|
Name |
Accession |
Description |
Interval |
E-value |
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
35-453 |
0e+00 |
|
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 695.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 35 SPVSVQGRVNHAVGQILNATGIRARLGEICELRTPNQPTLLAEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGREHVFPV 114
Cdd:COG1157 15 PPVRVSGRVTRVVGLLIEAVGPDASIGELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 115 GEGLFGRVLDGLGRPLDDRGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKSTLL 194
Cdd:COG1157 95 GDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 195 GMIARGAQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRVLLLVD 274
Cdd:COG1157 175 GMIARNTEADVNVIALIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 275 SLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGAHGSITALYTVLVEGDEESDPIAEEVRSILDGHIVLS 354
Cdd:COG1157 255 SLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAVRGILDGHIVLS 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 355 RKIALANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALRARDAIGAFCAQ 434
Cdd:COG1157 335 RKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENEDLIRIGAYQPGSDPELDEAIALIPAIEAFLRQ 414
|
410
....*....|....*....
gi 1409814734 435 ASDEDVRFDALLAKLTKLA 453
Cdd:COG1157 415 GMDERVSFEESLAQLAELL 433
|
|
| III_secr_ATP |
TIGR02546 |
type III secretion apparatus H+-transporting two-sector ATPase; [Protein fate, Protein and ... |
35-454 |
0e+00 |
|
type III secretion apparatus H+-transporting two-sector ATPase; [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274191 [Multi-domain] Cd Length: 422 Bit Score: 605.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 35 SPVSVQGRVNHAVGQILNATGIRARLGEICELRTPNQPTLLAEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGREHVFPV 114
Cdd:TIGR02546 1 QPVRVRGRVTEVSGTLLKAVLPGARVGELCLIRRRDPSQLLAEVVGFTGDEALLSPLGELHGISPGSEVIPTGRPLSIRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 115 GEGLFGRVLDGLGRPLDDRG--PVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKST 192
Cdd:TIGR02546 81 GEALLGRVLDGFGRPLDGKGelPAGEIETRPLDADPPPPMSRQPIDQPLPTGVRAIDGLLTCGEGQRIGIFAGAGVGKST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 193 LLGMIARGAQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRVLLL 272
Cdd:TIGR02546 161 LLGMIARGASADVNVIALIGERGREVREFIEHHLGEEGRKRSVLVVSTSDRPSLERLKAAYTATAIAEYFRDQGKRVLLM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 273 VDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGAHGSITALYTVLVEGDEESDPIAEEVRSILDGHIV 352
Cdd:TIGR02546 241 MDSLTRFARALREIGLAAGEPPARGGYPPSVFSSLPRLLERAGNGEKGSITALYTVLVEGDDMNDPIADEVRSILDGHIV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 353 LSRKIALANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALRARDAIGAFC 432
Cdd:TIGR02546 321 LSRALAERNHYPAIDVLASLSRVMSQVVSTEHRRAAGKLRRLLATYKEVELLIRLGEYQPGSDPETDDAIDKIDAIRAFL 400
|
410 420
....*....|....*....|..
gi 1409814734 433 AQASDEDVRFDALLAKLTKLAN 454
Cdd:TIGR02546 401 RQSTDEYSPYEETLEQLHALVA 422
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
35-454 |
0e+00 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 592.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 35 SPVSVQGRVNHAVGQILNATGIRARLGEICELRTPNQP-TLLAEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGREHVFP 113
Cdd:PRK06936 19 RLIQIRGRVTQVTGTILKAVVPGVRIGELCYLRNPDNSlSLQAEVIGFAQHQALLTPLGEMYGISSNTEVSPTGTMHQVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 114 VGEGLFGRVLDGLGRPLDDRGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKSTL 193
Cdd:PRK06936 99 VGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 194 LGMIARGAQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRVLLLV 273
Cdd:PRK06936 179 LASLIRSAEVDVTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 274 DSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGAHGSITALYTVLVEGDEESDPIAEEVRSILDGHIVL 353
Cdd:PRK06936 259 DSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIIL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 354 SRKIALANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALRARDAIGAFCA 433
Cdd:PRK06936 339 SRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIGEYQKGQDKEADQAIERIGAIRGFLR 418
|
410 420
....*....|....*....|.
gi 1409814734 434 QASDEDVRFDALLAKLTKLAN 454
Cdd:PRK06936 419 QGTHELSHFNETLNLLETLTQ 439
|
|
| FliI_clade2 |
TIGR03497 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
41-452 |
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: 573.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 41 GRVNHAVGQILNATGIRARLGEICELRTPNQPTLLAEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGREHVFPVGEGLFG 120
Cdd:TIGR03497 1 GKVTRVIGLTIESKGPKASIGELCSILTKGGKPVLAEVVGFKEENVLLMPLGEVEGIGPGSLVIATGRPLAIKVGKGLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 121 RVLDGLGRPLDDRGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKSTLLGMIARG 200
Cdd:TIGR03497 81 RVLDGLGRPLDGEGPIIGEEPYPLDNPPPNPLKRPRIRDPLETGIKAIDGLLTIGKGQRVGIFAGSGVGKSTLLGMIARN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 201 AQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRVLLLVDSLTRFA 280
Cdd:TIGR03497 161 AKADINVIALIGERGREVRDFIEKDLGEEGLKRSVVVVATSDQPALMRLKAAFTATAIAEYFRDQGKDVLLMMDSVTRFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 281 RAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGAHGSITALYTVLVEGDEESDPIAEEVRSILDGHIVLSRKIALA 360
Cdd:TIGR03497 241 MAQREIGLAVGEPPTTRGYTPSVFSLLPKLLERSGNSQKGSITGFYTVLVDGDDMNEPIADAVRGILDGHIVLSRELAAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 361 NRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALRARDAIGAFCAQASDEDV 440
Cdd:TIGR03497 321 NHYPAIDVLASVSRVMNEIVSEEHKELAGKLRELLAVYKEAEDLINIGAYKRGSNPKIDEAIRYIEKINSFLKQGIDEKF 400
|
410
....*....|..
gi 1409814734 441 RFDALLAKLTKL 452
Cdd:TIGR03497 401 TFEETVQLLKEL 412
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
22-455 |
0e+00 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 568.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 22 RLVGELDAGLAFFSPVSVQGRVNHAVGQILNATGIRARLGEICELRTPnQPTLL--AEVVGFSRQTTLLTPLGDVAGLSP 99
Cdd:PRK09099 7 RLADALERELAALPAVRRTGKVVEVIGTLLRVSGLDVTLGELCELRQR-DGTLLqrAEVVGFSRDVALLSPFGELGGLSR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 100 ETTVVPSGREHVFPVGEGLFGRVLDGLGRPLDDRGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQR 179
Cdd:PRK09099 86 GTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 180 VGIFAPSGVGKSTLLGMIARGAQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIA 259
Cdd:PRK09099 166 MGIFAPAGVGKSTLMGMFARGTQCDVNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 260 EHFRDAGKRVLLLVDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGAHGSITALYTVLVEGDEESDPI 339
Cdd:PRK09099 246 EYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 340 AEEVRSILDGHIVLSRKIALANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGD 419
Cdd:PRK09099 326 AEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVGEYRAGSDPVAD 405
|
410 420 430
....*....|....*....|....*....|....*.
