|
Name |
Accession |
Description |
Interval |
E-value |
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
1-758 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 1603.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 1 MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQP 80
Cdd:PRK11034 1 MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 81 TLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPSQSSDPGSQPNTE 160
Cdd:PRK11034 81 TLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPSQSSDPGSQPNSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 161 EQAGGEERMENFTTNLNQLARVGGIDPLIGRDKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVM 240
Cdd:PRK11034 161 EQAGGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 241 ADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSGGKIRVIG 320
Cdd:PRK11034 241 ADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 321 STTYQEFSNIFEKDRALARRFQKIDITEPSVEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAID 400
Cdd:PRK11034 321 STTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAID 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 401 VIDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAG 480
Cdd:PRK11034 401 VIDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 481 LGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAV 560
Cdd:PRK11034 481 LGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 561 LLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMSEIKKVFTPEF 640
Cdd:PRK11034 561 LLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMEEIKKIFTPEF 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 641 RNRLDNIIWFEHLSTEVIHQVVDKFIVELQVQLDQKGVSLEVSQEARNWLAEKGYDRAMGARPMARVIQDNLKKPLANEL 720
Cdd:PRK11034 641 RNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANEL 720
|
730 740 750
....*....|....*....|....*....|....*...
gi 1769930133 721 LFGSLVDGGQVTVALDKEKNELTYGFQSAQKHKPEAAH 758
Cdd:PRK11034 721 LFGSLVDGGQVTVALDKEKNELTYGFQSAQKHKAEAAH 758
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
2-735 |
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: 1121.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPaSEEERDTQPT 81
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAIEILEECGGDVELLRKRLEDYLEENLPVIP-EDIDEEPEQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 82 LSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEpsQSSDPGSQPNTEE 161
Cdd:TIGR02639 80 VGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITRLDILNYISHGISKDD--GKDQLGEEAGKEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 162 QAGgEERMENFTTNLNQLARVGGIDPLIGRDKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMA 241
Cdd:TIGR02639 158 EKG-QDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERLK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 242 DCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSGGKIRVIGS 321
Cdd:TIGR02639 237 NAKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFIDEIHTIVGAGATSGGSMDASNLLKPALSSGKIRCIGS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 322 TTYQEFSNIFEKDRALARRFQKIDITEPSVEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDV 401
Cdd:TIGR02639 317 TTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 402 IDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGL 481
Cdd:TIGR02639 397 IDEAGAAFRLRPKAKKKANVNVKDIENVVAKMAKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 482 GHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVL 561
Cdd:TIGR02639 477 GDPNKPVGSFLFVGPTGVGKTELAKQLAEELGVHLLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVL 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 562 LLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIhQDNSTDAMSE-IKKVFTPEF 640
Cdd:TIGR02639 557 LLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTSNAGASEMSKPPIGFG-GENRESKSLKaIKKLFSPEF 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 641 RNRLDNIIWFEHLSTEVIHQVVDKFIVELQVQLDQKGVSLEVSQEARNWLAEKGYDRAMGARPMARVIQDNLKKPLANEL 720
Cdd:TIGR02639 636 RNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEI 715
|
730
....*....|....*
gi 1769930133 721 LFGSLVDGGQVTVAL 735
Cdd:TIGR02639 716 LFGKLKKGGSVKISL 730
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2-743 |
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: 862.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPS--AREALEACSVDLVALRQELEAFIEQTTPVLPASEeerdtQ 79
Cdd:COG0542 6 FTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEglAAKLLRKLGVDLDALREELEEALGRLPKVSGSSG-----Q 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 80 PTLS--FQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFIShGTRKDEPSQSSDPGSQP 157
Cdd:COG0542 81 PYLSprLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITLEALREALE-ELRGGSRVTSQNPESKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 158 NTeeqaggeerMENFTTNLNQLARVGGIDPLIGRDKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVP 237
Cdd:COG0542 160 PA---------LDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 238 EVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQ-DTNSILFIDEIHTIIGAGAASgGQVDAANLIKPLLSGGKI 316
Cdd:COG0542 231 ESLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKsEGNIILFIDELHTLVGAGGAE-GAMDAANLLKPALARGEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 317 RVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSVEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPD 396
Cdd:COG0542 310 RCIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPD 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 397 KAIDVIDEAGARARLMPVSK------------------------------------------------------------ 416
Cdd:COG0542 390 KAIDLIDEAAARVRMEIDSKpeeldelerrleqleiekealkkeqdeasferlaelrdelaeleeelealkarweaekel 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 417 --------------------------------------RKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKM 458
Cdd:COG0542 470 ieeiqelkeeleqrygkipelekelaeleeelaelaplLREEVTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEEELHE 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 459 LVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEvtvqLSKAL-----GIE--LLRFDMSEYMERHTVS 531
Cdd:COG0542 550 RVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTE----LAKALaeflfGDEdaLIRIDMSEYMEKHSVS 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 532 RLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRE 611
