|
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: 1158.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 1 MLNRELEVTLNLAFKEARSKRHEFMTVEHLLLALLDNEAAATVLRACGANLDKLKHDLQEFIDSTTPLIPVHDEDRETQP 80
Cdd:PRK11034 1 MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 81 TLGFQRVLQRAVFHVQSSGKREVTGANVLVAIFSEQESQAVFLLKQQSVARIDVVNYIAHGISKVPGHGEHSDGEqdmqD 160
Cdd:PRK11034 81 TLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPSQSSDPGS----Q 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 161 EEGGETSSSGNPLDAYASNLNEQARQGRIDPLVGRELEVERVAQILARRRKNNPLLVGEAGVGKTAIAEGLAKRIVDGQV 240
Cdd:PRK11034 157 PNSEEQAGGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 241 PDLLAQSVVYSLDLGALLAGTKYRGDFEKRFKALLGELKKRPQAILFIDEIHTIIGAGAASGGVMDASNLLKPLLSSGDI 320
Cdd:PRK11034 237 PEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 321 RCIGSTTFQEFRGIFEKDRALARRFQKVDVSEPSVEDTVGILRGLKGRFESHHNIEYSDEALRAAAELAARYINDRHMPD 400
Cdd:PRK11034 317 RVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 401 KAIDVIDEAGAYQRLQPVEMRVKRIDVPQVEDIVAKIARIPPKHVTSSDKELLRNLERDLKLTVFGQDAAIDSLATAIKL 480
Cdd:PRK11034 397 KAIDVIDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKM 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 481 SRAGLKSPDKPVGSFLFAGPTGVGKTEAARQLAKALGVELVRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTEAITKQ 560
Cdd:PRK11034 477 SRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKH 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 561 PHCVLLLDEIEKAHPEVFNLLLQVMDHGTLTDNNGRKADFRNVIVIMTTNAGAETAARASIGFTQQDHSSDAMEVIKKSF 640
Cdd:PRK11034 557 PHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMEEIKKIF 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 641 TPEFRNRLDTIIQFGRLSHETIKSVVDKFLIELQAQLEDKRVLLEVSDAARSWLAAGGYDAMMGARPMARLIQDKIKRPL 720
Cdd:PRK11034 637 TPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPL 716
|
730 740 750
....*....|....*....|....*....|....
gi 1944675807 721 AEEILFGELAeHGGVVHIDIREGELVFEFETTAE 754
Cdd:PRK11034 717 ANELLFGSLV-DGGQVTVALDKEKNELTYGFQSA 749
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
2-740 |
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: 1102.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 2 LNRELEVTLNLAFKEARSKRHEFMTVEHLLLALLDNEAAATVLRACGANLDKLKHDLQEFIDSTTPLIPvHDEDRETQPT 81
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAIEILEECGGDVELLRKRLEDYLEENLPVIP-EDIDEEPEQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 82 LGFQRVLQRAVFHVQSSGKREVTGANVLVAIFSEQESQAVFLLKQQSVARIDVVNYIAHGISKVPGhgEHSDGEQDMQDE 161
Cdd:TIGR02639 80 VGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITRLDILNYISHGISKDDG--KDQLGEEAGKEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 162 EGGETsssgnPLDAYASNLNEQARQGRIDPLVGRELEVERVAQILARRRKNNPLLVGEAGVGKTAIAEGLAKRIVDGQVP 241
Cdd:TIGR02639 158 EKGQD-----ALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 242 DLLAQSVVYSLDLGALLAGTKYRGDFEKRFKALLGELKKRPQAILFIDEIHTIIGAGAASGGVMDASNLLKPLLSSGDIR 321
Cdd:TIGR02639 233 ERLKNAKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFIDEIHTIVGAGATSGGSMDASNLLKPALSSGKIR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 322 CIGSTTFQEFRGIFEKDRALARRFQKVDVSEPSVEDTVGILRGLKGRFESHHNIEYSDEALRAAAELAARYINDRHMPDK 401
Cdd:TIGR02639 313 CIGSTTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 402 AIDVIDEAGAYQRLQPVEMRVKRIDVPQVEDIVAKIARIPPKHVTSSDKELLRNLERDLKLTVFGQDAAIDSLATAIKLS 481
Cdd:TIGR02639 393 AIDVIDEAGAAFRLRPKAKKKANVNVKDIENVVAKMAKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRS 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 482 RAGLKSPDKPVGSFLFAGPTGVGKTEAARQLAKALGVELVRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTEAITKQP 561
Cdd:TIGR02639 473 RAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEELGVHLLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHP 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 562 HCVLLLDEIEKAHPEVFNLLLQVMDHGTLTDNNGRKADFRNVIVIMTTNAGAETAARASIGFTQQDHSSDAMEVIKKSFT 641
Cdd:TIGR02639 553 HCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTSNAGASEMSKPPIGFGGENRESKSLKAIKKLFS 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 642 PEFRNRLDTIIQFGRLSHETIKSVVDKFLIELQAQLEDKRVLLEVSDAARSWLAAGGYDAMMGARPMARLIQDKIKRPLA 721
Cdd:TIGR02639 633 PEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLS 712
|
730
....*....|....*....
gi 1944675807 722 EEILFGELAEhGGVVHIDI 740
Cdd:TIGR02639 713 DEILFGKLKK-GGSVKISL 730
|
|
| 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: 836.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 2 LNRELEVTLNLAFKEARSKRHEFMTVEHLLLALLDNE--AAATVLRACGANLDKLKHDLQEFIDSttpLIPVHDEDRETQ 79
Cdd:COG0542 6 FTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGegLAAKLLRKLGVDLDALREELEEALGR---LPKVSGSSGQPY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 80 PTLGFQRVLQRAVFHVQSSGKREVTGANVLVAIFSEQESQAVFLLKQQSVARIDVvnyiahgiskvpghgehsdgEQDMQ 159
Cdd:COG0542 83 LSPRLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITLEAL--------------------REALE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 160 DEEGGETSSSGNP------LDAYASNLNEQARQGRIDPLVGRELEVERVAQILARRRKNNPLLVGEAGVGKTAIAEGLAK 233
Cdd:COG0542 143 ELRGGSRVTSQNPesktpaLDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 234 RIVDGQVPDLLAQSVVYSLDLGALLAGTKYRGDFEKRFKALLGELKKRP-QAILFIDEIHTIIGAGAASGGvMDASNLLK 312
Cdd:COG0542 223 RIVNGDVPESLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKSEgNIILFIDELHTLVGAGGAEGA-MDAANLLK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 313 PLLSSGDIRCIGSTTFQEFRGIFEKDRALARRFQKVDVSEPSVEDTVGILRGLKGRFESHHNIEYSDEALRAAAELAARY 392
Cdd:COG0542 302 PALARGELRCIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 393 INDRHMPDKAIDVIDEAGAYQRLQ----PVEMRVKR-------------------------------------------- 424
Cdd:COG0542 382 ITDRFLPDKAIDLIDEAAARVRMEidskPEELDELErrleqleiekealkkeqdeasferlaelrdelaeleeelealka 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 425 --------------------------------------------------IDVPQVEDIVAKIARIPPKHVTSSDKELLR 454
Cdd:COG0542 462 rweaekelieeiqelkeeleqrygkipelekelaeleeelaelapllreeVTEEDIAEVVSRWTGIPVGKLLEGEREKLL 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 455 NLERDLKLTVFGQDAAIDSLATAIKLSRAGLKSPDKPVGSFLFAGPTGVGKTEAARQLAKAL-GVE--LVRFDMSEYMER 531
