|
Name |
Accession |
Description |
Interval |
E-value |
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
1-754 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 1162.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 1 MLNRELEVTLNLAFKEARSKRHEFMTVEHLLLALLDNEAAATVLRACGANLDKLKHDLQEFIDSTTPLIPVHDEDRETQP 80
Cdd:PRK11034 1 MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 81 TLGFQRVLQRAVFHVQSSGKREVTGANVLVAIFSEQESQAVFLLKQQSVARIDVVNYIAHGISKVPGHGDQSEGEqdmqD 160
Cdd:PRK11034 81 TLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPSQSSDPGS----Q 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 161 DEGGESSSSGNPLDAYASNLNELARQGRIDPLVGREMEVERVAQILARRRKNNPLLVGEAGVGKTAIAEGLAKRIVDNQV 240
Cdd:PRK11034 157 PNSEEQAGGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 241 PDLLANSVVYSLDLGALLAGTKYRGDFEKRFKALLGELKKRPHAILFIDEIHTIIGAGAASGGVMDASNLLKPLLSSGDI 320
Cdd:PRK11034 237 PEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 321 RCIGSTTFQEFRGIFEKDRALARRFQKVDVSEPSVEDTIGILRGLKGRFEQHHNIEYSDEALRAAAELASRYINDRHMPD 400
Cdd:PRK11034 317 RVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 401 KAIDVIDEAGAYQRLQPVEMRVKRIEVPQVEDIVAKIARIPPKHVNSSDKELLRNLERDLKLTVFGQDAAIDSLSTAIKL 480
Cdd:PRK11034 397 KAIDVIDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKM 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 481 SRAGLKSPDKPVGSFLFAGPTGVGKTEAARQLAKALGIELVRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTEAVTKQ 560
Cdd:PRK11034 477 SRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKH 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 561 PHCVLLLDEIEKAHPEVFNLLLQVMDHGTLTDNNGRKADFRNVIVIMTTNAGAETAARASIGFTHQDHSSDAMEVIKKSF 640
Cdd:PRK11034 557 PHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMEEIKKIF 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 641 TPEFRNRLDTIIQFGRLSHEVIKNVVDKFLTELQAQLEDKRVLLEVTDAVRGYLAEEGYDAAMGARPMARLIQEKIKRPL 720
Cdd:PRK11034 637 TPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPL 716
|
730 740 750
....*....|....*....|....*....|....
gi 1598135533 721 AEEILFGELSeHGGVVHIDFKDGEITFEYETTAE 754
Cdd:PRK11034 717 ANELLFGSLV-DGGQVTVALDKEKNELTYGFQSA 749
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
2-739 |
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: 1112.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 2 LNRELEVTLNLAFKEARSKRHEFMTVEHLLLALLDNEAAATVLRACGANLDKLKHDLQEFIDSTTPLIPvHDEDRETQPT 81
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAIEILEECGGDVELLRKRLEDYLEENLPVIP-EDIDEEPEQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 82 LGFQRVLQRAVFHVQSSGKREVTGANVLVAIFSEQESQAVFLLKQQSVARIDVVNYIAHGISKVPGhgDQSEGEQDMQDD 161
Cdd:TIGR02639 80 VGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITRLDILNYISHGISKDDG--KDQLGEEAGKEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 162 EGGESsssgnPLDAYASNLNELARQGRIDPLVGREMEVERVAQILARRRKNNPLLVGEAGVGKTAIAEGLAKRIVDNQVP 241
Cdd:TIGR02639 158 EKGQD-----ALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 242 DLLANSVVYSLDLGALLAGTKYRGDFEKRFKALLGELKKRPHAILFIDEIHTIIGAGAASGGVMDASNLLKPLLSSGDIR 321
Cdd:TIGR02639 233 ERLKNAKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFIDEIHTIVGAGATSGGSMDASNLLKPALSSGKIR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 322 CIGSTTFQEFRGIFEKDRALARRFQKVDVSEPSVEDTIGILRGLKGRFEQHHNIEYSDEALRAAAELASRYINDRHMPDK 401
Cdd:TIGR02639 313 CIGSTTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 402 AIDVIDEAGAYQRLQPVEMRVKRIEVPQVEDIVAKIARIPPKHVNSSDKELLRNLERDLKLTVFGQDAAIDSLSTAIKLS 481
Cdd:TIGR02639 393 AIDVIDEAGAAFRLRPKAKKKANVNVKDIENVVAKMAKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRS 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 482 RAGLKSPDKPVGSFLFAGPTGVGKTEAARQLAKALGIELVRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTEAVTKQP 561
Cdd:TIGR02639 473 RAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEELGVHLLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHP 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 562 HCVLLLDEIEKAHPEVFNLLLQVMDHGTLTDNNGRKADFRNVIVIMTTNAGAETAARASIGFTHQDHSSDAMEVIKKSFT 641
Cdd:TIGR02639 553 HCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTSNAGASEMSKPPIGFGGENRESKSLKAIKKLFS 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 642 PEFRNRLDTIIQFGRLSHEVIKNVVDKFLTELQAQLEDKRVLLEVTDAVRGYLAEEGYDAAMGARPMARLIQEKIKRPLA 721
Cdd:TIGR02639 633 PEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLS 712
|
730
....*....|....*...
gi 1598135533 722 EEILFGELSEhGGVVHID 739
Cdd:TIGR02639 713 DEILFGKLKK-GGSVKIS 729
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2-746 |
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: 850.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 2 LNRELEVTLNLAFKEARSKRHEFMTVEHLLLALLDNE--AAATVLRACGANLDKLKHDLQEFIDSttpLIPVHDEDRETQ 79
Cdd:COG0542 6 FTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGegLAAKLLRKLGVDLDALREELEEALGR---LPKVSGSSGQPY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 80 PTLGFQRVLQRAVFHVQSSGKREVTGANVLVAIFSEQESQAVFLLKQQSVARIDVvnyiAHGISKVPGHgdqsegeqdmQ 159
Cdd:COG0542 83 LSPRLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITLEAL----REALEELRGG----------S 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 160 DDEGGESSSSGNPLDAYASNLNELARQGRIDPLVGREMEVERVAQILARRRKNNPLLVGEAGVGKTAIAEGLAKRIVDNQ 239
Cdd:COG0542 149 RVTSQNPESKTPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 240 VPDLLANSVVYSLDLGALLAGTKYRGDFEKRFKALLGELKKRPH-AILFIDEIHTIIGAGAASGGvMDASNLLKPLLSSG 318
Cdd:COG0542 229 VPESLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKSEGnIILFIDELHTLVGAGGAEGA-MDAANLLKPALARG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 319 DIRCIGSTTFQEFRGIFEKDRALARRFQKVDVSEPSVEDTIGILRGLKGRFEQHHNIEYSDEALRAAAELASRYINDRHM 398
Cdd:COG0542 308 ELRCIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 399 PDKAIDVIDEAGAYQRLQ----PVEMRVKRIEVPQVE------------------------------------------- 431
Cdd:COG0542 388 PDKAIDLIDEAAARVRMEidskPEELDELERRLEQLEiekealkkeqdeasferlaelrdelaeleeelealkarweaek 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 432 ---------------------------------------------------DIVAKIARIPPKHVNSSDKELLRNLERDL 460
Cdd:COG0542 468 elieeiqelkeeleqrygkipelekelaeleeelaelapllreevteediaEVVSRWTGIPVGKLLEGEREKLLNLEEEL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 461 KLTVFGQDAAIDSLSTAIKLSRAGLKSPDKPVGSFLFAGPTGVGKTEAARQLAKAL-GIE--LVRFDMSEYMERHTVSRL 537
