|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
4-431 |
0e+00 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 820.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 4 QCLVHLAHPLRIQGNVIEAHLPGTRIGEICEIQKSLLEPEVLGTAQVIGFNKEHTLLSLLNDNQGFSRSNVLLPTGKPFR 83
Cdd:PRK08149 2 RLLQRLAHPLRIQGPIIEAELPDVAIGEICEIRAGWHSNEVIARAQVVGFQRERTILSLIGNAQGLSRQVVLKPTGKPLS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 84 IDVHKNIAGAIIDATGTVRGRLDNAVQqSLTGAQSLEACGAPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAA 163
Cdd:PRK08149 82 VWVGEALLGAVLDPTGKIVERFDAPPT-VGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 164 GCGKTSLMSMIVEHSEADIYVIGLIGERGREVTEFVEELKRSSRCSQIVLVYATSDRSCVERCNAAQIATTIAEFFSEQG 243
Cdd:PRK08149 161 GCGKTSLMNMLIEHSEADVFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 244 KNVLLFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFLTGSITAFYTVLIENEEESDVIGDEVRSI 323
Cdd:PRK08149 241 KRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 324 LDGHIYLSKKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDLGEYRRGENPENDAAFDRKN 403
Cdd:PRK08149 321 LDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGEYRRGENADNDRAMDKRP 400
|
410 420
....*....|....*....|....*...
gi 1591723376 404 QMEAFLQQSMDEKTGMQACLESLHGSVA 431
Cdd:PRK08149 401 ALEAFLKQDVAEKSSFSDTLERLNEFAA 428
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
3-427 |
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: 579.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 3 AQCLVHLAHPLRIQGNVIEAHLPGTRIGEICEIQKSLlEPEVLgtAQVIGFNKEHTLLSLLNDNQGFSRSNVLLPTGKPF 82
Cdd:COG1157 14 LPPVRVSGRVTRVVGLLIEAVGPDASIGELCEIETAD-GRPVL--AEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 83 RIDVHKNIAGAIIDATGTVrgrLDNavQQSLTGAQSLEACGAPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAA 162
Cdd:COG1157 91 SVPVGDGLLGRVLDGLGRP---LDG--KGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 163 AGCGKTSLMSMIVEHSEADIYVIGLIGERGREVTEFVEE------LKRSsrcsqiVLVYATSDRSCVERCNAAQIATTIA 236
Cdd:COG1157 166 SGVGKSTLLGMIARNTEADVNVIALIGERGREVREFIEDdlgeegLARS------VVVVATSDEPPLMRLRAAYTATAIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 237 EFFSEQGKNVLLFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFLTGSITAFYTVLIENEEESDVI 316
Cdd:COG1157 240 EYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 317 GDEVRSILDGHIYLSKKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDLGEYRRGENPEND 396
Cdd:COG1157 320 ADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENEDLIRIGAYQPGSDPELD 399
|
410 420 430
....*....|....*....|....*....|.
gi 1591723376 397 AAFDRKNQMEAFLQQSMDEKTGMQACLESLH 427
Cdd:COG1157 400 EAIALIPAIEAFLRQGMDERVSFEESLAQLA 430
|
|
| III_secr_ATP |
TIGR02546 |
type III secretion apparatus H+-transporting two-sector ATPase; [Protein fate, Protein and ... |
12-431 |
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: 511.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 12 PLRIQGNVIEAHLPGTRIGEICEIQKSLLEPEVlgtAQVIGFNKEHTLLSLLNDNQGFSRSNVLLPTGKPFRIDVHKNIA 91
Cdd:TIGR02546 9 VTEVSGTLLKAVLPGARVGELCLIRRRDPSQLL---AEVVGFTGDEALLSPLGELHGISPGSEVIPTGRPLSIRVGEALL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 92 GAIIDATGTVrgrLDNAVQQSLTGAQSLEACGAPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSLM 171
Cdd:TIGR02546 86 GRVLDGFGRP---LDGKGELPAGEIETRPLDADPPPPMSRQPIDQPLPTGVRAIDGLLTCGEGQRIGIFAGAGVGKSTLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 172 SMIVEHSEADIYVIGLIGERGREVTEFVEELKRSSRCSQIVLVYATSDRSCVERCNAAQIATTIAEFFSEQGKNVLLFID 251
Cdd:TIGR02546 163 GMIARGASADVNVIALIGERGREVREFIEHHLGEEGRKRSVLVVSTSDRPSLERLKAAYTATAIAEYFRDQGKRVLLMMD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 252 SITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFLTGSITAFYTVLIENEEESDVIGDEVRSILDGHIYLS 331
Cdd:TIGR02546 243 SLTRFARALREIGLAAGEPPARGGYPPSVFSSLPRLLERAGNGEKGSITALYTVLVEGDDMNDPIADEVRSILDGHIVLS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 332 KKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDLGEYRRGENPENDAAFDRKNQMEAFLQQ 411
Cdd:TIGR02546 323 RALAERNHYPAIDVLASLSRVMSQVVSTEHRRAAGKLRRLLATYKEVELLIRLGEYQPGSDPETDDAIDKIDAIRAFLRQ 402
|
410 420
....*....|....*....|
gi 1591723376 412 SMDEKTGMQACLESLHGSVA 431
Cdd:TIGR02546 403 STDEYSPYEETLEQLHALVA 422
|
|
| FliI_clade1 |
TIGR03496 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
14-426 |
8.31e-160 |
|
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of bacterial flagellum systems. This protein acts to drive protein export for flagellar biosynthesis. The most closely related family is the YscN family of bacterial type III secretion systems. This model represents one (of three) segment of the FliI family tree. These have been modeled separately in order to exclude the type III secretion ATPases more effectively. [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274607 [Multi-domain] Cd Length: 411 Bit Score: 456.94 E-value: 8.31e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 14 RIQGNVIEAHLPGTRIGEICEIQKSllEPEVLgTAQVIGFNKEHTLLSLLNDNQGFSRSNVLLPTGKPFRIDVHKNIAGA 93
Cdd:TIGR03496 5 RVVGLVLEAVGLRAPVGSRCEIESS--DGDPI-EAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLGGPLRLPVGDSLLGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 94 IIDATGTVrgrLDNAVQqsLTGAQSLEACGAPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSLMSM 173
Cdd:TIGR03496 82 VIDGLGRP---LDGKGP--LDAGERVPLYAPPINPLKRAPIDEPLDVGVRAINGLLTVGRGQRMGIFAGSGVGKSTLLGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 174 IVEHSEADIYVIGLIGERGREVTEFVEE------LKRSsrcsqiVLVYATSDRSCVERCNAAQIATTIAEFFSEQGKNVL 247
Cdd:TIGR03496 157 MARYTEADVVVVGLIGERGREVKEFIEDilgeegLARS------VVVAATADESPLMRLRAAFYATAIAEYFRDQGKDVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 248 LFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFLT--GSITAFYTVLIENEEESDVIGDEVRSILD 325
Cdd:TIGR03496 231 LLMDSLTRFAMAQREIALAIGEPPATKGYPPSVFAKLPQLVERAGNGEEgkGSITAFYTVLVEGDDQQDPIADAARAILD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 326 GHIYLSKKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDLGEYRRGENPENDAAFDRKNQM 405
Cdd:TIGR03496 311 GHIVLSRELAEQGHYPAIDILASISRVMPDVVSPEHRQAARRFKQLLSRYQENRDLISIGAYQAGSDPELDQAIALYPRI 390
|
410 420
....*....|....*....|.
