|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
4-430 |
0e+00 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 805.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 4 LKLLNKYSYLHSINGSLIEAELDDVSVGEVCEIYASWQANERIARAQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTGEQL 83
Cdd:PRK08149 1 LRLLQRLAHPLRIQGPIIEAELPDVAIGEICEIRAGWHSNEVIARAQVVGFQRERTILSLIGNAQGLSRQVVLKPTGKPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 84 TIQISDAFLGSVLNASGQIMERFV-PDTPGERGNLRLIDELPPSYQERRVINTPLETRIRVIDGVLTCGIGQRVGIFASA 162
Cdd:PRK08149 81 SVWVGEALLGAVLDPTGKIVERFDaPPTVGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 163 GCGKTVLMHMLVNNTEADVFVIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFSSVDRCNAALMATTVAEYFRDRG 242
Cdd:PRK08149 161 GCGKTSLMNMLIEHSEADVFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 243 KRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTLKGSITAFYTVLLEGEDESDPLGDEIRSI 322
Cdd:PRK08149 241 KRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 323 LDGHIYLSRKLAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLEDLQVFIDLGEYRAGQNAENDFAMNARP 402
Cdd:PRK08149 321 LDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGEYRRGENADNDRAMDKRP 400
|
410 420
....*....|....*....|....*...
gi 446656971 403 KLTNWLKQSVNEKMPMSETLKELERIVK 430
Cdd:PRK08149 401 ALEAFLKQDVAEKSSFSDTLERLNEFAA 428
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
1-429 |
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: 600.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 1 MKKLKLLNKYSYLHSINGSLIEAELDDVSVGEVCEIYASWQaneRIARAQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTG 80
Cdd:COG1157 11 LEELPPVRVSGRVTRVVGLLIEAVGPDASIGELCEIETADG---RPVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 81 EQLTIQISDAFLGSVLNASGQIMERFVPDTPGERgnlRLIDELPPSYQERRVINTPLETRIRVIDGVLTCGIGQRVGIFA 160
Cdd:COG1157 88 RPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEER---RPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 161 SAGCGKTVLMHMLVNNTEADVFVIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFSSVDRCNAALMATTVAEYFRD 240
Cdd:COG1157 165 GSGVGKSTLLGMIARNTEADVNVIALIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEYFRD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 241 RGKRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTLKGSITAFYTVLLEGEDESDPLGDEIR 320
Cdd:COG1157 245 QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAVR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 321 SILDGHIYLSRKLAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLEDLQVFIDLGEYRAGQNAENDFAMNA 400
Cdd:COG1157 325 GILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENEDLIRIGAYQPGSDPELDEAIAL 404
|
410 420
....*....|....*....|....*....
gi 446656971 401 RPKLTNWLKQSVNEKMPMSETLKELERIV 429
Cdd:COG1157 405 IPAIEAFLRQGMDERVSFEESLAQLAELL 433
|
|
| III_secr_ATP |
TIGR02546 |
type III secretion apparatus H+-transporting two-sector ATPase; [Protein fate, Protein and ... |
16-429 |
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: 553.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 16 INGSLIEAELDDVSVGEVCEIYASwqaNERIARAQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTGEQLTIQISDAFLGSV 95
Cdd:TIGR02546 12 VSGTLLKAVLPGARVGELCLIRRR---DPSQLLAEVVGFTGDEALLSPLGELHGISPGSEVIPTGRPLSIRVGEALLGRV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 96 LNASGQIMERFVPDTPGERgNLRLIDELPPSYQERRVINTPLETRIRVIDGVLTCGIGQRVGIFASAGCGKTVLMHMLVN 175
Cdd:TIGR02546 89 LDGFGRPLDGKGELPAGEI-ETRPLDADPPPPMSRQPIDQPLPTGVRAIDGLLTCGEGQRIGIFAGAGVGKSTLLGMIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 176 NTEADVFVIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFSSVDRCNAALMATTVAEYFRDRGKRVVLFIDSMTRY 255
Cdd:TIGR02546 168 GASADVNVIALIGERGREVREFIEHHLGEEGRKRSVLVVSTSDRPSLERLKAAYTATAIAEYFRDQGKRVLLMMDSLTRF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 256 ARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTLKGSITAFYTVLLEGEDESDPLGDEIRSILDGHIYLSRKLAG 335
Cdd:TIGR02546 248 ARALREIGLAAGEPPARGGYPPSVFSSLPRLLERAGNGEKGSITALYTVLVEGDDMNDPIADEVRSILDGHIVLSRALAE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 336 QGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLEDLQVFIDLGEYRAGQNAENDFAMNARPKLTNWLKQSVNEK 415
Cdd:TIGR02546 328 RNHYPAIDVLASLSRVMSQVVSTEHRRAAGKLRRLLATYKEVELLIRLGEYQPGSDPETDDAIDKIDAIRAFLRQSTDEY 407
|
410
....*....|....
gi 446656971 416 MPMSETLKELERIV 429
Cdd:TIGR02546 408 SPYEETLEQLHALV 421
|
|
| FliI_clade1 |
TIGR03496 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
15-425 |
1.88e-157 |
|
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: 450.77 E-value: 1.88e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 15 SINGSLIEAELDDVSVGEVCEIYaswQANERIARAQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTGEQLTIQISDAFLGS 94
Cdd:TIGR03496 5 RVVGLVLEAVGLRAPVGSRCEIE---SSDGDPIEAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLGGPLRLPVGDSLLGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 95 VLNASGQIMERFVPDTPGERgnlRLIDELPPSYQERRVINTPLETRIRVIDGVLTCGIGQRVGIFASAGCGKTVLMHMLV 174
Cdd:TIGR03496 82 VIDGLGRPLDGKGPLDAGER---VPLYAPPINPLKRAPIDEPLDVGVRAINGLLTVGRGQRMGIFAGSGVGKSTLLGMMA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 175 NNTEADVFVIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFSSVDRCNAALMATTVAEYFRDRGKRVVLFIDSMTR 254
Cdd:TIGR03496 159 RYTEADVVVVGLIGERGREVKEFIEDILGEEGLARSVVVAATADESPLMRLRAAFYATAIAEYFRDQGKDVLLLMDSLTR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 255 YARALRDMKLAAGEPPARRGYPASVFDSLPRLLER--PGPTLKGSITAFYTVLLEGEDESDPLGDEIRSILDGHIYLSRK 332
Cdd:TIGR03496 239 FAMAQREIALAIGEPPATKGYPPSVFAKLPQLVERagNGEEGKGSITAFYTVLVEGDDQQDPIADAARAILDGHIVLSRE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 333 LAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLEDLQVFIDLGEYRAGQNAENDFAMNARPKLTNWLKQSV 412
Cdd:TIGR03496 319 LAEQGHYPAIDILASISRVMPDVVSPEHRQAARRFKQLLSRYQENRDLISIGAYQAGSDPELDQAIALYPRIEAFLQQGM 398
|
410
....*....|...
gi 446656971 413 NEKMPMSETLKEL 425
Cdd:TIGR03496 399 RERASFEESLEAL 411
|
|
| FliI_clade2 |
TIGR03497 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
14-429 |
1.88e-154 |
|
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: 443.29 E-value: 1.88e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 14 HSINGSLIEAELDDVSVGEVCEIYAswQANERIaRAQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTGEQLTIQISDAFLG 93
Cdd:TIGR03497 4 TRVIGLTIESKGPKASIGELCSILT--KGGKPV-LAEVVGFKEENVLLMPLGEVEGIGPGSLVIATGRPLAIKVGKGLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 94 SVLNASGQIMERFVPDTPGERgnlRLIDELPPSYQERRVINTPLETRIRVIDGVLTCGIGQRVGIFASAGCGKTVLMHML 173
Cdd:TIGR03497 81 RVLDGLGRPLDGEGPIIGEEP---YPLDNPPPNPLKRPRIRDPLETGIKAIDGLLTIGKGQRVGIFAGSGVGKSTLLGMI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 174 VNNTEADVFVIGLIGERGREVTE------CAESLKKSVnaakcvLVYATSDFSSVDRCNAALMATTVAEYFRDRGKRVVL 247
Cdd:TIGR03497 158 ARNAKADINVIALIGERGREVRDfiekdlGEEGLKRSV------VVVATSDQPALMRLKAAFTATAIAEYFRDQGKDVLL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 248 FIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTLKGSITAFYTVLLEGEDESDPLGDEIRSILDGHI 327
Cdd:TIGR03497 232 MMDSVTRFAMAQREIGLAVGEPPTTRGYTPSVFSLLPKLLERSGNSQKGSITGFYTVLVDGDDMNEPIADAVRGILDGHI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 328 YLSRKLAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLEDLQVFIDLGEYRAGQNAENDFAMNARPKLTNW 407
Cdd:TIGR03497 312 VLSRELAAKNHYPAIDVLASVSRVMNEIVSEEHKELAGKLRELLAVYKEAEDLINIGAYKRGSNPKIDEAIRYIEKINSF 391
|
410 420
....*....|....*....|..