Cdd:COG0542 548 HERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLfGDEdaLIRIDMSEYMEKHSVSRL 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 538 IGAPPGYVGFDQGGLLTEAVTKQPHCVLLLDEIEKAHPEVFNLLLQVMDHGTLTDNNGRKADFRNVIVIMTTNAGAET-A 616
Cdd:COG0542 628 IGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIGSELiL 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 617 ARASIGFTHQDHSSDAMEVIKKSFTPEFRNRLDTIIQFGRLSHEVIKNVVDKFLTELQAQLEDKRVLLEVTDAVRGYLAE 696
Cdd:COG0542 708 DLAEDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAAKDFLAE 787
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 1598135533 697 EGYDAAMGARPMARLIQEKIKRPLAEEILFGELSEhGGVVHIDFKDGEIT 746
Cdd:COG0542 788 KGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKE-GDTITVDVDDGELV 836
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
10-746 |
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: 701.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 10 LNLAFKEARSKRHEFMTVEHLLLALLDNEA--AATVLRACGANLDKLKHDLQEFIDSttpLIPVHDEDRETQPTLGFQRV 87
Cdd:TIGR03346 9 LQAAQSLALGRDHQQIEPEHLLKALLDQEGglARPLLQKAGVNVGALRQALEKELER---LPKVSGPGGQVYLSPDLNRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 88 LQRAVFHVQSSGKREVTGANVLVAIFSEQESQAVfLLKQQSVARIDVvnyiahgiskvpghgdqsegEQDMQDDEGGESS 167
Cdd:TIGR03346 86 LNLAEKLAQKRGDEFISSEHLLLALLDDKGTLGK-LLKEAGATADAL--------------------EAAINAVRGGQKV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 168 SSGNP------LDAYASNLNELARQGRIDPLVGREMEVERVAQILARRRKNNPLLVGEAGVGKTAIAEGLAKRIVDNQVP 241
Cdd:TIGR03346 145 TDANAedqyeaLEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 242 DLLANSVVYSLDLGALLAGTKYRGDFEKRFKALLGELKKRP-HAILFIDEIHTIIGAGAAsGGVMDASNLLKPLLSSGDI 320
Cdd:TIGR03346 225 EGLKNKRLLALDMGALIAGAKYRGEFEERLKAVLNEVTKSEgQIILFIDELHTLVGAGKA-EGAMDAGNMLKPALARGEL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 321 RCIGSTTFQEFRGIFEKDRALARRFQKVDVSEPSVEDTIGILRGLKGRFEQHHNIEYSDEALRAAAELASRYINDRHMPD 400
Cdd:TIGR03346 304 HCIGATTLDEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPD 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 401 KAIDVIDEAGAYQRLQ----PVEM---------------------------RVKRIE----------------------- 426
Cdd:TIGR03346 384 KAIDLIDEAAARIRMEidskPEELdeldrriiqleierealkkekdeaskkRLEDLEkeladleeeyaeleeqwkaekas 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 427 -------------------------------------VPQVE----------------------------DIVAKIARIP 441
Cdd:TIGR03346 464 iqgiqqikeeieqvrleleqaeregdlakaaelqygkLPELEkqlqaaeqklgeeqnrllreevtaeeiaEVVSRWTGIP 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 442 PKHVNSSDKELLRNLERDLKLTVFGQDAAIDSLSTAIKLSRAGLKSPDKPVGSFLFAGPTGVGKTEAARQLAKAL---GI 518
Cdd:TIGR03346 544 VSKMLEGEREKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLfdsED 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 519 ELVRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTEAVTKQPHCVLLLDEIEKAHPEVFNLLLQVMDHGTLTDNNGRKA 598
Cdd:TIGR03346 624 AMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTV 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 599 DFRNVIVIMTTNAGAETAARASIGFTHQDHSSDAMEVIKKSFTPEFRNRLDTIIQFGRLSHEVIKNVVDKFLTELQAQLE 678
Cdd:TIGR03346 704 DFRNTVIIMTSNLGSDFIQELAGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLA 783
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1598135533 679 DKRVLLEVTDAVRGYLAEEGYDAAMGARPMARLIQEKIKRPLAEEILFGELsEHGGVVHIDFKDGEIT 746
Cdd:TIGR03346 784 ERKITLELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEV-APGDTIRVDVEGGRLV 850
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
12-725 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 674.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 12 LAFKEARSKRHEFMTVEHLLLALL--DNEAAATVLRACGANLDKLKHDLQE-------FIDSTTPLIPvhdedRETqptl 82
Cdd:CHL00095 15 LSQEEARRLGHNFVGTEQILLGLIgeGTGIAARALKSMGVTLKDARIEVEKiigrgtgFVAVEIPFTP-----RAK---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 83 gfqRVLQRAVFHVQSSGKREVTGANVLVAIFSEQESQAVFLLKQQSVARIDVVNYIAHGIskvpghGDQSEgeqdmqDDE 162
Cdd:CHL00095 86 ---RVLEMSLEEARDLGHNYIGTEHLLLALLEEGEGVAARVLENLGVDLSKIRSLILNLI------GEIIE------AIL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 163 GGESSSSGNP-LDAYASNLNELARQGRIDPLVGREMEVERVAQILARRRKNNPLLVGEAGVGKTAIAEGLAKRIVDNQVP 241
Cdd:CHL00095 151 GAEQSRSKTPtLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 242 DLLANSVVYSLDLGALLAGTKYRGDFEKRFKALLGELKKRPHAILFIDEIHTIIGAGAASGGVmDASNLLKPLLSSGDIR 321
Cdd:CHL00095 231 DILEDKLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAAEGAI-DAANILKPALARGELQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 322 CIGSTTFQEFRGIFEKDRALARRFQKVDVSEPSVEDTIGILRGLKGRFEQHHNIEYSDEALRAAAELASRYINDRHMPDK 401
Cdd:CHL00095 310 CIGATTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 402 AIDVIDEAGAYQRL--------------------------------------QPVEMRVK----------------RIEV 427
Cdd:CHL00095 390 AIDLLDEAGSRVRLinsrlppaareldkelreilkdkdeaireqdfetakqlRDREMEVRaqiaaiiqskkteeekRLEV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 428 PQV--EDIVAKIA---RIPPKHVNSSDKELLRNLERDLKLTVFGQDAAIDSLSTAIKLSRAGLKSPDKPVGSFLFAGPTG 502
Cdd:CHL00095 470 PVVteEDIAEIVSawtGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTG 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 503 VGKTEAARQLAKAL-GIE--LVRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTEAVTKQPHCVLLLDEIEKAHPEVFN 579
Cdd:CHL00095 550 VGKTELTKALASYFfGSEdaMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFN 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 580 LLLQVMDHGTLTDNNGRKADFRNVIVIMTTNAGAETAAR--ASIGFTHQDH----------SSDAMEVIKKSFTPEFRNR 647
Cdd:CHL00095 630 LLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSKVIETnsGGLGFELSENqlsekqykrlSNLVNEELKQFFRPEFLNR 709
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1598135533 648 LDTIIQFGRLSHEVIKNVVDKFLTELQAQLEDKRVLLEVTDAVRGYLAEEGYDAAMGARPMARLIQEKIKRPLAEEIL 725
Cdd:CHL00095 710 LDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVL 787
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
12-746 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 567.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 12 LAFKEARS----KRHEFMTVEHLLLALLDNEAAAT--VLRACGANLDKLKHDLQEFIDSttpLIPVHDEDRETQPTLGFQ 85