Cdd:COG0542 626 RLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIGSEL 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 612 -TERKSIGLIHQDNSTDAMSEIKKVFTPEFRNRLDNIIWFEHLSTEVIHQVVDKFIVELQVQLDQKGVSLEVSQEARNWL 690
Cdd:COG0542 706 iLDLAEDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAAKDFL 785
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1769930133 691 AEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTValDKEKNELT 743
Cdd:COG0542 786 AEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITV--DVDDGELV 836
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
17-739 |
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: 677.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 17 AREHRHEFMTVEHLLLALL--SNPSAREALEACSVDLVALRQELEAFIEQttpvLPA-SEEERDTQPTLSFQRVLQRAVF 93
Cdd:TIGR03346 16 ALGRDHQQIEPEHLLKALLdqEGGLARPLLQKAGVNVGALRQALEKELER----LPKvSGPGGQVYLSPDLNRLLNLAEK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 94 HVQSSGRSEVTGANVLVAIfSEQESQAAYLLRKHEVSRLDVVNFIsHGTRKDEPSQSsdpgsqPNTEEQaggEERMENFT 173
Cdd:TIGR03346 92 LAQKRGDEFISSEHLLLAL-LDDKGTLGKLLKEAGATADALEAAI-NAVRGGQKVTD------ANAEDQ---YEALEKYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 174 TNLNQLARVGGIDPLIGRDKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSLDIGSL 253
Cdd:TIGR03346 161 RDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLALDMGAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 254 LAGTKYRGDFEKRFKALLKQLE-QDTNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSGGKIRVIGSTTYQEFSNIFE 332
Cdd:TIGR03346 241 IAGAKYRGEFEERLKAVLNEVTkSEGQIILFIDELHTLVGAGKAEGA-MDAGNMLKPALARGELHCIGATTLDEYRKYIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 333 KDRALARRFQKIDITEPSVEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGARARL- 411
Cdd:TIGR03346 320 KDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAARIRMe 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 412 ---MP--------------------------------------------------------------------------- 413
Cdd:TIGR03346 400 idsKPeeldeldrriiqleierealkkekdeaskkrledlekeladleeeyaeleeqwkaekasiqgiqqikeeieqvrl 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 414 ---VSKR-------------------------------------KKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLG 453
Cdd:TIGR03346 480 eleQAERegdlakaaelqygklpelekqlqaaeqklgeeqnrllREEVTAEEIAEVVSRWTGIPVSKMLEGEREKLLHME 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 454 DRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEvtvqLSKALGIEL-------LRFDMSEYME 526
Cdd:TIGR03346 560 EELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTE----LAKALAEFLfdsedamVRIDMSEYME 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 527 RHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTN 606
Cdd:TIGR03346 636 KHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMTSN 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 607 AGVRETERKSIGLIHQDNSTDAMSEIKKVFTPEFRNRLDNIIWFEHLSTEVIHQVVDKFIVELQVQLDQKGVSLEVSQEA 686
Cdd:TIGR03346 716 LGSDFIQELAGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKITLELSDAA 795
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1769930133 687 RNWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKEK 739
Cdd:TIGR03346 796 LDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGR 848
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
1-740 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 672.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 1 MLNQELelslnmafarAREHRHEFMTVEHLLLALL--SNPSAREALEACSVDLVALRQELEAFIEQTTPVLpASEeerdT 78
Cdd:CHL00095 14 MLSQEE----------ARRLGHNFVGTEQILLGLIgeGTGIAARALKSMGVTLKDARIEVEKIIGRGTGFV-AVE----I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 79 QPTLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVS----RLDVVNFIshGTRKDEPSQSSDPG 154
Cdd:CHL00095 79 PFTPRAKRVLEMSLEEARDLGHNYIGTEHLLLALLEEGEGVAARVLENLGVDlskiRSLILNLI--GEIIEAILGAEQSR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 155 SQPNTeeqaggeerMENFTTNLNQLARVGGIDPLIGRDKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQG 234
Cdd:CHL00095 157 SKTPT---------LEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 235 DVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSGG 314
Cdd:CHL00095 228 DVPDILEDKLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAAEGA-IDAANILKPALARG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 315 KIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSVEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHL 394
Cdd:CHL00095 307 ELQCIGATTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 395 PDKAIDVIDEAGARARLM-----------------------------------------------------------PVS 415
Cdd:CHL00095 387 PDKAIDLLDEAGSRVRLInsrlppaareldkelreilkdkdeaireqdfetakqlrdremevraqiaaiiqskkteeEKR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 416 KRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAG 495
Cdd:CHL00095 467 LEVPVVTEEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 496 PTGVGKTEVTVQLSKAL-GIE--LLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPD 572
Cdd:CHL00095 547 PTGVGKTELTKALASYFfGSEdaMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPD 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 573 VFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGL-------IHQDNSTDAMS-----EIKKVFTPEF 640
Cdd:CHL00095 627 IFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSKVIETNSGGLgfelsenQLSEKQYKRLSnlvneELKQFFRPEF 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 641 RNRLDNIIWFEHLSTEVIHQVVDKFIVELQVQLDQKGVSLEVSQEARNWLAEKGYDRAMGARPMARVIQDNLKKPLANEL 720
Cdd:CHL00095 707 LNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEV 786
|
810 820
....*....|....*....|
gi 1769930133 721 LFGSLVDGGQVTVALDKEKN 740
Cdd:CHL00095 787 LSFKIKPGDIIIVDVNDEKE 806
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
2-721 |
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: 540.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPS--AREALEACSVDLVALRQELEAFIEQttpvLPASEEERdtq 79
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDsdLAAILRHFGVDLGRLKADLARALDK----LPRGNTRT--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 80 PTLS--FQRVLQRAvFHVQSS--GRSEVTGANVLVAIFSEQE-----SQAAYLLRKHEVSRLD-VVNFISHGTRkdEPSQ 149
Cdd:TIGR03345 74 PVFSphLVELLQEA-WLLASLelGDGRIRSGHLLLALLTDPElrrllGSISPELAKIDREALReALPALVEGSA--EASA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 150 SSDPGSQPNTEEQAGGEERMENFTTNLNQLARVGGIDPLIGRDKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAW 229