gi 1591723376 406 EAFLQQSMDEKTGMQACLESL 426
Cdd:TIGR03496 391 EAFLQQGMRERASFEESLEAL 411
|
|
| FliI_clade2 |
TIGR03497 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
14-430 |
1.47e-153 |
|
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: 440.97 E-value: 1.47e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 14 RIQGNVIEAHLPGTRIGEICEIQKSLlEPEVLgtAQVIGFNKEHTLLSLLNDNQGFSRSNVLLPTGKPFRIDVHKNIAGA 93
Cdd:TIGR03497 5 RVIGLTIESKGPKASIGELCSILTKG-GKPVL--AEVVGFKEENVLLMPLGEVEGIGPGSLVIATGRPLAIKVGKGLLGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 94 IIDATGTVrgrLDNAVQQSLTGAQSLEAcgAPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSLMSM 173
Cdd:TIGR03497 82 VLDGLGRP---LDGEGPIIGEEPYPLDN--PPPNPLKRPRIRDPLETGIKAIDGLLTIGKGQRVGIFAGSGVGKSTLLGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 174 IVEHSEADIYVIGLIGERGREVTEFVEE------LKRSsrcsqiVLVYATSDRSCVERCNAAQIATTIAEFFSEQGKNVL 247
Cdd:TIGR03497 157 IARNAKADINVIALIGERGREVRDFIEKdlgeegLKRS------VVVVATSDQPALMRLKAAFTATAIAEYFRDQGKDVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 248 LFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFLTGSITAFYTVLIENEEESDVIGDEVRSILDGH 327
Cdd:TIGR03497 231 LMMDSVTRFAMAQREIGLAVGEPPTTRGYTPSVFSLLPKLLERSGNSQKGSITGFYTVLVDGDDMNEPIADAVRGILDGH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 328 IYLSKKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDLGEYRRGENPENDAAFDRKNQMEA 407
Cdd:TIGR03497 311 IVLSRELAAKNHYPAIDVLASVSRVMNEIVSEEHKELAGKLRELLAVYKEAEDLINIGAYKRGSNPKIDEAIRYIEKINS 390
|
410 420
....*....|....*....|...
gi 1591723376 408 FLQQSMDEKTGMQACLESLHGSV 430
Cdd:TIGR03497 391 FLKQGIDEKFTFEETVQLLKELL 413
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
6-431 |
5.58e-149 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 430.33 E-value: 5.58e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 6 LVHLAHPLRIQGNV-------IEAHLPGTRIGEICEIQKSLLEPEVLgtAQVIGFNKEHTLLSLLNDNQGFSRSNVLLPT 78
Cdd:PRK06936 14 AIVGSRLIQIRGRVtqvtgtiLKAVVPGVRIGELCYLRNPDNSLSLQ--AEVIGFAQHQALLTPLGEMYGISSNTEVSPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 79 GKPFRIDVHKNIAGAIIDATGTvrgRLDNAvqQSLTGAQSLEACGAPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMG 158
Cdd:PRK06936 92 GTMHQVGVGEHLLGRVLDGLGQ---PFDGG--HPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 159 IFAAAGCGKTSLMSMIVEHSEADIYVIGLIGERGREVTEFVEE------LKRSsrcsqiVLVYATSDRSCVERCNAAQIA 232
Cdd:PRK06936 167 IFAAAGGGKSTLLASLIRSAEVDVTVLALIGERGREVREFIESdlgeegLRKA------VLVVATSDRPSMERAKAGFVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 233 TTIAEFFSEQGKNVLLFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFLTGSITAFYTVLIENEEE 312
Cdd:PRK06936 241 TSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 313 SDVIGDEVRSILDGHIYLSKKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDLGEYRRGEN 392
Cdd:PRK06936 321 TEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIGEYQKGQD 400
|
410 420 430
....*....|....*....|....*....|....*....
gi 1591723376 393 PENDAAFDRKNQMEAFLQQSMDEKTGMQACLESLHGSVA 431
Cdd:PRK06936 401 KEADQAIERIGAIRGFLRQGTHELSHFNETLNLLETLTQ 439
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
14-426 |
9.91e-146 |
|
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: 422.16 E-value: 9.91e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 14 RIQGNVIEAHLPGTRIGEICEIQKSLLEPEVLgtAQVIGFNKEHTLLSLLNDNQGFSRSNVLLPTGKPFRIDVHKNIAGA 93
Cdd:TIGR01026 29 KVKGLLIEAVGPQASVGDLCLIERRGSEGRLV--AEVVGFNGEFVFLMPYEEVEGVRPGSKVLATGEGLSIKVGDGLLGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 94 IIDATGTVRGRLDNAVQQSLTGAQSLeacgAPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSLMSM 173
Cdd:TIGR01026 107 VLDGLGKPIDGKGKFLDNVETEGLIT----APINPLKRAPIREILSTGVRSIDGLLTVGKGQRIGIFAGSGVGKSTLLGM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 174 IVEHSEADIYVIGLIGERGREVTEFVEE------LKRSsrcsqiVLVYATSDRSCVERCNAAQIATTIAEFFSEQGKNVL 247
Cdd:TIGR01026 183 IARNTEADVNVIALIGERGREVREFIEHdlgeegLKRS------VVVVATSDQSPLLRLKGAYVATAIAEYFRDQGKDVL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 248 LFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFLTGSITAFYTVLIENEEESDVIGDEVRSILDGH 327
Cdd:TIGR01026 257 LLMDSVTRFAMAQREIGLAAGEPPATKGYTPSVFSTLPRLLERAGASGKGSITAFYTVLVEGDDMNEPIADSVRGILDGH 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 328 IYLSKKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDLGEYRRGENPENDAAFDRKNQMEA 407
Cdd:TIGR01026 337 IVLSRALAQRGHYPAIDVLASISRLMTAIVSEEHRRAARKFRELLSKYKDNEDLIRIGAYQRGSDRELDFAIAKYPKLER 416
|
410
....*....|....*....
gi 1591723376 408 FLQQSMDEKTGMQACLESL 426
Cdd:TIGR01026 417 FLKQGINEKVNFEESLQQL 435
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
19-426 |
1.12e-136 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 399.19 E-value: 1.12e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 19 VIEAHLPGTRIGEICEIQKSLLEPEVLGTAQvigfnkEHTLLSLLNDNQGFSRSNVLLPTGKPFRIDVHKNIAGAIIDAT 98
Cdd:PRK06820 40 LLRASLPGVAQGELCRIEPQGMLAEVVSIEQ------EMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 99 GTVrgrLDNAvqqSLTGAQSLEACGAPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSLMSMIVEHS 178
Cdd:PRK06820 114 GAP---IDGG---PPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCADS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 179 EADIYVIGLIGERGREVTEFVEELKRSSRCSQIVLVYATSDRSCVERCNAAQIATTIAEFFSEQGKNVLLFIDSITRYAR 258
Cdd:PRK06820 188 AADVMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYAR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 259 ALRDVALSMGELPARRGYPASVFEALPKLLERPGRFLTGSITAFYTVLIENEEESDVIGDEVRSILDGHIYLSKKLAAKG 338
Cdd:PRK06820 268 AAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 339 HYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDLGEYRRGENPENDAAFDRKNQMEAFLQQSMDEKTG 418
Cdd:PRK06820 348 HYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGEYQAGEDLQADEALQRYPAICAFLQQDHSETAH 427
|
....*...
gi 1591723376 419 MQACLESL 426
Cdd:PRK06820 428 LETTLEHL 435
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
92-352 |
7.46e-130 |
|
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: 374.97 E-value: 7.46e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 92 GAIIDATGTVrgrLDNAVQQSLTGAQSLEAcgAPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSLM 171
Cdd:cd01136 10 GRVIDALGEP---LDGKGLPDEPERRPLIA--APPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 172 SMIVEHSEADIYVIGLIGERGREVTEFVEELKRSSRCSQIVLVYATSDRSCVERCNAAQIATTIAEFFSEQGKNVLLFID 251
Cdd:cd01136 85 GMIARNTDADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 252 SITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFLTGSITAFYTVLIENEEESDVIGDEVRSILDGHIYLS 331
Cdd:cd01136 165 SLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRSILDGHIVLS 244
|
250 260
....*....|....*....|.
