|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
2-731 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 274241 [Multi-domain] Cd Length: 730 Bit Score: 989.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 2 LSEHLQAALQRAADLAQAAGHEYITQEHLLLALLGDPEAKDALNALGADLNALREALTEQLAELDIL----DDPDPDFTL 77
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAIEILEECGGDVELLRKRLEDYLEENLPVipedIDEEPEQTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 78 GVHRVVQGAVLqlHASGKGKEQADGARVLVELLEEDDSPARAALEAQGVTRLDLLNYLSHGVAKAPGHSRERRVAGVDGE 157
Cdd:TIGR02639 81 GVQRVIQRALL--HVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITRLDILNYISHGISKDDGKDQLGEEAGKEEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 158 ltaegapAEENPLEAYAQNLTEAAKNGEFDPVIGRGAELERVVHILARRGKNNPVLVGEPGVGKTALAEGLAQRVADGKA 237
Cdd:TIGR02639 159 -------KGQDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 238 PGFLRGASVYALDLGALLAGTRYRGDFEGRLKAVLAALDGQ-NSVLFIDELHTLVGAGATEGGSVDAANLLKPALARGKL 316
Cdd:TIGR02639 232 PERLKNAKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEpNAILFIDEIHTIVGAGATSGGSMDASNLLKPALSSGKI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 317 RVMGATTPAELR-LLEKDRALWRRFQTVDVPEPSEADAVQILQGLAPKYAAHHGVTYTPPALEAAVRLSARYLRDRFLPD 395
Cdd:TIGR02639 312 RCIGSTTYEEYKnHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 396 KAIDVLDEAGAA---RSSTGQGGEIDVPDIESTVARMARVPVGAVKAEEVQSLATLEADLNRRVYGQEPAVSAVSSAVKL 472
Cdd:TIGR02639 392 KAIDVIDEAGAAfrlRPKAKKKANVNVKDIENVVAKMAKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 473 ARAGLRNPQKPQGSFLFAGPTGVGKTELARALAERLGVELIRFDMSEYQEPHTVARLIGAPPGYVGFDQGGLLTDAVAKN 552
Cdd:TIGR02639 472 SRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEELGVHLLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKH 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 553 PHAVLLLDEIEKAHPDVYNIFLQLMDHGTLTDHAGKKVDGRGLILIFTTNAGAADASRPALGFSREGRAGEQAEAVKRTF 632
Cdd:TIGR02639 552 PHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTSNAGASEMSKPPIGFGGENRESKSLKAIKKLF 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 633 TPEFRNRLDAVIYFAPLSRTVMTSVVDKFLRELGEQLTERGVTLTVTPAARARLAELGYDPLLGARPLARVIEDKLGRPL 712
Cdd:TIGR02639 632 SPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPL 711
|
730
....*....|....*....
gi 499189693 713 ADELLFGRLKDGGAVKVGV 731
Cdd:TIGR02639 712 SDEILFGKLKKGGSVKISL 730
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2-737 |
0e+00 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 837.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 2 LSEHLQAALQRAADLAQAAGHEYITQEHLLLALLGDPE--AKDALNALGADLNALREALTEQLAELDILDDPDPDFTLGV 79
Cdd:COG0542 6 FTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEglAAKLLRKLGVDLDALREELEEALGRLPKVSGSSGQPYLSP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 80 H--RVVQGAvlQLHASGKGKEQADGARVLVELLEEDDSPARAALEAQGVTRLDLLNYLshgvAKAPGHSRErrvagvdge 157
Cdd:COG0542 86 RlkRVLELA--ELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITLEALREAL----EELRGGSRV--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 158 lTAEGAPAEENPLEAYAQNLTEAAKNGEFDPVIGRGAELERVVHILARRGKNNPVLVGEPGVGKTALAEGLAQRVADGKA 237
Cdd:COG0542 151 -TSQNPESKTPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 238 PGFLRGASVYALDLGALLAGTRYRGDFEGRLKAVLAALDGQNS--VLFIDELHTLVGAGATEgGSVDAANLLKPALARGK 315
Cdd:COG0542 230 PESLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKSEGniILFIDELHTLVGAGGAE-GAMDAANLLKPALARGE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 316 LRVMGATTPAELRL-LEKDRALWRRFQTVDVPEPSEADAVQILQGLAPKYAAHHGVTYTPPALEAAVRLSARYLRDRFLP 394
Cdd:COG0542 309 LRCIGATTLDEYRKyIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 395 DKAIDVLDEAGA-------------------------------------------------------------------- 406
Cdd:COG0542 389 DKAIDLIDEAAArvrmeidskpeeldelerrleqleiekealkkeqdeasferlaelrdelaeleeelealkarweaeke 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 407 ----------------------------ARSSTGQGG-----EIDVPDIESTVARMARVPVGAVKAEEVQSLATLEADLN 453
Cdd:COG0542 469 lieeiqelkeeleqrygkipelekelaeLEEELAELApllreEVTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEEELH 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 454 RRVYGQEPAVSAVSSAVKLARAGLRNPQKPQGSFLFAGPTGVGKTELARALAERL-GVE--LIRFDMSEYQEPHTVARLI 530
Cdd:COG0542 549 ERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLfGDEdaLIRIDMSEYMEKHSVSRLI 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 531 GAPPGYVGFDQGGLLTDAVAKNPHAVLLLDEIEKAHPDVYNIFLQLMDHGTLTDHAGKKVDGRGLILIFTTNAGAADASR 610
Cdd:COG0542 629 GAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIGSELILD 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 611 PALGFSREGRAGEQA-EAVKRTFTPEFRNRLDAVIYFAPLSRTVMTSVVDKFLRELGEQLTERGVTLTVTPAARARLAEL 689
Cdd:COG0542 709 LAEDEPDYEEMKEAVmEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAAKDFLAEK 788
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 499189693 690 GYDPLLGARPLARVIEDKLGRPLADELLFGRLKDGGAVKVGVQGGEFS 737
Cdd:COG0542 789 GYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGELV 836
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
1-738 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 815.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 1 MLSEHLQAALQRAADLAQAAGHEYITQEHLLLALLGDPEAKDALNALGADLNALR---EALTEQLAELDILDDPDPDF-- 75
Cdd:PRK11034 1 MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRqelEAFIEQTTPVLPASEEERDTqp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 76 TLGVHRVVQGAVLQLHASGKgkEQADGARVLVELLEEDDSPARAALEAQGVTRLDLLNYLSHGVAKAPGHSRErrvAGVD 155
Cdd:PRK11034 81 TLSFQRVLQRAVFHVQSSGR--SEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPSQSS---DPGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 156 GELTAEGAPAEENpLEAYAQNLTEAAKNGEFDPVIGRGAELERVVHILARRGKNNPVLVGEPGVGKTALAEGLAQRVADG 235
Cdd:PRK11034 156 QPNSEEQAGGEER-MENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 236 KAPGFLRGASVYALDLGALLAGTRYRGDFEGRLKAVLAALD-GQNSVLFIDELHTLVGAGATEGGSVDAANLLKPALARG 314
Cdd:PRK11034 235 DVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEqDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 315 KLRVMGATTPAEL-RLLEKDRALWRRFQTVDVPEPSEADAVQILQGLAPKYAAHHGVTYTPPALEAAVRLSARYLRDRFL 393
Cdd:PRK11034 315 KIRVIGSTTYQEFsNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 394 PDKAIDVLDEAGAaRS----STGQGGEIDVPDIESTVARMARVPVGAVKAEEVQSLATLEADLNRRVYGQEPAVSAVSSA 469
Cdd:PRK11034 395 PDKAIDVIDEAGA-RArlmpVSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 470 VKLARAGLRNPQKPQGSFLFAGPTGVGKTELARALAERLGVELIRFDMSEYQEPHTVARLIGAPPGYVGFDQGGLLTDAV 549
Cdd:PRK11034 474 IKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAV 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 550 AKNPHAVLLLDEIEKAHPDVYNIFLQLMDHGTLTDHAGKKVDGRGLILIFTTNAGAADASRPALGFSREGRAGEQAEAVK 629
Cdd:PRK11034 554 IKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMEEIK 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 630 RTFTPEFRNRLDAVIYFAPLSRTVMTSVVDKFLRELGEQLTERGVTLTVTPAARARLAELGYDPLLGARPLARVIEDKLG 709
Cdd:PRK11034 634 KIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLK 713
|
730 740
....*....|....*....|....*....