gi 446656971 408 LKQSVNEKMPMSETLKELERIV 429
Cdd:TIGR03497 392 LKQGIDEKFTFEETVQLLKELL 413
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
18-430 |
6.25e-148 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 427.63 E-value: 6.25e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 18 GSLIEAELDDVSVGEVCEIYASWqaNERIARAQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTGEQLTIQISDAFLGSVLN 97
Cdd:PRK06936 32 GTILKAVVPGVRIGELCYLRNPD--NSLSLQAEVIGFAQHQALLTPLGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 98 ASGQIMERFVPDTPGERgnlRLIDELPPSYQERRVINTPLETRIRVIDGVLTCGIGQRVGIFASAGCGKTVLMHMLVNNT 177
Cdd:PRK06936 110 GLGQPFDGGHPPEPAAW---YPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 178 EADVFVIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFSSVDRCNAALMATTVAEYFRDRGKRVVLFIDSMTRYAR 257
Cdd:PRK06936 187 EVDVTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFAR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 258 ALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTLKGSITAFYTVLLEGEDESDPLGDEIRSILDGHIYLSRKLAGQG 337
Cdd:PRK06936 267 AQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAAN 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 338 HYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLEDLQVFIDLGEYRAGQNAENDFAMNARPKLTNWLKQSVNEKMP 417
Cdd:PRK06936 347 HYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIGEYQKGQDKEADQAIERIGAIRGFLRQGTHELSH 426
|
410
....*....|...
gi 446656971 418 MSETLKELERIVK 430
Cdd:PRK06936 427 FNETLNLLETLTQ 439
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
1-428 |
5.37e-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: 422.94 E-value: 5.37e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 1 MKKLKLLNKYSYLHSINGSLIEAELDDVSVGEVCEIYAswQANERIARAQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTG 80
Cdd:TIGR01026 15 EMDLRLVKRVGRVTKVKGLLIEAVGPQASVGDLCLIER--RGSEGRLVAEVVGFNGEFVFLMPYEEVEGVRPGSKVLATG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 81 EQLTIQISDAFLGSVLNASGQIMerfvpDTPGER-GNLRLIDEL--PPSYQERRVINTPLETRIRVIDGVLTCGIGQRVG 157
Cdd:TIGR01026 93 EGLSIKVGDGLLGRVLDGLGKPI-----DGKGKFlDNVETEGLItaPINPLKRAPIREILSTGVRSIDGLLTVGKGQRIG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 158 IFASAGCGKTVLMHMLVNNTEADVFVIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFSSVDRCNAALMATTVAEY 237
Cdd:TIGR01026 168 IFAGSGVGKSTLLGMIARNTEADVNVIALIGERGREVREFIEHDLGEEGLKRSVVVVATSDQSPLLRLKGAYVATAIAEY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 238 FRDRGKRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTLKGSITAFYTVLLEGEDESDPLGD 317
Cdd:TIGR01026 248 FRDQGKDVLLLMDSVTRFAMAQREIGLAAGEPPATKGYTPSVFSTLPRLLERAGASGKGSITAFYTVLVEGDDMNEPIAD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 318 EIRSILDGHIYLSRKLAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLEDLQVFIDLGEYRAGQNAENDFA 397
Cdd:TIGR01026 328 SVRGILDGHIVLSRALAQRGHYPAIDVLASISRLMTAIVSEEHRRAARKFRELLSKYKDNEDLIRIGAYQRGSDRELDFA 407
|
410 420 430
....*....|....*....|....*....|.
gi 446656971 398 MNARPKLTNWLKQSVNEKMPMSETLKELERI 428
Cdd:TIGR01026 408 IAKYPKLERFLKQGINEKVNFEESLQQLEEI 438
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
16-429 |
3.55e-145 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 420.76 E-value: 3.55e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 16 INGSLIEAELDDVSVGEVCEIyaswqANERIaRAQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTGEQLTIQISDAFLGSV 95
Cdd:PRK06820 36 IGPTLLRASLPGVAQGELCRI-----EPQGM-LAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 96 LNASGQIMErfvpDTPGERGNLRLIDELPPSYQERRVINTPLETRIRVIDGVLTCGIGQRVGIFASAGCGKTVLMHMLVN 175
Cdd:PRK06820 110 LDGLGAPID----GGPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 176 NTEADVFVIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFSSVDRCNAALMATTVAEYFRDRGKRVVLFIDSMTRY 255
Cdd:PRK06820 186 DSAADVMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRY 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 256 ARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTLKGSITAFYTVLLEGEDESDPLGDEIRSILDGHIYLSRKLAG 335
Cdd:PRK06820 266 ARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 336 QGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLEDLQVFIDLGEYRAGQNAENDFAMNARPKLTNWLKQSVNEK 415
Cdd:PRK06820 346 AGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGEYQAGEDLQADEALQRYPAICAFLQQDHSET 425
|
410
....*....|....
gi 446656971 416 MPMSETLKELERIV 429
Cdd:PRK06820 426 AHLETTLEHLAQVV 439
|
|
| FliI_clade3 |
TIGR03498 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
16-429 |
1.62e-138 |
|
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of bacterial flagellum systems. This protein acts to drive protein export for flagellar biosynthesis. The most closely related family is the YscN family of bacterial type III secretion systems. This model represents one (of three) segment of the FliI family tree. These have been modeled separately in order to exclude the type III secretion ATPases more effectively.
Pssm-ID: 163293 [Multi-domain] Cd Length: 418 Bit Score: 402.84 E-value: 1.62e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 16 INGSLIEAE--LDDVSVGEVCEIYAswqANERIARAQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTGEQLTIQISDAFLG 93
Cdd:TIGR03498 6 VTGLLIEVRglSRAVRLGDRCAIRA---RDGRPVLAEVVGFNGDRVLLMPFEPLEGVGLGCAVFAREGPLAVRPHPSWLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 94 SVLNASGQIMERFVPDTPGERGnlRLIDELPPSYQERRVINTPLETRIRVIDGVLTCGIGQRVGIFASAGCGKTVLMHML 173
Cdd:TIGR03498 83 RVINALGEPIDGKGPLPQGERR--YPLRASPPPAMSRARVGEPLDTGVRVIDTFLPLCRGQRLGIFAGSGVGKSTLLSML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 174 VNNTEADVFVIGLIGERGREVTE------CAESLKKSVnaakcvLVYATSDFSSVDRCNAALMATTVAEYFRDRGKRVVL 247
Cdd:TIGR03498 161 ARNTDADVVVIALVGERGREVREfleddlGEEGLKRSV------VVVATSDESPLMRRQAAYTATAIAEYFRDQGKDVLL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 248 FIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTL--KGSITAFYTVLLEGEDESDPLGDEIRSILDG 325
Cdd:TIGR03498 235 LMDSVTRFAMAQREIGLAAGEPPVARGYTPSVFSELPRLLERAGPGAegKGSITGIFTVLVDGDDHNEPVADAVRGILDG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 326 HIYLSRKLAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLEDLQVFIDLGEYRAGQNAENDFAMNARPKLT 405
Cdd:TIGR03498 315 HIVLDRAIAERGRYPAINVLASVSRLAPRVWSPEERKLVRRLRALLARYEETEDLIRLGAYRKGSDPELDEAIRLVPKIY 394
|
410 420
....*....|....*....|....
gi 446656971 406 NWLKQSVNEKMPMSETLKELERIV 429
Cdd:TIGR03498 395 EFLTQGPDEPTSLQDPFADLAAIL 418
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
84-351 |
8.20e-138 |
|
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: 395.39 E-value: 8.20e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 84 TIQISDAFLGSVLNASGQ-IMERFVPDTPGERGnlrlIDELPPSYQERRVINTPLETRIRVIDGVLTCGIGQRVGIFASA 162
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEpLDGKGLPDEPERRP----LIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 163 GCGKTVLMHMLVNNTEADVFVIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFSSVDRCNAALMATTVAEYFRDRG 242
Cdd:cd01136 77 GVGKSTLLGMIARNTDADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 243 KRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTLKGSITAFYTVLLEGEDESDPLGDEIRSI 322
Cdd:cd01136 157 KKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRSI 236
|
250 260
....*....|....*....|....*....