gi 1591723376 332 KKLAAKGHYPAIDIMQSISRV 352
Cdd:cd01136 245 RRLAERGHYPAIDVLASISRV 265
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
14-417 |
4.45e-128 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 377.14 E-value: 4.45e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 14 RIQGNVIEAHLPGTRIGEICEIQKSLLEPEVLgTAQVIGFNKEHTLLSLLNDNQGFSRSNVLLPTGKPFRIDVHKNIAGA 93
Cdd:PRK07721 24 RVIGLMIESKGPESSIGDVCYIHTKGGGDKAI-KAEVVGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVGSGLIGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 94 IIDATGtvrgrldNAVQQSL--TGAQSLEACGAPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSLM 171
Cdd:PRK07721 103 VLDALG-------EPLDGSAlpKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 172 SMIVEHSEADIYVIGLIGERGREVTEFVEE------LKRSsrcsqiVLVYATSDRSCVERCNAAQIATTIAEFFSEQGKN 245
Cdd:PRK07721 176 GMIARNTSADLNVIALIGERGREVREFIERdlgpegLKRS------IVVVATSDQPALMRIKGAYTATAIAEYFRDQGLN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 246 VLLFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFLTGSITAFYTVLIENEEESDVIGDEVRSILD 325
Cdd:PRK07721 250 VMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTVRGILD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 326 GHIYLSKKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDLGEYRRGENPENDAAFDRKNQM 405
Cdd:PRK07721 330 GHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLINIGAYKRGSSREIDEAIQFYPQI 409
|
410
....*....|..
gi 1591723376 406 EAFLQQSMDEKT 417
Cdd:PRK07721 410 ISFLKQGTDEKA 421
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
28-428 |
1.46e-127 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 376.03 E-value: 1.46e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 28 RIGEICEIQKSllEPEVLGTAQVIGFNKEHTLLSLLNDNQGFSRSNVLLPTGKPFRIDVHKNIAGAIIDATGTV---RGR 104
Cdd:PRK09099 44 TLGELCELRQR--DGTLLQRAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPidgGGP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 105 LDNAVQQSLTGAqsleacgaPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSLMSMIVEHSEADIYV 184
Cdd:PRK09099 122 LDCDELVPVIAA--------PPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQCDVNV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 185 IGLIGERGREVTEFVEELKRSSRCSQIVLVYATSDRSCVERCNAAQIATTIAEFFSEQGKNVLLFIDSITRYARALRDVA 264
Cdd:PRK09099 194 IALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 265 LSMGELPARRGYPASVFEALPKLLERPGRFLTGSITAFYTVLIENEEESDVIGDEVRSILDGHIYLSKKLAAKGHYPAID 344
Cdd:PRK09099 274 LAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAID 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 345 IMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDLGEYRRGENPENDAAFDRKNQMEAFLQQSMDEKTGMQACLE 424
Cdd:PRK09099 354 VLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVGEYRAGSDPVADEAIAKIDAIRDFLSQRTDEYSDPDATLA 433
|
....
gi 1591723376 425 SLHG 428
Cdd:PRK09099 434 ALAE 437
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
1-427 |
2.54e-122 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 362.35 E-value: 2.54e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 1 MVAQCLVHLAHP----------LRIQGNVIEAHLPGTRIGEICEIQksllePEVlGTAQVIGFNKEHTLLSLLNDNQGFS 70
Cdd:PRK07594 4 ELMQRLRLKYPPpdgycrwgriQDVSATLLNAWLPGVFMGELCCIK-----PGE-ELAEVVGINGSKALLSPFTSTIGLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 71 RSNVLLPTGKPFRIDVHKNIAGAIIDATGtvrgrldnavqQSLTGAQSLEAC-----GAPKDFTQRKPIAKSLATGVRAI 145
Cdd:PRK07594 78 CGQQVMALRRRHQVPVGEALLGRVIDGFG-----------RPLDGRELPDVCwkdydAMPPPAMVRQPITQPLMTGIRAI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 146 DGLLTCGKGQRMGIFAAAGCGKTSLMSMIVEHSEADIYVIGLIGERGREVTEFVEE-LKRSSRcSQIVLVYATSDRSCVE 224
Cdd:PRK07594 147 DSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDADSNVLVLIGERGREVREFIDFtLSEETR-KRCVIVVATSDRPALE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 225 RCNAAQIATTIAEFFSEQGKNVLLFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFLTGSITAFYT 304
Cdd:PRK07594 226 RVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFYT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 305 VLIENEEESDVIGDEVRSILDGHIYLSKKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDL 384
Cdd:PRK07594 306 VLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRI 385
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1591723376 385 GEYRRGENPENDAAFDRKNQMEAFLQQSMDEKTGMQACLESLH 427
Cdd:PRK07594 386 GEYQRGVDTDTDKAIDTYPDICTFLRQSKDEVCGPELLIEKLH 428
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
13-426 |
5.23e-114 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 341.71 E-value: 5.23e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 13 LRIQGNVIEAHLPGTRIGEICEIQKSLLEPEVLGTAQVIGFNKEHTLLSLLNDNQGFSRSNVLLPTGKPFRIDVHKNIAG 92
Cdd:PRK05688 32 LRMVGLTLEAEGLRAAVGSRCLVINDDSYHPVQVEAEVMGFSGDKVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 93 AIIDATGTVrgrLDNavQQSLTGAQSLEACGAPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSLMS 172
Cdd:PRK05688 112 RVLDGAGRA---LDG--KGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 173 MIVEHSEADIYVIGLIGERGREVTEFVEE------LKRSsrcsqiVLVYATSDRSCVERCNAAQIATTIAEFFSEQGKNV 246
Cdd:PRK05688 187 MMTRFTEADIIVVGLIGERGREVKEFIEHilgeegLKRS------VVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 247 LLFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPG--RFLTGSITAFYTVLIENEEESDVIGDEVRSIL 324
Cdd:PRK05688 261 LLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGnaEPGGGSITAFYTVLSEGDDQQDPIADSARGVL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 325 DGHIYLSKKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDLGEYRRGENPENDAAFDRKNQ 404
Cdd:PRK05688 341 DGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPH 420
|
410 420
....*....|....*....|..
gi 1591723376 405 MEAFLQQSMDEKTGMQACLESL 426
Cdd:PRK05688 421 LVQFLRQGLRENVSLAQSREQL 442
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
14-426 |
3.47e-113 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 339.37 E-value: 3.47e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 14 RIQGNVIEAhlPGTR--IGEICEIQKSLLEPEvlgtAQVIGFNKEHTLLSLLNDNQGFSRSNVLLPTGKPFRIDVHKNIA 91
Cdd:PRK08972 31 RVVGLTLEA--TGCRapVGSLCSIETMAGELE----AEVVGFDGDLLYLMPIEELRGVLPGARVTPLGEQSGLPVGMSLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 92 GAIIDATGTV---RGRLDNAVQQSLTGAqsleacgaPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKT 168
Cdd:PRK08972 105 GRVIDGVGNPldgLGPIYTDQRASRHSP--------PINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 169 SLMSMIVEHSEADIYVIGLIGERGREVTEFVEEL------KRSsrcsqiVLVYATSDRSCVERCNAAQIATTIAEFFSEQ 242
Cdd:PRK08972 177 VLLGMMTRGTTADVIVVGLVGERGREVKEFIEEIlgeegrARS------VVVAAPADTSPLMRLKGCETATTIAEYFRDQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 243 GKNVLLFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRF--LTGSITAFYTVLIENEEESDVIGDEV 320
Cdd:PRK08972 251 GLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGgpGQGSITAFYTVLTEGDDLQDPIADAS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 321 RSILDGHIYLSKKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDLGEYRRGENPENDAAFD 400
Cdd:PRK08972 331 RAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLYQQNRDLISIGAYKQGSDPRIDNAIR 410
|
410 420
....*....|....*....|....*.