Cdd:COG0542 542 NLEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLfGDEdaLIRIDMSEYMEK 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 532 HTVSRLIGAPPGYVGFDQGGLLTEAITKQPHCVLLLDEIEKAHPEVFNLLLQVMDHGTLTDNNGRKADFRNVIVIMTTNA 611
Cdd:COG0542 622 HSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNI 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 612 GAETAARASIGFTQQDHSSDA-MEVIKKSFTPEFRNRLDTIIQFGRLSHETIKSVVDKFLIELQAQLEDKRVLLEVSDAA 690
Cdd:COG0542 702 GSELILDLAEDEPDYEEMKEAvMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAA 781
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 1944675807 691 RSWLAAGGYDAMMGARPMARLIQDKIKRPLAEEILFGELAEhGGVVHIDIREGELV 746
Cdd:COG0542 782 KDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKE-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: 694.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 10 LNLAFKEARSKRHEFMTVEHLLLALLDNEA--AATVLRACGANLDKLKHDLQEFIDSttpLIPVHDEDRETQPTLGFQRV 87
Cdd:TIGR03346 9 LQAAQSLALGRDHQQIEPEHLLKALLDQEGglARPLLQKAGVNVGALRQALEKELER---LPKVSGPGGQVYLSPDLNRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 88 LQRAVFHVQSSGKREVTGANVLVAIFSEQESQAVfLLKQQSVARIDVvnyiahgiskvpghgehsdgEQDMQDEEGGETS 167
Cdd:TIGR03346 86 LNLAEKLAQKRGDEFISSEHLLLALLDDKGTLGK-LLKEAGATADAL--------------------EAAINAVRGGQKV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 168 SSGNP------LDAYASNLNEQARQGRIDPLVGRELEVERVAQILARRRKNNPLLVGEAGVGKTAIAEGLAKRIVDGQVP 241
Cdd:TIGR03346 145 TDANAedqyeaLEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 242 DLLAQSVVYSLDLGALLAGTKYRGDFEKRFKALLGELKKRP-QAILFIDEIHTIIGAGAAsGGVMDASNLLKPLLSSGDI 320
Cdd:TIGR03346 225 EGLKNKRLLALDMGALIAGAKYRGEFEERLKAVLNEVTKSEgQIILFIDELHTLVGAGKA-EGAMDAGNMLKPALARGEL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 321 RCIGSTTFQEFRGIFEKDRALARRFQKVDVSEPSVEDTVGILRGLKGRFESHHNIEYSDEALRAAAELAARYINDRHMPD 400
Cdd:TIGR03346 304 HCIGATTLDEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPD 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 401 KAIDVIDEAGAYQRLQ----PVEM---------------------------RVKRID----------------------- 426
Cdd:TIGR03346 384 KAIDLIDEAAARIRMEidskPEELdeldrriiqleierealkkekdeaskkRLEDLEkeladleeeyaeleeqwkaekas 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 427 -------------------------------------VPQVE----------------------------DIVAKIARIP 441
Cdd:TIGR03346 464 iqgiqqikeeieqvrleleqaeregdlakaaelqygkLPELEkqlqaaeqklgeeqnrllreevtaeeiaEVVSRWTGIP 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 442 PKHVTSSDKELLRNLERDLKLTVFGQDAAIDSLATAIKLSRAGLKSPDKPVGSFLFAGPTGVGKTEAARQLAKAL---GV 518
Cdd:TIGR03346 544 VSKMLEGEREKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLfdsED 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 519 ELVRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTEAITKQPHCVLLLDEIEKAHPEVFNLLLQVMDHGTLTDNNGRKA 598
Cdd:TIGR03346 624 AMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTV 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 599 DFRNVIVIMTTNAGAETAARASIGFTQQDHSSDAMEVIKKSFTPEFRNRLDTIIQFGRLSHETIKSVVDKFLIELQAQLE 678
Cdd:TIGR03346 704 DFRNTVIIMTSNLGSDFIQELAGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLA 783
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1944675807 679 DKRVLLEVSDAARSWLAAGGYDAMMGARPMARLIQDKIKRPLAEEILFGELAEhGGVVHIDIREGELV 746
Cdd:TIGR03346 784 ERKITLELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAP-GDTIRVDVEGGRLV 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: 654.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 12 LAFKEARSKRHEFMTVEHLLLALL--DNEAAATVLRACGANLDKLKHDLQE-------FIDSTTPLIPvhdedRETqptl 82
Cdd:CHL00095 15 LSQEEARRLGHNFVGTEQILLGLIgeGTGIAARALKSMGVTLKDARIEVEKiigrgtgFVAVEIPFTP-----RAK---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 83 gfqRVLQRAVFHVQSSGKREVTGANVLVAIFSEQESQAVFLLKQQSVARIDVVNYIAHGIskvpghgehsdgEQDMQDEE 162
Cdd:CHL00095 86 ---RVLEMSLEEARDLGHNYIGTEHLLLALLEEGEGVAARVLENLGVDLSKIRSLILNLI------------GEIIEAIL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 163 GGETSSSGNP-LDAYASNLNEQARQGRIDPLVGRELEVERVAQILARRRKNNPLLVGEAGVGKTAIAEGLAKRIVDGQVP 241
Cdd:CHL00095 151 GAEQSRSKTPtLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 242 DLLAQSVVYSLDLGALLAGTKYRGDFEKRFKALLGELKKRPQAILFIDEIHTIIGAGAASGGVmDASNLLKPLLSSGDIR 321
Cdd:CHL00095 231 DILEDKLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAAEGAI-DAANILKPALARGELQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 322 CIGSTTFQEFRGIFEKDRALARRFQKVDVSEPSVEDTVGILRGLKGRFESHHNIEYSDEALRAAAELAARYINDRHMPDK 401
Cdd:CHL00095 310 CIGATTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 402 AIDVIDEAGAYQRL--------------------------------------QPVEMRVK----------------RIDV 427
Cdd:CHL00095 390 AIDLLDEAGSRVRLinsrlppaareldkelreilkdkdeaireqdfetakqlRDREMEVRaqiaaiiqskkteeekRLEV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 428 PQV--EDIVAKIA---RIPPKHVTSSDKELLRNLERDLKLTVFGQDAAIDSLATAIKLSRAGLKSPDKPVGSFLFAGPTG 502
Cdd:CHL00095 470 PVVteEDIAEIVSawtGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTG 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 503 VGKTEAARQLAKAL-GVE--LVRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTEAITKQPHCVLLLDEIEKAHPEVFN 579
Cdd:CHL00095 550 VGKTELTKALASYFfGSEdaMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFN 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 580 LLLQVMDHGTLTDNNGRKADFRNVIVIMTTNAGAETAAR--ASIGF----TQQDHSSDAM------EVIKKSFTPEFRNR 647
Cdd:CHL00095 630 LLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSKVIETnsGGLGFelseNQLSEKQYKRlsnlvnEELKQFFRPEFLNR 709
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1944675807 648 LDTIIQFGRLSHETIKSVVDKFLIELQAQLEDKRVLLEVSDAARSWLAAGGYDAMMGARPMARLIQDKIKRPLAEEIL 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: 558.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 12 LAFKEARS----KRHEFMTVEHLLLALLDNEAAAT--VLRACGANLDKLKHDLQEFIDSttpLIPVHDEDRETQPTLGFQ 85
Cdd:PRK10865 12 LALADAQSlalgHDNQFIEPLHLMSALLNQEGGSVrpLLTSAGINAGQLRTDINQALSR---LPQVEGTGGDVQPSQDLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 86 RVLQRAVFHVQSSGKREVTGANVLVAIFsEQESQAVFLLKQQSVARidvvNYIAHGISKVPGhgehsdGEQdmQDEEGGE 165