gi 446656971 323 LDGHIYLSRKLAGQGHYPAIDVLKSVSRV 351
Cdd:cd01136 237 LDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
18-430 |
5.88e-134 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 392.16 E-value: 5.88e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 18 GSLIEAELDDVSVGEVCEIYASWQANERIaRAQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTGEQLTIQISDAFLGSVLN 97
Cdd:PRK07721 27 GLMIESKGPESSIGDVCYIHTKGGGDKAI-KAEVVGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVGSGLIGQVLD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 98 ASGQIME-RFVPD--TPgergnlRLIDELPPSYQERRVINTPLETRIRVIDGVLTCGIGQRVGIFASAGCGKTVLMHMLV 174
Cdd:PRK07721 106 ALGEPLDgSALPKglAP------VSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 175 NNTEADVFVIGLIGERGREVTEC------AESLKKSVnaakcvLVYATSDFSSVDRCNAALMATTVAEYFRDRGKRVVLF 248
Cdd:PRK07721 180 RNTSADLNVIALIGERGREVREFierdlgPEGLKRSI------VVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLM 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 249 IDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTLKGSITAFYTVLLEGEDESDPLGDEIRSILDGHIY 328
Cdd:PRK07721 254 MDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 329 LSRKLAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLEDLQVFIDLGEYRAGQNAENDFAMNARPKLTNWL 408
Cdd:PRK07721 334 LDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLINIGAYKRGSSREIDEAIQFYPQIISFL 413
|
410 420
....*....|....*....|..
gi 446656971 409 KQSVNEKMPMSETLKELERIVK 430
Cdd:PRK07721 414 KQGTDEKATFEESIQALLSLFG 435
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
18-429 |
9.05e-132 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 386.43 E-value: 9.05e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 18 GSLIEAELDDVSVGEVCEIYAswQANERIARAQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTGEQLTIQISDAFLGSVLN 97
Cdd:PRK09099 33 GTLLRVSGLDVTLGELCELRQ--RDGTLLQRAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVGPALLGRVID 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 98 ASGQIMErfvPDTPGERGNLRLIDELPPSYQERRVINTPLETRIRVIDGVLTCGIGQRVGIFASAGCGKTVLMHMLVNNT 177
Cdd:PRK09099 111 GLGEPID---GGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 178 EADVFVIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFSSVDRCNAALMATTVAEYFRDRGKRVVLFIDSMTRYAR 257
Cdd:PRK09099 188 QCDVNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFAR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 258 ALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTLKGSITAFYTVLLEGEDESDPLGDEIRSILDGHIYLSRKLAGQG 337
Cdd:PRK09099 268 AQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARN 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 338 HYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLEDLQVFIDLGEYRAGQNAENDFAMNARPKLTNWLKQSVNEKMP 417
Cdd:PRK09099 348 QYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVGEYRAGSDPVADEAIAKIDAIRDFLSQRTDEYSD 427
|
410
....*....|..
gi 446656971 418 MSETLKELERIV 429
Cdd:PRK09099 428 PDATLAALAELS 439
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
15-429 |
1.28e-127 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 375.86 E-value: 1.28e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 15 SINGSLIEAE--LDDVSVGEVCEIYAswqANERIARAQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTGEQLTIQISDAFL 92
Cdd:PRK08927 23 AVRGLLVEVAgpIHALSVGARIVVET---RGGRPVPCEVVGFRGDRALLMPFGPLEGVRRGCRAVIANAAAAVRPSRAWL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 93 GSVLNASGQIMERFVPDTPGERGnlRLIDELPPSYQERRVINTPLETRIRVIDGVLTCGIGQRVGIFASAGCGKTVLMHM 172
Cdd:PRK08927 100 GRVVNALGEPIDGKGPLPQGPVP--YPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 173 LVNNTEADVFVIGLIGERGREVTEC------AESLKKSVnaakcvLVYATSDFSSVDRCNAALMATTVAEYFRDRGKRVV 246
Cdd:PRK08927 178 LARNADADVSVIGLIGERGREVQEFlqddlgPEGLARSV------VVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 247 LFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLER--PGPTLKGSITAFYTVLLEGEDESDPLGDEIRSILD 324
Cdd:PRK08927 252 CLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERagPGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 325 GHIYLSRKLAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLEDLQVFIDLGEYRAGQNAENDFAMNARPKL 404
Cdd:PRK08927 332 GHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLGAYRAGSDPEVDEAIRLNPAL 411
|
410 420
....*....|....*....|....*
gi 446656971 405 TNWLKQSVNEKMPMSETLKELERIV 429
Cdd:PRK08927 412 EAFLRQGKDEATSLAEGYARLAQIL 436
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
13-429 |
6.98e-125 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 368.90 E-value: 6.98e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 13 LHSINGSLIEAELDDVSVGEVCEIYASWQAneriarAQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTGEQLTIQISDAFL 92
Cdd:PRK07594 25 IQDVSATLLNAWLPGVFMGELCCIKPGEEL------AEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 93 GSVLNASGqimeRFVPDTPGERGNLRLIDELPPSYQERRVINTPLETRIRVIDGVLTCGIGQRVGIFASAGCGKTVLMHM 172
Cdd:PRK07594 99 GRVIDGFG----RPLDGRELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 173 LVNNTEADVFVIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFSSVDRCNAALMATTVAEYFRDRGKRVVLFIDSM 252
Cdd:PRK07594 175 LCNAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 253 TRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTLKGSITAFYTVLLEGEDESDPLGDEIRSILDGHIYLSRK 332
Cdd:PRK07594 255 TRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 333 LAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLEDLQVFIDLGEYRAGQNAENDFAMNARPKLTNWLKQSV 412
Cdd:PRK07594 335 LAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEYQRGVDTDTDKAIDTYPDICTFLRQSK 414
|
410
....*....|....*..
gi 446656971 413 NEKMPMSETLKELERIV 429
Cdd:PRK07594 415 DEVCGPELLIEKLHQIL 431
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
18-430 |
4.36e-115 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 344.41 E-value: 4.36e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 18 GSLIEAELDDVSVGEVCEIYASWQANERIARAQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTGEQLTIQISDAFLGSVLN 97
Cdd:PRK05688 36 GLTLEAEGLRAAVGSRCLVINDDSYHPVQVEAEVMGFSGDKVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 98 ASGQIM--------ERFVPDTPgergnlRLIDELppsyqERRVINTPLETRIRVIDGVLTCGIGQRVGIFASAGCGKTVL 169
Cdd:PRK05688 116 GAGRALdgkgpmkaEDWVPMDG------PTINPL-----NRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 170 MHMLVNNTEADVFVIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFSSVDRCNAALMATTVAEYFRDRGKRVVLFI 249
Cdd:PRK05688 185 LGMMTRFTEADIIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLM 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 250 DSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTLK--GSITAFYTVLLEGEDESDPLGDEIRSILDGHI 327
Cdd:PRK05688 265 DSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPggGSITAFYTVLSEGDDQQDPIADSARGVLDGHI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 328 YLSRKLAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLEDLQVFIDLGEYRAGQNAENDFAMNARPKLTNW 407
Cdd:PRK05688 345 VLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPHLVQF 424
|
410 420
....*....|....*....|...