gi 1591723376 401 RKNQMEAFLQQSMDEKTGMQACLESL 426
Cdd:PRK08972 411 LQPAMNAFLQQTMKEAVPYDMSVNML 436
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
14-426 |
9.00e-111 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 332.81 E-value: 9.00e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 14 RIQGNVIEAHLPGTRIGEICEIQKSLLEPEVLGtaQVIGFNKEHTLLSLLNDNQGFSRSNVLLPTGKPFRIDVHKNIAGA 93
Cdd:PRK08472 24 KISPTIIEADGLNPSVGDIVKIESSDNGKECLG--MVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNLLGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 94 IIDATGTVrgrLDNavQQSLTGAQSLEACGAPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSLMSM 173
Cdd:PRK08472 102 VVDPLGRP---IDG--KGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 174 IVEHSEADIYVIGLIGERGREVTEFVEElKRSSRCSQIVLVYATSDRSCVERCNAAQIATTIAEFFSEQGKNVLLFIDSI 253
Cdd:PRK08472 177 IVKGCLAPIKVVALIGERGREIPEFIEK-NLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 254 TRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRF-LTGSITAFYTVLIENEEESDVIGDEVRSILDGHIYLSK 332
Cdd:PRK08472 256 TRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEeGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 333 KLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDLGEYRRGENPENDAAFDRKNQMEAFLQQS 412
Cdd:PRK08472 336 ELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAYQKGNDKELDEAISKKEFMEQFLKQN 415
|
410
....*....|....
gi 1591723376 413 MDEKTGMQACLESL 426
Cdd:PRK08472 416 PNELFPFEQTFEQL 429
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
141-350 |
8.01e-110 |
|
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: 322.00 E-value: 8.01e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 141 GVRAIDGLLTCGKGQRMGIFAAAGCGKTSLMSMIVEHSEADIYVIGLIGERGREVTEFVEELKRSSRCSQIVLVYATSDR 220
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLGSGALKRTVVVVATSDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 221 SCVERCNAAQIATTIAEFFSEQGKNVLLFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFL--TGS 298
Cdd:pfam00006 81 PPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKgkGGS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1591723376 299 ITAFYTVLIENEEESDVIGDEVRSILDGHIYLSKKLAAKGHYPAIDIMQSIS 350
Cdd:pfam00006 161 ITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
94-426 |
1.80e-106 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 321.93 E-value: 1.80e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 94 IIDATGTVR------GRLDNAVQQSLTGAQSLEACGAPKDFTQRKPIAKS-------LATGVRAIDGLLTCGKGQRMGIF 160
Cdd:PRK08927 85 IANAAAAVRpsrawlGRVVNALGEPIDGKGPLPQGPVPYPLRAPPPPAHSrarvgepLDLGVRALNTFLTCCRGQRMGIF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 161 AAAGCGKTSLMSMIVEHSEADIYVIGLIGERGREVTEFVEE------LKRSsrcsqiVLVYATSDRSCVERCNAAQIATT 234
Cdd:PRK08927 165 AGSGVGKSVLLSMLARNADADVSVIGLIGERGREVQEFLQDdlgpegLARS------VVVVATSDEPALMRRQAAYLTLA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 235 IAEFFSEQGKNVLLFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLER--PGRFLTGSITAFYTVLIENEEE 312
Cdd:PRK08927 239 IAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERagPGPIGEGTITGLFTVLVDGDDH 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 313 SDVIGDEVRSILDGHIYLSKKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDLGEYRRGEN 392
Cdd:PRK08927 319 NEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLGAYRAGSD 398
|
330 340 350
....*....|....*....|....*....|....
gi 1591723376 393 PENDAAFDRKNQMEAFLQQSMDEKTGMQACLESL 426
Cdd:PRK08927 399 PEVDEAIRLNPALEAFLRQGKDEATSLAEGYARL 432
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
14-427 |
2.96e-102 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 311.72 E-value: 2.96e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 14 RIQGNVIEA---HLPgtrIGEICEIQ----KSLLEPEvlgtAQVIGFNKEHTLLSLLNDNQG-------FSRSNVLLPTG 79
Cdd:PRK07960 33 RATGLVLEAtglQLP---LGATCVIErqngSETHEVE----SEVVGFNGQRLFLMPLEEVEGilpgarvYARNISGEGLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 80 KPFRIDVHKNIAGAIIDATGTvrgRLDN--AVQQSLTGAQSleacGAPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRM 157
Cdd:PRK07960 106 SGKQLPLGPALLGRVLDGSGK---PLDGlpAPDTGETGALI----TPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 158 GIFAAAGCGKTSLMSMIVEHSEADIYVIGLIGERGREVTEFVEELKRSSRCSQIVLVYATSDRSCVERCNAAQIATTIAE 237
Cdd:PRK07960 179 GLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 238 FFSEQGKNVLLFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFLT--GSITAFYTVLIENEEESDV 315
Cdd:PRK07960 259 DFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISggGSITAFYTVLTEGDDQQDP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 316 IGDEVRSILDGHIYLSKKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDLGEYRRGENPEN 395
Cdd:PRK07960 339 IADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLLSSFQRNRDLVSVGAYAKGSDPML 418
|
410 420 430
....*....|....*....|....*....|..
gi 1591723376 396 DAAFDRKNQMEAFLQQSMDEKTGMQACLESLH 427
Cdd:PRK07960 419 DKAIALWPQLEAFLQQGIFERADWEDSLQALE 450
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
14-431 |
3.48e-99 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 302.97 E-value: 3.48e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 14 RIQGNVIEAHLPGTRIGEICEIQKSllePEVLGTAQVIGFNKEHTLLSLLNDNQGFSRSNVLLPTGKPFRIDVHKNIAGA 93
Cdd:PRK07196 23 RVTGLLLESVGCRLAIGQRCRIESV---DETFIEAQVVGFDRDITYLMPFKHPGGVLGGARVFPSEQDGELLIGDSWLGR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 94 IIDATGTVrgrLDNAVQqsLTGAQSLEACGAPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSLMSM 173
Cdd:PRK07196 100 VINGLGEP---LDGKGQ--LGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 174 IVEHSEADIYVIGLIGERGREVTEFVEELKRSSRCSQIVLVYATSDRSCVERCNAAQIATTIAEFFSEQGKNVLLFIDSI 253
Cdd:PRK07196 175 ITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 254 TRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGR-FLTGSITAFYTVLIENEEESDVIGDEVRSILDGHIYLSK 332
Cdd:PRK07196 255 TRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNsSGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 333 KLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDLGEYRRGENPENDAAFDRKNQMEAFLQQS 412
Cdd:PRK07196 335 KLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVAGADPMADQAVHYYPAITQFLRQE 414
|
410
....*....|....*....
gi 1591723376 413 MDEKTGMQACLESLHGSVA 431
Cdd:PRK07196 415 VGHPALFSASVEQLTGMFP 433
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
81-424 |
1.98e-94 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 291.52 E-value: 1.98e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 81 PFRIDVHKNIAGAIIDATGTV---RGRLdnavqqsLTGAQSLEACGAPKDFTQRKPIAKSLATGVRAIDgLLT--CgKGQ 155
Cdd:PRK06002 96 PLRIRPDPSWKGRVINALGEPidgLGPL-------APGTRPMSIDATAPPAMTRARVETGLRTGVRVID-IFTplC-AGQ 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 156 RMGIFAAAGCGKTSLMSMIVEHSEADIYVIGLIGERGREVTEFVEELKRSSRcSQIVLVYATSDRSCVERCNAAQIATTI 235
Cdd:PRK06002 167 RIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGREVREFLEDTLADNL-KKAVAVVATSDESPMMRRLAPLTATAI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 236 AEFFSEQGKNVLLFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLER--PGRFLTGSITAFYTVLIENEEES 313
Cdd:PRK06002 246 AEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERagPGAEGGGSITGIFSVLVDGDDHN 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 314 DVIGDEVRSILDGHIYLSKKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDLGEYRRGENP 393
Cdd:PRK06002 326 DPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEETRDLRLIGGYRAGSDP 405
|
330 340 350
....*....|....*....|....*....|.
