIAVKELPI-GGKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGIL 327
Cdd:PRK09099 254 RVLLMMDSLTRFARAQREIGLAAGEPPArRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVRGIL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 328 DGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENELYFKLGTIQENeENAYIFECKNKVE 407
Cdd:PRK09099 334 DGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVGEYRAG-SDPVADEAIAKID 412
|
410 420
....*....|....*....|....*..
gi 1261856570 408 GINTFLKQGRSDSFQFDDIVEAIHHIV 434
Cdd:PRK09099 413 AIRDFLSQRTDEYSDPDATLAALAELS 439
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
40-434 |
3.15e-108 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 326.18 E-value: 3.15e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 40 PKAKIGDVCFV----GEHNVLCE--VIAIEKENNMLlpfeqtekVCYGDSVTLVSEDVVVPRG--------NHLLGKVLS 105
Cdd:PRK08149 23 PDVAIGEICEIragwHSNEVIARaqVVGFQRERTIL--------SLIGNAQGLSRQVVLKPTGkplsvwvgEALLGAVLD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 106 ANGEV---LNEEAENIPLQKIKL-DAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN 181
Cdd:PRK08149 95 PTGKIverFDAPPTVGPISEERViDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 182 AKADINVISLVGERGREVKDFIrkelgeEGMRKS------VVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMD 255
Cdd:PRK08149 175 SEADVFVIGLIGERGREVTEFV------ESLRASsrrekcVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFID 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 256 SVTRFADARRSVDIAVKELPI--GGKTLLMESyMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVL 333
Cdd:PRK08149 249 SMTRYARALRDVALAAGELPArrGYPASVFDS-LPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 334 KRELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENELYFKLGTIQ--ENEENAYIFECKNKVEGint 411
Cdd:PRK08149 328 SRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGEYRrgENADNDRAMDKRPALEA--- 404
|
410 420
....*....|....*....|...
gi 1261856570 412 FLKQGRSDSFQFDDIVEAIHHIV 434
Cdd:PRK08149 405 FLKQDVAEKSSFSDTLERLNEFA 427
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
25-380 |
2.75e-99 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 303.84 E-value: 2.75e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 25 GKVHSVQEQFFVAKG--PKAKIGD-VCF-VGEHNVLCEVIAIEKENNMLLPFEQTEKVCYGDsvtlvsedVVVPRGNHLL 100
Cdd:PRK06002 28 GTVSEVTASHYRVRGlsRFVRLGDfVAIrADGGTHLGEVVRVDPDGVTVKPFEPRIEIGLGD--------AVFRKGPLRI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 101 GKVLSANGEVLNEEAENI----PLQK------IKLDAPPihAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVG 170
Cdd:PRK06002 100 RPDPSWKGRVINALGEPIdglgPLAPgtrpmsIDATAPP--AMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 171 KSTLLGMIAKNAKADINVISLVGERGREVKDFIRKELGEEgMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNV 250
Cdd:PRK06002 178 KSTLLAMLARADAFDTVVIALVGERGREVREFLEDTLADN-LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 251 LLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSG--KTQKGSITGIYTVLVDGDDLNGPVPDLARGIL 327
Cdd:PRK06002 257 LLIVDSVTRFAHAAREVALAAGEPPVArGYPPSVFSELPRLLERAGpgAEGGGSITGIFSVLVDGDDHNDPVADSIRGTL 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1261856570 328 DGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKE 380
Cdd:PRK06002 337 DGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEE 389
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
17-430 |
7.59e-97 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 297.19 E-value: 7.59e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 17 ETPLYTKVGKVHSVQEQFFVAKGPKAKIGDVCFV---GEHNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLVSEDVVV 93
Cdd:PRK07196 11 NIHLARVAGRLVRVTGLLLESVGCRLAIGQRCRIesvDETFIEAQVVGFDRDITYLMPFKHPGGVLGGARVFPSEQDGEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 94 PRGNHLLGKVLSANGEVLNEEAE---NIPLQKiklDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVG 170
Cdd:PRK07196 91 LIGDSWLGRVINGLGEPLDGKGQlggSTPLQQ---QLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 171 KSTLLGMIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNV 250
Cdd:PRK07196 168 KSVLLGMITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 251 LLMMDSVTRFADARRSVDIAVKELP-IGGKTLLMESYMKKLLERSGKTQ-KGSITGIYTVLVDGDDLNGPVPDLARGILD 328
Cdd:PRK07196 248 LLLVDSLTRYAMAQREIALSLGEPPaTKGYPPSAFSIIPRLAESAGNSSgNGTMTAIYTVLAEGDDQQDPIVDCARAVLD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 329 GHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENELYFKLGTIQENEENAyIFECKNKVEG 408
Cdd:PRK07196 328 GHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVAGADPM-ADQAVHYYPA 406
|
410 420
....*....|....*....|..