gi 446656971 408 LKQSVNEKMPMSETLKELERIVK 430
Cdd:PRK05688 425 LRQGLRENVSLAQSREQLAAIFA 447
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
1-430 |
2.65e-114 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 341.67 E-value: 2.65e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 1 MKKLKLLNKYSYLHSINGSLIEAELDDVSVGEVCEIYASWQANERIARAQVV--------------GFRngktllnlIGS 66
Cdd:PRK08472 10 LQKFNLSPRFGSITKISPTIIEADGLNPSVGDIVKIESSDNGKECLGMVVVIekeqfgispfsfieGFK--------IGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 67 SVGLTRTAVLKPTGEQLTIQISDAFlGSVLNASGQI-MERFVPdtpgergnlrlIDELPPSYQERRVINTPLETRIRVID 145
Cdd:PRK08472 82 KVFISKEGLNIPVGRNLLGRVVDPL-GRPIDGKGAIdYERYAP-----------IMKAPIAAMKRGLIDEVFSVGVKSID 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 146 GVLTCGIGQRVGIFASAGCGKTVLMHMLVNNTEADVFVIGLIGERGREVTECAEslkKSVNA--AKCVLVYATSDFSSVD 223
Cdd:PRK08472 150 GLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGCLAPIKVVALIGERGREIPEFIE---KNLGGdlENTVIVVATSDDSPLM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 224 RCNAALMATTVAEYFRDRGKRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPT-LKGSITAFY 302
Cdd:PRK08472 227 RKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEeGKGSITAFF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 303 TVLLEGEDESDPLGDEIRSILDGHIYLSRKLAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLEDLQVFID 382
Cdd:PRK08472 307 TVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIR 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 446656971 383 LGEYRAGQNAENDFAMNARPKLTNWLKQSVNEKMPMSETLKELERIVK 430
Cdd:PRK08472 387 IGAYQKGNDKELDEAISKKEFMEQFLKQNPNELFPFEQTFEQLEEILR 434
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
49-430 |
2.16e-112 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 337.06 E-value: 2.16e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 49 AQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTGEQLTIQISDAFLGSVLNASGQIMERFVPDTPGERGNLRLIDELPPSyq 128
Cdd:PRK08972 61 AEVVGFDGDLLYLMPIEELRGVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLS-- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 129 eRRVINTPLETRIRVIDGVLTCGIGQRVGIFASAGCGKTVLMHMLVNNTEADVFVIGLIGERGREVTECAESLKKSVNAA 208
Cdd:PRK08972 139 -RRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTTADVIVVGLVGERGREVKEFIEEILGEEGRA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 209 KCVLVYATSDFSSVDRCNAALMATTVAEYFRDRGKRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLE 288
Cdd:PRK08972 218 RSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 289 RP--GPTLKGSITAFYTVLLEGEDESDPLGDEIRSILDGHIYLSRKLAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAAR 366
Cdd:PRK08972 298 RAgnGGPGQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRR 377
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446656971 367 VRKILTTLEDLQVFIDLGEYRAGQNAENDFAMNARPKLTNWLKQSVNEKMPMSETLKELERIVK 430
Cdd:PRK08972 378 VKQVYSLYQQNRDLISIGAYKQGSDPRIDNAIRLQPAMNAFLQQTMKEAVPYDMSVNMLKQLAA 441
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
141-349 |
8.49e-111 |
|
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: 324.31 E-value: 8.49e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 141 IRVIDGVLTCGIGQRVGIFASAGCGKTVLMHMLVNNTEADVFVIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFS 220
Cdd:pfam00006 2 IRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLGSGALKRTVVVVATSDEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 221 SVDRCNAALMATTVAEYFRDRGKRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTL--KGSI 298
Cdd:pfam00006 82 PLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKgkGGSI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446656971 299 TAFYTVLLEGEDESDPLGDEIRSILDGHIYLSRKLAGQGHYPAIDVLKSVS 349
Cdd:pfam00006 162 TALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
13-429 |
2.69e-104 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 316.06 E-value: 2.69e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 13 LHSINGSLIEAELDDVSVGEVCEIYAswqANERIARAQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTGEQLTIQISDAFL 92
Cdd:PRK07196 21 LVRVTGLLLESVGCRLAIGQRCRIES---VDETFIEAQVVGFDRDITYLMPFKHPGGVLGGARVFPSEQDGELLIGDSWL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 93 GSVLNASGQIMerfvpDTPGERGNLRLIDELPPSYQ--ERRVINTPLETRIRVIDGVLTCGIGQRVGIFASAGCGKTVLM 170
Cdd:PRK07196 98 GRVINGLGEPL-----DGKGQLGGSTPLQQQLPQIHplQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 171 HMLVNNTEADVFVIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFSSVDRCNAALMATTVAEYFRDRGKRVVLFID 250
Cdd:PRK07196 173 GMITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 251 SMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTL-KGSITAFYTVLLEGEDESDPLGDEIRSILDGHIYL 329
Cdd:PRK07196 253 SLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSgNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 330 SRKLAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLEDLQVFIDLGEYRAGQNAENDFAMNARPKLTNWLK 409
Cdd:PRK07196 333 SRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVAGADPMADQAVHYYPAITQFLR 412
|
410 420
....*....|....*....|
gi 446656971 410 QSVNEKMPMSETLKELERIV 429
Cdd:PRK07196 413 QEVGHPALFSASVEQLTGMF 432
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
65-411 |
7.72e-101 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 307.69 E-value: 7.72e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 65 GSSVGLTRTAVLKPTgeqLTIQISDAFLGSVLNASGQIMERFVPDTPGERGnlRLIDELPPSYQERRVINTPLETRIRVI 144
Cdd:PRK06002 82 RIEIGLGDAVFRKGP---LRIRPDPSWKGRVINALGEPIDGLGPLAPGTRP--MSIDATAPPAMTRARVETGLRTGVRVI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 145 DGVLTCGIGQRVGIFASAGCGKTVLMHMLVNNTEADVFVIGLIGERGREVTECAESLKKSvNAAKCVLVYATSDFSSVDR 224
Cdd:PRK06002 157 DIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGREVREFLEDTLAD-NLKKAVAVVATSDESPMMR 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 225 CNAALMATTVAEYFRDRGKRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLER--PGPTLKGSITAFY 302
Cdd:PRK06002 236 RLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERagPGAEGGGSITGIF 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 303 TVLLEGEDESDPLGDEIRSILDGHIYLSRKLAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLEDLQVFID 382
Cdd:PRK06002 316 SVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEETRDLRL 395
|
330 340
....*....|....*....|....*....
gi 446656971 383 LGEYRAGQNAENDFAMNARPKLTNWLKQS 411
Cdd:PRK06002 396 IGGYRAGSDPDLDQAVDLVPRIYEALRQS 424
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
1-429 |
4.46e-99 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 303.63 E-value: 4.46e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 1 MKKLKLLNKYSYLHSINGSLIEAELDDVSVGEVCEIYASWQANERIARAQVVGFRNGKTLLNLIGSSVGLTRTAVL---- 76
Cdd:PRK07960 19 MAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCVIERQNGSETHEVESEVVGFNGQRLFLMPLEEVEGILPGARVyarn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 77 -----KPTGEQLTIqiSDAFLGSVLNASGQIMERFVPDTPGERGNLRLidelPP-SYQERRVINTPLETRIRVIDGVLTC 150
Cdd:PRK07960 99 isgegLQSGKQLPL--GPALLGRVLDGSGKPLDGLPAPDTGETGALIT----PPfNPLQRTPIEHVLDTGVRAINALLTV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 151 GIGQRVGIFASAGCGKTVLMHMLVNNTEADVFVIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFSSVDRCNAALM 230
Cdd:PRK07960 173 GRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 231 ATTVAEYFRDRGKRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTLK--GSITAFYTVLLEG 308
Cdd:PRK07960 253 ATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISggGSITAFYTVLTEG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 309 EDESDPLGDEIRSILDGHIYLSRKLAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLEDLQVFIDLGEYRA 388
Cdd:PRK07960 333 DDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLLSSFQRNRDLVSVGAYAK 412
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 446656971 389 GQNAENDFAMNARPKLTNWLKQSVNEKMPMSETLKELERIV 429
Cdd:PRK07960 413 GSDPMLDKAIALWPQLEAFLQQGIFERADWEDSLQALERIF 453
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
65-429 |
3.09e-88 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 274.93 E-value: 3.09e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 65 GSSVGLTRTAVLKPTGEQLtiqisdafLGSVLNASGQIMERFVPDTPGERGNLrlidELPPSYQ-ERRVINTPLETRIRV 143
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHL--------LGKVLSANGEVLNEEAENIPLQKIKL----DAPPIHAfEREEITDVFETGIKS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 144 IDGVLTCGIGQRVGIFASAGCGKTVLMHMLVNNTEADVFVIGLIGERGREVTEC------AESLKKSVnaakcvLVYATS 217
Cdd:PRK06793 147 IDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREVKDFirkelgEEGMRKSV------VVVATS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 218 DFSSVDRCNAALMATTVAEYFRDRGKRVVLFIDSMTRYARALRDMKLAAGEPPArrGYPASVFDS-LPRLLERPGPTLKG 296
Cdd:PRK06793 221 DESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELPI--GGKTLLMESyMKKLLERSGKTQKG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 297 SITAFYTVLLEGEDESDPLGDEIRSILDGHIYLSRKLAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLED 376
Cdd:PRK06793 299 SITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKE 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 446656971 377 LQVFIDLGEYRagQNAENDFAMNARPK---LTNWLKQSVNEKMPMSETLKELERIV 429
Cdd:PRK06793 379 NELYFKLGTIQ--ENAENAYIFECKNKvegINTFLKQGRSDSFQFDDIVEAMHHIV 432
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
85-351 |
1.71e-85 |
|
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: 262.01 E-value: 1.71e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 85 IQISDAFLGSVLNASGQIMERFVPDTPGERGNLRLideLPPSYQERRVINTPLETRIRVIDGVLTCGIGQRVGIFASAGC 164
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHL---KAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 165 GKTVLMHMLVNNT---EADVFVIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFSSVDRCNAALMATTVAEYFRDR 241
Cdd:cd19476 79 GKTVLAMQLARNQakaHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 242 GKRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTL--KGSITAFYTVLLEGEDESDPLGDEI 319
Cdd:cd19476 159 GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDPIPDNT 238
|
250 260 270
....*....|....*....|....*....|..
