|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
4-429 |
0e+00 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 822.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 4 PRLLQYLAYPQKITGPIIEAELRDVAIGELCEIRRGWHQKQVVARAQVVGLQRERTVLSLIGNAQGLTRDVVLYPTGRAL 83
Cdd:PRK08149 1 LRLLQRLAHPLRIQGPIIEAELPDVAIGEICEIRAGWHSNEVIARAQVVGFQRERTILSLIGNAQGLSRQVVLKPTGKPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 84 SAWVGYSVLGAVLDPTGKIIERFTSEVAP--ISEERVIDVAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASA 161
Cdd:PRK08149 81 SVWVGEALLGAVLDPTGKIVERFDAPPTVgpISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 162 GCGKTMLMHMLIEQTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQG 241
Cdd:PRK08149 161 GCGKTSLMNMLIEHSEADVFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 242 KRVVLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSEGSITAFYTVLLESEEEADPMADEIRSI 321
Cdd:PRK08149 241 KRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 322 LDGHLYLSRKLAGQGHYPAIDVLKSVSRVFGQVTTPTHAEQASAVRKLMTRLEELQLFIDLGEYRPGENIENDRAMQMRD 401
Cdd:PRK08149 321 LDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGEYRRGENADNDRAMDKRP 400
|
410 420
....*....|....*....|....*...
gi 554684202 402 SLKAWLCQSVAQYSSFDDTLSGMNAFAD 429
Cdd:PRK08149 401 ALEAFLKQDVAEKSSFSDTLERLNEFAA 428
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
1-426 |
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: 584.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 1 MKTPRLLQYLAYPQKITGPIIEAELRDVAIGELCEIRRGWHQKqvvARAQVVGLQRERTVLSLIGNAQGLTRDVVLYPTG 80
Cdd:COG1157 11 LEELPPVRVSGRVTRVVGLLIEAVGPDASIGELCEIETADGRP---VLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 81 RALSAWVGYSVLGAVLDPTGKIIERFtsevAPI--SEERVIDVAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIF 158
Cdd:COG1157 88 RPLSVPVGDGLLGRVLDGLGRPLDGK----GPLpgEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 159 ASAGCGKTMLMHMLIEQTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFR 238
Cdd:COG1157 164 AGSGVGKSTLLGMIARNTEADVNVIALIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEYFR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 239 DQGKRVVLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSEGSITAFYTVLLESEEEADPMADEI 318
Cdd:COG1157 244 DQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 319 RSILDGHLYLSRKLAGQGHYPAIDVLKSVSRVFGQVTTPTHAEQASAVRKLMTRLEELQLFIDLGEYRPGENIENDRAMQ 398
Cdd:COG1157 324 RGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENEDLIRIGAYQPGSDPELDEAIA 403
|
410 420
....*....|....*....|....*...
gi 554684202 399 MRDSLKAWLCQSVAQYSSFDDTLSGMNA 426
Cdd:COG1157 404 LIPAIEAFLRQGMDERVSFEESLAQLAE 431
|
|
| III_secr_ATP |
TIGR02546 |
type III secretion apparatus H+-transporting two-sector ATPase; [Protein fate, Protein and ... |
5-429 |
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: 573.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 5 RLLQYLAYPQKITGPIIEAELRDVAIGELCEIRRgwhQKQVVARAQVVGLQRERTVLSLIGNAQGLTRDVVLYPTGRALS 84
Cdd:TIGR02546 1 QPVRVRGRVTEVSGTLLKAVLPGARVGELCLIRR---RDPSQLLAEVVGFTGDEALLSPLGELHGISPGSEVIPTGRPLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 85 AWVGYSVLGAVLDPTGKIIERFTSEVAPISEERVIDVAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCG 164
Cdd:TIGR02546 78 IRVGEALLGRVLDGFGRPLDGKGELPAGEIETRPLDADPPPPMSRQPIDQPLPTGVRAIDGLLTCGEGQRIGIFAGAGVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 165 KTMLMHMLIEQTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQGKRV 244
Cdd:TIGR02546 158 KSTLLGMIARGASADVNVIALIGERGREVREFIEHHLGEEGRKRSVLVVSTSDRPSLERLKAAYTATAIAEYFRDQGKRV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 245 VLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSEGSITAFYTVLLESEEEADPMADEIRSILDG 324
Cdd:TIGR02546 238 LLMMDSLTRFARALREIGLAAGEPPARGGYPPSVFSSLPRLLERAGNGEKGSITALYTVLVEGDDMNDPIADEVRSILDG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 325 HLYLSRKLAGQGHYPAIDVLKSVSRVFGQVTTPTHAEQASAVRKLMTRLEELQLFIDLGEYRPGENIENDRAMQMRDSLK 404
Cdd:TIGR02546 318 HIVLSRALAERNHYPAIDVLASLSRVMSQVVSTEHRRAAGKLRRLLATYKEVELLIRLGEYQPGSDPETDDAIDKIDAIR 397
|
410 420
....*....|....*....|....*
gi 554684202 405 AWLCQSVAQYSSFDDTLSGMNAFAD 429
Cdd:TIGR02546 398 AFLRQSTDEYSPYEETLEQLHALVA 422
|
|
| FliI_clade1 |
TIGR03496 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
15-424 |
1.93e-150 |
|
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: 433.06 E-value: 1.93e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 15 KITGPIIEAELRDVAIGELCEIRRgwHQKQVVaRAQVVGLQRERTVLSLIGNAQGLTRDVVLYPTGRALSAWVGYSVLGA 94
Cdd:TIGR03496 5 RVVGLVLEAVGLRAPVGSRCEIES--SDGDPI-EAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLGGPLRLPVGDSLLGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 95 VLDPTGKIIERFTsevAPISEERV-IDVAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTMLMHMLI 173
Cdd:TIGR03496 82 VIDGLGRPLDGKG---PLDAGERVpLYAPPINPLKRAPIDEPLDVGVRAINGLLTVGRGQRMGIFAGSGVGKSTLLGMMA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 174 EQTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQGKRVVLFIDSMTR 253
Cdd:TIGR03496 159 RYTEADVVVVGLIGERGREVKEFIEDILGEEGLARSVVVAATADESPLMRLRAAFYATAIAEYFRDQGKDVLLLMDSLTR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 254 YARALRDVALASGERPARRGYPASVFDNLPRLLER--PGATSEGSITAFYTVLLESEEEADPMADEIRSILDGHLYLSRK 331
Cdd:TIGR03496 239 FAMAQREIALAIGEPPATKGYPPSVFAKLPQLVERagNGEEGKGSITAFYTVLVEGDDQQDPIADAARAILDGHIVLSRE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 332 LAGQGHYPAIDVLKSVSRVFGQVTTPTHAEQASAVRKLMTRLEELQLFIDLGEYRPGENIENDRAMQMRDSLKAWLCQSV 411
Cdd:TIGR03496 319 LAEQGHYPAIDILASISRVMPDVVSPEHRQAARRFKQLLSRYQENRDLISIGAYQAGSDPELDQAIALYPRIEAFLQQGM 398
|
410
....*....|...
gi 554684202 412 AQYSSFDDTLSGM 424
Cdd:TIGR03496 399 RERASFEESLEAL 411
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
5-428 |
5.64e-149 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 430.33 E-value: 5.64e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 5 RLLQYLAYPQKITGPIIEAELRDVAIGELCEIRRGWHQKQVvaRAQVVGLQRERTVLSLIGNAQGLTRDVVLYPTGRALS 84
Cdd:PRK06936 19 RLIQIRGRVTQVTGTILKAVVPGVRIGELCYLRNPDNSLSL--QAEVIGFAQHQALLTPLGEMYGISSNTEVSPTGTMHQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 85 AWVGYSVLGAVLDPTGKIIErftseVAPISEERV---IDVAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASA 161
Cdd:PRK06936 97 VGVGEHLLGRVLDGLGQPFD-----GGHPPEPAAwypVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 162 GCGKTMLMHMLIEQTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQG 241
Cdd:PRK06936 172 GGGKSTLLASLIRSAEVDVTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 242 KRVVLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSEGSITAFYTVLLESEEEADPMADEIRSI 321
Cdd:PRK06936 252 KRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVADETRSI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 322 LDGHLYLSRKLAGQGHYPAIDVLKSVSRVFGQVTTPTHAEQASAVRKLMTRLEELQLFIDLGEYRPGENIENDRAMQMRD 401
Cdd:PRK06936 332 LDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIGEYQKGQDKEADQAIERIG 411
|
410 420
....*....|....*....|....*..