Cdd:TIGR03345 151 AAADAAPAGAAAGAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 230 RIVQGDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQ-DTNSILFIDEIHTIIGAGAASgGQVDAANLIK 308
Cdd:TIGR03345 231 RIAAGDVPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKAsPQPIILFIDEAHTLIGAGGQA-GQGDAANLLK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 309 PLLSGGKIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSVEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKY 388
Cdd:TIGR03345 310 PALARGELRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 389 INDRHLPDKAIDVIDEAGARARL--------------------------------------------------------- 411
Cdd:TIGR03345 390 IPGRQLPDKAVSLLDTACARVALsqnatpaaledlrrriaaleleldalereaalgadhderlaelraelaaleaelaal 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 412 --------------------------MPVSKRKKT------------------------VNVADIESVVARIARIPEKSV 441
Cdd:TIGR03345 470 earwqqekelveailalraeleadadAPADDDDALraqlaeleaalasaqgeeplvfpeVDAQAVAEVVADWTGIPVGRM 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 442 SQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL-GIE--LLR 518
Cdd:TIGR03345 550 VRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLyGGEqnLIT 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 519 FDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRN 598
Cdd:TIGR03345 630 INMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKN 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 599 VVLVMTTNAGvreTERKSIGLIHQDNSTDA-------MSEIKKVFTPEFRNRLdNIIWFEHLSTEVIHQVVDKFIVELQV 671
Cdd:TIGR03345 710 TVILLTSNAG---SDLIMALCADPETAPDPeallealRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRIAR 785
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1769930133 672 QL-DQKGVSLEVSQEARNWLAEKGYDRAMGARPMARVIQDNLKKPLANELL 721
Cdd:TIGR03345 786 RLkENHGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQIL 836
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
2-738 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 539.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNP--SAREALEACSVDLVALRQELEAFIEQttpvLPASE-EERDT 78
Cdd:PRK10865 6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEggSVRPLLTSAGINAGQLRTDINQALSR----LPQVEgTGGDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 79 QPTLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFsEQESQAAYLLRKHEVSRLDVVNFIshgtrkdEPSQSSDPGSQPN 158
Cdd:PRK10865 82 QPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAAL-ESRGTLADILKAAGATTANITQAI-------EQMRGGESVNDQG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 159 TEEQaggEERMENFTTNLNQLARVGGIDPLIGRDKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPE 238
Cdd:PRK10865 154 AEDQ---RQALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 239 VMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQL-EQDTNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSGGKIR 317
Cdd:PRK10865 231 GLKGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLaKQEGNVILFIDELHTMVGAGKADGA-MDAGNMLKPALARGELH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 318 VIGSTTYQEFSNIFEKDRALARRFQKIDITEPSVEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDK 397
Cdd:PRK10865 310 CVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 398 AIDVIDEAGARARLMPVSK---------------------RKKT------------------------------------ 420
Cdd:PRK10865 390 AIDLIDEAASSIRMQIDSKpeeldrldrriiqlkleqqalMKESdeaskkrldmlneelsdkerqyseleeewkaekasl 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 421 -------------------------------------------------------------VNVADIESVVARIARIPEK 439
Cdd:PRK10865 470 sgtqtikaeleqakiaieqarrvgdlarmselqygkipelekqlaaatqlegktmrllrnkVTDAEIAEVLARWTGIPVS 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 440 SVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEvtvqLSKALGIEL--- 516
Cdd:PRK10865 550 RMLESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTE----LCKALANFMfds 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 517 ----LRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGR 592
Cdd:PRK10865 626 ddamVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGR 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 593 KADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMSEIKKVFTPEFRNRLDNIIWFEHLSTEVIHQVVDKFIVELQVQ 672
Cdd:PRK10865 706 TVDFRNTVVIMTSNLGSDLIQERFGELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKR 785
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1769930133 673 LDQKGVSLEVSQEARNWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKE 738
Cdd:PRK10865 786 LEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDD 851
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
449-650 |
2.99e-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: 269.82 E-value: 2.99e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 449 LKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL---GIELLRFDMSEYM 525
Cdd:cd19499 2 LLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMSEYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 526 ERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTT 605
Cdd:cd19499 82 EKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTS 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1769930133 606 NAgvreterksiglihqdnstdamseikkvFTPEFRNRLDNIIWF 650
Cdd:cd19499 162 NH----------------------------FRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
486-647 |
9.51e-76 |
|
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: 242.10 E-value: 9.51e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 486 KPVGSFLFAGPTGVGKTEVTVQLSKALGI---ELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLL 562
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 563 LDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNST---DAMSEIKKVFTPE 639
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRLGDSPDYELlkeEVMDLLKKGFIPE 160
|
....*...
gi 1769930133 640 FRNRLDNI 647
Cdd:pfam07724 161 FLGRLPII 168
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
350-452 |
2.30e-37 |
|
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: 134.92 E-value: 2.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 350 SVEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGARARLmpvSKRKKTVNVADIESV 429
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRL---SQESKPEELEDLERE 77
|
90 100
....*....|....*....|...
