|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1-863 |
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: 1037.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 1 MNDQtQFTERALTILTLAQKLASDHQHPQLQPIHILAAFIETpEDGSVPylqNLIEKGRYDYDLFKKVVNRNLVRIPQQQ 80
Cdd:COG0542 1 MNFE-KFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQ-GEGLAA---KLLRKLGVDLDALREELEEALGRLPKVS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 81 PAPAEITPSYALGKVLQDAAKIQKQQKDSFIAQDHILFALFNDSS--IQQIFKEAQVDIEAIKQQALELRGNTRIDSRGA 158
Cdd:COG0542 76 GSSGQPYLSPRLKRVLELAELEARKLGDEYISTEHLLLALLREGEgvAARILKKLGITLEALREALEELRGGSRVTSQNP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 159 DTNTPLeyLSKYAIDMTEQARQGKLDPVIGREEEIRSTIRVLARRIKSNPCLIGEPGIGKTAIIEGVAQRIIDDDVPTIL 238
Cdd:COG0542 156 ESKTPA--LDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 239 QGAKLFSLDLAALTAGAKYKGDFEERFKGVLKEIEESKTLIVLFIDEIHMLMGNGKD----DAANILKPALSRGQLKVIG 314
Cdd:COG0542 234 KDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKSEGNIILFIDELHTLVGAGGAegamDAANLLKPALARGELRCIG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 315 ATTNNEYRSIVEKDGAFERRFQKIEVAEPSVRQTVAILRGLQPKYEIHHGVRILDSALVTAAQLAKRYLPYRRLPDSALD 394
Cdd:COG0542 314 ATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAID 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 395 LVDISCAGVAVARDSKPEELDSKERQLQLIQVEIKALERDEDADSttKDRLKLARQKEASLQEELEPLRQRYNEEKHGHE 474
Cdd:COG0542 394 LIDEAAARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEAS--FERLAELRDELAELEEELEALKARWEAEKELIE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 475 ELTQAKKKLDElenkaldaerrydtataadlRYFAIPDIKKQIEKLEDQVAEEERragansMIQNVVDSDTISETAARLT 554
Cdd:COG0542 472 EIQELKEELEQ--------------------RYGKIPELEKELAELEEELAELAP------LLREEVTEEDIAEVVSRWT 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 555 GIPVKKLSESENEKLIHMERDLSSEVVGQMDAIKAVSNAVRLSRSGLANPRQP-ASFLFLGLSGSGKTELAKKVAGFLFN 633
Cdd:COG0542 526 GIPVGKLLEGEREKLLNLEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPiGSFLFLGPTGVGKTELAKALAEFLFG 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 634 DEDMMIRVDCSELSEKYAVSKLLGTTAGYVGYDEGGFLTNQLQYKPYSVLLFDEVEKAHPDVLTVMLQMLDDGRITSGQG 713
Cdd:COG0542 606 DEDALIRIDMSEYMEKHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQG 685
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 714 KTIDCSNCIVIMTSNLGAEFI-NSQQGSKIQESTKNLVMGAVRQHFRPEFLNRISSIVIFNKLSRKAIHKIVDIRLKEIE 792
Cdd:COG0542 686 RTVDFRNTIIIMTSNIGSELIlDLAEDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLR 765
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1346246 793 ERFEqnDKHYKLNLTQEAKDFLAKYGYSDDMGARPLNRLIQNEILNKLALRILKNEIKDKETVNVVLKKGK 863
Cdd:COG0542 766 KRLA--ERGITLELTDAAKDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGE 834
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
7-863 |
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: 963.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 7 FTERALTILTLAQKLASDHQHPQLQPIHILAAFIETpEDGSVPylqNLIEKGRYDYDLFKKVVNRNLVRIPQQQPAPAEI 86
Cdd:TIGR03346 1 LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQ-EGGLAR---PLLQKAGVNVGALRQALEKELERLPKVSGPGGQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 87 TPSYALGKVLQDAAKIQKQQKDSFIAQDHILFALFND-SSIQQIFKEAQVDIEAIKQQALELRGNTRIDSRGADTNtpLE 165
Cdd:TIGR03346 77 YLSPDLNRLLNLAEKLAQKRGDEFISSEHLLLALLDDkGTLGKLLKEAGATADALEAAINAVRGGQKVTDANAEDQ--YE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 166 YLSKYAIDMTEQARQGKLDPVIGREEEIRSTIRVLARRIKSNPCLIGEPGIGKTAIIEGVAQRIIDDDVPTILQGAKLFS 245