gi 554684202 402 SLKAWLCQSVAQYSSFDDTLSGMNAFA 428
Cdd:PRK06936 412 AIRGFLRQGTHELSHFNETLNLLETLT 438
|
|
| FliI_clade2 |
TIGR03497 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
15-427 |
6.27e-148 |
|
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: 426.72 E-value: 6.27e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 15 KITGPIIEAELRDVAIGELCEIRRgwHQKQVVaRAQVVGLQRERTVLSLIGNAQGLTRDVVLYPTGRALSAWVGYSVLGA 94
Cdd:TIGR03497 5 RVIGLTIESKGPKASIGELCSILT--KGGKPV-LAEVVGFKEENVLLMPLGEVEGIGPGSLVIATGRPLAIKVGKGLLGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 95 VLDPTGKIIErftsEVAPIS--EERVIDVAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTMLMHML 172
Cdd:TIGR03497 82 VLDGLGRPLD----GEGPIIgeEPYPLDNPPPNPLKRPRIRDPLETGIKAIDGLLTIGKGQRVGIFAGSGVGKSTLLGMI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 173 IEQTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQGKRVVLFIDSMT 252
Cdd:TIGR03497 158 ARNAKADINVIALIGERGREVRDFIEKDLGEEGLKRSVVVVATSDQPALMRLKAAFTATAIAEYFRDQGKDVLLMMDSVT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 253 RYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSEGSITAFYTVLLESEEEADPMADEIRSILDGHLYLSRKL 332
Cdd:TIGR03497 238 RFAMAQREIGLAVGEPPTTRGYTPSVFSLLPKLLERSGNSQKGSITGFYTVLVDGDDMNEPIADAVRGILDGHIVLSREL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 333 AGQGHYPAIDVLKSVSRVFGQVTTPTHAEQASAVRKLMTRLEELQLFIDLGEYRPGENIENDRAMQMRDSLKAWLCQSVA 412
Cdd:TIGR03497 318 AAKNHYPAIDVLASVSRVMNEIVSEEHKELAGKLRELLAVYKEAEDLINIGAYKRGSNPKIDEAIRYIEKINSFLKQGID 397
|
410
....*....|....*
gi 554684202 413 QYSSFDDTLSGMNAF 427
Cdd:TIGR03497 398 EKFTFEETVQLLKEL 412
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
4-421 |
2.33e-139 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 406.12 E-value: 2.33e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 4 PRLLQYLAYPQKITGPIIEAELRDVAIGELCEIRrgwHQKqvvARAQVVGLQRERTVLSLIGNAQGLTRDVVLYPTGRAL 83
Cdd:PRK06820 24 PEGLRYRGPIVEIGPTLLRASLPGVAQGELCRIE---PQG---MLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 84 SAWVGYSVLGAVLDPTGKIIERFTSEVapiSEERVIDVAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGC 163
Cdd:PRK06820 98 QVQVGADLAGRILDGLGAPIDGGPPLT---GQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 164 GKTMLMHMLIEQTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQGKR 243
Cdd:PRK06820 175 GKSTLLGMLCADSAADVMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 244 VVLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSEGSITAFYTVLLESEEEADPMADEIRSILD 323
Cdd:PRK06820 255 VLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 324 GHLYLSRKLAGQGHYPAIDVLKSVSRVFGQVTTPTHAEQASAVRKLMTRLEELQLFIDLGEYRPGENIENDRAMQMRDSL 403
Cdd:PRK06820 335 GHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGEYQAGEDLQADEALQRYPAI 414
|
410
....*....|....*...
gi 554684202 404 KAWLCQSVAQYSSFDDTL 421
Cdd:PRK06820 415 CAFLQQDHSETAHLETTL 432
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
1-426 |
2.43e-138 |
|
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: 403.29 E-value: 2.43e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 1 MKTPRLLQYLAYPQKITGPIIEAELRDVAIGELCEIRRGWHQKQVVAraQVVGLQRERTVLSLIGNAQGLTRDVVLYPTG 80
Cdd:TIGR01026 15 EMDLRLVKRVGRVTKVKGLLIEAVGPQASVGDLCLIERRGSEGRLVA--EVVGFNGEFVFLMPYEEVEGVRPGSKVLATG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 81 RALSAWVGYSVLGAVLDPTGKIIERFTSEVAPISEERVIdVAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFAS 160
Cdd:TIGR01026 93 EGLSIKVGDGLLGRVLDGLGKPIDGKGKFLDNVETEGLI-TAPINPLKRAPIREILSTGVRSIDGLLTVGKGQRIGIFAG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 161 AGCGKTMLMHMLIEQTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQ 240
Cdd:TIGR01026 172 SGVGKSTLLGMIARNTEADVNVIALIGERGREVREFIEHDLGEEGLKRSVVVVATSDQSPLLRLKGAYVATAIAEYFRDQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 241 GKRVVLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSEGSITAFYTVLLESEEEADPMADEIRS 320
Cdd:TIGR01026 252 GKDVLLLMDSVTRFAMAQREIGLAAGEPPATKGYTPSVFSTLPRLLERAGASGKGSITAFYTVLVEGDDMNEPIADSVRG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 321 ILDGHLYLSRKLAGQGHYPAIDVLKSVSRVFGQVTTPTHAEQASAVRKLMTRLEELQLFIDLGEYRPGENIENDRAMQMR 400
Cdd:TIGR01026 332 ILDGHIVLSRALAQRGHYPAIDVLASISRLMTAIVSEEHRRAARKFRELLSKYKDNEDLIRIGAYQRGSDRELDFAIAKY 411
|
410 420
....*....|....*....|....*.
gi 554684202 401 DSLKAWLCQSVAQYSSFDDTLSGMNA 426
Cdd:TIGR01026 412 PKLERFLKQGINEKVNFEESLQQLEE 437
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
14-429 |
1.77e-134 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 393.36 E-value: 1.77e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 14 QKITGPIIEAELRDVAIGELCEIRRGwhQKQVVARAQVVGLQRERTVLSLIGNAQGLTRDVVLYPTGRALSAWVGYSVLG 93
Cdd:PRK09099 29 VEVIGTLLRVSGLDVTLGELCELRQR--DGTLLQRAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVGPALLG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 94 AVLDPTGKIIErftsEVAPI--SEERVIDVAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTMLMHM 171
Cdd:PRK09099 107 RVIDGLGEPID----GGGPLdcDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 172 LIEQTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQGKRVVLFIDSM 251
Cdd:PRK09099 183 FARGTQCDVNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 252 TRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSEGSITAFYTVLLESEEEADPMADEIRSILDGHLYLSRK 331
Cdd:PRK09099 263 TRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSRE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 332 LAGQGHYPAIDVLKSVSRVFGQVTTPTHAEQASAVRKLMTRLEELQLFIDLGEYRPGENIENDRAMQMRDSLKAWLCQSV 411
Cdd:PRK09099 343 IAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVGEYRAGSDPVADEAIAKIDAIRDFLSQRT 422
|
410
....*....|....*...