gi 1409814734 420 LALRARDAIGAFCAQASDEDVRFDALLAKLTKLAND 455
Cdd:PRK09099 406 EAIAKIDAIRDFLSQRTDEYSDPDATLAALAELSGD 441
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
37-452 |
0e+00 |
|
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP synthase F1, beta subunit. It is a mixture of members with two different protein functions. The first group is exemplified by Salmonella typhimurium FliI protein. It is needed for flagellar assembly, its ATPase activity is required for flagellation, and it may be involved in a specialized protein export pathway that proceeds without signal peptide cleavage. The second group of proteins function in the export of virulence proteins; exemplified by Yersinia sp. YscN protein an ATPase involved in the type III secretory pathway for the antihost Yops proteins. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 273401 [Multi-domain] Cd Length: 440 Bit Score: 517.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 37 VSVQGRVNHAVGQILNATGIRARLGEICELRTPNQ-PTLLAEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGREHVFPVG 115
Cdd:TIGR01026 21 VKRVGRVTKVKGLLIEAVGPQASVGDLCLIERRGSeGRLVAEVVGFNGEFVFLMPYEEVEGVRPGSKVLATGEGLSIKVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 116 EGLFGRVLDGLGRPLDDRG-PVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKSTLL 194
Cdd:TIGR01026 101 DGLLGRVLDGLGKPIDGKGkFLDNVETEGLITAPINPLKRAPIREILSTGVRSIDGLLTVGKGQRIGIFAGSGVGKSTLL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 195 GMIARGAQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRVLLLVD 274
Cdd:TIGR01026 181 GMIARNTEADVNVIALIGERGREVREFIEHDLGEEGLKRSVVVVATSDQSPLLRLKGAYVATAIAEYFRDQGKDVLLLMD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 275 SLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGAHGSITALYTVLVEGDEESDPIAEEVRSILDGHIVLS 354
Cdd:TIGR01026 261 SVTRFAMAQREIGLAAGEPPATKGYTPSVFSTLPRLLERAGASGKGSITAFYTVLVEGDDMNEPIADSVRGILDGHIVLS 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 355 RKIALANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALRARDAIGAFCAQ 434
Cdd:TIGR01026 341 RALAQRGHYPAIDVLASISRLMTAIVSEEHRRAARKFRELLSKYKDNEDLIRIGAYQRGSDRELDFAIAKYPKLERFLKQ 420
|
410
....*....|....*...
gi 1409814734 435 ASDEDVRFDALLAKLTKL 452
Cdd:TIGR01026 421 GINEKVNFEESLQQLEEI 438
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
41-454 |
0e+00 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 515.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 41 GRVNHAVGQILNATGIRARLGEICELRT-PNQP-TLLAEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGREHVFPVGEGL 118
Cdd:PRK07721 20 GKVSRVIGLMIESKGPESSIGDVCYIHTkGGGDkAIKAEVVGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVGSGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 119 FGRVLDGLGRPLDDRGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKSTLLGMIA 198
Cdd:PRK07721 100 IGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 199 RGAQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRVLLLVDSLTR 278
Cdd:PRK07721 180 RNTSADLNVIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 279 FARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGAHGSITALYTVLVEGDEESDPIAEEVRSILDGHIVLSRKIA 358
Cdd:PRK07721 260 VAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 359 LANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALRARDAIGAFCAQASDE 438
Cdd:PRK07721 340 NKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLINIGAYKRGSSREIDEAIQFYPQIISFLKQGTDE 419
|
410
....*....|....*.
gi 1409814734 439 DVRFDALLAKLTKLAN 454
Cdd:PRK07721 420 KATFEESIQALLSLFG 435
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
30-452 |
3.97e-177 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 503.19 E-value: 3.97e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 30 GLAFFSPVSVQGRVnhavgqILNATGIRARLGEICELRtPNQptLLAEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGRE 109
Cdd:PRK06820 26 GLRYRGPIVEIGPT------LLRASLPGVAQGELCRIE-PQG--MLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 110 HVFPVGEGLFGRVLDGLGRPLDDrGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVG 189
Cdd:PRK06820 97 HQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 190 KSTLLGMIARGAQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRV 269
Cdd:PRK06820 176 KSTLLGMLCADSAADVMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 270 LLLVDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGAHGSITALYTVLVEGDEESDPIAEEVRSILDG 349
Cdd:PRK06820 256 LLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 350 HIVLSRKIALANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALRARDAIG 429
Cdd:PRK06820 336 HIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGEYQAGEDLQADEALQRYPAIC 415
|
410 420
....*....|....*....|...
gi 1409814734 430 AFCAQASDEDVRFDALLAKLTKL 452
Cdd:PRK06820 416 AFLQQDHSETAHLETTLEHLAQV 438
|
|
| FliI_clade3 |
TIGR03498 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
41-449 |
1.89e-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.
Pssm-ID: 163293 [Multi-domain] Cd Length: 418 Bit Score: 480.26 E-value: 1.89e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 41 GRVNHAVGQILNATGI--RARLGEICELRTPNQPTLLAEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGREHVFPVGEGL 118
Cdd:TIGR03498 1 GRVTAVTGLLIEVRGLsrAVRLGDRCAIRARDGRPVLAEVVGFNGDRVLLMPFEPLEGVGLGCAVFAREGPLAVRPHPSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 119 FGRVLDGLGRPLDDRGPV-TGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKSTLLGMI 197
Cdd:TIGR03498 81 LGRVINALGEPIDGKGPLpQGERRYPLRASPPPAMSRARVGEPLDTGVRVIDTFLPLCRGQRLGIFAGSGVGKSTLLSML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 198 ARGAQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRVLLLVDSLT 277
Cdd:TIGR03498 161 ARNTDADVVVIALVGERGREVREFLEDDLGEEGLKRSVVVVATSDESPLMRRQAAYTATAIAEYFRDQGKDVLLLMDSVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 278 RFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGA--HGSITALYTVLVEGDEESDPIAEEVRSILDGHIVLSR 355
Cdd:TIGR03498 241 RFAMAQREIGLAAGEPPVARGYTPSVFSELPRLLERAGPGAegKGSITGIFTVLVDGDDHNEPVADAVRGILDGHIVLDR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 356 KIALANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALRARDAIGAFCAQA 435
Cdd:TIGR03498 321 AIAERGRYPAINVLASVSRLAPRVWSPEERKLVRRLRALLARYEETEDLIRLGAYRKGSDPELDEAIRLVPKIYEFLTQG 400
|
410
....*....|....
gi 1409814734 436 SDEDVRFDALLAKL 449
Cdd:TIGR03498 401 PDEPTSLQDPFADL 414
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
112-375 |
3.70e-159 |
|
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: 450.47 E-value: 3.70e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 112 FPVGEGLFGRVLDGLGRPLDDRGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKS 191
Cdd:cd01136 2 IPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 192 TLLGMIARGAQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRVLL 271
Cdd:cd01136 82 TLLGMIARNTDADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 272 LVDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGAHGSITALYTVLVEGDEESDPIAEEVRSILDGHI 351
Cdd:cd01136 162 LMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRSILDGHI 241
|
250 260
....*....|....*....|....
gi 1409814734 352 VLSRKIALANRYPAIDVLASLSRV 375
Cdd:cd01136 242 VLSRRLAERGHYPAIDVLASISRV 265
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
36-454 |
8.46e-159 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 456.47 E-value: 8.46e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 36 PVSVQGRVNHAVGQILNATGIRARLGEICELRTPNQpTLLAEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGREHVFPVG 115
Cdd:PRK08972 22 RAVASGKLVRVVGLTLEATGCRAPVGSLCSIETMAG-ELEAEVVGFDGDLLYLMPIEELRGVLPGARVTPLGEQSGLPVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 116 EGLFGRVLDGLGRPLDDRGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKSTLLG 195
Cdd:PRK08972 101 MSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 196 MIARGAQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRVLLLVDS 275
Cdd:PRK08972 181 MMTRGTTADVIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMDS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 276 LTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGA--HGSITALYTVLVEGDEESDPIAEEVRSILDGHIVL 353
Cdd:PRK08972 261 LTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGpgQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 354 SRKIALANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALRARDAIGAFCA 433
Cdd:PRK08972 341 SRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLYQQNRDLISIGAYKQGSDPRIDNAIRLQPAMNAFLQ 420
|
410 420
....*....|....*....|.
gi 1409814734 434 QASDEDVRFDALLAKLTKLAN 454
Cdd:PRK08972 421 QTMKEAVPYDMSVNMLKQLAA 441
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
48-454 |
1.54e-152 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 440.20 E-value: 1.54e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 48 GQILNATGIRARLGEICELRTP-NQPTLL--AEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGREHVFPVGEGLFGRVLD 124
Cdd:PRK08149 15 GPIIEAELPDVAIGEICEIRAGwHSNEVIarAQVVGFQRERTILSLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 125 GLGRPLDDRG----PVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKSTLLGMIARG 200
Cdd:PRK08149 95 PTGKIVERFDapptVGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 201 AQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRVLLLVDSLTRFA 280
Cdd:PRK08149 175 SEADVFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 281 RAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGAHGSITALYTVLVEGDEESDPIAEEVRSILDGHIVLSRKIALA 360
Cdd:PRK08149 255 RALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 361 NRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALRARDAIGAFCAQASDEDV 440
Cdd:PRK08149 335 GHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGEYRRGENADNDRAMDKRPALEAFLKQDVAEKS 414
|
410
....*....|....