Cdd:PRK10865 12 LALADAQSlalgHDNQFIEPLHLMSALLNQEGGSVrpLLTSAGINAGQLRTDINQALSR---LPQVEGTGGDVQPSQDLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 86 RVLQRAVFHVQSSGKREVTGANVLVAIFsEQESQAVFLLKQQSVARidvvNYIAHGISKVPGhgdqseGEQdmQDDEGGE 165
Cdd:PRK10865 89 RVLNLCDKLAQKRGDNFISSELFVLAAL-ESRGTLADILKAAGATT----ANITQAIEQMRG------GES--VNDQGAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 166 SSSSGnpLDAYASNLNELARQGRIDPLVGREMEVERVAQILARRRKNNPLLVGEAGVGKTAIAEGLAKRIVDNQVPDLLA 245
Cdd:PRK10865 156 DQRQA--LKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 246 NSVVYSLDLGALLAGTKYRGDFEKRFKALLGEL-KKRPHAILFIDEIHTIIGAGAASGGvMDASNLLKPLLSSGDIRCIG 324
Cdd:PRK10865 234 GRRVLALDMGALVAGAKYRGEFEERLKGVLNDLaKQEGNVILFIDELHTMVGAGKADGA-MDAGNMLKPALARGELHCVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 325 STTFQEFRGIFEKDRALARRFQKVDVSEPSVEDTIGILRGLKGRFEQHHNIEYSDEALRAAAELASRYINDRHMPDKAID 404
Cdd:PRK10865 313 ATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAID 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 405 VIDEAGAYQRLQ---------PVEMRV-------------------KRIE------------------------------ 426
Cdd:PRK10865 393 LIDEAASSIRMQidskpeeldRLDRRIiqlkleqqalmkesdeaskKRLDmlneelsdkerqyseleeewkaekaslsgt 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 427 ---------------------------------VPQVE---------------------------DIVAKIARIPPKHVN 446
Cdd:PRK10865 473 qtikaeleqakiaieqarrvgdlarmselqygkIPELEkqlaaatqlegktmrllrnkvtdaeiaEVLARWTGIPVSRML 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 447 SSDKELLRNLERDLKLTVFGQDAAIDSLSTAIKLSRAGLKSPDKPVGSFLFAGPTGVGKTEAARQLAKAL---GIELVRF 523
Cdd:PRK10865 553 ESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMfdsDDAMVRI 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 524 DMSEYMERHTVSRLIGAPPGYVGFDQGGLLTEAVTKQPHCVLLLDEIEKAHPEVFNLLLQVMDHGTLTDNNGRKADFRNV 603
Cdd:PRK10865 633 DMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNT 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 604 IVIMTTNAGAETAARASIGFTHQDHSSDAMEVIKKSFTPEFRNRLDTIIQFGRLSHEVIKNVVDKFLTELQAQLEDKRVL 683
Cdd:PRK10865 713 VVIMTSNLGSDLIQERFGELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYE 792
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1598135533 684 LEVTDAVRGYLAEEGYDAAMGARPMARLIQEKIKRPLAEEILFGELSEhGGVVHIDFKDGEIT 746
Cdd:PRK10865 793 IHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVP-GKVIRLEVNDDRIV 854
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
2-725 |
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: 538.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 2 LNRELEVTLNLAFKEARSKRHEFMTVEHLLLALLDNEA--AATVLRACGANLDKLKHDLQEFID------STTPLIPVHd 73
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDsdLAAILRHFGVDLGRLKADLARALDklprgnTRTPVFSPH- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 74 edretqptlgFQRVLQRAvFHVQSS--GKREVTGANVLVAIFSEQESQAVFLLKQQSVARIDVVNYIAHGISKVPGHGDQ 151
Cdd:TIGR03345 80 ----------LVELLQEA-WLLASLelGDGRIRSGHLLLALLTDPELRRLLGSISPELAKIDREALREALPALVEGSAEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 152 SEGEQDMQDDEGGESSSSGNPLDAYASNLNELARQGRIDPLVGREMEVERVAQILARRRKNNPLLVGEAGVGKTAIAEGL 231
Cdd:TIGR03345 149 SAAAADAAPAGAAAGAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 232 AKRIVDNQVPDLLANSVVYSLDLGALLAGTKYRGDFEKRFKALLGELKKRPHA-ILFIDEIHTIIGAGAASGGvMDASNL 310
Cdd:TIGR03345 229 ALRIAAGDVPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPiILFIDEAHTLIGAGGQAGQ-GDAANL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 311 LKPLLSSGDIRCIGSTTFQEFRGIFEKDRALARRFQKVDVSEPSVEDTIGILRGLKGRFEQHHNIEYSDEALRAAAELAS 390
Cdd:TIGR03345 308 LKPALARGELRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSH 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 391 RYINDRHMPDKAIDVIDEAGA----------------YQRLQPVEMRVKRIE---------------------------- 426
Cdd:TIGR03345 388 RYIPGRQLPDKAVSLLDTACArvalsqnatpaaledlRRRIAALELELDALEreaalgadhderlaelraelaaleaela 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 427 ---------------------------------------------------------VP------QVEDIVAKIARIPPK 443
Cdd:TIGR03345 468 alearwqqekelveailalraeleadadapaddddalraqlaeleaalasaqgeeplVFpevdaqAVAEVVADWTGIPVG 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 444 HVNSSDKELLRNLERDLKLTVFGQDAAIDSLSTAIKLSRAGLKSPDKPVGSFLFAGPTGVGKTEAARQLAKAL-GIE--L 520
Cdd:TIGR03345 548 RMVRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLyGGEqnL 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 521 VRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTEAVTKQPHCVLLLDEIEKAHPEVFNLLLQVMDHGTLTDNNGRKADF 600
Cdd:TIGR03345 628 ITINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDF 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 601 RNVIVIMTTNAGAETAARASIGfthQDHSSDAMEVIK-------KSFTPEFRNRLdTIIQFGRLSHEVIKNVVDKFLTEL 673
Cdd:TIGR03345 708 KNTVILLTSNAGSDLIMALCAD---PETAPDPEALLEalrpellKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRI 783
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1598135533 674 QAQLEDK-RVLLEVTDAVRGYLAEEGYDAAMGARPMARLIQEKIKRPLAEEIL 725
Cdd:TIGR03345 784 ARRLKENhGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQIL 836
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
453-654 |
2.16e-86 |
|
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: 270.20 E-value: 2.16e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 453 LRNLERDLKLTVFGQDAAIDSLSTAIKLSRAGLKSPDKPVGSFLFAGPTGVGKTEAARQLAKAL---GIELVRFDMSEYM 529
Cdd:cd19499 2 LLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMSEYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 530 ERHTVSRLIGAPPGYVGFDQGGLLTEAVTKQPHCVLLLDEIEKAHPEVFNLLLQVMDHGTLTDNNGRKADFRNVIVIMTT 609
Cdd:cd19499 82 EKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTS 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1598135533 610 NAgaetaarasigfthqdhssdamevikksFTPEFRNRLDTIIQF 654
Cdd:cd19499 162 NH----------------------------FRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
490-651 |
6.61e-79 |
|
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: 250.19 E-value: 6.61e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 490 KPVGSFLFAGPTGVGKTEAARQLAKALGI---ELVRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTEAVTKQPHCVLL 566
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 567 LDEIEKAHPEVFNLLLQVMDHGTLTDNNGRKADFRNVIVIMTTNAGAE---TAARASIGFTHQDHSSDAMEVIKKSFTPE 643
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEkisDASRLGDSPDYELLKEEVMDLLKKGFIPE 160
|
....*...