gi 554684202 412 AQYSSFDDTLSGMNAFAD 429
Cdd:PRK09099 423 DEYSDPDATLAALAELSG 440
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
87-350 |
8.60e-132 |
|
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: 379.98 E-value: 8.60e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 87 VGYSVLGAVLDPTGKIIERFtsEVAPISEERVIDVAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCGKT 166
Cdd:cd01136 4 VGDGLLGRVIDALGEPLDGK--GLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 167 MLMHMLIEQTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQGKRVVL 246
Cdd:cd01136 82 TLLGMIARNTDADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 247 FIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSEGSITAFYTVLLESEEEADPMADEIRSILDGHL 326
Cdd:cd01136 162 LMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRSILDGHI 241
|
250 260
....*....|....*....|....
gi 554684202 327 YLSRKLAGQGHYPAIDVLKSVSRV 350
Cdd:cd01136 242 VLSRRLAERGHYPAIDVLASISRV 265
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
15-424 |
1.18e-127 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 375.98 E-value: 1.18e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 15 KITGPIIEAELRDVAIGELCEIRRGWHQKQVVaRAQVVGLQRERTVLSLIGNAQGLTRDVVLYPTGRALSAWVGYSVLGA 94
Cdd:PRK07721 24 RVIGLMIESKGPESSIGDVCYIHTKGGGDKAI-KAEVVGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVGSGLIGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 95 VLDPTGKII--ERFTSEVAPISEERvidvAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTMLMHML 172
Cdd:PRK07721 103 VLDALGEPLdgSALPKGLAPVSTDQ----DPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 173 IEQTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQGKRVVLFIDSMT 252
Cdd:PRK07721 179 ARNTSADLNVIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 253 RYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSEGSITAFYTVLLESEEEADPMADEIRSILDGHLYLSRKL 332
Cdd:PRK07721 259 RVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 333 AGQGHYPAIDVLKSVSRVFGQVTTPTHAEQASAVRKLMTRLEELQLFIDLGEYRPGENIENDRAMQMRDSLKAWLCQSVA 412
Cdd:PRK07721 339 ANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLINIGAYKRGSSREIDEAIQFYPQIISFLKQGTD 418
|
410
....*....|..
gi 554684202 413 QYSSFDDTLSGM 424
Cdd:PRK07721 419 EKATFEESIQAL 430
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
14-410 |
9.43e-120 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 355.80 E-value: 9.43e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 14 QKITGPIIEAELRDVAIGELCEIRRGWhqkqvvARAQVVGLQRERTVLSLIGNAQGLTRDVVLYPTGRALSAWVGYSVLG 93
Cdd:PRK07594 26 QDVSATLLNAWLPGVFMGELCCIKPGE------ELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 94 AVLDPTGKIIERFTSEVAPISEervIDVAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTMLMHMLI 173
Cdd:PRK07594 100 RVIDGFGRPLDGRELPDVCWKD---YDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 174 EQTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQGKRVVLFIDSMTR 253
Cdd:PRK07594 177 NAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 254 YARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSEGSITAFYTVLLESEEEADPMADEIRSILDGHLYLSRKLA 333
Cdd:PRK07594 257 YARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLA 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 554684202 334 GQGHYPAIDVLKSVSRVFGQVTTPTHAEQASAVRKLMTRLEELQLFIDLGEYRPGENIENDRAMQMRDSLKAWLCQS 410
Cdd:PRK07594 337 ERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEYQRGVDTDTDKAIDTYPDICTFLRQS 413
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
49-430 |
2.02e-115 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 345.15 E-value: 2.02e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 49 AQVVGLQRERTVLSLIGNAQGLTRDVVLYPTGRALSAWVGYSVLGAVLDPTGKIIErftsEVAPI-SEERVIDVAPP-SY 126
Cdd:PRK08972 61 AEVVGFDGDLLYLMPIEELRGVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLD----GLGPIyTDQRASRHSPPiNP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 127 ASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTMLMHMLIEQTEADVFVIGLIGERGREVTEFVDMLRASHKK 206
Cdd:PRK08972 137 LSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTTADVIVVGLVGERGREVKEFIEEILGEEGR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 207 EKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLL 286
Cdd:PRK08972 217 ARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALV 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 287 ERPGATSE--GSITAFYTVLLESEEEADPMADEIRSILDGHLYLSRKLAGQGHYPAIDVLKSVSRVFGQVTTPTHAEQAS 364
Cdd:PRK08972 297 ERAGNGGPgqGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMR 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 554684202 365 AVRKLMTRLEELQLFIDLGEYRPGENIENDRAMQMRDSLKAWLCQSVAQYSSFDDTLSGMNAFADQ 430
Cdd:PRK08972 377 RVKQVYSLYQQNRDLISIGAYKQGSDPRIDNAIRLQPAMNAFLQQTMKEAVPYDMSVNMLKQLAAQ 442
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
15-426 |
1.10e-111 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 335.55 E-value: 1.10e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 15 KITGPIIEAELRDVAIGELCEI--RRGWHQKQVvaRAQVVGLQRERTVLSLIGNAQGL---TRDVVLYPTGRALsawVGY 89
Cdd:PRK05688 33 RMVGLTLEAEGLRAAVGSRCLVinDDSYHPVQV--EAEVMGFSGDKVFLMPVGSVAGIapgARVVPLADTGRLP---MGM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 90 SVLGAVLDPTGKIIErftsEVAPISEERVIDVAPPSY--ASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTM 167
Cdd:PRK05688 108 SMLGRVLDGAGRALD----GKGPMKAEDWVPMDGPTInpLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 168 LMHMLIEQTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQGKRVVLF 247
Cdd:PRK05688 184 LLGMMTRFTEADIIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 248 IDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPG--ATSEGSITAFYTVLLESEEEADPMADEIRSILDGH 325
Cdd:PRK05688 264 MDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGnaEPGGGSITAFYTVLSEGDDQQDPIADSARGVLDGH 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 326 LYLSRKLAGQGHYPAIDVLKSVSRVFGQVTTPTHAEQASAVRKLMTRLEELQLFIDLGEYRPGENIENDRAMQMRDSLKA 405
Cdd:PRK05688 344 IVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPHLVQ 423
|
410 420
....*....|....*....|.
gi 554684202 406 WLCQSVAQYSSFDDTLSGMNA 426
Cdd:PRK05688 424 FLRQGLRENVSLAQSREQLAA 444
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
15-422 |
1.57e-111 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 334.73 E-value: 1.57e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 15 KITGPIIEAELRDVAIGELCEIRRGWHQKQVVAraQVVGLQRERTVLSLIGNAQGLTRDVVLYPTGRALSAWVGYSVLGA 94
Cdd:PRK08472 24 KISPTIIEADGLNPSVGDIVKIESSDNGKECLG--MVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNLLGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 95 VLDPTGKIIER----FTSEVAPISEervidvAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTMLMH 170
Cdd:PRK08472 102 VVDPLGRPIDGkgaiDYERYAPIMK------APIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 171 MLIEQTEADVFVIGLIGERGREVTEFVdmlrasHKK-----EKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQGKRVV 245
Cdd:PRK08472 176 MIVKGCLAPIKVVALIGERGREIPEFI------EKNlggdlENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 246 LFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGAT-SEGSITAFYTVLLESEEEADPMADEIRSILDG 324
Cdd:PRK08472 250 FIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEeGKGSITAFFTVLVEGDDMSDPIADQSRSILDG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 325 HLYLSRKLAGQGHYPAIDVLKSVSRVFGQVTTPTHAEQASAVRKLMTRLEELQLFIDLGEYRPGENIENDRAMQMRDSLK 404
Cdd:PRK08472 330 HIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAYQKGNDKELDEAISKKEFME 409
|
410
....*....|....*...