gi 1769930133 430 VARIARIPEKSVSQSDRDTLKNL 452
Cdd:pfam17871 78 LAKLEIEKEALEREQDFEKAERL 100
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
653-733 |
3.22e-29 |
|
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: 110.96 E-value: 3.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 653 LSTEVIHQVVDKFIVELQVQLDQKGVSLEVSQEARNWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVT 732
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 1769930133 733 V 733
Cdd:pfam10431 81 V 81
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
653-742 |
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 1769930133 653 LSTEVIHQVVDKFIVELQVQLDQKGVSLEVSQEARNWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVT 732
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
90
....*....|
gi 1769930133 733 VALDKEKNEL 742
Cdd:smart01086 81 VDVDDGELVF 90
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
189-344 |
5.77e-22 |
|
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: 92.98 E-value: 5.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 189 IGRDKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPevmadctIYSLDIGSLLAGTKYRGDFE-KRF 267
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGhFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1769930133 268 KALLKQLEQDTNSILFIDEIHTIigAGAASGGQVDAAN-LIKPLLSGGKIRVIGSTTYqefSNIFEKDRALARRFQKI 344
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDSL--SRGAQNALLRVLEtLNDLRIDRENVRVIGATNR---PLLGDLDRALYDRLDIR 146
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
26-387 |
5.81e-17 |
|
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: 83.81 E-value: 5.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 26 TVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQPTLSFQRVLQRAVFHVQSSGRSEVTG 105
Cdd:COG0464 5 LALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 106 ANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPSQSSDPGSQPNTEEQAGGEErmENFTTNLNQLARVGGI 185
Cdd:COG0464 85 LLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEE--ELLELREAILDDLGGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 186 DPLIGRDKELERAIQVLCRRRKNNP-------LLVGESGVGKTAIAEGLAwRIVQGDVpevmadctiYSLDIGSLLAgtK 258
Cdd:COG0464 163 EEVKEELRELVALPLKRPELREEYGlppprglLLYGPPGTGKTLLARALA-GELGLPL---------IEVDLSDLVS--K 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 259 YRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDA----------ANLIKPLLsggkirVIGsTTYQeFS 328
Cdd:COG0464 231 YVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRrvvntlltemEELRSDVV------VIA-ATNR-PD 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 329 NIfekDRALARRFQ-KIDITEPSVEETVQIINGLKPKYEAHHDV----------RYTAKAVRAAVELAVK 387
Cdd:COG0464 303 LL---DPALLRRFDeIIFFPLPDAEERLEIFRIHLRKRPLDEDVdleelaeateGLSGADIRNVVRRAAL 369
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
211-344 |
8.79e-17 |
|
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: 77.25 E-value: 8.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 211 LLVGESGVGKTAIAEGLAWrivqgdvpevMADCTIYSLDIGSLLAgtKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAK----------ELGAPFIEISGSELVS--KYVGESEKRLRELFEAAKKLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1769930133 291 IGAGAASGGQV--DAANLIKPLLSG-----GKIRVIGSTTYqefsnIFEKDRALARRFQKI 344
Cdd:pfam00004 70 AGSRGSGGDSEsrRVVNQLLTELDGftssnSKVIVIAATNR-----PDKLDPALLGRFDRI 125
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
461-617 |
2.02e-12 |
|
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: 65.63 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 461 FGQDKAIEALTEAIkmsraglghEHKPVGSFLFAGPTGVGKTEVTVQLSKAL---GIELLRFDMSEYMERHTVSRLIgap 537
Cdd:cd00009 1 VGQEEAIEALREAL---------ELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELF--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 538 pgyvGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGtltdnNGRKADFRNVVLVMTTNAGVRETERKSI 617
Cdd:cd00009 69 ----GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETL-----NDLRIDRENVRVIGATNRPLLGDLDRAL 139
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
206-344 |
2.17e-12 |
|
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: 65.47 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 206 RKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSLDIGSLL-----AGTKYRGDFEKRFKALLKQLEQDTNS 280
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLlliivGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1769930133 281 ILFIDEIHTIIGAGAASGGQVDA-ANLIKPLLSGGKIRVIGSTTYQEFSnifeKDRALARRFQKI 344
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEeLRLLLLLKSEKNLTVILTTNDEKDL----GPALLRRRFDRR 141
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
490-606 |
4.89e-12 |
|
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: 63.85 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 490 SFLFAGPTGVGKTEVTVQLSKAL-GIELLRFDMSEYMerhTVSRLIGappGYVGFDQGGLLTDAVI----KHPHaVLLLD 564
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDT---TEEDLFG---RRNIDPGGASWVDGPLvraaREGE-IAVLD 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1769930133 565 EIEKAHPDVFNLLLQVMDNGTLTDNNGR---KADFRNVVLVMTTN 606
Cdd:pfam07728 74 EINRANPDVLNSLLSLLDERRLLLPDGGelvKAAPDGFRLIATMN 118
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
13-63 |
1.26e-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: 59.84 E-value: 1.26e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1769930133 13 AFARAREHRHEFMTVEHLLLALLSNPS--AREALEACSVDLVALRQELEAFIE 63
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDglAARLLKKAGVDLDALREAIEKLLG 53
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
211-344 |
4.37e-10 |
|
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: 58.83 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 211 LLVGESGVGKTAIAEGLAwrivqgdvpeVMADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290