gi 1261856570 409 INTFLKQGRSDSFQFDDIVEAI 430
Cdd:PRK07196 407 ITQFLRQEVGHPALFSASVEQL 428
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
37-381 |
2.18e-96 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 296.69 E-value: 2.18e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 37 AKGPKAKIGDVCFVGEHN------VLCEVIAIEKENNMLLPFEQTEKVCYGDSV---TLVSEDVV----VPRGNHLLGKV 103
Cdd:PRK07960 41 ATGLQLPLGATCVIERQNgsetheVESEVVGFNGQRLFLMPLEEVEGILPGARVyarNISGEGLQsgkqLPLGPALLGRV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 104 LSANGEVLN-----EEAENIPLQkikldAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMI 178
Cdd:PRK07960 121 LDGSGKPLDglpapDTGETGALI-----TPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMM 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 179 AKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVT 258
Cdd:PRK07960 196 ARYTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLT 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 259 RFADARRSVDIAVKELP-IGGKTLLMESYMKKLLERSGK--TQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKR 335
Cdd:PRK07960 276 RYAMAQREIALAIGEPPaTKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSR 355
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1261856570 336 ELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKEN 381
Cdd:PRK07960 356 RLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLLSSFQRN 401
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
93-355 |
4.03e-83 |
|
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: 256.23 E-value: 4.03e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 93 VPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKS 172
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 173 TLLGMIAKN---AKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNN 249
Cdd:cd19476 82 VLAMQLARNqakAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 250 VLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSG--KTQKGSITGIYTVLVDGDDLNGPVPDLARGI 326
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGReGYPPYLFTKLATLYERAGkvKDGGGSITAIPAVSTPGDDLTDPIPDNTFAI 241
|
250 260
....*....|....*....|....*....
gi 1261856570 327 LDGHIVLKRELATLSHYPAISVLDSVSRI 355
Cdd:cd19476 242 LDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
21-434 |
5.28e-73 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 235.57 E-value: 5.28e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 21 YTKVGKVHSVQEQFFVAKGPKAKIGDVCFVG---EHNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLVSEDVVVPRGN 97
Cdd:PRK05922 17 YRECGLLSRVSGNLLEAQGLSACLGELCQISlskSPPILAEVIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 98 HLLGKVLSANGEVLNEEaENIPLQKIK-LDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLG 176
Cdd:PRK05922 97 HLLGRVLDGFGNPLDGK-EQLPKTHLKpLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 177 MIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDS 256
Cdd:PRK05922 176 TIAKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 257 VTRFADARRSVDIAVkelpigGKTLLMESY-------MKKLLERSGKTQKGSITGIYTVLVDGddlNGP--VPDLARGIL 327
Cdd:PRK05922 256 LSRWIAALQEVALAR------GETLSAHHYaasvfhhVSEFTERAGNNDKGSITALYAILHYP---NHPdiFTDYLKSLL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 328 DGHIVLKRELATLSHyPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENELYFKLGTIQENEEnAYIFECKNKVE 407
Cdd:PRK05922 327 DGHFFLTPQGKALAS-PPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGAYVPGQD-AHLDRAVKLLP 404
|
410 420
....*....|....*....|....*..
gi 1261856570 408 GINTFLKQGRSDSFQFDDIVEAIHHIV 434
Cdd:PRK05922 405 SIKQFLSQPLSSYCALHNTLKQLEALL 431
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
75-415 |
4.61e-48 |
|
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: 170.67 E-value: 4.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 75 TEKVCYGDSVTLVSEDVVVPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLT 154
Cdd:TIGR01039 60 TDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 155 IGIGQKIGIFAGSGVGKSTLL-GMIAKNAKAD--INVISLVGERGREVKDFIRkELGEEG-MRKSVVVVATSDESHLMQL 230
Cdd:TIGR01039 140 YAKGGKIGLFGGAGVGKTVLIqELINNIAKEHggYSVFAGVGERTREGNDLYH-EMKESGvIDKTALVYGQMNEPPGARM 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 231 RAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVKELP--IGGK-TLLMEsyMKKLLERSGKTQKGSITGIY 306
Cdd:TIGR01039 219 RVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPsaVGYQpTLATE--MGELQERITSTKTGSITSVQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 307 TVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPHHWQLANEMRKILSIYKE-NELY 384
Cdd:TIGR01039 297 AVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVGEEHYDVARGVQQILQRYKElQDII 376
|
330 340 350
....*....|....*....|....*....|.