gi 1409814734 441 RFDALLAKLTKLAN 454
Cdd:PRK08149 415 SFSDTLERLNEFAA 428
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
41-452 |
1.19e-149 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 432.84 E-value: 1.19e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 41 GRVNHAVGQILNATGIRARLGEICELRTPNQptlLAEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGREHVFPVGEGLFG 120
Cdd:PRK07594 23 GRIQDVSATLLNAWLPGVFMGELCCIKPGEE---LAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 121 RVLDGLGRPLDDRgPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKSTLLGMIARG 200
Cdd:PRK07594 100 RVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 201 AQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRVLLLVDSLTRFA 280
Cdd:PRK07594 179 PDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 281 RAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGAHGSITALYTVLVEGDEESDPIAEEVRSILDGHIVLSRKIALA 360
Cdd:PRK07594 259 RAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAER 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 361 NRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALRARDAIGAFCAQASDEDV 440
Cdd:PRK07594 339 GHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEYQRGVDTDTDKAIDTYPDICTFLRQSKDEVC 418
|
410
....*....|..
gi 1409814734 441 RFDALLAKLTKL 452
Cdd:PRK07594 419 GPELLIEKLHQI 430
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
36-438 |
9.27e-146 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 423.24 E-value: 9.27e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 36 PVSVQGRVNHAVGQILNATGIRARL--GEICELRTPNQPTLLAEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGREHVFP 113
Cdd:PRK08927 14 TLVIYGRVVAVRGLLVEVAGPIHALsvGARIVVETRGGRPVPCEVVGFRGDRALLMPFGPLEGVRRGCRAVIANAAAAVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 114 VGEGLFGRVLDGLGRPLDDRGPVT-GAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKST 192
Cdd:PRK08927 94 PSRAWLGRVVNALGEPIDGKGPLPqGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 193 LLGMIARGAQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRVLLL 272
Cdd:PRK08927 174 LLSMLARNADADVSVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 273 VDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGA--HGSITALYTVLVEGDEESDPIAEEVRSILDGH 350
Cdd:PRK08927 254 MDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPigEGTITGLFTVLVDGDDHNEPVADAVRGILDGH 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 351 IVLSRKIALANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALRARDAIGA 430
Cdd:PRK08927 334 IVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLGAYRAGSDPEVDEAIRLNPALEA 413
|
....*...
gi 1409814734 431 FCAQASDE 438
Cdd:PRK08927 414 FLRQGKDE 421
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
41-452 |
2.41e-142 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 414.47 E-value: 2.41e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 41 GRVNHAVGQILNATGIRARLGEI-CELRTPNQPTLLAEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGREHVFPVGEGLF 119
Cdd:PRK08472 20 GSITKISPTIIEADGLNPSVGDIvKIESSDNGKECLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 120 GRVLDGLGRPLDDRGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKSTLLGMIAR 199
Cdd:PRK08472 100 GRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 200 GAQADVNVIALVGERGREVREFIEHSLSPEVrARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRVLLLVDSLTRF 279
Cdd:PRK08472 180 GCLAPIKVVALIGERGREIPEFIEKNLGGDL-ENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 280 ARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAG-QGAHGSITALYTVLVEGDEESDPIAEEVRSILDGHIVLSRKIA 358
Cdd:PRK08472 259 AMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGkEEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELT 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 359 LANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALRARDAIGAFCAQASDE 438
Cdd:PRK08472 339 DFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAYQKGNDKELDEAISKKEFMEQFLKQNPNE 418
|
410
....*....|....
gi 1409814734 439 DVRFDALLAKLTKL 452
Cdd:PRK08472 419 LFPFEQTFEQLEEI 432
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
39-440 |
8.66e-141 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 411.05 E-value: 8.66e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 39 VQGRVNHAVGQILNATGIRARLGEICEL-----RTPNQptLLAEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGREHVFP 113
Cdd:PRK05688 27 VEGRLLRMVGLTLEAEGLRAAVGSRCLVinddsYHPVQ--VEAEVMGFSGDKVFLMPVGSVAGIAPGARVVPLADTGRLP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 114 VGEGLFGRVLDGLGRPLDDRGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKSTL 193
Cdd:PRK05688 105 MGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 194 LGMIARGAQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRVLLLV 273
Cdd:PRK05688 185 LGMMTRFTEADIIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLM 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 274 DSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGAH--GSITALYTVLVEGDEESDPIAEEVRSILDGHI 351
Cdd:PRK05688 265 DSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPggGSITAFYTVLSEGDDQQDPIADSARGVLDGHI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 352 VLSRKIALANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALRARDAIGAF 431
Cdd:PRK05688 345 VLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPHLVQF 424
|
....*....
gi 1409814734 432 CAQASDEDV 440
Cdd:PRK05688 425 LRQGLRENV 433
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
39-453 |
1.52e-130 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 384.24 E-value: 1.52e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 39 VQGRVNHAVGQILNATGIRARLGEICELRTPNQPTLLAEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGREHVFPVGEGL 118
Cdd:PRK07196 17 VAGRLVRVTGLLLESVGCRLAIGQRCRIESVDETFIEAQVVGFDRDITYLMPFKHPGGVLGGARVFPSEQDGELLIGDSW 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 119 FGRVLDGLGRPLDDRGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKSTLLGMIA 198
Cdd:PRK07196 97 LGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMIT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 199 RGAQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRVLLLVDSLTR 278
Cdd:PRK07196 177 RYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 279 FARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQG-AHGSITALYTVLVEGDEESDPIAEEVRSILDGHIVLSRKI 357
Cdd:PRK07196 257 YAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSsGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 358 ALANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALRARDAIGAFCAQASD 437
Cdd:PRK07196 337 AEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVAGADPMADQAVHYYPAITQFLRQEVG 416
|
410
....*....|....*.