Cdd:cd19481 30 LLYGPPGTGKTLLAKALA----------GELGLPLIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDAI 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1769930133 291 IGAGAASGGQVDAA-------NLIKPLLSGGKIRVIGSTtyqefSNIFEKDRALAR--RFQKI 344
Cdd:cd19481 98 GRKRDSSGESGELRrvlnqllTELDGVNSRSKVLVIAAT-----NRPDLLDPALLRpgRFDEV 155
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
208-404 |
1.36e-09 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 59.13 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 208 NNPLLVGESGVGKTAIAEGLAWRIvqgDVPevmadctIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQdTNSILFIDEI 287
Cdd:COG1223 36 RKILFYGPPGTGKTMLAEALAGEL---KLP-------LLTVRLDSLI--GSYLGETARNLRKLFDFARR-APCVIFFDEF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 288 HTIigaGAASGGQVDAA------NLIKPLLSG--GKIRVIGSTTYQEFSnifekDRALARRFQ-KIDITEPSVEETVQI- 357
Cdd:COG1223 103 DAI---AKDRGDQNDVGevkrvvNALLQELDGlpSGSVVIAATNHPELL-----DSALWRRFDeVIEFPLPDKEERKEIl 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1769930133 358 ---INGLKPKYEAHHDV----------RYTAKAVRAAVELAV----KYINDRHLpDKAIDVIDE 404
Cdd:COG1223 175 elnLKKFPLPFELDLKKlakkleglsgADIEKVLKTALKKAIledrEKVTKEDL-EEALKQRKE 237
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
466-606 |
6.04e-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: 55.75 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 466 AIEALTEAIKMSRAGLGhehkPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTvsrligappGYVGfDQ 545
Cdd:cd19481 8 AVEAPRRGSRLRRYGLG----LPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYV---------GESE-KN 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1769930133 546 GGLLTDAVIKHPHAVLLLDEIEKAHPD------------VFNLLLQVMDNGTLTDnngrkadfrNVVLVMTTN 606
Cdd:cd19481 74 LRKIFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAATN 137
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
211-440 |
1.48e-08 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 56.94 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 211 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290
Cdd:COG1222 116 LLYGPPGTGKTLLAKAVAGE----------LGAPFIRVRGSELV--SKYIGEGARNVREVFELAREKAPSIIFIDEIDAI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 291 IGA--GAASGGQVDaaNLIKPLL-------SGGKIRVIGSTTYQEfsnifEKDRALAR--RF-QKIDITEPSVEETVQII 358
Cdd:COG1222 184 AARrtDDGTSGEVQ--RTVNQLLaeldgfeSRGDVLIIAATNRPD-----LLDPALLRpgRFdRVIEVPLPDEEAREEIL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 359 NGLKPKYEAHHDVRYTAKAVRA----AVELAVkyindrhlpdkaidVIDEAGARArlmpVSKRKKTVNVADIESVVARIA 434
Cdd:COG1222 257 KIHLRDMPLADDVDLDKLAKLTegfsGADLKA--------------IVTEAGMFA----IREGRDTVTMEDLEKAIEKVK 318
|
....*.
gi 1769930133 435 RIPEKS 440
Cdd:COG1222 319 KKTETA 324
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
492-606 |
2.33e-08 |
|
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: 52.98 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 492 LFAGPTGVGKTEVTVQLSKALGIELLRFDMSEymerhTVSRLIGAPPGYVgfdqGGLLTDAVIKHPHaVLLLDEIEKAHP 571
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSE-----LVSKYVGESEKRL----RELFEAAKKLAPC-VIFIDEIDALAG 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1769930133 572 -----------DVFNLLLQVMDngtltdnnGRKADFRNVVLVMTTN 606
Cdd:pfam00004 72 srgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
211-343 |
1.47e-07 |
|
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: 51.58 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 211 LLVGESGVGKTAIAEGLAWRIvqgdvpevmaDCTIYSLDIGSLLAgtKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290
Cdd:cd19509 36 LLYGPPGTGKTLLARAVASES----------GSTFFSISASSLVS--KWVGESEKIVRALFALARELQPSIIFIDEIDSL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1769930133 291 IgaGAASGGQVDAANLIKPLL----------SGGKIRVIGSTtyqefSNIFEKDRALARRFQK 343
Cdd:cd19509 104 L--SERGSGEHEASRRVKTEFlvqmdgvlnkPEDRVLVLGAT-----NRPWELDEAFLRRFEK 159
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
492-606 |
2.98e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.45 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 492 LFAGPTGVGKTEVTVQLSKAL---GIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGG----LLTDAVIKHPHAVLLLD 564
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGElrlrLALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1769930133 565 EIEKAHPDVFNLLLQVMDNGTLTDnngRKADFRNVVLVMTTN 606
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLL---LLKSEKNLTVILTTN 124
|
|
| RecA-like_VPS4 |
cd19521 |
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ... |
211-343 |
3.94e-07 |
|
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: 50.63 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 211 LLVGESGVGKTAIAEGLAwrivqgdvpeVMADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290
Cdd:cd19521 44 LLYGPPGTGKSYLAKAVA----------TEANSTFFSVSSSDLV--SKWMGESEKLVKQLFAMARENKPSIIFIDEVDSL 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1769930133 291 igAGAASGGQVDAANLIKPLL---------SGGKIRVIGSTtyqefsNI-FEKDRALARRFQK 343
Cdd:cd19521 112 --CGTRGEGESEASRRIKTELlvqmngvgnDSQGVLVLGAT------NIpWQLDSAIRRRFEK 166
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
211-515 |
1.62e-06 |
|
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: 51.45 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 211 LLVGESGVGKTAIAEGLAWRI----VQGDVPEVMadctiysldigsllagTKYRGDFEKRFKALLKQLEQDTNSILFIDE 286
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANEAgayfISINGPEIM----------------SKYYGESEERLREIFKEAEENAPSIIFIDE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 287 IHTIIGAGAASGGQVDAA------NLIKPLLSGGKIRVIGSTTYQEfsnifEKDRALAR--RFQK-IDITEPSVEETVQI 357
Cdd:TIGR01243 280 IDAIAPKREEVTGEVEKRvvaqllTLMDGLKGRGRVIVIGATNRPD-----ALDPALRRpgRFDReIVIRVPDKRARKEI 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 358 INGLKPKYEAHHDVR----------YTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGARARL--MPVSKRKKTVNVAD 425