gi 1598135533 644 FRNRLDTI 651
Cdd:pfam07724 161 FLGRLPII 168
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
657-738 |
3.48e-28 |
|
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: 107.88 E-value: 3.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 657 LSHEVIKNVVDKFLTELQAQLEDKRVLLEVTDAVRGYLAEEGYDAAMGARPMARLIQEKIKRPLAEEILFGELSEhGGVV 736
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKE-GDTV 79
|
..
gi 1598135533 737 HI 738
Cdd:pfam10431 80 RV 81
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
657-747 |
2.01e-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) 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: 106.37 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 657 LSHEVIKNVVDKFLTELQAQLEDKRVLLEVTDAVRGYLAEEGYDAAMGARPMARLIQEKIKRPLAEEILFGELSEhGGVV 736
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKD-GDTV 79
|
90
....*....|.
gi 1598135533 737 HIDFKDGEITF 747
Cdd:smart01086 80 VVDVDDGELVF 90
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
354-458 |
3.97e-25 |
|
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: 100.25 E-value: 3.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 354 SVEDTIGILRGLKGRFEQHHNIEYSDEALRAAAELASRYINDRHMPDKAIDVIDEAGAYQRLQpveMRVKRIEVPQVEDI 433
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLS---QESKPEELEDLERE 77
|
90 100
....*....|....*....|....*
gi 1598135533 434 VAKIARIPPKHVNSSDKELLRNLER 458
Cdd:pfam17871 78 LAKLEIEKEALEREQDFEKAERLAK 102
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
193-348 |
2.62e-20 |
|
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: 87.97 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 193 VGREMEVERVAQILARRRKNNPLLVGEAGVGKTAIAEGLAKRIVDNQVPdllansvVYSLDLGALLAGTKYRGDFE-KRF 271
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGhFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1598135533 272 KALLGELKKRPHAILFIDEIHTIigAGAASGGVMDASNLLKPLL-SSGDIRCIGSTTFQEFRgifEKDRALARRFQKV 348
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDSL--SRGAQNALLRVLETLNDLRiDRENVRVIGATNRPLLG---DLDRALYDRLDIR 146
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
465-610 |
3.40e-16 |
|
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: 76.42 E-value: 3.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 465 FGQDAAIDSLSTAIKLsraglkspdKPVGSFLFAGPTGVGKTEAARQLAKAL---GIELVRFDMSEYMERHTVSRLIgap 541
Cdd:cd00009 1 VGQEEAIEALREALEL---------PPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELF--- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1598135533 542 pgyvGFDQGGLLTEAVTKQPHCVLLLDEIEKAHPEVFNLLLQVMDHGtltdnNGRKADFRNVIVIMTTN 610
Cdd:cd00009 69 ----GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETL-----NDLRIDRENVRVIGATN 128
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
215-348 |
4.25e-14 |
|
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: 69.54 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 215 LLVGEAGVGKTAIAEGLAKRivdnqvpdllANSVVYSLDLGALLAgtKYRGDFEKRFKALLGELKKRPHAILFIDEIHTI 294
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKE----------LGAPFIEISGSELVS--KYVGESEKRLRELFEAAKKLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1598135533 295 IGAGAASGG--VMDASNLLKPLL-----SSGDIRCIGSTTFqefrgIFEKDRALARRFQKV 348
Cdd:pfam00004 70 AGSRGSGGDseSRRVVNQLLTELdgftsSNSKVIVIAATNR-----PDKLDPALLGRFDRI 125
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
496-656 |
5.85e-14 |
|
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: 69.16 E-value: 5.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 496 LFAGPTGVGKTEAARQLAKALGIELVRFDMSEymerhTVSRLIGAPPGYVgfdqGGLLTEAVTKQPhCVLLLDEIEKAHP 575
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSE-----LVSKYVGESEKRL----RELFEAAKKLAP-CVIFIDEIDALAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 576 -----------EVFNLLLQVMDhgtltdnnGRKADFRNVIVIMTTNagaetaarasigfthqdhssdamevIKKSFTPEF 644
Cdd:pfam00004 72 srgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN-------------------------RPDKLDPAL 118
|
170
....*....|..
gi 1598135533 645 RNRLDTIIQFGR 656
Cdd:pfam00004 119 LGRFDRIIEFPL 130
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
469-610 |
7.81e-14 |
|
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: 69.62 E-value: 7.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 469 AAIDSLSTAIKLSRAGLKSPDKPVGSFLFAGPTGVGKTEAARQLAKALGIELVRFDMSEYMERHTvsrligappGYVGfD 548
Cdd:cd19481 3 ASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYV---------GESE-K 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1598135533 549 QGGLLTEAVTKQPHCVLLLDEIEKA------------HPEVFNLLLQVMDHGTLTDnngrkadfrNVIVIMTTN 610
Cdd:cd19481 73 NLRKIFERARRLAPCILFIDEIDAIgrkrdssgesgeLRRVLNQLLTELDGVNSRS---------KVLVIAATN 137
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
494-610 |
7.83e-13 |
|
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: 66.16 E-value: 7.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 494 SFLFAGPTGVGKTEAARQLAKAL-GIELVRFDMSEYMerhTVSRLIGA---PPGYVGFDQGGLLTEAvtkQPHCVLLLDE 569
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDT---TEEDLFGRrniDPGGASWVDGPLVRAA---REGEIAVLDE 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1598135533 570 IEKAHPEVFNLLLQVMDHGTLTDNNGR---KADFRNVIVIMTTN 610
Cdd:pfam07728 75 INRANPDVLNSLLSLLDERRLLLPDGGelvKAAPDGFRLIATMN 118
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
13-63 |
2.12e-11 |
|
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: 59.46 E-value: 2.12e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1598135533 13 AFKEARSKRHEFMTVEHLLLALLDNE--AAATVLRACGANLDKLKHDLQEFID 63
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDdgLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
210-348 |
2.78e-11 |
|
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: 62.01 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 210 RKNNPLLVGEAGVGKTAIAEGLAKRIVDNQVPDLLAN-----SVVYSLDLGALLAGTKYRGDFEKRFKALLGELKKRPHA 284
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDgedilEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1598135533 285 ILFIDEIHTIIGA-GAASGGVMDASNLLKPLLSSGDIRCIGSTTfqefRGIFEKDRALARRFQKV 348
Cdd:smart00382 81 VLILDEITSLLDAeQEALLLLLEELRLLLLLKSEKNLTVILTTN----DEKDLGPALLRRRFDRR 141
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
496-621 |
2.16e-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: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 496 LFAGPTGVGKTEAARQLAKAL---GIELVRFDMSEYMERHTVSRLIGAPPGYVGFDQGG----LLTEAVTKQPHCVLLLD 568
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGElrlrLALALARKLKPDVLILD 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1598135533 569 EIEKAHPEVFNLLLQVMDHGTLTDNNGRKadfRNVIVIMTTNAGAETAARASI 621
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLLLLKSE---KNLTVILTTNDEKDLGPALLR 135
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
448-610 |
4.79e-10 |
|
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: 61.34 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 448 SDKELLRNLERDlkltVFGQDAAIDSLSTAIKLsraglkspDKPVgsfLFAGPTGVGKTEAARQLAKALGIELVRF---- 523
Cdd:COG0714 2 TEARLRAEIGKV----YVGQEELIELVLIALLA--------GGHL---LLEGVPGVGKTTLAKALARALGLPFIRIqftp 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 524 DMseymerhTVSRLIG---APPGYVGF--DQGGLLTeavtkqphCVLLLDEIEKAHPEVFNLLLQVMDHGTLT-DNNGRK 597
Cdd:COG0714 67 DL-------LPSDILGtyiYDQQTGEFefRPGPLFA--------NVLLADEINRAPPKTQSALLEAMEERQVTiPGGTYK 131
|
170
....*....|...