Cdd:PRK10865 89 RVLNLCDKLAQKRGDNFISSELFVLAAL-ESRGTLADILKAAGATT----ANITQAIEQMRG------GES--VNDQGAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 166 TSSSGnpLDAYASNLNEQARQGRIDPLVGRELEVERVAQILARRRKNNPLLVGEAGVGKTAIAEGLAKRIVDGQVPDLLA 245
Cdd:PRK10865 156 DQRQA--LKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 246 QSVVYSLDLGALLAGTKYRGDFEKRFKALLGEL-KKRPQAILFIDEIHTIIGAGAASGGvMDASNLLKPLLSSGDIRCIG 324
Cdd:PRK10865 234 GRRVLALDMGALVAGAKYRGEFEERLKGVLNDLaKQEGNVILFIDELHTMVGAGKADGA-MDAGNMLKPALARGELHCVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 325 STTFQEFRGIFEKDRALARRFQKVDVSEPSVEDTVGILRGLKGRFESHHNIEYSDEALRAAAELAARYINDRHMPDKAID 404
Cdd:PRK10865 313 ATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAID 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 405 VIDEAGAYQRLQ---------PVEMRV-------------------KRID------------------------------ 426
Cdd:PRK10865 393 LIDEAASSIRMQidskpeeldRLDRRIiqlkleqqalmkesdeaskKRLDmlneelsdkerqyseleeewkaekaslsgt 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 427 ---------------------------------VPQVE---------------------------DIVAKIARIPPKHVT 446
Cdd:PRK10865 473 qtikaeleqakiaieqarrvgdlarmselqygkIPELEkqlaaatqlegktmrllrnkvtdaeiaEVLARWTGIPVSRML 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 447 SSDKELLRNLERDLKLTVFGQDAAIDSLATAIKLSRAGLKSPDKPVGSFLFAGPTGVGKTEAARQLAKAL---GVELVRF 523
Cdd:PRK10865 553 ESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMfdsDDAMVRI 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 524 DMSEYMERHTVSRLIGAPPGYVGFDQGGLLTEAITKQPHCVLLLDEIEKAHPEVFNLLLQVMDHGTLTDNNGRKADFRNV 603
Cdd:PRK10865 633 DMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNT 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 604 IVIMTTNAGAETAARASIGFTQQDHSSDAMEVIKKSFTPEFRNRLDTIIQFGRLSHETIKSVVDKFLIELQAQLEDKRVL 683
Cdd:PRK10865 713 VVIMTSNLGSDLIQERFGELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYE 792
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1944675807 684 LEVSDAARSWLAAGGYDAMMGARPMARLIQDKIKRPLAEEILFGELAEhGGVVHIDIREGELV 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, ... |
2-740 |
6.37e-178 |
|
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: 531.06 E-value: 6.37e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 2 LNRELEVTLNLAFKEARSKRHEFMTVEHLLLALLDNEA--AATVLRACGANLDKLKHDLQEFID------STTPLIPVHd 73
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDsdLAAILRHFGVDLGRLKADLARALDklprgnTRTPVFSPH- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 74 edretqptlgFQRVLQRAvFHVQSS--GKREVTGANVLVAIFSEQESQAVFLLKQQSVARIDVVNYIAHGISKVPGHGEH 151
Cdd:TIGR03345 80 ----------LVELLQEA-WLLASLelGDGRIRSGHLLLALLTDPELRRLLGSISPELAKIDREALREALPALVEGSAEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 152 SDGEQDMQDEEGGETSSSGNPLDAYASNLNEQARQGRIDPLVGRELEVERVAQILARRRKNNPLLVGEAGVGKTAIAEGL 231
Cdd:TIGR03345 149 SAAAADAAPAGAAAGAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 232 AKRIVDGQVPDLLAQSVVYSLDLGALLAGTKYRGDFEKRFKALLGELKKRPQA-ILFIDEIHTIIGAGAASGGvMDASNL 310
Cdd:TIGR03345 229 ALRIAAGDVPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPiILFIDEAHTLIGAGGQAGQ-GDAANL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 311 LKPLLSSGDIRCIGSTTFQEFRGIFEKDRALARRFQKVDVSEPSVEDTVGILRGLKGRFESHHNIEYSDEALRAAAELAA 390
Cdd:TIGR03345 308 LKPALARGELRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSH 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 391 RYINDRHMPDKAIDVIDEAGA----------------YQRLQPVEMR--------------------------------- 421
Cdd:TIGR03345 388 RYIPGRQLPDKAVSLLDTACArvalsqnatpaaledlRRRIAALELEldalereaalgadhderlaelraelaaleaela 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 422 ------------VKRI----------------------------------------------DVPQVEDIVAKIARIPPK 443
Cdd:TIGR03345 468 alearwqqekelVEAIlalraeleadadapaddddalraqlaeleaalasaqgeeplvfpevDAQAVAEVVADWTGIPVG 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 444 HVTSSDKELLRNLERDLKLTVFGQDAAIDSLATAIKLSRAGLKSPDKPVGSFLFAGPTGVGKTEAARQLAKAL-GVE--L 520
Cdd:TIGR03345 548 RMVRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLyGGEqnL 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 521 VRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTEAITKQPHCVLLLDEIEKAHPEVFNLLLQVMDHGTLTDNNGRKADF 600
Cdd:TIGR03345 628 ITINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDF 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 601 RNVIVIMTTNAGAETAARASIgftQQDHSSDAMEVIK-------KSFTPEFRNRLdTIIQFGRLSHETIKSVVDKFLIEL 673
Cdd:TIGR03345 708 KNTVILLTSNAGSDLIMALCA---DPETAPDPEALLEalrpellKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRI 783
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1944675807 674 QAQLEDK-RVLLEVSDAARSWLAAGGYDAMMGARPMARLIQDKIKRPLAEEILfGELAEHGGVVHIDI 740
Cdd:TIGR03345 784 ARRLKENhGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQIL-ERLAAGEPIERIHL 850
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
453-654 |
1.77e-85 |
|
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: 267.89 E-value: 1.77e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 453 LRNLERDLKLTVFGQDAAIDSLATAIKLSRAGLKSPDKPVGSFLFAGPTGVGKTEAARQLAKAL---GVELVRFDMSEYM 529
Cdd:cd19499 2 LLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMSEYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 530 ERHTVSRLIGAPPGYVGFDQGGLLTEAITKQPHCVLLLDEIEKAHPEVFNLLLQVMDHGTLTDNNGRKADFRNVIVIMTT 609
Cdd:cd19499 82 EKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTS 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1944675807 610 NAgaetaarasigftqqdhssdamevikksFTPEFRNRLDTIIQF 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 |
9.45e-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: 249.80 E-value: 9.45e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 490 KPVGSFLFAGPTGVGKTEAARQLAKALGV---ELVRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTEAITKQPHCVLL 566
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 567 LDEIEKAHPEVFNLLLQVMDHGTLTDNNGRKADFRNVIVIMTTNAGAE---TAARASIGFTQQDHSSDAMEVIKKSFTPE 643
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEkisDASRLGDSPDYELLKEEVMDLLKKGFIPE 160
|
....*...