gi 554684202 405 AWLCQSVAQYSSFDDTLS 422
Cdd:PRK08472 410 QFLKQNPNELFPFEQTFE 427
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
139-348 |
3.54e-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: 322.77 E-value: 3.54e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 139 GVRAIDGLLTCGVGQRMGIFASAGCGKTMLMHMLIEQTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDF 218
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLGSGALKRTVVVVATSDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 219 PSVDRCNAAQLATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSE--GS 296
Cdd:pfam00006 81 PPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKGkgGS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 554684202 297 ITAFYTVLLESEEEADPMADEIRSILDGHLYLSRKLAGQGHYPAIDVLKSVS 348
Cdd:pfam00006 161 ITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
16-420 |
1.00e-109 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 330.40 E-value: 1.00e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 16 ITGPIIEAE--LRDVAIGELCEIRRGWHQkqvVARAQVVGLQRERTVLSLIGNAQGLTR---------DVVLYPTgralS 84
Cdd:PRK08927 24 VRGLLVEVAgpIHALSVGARIVVETRGGR---PVPCEVVGFRGDRALLMPFGPLEGVRRgcravianaAAAVRPS----R 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 85 AWvgysvLGAVLDPTGKIIERfTSEVAPISEERVIDVAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCG 164
Cdd:PRK08927 97 AW-----LGRVVNALGEPIDG-KGPLPQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 165 KTMLMHMLIEQTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQGKRV 244
Cdd:PRK08927 171 KSVLLSMLARNADADVSVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 245 VLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLER--PGATSEGSITAFYTVLLESEEEADPMADEIRSIL 322
Cdd:PRK08927 251 LCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERagPGPIGEGTITGLFTVLVDGDDHNEPVADAVRGIL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 323 DGHLYLSRKLAGQGHYPAIDVLKSVSRVFGQVTTPTHAEQASAVRKLMTRLEELQLFIDLGEYRPGENIENDRAMQMRDS 402
Cdd:PRK08927 331 DGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLGAYRAGSDPEVDEAIRLNPA 410
|
410
....*....|....*...
gi 554684202 403 LKAWLCQSVAQYSSFDDT 420
Cdd:PRK08927 411 LEAFLRQGKDEATSLAEG 428
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
2-426 |
1.42e-98 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 302.09 E-value: 1.42e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 2 KTPRLLQYlAYPQKITGPIIEAELRDVAIGELCEIRRGWHQKQVVARAQVVGLQRERTVLSLIGNAQGLTRDVVLYP--- 78
Cdd:PRK07960 21 QLPAVRRY-GRLTRATGLVLEATGLQLPLGATCVIERQNGSETHEVESEVVGFNGQRLFLMPLEEVEGILPGARVYArni 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 79 TGRALSAW----VGYSVLGAVLDPTGKIIERFTsevAPISEERVIDVAPP-SYASRVGVHEPLITGVRAIDGLLTCGVGQ 153
Cdd:PRK07960 100 SGEGLQSGkqlpLGPALLGRVLDGSGKPLDGLP---APDTGETGALITPPfNPLQRTPIEHVLDTGVRAINALLTVGRGQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 154 RMGIFASAGCGKTMLMHMLIEQTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTV 233
Cdd:PRK07960 177 RMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 234 AEYFRDQGKRVVLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERP--GATSEGSITAFYTVLLESEEEA 311
Cdd:PRK07960 257 AEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAgnGISGGGSITAFYTVLTEGDDQQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 312 DPMADEIRSILDGHLYLSRKLAGQGHYPAIDVLKSVSRVFGQVTTPTHAEQASAVRKLMTRLEELQLFIDLGEYRPGENI 391
Cdd:PRK07960 337 DPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLLSSFQRNRDLVSVGAYAKGSDP 416
|
410 420 430
....*....|....*....|....*....|....*
gi 554684202 392 ENDRAMQMRDSLKAWLCQSVAQYSSFDDTLSGMNA 426
Cdd:PRK07960 417 MLDKAIALWPQLEAFLQQGIFERADWEDSLQALER 451
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
16-428 |
1.67e-96 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 296.03 E-value: 1.67e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 16 ITGPIIEAELRDVAIGELCEIRR---GWHQkqvvarAQVVGLQRERTVLSLIGNAQGLTRDVVLYPTGRALSAWVGYSVL 92
Cdd:PRK07196 24 VTGLLLESVGCRLAIGQRCRIESvdeTFIE------AQVVGFDRDITYLMPFKHPGGVLGGARVFPSEQDGELLIGDSWL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 93 GAVLDPTGKIIErftsEVAPISEERVIDVAPPSY--ASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTMLMH 170
Cdd:PRK07196 98 GRVINGLGEPLD----GKGQLGGSTPLQQQLPQIhpLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 171 MLIEQTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQGKRVVLFIDS 250
Cdd:PRK07196 174 MITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 251 MTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPG-ATSEGSITAFYTVLLESEEEADPMADEIRSILDGHLYLS 329
Cdd:PRK07196 254 LTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGnSSGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 330 RKLAGQGHYPAIDVLKSVSRVFGQVTTPTHAEQASAVRKLMTRLEELQLFIDLGEYRPGENIENDRAMQMRDSLKAWLCQ 409
Cdd:PRK07196 334 RKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVAGADPMADQAVHYYPAITQFLRQ 413
|
410
....*....|....*....
gi 554684202 410 SVAQYSSFDDTLSGMNAFA 428
Cdd:PRK07196 414 EVGHPALFSASVEQLTGMF 432
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
80-429 |
2.57e-96 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 296.14 E-value: 2.57e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 80 GRALSAwvgysvLGAVLDPTGKIierftsevAPISEERVIDVAPPSYASRVGVHEPLITGVRAIDgLLT--CgVGQRMGI 157
Cdd:PRK06002 107 GRVINA------LGEPIDGLGPL--------APGTRPMSIDATAPPAMTRARVETGLRTGVRVID-IFTplC-AGQRIGI 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 158 FASAGCGKTMLMHMLIEQTEADVFVIGLIGERGREVTEFVDMLRASHKKeKCVLVFATSDFPSVDRCNAAQLATTVAEYF 237
Cdd:PRK06002 171 FAGSGVGKSTLLAMLARADAFDTVVIALVGERGREVREFLEDTLADNLK-KAVAVVATSDESPMMRRLAPLTATAIAEYF 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 238 RDQGKRVVLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLER--PGATSEGSITAFYTVLLESEEEADPMA 315
Cdd:PRK06002 250 RDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERagPGAEGGGSITGIFSVLVDGDDHNDPVA 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 316 DEIRSILDGHLYLSRKLAGQGHYPAIDVLKSVSRVFGQVTTPTHAEQASAVRKLMTRLEE---LQLfidLGEYRPGENIE 392
Cdd:PRK06002 330 DSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEEtrdLRL---IGGYRAGSDPD 406
|
330 340 350
....*....|....*....|....*....|....*..
gi 554684202 393 NDRAMQMRDSLKAWLCQSVAQYSSFDdtlsgmnAFAD 429
Cdd:PRK06002 407 LDQAVDLVPRIYEALRQSPGDPPSDD-------AFAD 436
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
28-424 |
8.92e-82 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 258.37 E-value: 8.92e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 28 VAIGELCEIrrGWHQkqvvARAQVVGLQRERTVL--------SLIGNAQGLTRDVVLYPTGRALsawvgysvLGAVLDPT 99
Cdd:PRK06793 40 AKIGDVCFV--GEHN----VLCEVIAIEKENNMLlpfeqtekVCYGDSVTLIAEDVVIPRGNHL--------LGKVLSAN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 100 GKIIERfTSEVAPIseERVIDVAPPSYA-SRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTMLMHMLIEQTEA 178
Cdd:PRK06793 106 GEVLNE-EAENIPL--QKIKLDAPPIHAfEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 179 DVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQGKRVVLFIDSMTRYARAL 258
Cdd:PRK06793 183 DINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADAR 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 259 RDVALASGERPArRGYPASVFDNLPRLLERPGATSEGSITAFYTVLLESEEEADPMADEIRSILDGHLYLSRKLAGQGHY 338
Cdd:PRK06793 263 RSVDIAVKELPI-GGKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHY 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 339 PAIDVLKSVSRVFGQVTTPTHAEQASAVRKLMTRLEELQLFIDLGEYRpgENIENDRAMQMR---DSLKAWLCQSVAQYS 415
Cdd:PRK06793 342 PAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGTIQ--ENAENAYIFECKnkvEGINTFLKQGRSDSF 419
|
....*....