gi 499189693 710 RPLADELLFGRLKDGGAVKVGVQGGEFSF 738
Cdd:PRK11034 714 KPLANELLFGSLVDGGQVTVALDKEKNEL 742
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
2-737 |
0e+00 |
|
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274529 [Multi-domain] Cd Length: 850 Bit Score: 674.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 2 LSEHLQAALQRAADLAQAAGHEYITQEHLLLALLGDPE--AKDALNALGADLNALREALTEQLAELDILDDPDPDFTLG- 78
Cdd:TIGR03346 1 LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQEGglARPLLQKAGVNVGALRQALEKELERLPKVSGPGGQVYLSp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 79 -VHRVVQGAvlQLHASGKGKEQADGARVLVELLEEDDSPARAaLEAQGVTRLDLLNylshgvakapghsrerRVAGVDGE 157
Cdd:TIGR03346 81 dLNRLLNLA--EKLAQKRGDEFISSEHLLLALLDDKGTLGKL-LKEAGATADALEA----------------AINAVRGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 158 LTAEGAPAEEN--PLEAYAQNLTEAAKNGEFDPVIGRGAELERVVHILARRGKNNPVLVGEPGVGKTALAEGLAQRVADG 235
Cdd:TIGR03346 142 QKVTDANAEDQyeALEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 236 KAPGFLRGASVYALDLGALLAGTRYRGDFEGRLKAVL---AALDGQnSVLFIDELHTLVGAGATEGgSVDAANLLKPALA 312
Cdd:TIGR03346 222 DVPEGLKNKRLLALDMGALIAGAKYRGEFEERLKAVLnevTKSEGQ-IILFIDELHTLVGAGKAEG-AMDAGNMLKPALA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 313 RGKLRVMGATTPAELR-LLEKDRALWRRFQTVDVPEPSEADAVQILQGLAPKYAAHHGVTYTPPALEAAVRLSARYLRDR 391
Cdd:TIGR03346 300 RGELHCIGATTLDEYRkYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 392 FLPDKAIDVLDEAGA----------------------------------------------------------------- 406
Cdd:TIGR03346 380 FLPDKAIDLIDEAAArirmeidskpeeldeldrriiqleierealkkekdeaskkrledlekeladleeeyaeleeqwka 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 407 -------------------------------ARSSTGQGG--------------------------EIDVPDIESTVARM 429
Cdd:TIGR03346 460 ekasiqgiqqikeeieqvrleleqaeregdlAKAAELQYGklpelekqlqaaeqklgeeqnrllreEVTAEEIAEVVSRW 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 430 ARVPVGAVKAEEVQSLATLEADLNRRVYGQEPAVSAVSSAVKLARAGLRNPQKPQGSFLFAGPTGVGKTELARALAERL- 508
Cdd:TIGR03346 540 TGIPVSKMLEGEREKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLf 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 509 --GVELIRFDMSEYQEPHTVARLIGAPPGYVGFDQGGLLTDAVAKNPHAVLLLDEIEKAHPDVYNIFLQLMDHGTLTDHA 586
Cdd:TIGR03346 620 dsEDAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQ 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 587 GKKVDGRGLILIFTTNAGAADASRPALGFSREGRAGEQAEAVKRTFTPEFRNRLDAVIYFAPLSRTVMTSVVDKFLRELG 666
Cdd:TIGR03346 700 GRTVDFRNTVIIMTSNLGSDFIQELAGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLR 779
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499189693 667 EQLTERGVTLTVTPAARARLAELGYDPLLGARPLARVIEDKLGRPLADELLFGRLKDGGAVKVGVQGGEFS 737
Cdd:TIGR03346 780 KRLAERKITLELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGRLV 850
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
13-732 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 657.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 13 AADLAQAAGHEYITQEHLLLALLGD--PEAKDALNALGADLNALREALTEQLAELDILDDPDPDFTLGVHRVVQGAVLQL 90
Cdd:CHL00095 16 SQEEARRLGHNFVGTEQILLGLIGEgtGIAARALKSMGVTLKDARIEVEKIIGRGTGFVAVEIPFTPRAKRVLEMSLEEA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 91 HASGK---GKEQadgarVLVELLEEDDSPARAALEAQGVT----RLDLLNYLShgvakapghsrERRVAGVDGELTAEGA 163
Cdd:CHL00095 96 RDLGHnyiGTEH-----LLLALLEEGEGVAARVLENLGVDlskiRSLILNLIG-----------EIIEAILGAEQSRSKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 164 PAeenpLEAYAQNLTEAAKNGEFDPVIGRGAELERVVHILARRGKNNPVLVGEPGVGKTALAEGLAQRVADGKAPGFLRG 243
Cdd:CHL00095 160 PT----LEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILED 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 244 ASVYALDLGALLAGTRYRGDFEGRLKAVLAALDGQNSV-LFIDELHTLVGAGATEGgSVDAANLLKPALARGKLRVMGAT 322
Cdd:CHL00095 236 KLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIiLVIDEVHTLIGAGAAEG-AIDAANILKPALARGELQCIGAT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 323 TPAELR-LLEKDRALWRRFQTVDVPEPSEADAVQILQGLAPKYAAHHGVTYTPPALEAAVRLSARYLRDRFLPDKAIDVL 401
Cdd:CHL00095 315 TLDEYRkHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 402 DEAGA---------------------------------------------------------ARSSTGQGGEIDVP---- 420
Cdd:CHL00095 395 DEAGSrvrlinsrlppaareldkelreilkdkdeaireqdfetakqlrdremevraqiaaiiQSKKTEEEKRLEVPvvte 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 421 -DIESTVARMARVPVGAVKAEEVQSLATLEADLNRRVYGQEPAVSAVSSAVKLARAGLRNPQKPQGSFLFAGPTGVGKTE 499
Cdd:CHL00095 475 eDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTE 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 500 LARALAERL-GVE--LIRFDMSEYQEPHTVARLIGAPPGYVGFDQGGLLTDAVAKNPHAVLLLDEIEKAHPDVYNIFLQL 576
Cdd:CHL00095 555 LTKALASYFfGSEdaMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQI 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 577 MDHGTLTDHAGKKVDGRGLILIFTTNAGAADASRPA--LGFSREGRAGEQA----------EAVKRTFTPEFRNRLDAVI 644
Cdd:CHL00095 635 LDDGRLTDSKGRTIDFKNTLIIMTSNLGSKVIETNSggLGFELSENQLSEKqykrlsnlvnEELKQFFRPEFLNRLDEII 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 645 YFAPLSRTVMTSVVDKFLRELGEQLTERGVTLTVTPAARARLAELGYDPLLGARPLARVIEDKLGRPLADELLFGRLKDG 724
Cdd:CHL00095 715 VFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPG 794
|
....*...