gi 1598135533 598 ADFRnVIVIMTTN 610
Cdd:COG0714 132 LPEP-FLVIATQN 143
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
38-377 |
1.07e-09 |
|
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: 61.08 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 38 EAAATVLRACGANLDKLKHDLQEFIDSTTPLIPVHDEDRETQPTLGFQRVLQRAVFHVQSSGKREVTGANVLVAIFSEQE 117
Cdd:COG0464 5 LALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 118 SQAVFLLKQQSVARIDVVNYIAHGISKVPGHGDQSEGEQDMQDDEGGESSSSGNPLDAYASNLNELARQGRIDPLVGREM 197
Cdd:COG0464 85 LLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 198 EVERVAQILARRRKNNP-------------LLVGEAGVGKTAIAEGLAKRIvdnQVPdllansvVYSLDLGALLAgtKYR 264
Cdd:COG0464 165 VKEELRELVALPLKRPElreeyglppprglLLYGPPGTGKTLLARALAGEL---GLP-------LIEVDLSDLVS--KYV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 265 GDFEKRFKALLGELKKRPHAILFIDEIHTIIGA-GAASGGVMDA--SNLLKPL-LSSGDIRCIGSTTFqefrgIFEKDRA 340
Cdd:COG0464 233 GETEKNLREVFDKARGLAPCVLFIDEADALAGKrGEVGDGVGRRvvNTLLTEMeELRSDVVVIAATNR-----PDLLDPA 307
|
330 340 350
....*....|....*....|....*....|....*...
gi 1598135533 341 LARRFQ-KVDVSEPSVEDTIGILRGLKGRFEQHHNIEY 377
Cdd:COG0464 308 LLRRFDeIIFFPLPDAEERLEIFRIHLRKRPLDEDVDL 345
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
396-674 |
1.67e-09 |
|
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: 60.70 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 396 RHMPDKAIDVIDEAGAYQRLQPVEMRVKRIEVPQVEDIVAKIARIPPKHVNSSDKELLRNLERDLKlTVFGQDAAIDSLS 475
Cdd:COG0464 92 LLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILD-DLGGLEEVKEELR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 476 TAIKLSRAGLKSPDK----PVGSFLFAGPTGVGKTEAARQLAKALGIELVRFDMSEymerhtvsrLIGappGYVGfdqgg 551
Cdd:COG0464 171 ELVALPLKRPELREEyglpPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSD---------LVS---KYVG----- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 552 lLTEAVTKQ--------PHCVLLLDEIEKAHP-----------EVFNLLLQVMDhgtltdnngrkaDFR-NVIVIMTTNA 611
Cdd:COG0464 234 -ETEKNLREvfdkarglAPCVLFIDEADALAGkrgevgdgvgrRVVNTLLTEME------------ELRsDVVVIAATNR 300
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1598135533 612 gaetaarasigFTHQDhssdamevikksftPEFRNRLDTIIQFGRLSHEVIKNVVDKFLTELQ 674
Cdd:COG0464 301 -----------PDLLD--------------PALLRRFDEIIFFPLPDAEERLEIFRIHLRKRP 338
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
215-348 |
6.96e-09 |
|
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: 55.37 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 215 LLVGEAGVGKTAIAEGLAKRivdnqvpdllANSVVYSLDLGALLagTKYRGDFEKRFKALLGELKKRPHAILFIDEIHTI 294
Cdd:cd19481 30 LLYGPPGTGKTLLAKALAGE----------LGLPLIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDAI 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1598135533 295 IGAGAASGGVMDAS-------NLLKPLLSSGDIRCIGSTTFQEfrgifEKDRALAR--RFQKV 348
Cdd:cd19481 98 GRKRDSSGESGELRrvlnqllTELDGVNSRSKVLVIAATNRPD-----LLDPALLRpgRFDEV 155
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
190-363 |
5.41e-08 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 54.50 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 190 DPLVGREMEVERVAQILA-RRRKNNP-----------LLVGEAGVGKTAIAEGLAKRIvdnQVPdllansvVYSLDLGAL 257
Cdd:COG1223 2 DDVVGQEEAKKKLKLIIKeLRRRENLrkfglwpprkiLFYGPPGTGKTMLAEALAGEL---KLP-------LLTVRLDSL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 258 LagTKYRGDFEKRFKALLGELKKRPhAILFIDEIHTIigagaasGGVMDASNLlkpllsSGDIRCIGSTTFQEFRGIFEK 337
Cdd:COG1223 72 I--GSYLGETARNLRKLFDFARRAP-CVIFFDEFDAI-------AKDRGDQND------VGEVKRVVNALLQELDGLPSG 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1598135533 338 -------------DRALARRFQ-KVDVSEPSVEDTIGILR 363
Cdd:COG1223 136 svviaatnhpellDSALWRRFDeVIEFPLPDKEERKEILE 175
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
464-697 |
8.49e-08 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 53.73 E-value: 8.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 464 VFGQDAAIDSLSTAIK-------LSRAGLKSPDKpvgsFLFAGPTGVGKTEAARQLAKALGIEL--VRFD--MSEYMERh 532
Cdd:COG1223 4 VVGQEEAKKKLKLIIKelrrrenLRKFGLWPPRK----ILFYGPPGTGKTMLAEALAGELKLPLltVRLDslIGSYLGE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 533 TVSRLigappgyvgfdqgGLLTEAVTKQPhCVLLLDEIE---------KAHPE---VFNLLLQVMDhgtltdnnGRKadf 600
Cdd:COG1223 79 TARNL-------------RKLFDFARRAP-CVIFFDEFDaiakdrgdqNDVGEvkrVVNALLQELD--------GLP--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 601 RNVIVIMTTNagaetaarasigfthQDHSSDamevikksftPEFRNRLDTIIQFGRLSHEVIKNVVDKFLTELQAQLE-D 679
Cdd:COG1223 134 SGSVVIAATN---------------HPELLD----------SALWRRFDEVIEFPLPDKEERKEILELNLKKFPLPFElD 188
|
250
....*....|....*...
gi 1598135533 680 KRVLLEVTDAVRGYLAEE 697
Cdd:COG1223 189 LKKLAKKLEGLSGADIEK 206
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
464-516 |
7.11e-07 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 52.12 E-value: 7.11e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1598135533 464 VFGQDAAIDSLSTAIKLSR---AglkspdkpvgsFLFAGPTGVGKTEAARQLAKAL 516
Cdd:COG2812 12 VVGQEHVVRTLKNALASGRlahA-----------YLFTGPRGVGKTTLARILAKAL 56
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
496-572 |
7.18e-07 |
|
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: 50.25 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 496 LFAGPTGVGKTEAARQLAKALGIELVRF------DMSEYM-ERHTvsrLIGAPPGYVgfDQGglLTEAVTKQPhcVLLLD 568
Cdd:cd19500 41 CLVGPPGVGKTSLGKSIARALGRKFVRIslggvrDEAEIRgHRRT---YVGAMPGRI--IQA--LKKAGTNNP--VFLLD 111
|
....