Cdd:TIGR03346 155 ALEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 246 LDLAALTAGAKYKGDFEERFKGVLKEIEESKTLIVLFIDEIHMLMGNGKD----DAANILKPALSRGQLKVIGATTNNEY 321
Cdd:TIGR03346 235 LDMGALIAGAKYRGEFEERLKAVLNEVTKSEGQIILFIDELHTLVGAGKAegamDAGNMLKPALARGELHCIGATTLDEY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 322 RSIVEKDGAFERRFQKIEVAEPSVRQTVAILRGLQPKYEIHHGVRILDSALVTAAQLAKRYLPYRRLPDSALDLVDISCA 401
Cdd:TIGR03346 315 RKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 402 GVAVARDSKPEELDSKERQLQLIQVEIKALERDEDADSttKDRLKLARQKEASLQEELEPLRQRYNEEKHGHEELTQAKK 481
Cdd:TIGR03346 395 RIRMEIDSKPEELDELDRRIIQLEIEREALKKEKDEAS--KKRLEDLEKELADLEEEYAELEEQWKAEKASIQGIQQIKE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 482 KLDELENKALDAERRYDTATAADLRYFAIPDIKKQIekledQVAEEERRAGANSMIQNVVDSDTISETAARLTGIPVKKL 561
Cdd:TIGR03346 473 EIEQVRLELEQAEREGDLAKAAELQYGKLPELEKQL-----QAAEQKLGEEQNRLLREEVTAEEIAEVVSRWTGIPVSKM 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 562 SESENEKLIHMERDLSSEVVGQMDAIKAVSNAVRLSRSGLANPRQP-ASFLFLGLSGSGKTELAKKVAGFLFNDEDMMIR 640
Cdd:TIGR03346 548 LEGEREKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPiGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVR 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 641 VDCSELSEKYAVSKLLGTTAGYVGYDEGGFLTNQLQYKPYSVLLFDEVEKAHPDVLTVMLQMLDDGRITSGQGKTIDCSN 720
Cdd:TIGR03346 628 IDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRN 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 721 CIVIMTSNLGAEFINSQQGSKIQESTKNLVMGAVRQHFRPEFLNRISSIVIFNKLSRKAIHKIVDIRLKEIEERFEqnDK 800
Cdd:TIGR03346 708 TVIIMTSNLGSDFIQELAGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLA--ER 785
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1346246 801 HYKLNLTQEAKDFLAKYGYSDDMGARPLNRLIQNEILNKLALRILKNEIKDKETVNVVLKKGK 863
Cdd:TIGR03346 786 KITLELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGR 848
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
15-849 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 729.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 15 LTLAQKLASDHQHPQLQPIHILAAFIeTPEDGSVpylQNLIEKGRYDYDLFKKVVNRNLVRIPQQQPAPAEITPSYALGK 94
Cdd:PRK10865 14 LADAQSLALGHDNQFIEPLHLMSALL-NQEGGSV---RPLLTSAGINAGQLRTDINQALSRLPQVEGTGGDVQPSQDLVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 95 VLQDAAKIQKQQKDSFIAQD-HILFALFNDSSIQQIFKEAQVDIEAIKQQALELRGNTRIDSRGADTNTplEYLSKYAID 173
Cdd:PRK10865 90 VLNLCDKLAQKRGDNFISSElFVLAALESRGTLADILKAAGATTANITQAIEQMRGGESVNDQGAEDQR--QALKKYTID 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 174 MTEQARQGKLDPVIGREEEIRSTIRVLARRIKSNPCLIGEPGIGKTAIIEGVAQRIIDDDVPTILQGAKLFSLDLAALTA 253
Cdd:PRK10865 168 LTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLALDMGALVA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 254 GAKYKGDFEERFKGVLKEIEESKTLIVLFIDEIHMLMGNGKD----DAANILKPALSRGQLKVIGATTNNEYRSIVEKDG 329
Cdd:PRK10865 248 GAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKAdgamDAGNMLKPALARGELHCVGATTLDEYRQYIEKDA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 330 AFERRFQKIEVAEPSVRQTVAILRGLQPKYEIHHGVRILDSALVTAAQLAKRYLPYRRLPDSALDLVDISCAGVAVARDS 409
Cdd:PRK10865 328 ALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASSIRMQIDS 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 410 KPEELDSKERQLQLIQVEIKALERDedADSTTKDRLKLAR----QKE---ASLQEELEPLRQRYNEEKHGHEELTQAKKK 482
Cdd:PRK10865 408 KPEELDRLDRRIIQLKLEQQALMKE--SDEASKKRLDMLNeelsDKErqySELEEEWKAEKASLSGTQTIKAELEQAKIA 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 483 LDElenkaldAERRYDTATAADLRYFAIPDIKKQIEkledqvAEEERRAGANSMIQNVVDSDTISETAARLTGIPVKKLS 562