gi 1261856570 385 FKLGTIQENEENAYIFECKNKVEginTFLKQ 415
Cdd:TIGR01039 377 AILGMDELSEEDKLTVERARRIQ---RFLSQ 404
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
93-358 |
7.25e-44 |
|
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: 154.68 E-value: 7.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 93 VPRGNHLLGKVLSANGEVLNEEAeniPLQKIKLDapPIH----AFEREEI-TDVFETGIKSIDSMLTIGIGQKIGIFAGS 167
Cdd:cd01133 2 VPVGEETLGRIFNVLGEPIDERG---PIKAKERW--PIHreapEFVELSTeQEILETGIKVVDLLAPYAKGGKIGLFGGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 168 GVGKSTLL-GMIAKNAKAD--INVISLVGERGREVKDFIR--KELG---EEGMRKSVVVVATSDESHLMQLRAAKLATSI 239
Cdd:cd01133 77 GVGKTVLImELINNIAKAHggYSVFAGVGERTREGNDLYHemKESGvinLDGLSKVALVYGQMNEPPGARARVALTGLTM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 240 AEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPIGG---KTLLMEsyMKKLLERSGKTQKGSITGIYTVLVDGDDL 315
Cdd:cd01133 157 AEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVgyqPTLATE--MGSLQERITSTKKGSITSVQAVYVPADDL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1261856570 316 NGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEE 358
Cdd:cd01133 235 TDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
93-380 |
1.28e-42 |
|
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: 156.02 E-value: 1.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 93 VPRGNHLLGKVLSANGEVLNEEAeniPLQKIKLDapPIH----AFEREEI-TDVFETGIKSIDSMLTIGIGQKIGIFAGS 167
Cdd:COG0055 81 VPVGEATLGRIFNVLGEPIDGKG---PIEAKERR--PIHrpapPFEEQSTkTEILETGIKVIDLLAPYAKGGKIGLFGGA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 168 GVGKsTLLGM-----IAKNAKAdINVISLVGERGREVKDFIRkELGEEG-MRKSVVVVATSDESHLMQLRAAKLATSIAE 241
Cdd:COG0055 156 GVGK-TVLIMelihnIAKEHGG-VSVFAGVGERTREGNDLYR-EMKESGvLDKTALVFGQMNEPPGARLRVALTALTMAE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 242 YFRD-QGNNVLLMMDSVTRFADARRSVdiavkelpiggKTLL--MES---Y-------MKKLLERSGKTQKGSITGIYTV 308
Cdd:COG0055 233 YFRDeEGQDVLLFIDNIFRFTQAGSEV-----------SALLgrMPSavgYqptlateMGALQERITSTKKGSITSVQAV 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261856570 309 LVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPHHWQLANEMRKILSIYKE 380
Cdd:COG0055 302 YVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDpLIVGEEHYRVAREVQRILQRYKE 374
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
52-380 |
1.02e-39 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 148.65 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 52 EHNVLCEVIAIEKENNM-LLPFEQTEKVCYGDSVTLVSEDVVVPRGNHLLGKVLSANGEVLNEeaenipLQKIKLDA-PP 129
Cdd:CHL00060 54 EINVTCEVQQLLGNNRVrAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDN------LGPVDTRTtSP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 130 IH----AFEREEIT-DVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKsTLLGM-----IAKnAKADINVISLVGERGREV 199
Cdd:CHL00060 128 IHrsapAFIQLDTKlSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK-TVLIMelinnIAK-AHGGVSVFGGVGERTREG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 200 KDfIRKELGEEGM--------RKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGN-NVLLMMDSVTRFADARRSVDIA 270
Cdd:CHL00060 206 ND-LYMEMKESGVineqniaeSKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSAL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 271 VKELP--IGGK-TLLMEsyMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAIS 347
Cdd:CHL00060 285 LGRMPsaVGYQpTLSTE--MGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 362
|
330 340 350
....*....|....*....|....*....|....
gi 1261856570 348 VLDSVSRIME-EIVSPHHWQLANEMRKILSIYKE 380
Cdd:CHL00060 363 PLDSTSTMLQpRIVGEEHYETAQRVKQTLQRYKE 396
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
87-356 |
1.48e-39 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 143.13 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 87 VSEDvvvprgnhLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAG 166
Cdd:cd01135 6 VSED--------MLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 167 SGVGKSTLLGMIAKNAK------ADINVISLVGERGREVKdFIRKELGEEG-MRKSVVVVATSDESHLMQLRAAKLATSI 239
Cdd:cd01135 78 SGLPHNELAAQIARQAGvvgseeNFAIVFAAMGVTMEEAR-FFKDDFEETGaLERVVLFLNLANDPTIERIITPRMALTT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 240 AEYFR-DQGNNVLLMMDSVTRFADARRSVDIAVKELPiG--GKTLLMESYMKKLLERSGKTQ--KGSITGIYTVLVDGDD 314
Cdd:cd01135 157 AEYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVP-GrrGYPGYMYTDLATIYERAGRVEgrKGSITQIPILTMPNDD 235
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1261856570 315 LNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIM 356
Cdd:cd01135 236 ITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLM 277
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
57-356 |
1.21e-31 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 125.71 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 57 CEVIAIEKENNMLLPFEQTEKVCYGDS-VTLVSEDVVVPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFER 135
Cdd:PRK04196 41 GQVLEVSEDKAVVQVFEGTTGLDLKDTkVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 136 EEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAK---ADIN---VISLVGERGREVkDFIRKELGE 209
Cdd:PRK04196 121 EYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIARQAKvlgEEENfavVFAAMGITFEEA-NFFMEDFEE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 210 EG-MRKSVVVVATSDESHLMQLRAAKLATSIAEYFR-DQGNNVLLMMDSVTRFADARRSVDIAVKELPiG--GKTLLMES 285
Cdd:PRK04196 200 TGaLERSVVFLNLADDPAIERILTPRMALTAAEYLAfEKGMHVLVILTDMTNYCEALREISAAREEVP-GrrGYPGYMYT 278
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261856570 286 YMKKLLERSG--KTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIM 356
Cdd:PRK04196 279 DLATIYERAGriKGKKGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLM 351
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
74-389 |
4.70e-31 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 124.64 E-value: 4.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 74 QTEKVCYGDSVTLVSEDVVVPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLD--APPIhaFEREEITDVFETGIKSIDS 151
Cdd:PRK13343 78 DTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLErpAPAI--IERDFVTEPLQTGIKVVDA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 152 MLTIGIGQKIGIFAGSGVGKSTllgmIAKNA---KADINVIS---LVGERGREVKDFIRKeLGEEG-MRKSVVVVATSDE 224
Cdd:PRK13343 156 LIPIGRGQRELIIGDRQTGKTA----IAIDAiinQKDSDVICvyvAIGQKASAVARVIET-LREHGaLEYTTVVVAEASD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 225 SHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELPigGKtllmESY-------MKKLLERSGKT 297
Cdd:PRK13343 231 PPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPP--GR----EAYpgdifylHSRLLERAAKL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 298 QK----GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRK 373
Cdd:PRK13343 305 SPelggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRL 384
|
330
....*....|....*.