gi 554684202 416 SFDDTLSGM 424
Cdd:PRK06793 420 QFDDIVEAM 428
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
15-429 |
1.48e-80 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 255.21 E-value: 1.48e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 15 KITGPIIEAELRDVAIGELCEIRRgwhQKQVVARAQVVGLQRERTVLSLIGNAQGLTRDVVLYPTGRALSAWVGYSVLGA 94
Cdd:PRK05922 25 RVSGNLLEAQGLSACLGELCQISL---SKSPPILAEVIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 95 VLDPTGKIIERftSEVAPISEERVIDVAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTMLMHMLIE 174
Cdd:PRK05922 102 VLDGFGNPLDG--KEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 175 QTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQGKRVVLFIDSMTRY 254
Cdd:PRK05922 180 GSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRW 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 255 ARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSEGSITAFYTVlLESEEEADPMADEIRSILDGHLYLS---RK 331
Cdd:PRK05922 260 IAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAI-LHYPNHPDIFTDYLKSLLDGHFFLTpqgKA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 332 LAGqghyPAIDVLKSVSRVFGQVTTPTHAEQASAVRKLMTRLEELQLFIDLGEYRPGENIENDRAMQMRDSLKAWLCQSV 411
Cdd:PRK05922 339 LAS----PPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGAYVPGQDAHLDRAVKLLPSIKQFLSQPL 414
|
410
....*....|....*...
gi 554684202 412 AQYSSFDDTLSGMNAFAD 429
Cdd:PRK05922 415 SSYCALHNTLKQLEALLK 432
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
87-350 |
3.73e-79 |
|
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: 245.83 E-value: 3.73e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 87 VGYSVLGAVLDPTGKIIErftsEVAPIS--EERVIDVAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCG 164
Cdd:cd19476 4 VGPELLGRILDGLGEPLD----GLPPIKtkQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 165 KTMLMHMLIEQT---EADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQG 241
Cdd:cd19476 80 KTVLAMQLARNQakaHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 242 KRVVLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGAT--SEGSITAFYTVLLESEEEADPMADEIR 319
Cdd:cd19476 160 QHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVkdGGGSITAIPAVSTPGDDLTDPIPDNTF 239
|
250 260 270
....*....|....*....|....*....|.
gi 554684202 320 SILDGHLYLSRKLAGQGHYPAIDVLKSVSRV 350
Cdd:cd19476 240 AILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
25-383 |
2.51e-47 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 169.33 E-value: 2.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 25 LRDVAIGELCEIRRGwhqkqvvARAQVVGLQRERTVLSLIGNAQGLTRDVVLYPTGRALSAWVGYSVLGAVLDPTGKIIE 104
Cdd:PRK13343 44 LPDAALDELLRFEGG-------SRGFAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 105 RFTSEVApiSEERVIDVAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTML-MHMLIEQTEADVFVI 183
Cdd:PRK13343 117 GGGPLQA--TARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIaIDAIINQKDSDVICV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 184 G-LIGERGREVTEFVDMLRASHKKEKCVLVFAT-SDFPSVDRCnAAQLATTVAEYFRDQGKRVVLFIDSMTRYARALRDV 261
Cdd:PRK13343 195 YvAIGQKASAVARVIETLREHGALEYTTVVVAEaSDPPGLQYL-APFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYREL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 262 ALASGERPARRGYPASVFDNLPRLLERPGATSE----GSITAFYTVllesEEEADPMADEIR----SILDGHLYLSRKLA 333
Cdd:PRK13343 274 SLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPelggGSLTALPII----ETLAGELSAYIPtnliSITDGQIYLDSDLF 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 554684202 334 GQGHYPAIDVLKSVSRVFGqvttpthAEQASAVRKLMTRL-------EELQLFIDLG 383
Cdd:PRK13343 350 AAGQRPAVDVGLSVSRVGG-------KAQHPAIRKESGRLrldyaqfLELEAFTRFG 399
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
15-380 |
2.22e-45 |
|
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 211621 [Multi-domain] Cd Length: 461 Bit Score: 163.35 E-value: 2.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 15 KITGPIIEAELRDVAIGEL---CEIRRGWHQKQVVARAQVVGLQRERTVLslIGNAQGLTRDVVLYPTGRALSAWVGYSV 91
Cdd:TIGR01039 7 QVIGPVVDVEFEQGELPRIynaLKVQNRAESELTLEVAQHLGDDTVRTIA--MGSTDGLVRGLEVIDTGAPISVPVGKET 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 92 LGAVLDPTGKIIErfTSEVAPISEERVIDVAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTMLMHM 171
Cdd:TIGR01039 85 LGRIFNVLGEPID--EKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 172 LIE---QTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRD-QGKRVVLF 247
Cdd:TIGR01039 163 LINniaKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 248 IDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSEGSITAFYTVLLESEEEADPMADEIRSILDGHLY 327
Cdd:TIGR01039 243 IDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTV 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 554684202 328 LSRKLAGQGHYPAIDVLKSVSRVFG-QVTTPTHAEQASAVRKLMTRLEELQLFI 380
Cdd:TIGR01039 323 LSRKIAELGIYPAVDPLDSTSRLLDpSVVGEEHYDVARGVQQILQRYKELQDII 376
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
16-377 |
3.95e-41 |
|
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: 151.78 E-value: 3.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 16 ITGPIIEAELRDV---AIGELCEIRRGWHQKQVVARAQVVGLQRERTVlSLiGNAQGLTRDVVLYPTGRALSAWVGYSVL 92
Cdd:COG0055 11 VIGPVVDVEFPEGelpAIYNALEVENEGGGELVLEVAQHLGDNTVRCI-AM-DSTDGLVRGMEVIDTGAPISVPVGEATL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 93 GAVLDPTGKIIErftsEVAPISEE--RVIDVAPPSYASRVGVHEPLITGVRAIDgLLTCGV-GQRMGIFASAGCGKTMLM 169
Cdd:COG0055 89 GRIFNVLGEPID----GKGPIEAKerRPIHRPAPPFEEQSTKTEILETGIKVID-LLAPYAkGGKIGLFGGAGVGKTVLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 170 HMLI-----EQTEADVFViGlIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRD-QGKR 243
Cdd:COG0055 164 MELIhniakEHGGVSVFA-G-VGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 244 VVLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSEGSITAFYTVLLESEEEADPMADEIRSILD 323
Cdd:COG0055 242 VLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLD 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 554684202 324 GHLYLSRKLAGQGHYPAIDVLKSVSR-----VFGQvttpTHAEQASAVRKLMTRLEELQ 377
Cdd:COG0055 322 ATTVLSRKIAELGIYPAVDPLDSTSRildplIVGE----EHYRVAREVQRILQRYKELQ 376
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
87-350 |
3.42e-40 |
|
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: 144.62 E-value: 3.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 87 VGYSVLGAVLDPTGKIIErftsEVAPI--SEERVIDVAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCG 164
Cdd:cd01132 6 VGEALLGRVVDALGNPID----GKGPIqtKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 165 KTML-MHMLIEQTEADVFVIGL-IGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQGK 242
Cdd:cd01132 82 KTAIaIDTIINQKGKKVYCIYVaIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 243 RVVLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSE----GSITAFYTVllesEEEADPMADEI 318
Cdd:cd01132 162 HALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGSLTALPII----ETQAGDVSAYI 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 554684202 319 R----SILDGHLYLSRKLAGQGHYPAIDVLKSVSRV 350
Cdd:cd01132 238 PtnviSITDGQIFLESELFNKGIRPAINVGLSVSRV 273
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
87-350 |
5.75e-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: 141.59 E-value: 5.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 87 VGYSVLGAVLDPTGKIIER----FTSEVAPISEErvidvaPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAG 162
Cdd:cd01133 4 VGEETLGRIFNVLGEPIDErgpiKAKERWPIHRE------APEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 163 CGKTMLMHMLIEQ--TEADVF-VIGLIGERGREVTEFVDMLRAS-----HKKEKCVLVFATSDFPSVDRCNAAQLATTVA 234
Cdd:cd01133 78 VGKTVLIMELINNiaKAHGGYsVFAGVGERTREGNDLYHEMKESgvinlDGLSKVALVYGQMNEPPGARARVALTGLTMA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 235 EYFRDQ-GKRVVLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSEGSITAFYTVLLESEEEADP 313
Cdd:cd01133 158 EYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDP 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 554684202 314 MADEIRSILDGHLYLSRKLAGQGHYPAIDVLKSVSRV 350
Cdd:cd01133 238 APATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
15-349 |
8.10e-39 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 145.35 E-value: 8.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 15 KITGPIIEAE-LRDVAIGELCEIRRGWHQKQvvaRAQVVGLQRERTVLSLIGNAQGL-TRDVVLYPTGRALSAWVGYSVL 92
Cdd:PRK04196 9 EIKGPLLFVEgVEGVAYGEIVEIELPNGEKR---RGQVLEVSEDKAVVQVFEGTTGLdLKDTKVRFTGEPLKLPVSEDML 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 93 GAVLDPTGKIIERFTsevAPISEERV-IDVAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTMLMHM 171
Cdd:PRK04196 86 GRIFDGLGRPIDGGP---EIIPEKRLdINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 172 LIEQ------TEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFR-DQGKRV 244
Cdd:PRK04196 163 IARQakvlgeEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAfEKGMHV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 245 VLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPG--ATSEGSITAFYTVLLESEEEADPMADEIRSIL 322
Cdd:PRK04196 243 LVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGriKGKKGSITQIPILTMPDDDITHPIPDLTGYIT 322
|
330 340
....*....|....*....|....*..