Cdd:TIGR01243 355 LKVHTRNMPLAEDVDldklaevthgFVGADLAALAKEAAMAALRRFIREGKINFEAEEIPAEVLkeLKVTMKDFMEALKM 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 426 IESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALteaikmSRAGLgheHKPVGSFLFaGPTGVGKTevt 505
Cdd:TIGR01243 435 VEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIF------EKMGI---RPPKGVLLF-GPPGTGKT--- 501
|
330
....*....|
gi 1769930133 506 vQLSKALGIE 515
Cdd:TIGR01243 502 -LLAKAVATE 510
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
334-606 |
4.74e-06 |
|
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: 49.52 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 334 DRALARRFQKIDITEPSVEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGARARLMP 413
Cdd:COG0464 29 LLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 414 VSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVF----GQDKAIEALTEAIK--------MSRAGL 481
Cdd:COG0464 109 LLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILddlgGLEEVKEELRELVAlplkrpelREEYGL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 482 ghehKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEymerhtvsrLIGappGYVG---------FDQgglltda 552
Cdd:COG0464 189 ----PPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSD---------LVS---KYVGeteknlrevFDK------- 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1769930133 553 VIKHPHAVLLLDEIEKAHPD-----------VFNLLLQVMDNGTltdnngrkadfRNVVLVMTTN 606
Cdd:COG0464 246 ARGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR-----------SDVVVIAATN 299
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
204-343 |
9.35e-06 |
|
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. 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: 410930 [Multi-domain] Cd Length: 170 Bit Score: 46.52 E-value: 9.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 204 RRRKNNPLLVGESGVGKTAIAEGLAwrivqgdvpevmADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILF 283
Cdd:cd19522 30 RRPWKGVLMVGPPGTGKTLLAKAVA------------TECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIF 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 284 IDEIHTIIGAgAASGGQVDAANLIKPLLSGGKIRVIGSTTYQEFSNI----------FEKDRALARRFQK 343
Cdd:cd19522 98 IDEIDSICSR-RGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMvmvlaatnfpWDIDEALRRRLEK 166
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
187-246 |
4.04e-05 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 44.80 E-value: 4.04e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1769930133 187 PLIGRDKELERAIQVLCRRRKNNP---LLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIY 246
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDEN 63
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
492-606 |
4.32e-05 |
|
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: 44.86 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 492 LFAGPTGVGKTEVTVQLSKALGIELLRF------DMSEYM-ERHTvsrLIGAPPGYVgfDQGglLTDAVIKHPhaVLLLD 564
Cdd:cd19500 41 CLVGPPGVGKTSLGKSIARALGRKFVRIslggvrDEAEIRgHRRT---YVGAMPGRI--IQA--LKKAGTNNP--VFLLD 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1769930133 565 EIEK----AHPDVFNLLLQVMD---NGTLTDNN-GRKADFRNVVLVMTTN 606
Cdd:cd19500 112 EIDKigssFRGDPASALLEVLDpeqNSTFSDHYlDVPFDLSKVLFIATAN 161
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
460-512 |
5.71e-05 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 45.95 E-value: 5.71e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1769930133 460 VFGQDKAIEALTEAIKMSRagLGHehkpvgSFLFAGPTGVGKTEVTVQLSKAL 512
Cdd:COG2812 12 VVGQEHVVRTLKNALASGR--LAH------AYLFTGPRGVGKTTLARILAKAL 56
|
|
| RecA-like_CDC48_r1-like |
cd19519 |
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ... |
211-345 |
6.09e-05 |
|
first of two ATPase domains of CDC48 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. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like 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: 410927 [Multi-domain] Cd Length: 166 Bit Score: 43.96 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 211 LLVGESGVGKTAIAEGLA------WRIVQGdvPEVMadctiysldigsllagTKYRGDFEKRFKALLKQLEQDTNSILFI 284
Cdd:cd19519 38 LLYGPPGTGKTLIARAVAnetgafFFLING--PEIM----------------SKLAGESESNLRKAFEEAEKNAPAIIFI 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1769930133 285 DEIHTIIGAGAASGGQVD---AANLIKpLLSGGKIR----VIGSTtyqefSNIFEKDRALaRRFQKID 345
Cdd:cd19519 100 DEIDAIAPKREKTHGEVErriVSQLLT-LMDGLKQRahviVMAAT-----NRPNSIDPAL-RRFGRFD 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 ... |
211-322 |
6.69e-05 |
|
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: 43.82 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 211 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTIYSLDIGSLLAgtKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290
Cdd:cd19503 38 LLHGPPGTGKTLLARAVANE----------AGANFLSISGPSIVS--KYLGESEKNLREIFEEARSHAPSIIFIDEIDAL 105
|
90 100 110
....*....|....*....|....*....|....*....
gi 1769930133 291 IGAGAASGGQVD---AANLIKpLLSG----GKIRVIGST 322
Cdd:cd19503 106 APKREEDQREVErrvVAQLLT-LMDGmssrGKVVVIAAT 143
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
207-290 |
8.52e-05 |
|
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: 44.90 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 207 KNNPLLVGESGVGKTAIAEGLAwRIVqgDVPEVMADCTiysldigSLL-AGtkYRG-DFEKRFKALLK----QLEQDTNS 280
Cdd:cd19497 50 KSNILLIGPTGSGKTLLAQTLA-KIL--DVPFAIADAT-------TLTeAG--YVGeDVENILLKLLQaadyDVERAQRG 117
|
90
....*....|
gi 1769930133 281 ILFIDEIHTI 290
Cdd:cd19497 118 IVYIDEIDKI 127
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
211-321 |
1.14e-04 |
|
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: 43.13 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 211 LLVGESGVGKTAIAEGLA--WRIvqgdvpevmadcTIYSLDIGSLLAGtkYRGDFEKRFKALLKQLEQDTNSILFIDEIH 288
Cdd:cd19507 35 LLVGIQGTGKSLTAKAIAgvWQL------------PLLRLDMGRLFGG--LVGESESRLRQMIQTAEAIAPCVLWIDEIE 100
|
90 100 110
....*....|....*....|....*....|...