gi 1409814734 438 EDVRFDALLAKLTKLA 453
Cdd:PRK07196 417 HPALFSASVEQLTGMF 432
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
21-452 |
4.40e-128 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 378.74 E-value: 4.40e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 21 GRLVGELDA---GLAFFSPVSVQGRVNHAVGQILNATGIRARLGEICELRTPNQPTLL---AEVVGFSRQTTLLTPLGDV 94
Cdd:PRK07960 6 TRWLTTLDNfeaKMAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCVIERQNGSETHeveSEVVGFNGQRLFLMPLEEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 95 AGLSPETTVVP---------SGREhvFPVGEGLFGRVLDGLGRPLDD-RGPVTG-AAWVSTQqdPPNPLARKMIDTPFPT 163
Cdd:PRK07960 86 EGILPGARVYArnisgeglqSGKQ--LPLGPALLGRVLDGSGKPLDGlPAPDTGeTGALITP--PFNPLQRTPIEHVLDT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 164 GVRVIDGLMTLGIGQRVGIFAPSGVGKSTLLGMIARGAQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDR 243
Cdd:PRK07960 162 GVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 244 PAMERVKSALVATAIAEHFRDAGKRVLLLVDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGAH--GS 321
Cdd:PRK07960 242 SPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISggGS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 322 ITALYTVLVEGDEESDPIAEEVRSILDGHIVLSRKIALANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEI 401
Cdd:PRK07960 322 ITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLLSSFQRN 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1409814734 402 ELLVQIGEYREGSDRLGDLALRARDAIGAFCAQASDEDVRFDALLAKLTKL 452
Cdd:PRK07960 402 RDLVSVGAYAKGSDPMLDKAIALWPQLEAFLQQGIFERADWEDSLQALERI 452
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
58-423 |
1.93e-123 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 366.63 E-value: 1.93e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 58 ARLGEICELRTPNQpTLLAEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGREHVFPvGEGLFGRVLDGLGRPLDDRGPVT 137
Cdd:PRK06002 47 VRLGDFVAIRADGG-THLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKGPLRIRP-DPSWKGRVINALGEPIDGLGPLA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 138 -GAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKSTLLGMIARGAQADVNVIALVGERGR 216
Cdd:PRK06002 125 pGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 217 EVREFIEHSLSpEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRVLLLVDSLTRFARAQREVGLASGEPPTR 296
Cdd:PRK06002 205 EVREFLEDTLA-DNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 297 RSFPPSTFAVLPRLLERAGQGA--HGSITALYTVLVEGDEESDPIAEEVRSILDGHIVLSRKIALANRYPAIDVLASLSR 374
Cdd:PRK06002 284 RGYPPSVFSELPRLLERAGPGAegGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISR 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1409814734 375 VMPLVASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALR 423
Cdd:PRK06002 364 LARHAWTPEQRKLVSRLKSMIARFEETRDLRLIGGYRAGSDPDLDQAVD 412
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
164-373 |
2.50e-119 |
|
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: 347.04 E-value: 2.50e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 164 GVRVIDGLMTLGIGQRVGIFAPSGVGKSTLLGMIARGAQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDR 243
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLGSGALKRTVVVVATSDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 244 PAMERVKSALVATAIAEHFRDAGKRVLLLVDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAG--QGAHGS 321
Cdd:pfam00006 81 PPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGrvKGKGGS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1409814734 322 ITALYTVLVEGDEESDPIAEEVRSILDGHIVLSRKIALANRYPAIDVLASLS 373
Cdd:pfam00006 161 ITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
35-443 |
7.56e-104 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 315.76 E-value: 7.56e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 35 SPVSVQGRVNHAVGQILNATGIRARLGEICELrtpNQPTLLAEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGREHVFPV 114
Cdd:PRK06793 17 PFYTKVGKVHSVQEQFFVAKGPKAKIGDVCFV---GEHNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 115 GEGLFGRVLDGLGRPLDDRGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKSTLL 194
Cdd:PRK06793 94 GNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 195 GMIARGAQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRVLLLVD 274
Cdd:PRK06793 174 GMIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 275 SLTRFARAQREVGLASGEPPT-RRSFPPSTFavLPRLLERAGQGAHGSITALYTVLVEGDEESDPIAEEVRSILDGHIVL 353
Cdd:PRK06793 254 SVTRFADARRSVDIAVKELPIgGKTLLMESY--MKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 354 SRKIALANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALRAR-DAIGAFC 432
Cdd:PRK06793 332 KRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGTIQENAENAYIFECKNKvEGINTFL 411
|
410
....*....|.
gi 1409814734 433 AQASDEDVRFD 443
Cdd:PRK06793 412 KQGRSDSFQFD 422
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
31-454 |
1.49e-101 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 310.30 E-value: 1.49e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 31 LAFFSPVSVQGRVNHAVGQILNATGIRARLGEICELRTPNQPTLLAEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGREH 110
Cdd:PRK05922 11 IHQWQPYRECGLLSRVSGNLLEAQGLSACLGELCQISLSKSPPILAEVIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 111 VFPVGEGLFGRVLDGLGRPLDDRGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGK 190
Cdd:PRK05922 91 SLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 191 STLLGMIARGAQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRVL 270
Cdd:PRK05922 171 SSLLSTIAKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 271 LLVDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGAHGSITALYTVLVEGDeESDPIAEEVRSILDGH 350
Cdd:PRK05922 251 FIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAILHYPN-HPDIFTDYLKSLLDGH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 351 IVLS-RKIALANryPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALRARDAIG 429
Cdd:PRK05922 330 FFLTpQGKALAS--PPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGAYVPGQDAHLDRAVKLLPSIK 407
|
410 420
....*....|....*....|....*
gi 1409814734 430 AFCAQASDEDVRFDALLAKLTKLAN 454
Cdd:PRK05922 408 QFLSQPLSSYCALHNTLKQLEALLK 432
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
113-375 |
2.31e-89 |
|
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: 273.18 E-value: 2.31e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 113 PVGEGLFGRVLDGLGRPLDDRGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKST 192
Cdd:cd19476 3 PVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 193 LLGMIAR---GAQADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRV 269
Cdd:cd19476 83 LAMQLARnqaKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 270 LLLVDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGAH--GSITALYTVLVEGDEESDPIAEEVRSIL 347
Cdd:cd19476 163 LLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDggGSITAIPAVSTPGDDLTDPIPDNTFAIL 242
|
250 260
....*....|....*....|....*...
gi 1409814734 348 DGHIVLSRKIALANRYPAIDVLASLSRV 375
Cdd:cd19476 243 DGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| T3SS_ATP_VscN2 |
NF040574 |
type III secretion system ATPase VscN2; |
56-437 |
7.68e-89 |
|
type III secretion system ATPase VscN2;
Pssm-ID: 468548 Cd Length: 420 Bit Score: 276.87 E-value: 7.68e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 56 IRARLGEICELRTPNQPTLLAEVV---GFSRQTTLLTPlgdvAGLSPETTVVPSGREHVFPVGE-GLFGRVLDGLGRPLd 131
Cdd:NF040574 22 IDTFVGQECFIHTVGDERIRGEIMkieGHRVEIKLLQP----GTIQRGAKVEITPRRFCFPLNEeALIGKVINCYGESL- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 132 drgpvTGAAWVSTQQD--------PPNPLA-RKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKSTLLGMIARGAQ 202
Cdd:NF040574 97 -----YGEPYLIDEGEykdlpiciEPIPLKeRAPIETVFPTKLKIIDGLFTIGEGQRLGLFAPAGAGKTTTVSIMANNMD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 203 ADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRVLLLVDSLTRFARA 282
Cdd:NF040574 172 ADVVIFAMIGERAREVVEFLEGEIGPEVIQKSITIVSTSEANPLEKVRSGLVAVSIARYFMEQGKKVVLYFDSLTRFARA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 283 QrevGLASGEPpTRRSFPPSTFAVLPRLLERAGQGAHGSITALYTVLVEGDEESDPIAEEVRSILDGHIVLSRKIALANR 362
Cdd:NF040574 252 Q---AMLDGTP-IQGGIPIGVSLALSRLVESCGNSIRGSVTGIFTVLIEKEIDSDPIAHEVKSLIDGHLVYSTTIASTGR 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1409814734 363 YPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALRARDAIGAFCAQASD 437
Cdd:NF040574 328 YPAIDVLKSKSRLQNKIQDKRYVQLSERIKDMVYRYFDVELLIRVGEYEKGNDLLTDEAIELYPQIMEFLKQGFD 402
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
91-408 |
1.81e-47 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 170.48 E-value: 1.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 91 LGDVAGLSPETTVVPSGREHVFPVGEGLFGRVLDGLGRPLDDRGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDG 170
Cdd:PRK13343 76 LDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 171 LMTLGIGQRVGIFAPSGVGKSTlLGMIARGAQADVNVI---ALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAME 247
Cdd:PRK13343 156 LIPIGRGQRELIIGDRQTGKTA-IAIDAIINQKDSDVIcvyVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 248 RVKSALVATAIAEHFRDAGKRVLLLVDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQ--GAH--GSIT 323
Cdd:PRK13343 235 QYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKlsPELggGSLT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 324 ALYTVLVEGDEESDPIAEEVRSILDGHIVLSRKIALANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKYQEIEL 403
Cdd:PRK13343 315 ALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEA 394
|
....*
gi 1409814734 404 LVQIG 408
Cdd:PRK13343 395 FTRFG 399
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
58-376 |
1.91e-47 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 169.62 E-value: 1.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 58 ARLGEICELRTPNQPTLLAEVVGFSRQTTLLTPLGDVAGLSPETTVVP-SGREHVFPVGEGLFGRVLDGLGRPLDDRGPV 136
Cdd:PRK04196 23 VAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRfTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 137 TGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKSTLLGMIARgaQADVN--------VI 208
Cdd:PRK04196 103 IPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIAR--QAKVLgeeenfavVF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 209 ALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFR-DAGKRVLLLVDSLTRFARAQREVG 287
Cdd:PRK04196 181 AAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAfEKGMHVLVILTDMTNYCEALREIS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 288 LASGEPPTRRSFPPSTFAVLPRLLERAG--QGAHGSITALYTVLVEGDEESDPIAEEVRSILDGHIVLSRKIALANRYPA 365
Cdd:PRK04196 261 AAREEVPGRRGYPGYMYTDLATIYERAGriKGKKGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPP 340
|
330
....*....|.