gi 499189693 725 GAVKVGVQ 732
Cdd:CHL00095 795 DIIIVDVN 802
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
2-728 |
0e+00 |
|
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, an ATPase associated with chaperone-related functions. These ClpB homologs, designated ClpV1, are a key component of the bacterial pathogenicity-associated type VI secretion system. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274528 [Multi-domain] Cd Length: 852 Bit Score: 543.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 2 LSEHLQAALQRAADLAQAAGHEYITQEHLLLALL--GDPEAKDALNALGADLNALREALTEQLAELDILDDPDPDFTLGV 79
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLdqPDSDLAAILRHFGVDLGRLKADLARALDKLPRGNTRTPVFSPHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 80 HRVVQGAVLqLHASGKGKEQADGARVLVELLEEDD-----SPARAALEAQGVTRLdllnylSHGVAKAPGHSRERRVAGV 154
Cdd:TIGR03345 81 VELLQEAWL-LASLELGDGRIRSGHLLLALLTDPElrrllGSISPELAKIDREAL------REALPALVEGSAEASAAAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 155 D-GELTAEGAPAEENPLEAYAQNLTEAAKNGEFDPVIGRGAELERVVHILARRGKNNPVLVGEPGVGKTALAEGLAQRVA 233
Cdd:TIGR03345 154 DaAPAGAAAGAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 234 DGKAPGFLRGASVYALDLGALLAGTRYRGDFEGRLKAVLAALDG--QNSVLFIDELHTLVGAGATEGGSvDAANLLKPAL 311
Cdd:TIGR03345 234 AGDVPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKAspQPIILFIDEAHTLIGAGGQAGQG-DAANLLKPAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 312 ARGKLRVMGATTPAEL-RLLEKDRALWRRFQTVDVPEPSEADAVQILQGLAPKYAAHHGVTYTPPALEAAVRLSARYLRD 390
Cdd:TIGR03345 313 ARGELRTIAATTWAEYkKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 391 RFLPDKAIDVLDEAGA---------------------------------------------------------------- 406
Cdd:TIGR03345 393 RQLPDKAVSLLDTACArvalsqnatpaaledlrrriaaleleldalereaalgadhderlaelraelaaleaelaalear 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 407 ---------------ARSSTGQGGEIDVPD-------------------------------IESTVARMARVPVGAVKAE 440
Cdd:TIGR03345 473 wqqekelveailalrAELEADADAPADDDDalraqlaeleaalasaqgeeplvfpevdaqaVAEVVADWTGIPVGRMVRD 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 441 EVQSLATLEADLNRRVYGQEPAVSAVSSAVKLARAGLRNPQKPQGSFLFAGPTGVGKTELARALAERL-GVE--LIRFDM 517
Cdd:TIGR03345 553 EIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLyGGEqnLITINM 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 518 SEYQEPHTVARLIGAPPGYVGFDQGGLLTDAVAKNPHAVLLLDEIEKAHPDVYNIFLQLMDHGTLTDHAGKKVDGRGLIL 597
Cdd:TIGR03345 633 SEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVI 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 598 IFTTNAGAADASRPALGFSREGRAGEQAEAVK----RTFTPEFRNRLDAVIYFaPLSRTVMTSVVDKFLRELGEQLTER- 672
Cdd:TIGR03345 713 LLTSNAGSDLIMALCADPETAPDPEALLEALRpellKVFKPAFLGRMTVIPYL-PLDDDVLAAIVRLKLDRIARRLKENh 791
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 499189693 673 GVTLTVTPAARARLAELGYDPLLGARPLARVIEDKLGRPLADELLfGRLKDGGAVK 728
Cdd:TIGR03345 792 GAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQIL-ERLAAGEPIE 846
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
2-734 |
3.88e-177 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 529.03 E-value: 3.88e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 2 LSEHLQAALQRAADLAQAAGHEYITQEHLLLALLGDP--EAKDALNALGADLNALREALTEQLAELDILDDpdpdfTLGV 79
Cdd:PRK10865 6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEggSVRPLLTSAGINAGQLRTDINQALSRLPQVEG-----TGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 80 HRVVQGAVLQLHASGKGKEQADGARVLVELLeeddspARAALEAQGvTRLDLLNylSHGVAKAPGHSRERRVAGVDgELT 159
Cdd:PRK10865 81 VQPSQDLVRVLNLCDKLAQKRGDNFISSELF------VLAALESRG-TLADILK--AAGATTANITQAIEQMRGGE-SVN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 160 AEGAPAEENPLEAYAQNLTEAAKNGEFDPVIGRGAELERVVHILARRGKNNPVLVGEPGVGKTALAEGLAQRVADGKAPG 239
Cdd:PRK10865 151 DQGAEDQRQALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 240 FLRGASVYALDLGALLAGTRYRGDFEGRLKAVLAALDGQ--NSVLFIDELHTLVGAGATEgGSVDAANLLKPALARGKLR 317
Cdd:PRK10865 231 GLKGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLAKQegNVILFIDELHTMVGAGKAD-GAMDAGNMLKPALARGELH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 318 VMGATTPAELR-LLEKDRALWRRFQTVDVPEPSEADAVQILQGLAPKYAAHHGVTYTPPALEAAVRLSARYLRDRFLPDK 396
Cdd:PRK10865 310 CVGATTLDEYRqYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 397 AIDVLDEAGA---------------------------------------------------------------------- 406
Cdd:PRK10865 390 AIDLIDEAASsirmqidskpeeldrldrriiqlkleqqalmkesdeaskkrldmlneelsdkerqyseleeewkaekasl 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 407 --------------------------ARSSTGQGGEI-----------------------DVPDIE--STVARMARVPVG 435
Cdd:PRK10865 470 sgtqtikaeleqakiaieqarrvgdlARMSELQYGKIpelekqlaaatqlegktmrllrnKVTDAEiaEVLARWTGIPVS 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 436 AVKAEEVQSLATLEADLNRRVYGQEPAVSAVSSAVKLARAGLRNPQKPQGSFLFAGPTGVGKTELARALAERL---GVEL 512
Cdd:PRK10865 550 RMLESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMfdsDDAM 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 513 IRFDMSEYQEPHTVARLIGAPPGYVGFDQGGLLTDAVAKNPHAVLLLDEIEKAHPDVYNIFLQLMDHGTLTDHAGKKVDG 592
Cdd:PRK10865 630 VRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDF 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 593 RGLILIFTTNAGaADASRPALGFSREGRAGEQA-EAVKRTFTPEFRNRLDAVIYFAPLSRTVMTSVVDKFLRELGEQLTE 671
Cdd:PRK10865 710 RNTVVIMTSNLG-SDLIQERFGELDYAHMKELVlGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEE 788
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499189693 672 RGVTLTVTPAARARLAELGYDPLLGARPLARVIEDKLGRPLADELLFGRLKDGGAVKVGVQGG 734
Cdd:PRK10865 789 RGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDD 851
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
444-646 |
1.29e-81 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 257.49 E-value: 1.29e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 444 SLATLEADLNRRVYGQEPAVSAVSSAVKLARAGLRNPQKPQGSFLFAGPTGVGKTELARALAERL---GVELIRFDMSEY 520
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 521 QEPHTVARLIGAPPGYVGFDQGGLLTDAVAKNPHAVLLLDEIEKAHPDVYNIFLQLMDHGTLTDHAGKKVDGRGLILIFT 600
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499189693 601 TNAgaadasrpalgfsregrageqaeavkrtFTPEFRNRLDAVIYF 646
Cdd:cd19499 161 SNH----------------------------FRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
482-643 |
2.16e-75 |
|
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400187 [Multi-domain] Cd Length: 168 Bit Score: 240.56 E-value: 2.16e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 482 KPQGSFLFAGPTGVGKTELARALAERLGV---ELIRFDMSEYQEPHTVARLIGAPPGYVGFDQGGLLTDAVAKNPHAVLL 558
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 559 LDEIEKAHPDVYNIFLQLMDHGTLTDHAGKKVDGRGLILIFTTNAGAA---DASRPALGFSREGRAGEQAEAVKRTFTPE 635
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEkisDASRLGDSPDYELLKEEVMDLLKKGFIPE 160
|
....*...