gi 554684202 323 DGHLYLSRKLAGQGHYPAIDVLKSVSR 349
Cdd:PRK04196 323 EGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
87-349 |
1.09e-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: 140.82 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 87 VGYSVLGAVLDPTGKIIERFtsevAPISEERVIDVAPPSY--ASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCG 164
Cdd:cd01135 6 VSEDMLGRIFNGSGKPIDGG----PPILPEDYLDINGPPInpVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 165 KTMLMHMLIEQT------EADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFR 238
Cdd:cd01135 82 HNELAAQIARQAgvvgseENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 239 -DQGKRVVLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATS--EGSITAFYTVLLESEEEADPMA 315
Cdd:cd01135 162 yEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEgrKGSITQIPILTMPNDDITHPIP 241
|
250 260 270
....*....|....*....|....*....|....
gi 554684202 316 DEIRSILDGHLYLSRKLAGQGHYPAIDVLKSVSR 349
Cdd:cd01135 242 DLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
16-369 |
7.45e-34 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 131.31 E-value: 7.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 16 ITGPIIEAELRDVAIGELCEIrrgwHQKQVVARAQVVGLQRERTVLSLIGNAQGL-TRDVVLYpTGRALSAWVGYSVLGA 94
Cdd:PRK02118 11 ITGNVITVEAEGVGYGELATV----ERKDGSSLAQVIRLDGDKVTLQVFGGTRGIsTGDEVVF-LGRPMQVTYSESLLGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 95 VLDPTGKIIERftsevAPISEERVIDVAPPSY--ASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTMLMHML 172
Cdd:PRK02118 86 RFNGSGKPIDG-----GPELEGEPIEIGGPSVnpVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLARI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 173 IEQTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFR-DQGKRVVLFIDSM 251
Cdd:PRK02118 161 ALQAEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 252 TRYARALRDVALASGERPARRGYPASVFDNLPRLLER----PGAtseGSITAFYTVLLESEEEADPMADEIRSILDGHLY 327
Cdd:PRK02118 241 TNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKavdfEDG---GSITIIAVTTMPGDDVTHPVPDNTGYITEGQFY 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 554684202 328 LsrklagqgHYPAIDVLKSVSR----VFGQVTTPTHAEQASAVRKL 369
Cdd:PRK02118 318 L--------RRGRIDPFGSLSRlkqlVIGKKTREDHGDLMNAMIRL 355
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
123-349 |
8.30e-33 |
|
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: 125.38 E-value: 8.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 123 PPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTMLMHMLIEQTEADVFVIGLIGERGREVTE----FVD 198
Cdd:cd01134 47 PRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEvleeFPE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 199 MLRASHKK---EKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALASGERPARRGYP 275
Cdd:cd01134 127 LKDPITGEslmERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 276 ASVFDNLPRLLERPGA-------TSEGSITAFYTVLLESEEEADPMADEIRSILDGHLYLSRKLAGQGHYPAIDVLKSVS 348
Cdd:cd01134 207 AYLGARLAEFYERAGRvrclgspGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYS 286
|
.
gi 554684202 349 R 349
Cdd:cd01134 287 K 287
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
50-377 |
1.71e-32 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 128.62 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 50 QVVGLQRERTVLslIGNAQGLTRDVVLYPTGRALSAWVGYSVLGAVLDPTGKIIErftsEVAPIS--EERVIDVAPPSYA 127
Cdd:CHL00060 63 QLLGNNRVRAVA--MSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVD----NLGPVDtrTTSPIHRSAPAFI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 128 ---SRVGVHEpliTGVRAIDGLLTCGVGQRMGIFASAGCGKTMLMHMLIE---QTEADVFVIGLIGERGREVTEFVDMLR 201
Cdd:CHL00060 137 qldTKLSIFE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINniaKAHGGVSVFGGVGERTREGNDLYMEMK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 202 ASH-------KKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQGKR-VVLFIDSMTRYARALRDVALASGERPARRG 273
Cdd:CHL00060 214 ESGvineqniAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 274 YPASVFDNLPRLLERPGATSEGSITAFYTVLLESEEEADPMADEIRSILDGHLYLSRKLAGQGHYPAIDVLKSVSRVFG- 352
Cdd:CHL00060 294 YQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQp 373
|
330 340
....*....|....*....|....*
gi 554684202 353 QVTTPTHAEQASAVRKLMTRLEELQ 377
Cdd:CHL00060 374 RIVGEEHYETAQRVKQTLQRYKELQ 398
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
63-382 |
2.07e-29 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 119.68 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 63 LIGNAQGLTRDVVLYPTGRALSAWVGYSVLGAVLDPTGKIIERfTSEVaPISEERVIDVAPPSYASRVGVHEPLITGVRA 142
Cdd:CHL00059 54 LMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDG-KGEI-SASESRLIESPAPGIISRRSVYEPLQTGLIA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 143 IDGLLTCGVGQRMGIFASAGCGKTML-MHMLIEQTEADVFVIGL-IGERGREVTEFVDMLRASHKKEKCVLVFATSDFPS 220
Cdd:CHL00059 132 IDSMIPIGRGQRELIIGDRQTGKTAVaTDTILNQKGQNVICVYVaIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 221 VDRCNAAQLATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATS----EGS 296
Cdd:CHL00059 212 TLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSsqlgEGS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 297 ITAFYTVllesEEEADPMADEIR----SILDGHLYLSRKLAGQGHYPAIDVLKSVSRVfgqvttpTHAEQASAVRKLMTR 372
Cdd:CHL00059 292 MTALPIV----ETQAGDVSAYIPtnviSITDGQIFLSADLFNAGIRPAINVGISVSRV-------GSAAQIKAMKQVAGK 360
|
330
....*....|.