gi 446656971 320 RSILDGHIYLSRKLAGQGHYPAIDVLKSVSRV 351
Cdd:cd19476 239 FAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
13-430 |
4.74e-76 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 243.27 E-value: 4.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 13 LHSINGSLIEAELDDVSVGEVCEIYASWQANeriARAQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTGEQLTIQISDAFL 92
Cdd:PRK05922 23 LSRVSGNLLEAQGLSACLGELCQISLSKSPP---ILAEVIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 93 GSVLNASGQIMERfVPDTPgeRGNLRLIDELPPSYQERRVINTPLETRIRVIDGVLTCGIGQRVGIFASAGCGKTVLMHM 172
Cdd:PRK05922 100 GRVLDGFGNPLDG-KEQLP--KTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLST 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 173 LVNNTEADVFVIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFSSVDRCNAALMATTVAEYFRDRGKRVVLFIDSM 252
Cdd:PRK05922 177 IAKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 253 TRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTLKGSITAFYTVlLEGEDESDPLGDEIRSILDGHIYLS-- 330
Cdd:PRK05922 257 SRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAI-LHYPNHPDIFTDYLKSLLDGHFFLTpq 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 331 -RKLAGqghyPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLEDLQVFIDLGEYRAGQNAENDFAMNARPKLTNWLK 409
Cdd:PRK05922 336 gKALAS----PPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGAYVPGQDAHLDRAVKLLPSIKQFLS 411
|
410 420
....*....|....*....|.
gi 446656971 410 QSVNEKMPMSETLKELERIVK 430
Cdd:PRK05922 412 QPLSSYCALHNTLKQLEALLK 432
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
64-381 |
5.37e-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: 162.20 E-value: 5.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 64 IGSSVGLTRTAVLKPTGEQLTIQISDAFLGSVLNASGQIMERFVPDTPGERGNlrlIDELPPSYQERRVINTPLETRIRV 143
Cdd:TIGR01039 57 MGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWP---IHRKAPSFEEQSTKVEILETGIKV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 144 IDGVLTCGIGQRVGIFASAGCGKTVLMHMLVNNT---EADVFVIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFS 220
Cdd:TIGR01039 134 IDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIakeHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 221 SVDRCNAALMATTVAEYFRD-RGKRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTLKGSIT 299
Cdd:TIGR01039 214 PGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSIT 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 300 AFYTVLLEGEDESDPLGDEIRSILDGHIYLSRKLAGQGHYPAIDVLKSVSRVFG-QVTDEKHRDNAARVRKILTTLEDLQ 378
Cdd:TIGR01039 294 SVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVGEEHYDVARGVQQILQRYKELQ 373
|
...
gi 446656971 379 VFI 381
Cdd:TIGR01039 374 DII 376
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
65-378 |
1.14e-39 |
|
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: 147.93 E-value: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 65 GSSVGLTRTAVLKPTGEQLTIQISDAFLGSVLNASGQIMERFVPDTPGERgnlRLIDELPPSYQERRVINTPLETRIRVI 144
Cdd:COG0055 61 DSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKER---RPIHRPAPPFEEQSTKTEILETGIKVI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 145 DgvLTCGI--GQRVGIFASAGCGKTVLMHMLVNNTEAD-----VFViGlIGERGREVTECAESLKKSVNAAKCVLVYATS 217
Cdd:COG0055 138 D--LLAPYakGGKIGLFGGAGVGKTVLIMELIHNIAKEhggvsVFA-G-VGERTREGNDLYREMKESGVLDKTALVFGQM 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 218 DFSSVDRCNAALMATTVAEYFRD-RGKRVVLFIDSMTRYARAlrDMKLAA--GEPPARRGYPASVFDSLPRLLERPGPTL 294
Cdd:COG0055 214 NEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQA--GSEVSAllGRMPSAVGYQPTLATEMGALQERITSTK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 295 KGSITAFYTVLLEGEDESDPLGDEIRSILDGHIYLSRKLAGQGHYPAIDVLKSVSRVFG-QVTDEKHRDNAARVRKILTT 373
Cdd:COG0055 292 KGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDpLIVGEEHYRVAREVQRILQR 371
|
....*
gi 446656971 374 LEDLQ 378
Cdd:COG0055 372 YKELQ 376
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
84-351 |
3.39e-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: 141.97 E-value: 3.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 84 TIQISDAFLGSVLNASGQIMERFVPDTPGERgnlRLIDELPPSYQERRVINTPLETRIRVIDgvLTCGI--GQRVGIFAS 161
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKER---WPIHREAPEFVELSTEQEILETGIKVVD--LLAPYakGGKIGLFGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 162 AGCGKTVLMHMLVNN--TEADVF-VIGLIGERGREVTECAESLKKS-----VNAAKCVLVYATSDFSSVDRCNAALMATT 233
Cdd:cd01133 76 AGVGKTVLIMELINNiaKAHGGYsVFAGVGERTREGNDLYHEMKESgvinlDGLSKVALVYGQMNEPPGARARVALTGLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 234 VAEYFRD-RGKRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTLKGSITAFYTVLLEGEDES 312
Cdd:cd01133 156 MAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLT 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 446656971 313 DPLGDEIRSILDGHIYLSRKLAGQGHYPAIDVLKSVSRV 351
Cdd:cd01133 236 DPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
63-384 |
5.54e-38 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 143.90 E-value: 5.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 63 LIGSSVGLTRTAVLKPTGEQLTIQISDAFLGSVLNASGQIMERFVPDTPGERgnlRLIDELPPSYQERRVINTPLETRIR 142
Cdd:PRK13343 75 LLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATAR---RPLERPAPAIIERDFVTEPLQTGIK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 143 VIDGVLTCGIGQRVGIFASAGCGKTVL-MHMLVNNTEADVFVIG-LIGERGREVTECAESLKKSVNAAKCVLVYATSDFS 220
Cdd:PRK13343 152 VVDALIPIGRGQRELIIGDRQTGKTAIaIDAIINQKDSDVICVYvAIGQKASAVARVIETLREHGALEYTTVVVAEASDP 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 221 SVDRCNAALMATTVAEYFRDRGKRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERP---GPTLK-G 296
Cdd:PRK13343 232 PGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAaklSPELGgG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 297 SITAFYTVllegEDESDPLGDEIR----SILDGHIYLSRKLAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILT 372
Cdd:PRK13343 312 SLTALPII----ETLAGELSAYIPtnliSITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYA 387
|
330
....*....|..
gi 446656971 373 TLEDLQVFIDLG 384
Cdd:PRK13343 388 QFLELEAFTRFG 399
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
85-351 |
4.48e-37 |
|
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: 136.15 E-value: 4.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 85 IQISDAFLGSVLNASGQIMERFVPDTPGERgnlRLIDELPPSYQERRVINTPLETRIRVIDGVLTCGIGQRVGIFASAGC 164
Cdd:cd01132 4 VPVGEALLGRVVDALGNPIDGKGPIQTKER---RRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 165 GKT-VLMHMLVNNTEADVFVIGL-IGERGREVTECAESLKKSVNAAKCVLVYATSDFSSVDRCNAALMATTVAEYFRDRG 242
Cdd:cd01132 81 GKTaIAIDTIINQKGKKVYCIYVaIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 243 KRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPG---PTL-KGSITAFYTVLLEGEDESDPLGDE 318
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklsDELgGGSLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|...