gi 499189693 636 FRNRLDAV 643
Cdd:pfam07724 161 FLGRLPII 168
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
349-450 |
2.27e-34 |
|
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.
Pssm-ID: 465544 [Multi-domain] Cd Length: 104 Bit Score: 126.45 E-value: 2.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 349 SEADAVQILQGLAPKYAAHHGVTYTPPALEAAVRLSARYLRDRFLPDKAIDVLDEAGAARSSTGQGGEIDVPDIESTVAR 428
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|..
gi 499189693 429 MARVPVGAVKAEEVQSLATLEA 450
Cdd:pfam17871 81 LEIEKEALEREQDFEKAERLAK 102
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
649-729 |
7.35e-27 |
|
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA, pfam00004) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerization, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilize the functional assembly. The domain is associated with two Clp_N, pfam02861, at the N-terminus as well as AAA, pfam00004 and AAA_2, pfam07724.
Pssm-ID: 463090 [Multi-domain] Cd Length: 81 Bit Score: 104.41 E-value: 7.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 649 LSRTVMTSVVDKFLRELGEQLTERGVTLTVTPAARARLAELGYDPLLGARPLARVIEDKLGRPLADELLFGRLKDGGAVK 728
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 499189693 729 V 729
Cdd:pfam10431 81 V 81
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
649-738 |
3.32e-26 |
|
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerisation, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilise the functional assembly. The domain is associated with two Clp_N at the N-terminus as well as AAA and AAA_2.
Pssm-ID: 198154 [Multi-domain] Cd Length: 90 Bit Score: 102.52 E-value: 3.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 649 LSRTVMTSVVDKFLRELGEQLTERGVTLTVTPAARARLAELGYDPLLGARPLARVIEDKLGRPLADELLFGRLKDGGAVK 728
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
90
....*....|
gi 499189693 729 VGVQGGEFSF 738
Cdd:smart01086 81 VDVDDGELVF 90
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
190-348 |
1.02e-17 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 80.65 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 190 IGRGAELERVVHILARRGKNNPVLVGEPGVGKTALAEGLAQRVadgkapgFLRGASVYALDLGALLAGTRYRGDFEGRLK 269
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANEL-------FRPGAPFLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 270 AVLAAL--DGQNSVLFIDELHTLvgAGATEGGSVDAANLLKPALA-RGKLRVMGATTPAELRLLekDRALWRRFQTVDVP 346
Cdd:cd00009 74 RLLFELaeKAKPGVLFIDEIDSL--SRGAQNALLRVLETLNDLRIdRENVRVIGATNRPLLGDL--DRALYDRLDIRIVI 149
|
..
gi 499189693 347 EP 348
Cdd:cd00009 150 PL 151
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
457-613 |
5.02e-15 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 72.95 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 457 YGQEPAVSAVSSAVKLaraglrnpqKPQGSFLFAGPTGVGKTELARALAERL---GVELIRFDMSEYQEPHTVARLIgap 533
Cdd:cd00009 1 VGQEEAIEALREALEL---------PPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELF--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 534 pgyvGFDQGGLLTDAVAKNPHAVLLLDEIEKAHPDVYNIFLQLMDHGTLTdhagkKVDGRGLILIFTTNAGAADASRPAL 613
Cdd:cd00009 69 ----GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATNRPLLGDLDRAL 139
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
213-341 |
1.17e-13 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 68.39 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 213 LVGEPGVGKTALAEGLAQRVadgkapgflrGASVYALDLGALLAGtrYRGDFEGRLKAVLAALDGQN-SVLFIDELHTLV 291
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELVSK--YVGESEKRLRELFEAAKKLApCVIFIDEIDALA 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 499189693 292 GAGATEGGSV--DAANLLKPAL-----ARGKLRVMGATTpaELRLLekDRALWRRFQ 341
Cdd:pfam00004 71 GSRGSGGDSEsrRVVNQLLTELdgftsSNSKVIVIAATN--RPDKL--DPALLGRFD 123
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
42-364 |
3.78e-12 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 68.78 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 42 DALNALGADLNALREALTEQLAELDILDDPDPDFTLGVHRVVQGAVLQLHASGKGKEQADGARVLVELLEEDDSPARAAL 121
Cdd:COG0464 9 VALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 122 EAQGVTRLDLLNYLSHGVAKAPGHSRERRVAGVDGELTAEGAPAEENPLEAYAQNLTEAAK---NGEFDPVIG------- 191
Cdd:COG0464 89 LELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLelrEAILDDLGGleevkee 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 192 ---RGAELERVVHILARRGKNNP---VLVGEPGVGKTALAEGLAQRVadgkapgflrGASVYALDLGALLAGtrYRGDFE 265
Cdd:COG0464 169 lreLVALPLKRPELREEYGLPPPrglLLYGPPGTGKTLLARALAGEL----------GLPLIEVDLSDLVSK--YVGETE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 266 GRLKAVLA-ALDGQNSVLFIDELHTLVGAGATEGGSVDA---ANLLKpALA--RGKLRVMGATTpaelRLLEKDRALWRR 339
Cdd:COG0464 237 KNLREVFDkARGLAPCVLFIDEADALAGKRGEVGDGVGRrvvNTLLT-EMEelRSDVVVIAATN----RPDLLDPALLRR 311
|
330 340
....*....|....*....|....*.
gi 499189693 340 FQ-TVDVPEPSEADAVQILQGLAPKY 364
Cdd:COG0464 312 FDeIIFFPLPDAEERLEIFRIHLRKR 337
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
488-646 |
2.50e-11 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 61.46 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 488 LFAGPTGVGKTELARALAERLGVELIRFDMSEyqephTVARLIGAPPGYVgfdqGGLLTDAVAKNPHaVLLLDEIEKAHP 567
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSE-----LVSKYVGESEKRL----RELFEAAKKLAPC-VIFIDEIDALAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 568 -----------DVYNIFLQLMDhgtltdhaGKKVDGRGLILIFTTNagaadasRPalgfsregrageqaeavkRTFTPEF 636
Cdd:pfam00004 72 srgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN-------RP------------------DKLDPAL 118
|
170
....*....|
gi 499189693 637 RNRLDAVIYF 646
Cdd:pfam00004 119 LGRFDRIIEF 128
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
462-602 |
2.84e-11 |
|
proteases similar to RecA; 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: 410889 [Multi-domain] Cd Length: 158 Bit Score: 62.30 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 462 AVSAVSSAVKLARAGLRNPQKPQG---SFLFAGPTGVGKTELARALAERLGVELIRFDMSEYQEPHTvarligappGYVG 538
Cdd:cd19481 1 LKASLREAVEAPRRGSRLRRYGLGlpkGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYV---------GESE 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499189693 539 FDQGGLLTDAVAKNPhAVLLLDEIEKAHPD------------VYNIFLQLMDHGTLTDhagkkvdgrGLILIFTTN 602
Cdd:cd19481 72 KNLRKIFERARRLAP-CILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAATN 137
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
13-63 |
1.48e-10 |
|
Clp amino terminal domain, pathogenicity island component; This short domain is found in one or two copies at the amino terminus of ClpA and ClpB proteins from bacteria and eukaryotes. The function of these domains is uncertain but they may form a protein binding site. In many bacterial species, including E.coli, this region represents the N-terminus of one of the key components of the pathogenicity island complex that injects toxin from one bacterium into another.