gi 1591723376 394 ENDAAFDRKNQMEAFLQQSMDEKTGMQACLE 424
Cdd:PRK06002 406 DLDQAVDLVPRIYEALRQSPGDPPSDDAFAD 436
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
15-427 |
3.18e-87 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 272.24 E-value: 3.18e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 15 IQGNVIEAHLPGTRIGEICEIQksllEPEVLgtAQVIGFNKEHTLLSLLNDNQGFSRSNVLLPTGKPFRIDVHKNIAGAI 94
Cdd:PRK06793 28 VQEQFFVAKGPKAKIGDVCFVG----EHNVL--CEVIAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 95 IDATGTVrgrLDNAVQQSLTGAQSLEAcgAPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSLMSMI 174
Cdd:PRK06793 102 LSANGEV---LNEEAENIPLQKIKLDA--PPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 175 VEHSEADIYVIGLIGERGREVTEFVEELKRSSRCSQIVLVYATSDRSCVERCNAAQIATTIAEFFSEQGKNVLLFIDSIT 254
Cdd:PRK06793 177 AKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 255 RYARALRDVALSMGELPArrGYPASVFEA-LPKLLERPGRFLTGSITAFYTVLIENEEESDVIGDEVRSILDGHIYLSKK 333
Cdd:PRK06793 257 RFADARRSVDIAVKELPI--GGKTLLMESyMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 334 LAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDLGEYRrgENPENDAAFDRKNQME---AFLQ 410
Cdd:PRK06793 335 LATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGTIQ--ENAENAYIFECKNKVEginTFLK 412
|
410
....*....|....*..
gi 1591723376 411 QSMDEKTGMQACLESLH 427
Cdd:PRK06793 413 QGRSDSFQFDDIVEAMH 429
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
103-352 |
3.45e-78 |
|
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: 243.52 E-value: 3.45e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 103 GRLDNAVQQSLTGA------QSLEACGAPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSLMSMIVE 176
Cdd:cd19476 10 GRILDGLGEPLDGLppiktkQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLAR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 177 HS---EADIYVIGLIGERGREVTEFVEELKRSSRCSQIVLVYATSDRSCVERCNAAQIATTIAEFFSEQGKNVLLFIDSI 253
Cdd:cd19476 90 NQakaHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 254 TRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFLT--GSITAFYTVLIENEEESDVIGDEVRSILDGHIYLS 331
Cdd:cd19476 170 SRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDggGSITAIPAVSTPGDDLTDPIPDNTFAILDGQIVLS 249
|
250 260
....*....|....*....|.
gi 1591723376 332 KKLAAKGHYPAIDIMQSISRV 352
Cdd:cd19476 250 RELARKGIYPAINVLDSTSRV 270
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
14-426 |
1.79e-76 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 244.43 E-value: 1.79e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 14 RIQGNVIEAHLPGTRIGEICEIQKSLlEPEVLgtAQVIGFNKEHTLLSLLNDNQGFSRSNVLLPTGKPFRIDVHKNIAGA 93
Cdd:PRK05922 25 RVSGNLLEAQGLSACLGELCQISLSK-SPPIL--AEVIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 94 IIDATGTvrgRLDNavQQSLTGAQSLEACGAPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSLMSM 173
Cdd:PRK05922 102 VLDGFGN---PLDG--KEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLST 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 174 IVEHSEADIYVIGLIGERGREVTEFVEELKRSSRCSQIVLVYATSDRSCVERCNAAQIATTIAEFFSEQGKNVLLFIDSI 253
Cdd:PRK05922 177 IAKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 254 TRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFLTGSITAFYTVLiENEEESDVIGDEVRSILDGHIYLS-- 331
Cdd:PRK05922 257 SRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIL-HYPNHPDIFTDYLKSLLDGHFFLTpq 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 332 -KKLAAkghyPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDLGEYRRGENPENDAAFDRKNQMEAFLQ 410
Cdd:PRK05922 336 gKALAS----PPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGAYVPGQDAHLDRAVKLLPSIKQFLS 411
|
410
....*....|....*.
gi 1591723376 411 QSMDEKTGMQACLESL 426
Cdd:PRK05922 412 QPLSSYCALHNTLKQL 427
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
125-351 |
1.39e-38 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 140.44 E-value: 1.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 125 PKDFTQrkpiakslaTGVRAIDGLLTCGKGQRMGIFAAAGCGKTSLMSMI------VEHSEADIYVIGLIGERGREVTEF 198
Cdd:cd01135 49 PEEMIQ---------TGISAIDVMNTLVRGQKLPIFSGSGLPHNELAAQIarqagvVGSEENFAIVFAAMGVTMEEARFF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 199 VEELKRSSRCSQIVLVYATSDRSCVERCNAAQIATTIAEFFS-EQGKNVLLFIDSITRYARALRDVALSMGELPARRGYP 277
Cdd:cd01135 120 KDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYP 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1591723376 278 ASVFEALPKLLERPGRF--LTGSITAFYTVLIENEEESDVIGDEVRSILDGHIYLSKKLAAKGHYPAIDIMQSISR 351
Cdd:cd01135 200 GYMYTDLATIYERAGRVegRKGSITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
24-385 |
4.36e-34 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 133.12 E-value: 4.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 24 LPGTRIGEiceiqksLLEPEVLGTAQVIGFNKEHTLLSLLNDNQGFSRSNVLLPTGKPFRIDVHKNIAGAIIDATGTVrg 103
Cdd:PRK13343 44 LPDAALDE-------LLRFEGGSRGFAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRP-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 104 rLD--NAVQqslTGAQSLEACGAPKdFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSL-MSMIVEHSEA 180
Cdd:PRK13343 115 -LDggGPLQ---ATARRPLERPAPA-IIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIaIDAIINQKDS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 181 D---IYVigLIGERGREVTEFVEELKRS---SRCsqIVLVYATSDRScvercnAAQ-IA----TTIAEFFSEQGKNVLLF 249
Cdd:PRK13343 190 DvicVYV--AIGQKASAVARVIETLREHgalEYT--TVVVAEASDPP------GLQyLApfagCAIAEYFRDQGQDALIV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 250 IDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFL----TGSITAFYTVLIENEEESDVIGDEVRSILD 325
Cdd:PRK13343 260 YDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSpelgGGSLTALPIIETLAGELSAYIPTNLISITD 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 326 GHIYLSKKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEMQLYLDLG 385
Cdd:PRK13343 340 GQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFG 399
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
124-352 |
9.43e-33 |
|
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: 124.64 E-value: 9.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 124 APKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSL-MSMI--VEHSEADIYVIGLIGERGREVTEFVE 200
Cdd:cd01133 37 EAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLiMELInnIAKAHGGYSVFAGVGERTREGNDLYH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 201 ELKRSS-----RCSQIVLVYATSDRSCVERCNAAQIATTIAEFF-SEQGKNVLLFIDSITRYARALRDVALSMGELPARR 274
Cdd:cd01133 117 EMKESGvinldGLSKVALVYGQMNEPPGARARVALTGLTMAEYFrDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAV 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1591723376 275 GYPASVFEALPKLLERPGRFLTGSITAFYTVLIENEEESDVIGDEVRSILDGHIYLSKKLAAKGHYPAIDIMQSISRV 352
Cdd:cd01133 197 GYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
130-352 |
1.82e-32 |
|
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: 123.82 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 130 QRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSL-MSMIVEHSEADIYVIGL-IGERGREVTEFVEELKRSSR 207
Cdd:cd01132 45 PRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTAIaIDTIINQKGKKVYCIYVaIGQKRSTVAQIVKTLEEHGA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 208 CSQIVLVYATSDRSCVERCNAAQIATTIAEFFSEQGKNVLLFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKL 287
Cdd:cd01132 125 MEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRL 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1591723376 288 LERPGRF----LTGSITAFYTVLIENEEESDVIGDEVRSILDGHIYLSKKLAAKGHYPAIDIMQSISRV 352
Cdd:cd01132 205 LERAAKLsdelGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRV 273
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
14-351 |
3.26e-32 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 127.25 E-value: 3.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 14 RIQGNVIEA-HLPGTRIGEICEIQkslLEPEVLGTAQVIGFNKEHTLLSLLNDNQGFSRSNVLLP-TGKPFRIDVHKNIA 91
Cdd:PRK04196 9 EIKGPLLFVeGVEGVAYGEIVEIE---LPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRfTGEPLKLPVSEDML 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 92 GAIIDATGTVRgrlDNAvqQSLTGAQSLEACGAPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSLM 171
Cdd:PRK04196 86 GRIFDGLGRPI---DGG--PEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 172 SMIVEH-----SEADIYVI-GLIGERGREVTEFVEELKRSSRCSQIVLVYATSDRSCVERCNAAQIATTIAEFFS-EQGK 244
Cdd:PRK04196 161 AQIARQakvlgEEENFAVVfAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAfEKGM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 245 NVLLFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFL--TGSITAFYTVLIENEEESDVIGDEVRS 322
Cdd:PRK04196 241 HVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKgkKGSITQIPILTMPDDDITHPIPDLTGY 320
|
330 340
....*....|....*....|....*....