gi 1409814734 366 IDVLASLSRVM 376
Cdd:PRK04196 341 IDVLPSLSRLM 351
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
113-376 |
5.93e-46 |
|
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: 160.85 E-value: 5.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 113 PVGEGLFGRVLDGLGRPLDDRGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKST 192
Cdd:cd01135 5 PVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLPHNE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 193 LLGMIARgaQADVN--------VIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFR- 263
Cdd:cd01135 85 LAAQIAR--QAGVVgseenfaiVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYLAy 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 264 DAGKRVLLLVDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQ--GAHGSITALYTVLVEGDEESDPIAE 341
Cdd:cd01135 163 EKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRveGRKGSITQIPILTMPNDDITHPIPD 242
|
250 260 270
....*....|....*....|....*....|....*
gi 1409814734 342 EVRSILDGHIVLSRKIALANRYPAIDVLASLSRVM 376
Cdd:cd01135 243 LTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLM 277
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
113-375 |
5.49e-42 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 150.02 E-value: 5.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 113 PVGEGLFGRVLDGLGRPLDDRGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKST 192
Cdd:cd01132 5 PVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 193 llgmIARGA---QADVNVIAL---VGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAG 266
Cdd:cd01132 85 ----IAIDTiinQKGKKVYCIyvaIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 267 KRVLLLVDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQ-----GAhGSITALYTVLVEGDEESDPIAE 341
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKlsdelGG-GSLTALPIIETQAGDVSAYIPT 239
|
250 260 270
....*....|....*....|....*....|....
gi 1409814734 342 EVRSILDGHIVLSRKIALANRYPAIDVLASLSRV 375
Cdd:cd01132 240 NVISITDGQIFLESELFNKGIRPAINVGLSVSRV 273
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
91-400 |
9.49e-40 |
|
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: 148.70 E-value: 9.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 91 LGDVAGLSPETTVVPSGREHVFPVGEGLFGRVLDGLGRPLDDRGPVTGAAWVSTQQDPPnPLARKMIDT-PFPTGVRVID 169
Cdd:COG0055 60 MDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAP-PFEEQSTKTeILETGIKVID 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 170 GLMTLGIGQRVGIFAPSGVGKSTLL-GMIARGAQAD--VNVIALVGERGRE----VREFIEHSlspeVRARSIVVVSTSD 242
Cdd:COG0055 139 LLAPYAKGGKIGLFGGAGVGKTVLImELIHNIAKEHggVSVFAGVGERTREgndlYREMKESG----VLDKTALVFGQMN 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 243 RPAMERVKSALVATAIAEHFRDAGKR-VLLLVDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGAHGS 321
Cdd:COG0055 215 EPPGARLRVALTALTMAEYFRDEEGQdVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGS 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 322 ITALYTVLVEGDEESDPIAEEVRSILDGHIVLSRKIALANRYPAIDVLASLSRVM-PLVASRAHQHAAARVRELIAKYQE 400
Cdd:COG0055 295 ITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILdPLIVGEEHYRVAREVQRILQRYKE 374
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
113-376 |
1.54e-39 |
|
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: 143.51 E-value: 1.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 113 PVGEGLFGRVLDGLGRPLDDRGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKsT 192
Cdd:cd01133 3 PVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK-T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 193 LLGM-----IARgAQADVNVIALVGERGRE----VREFIEHSLSPEVRARSIVVV-STSDRPAMERVKSALVATAIAEHF 262
Cdd:cd01133 82 VLIMelinnIAK-AHGGYSVFAGVGERTREgndlYHEMKESGVINLDGLSKVALVyGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 263 RDA-GKRVLLLVDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGAHGSITALYTVLVEGDEESDPIAE 341
Cdd:cd01133 161 RDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPA 240
|
250 260 270
....*....|....*....|....*....|....*
gi 1409814734 342 EVRSILDGHIVLSRKIALANRYPAIDVLASLSRVM 376
Cdd:cd01133 241 TTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
91-375 |
1.41e-36 |
|
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439826 [Multi-domain] Cd Length: 504 Bit Score: 140.56 E-value: 1.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 91 LGDVAGLSPETTVVPSGRehVF--PVGEGLFGRVLDGLGRPLDDRGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVI 168
Cdd:COG0056 76 LGDYEGIKEGDTVKRTGR--ILsvPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAI 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 169 DGLMTLGIGQRVGIFAPSGVGKSTllgmIARGA---QADVNVI----AlVGERGREVREFIEhslspEVR-----ARSIV 236
Cdd:COG0056 154 DAMIPIGRGQRELIIGDRQTGKTA----IAIDTiinQKGKDVIciyvA-IGQKASTVAQVVE-----TLEehgamEYTIV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 237 VVSTSDRPAmervksAL------VATAIAEHFRDAGKRVLLLVDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRL 310
Cdd:COG0056 224 VAATASDPA------PLqyiapyAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 311 LERAG-----QGAhGSITALytvlvegdeesdPIAE------------EVRSILDGHIVLSRKIALANRYPAIDVLASLS 373
Cdd:COG0056 298 LERAAklsdeLGG-GSLTAL------------PIIEtqagdvsayiptNVISITDGQIFLESDLFNAGIRPAINVGLSVS 364
|
..
gi 1409814734 374 RV 375
Cdd:COG0056 365 RV 366
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
115-374 |
1.61e-36 |
|
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: 135.78 E-value: 1.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 115 GEGLFGRVLDGLGRPLDD----------RGpvtgaawVSTQQDP---PNPLARKMI-DTPFPTGVRVIDGLMTLGIGQRV 180
Cdd:cd01134 7 GPGLLGSIFDGIQRPLEViaetgsifipRG-------VNVQRWPvrqPRPVKEKLPpNVPLLTGQRVLDTLFPVAKGGTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 181 GIFAPSGVGKSTLLGMIARGAQADVNVIALVGERGREV----REFIEhsLSPEVRARSI-----VVVSTSDRPAMERVKS 251
Cdd:cd01134 80 AIPGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMaevlEEFPE--LKDPITGESLmertvLIANTSNMPVAAREAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 252 ALVATAIAEHFRDAGKRVLLLVDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQ-------GAHGSITA 324
Cdd:cd01134 158 IYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRvrclgspGREGSVTI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1409814734 325 LYTVLVEGDEESDPIAEEVRSILDGHIVLSRKIALANRYPAIDVLASLSR 374
Cdd:cd01134 238 VGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSK 287
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
96-425 |
8.99e-36 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 138.25 E-value: 8.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 96 GLSPETTVVPSGREHVFPVGEGLFGRVLDGLGRPLDDRGPVTGAAWVSTQQDPPnplARKMIDTP---FPTGVRVIDGLM 172
Cdd:CHL00060 80 GLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAP---AFIQLDTKlsiFETGIKVVDLLA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 173 TLGIGQRVGIFAPSGVGKsTLLGM-----IARgAQADVNVIALVGERGRE----VREFIEHSLSPEVR-ARSIV--VVST 240
Cdd:CHL00060 157 PYRRGGKIGLFGGAGVGK-TVLIMelinnIAK-AHGGVSVFGGVGERTREgndlYMEMKESGVINEQNiAESKValVYGQ 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 241 SDRPAMERVKSALVATAIAEHFRDAGKR-VLLLVDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQGAH 319
Cdd:CHL00060 235 MNEPPGARMRVGLTALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 320 GSITALYTVLVEGDEESDPIAEEVRSILDGHIVLSRKIALANRYPAIDVLASLSRVM-PLVASRAHQHAAARVRELIAKY 398
Cdd:CHL00060 315 GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGEEHYETAQRVKQTLQRY 394
|
330 340
....*....|....*....|....*....