Pssm-ID: 460724 [Multi-domain] Cd Length: 53 Bit Score: 56.76 E-value: 1.48e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 499189693 13 AADLAQAAGHEYITQEHLLLALLGDPE--AKDALNALGADLNALREALTEQLA 63
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDglAARLLKKAGVDLDALREAIEKLLG 53
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
486-602 |
1.86e-10 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 59.23 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 486 SFLFAGPTGVGKTELARALAERLG-----VELIRFDMSEyqephtvARLIGappGYVGFDQGGLLTDAV----AKNPHaV 556
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSnrpvfYVQLTRDTTE-------EDLFG---RRNIDPGGASWVDGPlvraAREGE-I 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 499189693 557 LLLDEIEKAHPDVYNIFLQLMDHGTLTDHAGK---KVDGRGLILIFTTN 602
Cdd:pfam07728 70 AVLDEINRANPDVLNSLLSLLDERRLLLPDGGelvKAAPDGFRLIATMN 118
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
483-602 |
2.15e-10 |
|
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: 59.69 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 483 PQGSFLFAGPTGVGKTELARALAERLGVE---LIRFDMSEYQEPHTVARLIGAPPGYVGFDQGG----LLTDAVAKNPHA 555
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVLDQLLLIIVGGKKASGSGElrlrLALALARKLKPD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 499189693 556 VLLLDEIEKAHPDVYNIFLQLMDHGTLTDHAGKKvdgRGLILIFTTN 602
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSE---KNLTVILTTN 124
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
116-358 |
6.32e-10 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 61.18 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 116 PARAALEAQGVTRLDLLNYLSHGVAKAPGHSRERRVAGVDGELTAEGAPAEENPLEAYAQNLTEAAkNGEFDPVIGRGAE 195
Cdd:COG1222 8 DENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESP-DVTFDDIGGLDEQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 196 LERVV----------HILARRGKNNP---VLVGEPGVGKTALAEGLAQRVadgkapgflrGASVYALDLGALLagTRYRG 262
Cdd:COG1222 87 IEEIReavelplknpELFRKYGIEPPkgvLLYGPPGTGKTLLAKAVAGEL----------GAPFIRVRGSELV--SKYIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 263 DFEGRLKAVL-AALDGQNSVLFIDELHTlVGAGATEGGSVDAANLLKPAL--------ARGKLRVMGAT-TPAELrllek 332
Cdd:COG1222 155 EGARNVREVFeLAREKAPSIIFIDEIDA-IAARRTDDGTSGEVQRTVNQLlaeldgfeSRGDVLIIAATnRPDLL----- 228
|
250 260
....*....|....*....|....*....
gi 499189693 333 DRALWR--RF-QTVDVPEPSEADAVQILQ 358
Cdd:COG1222 229 DPALLRpgRFdRVIEVPLPDEEAREEILK 257
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
213-358 |
4.09e-09 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 57.97 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 213 LVGEPGVGKTALAEGLAQRVadgKAPgflrgasVYALDLGALLagTRYRGDFEGRLKAVLAALDGQNSVLFIDELHTLvg 292
Cdd:COG1223 40 FYGPPGTGKTMLAEALAGEL---KLP-------LLTVRLDSLI--GSYLGETARNLRKLFDFARRAPCVIFFDEFDAI-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 293 agateGGSVDAANLlkpalaRGKLR------------------VMGATTPAELrLlekDRALWRRFQTV-DVPEPSEADA 353
Cdd:COG1223 106 -----AKDRGDQND------VGEVKrvvnallqeldglpsgsvVIAATNHPEL-L---DSALWRRFDEViEFPLPDKEER 170
|
....*
gi 499189693 354 VQILQ 358
Cdd:COG1223 171 KEILE 175
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
192-343 |
1.29e-08 |
|
proteases similar to RecA; 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: 410889 [Multi-domain] Cd Length: 158 Bit Score: 54.60 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 192 RGAELERVVHILARRGKNNP---VLVGEPGVGKTALAEGLAqrvadgkapGFLrGASVYALDLGALLagTRYRGDFEGRL 268
Cdd:cd19481 7 EAVEAPRRGSRLRRYGLGLPkgiLLYGPPGTGKTLLAKALA---------GEL-GLPLIVVKLSSLL--SKYVGESEKNL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 269 KAVLA-ALDGQNSVLFIDELHTLVGAGATEGGSVDAA-------NLLKPALARGKLRVMGATTpaelRLLEKDRALWR-- 338
Cdd:cd19481 75 RKIFErARRLAPCILFIDEIDAIGRKRDSSGESGELRrvlnqllTELDGVNSRSKVLVIAATN----RPDLLDPALLRpg 150
|
....*
gi 499189693 339 RFQTV 343
Cdd:cd19481 151 RFDEV 155
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
293-602 |
5.51e-08 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 55.69 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 293 AGATEGGSVDAANLLKPALARGKLRVMGATTPAELRLLEKDRALWRRFQTVDVPEPSEADAVQILQGLAPKYAAHHGVTY 372
Cdd:COG0464 1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 373 TPPALEAAVRLSARYLRDRFLpdkaIDVLDEAGAARSSTGQGGEIDVPDIESTVARMARVPVGAVKAEEVQSLATLEADL 452
Cdd:COG0464 81 LLAALLSALELLLLGELLLLL----LLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 453 NRrVYGQEPAVSAVSSAVKLARAGLRNPQK----PQGSFLFAGPTGVGKTELARALAERLGVELIRFDMSEyqephtvar 528
Cdd:COG0464 157 DD-LGGLEEVKEELRELVALPLKRPELREEyglpPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSD--------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 529 LIGappGYVG---------FDQgglltdaVAKNPHAVLLLDEIEKAHPD-----------VYNIFLQLMDHgtltdhagk 588
Cdd:COG0464 227 LVS---KYVGeteknlrevFDK-------ARGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEE--------- 287
|
330
....*....|....
gi 499189693 589 kvDGRGLILIFTTN 602
Cdd:COG0464 288 --LRSDVVVIAATN 299
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
212-513 |
8.70e-08 |
|
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.