gi 1769930133 289 TIIGaGAASGGQvdaanlikpllSGGKIRVIGS 321
Cdd:cd19507 101 KGFS-NADSKGD-----------SGTSSRVLGT 121
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
448-568 |
2.69e-04 |
|
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: 42.37 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 448 TLKNLGDRLKMLVFGQDKAIEALTEAIK------MSRAGLGHEHKPvGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDM 521
Cdd:cd19498 1 TPREIVSELDKYIIGQDEAKRAVAIALRnrwrrmQLPEELRDEVTP-KNILMIGPTGVGKTEIARRLAKLAGAPFIKVEA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1769930133 522 SEYMErhtvsrligapPGYVGFDQGGLLTDAVikhpHAVLLLDEIEK 568
Cdd:cd19498 80 TKFTE-----------VGYVGRDVESIIRDLV----EGIVFIDEIDK 111
|
|
| RecA-like_spastin |
cd19524 |
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ... |
211-343 |
4.68e-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: 41.37 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 211 LLVGESGVGKTAIAEGLAwrivqgdvpevmADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290
Cdd:cd19524 37 LLFGPPGNGKTMLAKAVA------------AESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSL 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1769930133 291 IgaGAASGGQVDAANLIKP--------LLSGGKIRVI--GSTTYQEfsnifEKDRALARRFQK 343
Cdd:cd19524 105 L--SERSEGEHEASRRLKTefliefdgVQSNGDDRVLvmGATNRPQ-----ELDDAVLRRFTK 160
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
184-340 |
6.44e-04 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 43.12 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 184 GIDPLIGRDKELERAIQVlcrRRKNNPLLVGESGVGKTAIAEGLAwRIVQGDVpevmadctiysLDIGSLLAGTKyrgDF 263
Cdd:PRK13341 32 GQDHILGEGRLLRRAIKA---DRVGSLILYGPPGVGKTTLARIIA-NHTRAHF-----------SSLNAVLAGVK---DL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1769930133 264 EKRFKALLKQLEQ-DTNSILFIDEIHTIIGAgaasggQVDAanlIKPLLSGGKIRVIGSTTYQEFsniFEKDRALARR 340
Cdd:PRK13341 94 RAEVDRAKERLERhGKRTILFIDEVHRFNKA------QQDA---LLPWVENGTITLIGATTENPY---FEVNKALVSR 159
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
462-512 |
6.89e-04 |
|
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: 41.04 E-value: 6.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1769930133 462 GQDKAIEALTEAIKMSRagLGHehkpvgSFLFAGPTGVGKTEVTVQLSKAL 512
Cdd:pfam13177 1 GQPEAIQLLQNSLENGR--LSH------AYLFSGPEGVGKLELALAFAKAL 43
|
|
| RecA-like_Figl-1 |
cd19525 |
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ... |
211-343 |
7.51e-04 |
|
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. 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: 410933 [Multi-domain] Cd Length: 186 Bit Score: 41.13 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 211 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290
Cdd:cd19525 59 LLFGPPGTGKTLIGKCIASQ----------SGATFFSISASSLT--SKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSL 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1769930133 291 IgaGAASGGQVDAANLIKPLL----------SGGKIRVIGSTTYQEfsnifEKDRALARRFQK 343
Cdd:cd19525 127 L--SQRGEGEHESSRRIKTEFlvqldgattsSEDRILVVGATNRPQ-----EIDEAARRRLVK 182
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
188-323 |
9.37e-04 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 42.38 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 188 LIGRDKELERAIQvlcRRRKNNPLLVGESGVGKTAIAEGLAwrivqgdvpeVMADCTIYSLDigSLLAGTKyrgDFEKRF 267
Cdd:PRK13342 20 LLGPGKPLRRMIE---AGRLSSMILWGPPGTGKTTLARIIA----------GATDAPFEALS--AVTSGVK---DLREVI 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1769930133 268 KALLKQLEQDTNSILFIDEIHTIigagaaSGGQVDAanlikpLLSG---GKIRVIGSTT 323
Cdd:PRK13342 82 EEARQRRSAGRRTILFIDEIHRF------NKAQQDA------LLPHvedGTITLIGATT 128
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
208-311 |
1.27e-03 |
|
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: 40.44 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 208 NNPLLVGESGVGKTAIAEGLAwRIVqgDVPEVMADCTIYSlDIGsllagtkYRG-DFEKRFKALlkqleqdTNSILFIDE 286
Cdd:cd19498 47 KNILMIGPTGVGKTEIARRLA-KLA--GAPFIKVEATKFT-EVG-------YVGrDVESIIRDL-------VEGIVFIDE 108
|
90 100
....*....|....*....|....*
gi 1769930133 287 IHTIIGAGAASGGQVDAANLIKPLL 311
Cdd:cd19498 109 IDKIAKRGGSSGPDVSREGVQRDLL 133
|
|
| clpX |
PRK05342 |
ATP-dependent Clp protease ATP-binding subunit ClpX; |
207-244 |
1.36e-03 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX;
Pssm-ID: 235422 [Multi-domain] Cd Length: 412 Bit Score: 41.68 E-value: 1.36e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1769930133 207 KNNPLLVGESGVGKTAIAEGLAwRIVqgDVPEVMADCT 244
Cdd:PRK05342 108 KSNILLIGPTGSGKTLLAQTLA-RIL--DVPFAIADAT 142
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
181-287 |
1.59e-03 |
|
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: 40.24 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 181 RVGGIDPLIgrdKELERAIQvLCR---RRKNNP----LLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYS-LDIGS 252
Cdd:cd19499 12 RVVGQDEAV---KAVSDAIR-RARaglSDPNRPigsfLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEYMeKHSVS 87
|
90 100 110
....*....|....*....|....*....|....*..