gi 1261856570 374 ILSIYKENELYFKLGT 389
Cdd:PRK13343 385 DYAQFLELEAFTRFGG 400
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
93-355 |
5.21e-27 |
|
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: 109.19 E-value: 5.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 93 VPRGNHLLGKVLSANGEVLN-----EEAENIPLQKIkldAPPIhaFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGS 167
Cdd:cd01132 4 VPVGEALLGRVVDALGNPIDgkgpiQTKERRRVESK---APGI--IPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 168 GVGKSTLL--GMIAKNAKADINVISLVGERGREVKDfIRKELGEEG-MRKSVVVVATSDESHLMQLRAAKLATSIAEYFR 244
Cdd:cd01132 79 QTGKTAIAidTIINQKGKKVYCIYVAIGQKRSTVAQ-IVKTLEEHGaMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 245 DQGNNVLLMMDSVTRFADARRSVDIAVKELPigGKtllmESY-------MKKLLERSGKTQK----GSITGIYTVLVDGD 313
Cdd:cd01132 158 DNGKHALIIYDDLSKQAVAYRQMSLLLRRPP--GR----EAYpgdvfylHSRLLERAAKLSDelggGSLTALPIIETQAG 231
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1261856570 314 DLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRI 355
Cdd:cd01132 232 DVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRV 273
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
81-357 |
8.45e-25 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 105.96 E-value: 8.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 81 GDSV-TLVSEDvvvprgnhLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQ 159
Cdd:TIGR01040 71 GDILrTPVSED--------MLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 160 KIGIFAGSGVGKSTLLGMIAKNAkadinviSLVGERGREVKD---------------------FIRKELGEEG-MRKSVV 217
Cdd:TIGR01040 143 KIPIFSAAGLPHNEIAAQICRQA-------GLVKLPTKDVHDghednfaivfaamgvnmetarFFKQDFEENGsMERVCL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 218 VVATSDESHLMQLRAAKLATSIAEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPiG--GKTLLMESYMKKLLERS 294
Cdd:TIGR01040 216 FLNLANDPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVP-GrrGFPGYMYTDLATIYERA 294
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261856570 295 GKTQ--KGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME 357
Cdd:TIGR01040 295 GRVEgrNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMK 359
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
20-380 |
2.24e-24 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 104.35 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 20 LYTKV----GKVHSVQeqffvAKGPKakIGDVCFVGEHN--VLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLVSEDVVV 93
Cdd:PRK02118 4 IYTKItditGNVITVE-----AEGVG--YGELATVERKDgsSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 94 PRGNHLLGKVLSANGEVLNEEAEnIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST 173
Cdd:PRK02118 77 TYSESLLGRRFNGSGKPIDGGPE-LEGEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 174 LLGMIAKNAKADINVIslvGERGREVKD--FIRKELGEEG-MRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGN-N 249
Cdd:PRK02118 156 LLARIALQAEADIIIL---GGMGLTFDDylFFKDTFENAGaLDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGKkK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 250 VLLMMDSVTRFADARRSVDIAVKELPigGKTLLMESYMKKLLERSGKT----QKGSITGIYTVLVDGDDLNGPVPDLARG 325
Cdd:PRK02118 233 VLVLLTDMTNFADALKEISITMDQIP--SNRGYPGSLYSDLASRYEKAvdfeDGGSITIIAVTTMPGDDVTHPVPDNTGY 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1261856570 326 ILDGHIVLKRElatlshypAISVLDSVSRIMEEIVSPH----HWQLANEMRKILSIYKE 380
Cdd:PRK02118 311 ITEGQFYLRRG--------RIDPFGSLSRLKQLVIGKKtredHGDLMNAMIRLYADSRE 361
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
134-354 |
5.13e-24 |
|
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.
Pssm-ID: 410878 [Multi-domain] Cd Length: 288 Bit Score: 101.11 E-value: 5.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 134 EREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREVKDFIRK--EL---- 207
Cdd:cd01134 52 EKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEVLEEfpELkdpi 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 208 -GEEGMRKSVVVVATSDeshlMQL--RAAKLAT--SIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP------- 275
Cdd:cd01134 132 tGESLMERTVLIANTSN----MPVaaREASIYTgiTIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPaeegypa 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 276 -IGGKtlLMESYmkkllERSGKTQ-------KGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAIS 347
Cdd:cd01134 208 yLGAR--LAEFY-----ERAGRVRclgspgrEGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSIN 280
|
....*..