gi 1409814734 399 QEIELLVQIGEYREGS--DRLgdLALRAR 425
Cdd:CHL00060 395 KELQDIIAILGLDELSeeDRL--TVARAR 421
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
91-406 |
5.17e-33 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 130.47 E-value: 5.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 91 LGDVAGLSPETTVVPSGREHVFPVGEGLFGRVLDGLGRPLDDRGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDG 170
Cdd:CHL00059 55 MGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 171 LMTLGIGQRVGIFAPSGVGKS-----TLLGmiargaQADVNVIAL---VGERGREVREFIEHSLSPEVRARSIVVVSTSD 242
Cdd:CHL00059 135 MIPIGRGQRELIIGDRQTGKTavatdTILN------QKGQNVICVyvaIGQKASSVAQVVTTLQERGAMEYTIVVAETAD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 243 RPAMERVKSALVATAIAEHFRDAGKRVLLLVDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAG----QGA 318
Cdd:CHL00059 209 SPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklssQLG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 319 HGSITALYTVLVEGDEESDPIAEEVRSILDGHIVLSRKIALANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIAKY 398
Cdd:CHL00059 289 EGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQF 368
|
....*...
gi 1409814734 399 QEIELLVQ 406
Cdd:CHL00059 369 AELEAFAQ 376
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
51-379 |
1.60e-31 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 125.53 E-value: 1.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 51 LNATGIRarLGEICELRTPNQpTLLAEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGREHVFPVGEGLFGRVLDGLGRPL 130
Cdd:PRK02118 18 VEAEGVG--YGELATVERKDG-SSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 131 dDRGPVTGAAWVSTQQDPPNP----LARKMIDtpfpTGVRVIDGLMTLGIGQRVGIFAPSGVGKSTLLGMIARGAQADVN 206
Cdd:PRK02118 95 -DGGPELEGEPIEIGGPSVNPvkriVPREMIR----TGIPMIDVFNTLVESQKIPIFSVSGEPYNALLARIALQAEADII 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 207 VIALVGERGREVREFIEHSLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFR-DAGKRVLLLVDSLTRFARAQRE 285
Cdd:PRK02118 170 ILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 286 VGLASGEPPTRRSFPPSTFAVLPRLLERAGQ--GAhGSITALYTVLVEGDEESDPIAEEVRSILDGHIVLSRkialaNRy 363
Cdd:PRK02118 250 ISITMDQIPSNRGYPGSLYSDLASRYEKAVDfeDG-GSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLRR-----GR- 322
|
330
....*....|....*.
gi 1409814734 364 paIDVLASLSRVMPLV 379
Cdd:PRK02118 323 --IDPFGSLSRLKQLV 336
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
91-375 |
7.06e-31 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 124.41 E-value: 7.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 91 LGDVAGLSPETTVVPSGREHVFPVGEGLFGRVLDGLGRPLDDRGPVTgaawvSTQQDP-----PNPLARKMIDTPFPTGV 165
Cdd:PRK09281 76 LGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIE-----ATETRPverkaPGVIDRKSVHEPLQTGI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 166 RVIDGLMTLGIGQRVGIFAPSGVGKSTllgmIARGA---QADVNVIAL---VGERGREVREFIEhslspEVRAR-----S 234
Cdd:PRK09281 151 KAIDAMIPIGRGQRELIIGDRQTGKTA----IAIDTiinQKGKDVICIyvaIGQKASTVAQVVR-----KLEEHgameyT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 235 IVVVST-SDRPAMERVkSALVATAIAEHFRDAGKRVLLLVDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLER 313
Cdd:PRK09281 222 IVVAATaSDPAPLQYL-APYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLER 300
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1409814734 314 AGQ-----GAhGSITALytvlvegdeesdPIAE------------EVRSILDGHIVLSRKIALANRYPAIDVLASLSRV 375
Cdd:PRK09281 301 AAKlsdelGG-GSLTAL------------PIIEtqagdvsayiptNVISITDGQIFLESDLFNAGIRPAINVGISVSRV 366
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
113-376 |
2.99e-29 |
|
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: 119.44 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 113 PVGEGLFGRVLDGLGRPLDDRGPVTGAAWVSTQQDPPNPLARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKST 192
Cdd:TIGR01040 77 PVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 193 LLGMIARGA------QADVN---------VIALVG---ERGREVREFIEHSLSPEvraRSIVVVSTSDRPAMERVKSALV 254
Cdd:TIGR01040 157 IAAQICRQAglvklpTKDVHdghednfaiVFAAMGvnmETARFFKQDFEENGSME---RVCLFLNLANDPTIERIITPRL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 255 ATAIAEHFR-DAGKRVLLLVDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAG--QGAHGSITALYTVLVE 331
Cdd:TIGR01040 234 ALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGrvEGRNGSITQIPILTMP 313
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1409814734 332 GDEESDPIAEEVRSILDGHIVLSRKiaLANR--YPAIDVLASLSRVM 376
Cdd:TIGR01040 314 NDDITHPIPDLTGYITEGQIYVDRQ--LHNRqiYPPINVLPSLSRLM 358
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
149-401 |
1.44e-25 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 109.49 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 149 PNPLARKMI-DTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKSTLLGMIARGAQADVNVIALVGERGREV----REFIE 223
Cdd:PRK04192 198 PRPYKEKLPpVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQLAKWADADIVIYVGCGERGNEMtevlEEFPE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 224 -------HSLSpevrARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRVLLLVDSLTRFARAQREVGLASGEPPTR 296
Cdd:PRK04192 278 lidpktgRPLM----ERTVLIANTSNMPVAAREASIYTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 297 RSFPPSTFAVLPRLLERAGQ-----GAHGSITALYTVLVEGDEESDPIAEEVRSILDGHIVLSRKIALANRYPAIDVLAS 371
Cdd:PRK04192 354 EGYPAYLASRLAEFYERAGRvktlgGEEGSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTS 433
|
250 260 270
....*....|....*....|....*....|
gi 1409814734 372 LSRVMPLVASRAHQHAAARVRELIAKYQEI 401
Cdd:PRK04192 434 YSLYLDQVAPWWEENVDPDWRELRDEAMDL 463
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
165-374 |
1.13e-22 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 99.00 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 165 VRVIDGLMTLGIGQRVGIFAPSGVGKSTLLGMIARGAQA---DVNVIA-LVGERGREVREFiehslspEVRARSIVVVST 240
Cdd:PRK12608 121 MRVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAAnhpEVHLMVlLIDERPEEVTDM-------RRSVKGEVYAST 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 241 SDRPAMERVKSALVATAIAEHFRDAGKRVLLLVDSLTRFARAQREVGLASGEPPT-----RRSFPPSTFAVLPRLLERAg 315
Cdd:PRK12608 194 FDRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAYNNEVESSGRTLSggvdaRALQRPKRLFGAARNIEEG- 272
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 316 qgahGSITALYTVLVE-GDEESDPIAEEVRSILDGHIVLSRKIALANRYPAIDVLASLSR 374
Cdd:PRK12608 273 ----GSLTIIATALVDtGSRMDEVIFEEFKGTGNMEIVLDRELADKRVFPAIDIAKSGTR 328
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
166-402 |
1.30e-22 |
|
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: 96.51 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 166 RVIDGLMTLGIGQRVGIFAPSGVGKSTLLGMIARG---AQADVNVIA-LVGERGREVREFIEhslspEVRArsIVVVSTS 241
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAiakNHPEVELIVlLIDERPEEVTDMRR-----SVKG--EVVASTF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 242 DRPAMERVKSALVATAIAEHFRDAGKRVLLLVDSLTRFARAQREVGLASGEPPTRRSFP-----PSTFAVLPRLLERAgq 316
Cdd:cd01128 78 DEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSGGVDAnalhkPKRFFGAARNIEEG-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 317 gahGSITALYTVLVE-GDEESDPIAEEVRSILDGHIVLSRKIALANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELI 395
Cdd:cd01128 156 ---GSLTIIATALVDtGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTRKEELLLTPEELQKIWLLRRIL 232
|
....*..