Cdd:PRK10865 486 IEQ-------ARRVGDLARMSELQYGKIPELEKQLA------AATQLEGKTMRLLRNKVTDAEIAEVLARWTGIPVSRML 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 563 ESENEKLIHMERDLSSEVVGQMDAIKAVSNAVRLSRSGLANPRQP-ASFLFLGLSGSGKTELAKKVAGFLFNDEDMMIRV 641
Cdd:PRK10865 553 ESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPiGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRI 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 642 DCSELSEKYAVSKLLGTTAGYVGYDEGGFLTNQLQYKPYSVLLFDEVEKAHPDVLTVMLQMLDDGRITSGQGKTIDCSNC 721
Cdd:PRK10865 633 DMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNT 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 722 IVIMTSNLGAEFINSQQGSKIQESTKNLVMGAVRQHFRPEFLNRISSIVIFNKLSRKAIHKIVDIRLKEIEERFEqnDKH 801
Cdd:PRK10865 713 VVIMTSNLGSDLIQERFGELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLE--ERG 790
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 1346246 802 YKLNLTQEAKDFLAKYGYSDDMGARPLNRLIQNEILNKLALRILKNEI 849
Cdd:PRK10865 791 YEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGEL 838
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
7-864 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 639.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 7 FTERALTILTLAQKLASDHQHPQLQPIHILAAFIEtpEDGSVPY--LQNLIEKGRYDYDLFKKVVNRN----LVRIPqqq 80
Cdd:CHL00095 5 FTEKAIKVIMLSQEEARRLGHNFVGTEQILLGLIG--EGTGIAAraLKSMGVTLKDARIEVEKIIGRGtgfvAVEIP--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 81 papaeITPSYAlgKVLQDAAKIQKQQKDSFIAQDHILFALFNDSS--IQQIFKEAQVDIEAIKQQALELRGNTRIDSRGA 158
Cdd:CHL00095 80 -----FTPRAK--RVLEMSLEEARDLGHNYIGTEHLLLALLEEGEgvAARVLENLGVDLSKIRSLILNLIGEIIEAILGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 159 DTN-TPLEYLSKYAIDMTEQARQGKLDPVIGREEEIRSTIRVLARRIKSNPCLIGEPGIGKTAIIEGVAQRIIDDDVPTI 237
Cdd:CHL00095 153 EQSrSKTPTLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 238 LQGAKLFSLDLAALTAGAKYKGDFEERFKGVLKEIEESKTlIVLFIDEIHMLMGNGKD----DAANILKPALSRGQLKVI 313
Cdd:CHL00095 233 LEDKLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQENNN-IILVIDEVHTLIGAGAAegaiDAANILKPALARGELQCI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 314 GATTNNEYRSIVEKDGAFERRFQKIEVAEPSVRQTVAILRGLQPKYEIHHGVRILDSALVTAAQLAKRYLPYRRLPDSAL 393
Cdd:CHL00095 312 GATTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 394 DLVDISCAGVAVARDSKPEELDSKERQLQLIQVEIKALERDEDAdsttkdrlklarqkeaslqEELEPLRQRYNEEKHGH 473
Cdd:CHL00095 392 DLLDEAGSRVRLINSRLPPAARELDKELREILKDKDEAIREQDF-------------------ETAKQLRDREMEVRAQI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 474 EELTQAKKKLDELENKALdaerrydtataadlryfaipdikkqiekledqvaeeerragansmiqnVVDSDTISETAARL 553
Cdd:CHL00095 453 AAIIQSKKTEEEKRLEVP------------------------------------------------VVTEEDIAEIVSAW 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 554 TGIPVKKLSESENEKLIHMERDLSSEVVGQMDAIKAVSNAVRLSRSGLANPRQP-ASFLFLGLSGSGKTELAKKVAGFLF 632
Cdd:CHL00095 485 TGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPiASFLFSGPTGVGKTELTKALASYFF 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 633 NDEDMMIRVDCSELSEKYAVSKLLGTTAGYVGYDEGGFLTNQLQYKPYSVLLFDEVEKAHPDVLTVMLQMLDDGRITSGQ 712
Cdd:CHL00095 565 GSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSK 644
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 713 GKTIDCSNCIVIMTSNLGAEFINSQQGS--------KIQEST----KNLVMGAVRQHFRPEFLNRISSIVIFNKLSRKAI 780
Cdd:CHL00095 645 GRTIDFKNTLIIMTSNLGSKVIETNSGGlgfelsenQLSEKQykrlSNLVNEELKQFFRPEFLNRLDEIIVFRQLTKNDV 724
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 781 HKIVDIRLKEIEERFEQNDkhYKLNLTQEAKDFLAKYGYSDDMGARPLNRLIQNEILNKLALRILKNEIKDKETVNVVLK 860
Cdd:CHL00095 725 WEIAEIMLKNLFKRLNEQG--IQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVDVN 802
|
....