gi 1769930133 253 LLAGT--KYRGdFEKRFKaLLKQLEQDTNSILFIDEI 287
Cdd:cd19499 88 RLIGAppGYVG-YTEGGQ-LTEAVRRKPYSVVLLDEI 122
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
5-236 |
2.37e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 41.38 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 5 ELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQPTLSF 84
Cdd:COG3899 105 LLLLLALALLLLALLALALLALLLALLLAAGVLGLLLGGLLLAALAALLALAALAAAAAAAAAAAAARAARLRRARAARL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 85 QRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNF-ISHGTRKDEPSQSSDPGSQPNTEEQA 163
Cdd:COG3899 185 AALALRALLLLVLLLLLLLLLLGLLLAAAAALAAAAAAAAAAAPAAPVVLVAAlLLALAALLALLLLAARLLGLAGAAAL 264
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1769930133 164 GGEERMENFTTNLNQLARVGGIDPLIGRDKELERAIQVL--CRRRKNNPLLV-GESGVGKTAIAEGLAWRIVQGDV 236
Cdd:COG3899 265 LLLGLLAAAAAGRRLLARRLIPQPLVGREAELAALLAALerARAGRGELVLVsGEAGIGKSRLVRELARRARARGG 340
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
204-288 |
2.46e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.86 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 204 RRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVP----EVMADCTIYSLdIGSLLAGTKYRGDFEKRFKALLKQLEQ--- 276
Cdd:pfam13401 2 RFGAGILVLTGESGTGKTTLLRRLLEQLPEVRDSvvfvDLPSGTSPKDL-LRALLRALGLPLSGRLSKEELLAALQQlll 80
|
90
....*....|....
gi 1769930133 277 --DTNSILFIDEIH 288
Cdd:pfam13401 81 alAVAVVLIIDEAQ 94
|
|
| RecA-like_ATAD1 |
cd19520 |
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ... |
211-343 |
3.30e-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: 38.94 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 211 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290
Cdd:cd19520 39 LLYGPPGCGKTMLAKATAKE----------AGARFINLQVSSLT--DKWYGESQKLVAAVFSLASKLQPSIIFIDEIDSF 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1769930133 291 IGAGAASGGQVDAA------NLIKPLLSGGKIRVI--GSTtyqefSNIFEKDRALARRFQK 343
Cdd:cd19520 107 LRQRSSTDHEATAMmkaefmSLWDGLSTDGNCRVIvmGAT-----NRPQDLDEAILRRMPK 162
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
211-323 |
3.88e-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: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 211 LLVGESGVGKTAIAEGLAWRIvqgDVPevmadctIYSLDIGSLLAGTKyrGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290
Cdd:cd19518 38 LLHGPPGCGKTMLANAIAGEL---KVP-------FLKISATEIVSGVS--GESEEKIRELFDQAISNAPCIVFIDEIDAI 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1769930133 291 igAGAASGGQVDAA------------NLIKPLLSGGKIRVIGSTT 323
Cdd:cd19518 106 --TPKRESAQREMErrivsqlltcmdELNNEKTAGGPVLVIGATN 148
|
|
| TIGR02928 |
TIGR02928 |
orc1/cdc6 family replication initiation protein; Members of this protein family are found ... |
186-327 |
4.99e-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: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 186 DPLIGRDKELE---RAIQVLCR-RRKNNPLLVGESGVGKTAIAEGLAwRIVQGDVPE-------VMADCTIYS------L 248
Cdd:TIGR02928 15 DRIVHRDEQIEelaKALRPILRgSRPSNVFIYGKTGTGKTAVTKYVM-KELEEAAEDrdvrvvtVYVNCQILDtlyqvlV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 249 DIGSLLAGTK----YRG-DFEKRFKALLKQLEQDTNSILFI-DEIHTIIGAG---------AASGGQVDaanlikpllsG 313
Cdd:TIGR02928 94 ELANQLRGSGeevpTTGlSTSEVFRRLYKELNERGDSLIIVlDEIDYLVGDDddllyqlsrARSNGDLD----------N 163
|
170
....*....|....
gi 1769930133 314 GKIRVIGSTTYQEF 327
Cdd:TIGR02928 164 AKVGVIGISNDLKF 177
|
|
| PRK14969 |
PRK14969 |
DNA polymerase III subunits gamma and tau; Provisional |
462-515 |
5.99e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237873 [Multi-domain] Cd Length: 527 Bit Score: 39.73 E-value: 5.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1769930133 462 GQDKAIEALTEAIKMSRagLGHehkpvgSFLFAGPTGVGKTEVTVQLSKALGIE 515
Cdd:PRK14969 20 GQEHVVRALTNALEQQR--LHH------AYLFTGTRGVGKTTLARILAKSLNCE 65
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
489-585 |
7.41e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 37.32 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769930133 489 GSFLFAGPTGVGKTEVTVQLSKAL---GIELLRFDMSEYME----RHTVSRLIGAPPgyVGFDQGGLLTDAVIKH----- 556
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLpevRDSVVFVDLPSGTSpkdlLRALLRALGLPL--SGRLSKEELLAALQQLllala 83
|
90 100
....*....|....*....|....*....
gi 1769930133 557 PHAVLLLDEIEKAHPDVFNLLLQVMDNGT 585
Cdd:pfam13401 84 VAVVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| |