gi 1261856570 348 VLDSVSR 354
Cdd:cd01134 281 WLISYSK 287
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
129-383 |
6.03e-22 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 98.32 E-value: 6.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 129 PIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREVKDFIRK--E 206
Cdd:PRK04192 198 PRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQLAKWADADIVIYVGCGERGNEMTEVLEEfpE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 207 L-----GEEGMRKSVVVVATSDeshlMQLrAAK-----LATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELPi 276
Cdd:PRK04192 278 LidpktGRPLMERTVLIANTSN----MPV-AAReasiyTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMP- 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 277 gGK--------TLLMESYmkkllERSGKTQ-----KGSITGIYTVLVDGDDLNGPVPD--LArgildghIV-----LKRE 336
Cdd:PRK04192 352 -GEegypaylaSRLAEFY-----ERAGRVKtlggeEGSVTIIGAVSPPGGDFSEPVTQntLR-------IVkvfwaLDAE 418
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1261856570 337 LATLSHYPAISVLDS-------VSRIMEEIVSPHHWQLANEMRKILsiYKENEL 383
Cdd:PRK04192 419 LADRRHFPAINWLTSyslyldqVAPWWEENVDPDWRELRDEAMDLL--QREAEL 470
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
360-429 |
3.79e-17 |
|
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: 75.55 E-value: 3.79e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 360 VSPHHWQLANEMRKILSIYKENELYFKLGTIQENeENAYIFECKNKVEGINTFLKQGRSDSFQFDDIVEA 429
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIGAYQAG-SDPEIDEAIAKRPAINAFLRQGVDEPVSFEETLAQ 69
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
149-382 |
1.30e-16 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 79.17 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 149 IDSMLTIGIGQKIGIFAGSGVGKSTLLGMIA----KNAKADINVISLVGERGREVKDFIRKELGEegmrksvVVVATSDE 224
Cdd:cd01128 7 IDLIAPIGKGQRGLIVAPPKAGKTTLLQNIAnaiaKNHPEVELIVLLIDERPEEVTDMRRSVKGE-------VVASTFDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 225 SHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDiavkelPIGGKTLL--MES---YMKKLLERSGKTQK 299
Cdd:cd01128 80 PPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVV------PSSGKTLSggVDAnalHKPKRFFGAARNIE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 300 --GSITGIYTVLVD-GDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILS 376
Cdd:cd01128 154 egGSLTIIATALVDtGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTRKEELLLTPEELQKIWLLRRILS 233
|
....*.
gi 1261856570 377 IYKENE 382
Cdd:cd01128 234 PMDPIE 239
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
81-355 |
6.78e-16 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 79.62 E-value: 6.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 81 GDSVTLVSEDVVVPRGNHLLGKVLSANGEVLNEEAENIPLQK--IKLDAPPIhaFEREEITDVFETGIKSIDSMLTIGIG 158
Cdd:CHL00059 64 GSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESrlIESPAPGI--ISRRSVYEPLQTGLIAIDSMIPIGRG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 159 QKIGIFAGSGVGKS-----TLLGMIAKNAkadINVISLVGERGREVKDfIRKELGEEG-MRKSVVVVATSDESHLMQLRA 232
Cdd:CHL00059 142 QRELIIGDRQTGKTavatdTILNQKGQNV---ICVYVAIGQKASSVAQ-VVTTLQERGaMEYTIVVAETADSPATLQYLA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 233 AKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELPigGKtllmESY-------MKKLLERSGKTQK----GS 301
Cdd:CHL00059 218 PYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPP--GR----EAYpgdvfylHSRLLERAAKLSSqlgeGS 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1261856570 302 ITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRI 355
Cdd:CHL00059 292 MTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRV 345
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
87-397 |
8.61e-16 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 78.59 E-value: 8.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 87 VSEDVVVPR-GNHLLGKVLSANGEVLNEEAENIPLQkiklDAPPIHAFER-EEITDVFETGIKSIDSMLTIGIGQKIGIF 164
Cdd:PRK12608 64 VVEGVARPReRYRVLVRVDSVNGTDPEKLARRPHFD----DLTPLHPRERlRLETGSDDLSMRVVDLVAPIGKGQRGLIV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 165 AGSGVGKSTLLGMIAK---NAKADINVIS-LVGERGREVKDFIRKELGEegmrksvVVVATSDESHLMQLRAAKLATSIA 240
Cdd:PRK12608 140 APPRAGKTVLLQQIAAavaANHPEVHLMVlLIDERPEEVTDMRRSVKGE-------VYASTFDRPPDEHIRVAELVLERA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 241 EYFRDQGNNVLLMMDSVTRFADARRSvdiavkELPIGGKTL---LMESYM---KKLLERSGKTQK-GSITGIYTVLVD-G 312
Cdd:PRK12608 213 KRLVEQGKDVVILLDSLTRLARAYNN------EVESSGRTLsggVDARALqrpKRLFGAARNIEEgGSLTIIATALVDtG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 313 DDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENE-LYFKLGTIQ 391
Cdd:PRK12608 287 SRMDEVIFEEFKGTGNMEIVLDRELADKRVFPAIDIAKSGTRREELLLDSKELEKVRRLRRALASRKPVEaMEALLEKLR 366
|
....*.