Pssm-ID: 273521 [Multi-domain] Cd Length: 733 Bit Score: 55.68 E-value: 8.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 212 VLVGEPGVGKTALAEGLAQRVadgkapgflrGASVYALDLGALLagTRYRGDFEGRLKAVLA-ALDGQNSVLFIDELHTL 290
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANEA----------GAYFISINGPEIM--SKYYGESEERLREIFKeAEENAPSIIFIDEIDAI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 291 VGAGATEGGSVDAA------NLLKPALARGKLRVMGATT------PA-----------ELRLLEKD-RALWRRFQTVDVP 346
Cdd:TIGR01243 284 APKREEVTGEVEKRvvaqllTLMDGLKGRGRVIVIGATNrpdaldPAlrrpgrfdreiVIRVPDKRaRKEILKVHTRNMP 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 347 EPSEADavqiLQGLAPKYAAHHGVTYTPPALEAAVRLsaryLRdRFLPDKAID---------VLDEAGAARSSTGQGgei 417
Cdd:TIGR01243 364 LAEDVD----LDKLAEVTHGFVGADLAALAKEAAMAA----LR-RFIREGKINfeaeeipaeVLKELKVTMKDFMEA--- 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 418 dVPDIESTVARMARVPVGAVKAEEVQSLATLEADLNRRVygqEPAVSAVSSAVKLaraGLRnpqKPQGSFLFaGPTGVGK 497
Cdd:TIGR01243 432 -LKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAV---EWPLKHPEIFEKM---GIR---PPKGVLLF-GPPGTGK 500
|
330
....*....|....*.
gi 499189693 498 TELARALAERLGVELI 513
Cdd:TIGR01243 501 TLLAKAVATESGANFI 516
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
450-564 |
1.88e-07 |
|
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410906 [Multi-domain] Cd Length: 183 Bit Score: 52.00 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 450 ADLNRRVYGQEPAVSAVSSAVK------LARAGLRNPQKPQgSFLFAGPTGVGKTELARALAERLGVELIRFDMSEYQEp 523
Cdd:cd19498 7 SELDKYIIGQDEAKRAVAIALRnrwrrmQLPEELRDEVTPK-NILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTE- 84
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 499189693 524 htvarligapPGYVGFDQGGLLTDAVaknpHAVLLLDEIEK 564
Cdd:cd19498 85 ----------VGYVGRDVESIIRDLV----EGIVFIDEIDK 111
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
208-343 |
9.27e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.91 E-value: 9.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 208 KNNPVLVGEPGVGKTALAEGLAQRVADGKAPGFL-----RGASVYALDLGALLAGTRYRGDFEGRLKAVLA-ALDGQNSV 281
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALAlARKLKPDV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499189693 282 LFIDELHTLVGAGATEGGSVDA-ANLLKPALARGKLRVMGATTPaelRLLEKDRALWRRFQTV 343
Cdd:smart00382 82 LILDEITSLLDAEQEALLLLLEeLRLLLLLKSEKNLTVILTTND---EKDLGPALLRRRFDRR 141
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
488-564 |
1.74e-06 |
|
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410908 [Multi-domain] Cd Length: 182 Bit Score: 49.09 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 488 LFAGPTGVGKTELARALAERLGVELIRF------DMSE-------YqephtvarlIGAPPGYVgfDQGglLTDAVAKNPh 554
Cdd:cd19500 41 CLVGPPGVGKTSLGKSIARALGRKFVRIslggvrDEAEirghrrtY---------VGAMPGRI--IQA--LKKAGTNNP- 106
|
90
....*....|
gi 499189693 555 aVLLLDEIEK 564
Cdd:cd19500 107 -VFLLDEIDK 115
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
456-578 |
4.47e-06 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 48.73 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 456 VYGQEPAVSAVSSAVK-------LARAGLRNPQKpqgsFLFAGPTGVGKTELARALAERLGVELIRFDMSEyqephtvar 528
Cdd:COG1223 4 VVGQEEAKKKLKLIIKelrrrenLRKFGLWPPRK----ILFYGPPGTGKTMLAEALAGELKLPLLTVRLDS--------- 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499189693 529 LIGAppgYVGFDQGGL--LTDAVAKNPhAVLLLDEIE---------KAHPD---VYNIFLQLMD 578
Cdd:COG1223 71 LIGS---YLGETARNLrkLFDFARRAP-CVIFFDEFDaiakdrgdqNDVGEvkrVVNALLQELD 130
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
484-578 |
6.27e-06 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 46.18 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 484 QGSFLFAGPTGVGKTELARALAERL---GVELIRFDMSEYQEP----HTVARLIGAPPGYvGFDQGGLLT----DAVAKN 552
Cdd:pfam13401 5 AGILVLTGESGTGKTTLLRRLLEQLpevRDSVVFVDLPSGTSPkdllRALLRALGLPLSG-RLSKEELLAalqqLLLALA 83
|
90 100
....*....|....*....|....*.
gi 499189693 553 PHAVLLLDEIEKAHPDVYNIFLQLMD 578
Cdd:pfam13401 84 VAVVLIIDEAQHLSLEALEELRDLLN 109
|
|
| PRK14953 |
PRK14953 |
DNA polymerase III subunits gamma and tau; Provisional |
454-508 |
1.68e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237867 [Multi-domain] Cd Length: 486 Bit Score: 47.90 E-value: 1.68e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 499189693 454 RRVYGQEPAVSAVSSAVKLaraglrnpQKPQGSFLFAGPTGVGKTELARALAERL 508
Cdd:PRK14953 16 KEVIGQEIVVRILKNAVKL--------QRVSHAYIFAGPRGTGKTTIARILAKVL 62
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
444-583 |
3.88e-05 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 46.31 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 444 SLATLEADLNRRVYGQEPAVSAVSSAVkLARaglrnpqkpqGSFLFAGPTGVGKTELARALAERLGVELIRF----DMse 519
Cdd:COG0714 2 TEARLRAEIGKVYVGQEELIELVLIAL-LAG----------GHLLLEGVPGVGKTTLAKALARALGLPFIRIqftpDL-- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499189693 520 yqephTVARLIG---APPGYVGF--DQGGLLTdavaknphAVLLLDEIEKAHPDVYNIFLQLMDHGTLT 583
Cdd:COG0714 69 -----LPSDILGtyiYDQQTGEFefRPGPLFA--------NVLLADEINRAPPKTQSALLEAMEERQVT 124
|
|
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
481-564 |
4.62e-05 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 46.93 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 481 QKPQGSFL-FAGPTGVGKTELARALAERLGVELIRF------DMSE-------YqephtvarlIGAPPGyvGFDQGglLT 546
Cdd:COG0466 348 KKLKGPILcLVGPPGVGKTSLGKSIARALGRKFVRIslggvrDEAEirghrrtY---------IGAMPG--RIIQG--LK 414
|
90
....*....|....*...
gi 499189693 547 DAVAKNPhaVLLLDEIEK 564
Cdd:COG0466 415 KAGTKNP--VFLLDEIDK 430
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
188-299 |
8.88e-05 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 43.65 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 188 PVIGRGAELERVVHILARRGKNNP---VLVGEPGVGKTALAEGLAQRVADGKApGFLRGASVYALDLGALLAGTryrgDF 264
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERDGG-YFLRGKCDENLPYSPLLEAL----TR 75
|
90 100 110
....*....|....*....|....*....|....*
gi 499189693 265 EGRLKAVLAALDGQNSVLFIDELHTLVGAGATEGG 299
Cdd:pfam13191 76 EGLLRQLLDELESSLLEAWRAALLEALAPVPELPG 110
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
471-563 |
1.78e-04 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 44.23 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 471 KLARAGLRNPQKpqgsFLFAGPTGVGKTELARALAERLGVELIRFDMSEYQEPhtvarligappgYVGfdQGG-----LL 545
Cdd:COG1222 103 LFRKYGIEPPKG----VLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK------------YIG--EGArnvreVF 164
|
90
....*....|....*...