gi 1346246 861 KGKS 864
Cdd:CHL00095 803 DEKE 806
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
18-858 |
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: 625.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 18 AQKLASDHQHPQLQPIHILAAFIETPedgsvpylQNLIEKGRYDYDLFKKVVNRNLVRIPQQQPAPAEITP--SYALGKV 95
Cdd:TIGR03345 12 AAALCVARGHPEVELEHWLLALLDQP--------DSDLAAILRHFGVDLGRLKADLARALDKLPRGNTRTPvfSPHLVEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 96 LQDA---AKIQKQqkDSFIAQDHILFALFNDSSIQQ----IFKE-AQVDIEAIKQQALELRGNTRIDSRGADTNTPLEY- 166
Cdd:TIGR03345 84 LQEAwllASLELG--DGRIRSGHLLLALLTDPELRRllgsISPElAKIDREALREALPALVEGSAEASAAAADAAPAGAa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 167 --------LSKYAIDMTEQARQGKLDPVIGREEEIRSTIRVLARRIKSNPCLIGEPGIGKTAIIEGVAQRIIDDDVPTIL 238
Cdd:TIGR03345 162 agaagtsaLDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVPPAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 239 QGAKLFSLDLAALTAGAKYKGDFEERFKGVLKEIEESKTLIVLFIDEIHMLMG----NGKDDAANILKPALSRGQLKVIG 314
Cdd:TIGR03345 242 RNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPIILFIDEAHTLIGaggqAGQGDAANLLKPALARGELRTIA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 315 ATTNNEYRSIVEKDGAFERRFQKIEVAEPSVRQTVAILRGLQPKYEIHHGVRILDSALVTAAQLAKRYLPYRRLPDSALD 394
Cdd:TIGR03345 322 ATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLPDKAVS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 395 LVDISCAGVAVARDSKPEELDSKERQLQLIQVEIKALERDEDADSTTKDRLKLARQKEASLQEELEPLRQRYNEEKhghe 474
Cdd:TIGR03345 402 LLDTACARVALSQNATPAALEDLRRRIAALELELDALEREAALGADHDERLAELRAELAALEAELAALEARWQQEK---- 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 475 ELTQAkkkLDELENKALDAERRYDTATAADLryfaipdikKQIEKLEDQVAEEErraGANSMIQNVVDSDTISETAARLT 554
Cdd:TIGR03345 478 ELVEA---ILALRAELEADADAPADDDDALR---------AQLAELEAALASAQ---GEEPLVFPEVDAQAVAEVVADWT 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 555 GIPVKKLSESENEKLIHMERDLSSEVVGQMDAIKAVSNAVRLSRSGLANPRQP-ASFLFLGLSGSGKTELAKKVAGFLFN 633
Cdd:TIGR03345 543 GIPVGRMVRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPlGVFLLVGPSGVGKTETALALAELLYG 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 634 DEDMMIRVDCSELSEKYAVSKLLGTTAGYVGYDEGGFLTNQLQYKPYSVLLFDEVEKAHPDVLTVMLQMLDDGRITSGQG 713
Cdd:TIGR03345 623 GEQNLITINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEG 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 714 KTIDCSNCIVIMTSNLGAEFIN--SQQGSKI--QESTKNLVMGAVRQHFRPEFLNRIsSIVIFNKLSRKAIHKIVDIRLK 789
Cdd:TIGR03345 703 REIDFKNTVILLTSNAGSDLIMalCADPETApdPEALLEALRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLD 781
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1346246 790 EIEERFEQNDKhYKLNLTQEAKDFLAKYGYSDDMGARPLNRLIQNEILNKLALRILkNEIKDKETVNVV 858
Cdd:TIGR03345 782 RIARRLKENHG-AELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQIL-ERLAAGEPIERI 848
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
15-863 |
2.00e-146 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 451.60 E-value: 2.00e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 15 LTLAQKLASDHQHPQLQPIHILAAFIETPEdgsvpyLQNLIEKGRYDYDLFKKVVNrnlVRIPQQQPA-PA-----EITP 88
Cdd:PRK11034 10 LNMAFARAREHRHEFMTVEHLLLALLSNPS------AREALEACSVDLVALRQELE---AFIEQTTPVlPAseeerDTQP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 89 SYALGKVLQDAAKIQKQQKDSFIAQDHILFALFNDSSIQQIFKEAQVDI----------EAIKQQALELRGNTRIDSRGA 158
Cdd:PRK11034 81 TLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVsrldvvnfisHGTRKDEPSQSSDPGSQPNSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 159 DTNTPLEYLSKYAIDMTEQARQGKLDPVIGREEEIRSTIRVLARRIKSNPCLIGEPGIGKTAIIEGVAQRIIDDDVPTIL 238
Cdd:PRK11034 161 EQAGGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 239 QGAKLFSLDLAALTAGAKYKGDFEERFKGVLKEIEESKTLIvLFIDEIHMLMG-----NGKDDAANILKPALSRGQLKVI 313
Cdd:PRK11034 241 ADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSI-LFIDEIHTIIGagaasGGQVDAANLIKPLLSSGKIRVI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 314 GATTNNEYRSIVEKDGAFERRFQKIEVAEPSVRQTVAILRGLQPKYEIHHGVRILDSALVTAAQLAKRYLPYRRLPDSAL 393
Cdd:PRK11034 320 GSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 394 DLVDiscagvavardskpeeldskerqlqliqveikalerdedadsttkdrlklarqkEASLQEELEPlrqryneekhgh 473