gi 1598135533 569 EIEK 572
Cdd:cd19500 112 EIDK 115
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
215-363 |
1.09e-06 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 51.16 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 215 LLVGEAGVGKTAIAEGLAKRivdnqvpdllANSVVYSLDLGALLagTKYRGDFEKRFKALLGELKKRPHAILFIDEIHTI 294
Cdd:COG1222 116 LLYGPPGTGKTLLAKAVAGE----------LGAPFIRVRGSELV--SKYIGEGARNVREVFELAREKAPSIIFIDEIDAI 183
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1598135533 295 IGAGAASGGVMDASNLLKPLL-------SSGDIRCIGSTTFQEfrgifEKDRALAR--RF-QKVDVSEPSVEDTIGILR 363
Cdd:COG1222 184 AARRTDDGTSGEVQRTVNQLLaeldgfeSRGDVLIIAATNRPD-----LLDPALLRpgRFdRVIEVPLPDEEAREEILK 257
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
191-311 |
2.74e-06 |
|
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: 48.27 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 191 PLVGREMEVERVAQILARRRKNNP---LLVGEAGVGKTAIAEGLAKRIVDNQVPDLLANSVVYSLDLGALLAGTkyrgdF 267
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPLLEALT-----R 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1598135533 268 EKRFKALLGELKKRPHAiLFIDEIHTIIGAGAASGGVMDASNLL 311
Cdd:pfam13191 76 EGLLRQLLDELESSLLE-AWRAALLEALAPVPELPGDLAERLLD 118
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
192-291 |
4.26e-06 |
|
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: 49.40 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 192 LVGREMEVERV-AQILARRrknnPLLV-GEAGVGKTAIAEGLAK-------RIvdnQV-PDLLANSVVYSLDLGallagt 261
Cdd:COG0714 14 YVGQEELIELVlIALLAGG----HLLLeGVPGVGKTTLAKALARalglpfiRI---QFtPDLLPSDILGTYIYD------ 80
|
90 100 110
....*....|....*....|....*....|..
gi 1598135533 262 KYRGDFekrfkallgELKKRP--HAILFIDEI 291
Cdd:COG0714 81 QQTGEF---------EFRPGPlfANVLLADEI 103
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
402-610 |
1.24e-05 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 48.08 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 402 AIDVIDEAGAYQRLQPVEMRVKRIEVPQVEDIVAKIARIPpkhvnSSDKELLRNLERDLKLT---VFGQDAAIDSLSTAI 478
Cdd:COG1222 20 ALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKR-----LGTPRGTAVPAESPDVTfddIGGLDEQIEEIREAV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 479 KLSragLKSPD-------KPVGSFLFAGPTGVGKTEAARQLAKALGIELVRFDMSEYMERhtvsrligappgYVGfdQGG 551
Cdd:COG1222 95 ELP---LKNPElfrkygiEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK------------YIG--EGA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1598135533 552 -----LLTEAVTKQPhCVLLLDEIE---------KAHPEV---FNLLLQVMDhgTLTDNNgrkadfrNVIVIMTTN 610
Cdd:COG1222 158 rnvreVFELAREKAP-SIIFIDEIDaiaarrtddGTSGEVqrtVNQLLAELD--GFESRG-------DVLIIAATN 223
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
215-347 |
1.39e-05 |
|
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: 45.81 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 215 LLVGEAGVGKTAIAEGLAKRIvdnqvpdllaNSVVYSLDLGALLAgtKYRGDFEKRFKALLGELKKRPHAILFIDEIHTI 294
Cdd:cd19509 36 LLYGPPGTGKTLLARAVASES----------GSTFFSISASSLVS--KWVGESEKIVRALFALARELQPSIIFIDEIDSL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1598135533 295 I---GAGAASGGVMDASNLLKPL-----LSSGDIRCIGSTTFqefrgIFEKDRALARRFQK 347
Cdd:cd19509 104 LserGSGEHEASRRVKTEFLVQMdgvlnKPEDRVLVLGATNR-----PWELDEAFLRRFEK 159
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
496-572 |
4.61e-05 |
|
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: 44.68 E-value: 4.61e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1598135533 496 LFAGPTGVGKTEAARQLAKALGIELVRFDMSEYMErhtvsrligapPGYVGFDQGGLLTEAVTKqphcVLLLDEIEK 572
Cdd:cd19498 50 LMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTE-----------VGYVGRDVESIIRDLVEG----IVFIDEIDK 111
|
|
| PRK14965 |
PRK14965 |
DNA polymerase III subunits gamma and tau; Provisional |
466-519 |
8.55e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237871 [Multi-domain] Cd Length: 576 Bit Score: 45.89 E-value: 8.55e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1598135533 466 GQDAAIDSLSTAIKLSRAGlkspdkpvGSFLFAGPTGVGKTEAARQLAKALGIE 519
Cdd:PRK14965 20 GQEHVSRTLQNAIDTGRVA--------HAFLFTGARGVGKTSTARILAKALNCE 65
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
493-586 |
9.52e-05 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 42.71 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 493 GSFLFAGPTGVGKTEAARQLAKAL---GIELVRFDMSEYME----RHTVSRLIGAPPGYvGFDQGGLLT----EAVTKQP 561
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLpevRDSVVFVDLPSGTSpkdlLRALLRALGLPLSG-RLSKEELLAalqqLLLALAV 84
|
90 100
....*....|....*....|....*
gi 1598135533 562 HCVLLLDEIEKAHPEVFNLLLQVMD 586
Cdd:pfam13401 85 AVVLIIDEAQHLSLEALEELRDLLN 109
|
|
| PRK14953 |
PRK14953 |
DNA polymerase III subunits gamma and tau; Provisional |
464-516 |
1.08e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237867 [Multi-domain] Cd Length: 486 Bit Score: 45.58 E-value: 1.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1598135533 464 VFGQDAAIDSLSTAIKLsraglkspDKPVGSFLFAGPTGVGKTEAARQLAKAL 516
Cdd:PRK14953 18 VIGQEIVVRILKNAVKL--------QRVSHAYIFAGPRGTGKTTIARILAKVL 62
|
|
| PRK06647 |
PRK06647 |
DNA polymerase III subunits gamma and tau; Validated |
463-516 |
1.29e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 235845 [Multi-domain] Cd Length: 563 Bit Score: 45.15 E-value: 1.29e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1598135533 463 TVFGQDAAIDSLSTAIklsraglkSPDKPVGSFLFAGPTGVGKTEAARQLAKAL 516
Cdd:PRK06647 17 SLEGQDFVVETLKHSI--------ESNKIANAYIFSGPRGVGKTSSARAFARCL 62
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
120-240 |
1.30e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 45.62 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 120 AVFLLKQQSVARIDVVNYIAHGISKVPGHGDQSEGEQDMQDDEGGESSSSGNPLDAYASNLNELARQGRIDPLVGREMEV 199
Cdd:COG3899 217 AAAAAAAAAAAPAAPVVLVAALLLALAALLALLLLAARLLGLAGAAALLLLGLLAAAAAGRRLLARRLIPQPLVGREAEL 296
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1598135533 200 ERVAQILARRRKNNP---LLVGEAGVGKTAIAEGLAKRIVDNQV 240
Cdd:COG3899 297 AALLAALERARAGRGelvLVSGEAGIGKSRLVRELARRARARGG 340
|
|
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
496-572 |