gi 1261856570 392 ENEENA 397
Cdd:PRK12608 367 ETPDNA 372
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
81-354 |
1.65e-15 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 78.18 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 81 GDSVTLVSEDVVVPRGNHLLGKVLSANGEVLN-----EEAENIPLQKIkldAPPIhaFEREEITDVFETGIKSIDSMLTI 155
Cdd:PRK09281 85 GDTVKRTGRILEVPVGEALLGRVVNPLGQPIDgkgpiEATETRPVERK---APGV--IDRKSVHEPLQTGIKAIDAMIPI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 156 GIGQKIGIFAGSGVGKSTllgmIAK----NAKaDINVISL---VGERGREVKDFIRKeLGEEG-MRKSVVVVATSDESHL 227
Cdd:PRK09281 160 GRGQRELIIGDRQTGKTA----IAIdtiiNQK-GKDVICIyvaIGQKASTVAQVVRK-LEEHGaMEYTIVVAATASDPAP 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 228 MQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVdiavkelpiggkTLLM------ESY-------MKKLLERS 294
Cdd:PRK09281 234 LQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQL------------SLLLrrppgrEAYpgdvfylHSRLLERA 301
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1261856570 295 GKTQK----GSITG---IYTvlvDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSR 354
Cdd:PRK09281 302 AKLSDelggGSLTAlpiIET---QAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSR 365
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
100-395 |
2.68e-15 |
|
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: 77.42 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 100 LGKVLSANGEVLNEEAENIPLQKIKldapPIHAFER---EEITDVFETGIksIDSMLTIGIGQKIGIFAGSGVGKSTLLG 176
Cdd:TIGR00767 113 LLKVESVNGDDPEKAKNRVLFENLT----PLYPNERlrlETSTEDLSTRV--LDLFAPIGKGQRGLIVAPPKAGKTVLLQ 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 177 MIAkNAKADIN-----VISLVGERGREVKDFIRKELGEegmrksvVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVL 251
Cdd:TIGR00767 187 KIA-QAITRNHpevelIVLLIDERPEEVTDMQRSVKGE-------VVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 252 LMMDSVTRFADARRSVdiavkeLPIGGKTLL--MESymkKLLERSGK--------TQKGSITGIYTVLVD-GDDLNGPVP 320
Cdd:TIGR00767 259 ILLDSITRLARAYNTV------TPASGKVLSggVDA---NALHRPKRffgaarniEEGGSLTIIATALIDtGSRMDEVIF 329
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261856570 321 DLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENE----LYFKLGTIQENEE 395
Cdd:TIGR00767 330 EEFKGTGNMELHLDRKLADRRIFPAIDIKKSGTRKEELLLTPEELQKIWVLRKIISPMDSIEamefLISKLKKTKTNEE 408
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
178-392 |
8.32e-15 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 76.98 E-value: 8.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 178 IAKNAKADINVISLVGERGREVKDFIRK-------ELGEEGMRKSVVVVATSDEShlMQLRAAKLAT--SIAEYFRDQGN 248
Cdd:PRK14698 676 LAKWSDAQVVIYIGCGERGNEMTDVLEEfpklkdpKTGKPLMERTVLIANTSNMP--VAAREASIYTgiTIAEYFRDMGY 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 249 NVLLMMDSVTRFADARRSVDIAVKELP-IGGKTLLMESYMKKLLERSGKT-------QKGSITGIYTVLVDGDDLNGPVP 320
Cdd:PRK14698 754 DVALMADSTSRWAEALREISGRLEEMPgEEGYPAYLASKLAEFYERAGRVvtlgsdyRVGSVSVIGAVSPPGGDFSEPVV 833
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261856570 321 DLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSiyKENELYFKLGTIQE 392
Cdd:PRK14698 834 QNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNVDPEWKAMRD--KAMELLQKEAELQE 903
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
59-380 |
1.62e-14 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 75.46 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 59 VIAIEKENNM-LLPFEQTEKVCYGDSVTLVSEDVVVPRGNHLLGKVLSANGE------------VLNEEAEnipLQKIKL 125
Cdd:PTZ00185 82 VFNLEKDGRIgIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHevpvglltrsraLLESEQT---LGKVDA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 126 DAPPIhaFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGK-----STLLGMIAKNAK-----ADINVISLVGER 195
Cdd:PTZ00185 159 GAPNI--VSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKtsiavSTIINQVRINQQilsknAVISIYVSIGQR 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 196 GREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP 275
Cdd:PTZ00185 237 CSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 276 ----IGGKTLLMESymkKLLERSGKTQK----GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAIS 347
Cdd:PTZ00185 317 greaYPGDVFYLHS---RLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVN 393
|
330 340 350
....*....|....*....|....*....|...