gi 1591723376 323 ILDGHIYLSKKLAAKGHYPAIDIMQSISR 351
Cdd:PRK04196 321 ITEGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
125-351 |
1.16e-31 |
|
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: 121.91 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 125 PKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSLMSMIVEHSEADIYVIGLIGERGREVTEFVEE--- 201
Cdd:cd01134 47 PRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEVLEEfpe 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 202 LKRSSRCSQI----VLVYATSDRSCVERcnAAQIAT--TIAEFFSEQGKNVLLFIDSITRYARALRDVALSMGELPARRG 275
Cdd:cd01134 127 LKDPITGESLmertVLIANTSNMPVAAR--EASIYTgiTIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 276 YPASVFEALPKLLERPGRFLT-------GSITAFYTVLIENEEESDVIGDEVRSILDGHIYLSKKLAAKGHYPAIDIMQS 348
Cdd:cd01134 205 YPAYLGARLAEFYERAGRVRClgspgreGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLIS 284
|
...
gi 1591723376 349 ISR 351
Cdd:cd01134 285 YSK 287
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
25-411 |
1.90e-31 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 125.54 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 25 PGTRIGEICEIQksllepevlgtaQVIGFNKEHTLLslLNDNQGFSRSNVLLPTGKPFRIDVHK-------NIAGAIIDA 97
Cdd:CHL00060 51 AGQEINVTCEVQ------------QLLGNNRVRAVA--MSATDGLMRGMEVIDTGAPLSVPVGGatlgrifNVLGEPVDN 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 98 TGTVRGRLDNAVQQSltgaqsleacgAPKdFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSL-MSMIVE 176
Cdd:CHL00060 117 LGPVDTRTTSPIHRS-----------APA-FIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLiMELINN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 177 HSEAD--IYVIGLIGERGREVTEFVEELKRSSRC-------SQIVLVYATSDRSCVERCNAAQIATTIAEFFSEQGK-NV 246
Cdd:CHL00060 185 IAKAHggVSVFGGVGERTREGNDLYMEMKESGVIneqniaeSKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 247 LLFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFLTGSITAFYTVLIENEEESDVIGDEVRSILDG 326
Cdd:CHL00060 265 LLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 327 HIYLSKKLAAKGHYPAIDIMQSISrVFLQ--VTDPEHRQLAKRFREYLVRQKEMQ-----LYLD-LGEyrrgenpENDAA 398
Cdd:CHL00060 345 TTVLSRGLAAKGIYPAVDPLDSTS-TMLQprIVGEEHYETAQRVKQTLQRYKELQdiiaiLGLDeLSE-------EDRLT 416
|
410
....*....|...
gi 1591723376 399 FDRKNQMEAFLQQ 411
Cdd:CHL00060 417 VARARKIERFLSQ 429
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
14-365 |
6.69e-29 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 117.44 E-value: 6.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 14 RIQGNVIEAHLPGTRIGEICEIQKSllepEVLGTAQVIGFNKEHTLLSLLNDNQGFSRSNVLLPTGKPFRIDVHKNIAGA 93
Cdd:PRK02118 10 DITGNVITVEAEGVGYGELATVERK----DGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 94 IIDATGTVRgrlDNAvqQSLTGaQSLEACGAPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSLMSM 173
Cdd:PRK02118 86 RFNGSGKPI---DGG--PELEG-EPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 174 IVEHSEADIYVIGLIGERGREVTEFVEELKRSSRCSQIVLVYATSDRSCVERCNAAQIATTIAEFFS-EQGKNVLLFIDS 252
Cdd:PRK02118 160 IALQAEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 253 ITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFL-TGSITAFYTVLIENEEESDVIGDEVRSILDGHIYLs 331
Cdd:PRK02118 240 MTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEdGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYL- 318
|
330 340 350
....*....|....*....|....*....|....*...
gi 1591723376 332 kklaakgHYPAIDIMQSISR----VFLQVTDPEHRQLA 365
Cdd:PRK02118 319 -------RRGRIDPFGSLSRlkqlVIGKKTREDHGDLM 349
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
125-412 |
7.66e-28 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 116.03 E-value: 7.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 125 PKDFTQRKPIAKSLATGVRAIDGLLTCGKGqrmGifAAA-----GCGKTSLMSMIVEHSEADIYVIGLIGERGREVTEFV 199
Cdd:PRK04192 198 PRPYKEKLPPVEPLITGQRVIDTFFPVAKG---G--TAAipgpfGSGKTVTQHQLAKWADADIVIYVGCGERGNEMTEVL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 200 EELKRssrcsqivLVYATSDRSCVER----CN------AAQIA-----TTIAEFFSEQGKNVLLFIDSITRYARALRDVA 264
Cdd:PRK04192 273 EEFPE--------LIDPKTGRPLMERtvliANtsnmpvAAREAsiytgITIAEYYRDMGYDVLLMADSTSRWAEALREIS 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 265 LSMGELPARRGYPASVFEALPKLLERPGRFLT-----GSITAFYTVlieneeeSDVIGD--E---------VRSILDghi 328
Cdd:PRK04192 345 GRLEEMPGEEGYPAYLASRLAEFYERAGRVKTlggeeGSVTIIGAV-------SPPGGDfsEpvtqntlriVKVFWA--- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 329 yLSKKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYlvRQKEMQLYL---DLGEYRR--GEN--PEND----- 396
Cdd:PRK04192 415 -LDAELADRRHFPAINWLTSYSLYLDQVAPWWEENVDPDWREL--RDEAMDLLQreaELQEIVRlvGPDalPEEDrlile 491
|
330
....*....|....*..