2.19e-04 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 44.62 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 496 LFAGPTGVGKTEAARQLAKALGIELVRF------DMSE-------YmerhtvsrlIGAPPGyvGFDQGglLTEAVTKQPh 562
Cdd:COG0466 356 CLVGPPGVGKTSLGKSIARALGRKFVRIslggvrDEAEirghrrtY---------IGAMPG--RIIQG--LKKAGTKNP- 421
|
90
....*....|
gi 1598135533 563 cVLLLDEIEK 572
Cdd:COG0466 422 -VFLLDEIDK 430
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
463-516 |
3.30e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 44.00 E-value: 3.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1598135533 463 TVFGQDAAIDSLSTAI---KLSRAglkspdkpvgsFLFAGPTGVGKTEAARQLAKAL 516
Cdd:PRK14971 18 SVVGQEALTTTLKNAIatnKLAHA-----------YLFCGPRGVGKTTCARIFAKTI 63
|
|
| PRK06305 |
PRK06305 |
DNA polymerase III subunits gamma and tau; Validated |
464-516 |
4.26e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 180523 [Multi-domain] Cd Length: 451 Bit Score: 43.61 E-value: 4.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1598135533 464 VFGQDAAIDSLSTAIKLSRAGlkspdkpvGSFLFAGPTGVGKTEAARQLAKAL 516
Cdd:PRK06305 19 ILGQDAVVAVLKNALRFNRAA--------HAYLFSGIRGTGKTTLARIFAKAL 63
|
|
| PRK11331 |
PRK11331 |
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional |
494-648 |
4.30e-04 |
|
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
Pssm-ID: 183088 [Multi-domain] Cd Length: 459 Bit Score: 43.54 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 494 SFLFAGPTGVGKTEAARQLAKALGIELV--RFDMSEYMERHTVSRLI-GAPPGYVGF-DQGGL---LTEAVTKQPH--CV 564
Cdd:PRK11331 196 NIILQGPPGVGKTFVARRLAYLLTGEKApqRVNMVQFHQSYSYEDFIqGYRPNGVGFrRKDGIfynFCQQAKEQPEkkYV 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 565 LLLDEIEKAH-PEVFNLLLQVMDHGT--------LTDNNGRKADF---RNVIVIMTTNAGAETAARASIGFTHQDHSSDa 632
Cdd:PRK11331 276 FIIDEINRANlSKVFGEVMMLMEHDKrgenwsvpLTYSENDEERFyvpENVYIIGLMNTADRSLAVVDYALRRRFSFID- 354
|
170
....*....|....*..
gi 1598135533 633 mevIKKSF-TPEFRNRL 648
Cdd:PRK11331 355 ---IEPGFdTPQFRNFL 368
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
464-654 |
6.88e-04 |
|
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: 42.20 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 464 VFGQDAAIDSLSTAI----KLSRAGLKSPDKPV----GSFLFAGPTGVGKTEAARQLAKALGIELVRFDMSEYMErhtvs 535
Cdd:cd19497 14 VIGQERAKKVLSVAVynhyKRIRNNLKQKDDDVelekSNILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTE----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 536 rligapPGYVGFDQGG----LLTEA---VTKQPHCVLLLDEIEK-----AHPE---------VFNLLLQVMDhGTL---T 591
Cdd:cd19497 89 ------AGYVGEDVENillkLLQAAdydVERAQRGIVYIDEIDKiarksENPSitrdvsgegVQQALLKILE-GTVanvP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 592 DNNGRKADFRNVIVIMTTN-----AGA-----ETAAR----ASIGFTHQDHSSDAME-------------VIKKSFTPEF 644
Cdd:cd19497 162 PQGGRKHPQQEFIQVDTTNilficGGAfvgleKIIARrlgkKSLGFGAETSSEKDEKerdellskvepedLIKFGLIPEF 241
|
250
....*....|
gi 1598135533 645 RNRLDTIIQF 654
Cdd:cd19497 242 VGRLPVIVTL 251
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
215-326 |
8.53e-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: 40.74 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 215 LLVGEAGVGKTAIAeglakRIVDNQvpdllANSVVYSLDLGALLAgtKYRGDFEKRFKALLGELKKRPHAILFIDEIHTI 294
Cdd:cd19503 38 LLHGPPGTGKTLLA-----RAVANE-----AGANFLSISGPSIVS--KYLGESEKNLREIFEEARSHAPSIIFIDEIDAL 105
|
90 100 110
....*....|....*....|....*....|....*...
gi 1598135533 295 IGAGAASGGVMDAS------NLLKPLLSSGDIRCIGST 326
Cdd:cd19503 106 APKREEDQREVERRvvaqllTLMDGMSSRGKVVVIAAT 143
|
|
| PRK14956 |
PRK14956 |
DNA polymerase III subunits gamma and tau; Provisional |
464-519 |
1.09e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184920 [Multi-domain] Cd Length: 484 Bit Score: 42.24 E-value: 1.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1598135533 464 VFGQDAAIDSLSTAIKLSRAGlkspdkpvGSFLFAGPTGVGKTEAARQLAKALGIE 519
Cdd:PRK14956 20 VIHQDLAIGALQNALKSGKIG--------HAYIFFGPRGVGKTTIARILAKRLNCE 67
|
|
| RecA-like_VPS4 |
cd19521 |
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ... |
215-347 |
1.24e-03 |
|
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. 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: 410929 [Multi-domain] Cd Length: 170 Bit Score: 40.23 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 215 LLVGEAGVGKTAIAEGLAKRivdnqvpdllANSVVYSLDLGALLagTKYRGDFEKRFKALLGELKKRPHAILFIDEIHTI 294
Cdd:cd19521 44 LLYGPPGTGKSYLAKAVATE----------ANSTFFSVSSSDLV--SKWMGESEKLVKQLFAMARENKPSIIFIDEVDSL 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1598135533 295 igAGAASGGVMDASNLLKPLL---------SSGDIRCIGSTTFQefrgiFEKDRALARRFQK 347
Cdd:cd19521 112 --CGTRGEGESEASRRIKTELlvqmngvgnDSQGVLVLGATNIP-----WQLDSAIRRRFEK 166
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
464-515 |
1.32e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 42.10 E-value: 1.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1598135533 464 VFGQDAAIDSLSTAIKLSRAGlkspdkpvGSFLFAGPTGVGKTEAARQLAKA 515
Cdd:PRK14950 18 LVGQEHVVQTLRNAIAEGRVA--------HAYLFTGPRGVGKTSTARILAKA 61
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
466-610 |
1.47e-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: 39.97 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 466 GQDAAIDSLSTAIKLSragLKSPD-------KPVGSFLFAGPTGVGKTEAARQLAKALGIELVRFD----MSEYM-ERHT 533
Cdd:cd19503 4 GLDEQIASLKELIELP---LKYPElfralglKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISgpsiVSKYLgESEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 534 VSRLIGAppgyvgfdqgglltEAVTKQPhCVLLLDEI-------EKAHPEVFN-LLLQVMdhgTLTDNNGRKadfRNVIV 605
Cdd:cd19503 81 NLREIFE--------------EARSHAP-SIIFIDEIdalapkrEEDQREVERrVVAQLL---TLMDGMSSR---GKVVV 139
|
....*
gi 1598135533 606 IMTTN 610
Cdd:cd19503 140 IAATN 144
|
|
| RecA-like_spastin |
cd19524 |
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ... |
215-347 |
1.62e-03 |
|
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. 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: 410932 [Multi-domain] Cd Length: 164 Bit Score: 39.83 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 215 LLVGEAGVGKTAIAEGLAKRivdnqvpdllANSVVYSLDLGALLagTKYRGDFEKRFKALLGELKKRPHAILFIDEIHTI 294