gi 1944675807 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 |
5.78e-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: 5.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 657 LSHETIKSVVDKFLIELQAQLEDKRVLLEVSDAARSWLAAGGYDAMMGARPMARLIQDKIKRPLAEEILFGELAEhGGVV 736
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKE-GDTV 79
|
..
gi 1944675807 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 |
2.59e-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: 102.91 E-value: 2.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 657 LSHETIKSVVDKFLIELQAQLEDKRVLLEVSDAARSWLAAGGYDAMMGARPMARLIQDKIKRPLAEEILFGELAEhGGVV 736
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKD-GDTV 79
|
90
....*....|.
gi 1944675807 737 HIDIREGELVF 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 |
1.14e-22 |
|
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: 93.32 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 354 SVEDTVGILRGLKGRFESHHNIEYSDEALRAAAELAARYINDRHMPDKAIDVIDEAGAYQRLQpveMRVKRIDVPQVEDI 433
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLS---QESKPEELEDLERE 77
|
90 100
....*....|....*....|....*
gi 1944675807 434 VAKIARIPPKHVTSSDKELLRNLER 458
Cdd:pfam17871 78 LAKLEIEKEALEREQDFEKAERLAK 102
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
193-348 |
8.21e-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: 86.82 E-value: 8.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 193 VGRELEVERVAQILARRRKNNPLLVGEAGVGKTAIAEGLAKRIVDGQVPdllaqsvVYSLDLGALLAGTKYRGDFE-KRF 271
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGhFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1944675807 272 KALLGELKKRPQAILFIDEIHTIigAGAASGGVMDASNLLKPLL-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 |
1.33e-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: 77.57 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 465 FGQDAAIDSLATAIKLsraglkspdKPVGSFLFAGPTGVGKTEAARQLAKAL---GVELVRFDMSEYMERHTVSRLIgap 541
Cdd:cd00009 1 VGQEEAIEALREALEL---------PPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELF--- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1944675807 542 pgyvGFDQGGLLTEAITKQPHCVLLLDEIEKAHPEVFNLLLQVMDHGtltdnNGRKADFRNVIVIMTTN 610
Cdd:cd00009 69 ----GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETL-----NDLRIDRENVRVIGATN 128
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
215-348 |
8.05e-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: 68.77 E-value: 8.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 215 LLVGEAGVGKTAIAEGLAKRIvdgQVPdllaqsvVYSLDLGALLAgtKYRGDFEKRFKALLGELKKRPQAILFIDEIHTI 294
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKEL---GAP-------FIEISGSELVS--KYVGESEKRLRELFEAAKKLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1944675807 295 IGAGAASGG--VMDASNLLKPLL-----SSGDIRCIGSTTFqefrgIFEKDRALARRFQKV 348
Cdd:pfam00004 70 AGSRGSGGDseSRRVVNQLLTELdgftsSNSKVIVIAATNR-----PDKLDPALLGRFDRI 125
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
494-610 |
1.03e-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: 68.47 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 494 SFLFAGPTGVGKTEAARQLAKAL-GVELVRFDMSEYMerhTVSRLIGA---PPGYVGFDQGGLLTEAITKqphCVLLLDE 569
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDT---TEEDLFGRrniDPGGASWVDGPLVRAAREG---EIAVLDE 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1944675807 570 IEKAHPEVFNLLLQVMDHGTLTDNNGR---KADFRNVIVIMTTN 610
Cdd:pfam07728 75 INRANPDVLNSLLSLLDERRLLLPDGGelvKAAPDGFRLIATMN 118
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
469-610 |
1.04e-13 |
|
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: 69.23 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 469 AAIDSLATAIKLSRAGLKSPDKPVGSFLFAGPTGVGKTEAARQLAKALGVELVRFDMSEYMERHTvsrligappGYVGfD 548
Cdd:cd19481 3 ASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYV---------GESE-K 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1944675807 549 QGGLLTEAITKQPHCVLLLDEIEKA------------HPEVFNLLLQVMDHGTLTDnngrkadfrNVIVIMTTN 610
Cdd:cd19481 73 NLRKIFERARRLAPCILFIDEIDAIgrkrdssgesgeLRRVLNQLLTELDGVNSRS---------KVLVIAATN 137
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
496-656 |
1.10e-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: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 496 LFAGPTGVGKTEAARQLAKALGVELVRFDMSEymerhTVSRLIGAPPGYVgfdqGGLLTEAITKQPhCVLLLDEIEKAHP 575
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSE-----LVSKYVGESEKRL----RELFEAAKKLAP-CVIFIDEIDALAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 576 -----------EVFNLLLQVMDhgtltdnnGRKADFRNVIVIMTTNagaetaarasigftqqdhssdamevIKKSFTPEF 644
Cdd:pfam00004 72 srgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN-------------------------RPDKLDPAL 118
|
170
....*....|..
gi 1944675807 645 RNRLDTIIQFGR 656
Cdd:pfam00004 119 LGRFDRIIEFPL 130
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
13-63 |
2.70e-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: 59.07 E-value: 2.70e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1944675807 13 AFKEARSKRHEFMTVEHLLLALLDNE--AAATVLRACGANLDKLKHDLQEFID 63
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDdgLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
496-621 |
1.98e-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: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 496 LFAGPTGVGKTEAARQLAKALGVE---LVRFDMSEYMERHTVSRL-IGAPPGYVGFDQGGLLTEAIT---KQPHCVLLLD 568
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVLDQLLlIIVGGKKASGSGELRLRLALAlarKLKPDVLILD 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1944675807 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 |
2.95e-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: 62.11 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 448 SDKELLRNLERDlkltVFGQDAAIDSLATAIKLsraglkspDKPVgsfLFAGPTGVGKTEAARQLAKALGVELVRF---- 523
Cdd:COG0714 2 TEARLRAEIGKV----YVGQEELIELVLIALLA--------GGHL---LLEGVPGVGKTTLAKALARALGLPFIRIqftp 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 524 DMseymerhTVSRLIG---APPGYVGF--DQGGLLTeaitkqphCVLLLDEIEKAHPEVFNLLLQVMDHGTLT-DNNGRK 597
Cdd:COG0714 67 DL-------LPSDILGtyiYDQQTGEFefRPGPLFA--------NVLLADEINRAPPKTQSALLEAMEERQVTiPGGTYK 131
|
170
....*....|...