Cdd:PRK11034 400 DVID------------------------------------------------------EAGARARLMP------------ 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 474 eeltqakkkldelenkaldAERRYDTATAADlryfaipdikkqiekledqvaeeerragansmIQNVVdsdtisetaARL 553
Cdd:PRK11034 414 -------------------VSKRKKTVNVAD--------------------------------IESVV---------ARI 433
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 554 TGIPVKKLSESENEKLIHMERDLSSEVVGQMDAIKAVSNAVRLSRSGLANPRQP-ASFLFLGLSGSGKTELAKKVAGFLf 632
Cdd:PRK11034 434 ARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPvGSFLFAGPTGVGKTEVTVQLSKAL- 512
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 633 ndEDMMIRVDCSELSEKYAVSKLLGTTAGYVGYDEGGFLTNQLQYKPYSVLLFDEVEKAHPDVLTVMLQMLDDGRITSGQ 712
Cdd:PRK11034 513 --GIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNN 590
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 713 GKTIDCSNCIVIMTSNLGAEFINSQQGSKIQESTKNLVMGAVRQHFRPEFLNRISSIVIFNKLSRKAIHKIVDIRLKEIE 792
Cdd:PRK11034 591 GRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQ 670
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1346246 793 ERFEQndKHYKLNLTQEAKDFLAKYGYSDDMGARPLNRLIQNEILNKLALRILKNEIKDKETVNVVLKKGK 863
Cdd:PRK11034 671 AQLDQ--KGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKEK 739
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
568-772 |
1.80e-83 |
|
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: 265.58 E-value: 1.80e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 568 KLIHMERDLSSEVVGQMDAIKAVSNAVRLSRSGLANP-RQPASFLFLGLSGSGKTELAKKVAGFLFNDEDMMIRVDCSEL 646
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPnRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 647 SEKYAVSKLLGTTAGYVGYDEGGFLTNQLQYKPYSVLLFDEVEKAHPDVLTVMLQMLDDGRITSGQGKTIDCSNCIVIMT 726
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1346246 727 SNlgaefinsqqgskiqestknlvmgavrqHFRPEFLNRISSIVIF 772
Cdd:cd19499 161 SN----------------------------HFRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
605-769 |
1.69e-69 |
|
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: 227.85 E-value: 1.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 605 RQPASFLFLGLSGSGKTELAKKVAGFLFNDEDMMIRVDCSELSEKYAVSKLLGTTAGYVGYDEGGFLTNQLQYKPYSVLL 684
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 685 FDEVEKAHPDVLTVMLQMLDDGRITSGQGKTIDCSNCIVIMTSNLGAEFINSQQG---SKIQESTKNLVMGAVRQHFRPE 761
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRlgdSPDYELLKEEVMDLLKKGFIPE 160
|
....*...
gi 1346246 762 FLNRISSI 769
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 ... |
344-439 |
5.91e-33 |
|
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: 122.60 E-value: 5.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 344 SVRQTVAILRGLQPKYEIHHGVRILDSALVTAAQLAKRYLPYRRLPDSALDLVDISCAGVAVARDSKPEELDSKERQLQL 423
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90
....*....|....*.
gi 1346246 424 IQVEIKALERDEDADS 439
Cdd:pfam17871 81 LEIEKEALEREQDFEK 96
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
775-857 |
2.93e-24 |
|
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: 97.09 E-value: 2.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 775 LSRKAIHKIVDIRLKEIEERFEqnDKHYKLNLTQEAKDFLAKYGYSDDMGARPLNRLIQNEILNKLALRILKNEIKDKET 854
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLA--ERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDT 78
|
...
gi 1346246 855 VNV 857
Cdd:pfam10431 79 VRV 81
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
775-863 |
4.75e-22 |
|
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: 90.97 E-value: 4.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 775 LSRKAIHKIVDIRLKEIEERFEqnDKHYKLNLTQEAKDFLAKYGYSDDMGARPLNRLIQNEILNKLALRILKNEIKDKET 854
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLA--EKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDT 78
|
....*....
gi 1346246 855 VNVVLKKGK 863
Cdd:smart01086 79 VVVDVDDGE 87
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
187-343 |
1.50e-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: 89.13 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 187 IGREEEIRSTIRVLARRIKSNPCLIGEPGIGKTAIIEGVAQRIIDDDVPtilqgakLFSLDLAALTAGAKYKGDFEERFK 266
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 267 GVLKEIEESKTLIVLFIDEIHMLMGNGKDDAANILKPAL----SRGQLKVIGATTNNEYRsivEKDGAFERRFQKIEVAE 342
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNdlriDRENVRVIGATNRPLLG---DLDRALYDRLDIRIVIP 150
|
.