gi 1409814734 396 AKYQEIE 402
Cdd:cd01128 233 SPMDPIE 239
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
103-401 |
6.08e-22 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 98.57 E-value: 6.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 103 VVPSGREHVFPVGEGLFGRVLDGLG-----------RPLDDRGPVTGaawvSTQQDPPNPLARKMIDTPFPTGVRVIDGL 171
Cdd:PTZ00185 108 VMATGKLLYIPVGAGVLGKVVNPLGhevpvglltrsRALLESEQTLG----KVDAGAPNIVSRSPVNYNLLTGFKAVDTM 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 172 MTLGIGQRVGIFAPSGVGK-----STLLGMIARGAQ-----ADVNVIALVGERGREVREFIEHSLSPEVRARSIVVVSTS 241
Cdd:PTZ00185 184 IPIGRGQRELIVGDRQTGKtsiavSTIINQVRINQQilsknAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 242 DRPAMERVKSALVATAIAEHFRDAGKRVLLLVDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERA-----GQ 316
Cdd:PTZ00185 264 AEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAamlspGK 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 317 GAhGSITALYTVLVEGDEESDPIAEEVRSILDGHIVLSRKIALANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELIA 396
Cdd:PTZ00185 344 GG-GSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAMKAVAGKLKGILA 422
|
....*
gi 1409814734 397 KYQEI 401
Cdd:PTZ00185 423 EYRKL 427
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
166-402 |
2.68e-21 |
|
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: 95.52 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 166 RVIDGLMTLGIGQRVGIFAPSGVGKSTLLGMIARGA---QADVNVIA-LVGERGREVREFIEhslspEVRARsiVVVSTS 241
Cdd:TIGR00767 157 RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAItrnHPEVELIVlLIDERPEEVTDMQR-----SVKGE--VVASTF 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 242 DRPAMERVKSALVATAIAEHFRDAGKRVLLLVDSLTRFARAQREVGLASGEPPT-----RRSFPPSTFAVLPRLLERAgq 316
Cdd:TIGR00767 230 DEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKVLSggvdaNALHRPKRFFGAARNIEEG-- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 317 gahGSITALYTVLVE-GDEESDPIAEEVRSILDGHIVLSRKIALANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELI 395
Cdd:TIGR00767 308 ---GSLTIIATALIDtGSRMDEVIFEEFKGTGNMELHLDRKLADRRIFPAIDIKKSGTRKEELLLTPEELQKIWVLRKII 384
|
....*..
gi 1409814734 396 AKYQEIE 402
Cdd:TIGR00767 385 SPMDSIE 391
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
380-449 |
3.65e-21 |
|
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: 86.72 E-value: 3.65e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 380 ASRAHQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALRARDAIGAFCAQASDEDVRFDALLAKL 449
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIGAYQAGSDPEIDEAIAKRPAINAFLRQGVDEPVSFEETLAQL 70
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
152-399 |
9.44e-20 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 91.57 E-value: 9.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 152 LARKMIDTPFPTGVRVIDGLMTLGIGQRVGIFAPSGVGKSTL-LGMIARGAQADVNVIAL-VGERgREVREFIEHSLSP- 228
Cdd:PRK07165 118 MTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIaLNTIINQKNTNVKCIYVaIGQK-RENLSRIYETLKEh 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 229 EVRARSIVVVSTSDRPaMERVKSALVATAIAE---HFRDagkrVLLLVDSLTRFARAQREVGLASGEPPTRRSFPPSTFA 305
Cdd:PRK07165 197 DALKNTIIIDAPSTSP-YEQYLAPYVAMAHAEnisYNDD----VLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFF 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 306 VLPRLLERAGQGAHG-SITALYTV-LVEGDEESdPIAEEVRSILDGHIVLSRKIALANRYPAIDVLASLSRVMPLVASRA 383
Cdd:PRK07165 272 AHSKLLERAGKFKNRkTITALPILqTVDNDITS-LISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKT 350
|
250
....*....|....*.
gi 1409814734 384 HQHAAARVRELIAKYQ 399
Cdd:PRK07165 351 ITKVAGEISKIYRAYK 366
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
166-402 |
9.60e-20 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 90.97 E-value: 9.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 166 RVIDGLMTLGIGQRVGIFAPSGVGKSTLLGMIARGAQA---DVNVIA-LVGERGREVREFIEHslspeVRARsiVVVSTS 241
Cdd:PRK09376 158 RIIDLIAPIGKGQRGLIVAPPKAGKTVLLQNIANSITTnhpEVHLIVlLIDERPEEVTDMQRS-----VKGE--VVASTF 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 242 DRPAMERVKSA-LV---ATAIAEHFRDagkrVLLLVDSLTRFARAQREVGLASG------------EPPTRrsfppstFA 305
Cdd:PRK09376 231 DEPAERHVQVAeMViekAKRLVEHGKD----VVILLDSITRLARAYNTVVPSSGkvlsggvdanalHRPKR-------FF 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 306 VLPRLLERAgqgahGSITALYTVLVE-GDEESDPIAEEVRSILDGHIVLSRKiaLANR--YPAIDVLASLSRVMPLVASR 382
Cdd:PRK09376 300 GAARNIEEG-----GSLTIIATALIDtGSRMDEVIFEEFKGTGNMELHLDRK--LAEKriFPAIDINRSGTRKEELLLSP 372
|
250 260
....*....|....*....|
gi 1409814734 383 AHQHAAARVRELIAKYQEIE 402
Cdd:PRK09376 373 EELQKVWILRKILSPMDEVE 392
|
|
| ATP-synt_flagellum-secretory_path_III_N |
cd18117 |
Flagellum-specific ATP synthase, N-terminal domain; The N-terminal domain of the ... |
41-108 |
2.55e-17 |
|
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: 76.03 E-value: 2.55e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1409814734 41 GRVNHAVGQILNATGIRARLGEICELRTPNQPTLLAEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGR 108
Cdd:cd18117 3 GRVVRVVGLLLEAVGPQAPIGELCLIETADGLSILAEVVGFSGEKVLLMPLGELSGLSPGARVVPLGR 70
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
197-439 |
2.52e-16 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 81.99 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 197 IARGAQADVNVIALVGERGREVREFIEH-------SLSPEVRARSIVVVSTSDRPAMERVKSALVATAIAEHFRDAGKRV 269
Cdd:PRK14698 676 LAKWSDAQVVIYIGCGERGNEMTDVLEEfpklkdpKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDV 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 270 LLLVDSLTRFARAQREVGLASGEPPTRRSFPPSTFAVLPRLLERAGQ----GAH---GSITALYTVLVEGDEESDPIAEE 342
Cdd:PRK14698 756 ALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRvvtlGSDyrvGSVSVIGAVSPPGGDFSEPVVQN 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 343 VRSILDGHIVLSRKIALANRYPAIDVLASLSRVMPLVASRAHQHAAARVRELiaKYQEIELLVQIGEYREGSDRLGDLAL 422
Cdd:PRK14698 836 TLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNVDPEWKAM--RDKAMELLQKEAELQEIVRIVGPDAL 913
|
250
....*....|....*..