gi 1261856570 348 VLDSVSRIMEEIVSPHHWQLANEMRKILSIYKE 380
Cdd:PTZ00185 394 IGLSVSRVGSSAQNVAMKAVAGKLKGILAEYRK 426
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
31-387 |
2.92e-14 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 74.62 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 31 QEQFFVAKGPKakigdvcfvgehNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLVSEDVVVPRGNHLLGKVLSANGEV 110
Cdd:PRK07165 23 QNQFFTLKNNP------------NVKAFVISATEDKAYLLINNEKGKIKINDELIELNNTNKVKTSKEYFGKIIDIDGNI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 111 L-NEEAENIPLQKIKLDAPPI----HAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTL-LGMIAKNAKA 184
Cdd:PRK07165 91 IyPEAQNPLSKKFLPNTSSIFnlahGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIaLNTIINQKNT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 185 DINVISL-VGERGREVKdFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFrDQGNNVLLMMDSVTRFADA 263
Cdd:PRK07165 171 NVKCIYVaIGQKRENLS-RIYETLKEHDALKNTIIIDAPSTSPYEQYLAPYVAMAHAENI-SYNDDVLIVFDDLTKHANI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 264 RRSVDIAVKElPIGGKTllMESYM----KKLLERSGK-TQKGSITGIYTV-LVDGDdLNGPVPDLARGILDGHIVLKREL 337
Cdd:PRK07165 249 YREIALLTNK-PVGKEA--FPGDMffahSKLLERAGKfKNRKTITALPILqTVDND-ITSLISSNIISITDGQIVTSSDL 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1261856570 338 ATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRKILSIYKENELYFKL 387
Cdd:PRK07165 325 FASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSML 374
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
102-395 |
8.04e-10 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 60.54 E-value: 8.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 102 KVLSANGEVLnEEAENIPL----------QKIKLdappihafEREEITDVfETGIksIDSMLTIGIGQKIGIFAGSGVGK 171
Cdd:PRK09376 115 KVETVNGEDP-EKARNRPLfenltplypnERLRL--------ETGNPEDL-STRI--IDLIAPIGKGQRGLIVAPPKAGK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 172 STLLGMIA----KNAKaDINVIS-LVGERGREVKDfirkelgeegMRKSV---VVVATSDESHLMQLRAAKLATSIAEYF 243
Cdd:PRK09376 183 TVLLQNIAnsitTNHP-EVHLIVlLIDERPEEVTD----------MQRSVkgeVVASTFDEPAERHVQVAEMVIEKAKRL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 244 RDQGNNVLLMMDSVTRFADARRSVdiavkeLPIGGKTLlmesymkkllerSG--------KTQK-----------GSITG 304
Cdd:PRK09376 252 VEHGKDVVILLDSITRLARAYNTV------VPSSGKVL------------SGgvdanalhRPKRffgaarnieegGSLTI 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 305 IYTVLVDG----DDLngpvpdlargI---LDG----HIVLKRELATLSHYPAISVLDSVSRIMEEIVSPHHWQLANEMRK 373
Cdd:PRK09376 314 IATALIDTgsrmDEV----------IfeeFKGtgnmELHLDRKLAEKRIFPAIDINRSGTRKEELLLSPEELQKVWILRK 383
|
330 340
....*....|....*....|....*.
gi 1261856570 374 ILSIYKENE----LYFKLGTIQENEE 395
Cdd:PRK09376 384 ILSPMDEVEamefLLDKLKKTKTNEE 409
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
158-337 |
4.37e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 49.29 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 158 GQKIGIFAGSGVGKSTLLGMIAKNAKAD-INVISLVGERGREVKDFIRKELGEEGmrksvvvvatsDESHLMQLRAAKLA 236
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPgGGVIYIDGEDILEEVLDQLLLIIVGG-----------KKASGSGELRLRLA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 237 TSIAEYFRdqgnNVLLMMDSVTRFADARRSVDIavkelpiggkTLLMESYMKKLLERSGKTqkgsitgiyTVLVDGDDLN 316
Cdd:smart00382 71 LALARKLK----PDVLILDEITSLLDAEQEALL----------LLLEELRLLLLLKSEKNL---------TVILTTNDEK 127
|
170 180
....*....|....*....|.
gi 1261856570 317 GPVPDLARGILDGHIVLKREL 337
Cdd:smart00382 128 DLGPALLRRRFDRRIVLLLIL 148
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
114-197 |
6.29e-05 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 43.30 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 114 EAENIP----LQKIKLDAPPIHAFEREEI-----TDVFETGIKSIDSMLTIG--IGQKIGIFAG-SGVGKSTLLGMIAKN 181
Cdd:pfam03193 50 EASGIEpvivLNKIDLLDEEEELEELLKIyraigYPVLFVSAKTGEGIEALKelLKGKTTVLAGqSGVGKSTLLNALLPE 129
|
90
....*....|....*.