gi 446656971 319 IRSILDGHIYLSRKLAGQGHYPAIDVLKSVSRV 351
Cdd:cd01132 241 VISITDGQIFLESELFNKGIRPAINVGLSVSRV 273
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
69-381 |
1.13e-35 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 137.48 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 69 GLTRTAVLKPTGEQLTIQISDAFLGSVLNASGQIMERFVPDTPGERgnlRLIDELPPSYQErrvINTPL---ETRIRVID 145
Cdd:CHL00060 80 GLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTT---SPIHRSAPAFIQ---LDTKLsifETGIKVVD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 146 GVLTCGIGQRVGIFASAGCGKTVLMHMLVNN---TEADVFVIGLIGERGREVTECAESLKKS-------VNAAKCVLVYA 215
Cdd:CHL00060 154 LLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakAHGGVSVFGGVGERTREGNDLYMEMKESgvineqnIAESKVALVYG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 216 TSDFSSVDRCNAALMATTVAEYFRDRGKR-VVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTL 294
Cdd:CHL00060 234 QMNEPPGARMRVGLTALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 295 KGSITAFYTVLLEGEDESDPLGDEIRSILDGHIYLSRKLAGQGHYPAIDVLKSVSRVFG-QVTDEKHRDNAARVRKILTT 373
Cdd:CHL00060 314 EGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGEEHYETAQRVKQTLQR 393
|
....*...
gi 446656971 374 LEDLQVFI 381
Cdd:CHL00060 394 YKELQDII 401
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
10-362 |
5.19e-34 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 132.26 E-value: 5.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 10 YSYLHSINGSLIEAE-LDDVSVGEVCEIYAswqANERIARAQVVGFRNGKTLLNLIGSSVGL-TRTAVLKPTGEQLTIQI 87
Cdd:PRK04196 4 YRTVSEIKGPLLFVEgVEGVAYGEIVEIEL---PNGEKRRGQVLEVSEDKAVVQVFEGTTGLdLKDTKVRFTGEPLKLPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 88 SDAFLGSVLNASGqimerfvpdtpgergnlRLIDELPPSYQERRV-IN-TPL------------ETRIRVIDGVLTCGIG 153
Cdd:PRK04196 81 SEDMLGRIFDGLG-----------------RPIDGGPEIIPEKRLdINgAPInpvareypeefiQTGISAIDGLNTLVRG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 154 QRVGIFASAGcgktvLMH-----------MLVNNTEADVFVIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFSSV 222
Cdd:PRK04196 144 QKLPIFSGSG-----LPHnelaaqiarqaKVLGEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 223 DRCNAALMATTVAEYFR-DRGKRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTL--KGSIT 299
Cdd:PRK04196 219 ERILTPRMALTAAEYLAfEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKgkKGSIT 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446656971 300 AFYTVLLEGEDESDPLGDEIRSILDGHIYLSRKLAGQGHYPAIDVLKSVSRVFGQ-----VTDEKHRD 362
Cdd:PRK04196 299 QIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDgigegKTREDHKD 366
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
83-350 |
7.64e-34 |
|
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: 127.72 E-value: 7.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 83 LTIQISDAFLGSVLNASGQIMERFVPDTPGERgnlRLIDELPPSYQERRVINTPLETRIRVIDGVLTCGIGQRVGIFASA 162
Cdd:cd01135 2 LKLPVSEDMLGRIFNGSGKPIDGGPPILPEDY---LDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 163 GCGKTVLMHM------LVNNTEADVFVIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFSSVDRCNAALMATTVAE 236
Cdd:cd01135 79 GLPHNELAAQiarqagVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 237 YFR-DRGKRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPG--PTLKGSITAFYTVLLEGEDESD 313
Cdd:cd01135 159 YLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGrvEGRKGSITQIPILTMPNDDITH 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 446656971 314 PLGDEIRSILDGHIYLSRKLAGQGHYPAIDVLKSVSR 350
Cdd:cd01135 239 PIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
124-350 |
1.87e-32 |
|
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.
Pssm-ID: 410878 [Multi-domain] Cd Length: 288 Bit Score: 124.22 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 124 PPSYQERRVINTPLETRIRVIDGVLTCGIGQRVGIFASAGCGKTVLMHMLVNNTEADVFVIGLIGERGREVTEC------ 197
Cdd:cd01134 47 PRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEVleefpe 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 198 ------AESLKKsvnaaKCVLVYATSDFSSVDRCNAALMATTVAEYFRDRGKRVVLFIDSMTRYARALRDMKLAAGEPPA 271
Cdd:cd01134 127 lkdpitGESLME-----RTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 272 RRGYPASVFDSLPRLLERPG-------PTLKGSITAFYTVLLEGEDESDPLGDEIRSILDGHIYLSRKLAGQGHYPAIDV 344
Cdd:cd01134 202 EEGYPAYLGARLAEFYERAGrvrclgsPGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINW 281
|
....*.
gi 446656971 345 LKSVSR 350
Cdd:cd01134 282 LISYSK 287
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
56-351 |
1.22e-31 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 125.85 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 56 NGKTLLNliGSSVgltrtavlKPTGEQLTIQISDAFLGSVLNASGQIMerfvpDTPGE--RGNLRLIDELPPSYQERRVI 133
Cdd:CHL00059 57 DGLMIQE--GSSV--------KATGKIAQIPVSEAYLGRVVNALAKPI-----DGKGEisASESRLIESPAPGIISRRSV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 134 NTPLETRIRVIDGVLTCGIGQRVGIFASAGCGKT-VLMHMLVNNTEADVFVIGL-IGERGREVTECAESLKKSVNAAKCV 211
Cdd:CHL00059 122 YEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTaVATDTILNQKGQNVICVYVaIGQKASSVAQVVTTLQERGAMEYTI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 212 LVYATSDFSSVDRCNAALMATTVAEYFRDRGKRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERP- 290
Cdd:CHL00059 202 VVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAa 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446656971 291 --GPTL-KGSITAFYTVLLEGEDESDPLGDEIRSILDGHIYLSRKLAGQGHYPAIDVLKSVSRV 351
Cdd:CHL00059 282 klSSQLgEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRV 345
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
1-407 |
5.97e-31 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 123.22 E-value: 5.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 1 MKKLkllnkYSYLHSINGSLIEAELDDVSVGEVCEIYASWQAneriARAQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTG 80
Cdd:PRK02118 1 MQKI-----YTKITDITGNVITVEAEGVGYGELATVERKDGS----SLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 81 EQLTIQISDAFLGSVLNASGQimerfvPDTPGERGNLRLIDELPPSYQE-RRVI-NTPLETRIRVIDGVLTCGIGQRVGI 158
Cdd:PRK02118 72 RPMQVTYSESLLGRRFNGSGK------PIDGGPELEGEPIEIGGPSVNPvKRIVpREMIRTGIPMIDVFNTLVESQKIPI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 159 FASAGCGKTVLMHMLVNNTEADVFVIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFSSVDRCNAALMATTVAEYF 238
Cdd:PRK02118 146 FSVSGEPYNALLARIALQAEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 239 R-DRGKRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLER----PGptlKGSITAFYTVLLEGEDESD 313
Cdd:PRK02118 226 AlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKavdfED---GGSITIIAVTTMPGDDVTH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 314 PLGDEIRSILDGHIYLsrklagqgHYPAIDVLKSVSR----VFGQVTDEKHRDnaarvrkILTTLEDLqvfidlgeYRAG 389
Cdd:PRK02118 303 PVPDNTGYITEGQFYL--------RRGRIDPFGSLSRlkqlVIGKKTREDHGD-------LMNAMIRL--------YADS 359
|
410
....*....|....*...