gi 1346246 343 P 343
Cdd:cd00009 151 L 151
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
581-774 |
1.82e-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: 77.19 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 581 VGQMDAIKAVSNAVRLsrsglanpRQPASFLFLGLSGSGKTELAKKVAGFLFNDEDMMIRVDCSELSEKYAVSkllgtta 660
Cdd:cd00009 1 VGQEEAIEALREALEL--------PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVA------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 661 GYVGYDEGGFLTNQLQYKPYSVLLFDEVEKAHPDVLTVMLQMLDDGRITsgqgkTIDCSNCIVIMTSNLGAEFInsqqgs 740
Cdd:cd00009 66 ELFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATNRPLLGD------ 134
|
170 180 190
....*....|....*....|....*....|....
gi 1346246 741 kiqestknlvmgavrqhFRPEFLNRISSIVIFNK 774
Cdd:cd00009 135 -----------------LDRALYDRLDIRIVIPL 151
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
209-338 |
1.02e-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: 68.77 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 209 CLIGEPGIGKTAIIEGVAQRIidddvptilqGAKLFSLDLAALTagAKYKGDFEERFKGVLKEIEESKtLIVLFIDEIHM 288
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELV--SKYVGESEKRLRELFEAAKKLA-PCVIFIDEIDA 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1346246 289 LMGNGKD-------DAANILKPALSRGQLK-----VIGATtnNEYRSIvekDGAFERRFQKI 338
Cdd:pfam00004 69 LAGSRGSggdsesrRVVNQLLTELDGFTSSnskviVIAAT--NRPDKL---DPALLGRFDRI 125
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
606-734 |
9.74e-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: 63.55 E-value: 9.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 606 QPASFLFLGLSGSGKTELAKKVAGFLFNDEDMMIRVDCSELSEKYAVSKLLGTTAGYVGYDEGG----FLTNQLQYKPYS 681
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGElrlrLALALARKLKPD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1346246 682 VLLFDEVEKAHPDVLTVMLQMLDDGRITsgqGKTIDCSNCIVIMTSNLGAEFI 734
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEELRLL---LLLKSEKNLTVILTTNDEKDLG 130
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
584-734 |
1.17e-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: 60.76 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 584 MDAIKAVSNAVRLSRSGLanpRQPASFLFLGLSGSGKTELAKKVAGFLFNDedmMIRVDCSELSEKYavskllgttaGYV 663
Cdd:cd19481 6 REAVEAPRRGSRLRRYGL---GLPKGILLYGPPGTGKTLLAKALAGELGLP---LIVVKLSSLLSKY----------VGE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 664 GYDEGGFLTNQLQYKPYSVLLFDEVEKAHPD------------VLTVMLQMLDDGRItsgqgktidCSNCIVIMTSNLGA 731
Cdd:cd19481 70 SEKNLRKIFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNS---------RSKVLVIAATNRPD 140
|
...
gi 1346246 732 EFI 734
Cdd:cd19481 141 LLD 143
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
176-367 |
1.22e-10 |
|
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: 64.55 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 176 EQARQGKLDPVIGrEEEIRSTIRVLARRIKSNP--------------CLIGEPGIGKTAIIEGVAQRIidddvptilqGA 241
Cdd:COG0464 149 LELREAILDDLGG-LEEVKEELRELVALPLKRPelreeyglppprglLLYGPPGTGKTLLARALAGEL----------GL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 242 KLFSLDLAALTagAKYKGDFEERFKGVLKEIEESKTlIVLFIDEIHMLMGNGKDDAANILKPALS---------RGQLKV 312
Cdd:COG0464 218 PLIEVDLSDLV--SKYVGETEKNLREVFDKARGLAP-CVLFIDEADALAGKRGEVGDGVGRRVVNtlltemeelRSDVVV 294
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1346246 313 IGATtnNEYRSIvekDGAFERRFQ-KIEVAEPSVRQTVAILRGLQPKYEIHHGVRI 367
Cdd:COG0464 295 IAAT--NRPDLL---DPALLRRFDeIIFFPLPDAEERLEIFRIHLRKRPLDEDVDL 345
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
99-149 |
1.70e-07 |
|
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: 48.67 E-value: 1.70e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1346246 99 AAKIQKQQKDSFIAQDHILFALFN--DSSIQQIFKEAQVDIEAIKQQALELRG 149
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEedDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
209-338 |
5.51e-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: 50.06 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 209 CLIGEPGIGKTAIIEGVAQRIIDDDVPTIL-----QGAKLFSLDLAALTAGAKYKGDFEERFKGVLKEIEESKtLIVLFI 283
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLK-PDVLIL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1346246 284 DEIHMLMGNG------KDDAANILKPALSRGQLKVIGATTnneyRSIVEKDGAFERRFQKI 338