gi 1591723376 397 -AAFDRknqmEAFLQQS 412
Cdd:PRK04192 492 vARLIR----EDFLQQN 504
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
75-371 |
2.47e-27 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 113.91 E-value: 2.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 75 LLPTGKPFRIDVHKNIAGAIIDATGTVRGRLDNAVQQSLTGAQSLEACGAPKDFTQRKPIAKSLATGVRAIDGLLTCGKG 154
Cdd:PRK07165 64 LIELNNTNKVKTSKEYFGKIIDIDGNIIYPEAQNPLSKKFLPNTSSIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 155 QRMGIFAAAGCGKTSL-MSMIVEHSEAD---IYVIglIGERGREVTEFVEELKRSSRCSQIVLVYATSDrSCVERCNAAQ 230
Cdd:PRK07165 144 QRELIIGDRQTGKTHIaLNTIINQKNTNvkcIYVA--IGQKRENLSRIYETLKEHDALKNTIIIDAPST-SPYEQYLAPY 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 231 IATTIAEFFSeQGKNVLLFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFLTG-SITAFYTVLIEN 309
Cdd:PRK07165 221 VAMAHAENIS-YNDDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNRkTITALPILQTVD 299
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1591723376 310 EEESDVIGDEVRSILDGHIYLSKKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLA----KRFREY 371
Cdd:PRK07165 300 NDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAgeisKIYRAY 365
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
59-401 |
3.81e-26 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 108.63 E-value: 3.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 59 LLSLLNDNQGFSRS----------NVLLPTGKPFRIDVHKniaGAIIDATGTVRGRldnavQQSLTGAQSL-----EACG 123
Cdd:PRK12608 22 VLEILGDGFGFLRSarrnylpspdDVFVPPALIRRFNLRT---GDVVEGVARPRER-----YRVLVRVDSVngtdpEKLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 124 APKDFTQRKPIAKS----LATG-----VRAIDGLLTCGKGQRMGIFAAAGCGKTSLMSMI-----VEHSEADIYVIgLIG 189
Cdd:PRK12608 94 RRPHFDDLTPLHPRerlrLETGsddlsMRVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIaaavaANHPEVHLMVL-LID 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 190 ERGREVTEFveelKRSSRCSqivlVYA-TSDRSCVERCNAAQIATTIAEFFSEQGKNVLLFIDSITRYARALRDVALSMG 268
Cdd:PRK12608 173 ERPEEVTDM----RRSVKGE----VYAsTFDRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAYNNEVESSG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 269 ELPArRGYPASVfealpklLERPGRFL--------TGSITAFYTVLIENEEESD-VIGDEVRSILDGHIYLSKKLAAKGH 339
Cdd:PRK12608 245 RTLS-GGVDARA-------LQRPKRLFgaarnieeGGSLTIIATALVDTGSRMDeVIFEEFKGTGNMEIVLDRELADKRV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1591723376 340 YPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVR---QKEMQLYLDLGEyrrgENPENDAAFDR 401
Cdd:PRK12608 317 FPAIDIAKSGTRREELLLDSKELEKVRRLRRALASrkpVEAMEALLEKLR----ETPDNAEFLNS 377
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
143-379 |
9.01e-24 |
|
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: 99.20 E-value: 9.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 143 RAIDGLLTCGKGQRMGIFAAAGCGKTSLMSMIVE-----HSEADIYVIgLIGERGREVTEFveelKRSSRCSqivLVYAT 217
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANaiaknHPEVELIVL-LIDERPEEVTDM----RRSVKGE---VVAST 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 218 SDRSCVERCNAAQIATTIAEFFSEQGKNVLLFIDSITRYARALRDVALSMGelparRGYPASVFealPKLLERPGRFL-- 295
Cdd:cd01128 77 FDEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSG-----KTLSGGVD---ANALHKPKRFFga 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 296 ------TGSITAFYTVLIENEEESD-VIGDEVRSILDGHIYLSKKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRF 368
Cdd:cd01128 149 arnieeGGSLTIIATALVDTGSRMDeVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTRKEELLLTPEELQKIWLL 228
|
250
....*....|.
gi 1591723376 369 REYLVRQKEMQ 379
Cdd:cd01128 229 RRILSPMDPIE 239
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
77-352 |
1.12e-23 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 102.73 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 77 PTGKPFRIDVHKNIAGAIIDATGT-VRGRLDNAVQQSltgaQSLEAcGAPkDFTQRKPIAKSLATGVRAIDGLLTCGKGQ 155
Cdd:CHL00059 69 ATGKIAQIPVSEAYLGRVVNALAKpIDGKGEISASES----RLIES-PAP-GIISRRSVYEPLQTGLIAIDSMIPIGRGQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 156 RMGIFAAAGCGKTSLM--SMIVEHSEADIYVIGLIGERGREVTEFVEELKRSSRCSQIVLVYATSDRSCVERCNAAQIAT 233
Cdd:CHL00059 143 RELIIGDRQTGKTAVAtdTILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 234 TIAEFFSEQGKNVLLFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFLT----GSITAFytVLIEN 309
Cdd:CHL00059 223 ALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSqlgeGSMTAL--PIVET 300
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1591723376 310 eEESDV---IGDEVRSILDGHIYLSKKLAAKGHYPAIDIMQSISRV 352
Cdd:CHL00059 301 -QAGDVsayIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRV 345
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
25-378 |
3.88e-23 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 102.04 E-value: 3.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 25 PGTRIGEICEIQKSllePEVLGTAQVIGFNKEHTLLSLLNDNQGFSRS-NVLLPTGKPFRIDVHKNIAGAIIDATG-TVR 102
Cdd:PTZ00185 60 PGVAYNTIIMIQVS---PTTFAAGLVFNLEKDGRIGIILMDNITEVQSgQKVMATGKLLYIPVGAGVLGKVVNPLGhEVP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 103 GRLDNAVQQSLTGAQSLEA--CGAPkDFTQRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSL-MSMIVEH-- 177
Cdd:PTZ00185 137 VGLLTRSRALLESEQTLGKvdAGAP-NIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIaVSTIINQvr 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 178 -------SEADIYVIGLIGERGREVTEFVEELKRSSRCSQIVLVYATSDRSCVERCNAAQIATTIAEFFSEQGKNVLLFI 250
Cdd:PTZ00185 216 inqqilsKNAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVY 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 251 DSITRYARALRDVALSMGELPARRGYPASVFEALPKLLER-----PGRFlTGSITAFYTVLIENEEESDVIGDEVRSILD 325
Cdd:PTZ00185 296 DDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERaamlsPGKG-GGSVTALPIVETLSNDVTAYIVTNVISITD 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1591723376 326 GHIYLSKKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRFREYLVRQKEM 378
Cdd:PTZ00185 375 GQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAMKAVAGKLKGILAEYRKL 427
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
78-352 |
3.99e-23 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 100.95 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 78 TGKPFRIDVHKNIAGAIIDATGTVrgrLDNAvqQSLTGAQSLEACGAPKDFTQRKPIAKSLATGVRAIDGLLTCGKGQRM 157
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKP---IDKG--PPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 158 GIFAAAG----------CGKTSLMS----MIVEHSEADI-YVIGLIGERGREVTEFVEELKRSSRCSQIVLVYATSDRSC 222
Cdd:TIGR01040 145 PIFSAAGlphneiaaqiCRQAGLVKlptkDVHDGHEDNFaIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 223 VERCNAAQIATTIAEFFSEQ-GKNVLLFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFL--TGSI 299
Cdd:TIGR01040 225 IERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrNGSI 304
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1591723376 300 TAFYTVLIENEEESDVIGDEVRSILDGHIYLSKKLAAKGHYPAIDIMQSISRV 352
Cdd:TIGR01040 305 TQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRL 357
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
357-426 |
4.97e-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: 86.33 E-value: 4.97e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 357 TDPEHRQLAKRFREYLVRQKEMQLYLDLGEYRRGENPENDAAFDRKNQMEAFLQQSMDEKTGMQACLESL 426
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIGAYQAGSDPEIDEAIAKRPAINAFLRQGVDEPVSFEETLAQL 70
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
168-379 |
5.46e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 92.78 E-value: 5.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 168 TSLMSMIVEH-----SEADIYVIGLIGERGREVTEFVEELKR-------SSRCSQIVLVYATSDRSCVERCNAAQIATTI 235
Cdd:PRK14698 665 TLLHNTVTQHqlakwSDAQVVIYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITI 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 236 AEFFSEQGKNVLLFIDSITRYARALRDVALSMGELPARRGYPASVFEALPKLLERPGRFLT-------GSITAFYTVLIE 308
Cdd:PRK14698 745 AEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTlgsdyrvGSVSVIGAVSPP 824
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1591723376 309 NEEESDVIGDEVRSILDGHIYLSKKLAAKGHYPAIDIMQSISRVFLQV-------TDPEHRQLAKRFREYLVRQKEMQ 379
Cdd:PRK14698 825 GGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVkdwwhknVDPEWKAMRDKAMELLQKEAELQ 902
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
143-372 |
1.07e-19 |
|
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: 90.52 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 143 RAIDGLLTCGKGQRMGIFAAAGCGKTSLM-----SMIVEHSEADIYVIgLIGERGREVTEfveeLKRSSRCSqivLVYAT 217
Cdd:TIGR00767 157 RVLDLFAPIGKGQRGLIVAPPKAGKTVLLqkiaqAITRNHPEVELIVL-LIDERPEEVTD----MQRSVKGE---VVAST 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 218 SDRSCVERCNAAQIATTIAEFFSEQGKNVLLFIDSITRYARALRDVALSMGELPArRGYPASVfealpklLERPGRFL-- 295
Cdd:TIGR00767 229 FDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKVLS-GGVDANA-------LHRPKRFFga 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 296 ------TGSITAFYTVLIENEEESD-VIGDEVRSILDGHIYLSKKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQLAKRF 368
Cdd:TIGR00767 301 arnieeGGSLTIIATALIDTGSRMDeVIFEEFKGTGNMELHLDRKLADRRIFPAIDIKKSGTRKEELLLTPEELQKIWVL 380
|
....