gi 499189693 546 TDAVAKNPhAVLLLDEIE 563
Cdd:COG1222 165 ELAREKAP-SIIFIDEID 181
|
|
| MiaA |
COG0324 |
tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; ... |
490-513 |
2.60e-04 |
|
tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; tRNA A37 N6-isopentenylltransferase MiaA is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440093 Cd Length: 306 Bit Score: 43.51 E-value: 2.60e-04
10 20
....*....|....*....|....
gi 499189693 490 AGPTGVGKTELARALAERLGVELI 513
Cdd:COG0324 8 VGPTASGKTALAIELAKRLGGEII 31
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
456-505 |
2.67e-04 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 43.64 E-value: 2.67e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 499189693 456 VYGQEPAVSAVSSAVKLAR---AglrnpqkpqgsFLFAGPTGVGKTELARALA 505
Cdd:COG2812 12 VVGQEHVVRTLKNALASGRlahA-----------YLFTGPRGVGKTTLARILA 53
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
213-322 |
2.72e-04 |
|
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410911 [Multi-domain] Cd Length: 165 Bit Score: 42.28 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 213 LVGEPGVGKTALAEGLAQRVadgkapgflrGASVYALDLGALLAGtrYRGDFEGRLKAVLA-ALDGQNSVLFIDELHTLV 291
Cdd:cd19503 39 LHGPPGTGKTLLARAVANEA----------GANFLSISGPSIVSK--YLGESEKNLREIFEeARSHAPSIIFIDEIDALA 106
|
90 100 110
....*....|....*....|....*....|....*..
gi 499189693 292 GAGATEGGSVDAA------NLLKPALARGKLRVMGAT 322
Cdd:cd19503 107 PKREEDQREVERRvvaqllTLMDGMSSRGKVVVIAAT 143
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
212-341 |
3.03e-04 |
|
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410917 [Multi-domain] Cd Length: 163 Bit Score: 41.95 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 212 VLVGEPGVGKTALAEGLAQRVadgkapgflrGASVYALDLGALLAgtRYRGDFEGRLKAVLA-ALDGQNSVLFIDELHTL 290
Cdd:cd19509 36 LLYGPPGTGKTLLARAVASES----------GSTFFSISASSLVS--KWVGESEKIVRALFAlARELQPSIIFIDEIDSL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 291 VGA-GATEGGSVD--AANLLK-----PALARGKLRVMGATT-PAELrllekDRALWRRFQ 341
Cdd:cd19509 104 LSErGSGEHEASRrvKTEFLVqmdgvLNKPEDRVLVLGATNrPWEL-----DEAFLRRFE 158
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
212-340 |
3.79e-04 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 41.12 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 212 VLVGEPGVGKTALAEGLAQRvadgkapgfLRGASVYALDLGA------LLAGTRYRGDFEGRLKAVL--AALDGQnsVLF 283
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAA---------LSNRPVFYVQLTRdtteedLFGRRNIDPGGASWVDGPLvrAAREGE--IAV 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499189693 284 IDELHTlvgagategGSVDAANLLKPALARGKL----------------RVMGATTPAELRLLEKDRALWRRF 340
Cdd:pfam07728 72 LDEINR---------ANPDVLNSLLSLLDERRLllpdggelvkaapdgfRLIATMNPLDRGLNELSPALRSRF 135
|
|
| PRK14956 |
PRK14956 |
DNA polymerase III subunits gamma and tau; Provisional |
454-511 |
5.84e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184920 [Multi-domain] Cd Length: 484 Bit Score: 43.01 E-value: 5.84e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 499189693 454 RRVYGQEPAVSAVSSAVKLARAGlrnpqkpqGSFLFAGPTGVGKTELARALAERLGVE 511
Cdd:PRK14956 18 RDVIHQDLAIGALQNALKSGKIG--------HAYIFFGPRGVGKTTIARILAKRLNCE 67
|
|
| IS21_help_AAA |
NF038214 |
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ... |
206-287 |
1.02e-03 |
|
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.
Pssm-ID: 439516 Cd Length: 232 Bit Score: 41.30 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 206 RGKNNPVLVGEPGVGKTALAEGLAQRVADgkapgflRGASVY---ALDLGALLAgtryRGDFEGRLKAVLAALDGqNSVL 282
Cdd:NF038214 88 ERAENVLLLGPPGTGKTHLAIALGYAACR-------QGYRVRfttAADLVEQLA----QARADGRLGRLLRRLAR-YDLL 155
|
....*
gi 499189693 283 FIDEL 287
Cdd:NF038214 156 IIDEL 160
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
487-516 |
1.12e-03 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 40.28 E-value: 1.12e-03
10 20 30
....*....|....*....|....*....|
gi 499189693 487 FLFAGPTGVGKTELARALAERLGVELIRFD 516
Cdd:COG0645 2 ILVCGLPGSGKSTLARALAERLGAVRLRSD 31
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
456-513 |
2.09e-03 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 41.44 E-value: 2.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 499189693 456 VYGQEPAVSAVSSAVKLARAGlrNPQKPqgsFLFAGPTGVGKTELARALAERLGVELI 513
Cdd:PRK04195 16 VVGNEKAKEQLREWIESWLKG--KPKKA---LLLYGPPGVGKTSLAHALANDYGWEVI 68
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
215-432 |
2.17e-03 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 41.22 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 215 GEPGVGKTALAEGLAQRVadgkapgflrGASVYALDlgALLAGTRyrgdfegRLKAVLAA-----LDGQNSVLFIDELHT 289
Cdd:PRK13342 43 GPPGTGKTTLARIIAGAT----------DAPFEALS--AVTSGVK-------DLREVIEEarqrrSAGRRTILFIDEIHR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 290 LvgagateggsvdaaN------LLkPALARGKLRVMGATT--------PAelrLLEkdRALWRRFQTVdvpepSEADAVQ 355
Cdd:PRK13342 104 F--------------NkaqqdaLL-PHVEDGTITLIGATTenpsfevnPA---LLS--RAQVFELKPL-----SEEDIEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 356 ILQglapKYAAHHG---VTYTPPALEAAVRLS---ARylrdrflpdKAIDVLDEAGAArsstgqGGEIDVPDIESTVARM 429
Cdd:PRK13342 159 LLK----RALEDKErglVELDDEALDALARLAngdAR---------RALNLLELAALG------VDSITLELLEEALQKR 219
|
...
gi 499189693 430 ARV 432
Cdd:PRK13342 220 AAR 222
|
|
| PRK06547 |
PRK06547 |
hypothetical protein; Provisional |
488-516 |
3.04e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235825 Cd Length: 172 Bit Score: 39.34 E-value: 3.04e-03
10 20
....*....|....*....|....*....