gi 554684202 373 LE-ELQLFIDL 382
Cdd:CHL00059 361 LKlELAQFAEL 371
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
79-386 |
9.88e-27 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 112.08 E-value: 9.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 79 TGRALSAWVGYSVLGAVLDPTGKiierftsevaPI--------SEERVIDVAPPSYASRVGVHEPLITGVRAIDGLLTCG 150
Cdd:PRK09281 91 TGRILEVPVGEALLGRVVNPLGQ----------PIdgkgpieaTETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 151 VGQRMGIFASAGCGKT-MLMHMLIEQTEADVFVIGL-IGERGREVTEFVDMLRASHKKEKCVLVFAT-SDfpsvdrcnAA 227
Cdd:PRK09281 161 RGQRELIIGDRQTGKTaIAIDTIINQKGKDVICIYVaIGQKASTVAQVVRKLEEHGAMEYTIVVAATaSD--------PA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 228 QL-------ATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSE----GS 296
Cdd:PRK09281 233 PLqylapyaGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 297 ITAFYTVllesEEEADPMADEIR----SILDGHLYLSRKLAGQGHYPAIDVLKSVSRVFGqvttpthAEQASAVRKLMTR 372
Cdd:PRK09281 313 LTALPII----ETQAGDVSAYIPtnviSITDGQIFLESDLFNAGIRPAINVGISVSRVGG-------AAQIKAMKKVAGT 381
|
330
....*....|....
gi 554684202 373 LEelqlfIDLGEYR 386
Cdd:PRK09281 382 LR-----LDLAQYR 390
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
126-377 |
5.25e-25 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 107.56 E-value: 5.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 126 YASRVGVHEPLITGVRAIDGLLTCGVGqrmGIFASAG---CGKTMLMHMLIEQTEADVFVIGLIGERGREVT----EF-- 196
Cdd:PRK04192 201 YKEKLPPVEPLITGQRVIDTFFPVAKG---GTAAIPGpfgSGKTVTQHQLAKWADADIVIYVGCGERGNEMTevleEFpe 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 197 -VD-------MlrashkkEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALASGER 268
Cdd:PRK04192 278 lIDpktgrplM-------ERTVLIANTSNMPVAAREASIYTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEM 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 269 PARRGYPASVFDNLPRLLERPG-----ATSEGSITAFYTVlleS------EEeadPMADEIRSILDGHLYLSRKLAGQGH 337
Cdd:PRK04192 351 PGEEGYPAYLASRLAEFYERAGrvktlGGEEGSVTIIGAV---SppggdfSE---PVTQNTLRIVKVFWALDAELADRRH 424
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 554684202 338 YPAIDVLKSVSRVFGQVtTPTHAEQASA-----VRKLMTRLE---ELQ 377
Cdd:PRK04192 425 FPAINWLTSYSLYLDQV-APWWEENVDPdwrelRDEAMDLLQreaELQ 471
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
79-372 |
1.86e-24 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 105.19 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 79 TGRALSAWVGYSVLGAVLDPTGKIIERftseVAPISEERVIDV--APPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMG 156
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDK----GPPVLAEDYLDIngQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 157 IFASAGCGKTMLMHMLIEQTeadvfviGLIGERGREVTEfvdmlrasHKKEKCVLVFA------------TSDF------ 218
Cdd:TIGR01040 146 IFSAAGLPHNEIAAQICRQA-------GLVKLPTKDVHD--------GHEDNFAIVFAamgvnmetarffKQDFeengsm 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 219 ------------PSVDRCNAAQLATTVAEYFRDQ-GKRVVLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRL 285
Cdd:TIGR01040 211 ervclflnlandPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 286 LERPGATS--EGSITAFYTVLLESEEEADPMADEIRSILDGHLYLSRKLAGQGHYPAIDVLKSVSRVFgqvttpthaeqA 363
Cdd:TIGR01040 291 YERAGRVEgrNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLM-----------K 359
|
....*....
gi 554684202 364 SAVRKLMTR 372
Cdd:TIGR01040 360 SAIGEGMTR 368
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
10-81 |
7.68e-24 |
|
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: 94.30 E-value: 7.68e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 554684202 10 LAYPQKITGPIIEAELR-DVAIGELCEIRRGWHQKQVVARAQVVGLQRERTVLSLIGNAQGLTRDVVLYPTGR 81
Cdd:cd01426 1 KGRVIRVNGPLVEAELEgEVAIGEVCEIERGDGNNETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
79-350 |
9.30e-23 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 100.89 E-value: 9.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 79 TGRALSAWVGYSVLGAVLDPTGK-----IIERFTSEVAPISEERVIDVAPPSYASRVGVHEPLITGVRAIDGLLTCGVGQ 153
Cdd:PTZ00185 111 TGKLLYIPVGAGVLGKVVNPLGHevpvgLLTRSRALLESEQTLGKVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQ 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 154 RMGIFASAGCGKTML-MHMLIEQTEADVFVIGL---------IGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDR 223
Cdd:PTZ00185 191 RELIVGDRQTGKTSIaVSTIINQVRINQQILSKnavisiyvsIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQ 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 224 CNAAQLATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSE----GSITA 299
Cdd:PTZ00185 271 YLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPgkggGSVTA 350
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 554684202 300 FYTVLLESEEEADPMADEIRSILDGHLYLSRKLAGQGHYPAIDVLKSVSRV 350
Cdd:PTZ00185 351 LPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRV 401
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
355-424 |
4.71e-19 |
|
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: 80.94 E-value: 4.71e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 355 TTPTHAEQASAVRKLMTRLEELQLFIDLGEYRPGENIENDRAMQMRDSLKAWLCQSVAQYSSFDDTLSGM 424
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIGAYQAGSDPEIDEAIAKRPAINAFLRQGVDEPVSFEETLAQL 70
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
166-348 |
4.18e-18 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 87.00 E-value: 4.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 166 TMLMHMLIEQTEADVFVIGLIGERGREVT----EFVDMLRASHKK---EKCVLVFATSDFPSVDRCNAAQLATTVAEYFR 238
Cdd:PRK14698 670 TVTQHQLAKWSDAQVVIYIGCGERGNEMTdvleEFPKLKDPKTGKplmERTVLIANTSNMPVAAREASIYTGITIAEYFR 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 239 DQGKRVVLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSE-------GSITAFYTVLLESEEEA 311
Cdd:PRK14698 750 DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTlgsdyrvGSVSVIGAVSPPGGDFS 829
|
170 180 190
....*....|....*....|....*....|....*..
gi 554684202 312 DPMADEIRSILDGHLYLSRKLAGQGHYPAIDVLKSVS 348
Cdd:PRK14698 830 EPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS 866
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
141-377 |
5.77e-18 |
|
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: 85.51 E-value: 5.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 141 RAIDGLLTCGVGQRMGIFASAGCGKTMLMHML---IEQTEADVFVIG-LIGERGREVTefvDMLRaSHKKEkcvLVFATS 216
Cdd:TIGR00767 157 RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIaqaITRNHPEVELIVlLIDERPEEVT---DMQR-SVKGE---VVASTF 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 217 DFPSVDRCNAAQLATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALASGeRPARRGYPASVFDNLPRLLerpGATSE-- 294
Cdd:TIGR00767 230 DEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASG-KVLSGGVDANALHRPKRFF---GAARNie 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 295 --GSITAFYTVLLESEEEADPMA-DEIRSILDGHLYLSRKLAGQGHYPAIDVLKSVSRVFGQVTTPTHAEQASAVRKLMT 371
Cdd:TIGR00767 306 egGSLTIIATALIDTGSRMDEVIfEEFKGTGNMELHLDRKLADRRIFPAIDIKKSGTRKEELLLTPEELQKIWVLRKIIS 385
|
....*.