gi 1591723376 369 REYL 372
Cdd:TIGR00767 381 RKII 384
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
130-352 |
4.27e-18 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 86.27 E-value: 4.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 130 QRKPIAKSLATGVRAIDGLLTCGKGQRMGIFAAAGCGKTSL-MSMIVEHSEAD---IYVIglIGERGREVTEFVEELKRS 205
Cdd:PRK09281 138 DRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIaIDTIINQKGKDvicIYVA--IGQKASTVAQVVRKLEEH 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 206 SRCSQIVLVYATSDRScvercnAAQ--IA----TTIAEFFSEQGKNVLLFIDSITRYARALRDVALSMGELPARRGYPAS 279
Cdd:PRK09281 216 GAMEYTIVVAATASDP------APLqyLApyagCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGD 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 280 VFEALPKLLERPGRFL----TGSITAfytvL--IENEEeSDV---IGDEVRSILDGHIYLSKKLAAKGHYPAIDIMQSIS 350
Cdd:PRK09281 290 VFYLHSRLLERAAKLSdelgGGSLTA----LpiIETQA-GDVsayIPTNVISITDGQIFLESDLFNAGIRPAINVGISVS 364
|
..
gi 1591723376 351 RV 352
Cdd:PRK09281 365 RV 366
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
9-80 |
2.03e-16 |
|
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: 73.50 E-value: 2.03e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1591723376 9 LAHPLRIQGNVIEAHLPG-TRIGEICEIQKSLLEPEVLGTAQVIGFNKEHTLLSLLNDNQGFSRSNVLLPTGK 80
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGeVAIGEVCEIERGDGNNETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
143-372 |
7.06e-16 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 79.03 E-value: 7.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 143 RAIDGLLTCGKGQRMGIFAAAGCGKTSLMSMI---VEHSEADIYVIG-LIGERGREVTEFveelKRSSRCSqivLVYATS 218
Cdd:PRK09376 158 RIIDLIAPIGKGQRGLIVAPPKAGKTVLLQNIansITTNHPEVHLIVlLIDERPEEVTDM----QRSVKGE---VVASTF 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 219 DRSCVERCNAAQIATTIAEFFSEQGKNVLLFIDSITRYARALRDVALSMGELparrgypasvfeaL-----PKLLERPGR 293
Cdd:PRK09376 231 DEPAERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKV-------------LsggvdANALHRPKR 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 294 FL--------TGSITAFYTVLIENEEESD-VIGDEVRSILDGHIYLSKKLAAKGHYPAIDIMQSISRVFLQVTDPEHRQL 364
Cdd:PRK09376 298 FFgaarnieeGGSLTIIATALIDTGSRMDeVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINRSGTRKEELLLSPEELQK 377
|
....*...
gi 1591723376 365 AKRFREYL 372
Cdd:PRK09376 378 VWILRKIL 385
|
|
| Rho |
COG1158 |
Transcription termination factor Rho [Transcription]; |
143-348 |
2.21e-13 |
|
Transcription termination factor Rho [Transcription];
Pssm-ID: 440772 [Multi-domain] Cd Length: 373 Bit Score: 71.21 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 143 RAIDgLLT-CGKGQRMGIFAAAGCGKTSLMSMIVE-----HSEADIYVIgLIGERGREVTEFveelKRSsrcsqiV---L 213
Cdd:COG1158 113 RVID-LVApIGKGQRGLIVAPPKAGKTTLLQDIANaitanHPEVHLIVL-LIDERPEEVTDM----QRS------VkgeV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 214 VYATSDRScvercnaAQIATTIAEF-------FSEQGKNVLLFIDSITRYARALRDVA------LSmGELPARrgypAsv 280
Cdd:COG1158 181 IASTFDEP-------AERHVQVAELvierakrLVELGKDVVILLDSITRLARAYNLVVpasgrtLS-GGVDAN----A-- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 281 fealpklLERPGRFLT--------GSITAFYTVLIENeeES---DVIGDEVRsildG----HIYLSKKLAAKGHYPAIDI 345
Cdd:COG1158 247 -------LYKPKRFFGaarnieegGSLTIIATALVDT--GSrmdEVIFEEFK----GtgnmELHLDRKLAEKRIFPAIDI 313
|
...
gi 1591723376 346 MQS 348
Cdd:COG1158 314 NKS 316
|
|
| ATP-synt_flagellum-secretory_path_III_C |
cd18114 |
Flagellum-specific ATP synthase, C-terminal domain; The C-terminal domain of the ... |
361-426 |
3.17e-12 |
|
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: 61.47 E-value: 3.17e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1591723376 361 HRQLAKRFREYLVRQKEMQLYLDLGEYRRGENPENDAAFDRKNQMEAFLQQSMDEKTGMQACLESL 426
Cdd:cd18114 1 HYLAARKFRELMSTYQENEDLIRIGAYKKGSDPEVDEAIRLKPQIEAFLKQGLNEKAPLEESLQQL 66
|
|
| ATP-synt_flagellum-secretory_path_III_N |
cd18117 |
Flagellum-specific ATP synthase, N-terminal domain; The N-terminal domain of the ... |
14-80 |
4.94e-08 |
|
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: 49.83 E-value: 4.94e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1591723376 14 RIQGNVIEAHLPGTRIGEICEIQKSLLEPEVlgtAQVIGFNKEHTLLSLLNDNQGFSRSNVLLPTGK 80
Cdd:cd18117 7 RVVGLLLEAVGPQAPIGELCLIETADGLSIL---AEVVGFSGEKVLLMPLGELSGLSPGARVVPLGR 70
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
141-351 |
6.94e-06 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 48.36 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 141 GVRAIDGLLTCGKGQRMGIFAAAGCGKTSLMSMI-----VEHSEADIYVIgLIGERGREVTEFveelKRSSRCSQIvlvY 215
Cdd:PRK12678 403 TTRVIDLIMPIGKGQRGLIVSPPKAGKTTILQNIanaitTNNPECHLMVV-LVDERPEEVTDM----QRSVKGEVI---A 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 216 ATSDRSCVERCNAAQIATTIAEFFSEQGKNVLLFIDSITRYARALRDVA------LSmGELPARRGYPasvfealPKlle 289
Cdd:PRK12678 475 STFDRPPSDHTTVAELAIERAKRLVELGKDVVVLLDSITRLGRAYNLAApasgriLS-GGVDSTALYP-------PK--- 543
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1591723376 290 rpgRFL--------TGSITAFYTVLIENEEESD-VIGDEVRSILDGHIYLSKKLAAKGHYPAIDIMQSISR 351
Cdd:PRK12678 544 ---RFFgaarnienGGSLTIIATALVETGSKMDeVIFEEFKGTGNMELKLDRKLADKRIFPAVDVNASGTR 611
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
153-334 |
1.39e-04 |
|
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: 41.98 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 153 KGQRMGIFAAAGCGKTSLMSMIvehseadiyvIGLIGERGREVTEFVEELKRSSRCSQIVLVYATSDRSCVERCNAAQIA 232
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL----------ARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591723376 233 TTIAeffsEQGKNVLLFIDSITRYARALRDVALSMGElparrgypasvFEALPKLLERPGRFltgsitafyTVLIENEEE 312
Cdd:smart00382 71 LALA----RKLKPDVLILDEITSLLDAEQEALLLLLE-----------ELRLLLLLKSEKNL---------TVILTTNDE 126
|
170 180
....*....|....*....|..
gi 1591723376 313 SDVIGDEVRSILDGHIYLSKKL 334
Cdd:smart00382 127 KDLGPALLRRRFDRRIVLLLIL 148
|
|
| |