gi 446656971 390 QNAENDFAMNArpKLTNW 407
Cdd:PRK02118 360 REAKEKMAMGF--KLSNW 375
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
10-351 |
4.80e-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: 4.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 10 YSYLHSINGSLIEaeLDDVSVGEVCEIYASWQANERIARAQVVGFRNGKTLLNLIGSSVGL-TRTAVLKPTGEQLTIQIS 88
Cdd:TIGR01040 2 YRTVSGVNGPLVI--LDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIdAKKTTCEFTGDILRTPVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 89 DAFLGSVLNASGQIMERFVPDTPGErgnLRLIDELPPSYQERRVINTPLETRIRVIDGVLTCGIGQRVGIFASAGcgktv 168
Cdd:TIGR01040 80 EDMLGRVFNGSGKPIDKGPPVLAED---YLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAG----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 169 LMHmlvNNTEADVF-VIGLIGERGREVTECAESLKKSVNAAKCVLV----YATSDFS------------------SVDRC 225
Cdd:TIGR01040 152 LPH---NEIAAQICrQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMetarFFKQDFEengsmervclflnlandpTIERI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 226 NAALMATTVAEYFR-DRGKRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTL--KGSITAFY 302
Cdd:TIGR01040 229 ITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrNGSITQIP 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446656971 303 TVLLEGEDESDPLGDEIRSILDGHIYLSRKLAGQGHYPAIDVLKSVSRV 351
Cdd:TIGR01040 309 ILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRL 357
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
127-374 |
1.48e-22 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 100.24 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 127 YQERRVINTPLETRIRVIDGVLTCGIGqrvGIFASAG---CGKTVLMHMLVNNTEADVFVIGLIGERGREVTECAESLKK 203
Cdd:PRK04192 201 YKEKLPPVEPLITGQRVIDTFFPVAKG---GTAAIPGpfgSGKTVTQHQLAKWADADIVIYVGCGERGNEMTEVLEEFPE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 204 SVNA-------AKCVLVYATSDF------SSVdrcnaaLMATTVAEYFRDRGKRVVLFIDSMTRYARALRDMKLAAGEPP 270
Cdd:PRK04192 278 LIDPktgrplmERTVLIANTSNMpvaareASI------YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMP 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 271 ARRGYPASVFDSLPRLLERPG--PTL---KGSITAFYTVLLEGEDESDPLGDEIRSILDGHIYLSRKLAGQGHYPAIDVL 345
Cdd:PRK04192 352 GEEGYPAYLASRLAEFYERAGrvKTLggeEGSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWL 431
|
250 260 270
....*....|....*....|....*....|...
gi 446656971 346 KSVSRVFGQVTD--EKH--RDNAARVRKILTTL 374
Cdd:PRK04192 432 TSYSLYLDQVAPwwEENvdPDWRELRDEAMDLL 464
|
|
| 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 |
5.89e-22 |
|
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: 88.91 E-value: 5.89e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446656971 10 YSYLHSINGSLIEAELD-DVSVGEVCEIYASWQANERIARAQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTGE 81
Cdd:cd01426 1 KGRVIRVNGPLVEAELEgEVAIGEVCEIERGDGNNETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
76-370 |
1.43e-20 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 93.88 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 76 LKPTGEQLTIQISDAFLGSVLNASGQIM----ERFVPDTPGERGNLrlIDELPPSYQERRVINTPLETRIRVIDGVLTCG 151
Cdd:PRK07165 64 LIELNNTNKVKTSKEYFGKIIDIDGNIIypeaQNPLSKKFLPNTSS--IFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 152 IGQRVGIFASAGCGKT-VLMHMLVNNTEADVFVIGL-IGERGREVTECAESLKKSVNAAKCVLVYATSDfSSVDRCNAAL 229
Cdd:PRK07165 142 KGQRELIIGDRQTGKThIALNTIINQKNTNVKCIYVaIGQKRENLSRIYETLKEHDALKNTIIIDAPST-SPYEQYLAPY 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 230 MATTVAE---YFRDrgkrVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGpTLKG--SITAFYTV 304
Cdd:PRK07165 221 VAMAHAEnisYNDD----VLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAG-KFKNrkTITALPIL 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446656971 305 LLEGEDESDPLGDEIRSILDGHIYLSRKLAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKI 370
Cdd:PRK07165 296 QTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKI 361
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
356-425 |
2.12e-20 |
|
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: 84.41 E-value: 2.12e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 356 TDEKHRDNAARVRKILTTLEDLQVFIDLGEYRAGQNAENDFAMNARPKLTNWLKQSVNEKMPMSETLKEL 425
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIGAYQAGSDPEIDEAIAKRPAINAFLRQGVDEPVSFEETLAQL 70
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
22-353 |
9.98e-20 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 91.28 E-value: 9.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 22 EAELDDV----SVGE-VCEIY--ASWQANEriaraqVVGFRNGkTL---LNLIGSSVGltrtAVL-------------KP 78
Cdd:PRK09281 22 EAEVEEVgtviSVGDgIARVYglDNVMAGE------LLEFPGG-VYgiaLNLEEDNVG----AVIlgdyedikegdtvKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 79 TGEQLTIQISDAFLGSVLNASGQimerfvP-DTPGERGNL--RLIDELPPSYQERRVINTPLETRIRVIDGVLTCGIGQR 155
Cdd:PRK09281 91 TGRILEVPVGEALLGRVVNPLGQ------PiDGKGPIEATetRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 156 VGIFASAGCGKT-VLMHMLVNNTEADVFVIGL-IGERGREVTECAESLKKSVNAAKCVLVYAT-SDfssvdrcNAALM-- 230
Cdd:PRK09281 165 ELIIGDRQTGKTaIAIDTIINQKGKDVICIYVaIGQKASTVAQVVRKLEEHGAMEYTIVVAATaSD-------PAPLQyl 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 231 ----ATTVAEYFRDRGKRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERP---GPTLK-GSITAFy 302
Cdd:PRK09281 238 apyaGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAaklSDELGgGSLTAL- 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446656971 303 tvllegedesdPL-----GD-------EIRSILDGHIYLSRKLAGQGHYPAIDVLKSVSRVFG 353
Cdd:PRK09281 317 -----------PIietqaGDvsayiptNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGG 368
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
167-362 |
1.59e-19 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 91.24 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 167 TVLMHMLVNNTEADVFVIGLIGERGREVTECAESLKKSVNA-------AKCVLVYATSDFSSVDRCNAALMATTVAEYFR 239
Cdd:PRK14698 670 TVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLKDPktgkplmERTVLIANTSNMPVAAREASIYTGITIAEYFR 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 240 DRGKRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLERPGPTLK-------GSITAFYTVLLEGEDES 312
Cdd:PRK14698 750 DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTlgsdyrvGSVSVIGAVSPPGGDFS 829
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446656971 313 DPLGDEIRSILDGHIYLSRKLAGQGHYPAIDVLKSVSRVFGQVTDEKHRD 362
Cdd:PRK14698 830 EPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKN 879
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
79-377 |
4.95e-19 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 89.33 E-value: 4.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 79 TGEQLTIQISDAFLGSVLNASGQ-------IMERFVPDTPGERGNlrlIDELPPSYQERRVINTPLETRIRVIDGVLTCG 151
Cdd:PTZ00185 111 TGKLLYIPVGAGVLGKVVNPLGHevpvgllTRSRALLESEQTLGK---VDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 152 IGQRVGIFASAGCGKTVL------------MHMLVNNTEADVFVIglIGERGREVTECAESLKKSVNAAKCVLVYATSDF 219
Cdd:PTZ00185 188 RGQRELIVGDRQTGKTSIavstiinqvrinQQILSKNAVISIYVS--IGQRCSNVARIHRLLRSYGALRYTTVMAATAAE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 220 SSVDRCNAALMATTVAEYFRDRGKRVVLFIDSMTRYARALRDMKLAAGEPPARRGYPASVFDSLPRLLER-----PGPTl 294
Cdd:PTZ00185 266 PAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERaamlsPGKG- 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 295 KGSITAFYTVLLEGEDESDPLGDEIRSILDGHIYLSRKLAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTL 374
Cdd:PTZ00185 345 GGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAMKAVAGKLKGILAEY 424
|
...