gi 499189693 488 LFAGPTGVGKTELARALAERLGVELIRFD 516
Cdd:PRK06547 19 LIDGRSGSGKTTLAGALAARTGFQLVHLD 47
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
452-564 |
3.06e-03 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410905 [Multi-domain] Cd Length: 251 Bit Score: 39.89 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 452 LNRRVYGQEPAVSAVSSAV----KLARAGLRNPQK----PQGSFLFAGPTGVGKTELARALAERLGVelirfdmseyqeP 523
Cdd:cd19497 10 LDKYVIGQERAKKVLSVAVynhyKRIRNNLKQKDDdvelEKSNILLIGPTGSGKTLLAQTLAKILDV------------P 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 499189693 524 HTVA---RLIGAppGYVGFDQGG----LLTDA---VAKNPHAVLLLDEIEK 564
Cdd:cd19497 78 FAIAdatTLTEA--GYVGEDVENillkLLQAAdydVERAQRGIVYIDEIDK 126
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
423-569 |
3.29e-03 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 41.08 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 423 ESTVAR-----MARVPVGA---VKAEEVQSLATLEADLN--RRVYGQEPAVSAVSSAVklaraglrnpQKPQGSFL-FAG 491
Cdd:PRK10787 287 EATVVRgyidwMVQVPWNArskVKKDLRQAQEILDTDHYglERVKDRILEYLAVQSRV----------NKIKGPILcLVG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 492 PTGVGKTELARALAERLGVELIRFDMSEYQEPhtvARLIGAPPGYVGFDQGGLLTDAV---AKNPhaVLLLDEIEKAHPD 568
Cdd:PRK10787 357 PPGVGKTSLGQSIAKATGRKYVRMALGGVRDE---AEIRGHRRTYIGSMPGKLIQKMAkvgVKNP--LFLLDEIDKMSSD 431
|
.
gi 499189693 569 V 569
Cdd:PRK10787 432 M 432
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
212-290 |
4.30e-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: 39.77 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 212 VLVGEPGVGKTALAEGLAQRVADGKAPGFLRGASVYALDLGALLA-------GTRYRGDFEGRLKAVLAAL--DGQNSVL 282
Cdd:COG3267 47 VLTGEVGTGKTTLLRRLLERLPDDVKVAYIPNPQLSPAELLRAIAdelglepKGASKADLLRQLQEFLLELaaAGRRVVL 126
|
....*...
gi 499189693 283 FIDELHTL 290
Cdd:COG3267 127 IIDEAQNL 134
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
482-620 |
4.32e-03 |
|
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410926 [Multi-domain] Cd Length: 169 Bit Score: 38.54 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 482 KPQGSFLFAGPTGVGKTELARALAERLGVELIRFDMSEyqephtvarLIGAPPGYVGFDQGGLLTDAVAKNPhAVLLLDE 561
Cdd:cd19518 32 EPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATE---------IVSGVSGESEEKIRELFDQAISNAP-CIVFIDE 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 562 IEKAHPD-----------VYNIFLQLMDHGTLtdhagKKVDGRGLILIFTTNagAADASRPALgfSREGR 620
Cdd:cd19518 102 IDAITPKresaqremerrIVSQLLTCMDELNN-----EKTAGGPVLVIGATN--RPDSLDPAL--RRAGR 162
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
477-513 |
4.66e-03 |
|
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410911 [Multi-domain] Cd Length: 165 Bit Score: 38.43 E-value: 4.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 499189693 477 LRNPQ-------KPQGSFLFAGPTGVGKTELARALAERLGVELI 513
Cdd:cd19503 20 LKYPElfralglKPPRGVLLHGPPGTGKTLLARAVANEAGANFL 63
|
|
| hslU |
PRK05201 |
ATP-dependent protease ATPase subunit HslU; |
491-540 |
4.80e-03 |
|
ATP-dependent protease ATPase subunit HslU;
Pssm-ID: 235364 [Multi-domain] Cd Length: 443 Bit Score: 40.06 E-value: 4.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499189693 491 GPTGVGKTELARalaeRLgvelirfdmseyqephtvARLIGAP-----------PGYVGFD 540
Cdd:PRK05201 57 GPTGVGKTEIAR----RL------------------AKLANAPfikveatkfteVGYVGRD 95
|
|
| HslU |
COG1220 |
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ... |
491-540 |
4.92e-03 |
|
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440833 [Multi-domain] Cd Length: 454 Bit Score: 40.03 E-value: 4.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499189693 491 GPTGVGKTELARalaeRLgvelirfdmseyqephtvARLIGAP-----------PGYVGFD 540
Cdd:COG1220 57 GPTGVGKTEIAR----RL------------------AKLANAPfikveatkfteVGYVGRD 95
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
485-515 |
5.06e-03 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 40.07 E-value: 5.06e-03
10 20 30
....*....|....*....|....*....|.
gi 499189693 485 GSFLFAGPTGVGKTELARALAERLGVELIRF 515
Cdd:PRK13342 37 SSMILWGPPGTGKTTLARIIAGATDAPFEAL 67
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
215-431 |
6.85e-03 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 39.65 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 215 GEPGVGKTALAEGLAQRVadgkapgflrGASVYALDlgALLAGTRyrgdfegRLKAVLAA-----LDGQNSVLFIDELHT 289
Cdd:COG2256 56 GPPGTGKTTLARLIANAT----------DAEFVALS--AVTSGVK-------DIREVIEEarerrAYGRRTILFVDEIHR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 290 LvgagateggsvdaaN------LLkPALARGKLRVMGATT--------PA--------ELRLLEKD--RALWRRfqtvdv 345
Cdd:COG2256 117 F--------------NkaqqdaLL-PHVEDGTITLIGATTenpsfevnSAllsrcrvfVLKPLSEEdlEQLLER------ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 346 pepSEADAVQILQGLApkyaahhgVTYTPPALEAAVRLS---ARylrdrflpdKAIDVLDEAGAARSSTGQgGEIDVPDI 422
Cdd:COG2256 176 ---ALADDERGLGGYK--------LELDDEALEALARLAdgdAR---------RALNALELAVLSAPPDGV-IEITLELV 234
|
....*....
gi 499189693 423 ESTVARMAR 431
Cdd:COG2256 235 EEALQRRAL 243
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
488-517 |
8.50e-03 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 37.02 E-value: 8.50e-03
10 20 30
....*....|....*....|....*....|
gi 499189693 488 LFAGPTGVGKTELARALAERLGVELIRFDM 517
Cdd:pfam13238 2 LITGTPGVGKTTLAKELSKRLGFGDNVRDL 31
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
204-290 |
9.63e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 36.94 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 204 ARRGKNNPVLVGEPGVGKTALAEGLAQRVADGK-------APGFLRGASVYALDLGALLAGTRYRGDFEGRLKAVLAALD 276
Cdd:pfam13401 1 IRFGAGILVLTGESGTGKTTLLRRLLEQLPEVRdsvvfvdLPSGTSPKDLLRALLRALGLPLSGRLSKEELLAALQQLLL 80
|
90
....*....|....*.
gi 499189693 277 GQNS--VLFIDELHTL 290
Cdd:pfam13401 81 ALAVavVLIIDEAQHL 96
|
|
| IstB_IS21 |
pfam01695 |
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is ... |
185-287 |
9.95e-03 |
|
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is found associated with IS21 family insertion sequences. The function of this protein is unknown, but it may perform a transposase function.
Pssm-ID: 426385 [Multi-domain] Cd Length: 238 Bit Score: 38.20 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189693 185 EFDPVIGRGAElERVVHILAR----RGKNNPVLVGEPGVGKTALAEGLAQRvadgkapGFLRGASVY---ALDLGALLAG 257
Cdd:pfam01695 66 DFDFTFAPGLD-QRIVAELASlsfiDRAQNVVLLGPPGVGKTHLAIALGVE-------ACRAGYSVRftsAADLVNQLKR 137
|
90 100 110
....*....|....*....|....*....|
gi 499189693 258 TRYRGDFEGRLKAVLAAldgqnSVLFIDEL 287
Cdd:pfam01695 138 AHGDGKLTRKLQQLLKP-----DVLILDEW 162
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|
| |