gi 1944675807 598 ADFRnVIVIMTTN 610
Cdd:COG0714 132 LPEP-FLVIATQN 143
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
210-348 |
3.21e-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: 58.92 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 210 RKNNPLLVGEAGVGKTAIAEGLAKRIVDGQVPDLLA-----QSVVYSLDLGALLAGTKYRGDFEKRFKALLGELKKRPQA 284
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIdgediLEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1944675807 285 ILFIDEIHTIIGA-GAASGGVMDASNLLKPLLSSGDIRCIGSTTfqefRGIFEKDRALARRFQKV 348
Cdd:smart00382 81 VLILDEITSLLDAeQEALLLLLEELRLLLLLKSEKNLTVILTTN----DEKDLGPALLRRRFDRR 141
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
490-670 |
1.41e-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: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 490 KPVGSFLFAGPTGVGKTEAARQLAKALGVELVRFDMSEymerhtvsrLIGappGYVGfdqgglLTEAITKQ--------P 561
Cdd:COG0464 189 PPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSD---------LVS---KYVG------ETEKNLREvfdkarglA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 562 HCVLLLDEIEKAHP-----------EVFNLLLQVMDhgtltdnngrkaDFR-NVIVIMTTNAgaetaarasigFTQQDhs 629
Cdd:COG0464 251 PCVLFIDEADALAGkrgevgdgvgrRVVNTLLTEME------------ELRsDVVVIAATNR-----------PDLLD-- 305
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1944675807 630 sdamevikksftPEFRNRLDTIIQFGRLSHETIKSVVDKFL 670
Cdd:COG0464 306 ------------PALLRRFDEIIFFPLPDAEERLEIFRIHL 334
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
38-363 |
2.86e-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: 59.92 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 38 EAAATVLRACGANLDKLKHDLQEFIDSTTPLIPVHDEDRETQPTLGFQRVLQRAVFHVQSSGKREVTGANVLVAIFSEQE 117
Cdd:COG0464 5 LALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 118 SQAVFLLKQQSVARIDVVNYIAHGISKVPGHGEHSDGEQDMQDEEGGETSSSGNPLDAYASNLNEQARQGRIDPLVGREL 197
Cdd:COG0464 85 LLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 198 EVERVAQILARRRKNNP-------------LLVGEAGVGKTAIAEGLAKRIvdgQVPdllaqsvVYSLDLGALLAgtKYR 264
Cdd:COG0464 165 VKEELRELVALPLKRPElreeyglppprglLLYGPPGTGKTLLARALAGEL---GLP-------LIEVDLSDLVS--KYV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 265 GDFEKRFKALLGELKKRPQAILFIDEIHTIIGA-GAASGGVMDA--SNLLKPL-LSSGDIRCIGSTTFqefrgIFEKDRA 340
Cdd:COG0464 233 GETEKNLREVFDKARGLAPCVLFIDEADALAGKrGEVGDGVGRRvvNTLLTEMeELRSDVVVIAATNR-----PDLLDPA 307
|
330 340
....*....|....*....|....
gi 1944675807 341 LARRFQ-KVDVSEPSVEDTVGILR 363
Cdd:COG0464 308 LLRRFDeIIFFPLPDAEERLEIFR 331
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
215-348 |
3.13e-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: 53.44 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 215 LLVGEAGVGKTAIAEGLAKRIVdgqvpdllaqSVVYSLDLGALLagTKYRGDFEKRFKALLGELKKRPQAILFIDEIHTI 294
Cdd:cd19481 30 LLYGPPGTGKTLLAKALAGELG----------LPLIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDAI 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1944675807 295 IGAGAASGGVMDAS-------NLLKPLLSSGDIRCIGSTTFQEfrgifEKDRALAR--RFQKV 348
Cdd:cd19481 98 GRKRDSSGESGELRrvlnqllTELDGVNSRSKVLVIAATNRPD-----LLDPALLRpgRFDEV 155
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
190-363 |
4.18e-08 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 54.89 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 190 DPLVGRELEVERVAQILA-RRRKNNP-----------LLVGEAGVGKTAIAEGLAKRIvdgQVPdllaqsvVYSLDLGAL 257
Cdd:COG1223 2 DDVVGQEEAKKKLKLIIKeLRRRENLrkfglwpprkiLFYGPPGTGKTMLAEALAGEL---KLP-------LLTVRLDSL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 258 LagTKYRGDFEKRFKALLGELKKRPqAILFIDEIHTIigagaasGGVMDASNLlkpllsSGDIRCIGSTTFQEFRGIFEK 337
Cdd:COG1223 72 I--GSYLGETARNLRKLFDFARRAP-CVIFFDEFDAI-------AKDRGDQND------VGEVKRVVNALLQELDGLPSG 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1944675807 338 -------------DRALARRFQ-KVDVSEPSVEDTVGILR 363
Cdd:COG1223 136 svviaatnhpellDSALWRRFDeVIEFPLPDKEERKEILE 175
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
464-610 |
1.41e-07 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 53.35 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 464 VFGQDAAIDSLATAIK-------LSRAGLKSPDKpvgsFLFAGPTGVGKTEAARQLAKALGVEL--VRFD--MSEYMERh 532
Cdd:COG1223 4 VVGQEEAKKKLKLIIKelrrrenLRKFGLWPPRK----ILFYGPPGTGKTMLAEALAGELKLPLltVRLDslIGSYLGE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 533 TVSRLigappgyvgfdqgGLLTEAITKQPhCVLLLDEIE---------KAHPE---VFNLLLQVMDhgtltdnnGRKadf 600
Cdd:COG1223 79 TARNL-------------RKLFDFARRAP-CVIFFDEFDaiakdrgdqNDVGEvkrVVNALLQELD--------GLP--- 133
|
170
....*....|
gi 1944675807 601 RNVIVIMTTN 610
Cdd:COG1223 134 SGSVVIAATN 143
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
496-572 |
6.98e-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: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 496 LFAGPTGVGKTEAARQLAKALGVELVRF------DMSEYM-ERHTvsrLIGAPPGYVgfDQGglLTEAITKQPhcVLLLD 568
Cdd:cd19500 41 CLVGPPGVGKTSLGKSIARALGRKFVRIslggvrDEAEIRgHRRT---YVGAMPGRI--IQA--LKKAGTNNP--VFLLD 111
|
....
gi 1944675807 569 EIEK 572
Cdd:cd19500 112 EIDK 115
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
464-516 |
1.42e-06 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 50.96 E-value: 1.42e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1944675807 464 VFGQDAAIDSLATAIKLSR---AglkspdkpvgsFLFAGPTGVGKTEAARQLAKAL 516
Cdd:COG2812 12 VVGQEHVVRTLKNALASGRlahA-----------YLFTGPRGVGKTTLARILAKAL 56
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
191-292 |
1.67e-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: 48.65 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 191 PLVGRELEVERVAQILARRRKNNP---LLVGEAGVGKTAIAEGLAKRIVD--------------------------GQVP 241
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERdggyflrgkcdenlpyspllealtreGLLR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1944675807 242 DLLAQSVVYSLD------LGALLAGTKYRGDFEKRFKALLGEL-----KKRPQAILFIDEIH 292
Cdd:pfam13191 81 QLLDELESSLLEawraalLEALAPVPELPGDLAERLLDLLLRLldllaRGERPLVLVLDDLQ 142
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
192-291 |
2.32e-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: 50.17 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 192 LVGRELEVERV-AQILARRrknnPLLV-GEAGVGKTAIAEGLAkRIVDGQV------PDLLAQSVVYSLDLGallagtKY 263
Cdd:COG0714 14 YVGQEELIELVlIALLAGG----HLLLeGVPGVGKTTLAKALA-RALGLPFiriqftPDLLPSDILGTYIYD------QQ 82
|
90 100 110
....*....|....*....|....*....|
gi 1944675807 264 RGDFekrfkallgELKKRP--QAILFIDEI 291
Cdd:COG0714 83 TGEF---------EFRPGPlfANVLLADEI 103
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
215-347 |