gi 446656971 375 EDL 377
Cdd:PTZ00185 425 RKL 427
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
104-375 |
8.69e-19 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 87.45 E-value: 8.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 104 ERFVPDTPGERGNLRLIDELPPSY-QERRVINTPLETRI-RVIDGVLTCGIGQRVGIFASAGCGKTVLMH-----MLVNN 176
Cdd:PRK12608 82 DSVNGTDPEKLARRPHFDDLTPLHpRERLRLETGSDDLSmRVVDLVAPIGKGQRGLIVAPPRAGKTVLLQqiaaaVAANH 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 177 TEADVFVIgLIGERGREVTEcaesLKKSVNAAkcvlVYA-TSDFSSVDRCNAALMATTVAEYFRDRGKRVVLFIDSMTRY 255
Cdd:PRK12608 162 PEVHLMVL-LIDERPEEVTD----MRRSVKGE----VYAsTFDRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 256 ARALRDMKLAAGepparRGYPASVfDSlpRLLERP----GPTLK----GSITAFYTVLLE-GEDESDPLGDEIRSILDGH 326
Cdd:PRK12608 233 ARAYNNEVESSG-----RTLSGGV-DA--RALQRPkrlfGAARNieegGSLTIIATALVDtGSRMDEVIFEEFKGTGNME 304
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 446656971 327 IYLSRKLAGQGHYPAIDVLKSVSR----VFGQVTDEKHRdnaaRVRKILTTLE 375
Cdd:PRK12608 305 IVLDRELADKRVFPAIDIAKSGTRreelLLDSKELEKVR----RLRRALASRK 353
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
109-378 |
2.66e-17 |
|
transcription termination factor Rho; This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding. [Transcription, Transcription factors]
Pssm-ID: 162030 [Multi-domain] Cd Length: 415 Bit Score: 83.20 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 109 DTPGERGNLRLIDELPPSYQERRVIntpLETR-----IRVIDGVLTCGIGQRVGIFASAGCGKTVLMHML-----VNNTE 178
Cdd:TIGR00767 122 DDPEKAKNRVLFENLTPLYPNERLR---LETStedlsTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIaqaitRNHPE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 179 ADVFVIgLIGERGREVTECAESLKKSVnaakcvlVYATSDFSSVDRCNAALMATTVAEYFRDRGKRVVLFIDSMTRYARA 258
Cdd:TIGR00767 199 VELIVL-LIDERPEEVTDMQRSVKGEV-------VASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 259 LRDMKLAAGE------------PPARrgypasvFDSLPRLLERpgptlKGSITAFYTVLLE-GEDESDPLGDEIRSILDG 325
Cdd:TIGR00767 271 YNTVTPASGKvlsggvdanalhRPKR-------FFGAARNIEE-----GGSLTIIATALIDtGSRMDEVIFEEFKGTGNM 338
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 446656971 326 HIYLSRKLAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAARVRKILTTLEDLQ 378
Cdd:TIGR00767 339 ELHLDRKLADRRIFPAIDIKKSGTRKEELLLTPEELQKIWVLRKIISPMDSIE 391
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
142-378 |
1.02e-14 |
|
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: 73.39 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 142 RVIDGVLTCGIGQRVGIFASAGCGKTVLMHMLV-----NNTEADVFVIgLIGERGREVTECAESLKKSVnaakcvlVYAT 216
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIAnaiakNHPEVELIVL-LIDERPEEVTDMRRSVKGEV-------VAST 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 217 SDFSSVDRCNAALMATTVAEYFRDRGKRVVLFIDSMTRYARALRdmklaAGEPPARRGYPASVFdslPRLLERP----GP 292
Cdd:cd01128 77 FDEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYN-----TVVPSSGKTLSGGVD---ANALHKPkrffGA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 293 TLK----GSITAFYTVLLE-GEDESDPLGDEIRSILDGHIYLSRKLAGQGHYPAIDVLKSVSRVFGQVTDEKHRDNAARV 367
Cdd:cd01128 149 ARNieegGSLTIIATALVDtGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTRKEELLLTPEELQKIWLL 228
|
250
....*....|.
gi 446656971 368 RKILTTLEDLQ 378
Cdd:cd01128 229 RRILSPMDPIE 239
|
|
| ATP-synt_flagellum-secretory_path_III_C |
cd18114 |
Flagellum-specific ATP synthase, C-terminal domain; The C-terminal domain of the ... |
360-428 |
6.17e-13 |
|
Flagellum-specific ATP synthase, C-terminal domain; The C-terminal domain of the flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The flagellum-specific ATPase FliI is the soluble export component that drives flagellar protein export, and it shows extensive similarity to the alpha and beta subunits of FoF1-ATP synthase. Although they both are proton driven rotary molecular devices, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 349749 [Multi-domain] Cd Length: 71 Bit Score: 63.40 E-value: 6.17e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446656971 360 HRDNAARVRKILTTLEDLQVFIDLGEYRAGQNAENDFAMNARPKLTNWLKQSVNEKMPMSETLKELERI 428
Cdd:cd18114 1 HYLAARKFRELMSTYQENEDLIRIGAYKKGSDPEVDEAIRLKPQIEAFLKQGLNEKAPLEESLQQLEEI 69
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
121-350 |
6.77e-12 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 66.70 E-value: 6.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 121 DELPPSYQERRV---INTPLETRIRVIDGVLTCGIGQRVGIFASAGCGKTVLMHML-----VNNTEADVFVIgLIGERGR 192
Cdd:PRK09376 134 ENLTPLYPNERLrleTGNPEDLSTRIIDLIAPIGKGQRGLIVAPPKAGKTVLLQNIansitTNHPEVHLIVL-LIDERPE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 193 EVTECAESLKKSVnaakcvlVYATSDfssvdrcNAALMATTVAEYFRDRGKR-------VVLFIDSMTRYARAlrdmkla 265
Cdd:PRK09376 213 EVTDMQRSVKGEV-------VASTFD-------EPAERHVQVAEMVIEKAKRlvehgkdVVILLDSITRLARA------- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 266 agepparrgYPASVFDS---L-----PRLLERPgptlK------------GSITAFYTVLLEGEDESDplgDEIRSILDG 325
Cdd:PRK09376 272 ---------YNTVVPSSgkvLsggvdANALHRP----KrffgaarnieegGSLTIIATALIDTGSRMD---EVIFEEFKG 335
|
250 260
....*....|....*....|....*....
gi 446656971 326 ----HIYLSRKLAGQGHYPAIDVLKSVSR 350
Cdd:PRK09376 336 tgnmELHLDRKLAEKRIFPAIDINRSGTR 364
|
|
| ATP-synt_flagellum-secretory_path_III_N |
cd18117 |
Flagellum-specific ATP synthase, N-terminal domain; The N-terminal domain of the ... |
15-81 |
2.30e-09 |
|
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: 53.30 E-value: 2.30e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446656971 15 SINGSLIEAELDDVSVGEVCEIYaswQANERIARAQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTGE 81
Cdd:cd18117 7 RVVGLLLEAVGPQAPIGELCLIE---TADGLSILAEVVGFSGEKVLLMPLGELSGLSPGARVVPLGR 70
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
123-258 |
2.30e-07 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 52.98 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 123 LPPSY-QER-RVINTP--LETRirVIDGVLTCGIGQRVGIFASAGCGKTVLMH-----MLVNNTEADVFVIgLIGERGRE 193
Cdd:PRK12678 384 LTPLYpNERlRLETEPkkLTTR--VIDLIMPIGKGQRGLIVSPPKAGKTTILQnianaITTNNPECHLMVV-LVDERPEE 460
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446656971 194 VTECAESLKKSVNAakcvlvyatsdfSSVDRcnAALMATTVAEYFRDRGKR-------VVLFIDSMTRYARA 258
Cdd:PRK12678 461 VTDMQRSVKGEVIA------------STFDR--PPSDHTTVAELAIERAKRlvelgkdVVVLLDSITRLGRA 518
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
153-333 |
2.00e-05 |
|
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: 44.29 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 153 GQRVGIFASAGCGKTVLMHMLvnnteadvfvIGLIGERGREVTECAESLKKSVNAAKCVLVYATSDFSSVDRCNAALMAT 232
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARAL----------ARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446656971 233 TVAEYFRDRgkrvVLFIDSMTRYARALRDMKLaagepparrgypasvfdslpRLLERPGPTLKGSITAFYTVLLEGEDES 312
Cdd:smart00382 72 ALARKLKPD----VLILDEITSLLDAEQEALL--------------------LLLEELRLLLLLKSEKNLTVILTTNDEK 127
|
170 180
....*....|....*....|.
gi 446656971 313 DPLGDEIRSILDGHIYLSRKL 333
Cdd:smart00382 128 DLGPALLRRRFDRRIVLLLIL 148
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
15-80 |
7.02e-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: 37.91 E-value: 7.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446656971 15 SINGSLIEAELD-DVSVGEVCEIYASWQANERIARAQVVGFRNGKTLLNLIGSSVGLTRTAVLKPTG 80
Cdd:pfam02874 3 QVIGPVVDVEFGiGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| |