gi 554684202 372 RLEELQ 377
Cdd:TIGR00767 386 PMDSIE 391
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
93-369 |
6.66e-17 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 82.71 E-value: 6.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 93 GAVLDPTGKIIERFTSEVAPISEERVIDVA---PPSYASRVGVHEPLITGVRAIDGLLTCGVGQRMGIFASAGCGKT-ML 168
Cdd:PRK07165 81 GKIIDIDGNIIYPEAQNPLSKKFLPNTSSIfnlAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKThIA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 169 MHMLIEQTEADVFVIGL-IGERGREVTEFVDMLRASHKKEKCVLVFATSDFPsVDRCNAAQLATTVAE---YFRDqgkrV 244
Cdd:PRK07165 161 LNTIINQKNTNVKCIYVaIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSP-YEQYLAPYVAMAHAEnisYNDD----V 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 245 VLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGA-TSEGSITAFYTVLLESEEEADPMADEIRSILD 323
Cdd:PRK07165 236 LIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKfKNRKTITALPILQTVDNDITSLISSNIISITD 315
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 554684202 324 GHLYLSRKLAGQGHYPAIDVLKSVSRVFGQVTTPTHAEQASAVRKL 369
Cdd:PRK07165 316 GQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKI 361
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
140-349 |
2.29e-16 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 80.13 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 140 VRAIDGLLTCGVGQRMGIFASAGCGKTMLMHMLIE-----QTEADVFVIgLIGERGREVTEFvdmlRASHKKEkcvlVFA 214
Cdd:PRK12608 121 MRVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAavaanHPEVHLMVL-LIDERPEEVTDM----RRSVKGE----VYA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 215 -TSDFPSVDRCNAAQLATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALASGeRPARRGYPAsvfdnlpRLLERP---- 289
Cdd:PRK12608 192 sTFDRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAYNNEVESSG-RTLSGGVDA-------RALQRPkrlf 263
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 554684202 290 GATSE----GSITAFYTVLLESEEEADPMA-DEIRSILDGHLYLSRKLAGQGHYPAIDVLKSVSR 349
Cdd:PRK12608 264 GAARNieegGSLTIIATALVDTGSRMDEVIfEEFKGTGNMEIVLDRELADKRVFPAIDIAKSGTR 328
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
141-349 |
6.64e-16 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 76.86 E-value: 6.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 141 RAIDGLLTCGVGQRMGIFASAGCGKTMLMHML---IEQTEADVFVIG-LIGERGREVTEFVDMLRAShkkekcvlVFA-T 215
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIanaIAKNHPEVELIVlLIDERPEEVTDMRRSVKGE--------VVAsT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 216 SDFPSVDRCNAAQLATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALASGerparRGYPASVFdnlPRLLERP----GA 291
Cdd:cd01128 77 FDEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSG-----KTLSGGVD---ANALHKPkrffGA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 554684202 292 TSE----GSITAFYTVLLESEEEADPMA-DEIRSILDGHLYLSRKLAGQGHYPAIDVLKSVSR 349
Cdd:cd01128 149 ARNieegGSLTIIATALVDTGSRMDEVIfEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTR 211
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
141-349 |
3.06e-11 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 64.78 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 141 RAIDGLLTCGVGQRMGIFASAGCGKTMLMHML---IEQTEADVFVIG-LIGERGREVTefvDMLRaSHKKEkcvLVFATS 216
Cdd:PRK09376 158 RIIDLIAPIGKGQRGLIVAPPKAGKTVLLQNIansITTNHPEVHLIVlLIDERPEEVT---DMQR-SVKGE---VVASTF 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 217 DFPSVdrcNAAQLATTVAEYFR---DQGKRVVLFIDSMTRYARALRDVALASGerparRGYPASVfDnlPRLLERP---- 289
Cdd:PRK09376 231 DEPAE---RHVQVAEMVIEKAKrlvEHGKDVVILLDSITRLARAYNTVVPSSG-----KVLSGGV-D--ANALHRPkrff 299
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 554684202 290 GA---TSE-GSITAFYTVLLESEEEadpMADEIRSILDG----HLYLSRKLAGQGHYPAIDVLKSVSR 349
Cdd:PRK09376 300 GAarnIEEgGSLTIIATALIDTGSR---MDEVIFEEFKGtgnmELHLDRKLAEKRIFPAIDINRSGTR 364
|
|
| ATP-synt_flagellum-secretory_path_III_N |
cd18117 |
Flagellum-specific ATP synthase, N-terminal domain; The N-terminal domain of the ... |
14-81 |
1.57e-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: 50.99 E-value: 1.57e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 554684202 14 QKITGPIIEAELRDVAIGELCEIRRGWHQKQvvaRAQVVGLQRERTVLSLIGNAQGLTRDVVLYPTGR 81
Cdd:cd18117 6 VRVVGLLLEAVGPQAPIGELCLIETADGLSI---LAEVVGFSGEKVLLMPLGELSGLSPGARVVPLGR 70
|
|
| ATP-synt_flagellum-secretory_path_III_C |
cd18114 |
Flagellum-specific ATP synthase, C-terminal domain; The C-terminal domain of the ... |
359-421 |
1.08e-07 |
|
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: 48.76 E-value: 1.08e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 554684202 359 HAEQASAVRKLMTRLEELQLFIDLGEYRPGENIENDRAMQMRDSLKAWLCQSVAQYSSFDDTL 421
Cdd:cd18114 1 HYLAARKFRELMSTYQENEDLIRIGAYKKGSDPEVDEAIRLKPQIEAFLKQGLNEKAPLEESL 63
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
134-266 |
4.47e-07 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 52.21 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 134 EPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTMLMH-----MLIEQTEADVFVIgLIGERGREVTefvDMLRaSHKKEk 208
Cdd:PRK12678 398 EPKKLTTRVIDLIMPIGKGQRGLIVSPPKAGKTTILQnianaITTNNPECHLMVV-LVDERPEEVT---DMQR-SVKGE- 471
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 554684202 209 cvlVFA-TSDFPSVDRCNAAQLATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALASG 266
Cdd:PRK12678 472 ---VIAsTFDRPPSDHTTVAELAIERAKRLVELGKDVVVLLDSITRLGRAYNLAAPASG 527
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
152-332 |
1.02e-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: 42.36 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 152 GQRMGIFASAGCGKTMLMHMLIEQTEADVF-VIGLIGERGREVTEFVDMlrashkkekcvLVFATSDFPSVDRCNAAQLA 230
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGgVIYIDGEDILEEVLDQLL-----------LIIVGGKKASGSGELRLRLA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 231 TTVAEYFRdqgkRVVLFIDSMTRYARALRDVALASGERpARRGYPASVFDNLprllerpgatsegsitafyTVLLESEEE 310
Cdd:smart00382 71 LALARKLK----PDVLILDEITSLLDAEQEALLLLLEE-LRLLLLLKSEKNL-------------------TVILTTNDE 126
|
170 180
....*....|....*....|..
gi 554684202 311 ADPMADEIRSILDGHLYLSRKL 332
Cdd:smart00382 127 KDLGPALLRRRFDRRIVLLLIL 148
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
15-80 |
2.66e-04 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 39.07 E-value: 2.66e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 554684202 15 KITGPIIEAE-LRDVAIGELCEIRRGWHQKQVVARAQVVGLQRERTVLSLIGNAQGLTRDVVLYPTG 80
Cdd:pfam02874 3 QVIGPVVDVEfGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
162-249 |
8.14e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.84 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554684202 162 GCGKTMLMHMLIEQTEADvFVIGLIGERGREVTEFVDMLRAshkkekcvlvfatsDF-PSVDRCNAAQLATTVAEYFRD- 239
Cdd:COG3267 53 GTGKTTLLRRLLERLPDD-VKVAYIPNPQLSPAELLRAIAD--------------ELgLEPKGASKADLLRQLQEFLLEl 117
|
90
....*....|..
gi 554684202 240 --QGKRVVLFID 249
Cdd:COG3267 118 aaAGRRVVLIID 129
|
|
| |