Cdd:cd19524 37 LLFGPPGNGKTMLAKAVAAE----------SNATFFNISAASLT--SKYVGEGEKLVRALFAVARELQPSIIFIDEVDSL 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1598135533 295 IgaGAASGGVMDASNLLKP--------LLSSGDIRCI--GSTTFQEfrgifEKDRALARRFQK 347
Cdd:cd19524 105 L--SERSEGEHEASRRLKTefliefdgVQSNGDDRVLvmGATNRPQ-----ELDDAVLRRFTK 160
|
|
| PRK07399 |
PRK07399 |
DNA polymerase III subunit delta'; Validated |
459-516 |
1.75e-03 |
|
DNA polymerase III subunit delta'; Validated
Pssm-ID: 236011 [Multi-domain] Cd Length: 314 Bit Score: 41.04 E-value: 1.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1598135533 459 DLKLTVFGQDAAIDSLSTAIKLSRAglkSPdkpvgSFLFAGPTGVGKTEAARQLAKAL 516
Cdd:PRK07399 1 NLFANLIGQPLAIELLTAAIKQNRI---AP-----AYLFAGPEGVGRKLAALCFIEGL 50
|
|
| hslU |
PRK05201 |
ATP-dependent protease ATPase subunit HslU; |
499-514 |
2.93e-03 |
|
ATP-dependent protease ATPase subunit HslU;
Pssm-ID: 235364 [Multi-domain] Cd Length: 443 Bit Score: 40.83 E-value: 2.93e-03
|
| PRK14948 |
PRK14948 |
DNA polymerase III subunit gamma/tau; |
466-516 |
2.96e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237862 [Multi-domain] Cd Length: 620 Bit Score: 41.10 E-value: 2.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1598135533 466 GQDAAIDSLSTAIKLSRAglkSPdkpvgSFLFAGPTGVGKTEAARQLAKAL 516
Cdd:PRK14948 20 GQEAIATTLKNALISNRI---AP-----AYLFTGPRGTGKTSSARILAKSL 62
|
|
| HslU |
COG1220 |
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ... |
499-514 |
2.98e-03 |
|
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440833 [Multi-domain] Cd Length: 454 Bit Score: 40.80 E-value: 2.98e-03
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
474-529 |
4.66e-03 |
|
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities: AAA1-AAA6). This is the first site (out of four nucleotide binding sites in the dynein motor) where the movement depends on ATP hydrolysis. When this site is nucleotide free or bound to ADP, the microtubule binding domain (MTBD) binds to the microtubule and the linker adopts the straight post-power-stroke conformation. Upon ATP binding and hydrolysis, the MTBD detaches from the microtubule and the linker is primed into the pre-power-stroke conformation. Dynein's AAA+ domains are each divided into an alpha/beta large subdomain designated with an L and and alpha small subdomains designated with an S. This is the AAA1 large (AAA1L) subdomain with the accompanying small subdomain (AAA1S). AAA1L, AAA1S and AAA2L enclose ADP.vanadate (ADP.Vi, ATP-hydrolysis transition state analogue). The AAA1L sensor-I loop, which varies in position depending on dynein's nucleotide state, swings in to contact AAA2L forming the important AAA1 nucleotide-binding site.
Pssm-ID: 463697 [Multi-domain] Cd Length: 327 Bit Score: 39.77 E-value: 4.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1598135533 474 LSTAIKLSRAGlkSPdkpvgsflfAGPTGVGKTEAARQLAKALGIELVRFDMSEYM 529
Cdd:pfam12774 25 LTQALHLHLGG--AP---------AGPAGTGKTETVKDLAKALAKQVVVFNCSDGL 69
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|
| PRK14952 |
PRK14952 |
DNA polymerase III subunits gamma/tau; |
464-516 |
4.72e-03 |
|
DNA polymerase III subunits gamma/tau;
Pssm-ID: 237866 [Multi-domain] Cd Length: 584 Bit Score: 40.25 E-value: 4.72e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1598135533 464 VFGQDAAIDSLSTAIKLSRAGlkspdkpvGSFLFAGPTGVGKTEAARQLAKAL 516
Cdd:PRK14952 15 VVGQEHVTEPLSSALDAGRIN--------HAYLFSGPRGCGKTSSARILARSL 59
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
466-516 |
5.16e-03 |
|
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required for, along with delta' subunit, the assembly of the processivity factor beta(2) onto primed DNA in the DNA polymerase III holoenzyme-catalyzed reaction. The delta subunit is also known as HolA.
Pssm-ID: 433013 [Multi-domain] Cd Length: 161 Bit Score: 38.35 E-value: 5.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1598135533 466 GQDAAIDSLSTAIKlsraglksPDKPVGSFLFAGPTGVGKTEAARQLAKAL 516
Cdd:pfam13177 1 GQPEAIQLLQNSLE--------NGRLSHAYLFSGPEGVGKLELALAFAKAL 43
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
496-573 |
5.68e-03 |
|
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. 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: 410915 [Multi-domain] Cd Length: 161 Bit Score: 38.12 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 496 LFAGPTGVGKTEAARQLAKALGIELVRFDMseymerhtvSRLIGappGYVG-----FDQGGLLTEAVTKqphCVLLLDEI 570
Cdd:cd19507 35 LLVGIQGTGKSLTAKAIAGVWQLPLLRLDM---------GRLFG---GLVGesesrLRQMIQTAEAIAP---CVLWIDEI 99
|
...
gi 1598135533 571 EKA 573
Cdd:cd19507 100 EKG 102
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
215-294 |
5.72e-03 |
|
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: 40.28 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 215 LLVGEAGVGKTAIAEGLAKRivdnqvpdllANSVVYSLDLGALLagTKYRGDFEKRFKALLGELKKRPHAILFIDEIHTI 294
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANE----------AGAYFISINGPEIM--SKYYGESEERLREIFKEAEENAPSIIFIDEIDAI 283
|
|
| PRK05563 |
PRK05563 |
DNA polymerase III subunits gamma and tau; Validated |
464-516 |
8.46e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 235505 [Multi-domain] Cd Length: 559 Bit Score: 39.47 E-value: 8.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1598135533 464 VFGQDAAIDSLSTAIKLSRAGlkspdkpvGSFLFAGPTGVGKTEAARQLAKAL 516
Cdd:PRK05563 18 VVGQEHITKTLKNAIKQGKIS--------HAYLFSGPRGTGKTSAAKIFAKAV 62
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
490-610 |
9.86e-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: 37.77 E-value: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1598135533 490 KPVGSFLFAGPTGVGKTEAARQLAKALGIELVRFDMSEymerhTVSRLIGAPPGYVgfdqGGLLTEAVTKQPhCVLLLDE 569
Cdd:cd19518 32 EPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATE-----IVSGVSGESEEKI----RELFDQAISNAP-CIVFIDE 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1598135533 570 IEKAHPE-----------VFNLLLQVMDHGTLTDNNGRKadfrnVIVIMTTN 610
Cdd:cd19518 102 IDAITPKresaqremerrIVSQLLTCMDELNNEKTAGGP-----VLVIGATN 148
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