gi 1409814734 423 RARDAIGAFCAQASDED 439
Cdd:PRK14698 914 PERERAILLVARMLRED 930
|
|
| ATP-synt_flagellum-secretory_path_III_C |
cd18114 |
Flagellum-specific ATP synthase, C-terminal domain; The C-terminal domain of the ... |
384-452 |
1.15e-13 |
|
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: 65.71 E-value: 1.15e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1409814734 384 HQHAAARVRELIAKYQEIELLVQIGEYREGSDRLGDLALRARDAIGAFCAQASDEDVRFDALLAKLTKL 452
Cdd:cd18114 1 HYLAARKFRELMSTYQENEDLIRIGAYKKGSDPEVDEAIRLKPQIEAFLKQGLNEKAPLEESLQQLEEI 69
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
164-374 |
1.00e-10 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 63.77 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 164 GVRVIDGLMTLGIGQRVGIFAPSGVGKSTLLGMIArgaqadvNVIA-----------LVGERGREVREFiEHSLSPEVRA 232
Cdd:PRK12678 403 TTRVIDLIMPIGKGQRGLIVSPPKAGKTTILQNIA-------NAITtnnpechlmvvLVDERPEEVTDM-QRSVKGEVIA 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 233 rsivvvSTSDRPAMERVKSALVATAIAEHFRDAGKRVLLLVDSLTRFARAQREVGLASGepptrRS----------FPPS 302
Cdd:PRK12678 475 ------STFDRPPSDHTTVAELAIERAKRLVELGKDVVVLLDSITRLGRAYNLAAPASG-----RIlsggvdstalYPPK 543
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1409814734 303 TFAVLPRLLERAgqgahGSITALYTVLVE----GDEesdPIAEEVRSILDGHIVLSRKIALANRYPAIDVLASLSR 374
Cdd:PRK12678 544 RFFGAARNIENG-----GSLTIIATALVEtgskMDE---VIFEEFKGTGNMELKLDRKLADKRIFPAVDVNASGTR 611
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
40-108 |
6.95e-10 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 55.01 E-value: 6.95e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1409814734 40 QGRVNHAVGQILNATGIR-ARLGEICELRTPNQPT---LLAEVVGFSRQTTLLTPLGDVAGLSPETTVVPSGR 108
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGeVAIGEVCEIERGDGNNetvLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
177-355 |
1.87e-06 |
|
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: 47.37 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 177 GQRVGIFAPSGVGKSTLLGMIARGAQAD-VNVIALVGERGREVrefiehslspeVRARSIVVVSTSDRPAMERVKSALVA 255
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPgGGVIYIDGEDILEE-----------VLDQLLLIIVGGKKASGSGELRLRLA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 256 TAIAEHFRdagkRVLLLVDSLTRFARAQREVGLasgepptrrsfppstfavlpRLLERAGQGAHGSITALYTVLVEGDEE 335
Cdd:smart00382 71 LALARKLK----PDVLILDEITSLLDAEQEALL--------------------LLLEELRLLLLLKSEKNLTVILTTNDE 126
|
170 180
....*....|....*....|
gi 1409814734 336 SDPIAEEVRSILDGHIVLSR 355
Cdd:smart00382 127 KDLGPALLRRRFDRRIVLLL 146
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
120-226 |
1.84e-04 |
|
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: 43.81 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 120 GRVLDGLGRPLDDRGPVTGAawvstqqdPPNPLARKMIDTPFPTGVRVIDGL-MTLGIGQRVGIFAPSGVGKSTLLGMIA 198
Cdd:TIGR02857 298 FAVLDAAPRPLAGKAPVTAA--------PASSLEFSGVSVAYPGRRPALRPVsFTVPPGERVALVGPSGAGKSTLLNLLL 369
|
90 100
....*....|....*....|....*...
gi 1409814734 199 RGAQADVNVIALVgerGREVREFIEHSL 226
Cdd:TIGR02857 370 GFVDPTEGSIAVN---GVPLADADADSW 394
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
161-369 |
1.15e-03 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 40.28 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 161 FPTGVRVIDGLMTLGI--GQRVGIFAPSGVGKSTL-LGMIARGAQADVNVIAL-VGERGREVREFIEH---SLSPEVRAR 233
Cdd:COG0467 2 VPTGIPGLDELLGGGLprGSSTLLSGPPGTGKTTLaLQFLAEGLRRGEKGLYVsFEESPEQLLRRAESlglDLEEYIESG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 234 SIVVVSTSDRPAMERVKSalVATAIAEHFRDAGKRVlLLVDSLTRFAraqrevgLASGEPPTRRSFppstFAVLPRLLER 313
Cdd:COG0467 82 LLRIIDLSPEELGLDLEE--LLARLREAVEEFGAKR-VVIDSLSGLL-------LALPDPERLREF----LHRLLRYLKK 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1409814734 314 AGqgahgsITALYTVLVEGDEESDPIaEEVRSILDGHIVLSRKIALANRYPAIDVL 369
Cdd:COG0467 148 RG------VTTLLTSETGGLEDEATE-GGLSYLADGVILLRYVELGGELRRALSVL 196
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
167-239 |
1.42e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 40.96 E-value: 1.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1409814734 167 VIDGL-MTLGIGQRVGIFAPSGVGKSTLLGMIARGAQADVNVIALvgeRGREVREFIEHSLspevRArSIVVVS 239
Cdd:PRK11160 355 VLKGLsLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL---NGQPIADYSEAAL----RQ-AISVVS 420
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
172-264 |
1.68e-03 |
|
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: 38.78 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 172 MTLGIGQRVGIFAPSGVGKSTLLGMIARGAQAD-----VNVIALVGERGREVREFI-----EHSLSPEVRARSIVVVSTS 241
Cdd:pfam00005 6 LTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTegtilLDGQDLTDDERKSLRKEIgyvfqDPQLFPRLTVRENLRLGLL 85
|
90 100
....*....|....*....|....*..
gi 1409814734 242 DRPAMERVKSALVATAIAE----HFRD 264
Cdd:pfam00005 86 LKGLSKREKDARAEEALEKlglgDLAD 112
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
177-198 |
2.36e-03 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 39.35 E-value: 2.36e-03
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
177-199 |
2.48e-03 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 39.03 E-value: 2.48e-03
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
164-198 |
4.08e-03 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 38.92 E-value: 4.08e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1409814734 164 GVRVIDGL-MTLGIGQRVGIFAPSGVGKSTLLGMIA 198
Cdd:COG1116 23 GVTALDDVsLTVAAGEFVALVGPSGCGKSTLLRLIA 58
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
167-227 |
4.08e-03 |
|
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: 38.06 E-value: 4.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1409814734 167 VIDGL-MTLGIGQRVGIFAPSGVGKSTLLGMIARGAQADVNVIALVGERGREVREFIEHSLS 227
Cdd:cd03247 17 VLKNLsLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLIS 78
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
177-198 |
4.29e-03 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 38.79 E-value: 4.29e-03
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
161-198 |
4.91e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 39.06 E-value: 4.91e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1409814734 161 FPTGVRVIDGL-MTLGIGQRVGIFAPSGVGKSTLLGMIA 198
Cdd:PRK11650 13 YDGKTQVIKGIdLDVADGEFIVLVGPSGCGKSTLLRMVA 51
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
162-239 |
5.36e-03 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 38.97 E-value: 5.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1409814734 162 PTGVRVIDGL-MTLGIGQRVGIFAPSGVGKSTLLGMIARGAQADVNVIALvgeRGREVREfiehsLSPEVRARSIVVVS 239
Cdd:COG4988 347 PGGRPALDGLsLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI---NGVDLSD-----LDPASWRRQIAWVP 417
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
165-203 |
6.15e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 38.95 E-value: 6.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1409814734 165 VRVIDGLmTLGI--GQRVGIFAPSGVGKSTLLGMIArGAQA 203
Cdd:NF033858 14 TVALDDV-SLDIpaGCMVGLIGPDGVGKSSLLSLIA-GARK 52
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
164-198 |
6.54e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 38.89 E-value: 6.54e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1409814734 164 GVRVIDGL-MTLGIGQRVGIFAPSGVGKSTLLGMIA 198
Cdd:COG0488 327 DKTLLDDLsLRIDRGDRIGLIGPNGAGKSTLLKLLA 362
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
164-249 |
6.67e-03 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 37.41 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814734 164 GVRVIDGL-MTLGIGQRVGIFAPSGVGKSTLLGMIARGAQADVNVIALvgeRGREVrefieHSLSPEVRARSIVVVSTsd 242
Cdd:cd03214 11 GRTVLDDLsLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL---DGKDL-----ASLSPKELARKIAYVPQ-- 80
|
....*..
gi 1409814734 243 rpAMERV 249
Cdd:cd03214 81 --ALELL 85
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
161-198 |
7.22e-03 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 37.72 E-value: 7.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1409814734 161 FPTG---VRVIDGL-MTLGIGQRVGIFAPSGVGKSTLLGMIA 198
Cdd:COG1136 14 YGTGegeVTALRGVsLSIEAGEFVAIVGPSGSGKSTLLNILG 55
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
164-198 |
8.86e-03 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 37.50 E-value: 8.86e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1409814734 164 GVRVIDGL-MTLGIGQRVGIFAPSGVGKSTLLGMIA 198
Cdd:cd03259 12 SVRALDDLsLTVEPGEFLALLGPSGCGKTTLLRLIA 47
|
|
| |