1.15e-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: 46.19 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 215 LLVGEAGVGKTAIAEGLAKRIvdgqvpdllaQSVVYSLDLGALLAgtKYRGDFEKRFKALLGELKKRPQAILFIDEIHTI 294
Cdd:cd19509 36 LLYGPPGTGKTLLARAVASES----------GSTFFSISASSLVS--KWVGESEKIVRALFALARELQPSIIFIDEIDSL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1944675807 295 I---GAGAASGGVMDASNLLKPL-----LSSGDIRCIGSTTFqefrgIFEKDRALARRFQK 347
Cdd:cd19509 104 LserGSGEHEASRRVKTEFLVQMdgvlnKPEDRVLVLGATNR-----PWELDEAFLRRFEK 159
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
215-363 |
1.66e-05 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 47.69 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 215 LLVGEAGVGKTAIAEGLAKRivdgqvpdllAQSVVYSLDLGALLagTKYRGDFEKRFKALLGELKKRPQAILFIDEIHTI 294
Cdd:COG1222 116 LLYGPPGTGKTLLAKAVAGE----------LGAPFIRVRGSELV--SKYIGEGARNVREVFELAREKAPSIIFIDEIDAI 183
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1944675807 295 IGAGAASGGVMDASNLLKPLL-------SSGDIRCIGSTTFQEfrgifEKDRALAR--RF-QKVDVSEPSVEDTVGILR 363
Cdd:COG1222 184 AARRTDDGTSGEVQRTVNQLLaeldgfeSRGDVLIIAATNRPD-----LLDPALLRpgRFdRVIEVPLPDEEAREEILK 257
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
454-572 |
2.73e-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: 45.45 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 454 RNLERDLKLTVFGQDAAIDSLATAIK------LSRAGLKSPDKPvGSFLFAGPTGVGKTEAARQLAKALGVELVRFDMSE 527
Cdd:cd19498 3 REIVSELDKYIIGQDEAKRAVAIALRnrwrrmQLPEELRDEVTP-KNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATK 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1944675807 528 YMErhtvsrligapPGYVGFDQGGL---LTEAItkqphcvLLLDEIEK 572
Cdd:cd19498 82 FTE-----------VGYVGRDVESIirdLVEGI-------VFIDEIDK 111
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
402-610 |
3.32e-05 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 46.54 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 402 AIDVIDEAGAYQRLQPVEMRVKRIDVPQVEDIVAKIARIPpkhvtSSDKELLRNLERDLKLT---VFGQDAAIDSLATAI 478
Cdd:COG1222 20 ALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKR-----LGTPRGTAVPAESPDVTfddIGGLDEQIEEIREAV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 479 KLSragLKSPD-------KPVGSFLFAGPTGVGKTEAARQLAKALGVELVRFDMSEYMERhtvsrligappgYVGfdQGG 551
Cdd:COG1222 95 ELP---LKNPElfrkygiEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK------------YIG--EGA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1944675807 552 -----LLTEAITKQPhCVLLLDEIE---------KAHPEV---FNLLLQVMDhgTLTDNNgrkadfrNVIVIMTTN 610
Cdd:COG1222 158 rnvreVFELAREKAP-SIIFIDEIDaiaarrtddGTSGEVqrtVNQLLAELD--GFESRG-------DVLIIAATN 223
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
493-586 |
5.94e-05 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 43.48 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 493 GSFLFAGPTGVGKTEAARQLAKAL---GVELVRFDMSEYME----RHTVSRLIGAPPgyVGFDQGGLLTEAITKQ----- 560
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLpevRDSVVFVDLPSGTSpkdlLRALLRALGLPL--SGRLSKEELLAALQQLllala 83
|
90 100
....*....|....*....|....*.
gi 1944675807 561 PHCVLLLDEIEKAHPEVFNLLLQVMD 586
Cdd:pfam13401 84 VAVVLIIDEAQHLSLEALEELRDLLN 109
|
|
| PRK14953 |
PRK14953 |
DNA polymerase III subunits gamma and tau; Provisional |
464-516 |
1.02e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237867 [Multi-domain] Cd Length: 486 Bit Score: 45.58 E-value: 1.02e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1944675807 464 VFGQDAAIDSLATAIKLsraglkspDKPVGSFLFAGPTGVGKTEAARQLAKAL 516
Cdd:PRK14953 18 VIGQEIVVRILKNAVKL--------QRVSHAYIFAGPRGTGKTTIARILAKVL 62
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
464-654 |
1.63e-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: 44.13 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 464 VFGQDAAIDSLATAI----KLSRAGLKSPDKPV----GSFLFAGPTGVGKTEAARQLAKALGVELVRFDMSEYMErhtvs 535
Cdd:cd19497 14 VIGQERAKKVLSVAVynhyKRIRNNLKQKDDDVelekSNILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTE----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 536 rligapPGYVGFDQGG----LLTEA---ITKQPHCVLLLDEIEK-----AHPE---------VFNLLLQVMDhGTL---T 591
Cdd:cd19497 89 ------AGYVGEDVENillkLLQAAdydVERAQRGIVYIDEIDKiarksENPSitrdvsgegVQQALLKILE-GTVanvP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 592 DNNGRKADFRNVIVIMTTN-----AGA-----ETAAR----ASIGFTQQDHSSDAME-------------VIKKSFTPEF 644
Cdd:cd19497 162 PQGGRKHPQQEFIQVDTTNilficGGAfvgleKIIARrlgkKSLGFGAETSSEKDEKerdellskvepedLIKFGLIPEF 241
|
250
....*....|
gi 1944675807 645 RNRLDTIIQF 654
Cdd:cd19497 242 VGRLPVIVTL 251
|
|
| PRK14965 |
PRK14965 |
DNA polymerase III subunits gamma and tau; Provisional |
466-519 |
2.40e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237871 [Multi-domain] Cd Length: 576 Bit Score: 44.35 E-value: 2.40e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1944675807 466 GQDAAIDSLATAIKLSRAGlkspdkpvGSFLFAGPTGVGKTEAARQLAKALGVE 519
Cdd:PRK14965 20 GQEHVSRTLQNAIDTGRVA--------HAFLFTGARGVGKTSTARILAKALNCE 65
|
|
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
496-572 |
2.68e-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: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 496 LFAGPTGVGKTEAARQLAKALGVELVRF------DMSE-------YmerhtvsrlIGAPPGyvGFDQGglLTEAITKQPh 562
Cdd:COG0466 356 CLVGPPGVGKTSLGKSIARALGRKFVRIslggvrDEAEirghrrtY---------IGAMPG--RIIQG--LKKAGTKNP- 421
|
90
....*....|
gi 1944675807 563 cVLLLDEIEK 572
Cdd:COG0466 422 -VFLLDEIDK 430
|
|
| PRK06647 |
PRK06647 |
DNA polymerase III subunits gamma and tau; Validated |
463-516 |
2.69e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 235845 [Multi-domain] Cd Length: 563 Bit Score: 44.38 E-value: 2.69e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1944675807 463 TVFGQDAAIDSLATAIklsraglkSPDKPVGSFLFAGPTGVGKTEAARQLAKAL 516
Cdd:PRK06647 17 SLEGQDFVVETLKHSI--------ESNKIANAYIFSGPRGVGKTSSARAFARCL 62
|
|
| PRK11331 |
PRK11331 |
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional |
494-648 |
3.46e-04 |
|
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
Pssm-ID: 183088 [Multi-domain] Cd Length: 459 Bit Score: 43.92 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 494 SFLFAGPTGVGKTEAARQLAKALGVELV--RFDMSEYMERHTVSRLI-GAPPGYVGF-DQGGL---LTEAITKQPH--CV 564
Cdd:PRK11331 196 NIILQGPPGVGKTFVARRLAYLLTGEKApqRVNMVQFHQSYSYEDFIqGYRPNGVGFrRKDGIfynFCQQAKEQPEkkYV 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 565 LLLDEIEKAH-PEVFNLLLQVMDHGT--------LTDNNGRKADF---RNVIVIMTTNAGAETAARASIGFTQQDHSSDa 632
Cdd:PRK11331 276 FIIDEINRANlSKVFGEVMMLMEHDKrgenwsvpLTYSENDEERFyvpENVYIIGLMNTADRSLAVVDYALRRRFSFID- 354
|
170
....*....|....*..