Cdd:smart00382 85 DEITSLLDAEqealllLLEELRLLLLLKSEKNLTVILTTN----DEKDLGPALLRRRFDRR 141
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
412-530 |
3.55e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 412 EELDSKERQLQLIQVEIKALERDEDADSTTKD------RLKLARQKEASLQEELEPLRQRYNEEKHGHEELTQAKKKLDE 485
Cdd:COG4717 95 EELEELEEELEELEAELEELREELEKLEKLLQllplyqELEALEAELAELPERLEELEERLEELRELEEELEELEAELAE 174
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1346246 486 LENKALDAERRYDTATAADLRyfaipDIKKQIEKLEDQVAEEERR 530
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQ-----DLAEELEELQQRLAELEEE 214
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
209-335 |
7.06e-06 |
|
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: 46.52 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 209 CLIGEPGIGKTAIIEGVAQRIIDDDVPTILQGAKLFSLDlaaLTAGAKYKGDFEERFKGVLKEIEESKTliVLFIDEIHM 288
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSNRPVFYVQLTRDTTEED---LFGRRNIDPGGASWVDGPLVRAAREGE--IAVLDEINR 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1346246 289 lmgnGKDDAANILKPALSRGQL------KVIG---------ATTNNEYRSIVEKDGAFERRF 335
Cdd:pfam07728 78 ----ANPDVLNSLLSLLDERRLllpdggELVKaapdgfrliATMNPLDRGLNELSPALRSRF 135
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
611-728 |
1.88e-05 |
|
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: 44.89 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 611 LFLGLSGSGKTELAKKVAGFLFNDedmMIRVDCSELsekyaVSKLLGTTAGYVgydEGGFltNQLQYKPYSVLLFDEVEK 690
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAP---FIEISGSEL-----VSKYVGESEKRL---RELF--EAAKKLAPCVIFIDEIDA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1346246 691 AHP-----------DVLTVMLQMLDdgritsgqGKTIDCSNCIVIMTSN 728
Cdd:pfam00004 69 LAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
182-325 |
2.17e-05 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 47.77 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 182 KLDPVIGrEEEIRSTIRVLARRIKSN--PCLI--GEPGIGKTAIIEGVAQRIidddvptilqGAKLFSLDlaALTAGAKy 257
Cdd:PRK13342 10 TLDEVVG-QEHLLGPGKPLRRMIEAGrlSSMIlwGPPGTGKTTLARIIAGAT----------DAPFEALS--AVTSGVK- 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1346246 258 kgDFEErfkgVLKEIEESKTL---IVLFIDEIHMLmgN-GKDDAaniLKPALSRGQLKVIGATTNNEYRSIV 325
Cdd:PRK13342 76 --DLRE----VIEEARQRRSAgrrTILFIDEIHRF--NkAQQDA---LLPHVEDGTITLIGATTENPSFEVN 136
|
|
| RecA-like_Figl-1 |
cd19525 |
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ... |
210-337 |
2.56e-05 |
|
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: 45.75 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 210 LIGEPGIGKTAIIEGVAQRiidddvptilQGAKLFSLDLAALTagAKYKGDFEERFKGvLKEIEESKTLIVLFIDEIHML 289
Cdd:cd19525 60 LFGPPGTGKTLIGKCIASQ----------SGATFFSISASSLT--SKWVGEGEKMVRA-LFSVARCKQPAVIFIDEIDSL 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1346246 290 M---GNGKDDAANILKPALsrgQLKVIGATTNNEYRSIV--------EKDGAFERRFQK 337
Cdd:cd19525 127 LsqrGEGEHESSRRIKTEF---LVQLDGATTSSEDRILVvgatnrpqEIDEAARRRLVK 182
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
189-316 |
3.84e-05 |
|
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: 44.97 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 189 REEEIRSTIRVLARRIKSNPCLIGEPGIGKTAIIEGVAQRIidddvptilqGAKLFSLDLAALTagAKYKGDFEERFKGV 268
Cdd:cd19481 10 EAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGEL----------GLPLIVVKLSSLL--SKYVGESEKNLRKI 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 269 LKEIEESKTLIVlFIDEIHMLMGN----GKDDAANILKPAL--------SRGQLKVIGAT 316
Cdd:cd19481 78 FERARRLAPCIL-FIDEIDAIGRKrdssGESGELRRVLNQLlteldgvnSRSKVLVIAAT 136
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
415-792 |
4.94e-05 |
|
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: 46.83 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 415 DSKERQLQLIQVEIKALERDEDADSTTKDRLKLARQKEASLQEELEPLRQRYNEEKHGHEELTQAKKKLDELENKALDAE 494
Cdd:COG0464 1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 495 RRYDTATAADLRYFAIPDIKKQIEKLEDQVAEEERRAgansmiQNVVDSDTISETAARLTGIPVKKLSESENEKLIHMER 574
Cdd:COG0464 81 LLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERA------LLELLRESAEALALAAPLVTYEDIGGLEEELLELREA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 575 DLSsEVVG---QMDAIKAVSNAVR-----LSRSGLANPRqpaSFLFLGLSGSGKTELAKKVAGFLfndeDM-MIRVDCSE 645