gi 1261856570 182 AKADINVISLVGERGR 197
Cdd:pfam03193 130 LDLRTGEISEKLGRGR 145
|
|
| ATP-synt_flagellum-secretory_path_III_C |
cd18114 |
Flagellum-specific ATP synthase, C-terminal domain; The C-terminal domain of the ... |
364-429 |
1.89e-04 |
|
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: 39.51 E-value: 1.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261856570 364 HWQLANEMRKILSIYKENELYFKLGtiqeneenAY-------IFECKNKVEGINTFLKQGRSDSFQFDDIVEA 429
Cdd:cd18114 1 HYLAARKFRELMSTYQENEDLIRIG--------AYkkgsdpeVDEAIRLKPQIEAFLKQGLNEKAPLEESLQQ 65
|
|
| TIGR00157 |
TIGR00157 |
ribosome small subunit-dependent GTPase A; Members of this protein were designated YjeQ and ... |
55-197 |
1.93e-04 |
|
ribosome small subunit-dependent GTPase A; Members of this protein were designated YjeQ and are now designated RsgA (ribosome small subunit-dependent GTPase A). The strongest motif in the alignment of these proteins is GXSGVGKS[ST], a classic P-loop for nucleotide binding. This protein has been shown to cleave GTP and remain bound to GDP. A role as a regulator of translation has been suggested. The Aquifex aeolicus ortholog is split into consecutive open reading frames. Consequently, this model was build in fragment mode (-f option). [Protein synthesis, Translation factors]
Pssm-ID: 272934 [Multi-domain] Cd Length: 245 Bit Score: 42.79 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 55 VLCEVIAiEKENNMLLPfeqteKVCYGDSVTLVSEDVVVPRGNHLLGKVLsangeVLNEEAENIPL----QKIKLDAPPI 130
Cdd:TIGR00157 17 VYGGAIA-ERKNELTRP-----IVANIDQIVIVSSAVLPELSLNQLDRFL-----VVAEAQNIEPIivlnKIDLLDDEDM 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261856570 131 HAFEREEITD----VFETGIKSIDSMLTI--GIGQKIGIFAG-SGVGKSTLLGMIAKNAKADINVISLVGERGR 197
Cdd:TIGR00157 86 EKEQLDIYRNigyqVLMTSSKNQDGLKELieALQNRISVFAGqSGVGKSSLINALDPSVKQQVNDISSKLGLGK 159
|
|
| ATP-synt_flagellum-secretory_path_III_N |
cd18117 |
Flagellum-specific ATP synthase, N-terminal domain; The N-terminal domain of the ... |
37-75 |
2.22e-04 |
|
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: 39.43 E-value: 2.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1261856570 37 AKGPKAKIGDVCFV---GEHNVLCEVIAIEKENNMLLPFEQT 75
Cdd:cd18117 15 AVGPQAPIGELCLIetaDGLSILAEVVGFSGEKVLLMPLGEL 56
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
153-208 |
3.50e-04 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 41.14 E-value: 3.50e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1261856570 153 LTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREVKDFIRKELG 208
Cdd:cd03247 23 LELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLIS 78
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
157-197 |
4.52e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 41.23 E-value: 4.52e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1261856570 157 IGQKIGIFAG-SGVGKSTLLGMIAKNAKADINVISLVGERGR 197
Cdd:cd01854 83 LKGKTSVLVGqSGVGKSTLLNALLPELVLATGEISEKLGRGR 124
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
157-197 |
4.52e-04 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 42.02 E-value: 4.52e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1261856570 157 IGQKIGIFAG-SGVGKSTLLGMIAKNAKADINVISLVGERGR 197
Cdd:COG1162 164 LKGKTSVLVGqSGVGKSTLINALLPDADLATGEISEKLGRGR 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
153-219 |
9.55e-04 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 39.55 E-value: 9.55e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1261856570 153 LTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLvgeRGREVKDFIRKELgeegmRKSVVVV 219
Cdd:pfam00005 6 LTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILL---DGQDLTDDERKSL-----RKEIGYV 64
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
153-219 |
1.52e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 40.96 E-value: 1.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1261856570 153 LTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLvgeRGREVKDFirkelGEEGMRKSVVVV 219
Cdd:PRK11160 361 LQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL---NGQPIADY-----SEAALRQAISVV 419
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
144-349 |
4.33e-03 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 38.36 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 144 TGIKSIDSMLTIGI--GQKIGIFAGSGVGKSTLLGMIAKNAKADinvislvGERG-----REVKDFIRKELGEEGM---- 212
Cdd:COG0467 4 TGIPGLDELLGGGLprGSSTLLSGPPGTGKTTLALQFLAEGLRR-------GEKGlyvsfEESPEQLLRRAESLGLdlee 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 213 ---RKSVVVVATSDEShlMQLRAAKLATSIAEYFRDQGNNVlLMMDSVTRFADARRSVDIAVKELpiggktllmeSYMKK 289
Cdd:COG0467 77 yieSGLLRIIDLSPEE--LGLDLEELLARLREAVEEFGAKR-VVIDSLSGLLLALPDPERLREFL----------HRLLR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 290 LLERSGktqkgsITGIYTVLVDGDDLNGPVPDLARgILDGHIVLKRELATLSHYPAISVL 349
Cdd:COG0467 144 YLKKRG------VTTLLTSETGGLEDEATEGGLSY-LADGVILLRYVELGGELRRALSVL 196
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
147-179 |
6.23e-03 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 38.18 E-value: 6.23e-03
10 20 30
....*....|....*....|....*....|...
gi 1261856570 147 KSIDsmLTIGIGQKIGIFAGSGVGKSTLLGMIA 179
Cdd:COG4181 29 KGIS--LEVEAGESVAIVGASGSGKSTLLGLLA 59
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
153-179 |
6.97e-03 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 37.81 E-value: 6.97e-03
10 20
....*....|....*....|....*..
gi 1261856570 153 LTIGIGQKIGIFAGSGVGKSTLLGMIA 179
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIA 46
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
100-194 |
7.08e-03 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 38.81 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261856570 100 LGKVLSANGEVLNEEAEniplqkikLDAPPIHAFEREEITDVFETGIKSIDSM-LTIGIGQKIGIFAGSGVGKSTLLGMI 178
Cdd:TIGR02857 297 LFAVLDAAPRPLAGKAP--------VTAAPASSLEFSGVSVAYPGRRPALRPVsFTVPPGERVALVGPSGAGKSTLLNLL 368
|
90
....*....|....*.
gi 1261856570 179 AKNAKADINVISLVGE 194
Cdd:TIGR02857 369 LGFVDPTEGSIAVNGV 384
|
|
| |