gi 1944675807 633 mevIKKSF-TPEFRNRL 648
Cdd:PRK11331 355 ---IEPGFdTPQFRNFL 368
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
463-516 |
3.88e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 44.00 E-value: 3.88e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1944675807 463 TVFGQDAAIDSLATAI---KLSRAglkspdkpvgsFLFAGPTGVGKTEAARQLAKAL 516
Cdd:PRK14971 18 SVVGQEALTTTLKNAIatnKLAHA-----------YLFCGPRGVGKTTCARIFAKTI 63
|
|
| PRK06305 |
PRK06305 |
DNA polymerase III subunits gamma and tau; Validated |
464-516 |
5.15e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 180523 [Multi-domain] Cd Length: 451 Bit Score: 43.22 E-value: 5.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1944675807 464 VFGQDAAIDSLATAIKLSRAGlkspdkpvGSFLFAGPTGVGKTEAARQLAKAL 516
Cdd:PRK06305 19 ILGQDAVVAVLKNALRFNRAA--------HAYLFSGIRGTGKTTLARIFAKAL 63
|
|
| RecA-like_spastin |
cd19524 |
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ... |
215-347 |
7.99e-04 |
|
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: 40.99 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 215 LLVGEAGVGKTAIAEGLAkrivdgqvpdllAQSVVYSLDLGALLAGTKYRGDFEKRFKALLGELKKRPQAILFIDEIHTI 294
Cdd:cd19524 37 LLFGPPGNGKTMLAKAVA------------AESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSL 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1944675807 295 IgaGAASGGVMDASNLLKP--------LLSSGDIRCI--GSTTFQEfrgifEKDRALARRFQK 347
Cdd:cd19524 105 L--SERSEGEHEASRRLKTefliefdgVQSNGDDRVLvmGATNRPQ-----ELDDAVLRRFTK 160
|
|
| 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 |
9.28e-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: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 215 LLVGEAGVGKTAIAEGLAkRIVDGQVPDLLAQSVVysldlgallagTKYRGDFEKRFKALLGELKKRPQAILFIDEIHTI 294
Cdd:cd19503 38 LLHGPPGTGKTLLARAVA-NEAGANFLSISGPSIV-----------SKYLGESEKNLREIFEEARSHAPSIIFIDEIDAL 105
|
90 100 110
....*....|....*....|....*....|....*...
gi 1944675807 295 IGAGAASGGVMDAS------NLLKPLLSSGDIRCIGST 326
Cdd:cd19503 106 APKREEDQREVERRvvaqllTLMDGMSSRGKVVVIAAT 143
|
|
| PRK14956 |
PRK14956 |
DNA polymerase III subunits gamma and tau; Provisional |
464-519 |
1.01e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184920 [Multi-domain] Cd Length: 484 Bit Score: 42.24 E-value: 1.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1944675807 464 VFGQDAAIDSLATAIKLSRAGlkspdkpvGSFLFAGPTGVGKTEAARQLAKALGVE 519
Cdd:PRK14956 20 VIHQDLAIGALQNALKSGKIG--------HAYIFFGPRGVGKTTIARILAKRLNCE 67
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
120-240 |
1.27e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.54 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 120 AVFLLKQQSVARIDVVNYIAHGISKVPGHGEHSDGEQDMQDEEGGETSSSGNPLDAYASNLNEQARQGRIDPLVGRELEV 199
Cdd:COG3899 217 AAAAAAAAAAAPAAPVVLVAALLLALAALLALLLLAARLLGLAGAAALLLLGLLAAAAAGRRLLARRLIPQPLVGREAEL 296
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1944675807 200 ERVAQILARRRKNNP---LLVGEAGVGKTAIAEGLAKRIVDGQV 240
Cdd:COG3899 297 AALLAALERARAGRGelvLVSGEAGIGKSRLVRELARRARARGG 340
|
|
| 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 |
1.59e-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: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 466 GQDAAIDSLATAIKLSragLKSPD-------KPVGSFLFAGPTGVGKTEAARQLAKALGVELVRFD----MSEYM-ERHT 533
Cdd:cd19503 4 GLDEQIASLKELIELP---LKYPElfralglKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISgpsiVSKYLgESEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 534 VSRLIGAppgyvgfdqgglltEAITKQPhCVLLLDEI-------EKAHPEVFN-LLLQVMdhgTLTDNNGRKadfRNVIV 605
Cdd:cd19503 81 NLREIFE--------------EARSHAP-SIIFIDEIdalapkrEEDQREVERrVVAQLL---TLMDGMSSR---GKVVV 139
|
....*
gi 1944675807 606 IMTTN 610
Cdd:cd19503 140 IAATN 144
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
464-515 |
1.74e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 41.72 E-value: 1.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1944675807 464 VFGQDAAIDSLATAIKLSRAGlkspdkpvGSFLFAGPTGVGKTEAARQLAKA 515
Cdd:PRK14950 18 LVGQEHVVQTLRNAIAEGRVA--------HAYLFTGPRGVGKTSTARILAKA 61
|
|
| 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
|
| 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 |
3.55e-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: 40.16 E-value: 3.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1944675807 474 LATAIKLSRAGlkSPdkpvgsflfAGPTGVGKTEAARQLAKALGVELVRFDMSEYM 529
Cdd:pfam12774 25 LTQALHLHLGG--AP---------AGPAGTGKTETVKDLAKALAKQVVVFNCSDGL 69
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
464-575 |
3.59e-03 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 40.67 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 464 VFGQDAAIDSLATAIKLSRAGlkSPDKPVgsfLFAGPTGVGKTEAARQLAKALGVELVRFDMSEYMERHTVSRLIGAppg 543
Cdd:PRK04195 16 VVGNEKAKEQLREWIESWLKG--KPKKAL---LLYGPPGVGKTSLAHALANDYGWEVIELNASDQRTADVIERVAGE--- 87
|
90 100 110
....*....|....*....|....*....|..
gi 1944675807 544 yvgfdqgGLLTEAITKQPHCVLLLDEIEKAHP 575
Cdd:PRK04195 88 -------AATSGSLFGARRKLILLDEVDGIHG 112
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
490-610 |
4.06e-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: 38.92 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 490 KPVGSFLFAGPTGVGKTEAARQLAKALGVELVRFDMSEymerhTVSRLIGAPPGYVgfdqGGLLTEAITKQPhCVLLLDE 569
Cdd:cd19518 32 EPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATE-----IVSGVSGESEEKI----RELFDQAISNAP-CIVFIDE 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1944675807 570 IEKAHPE-----------VFNLLLQVMDHGTLTDNNGRKadfrnVIVIMTTN 610
Cdd:cd19518 102 IDAITPKresaqremerrIVSQLLTCMDELNNEKTAGGP-----VLVIGATN 148
|
|
| RecA-like_VPS4 |
cd19521 |
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ... |
215-347 |
4.30e-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: 38.69 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 215 LLVGEAGVGKTAIAEGLAKRivdgqvpdllAQSVVYSLDLGALLagTKYRGDFEKRFKALLGELKKRPQAILFIDEIHTI 294
Cdd:cd19521 44 LLYGPPGTGKSYLAKAVATE----------ANSTFFSVSSSDLV--SKWMGESEKLVKQLFAMARENKPSIIFIDEVDSL 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1944675807 295 igAGAASGGVMDASNLLKPLL---------SSGDIRCIGSTTFQefrgiFEKDRALARRFQK 347
Cdd:cd19521 112 --CGTRGEGESEASRRIKTELlvqmngvgnDSQGVLVLGATNIP-----WQLDSAIRRRFEK 166
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
466-516 |
4.65e-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: 4.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1944675807 466 GQDAAIDSLATAIKlsraglksPDKPVGSFLFAGPTGVGKTEAARQLAKAL 516
Cdd:pfam13177 1 GQPEAIQLLQNSLE--------NGRLSHAYLFSGPEGVGKLELALAFAKAL 43
|
|
| PRK07399 |
PRK07399 |
DNA polymerase III subunit delta'; Validated |
459-516 |
4.93e-03 |
|
DNA polymerase III subunit delta'; Validated
Pssm-ID: 236011 [Multi-domain] Cd Length: 314 Bit Score: 39.88 E-value: 4.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1944675807 459 DLKLTVFGQDAAIDSLATAIKLSRAglkSPdkpvgSFLFAGPTGVGKTEAARQLAKAL 516
Cdd:PRK07399 1 NLFANLIGQPLAIELLTAAIKQNRI---AP-----AYLFAGPEGVGRKLAALCFIEGL 50
|
|
| TIGR02928 |
TIGR02928 |
orc1/cdc6 family replication initiation protein; Members of this protein family are found ... |
190-298 |
4.97e-03 |
|
orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 274354 [Multi-domain] Cd Length: 365 Bit Score: 39.92 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 190 DPLVGRELEVERVAQIL--ARR--RKNNPLLVGEAGVGKTAIAEGLAKRI---------------VDGQVPDLLAQSVVY 250
Cdd:TIGR02928 15 DRIVHRDEQIEELAKALrpILRgsRPSNVFIYGKTGTGKTAVTKYVMKELeeaaedrdvrvvtvyVNCQILDTLYQVLVE 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1944675807 251 sldLGALLAGTK----YRG-DFEKRFKALLGELKKRPQAILFI-DEIHTIIGAG 298
Cdd:TIGR02928 95 ---LANQLRGSGeevpTTGlSTSEVFRRLYKELNERGDSLIIVlDEIDYLVGDD 145
|
|
| PRK14948 |
PRK14948 |
DNA polymerase III subunit gamma/tau; |
466-516 |
5.63e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237862 [Multi-domain] Cd Length: 620 Bit Score: 39.95 E-value: 5.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1944675807 466 GQDAAIDSLATAIKLSRAglkSPdkpvgSFLFAGPTGVGKTEAARQLAKAL 516
Cdd:PRK14948 20 GQEAIATTLKNALISNRI---AP-----AYLFTGPRGTGKTSSARILAKSL 62
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
496-573 |
5.90e-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: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 496 LFAGPTGVGKTEAARQLAKALGVELVRFDMseymerhtvSRLIGappGYVG-----FDQGGLLTEAITKqphCVLLLDEI 570
Cdd:cd19507 35 LLVGIQGTGKSLTAKAIAGVWQLPLLRLDM---------GRLFG---GLVGesesrLRQMIQTAEAIAP---CVLWIDEI 99
|
...
gi 1944675807 571 EKA 573
Cdd:cd19507 100 EKG 102
|
|
| Torsin |
pfam06309 |
Torsin; This family consists of several eukaryotic torsin proteins. Torsion dystonia is an ... |
456-516 |
6.60e-03 |
|
Torsin; This family consists of several eukaryotic torsin proteins. Torsion dystonia is an autosomal dominant movement disorder characterized by involuntary, repetitive muscle contractions and twisted postures. The most severe early-onset form of dystonia has been linked to mutations in the human DYT1 (TOR1A) gene encoding a protein termed torsinA. While causative genetic alterations have been identified, the function of torsin proteins and the molecular mechanism underlying dystonia remain unknown. Phylogenetic analysis of the torsin protein family indicates these proteins share distant sequence similarity with the large and diverse family of (pfam00004) proteins. It has been suggested that torsins play a role in effectively managing protein folding and that possible breakdown in a neuroprotective mechanism that is, in part, mediated by torsins may be responsible for the neuronal dysfunction associated with dystonia.
Pssm-ID: 399367 [Multi-domain] Cd Length: 120 Bit Score: 37.32 E-value: 6.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1944675807 456 LERDLKLTVFGQDAAIDSLATAIKlSRAGLKSPDKPVgSFLFAGPTGVGKTEAARQLAKAL 516
Cdd:pfam06309 12 LERDLARRLFGQHLVKQLVVRSVK-GHWENPKPRKPL-VLSFHGWTGTGKNFVAEIIADNL 70
|
|
| RecA-like_ATAD1 |
cd19520 |
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ... |
215-296 |
7.29e-03 |
|
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. 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: 410928 [Multi-domain] Cd Length: 166 Bit Score: 38.17 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 215 LLVGEAGVGKTAIAEGLAKRivdgqvpdllAQSVVYSLDLGALLagTKYRGDFEKRFKALLGELKKRPQAILFIDEIHTI 294
Cdd:cd19520 39 LLYGPPGCGKTMLAKATAKE----------AGARFINLQVSSLT--DKWYGESQKLVAAVFSLASKLQPSIIFIDEIDSF 106
|
..
gi 1944675807 295 IG 296
Cdd:cd19520 107 LR 108
|
|
| ruvB |
PRK00080 |
Holliday junction branch migration DNA helicase RuvB; |
466-619 |
7.46e-03 |
|
Holliday junction branch migration DNA helicase RuvB;
Pssm-ID: 234619 [Multi-domain] Cd Length: 328 Bit Score: 39.34 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 466 GQDAAIDSLATAIKLSRAGLKSPDkPVgsfLFAGPTGVGKTEAARQLAKALGVELvrfdmseymerHTVSrligAP---- 541
Cdd:PRK00080 29 GQEKVKENLKIFIEAAKKRGEALD-HV---LLYGPPGLGKTTLANIIANEMGVNI-----------RITS----GPalek 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1944675807 542 PGyvgfDQGGLLTEAitkQPHCVLLLDEIEKAHPEVFNLLLQVMDhgtltdnngrkaDFRNVIVImttnaGAETAARA 619
Cdd:PRK00080 90 PG----DLAAILTNL---EEGDVLFIDEIHRLSPVVEEILYPAME------------DFRLDIMI-----GKGPAARS 143
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
215-294 |
9.83e-03 |
|
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: 36.89 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944675807 215 LLVGEAGVGKTAIAEGLAKRIVDGQV------PDLLAQSVVYSLDLGallAGTKYRGDfekrfkallGELKK--RPQAIL 286
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSNRPVfyvqltRDTTEEDLFGRRNID---PGGASWVD---------GPLVRaaREGEIA 70
|
....*...
gi 1944675807 287 FIDEIHTI 294
Cdd:pfam07728 71 VLDEINRA 78
|
|
| PRK05563 |
PRK05563 |
DNA polymerase III subunits gamma and tau; Validated |
464-516 |
9.96e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 235505 [Multi-domain] Cd Length: 559 Bit Score: 39.08 E-value: 9.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1944675807 464 VFGQDAAIDSLATAIKLSRAGlkspdkpvGSFLFAGPTGVGKTEAARQLAKAL 516
Cdd:PRK05563 18 VVGQEHITKTLKNAIKQGKIS--------HAYLFSGPRGTGKTSAAKIFAKAV 62
|
|
| |