Cdd:COG0464 155 ILD-DLGGleeVKEELRELVALPLkrpelREEYGLPPPR---GLLLYGPPGTGKTLLARALAGEL----GLpLIEVDLSD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 646 LsekyaVSKLLGTTAGYVgyDEggfLTNQLQYKPYSVLLFDEVEKAHPD-----------VLTVMLQMLDDGRitsgqgk 714
Cdd:COG0464 227 L-----VSKYVGETEKNL--RE---VFDKARGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR------- 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1346246 715 tidcSNCIVIMTSNLgaefinsqqgskiqestknlvmgavRQHFRPEFLNRISSIVIFNKLSRKAIHKIVDIRLKEIE 792
Cdd:COG0464 290 ----SDVVVIAATNR-------------------------PDLLDPALLRRFDEIIFFPLPDAEERLEIFRIHLRKRP 338
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
210-353 |
4.96e-05 |
|
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: 47.21 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 210 LIGEPGIGKTAIIEGVAQRIidddvptilqGAKLFSLDLAALTAgaKYKGDFEERFKGVLKEIEESKTLIVlFIDEIHML 289
Cdd:TIGR01243 217 LYGPPGTGKTLLAKAVANEA----------GAYFISINGPEIMS--KYYGESEERLREIFKEAEENAPSII-FIDEIDAI 283
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1346246 290 MGNGKDDAANILKPALS-----------RGQLKVIGATTN-NEYRSIVEKDGAFERrfqKIEVAEPSVRQTVAILR 353
Cdd:TIGR01243 284 APKREEVTGEVEKRVVAqlltlmdglkgRGRVIVIGATNRpDALDPALRRPGRFDR---EIVIRVPDKRARKEILK 356
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
185-287 |
5.44e-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: 44.42 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 185 PVIGREEEIRSTIRVLARRIKSNPCLI---GEPGIGKTAIIEGVAQRIIDDDV-------------PTILQGAKLFSL-- 246
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPPSVlltGEAGTGKTTLLRELLRALERDGGyflrgkcdenlpySPLLEALTREGLlr 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1346246 247 -----------------DLAALTAGAKYKGDFEERFKGVLKEI----EESKTLIVLFIDEIH 287
Cdd:pfam13191 81 qlldelesslleawraaLLEALAPVPELPGDLAERLLDLLLRLldllARGERPLVLVLDDLQ 142
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
418-575 |
8.06e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 418 ERQLQLIQVEIKALERDEDAdsttkdrlklARQKEASLQEELEPLRQRYNEEKhghEELTQAKKKLDELENKALDAERRy 497
Cdd:COG3883 15 DPQIQAKQKELSELQAELEA----------AQAELDALQAELEELNEEYNELQ---AELEALQAEIDKLQAEIAEAEAE- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1346246 498 dtataadlryfaipdIKKQIEKLEDQVAEEERRAGANSMIQNVVDSDTISETAARLTGipVKKLSESENEKLIHMERD 575
Cdd:COG3883 81 ---------------IEERREELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSA--LSKIADADADLLEELKAD 141
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
182-325 |
1.31e-04 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 45.43 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 182 KLDPVIGrEEEIRSTIRVLARRIKSN--PCLI--GEPGIGKTAIIEGVAQRIidddvptilqGAKLFSLDlaALTAGAKy 257
Cdd:COG2256 23 TLDEVVG-QEHLLGPGKPLRRAIEAGrlSSMIlwGPPGTGKTTLARLIANAT----------DAEFVALS--AVTSGVK- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1346246 258 kgDfeerfkgvLKE-IEESKTL------IVLFIDEIHMLmgN-GKDDAaniLKPALSRGQLKVIGATTNNEYRSIV 325
Cdd:COG2256 89 --D--------IREvIEEARERraygrrTILFVDEIHRF--NkAQQDA---LLPHVEDGTITLIGATTENPSFEVN 149
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
210-337 |
2.26e-04 |
|
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410917 [Multi-domain] Cd Length: 163 Bit Score: 42.72 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 210 LIGEPGIGKTAIIEGVAQRIidddvptilqGAKLFSLDLAALTAgaKYKGDFEERFKGVLKEIEESKTLIVlFIDEIHML 289
Cdd:cd19509 37 LYGPPGTGKTLLARAVASES----------GSTFFSISASSLVS--KWVGESEKIVRALFALARELQPSII-FIDEIDSL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1346246 290 M---GNGKDDAANILK----------PALSRGQLKVIGATTNNEyrsivEKDGAFERRFQK 337
Cdd:cd19509 104 LserGSGEHEASRRVKteflvqmdgvLNKPEDRVLVLGATNRPW-----ELDEAFLRRFEK 159
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
210-313 |
4.10e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 41.17 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 210 LIGEPGIGKTAIIEGVAQRIIDDDVPTIL------QGAKLFSLDLA-ALTAGAKYKGDFEERFKGVLKEIEESKTLIVLF 282
Cdd:pfam13401 10 LTGESGTGKTTLLRRLLEQLPEVRDSVVFvdlpsgTSPKDLLRALLrALGLPLSGRLSKEELLAALQQLLLALAVAVVLI 89
|
90 100 110
....*....|....*....|....*....|...
gi 1346246 283 IDEIHMLmgngKDDAANILK--PALSRGQLKVI 313
Cdd:pfam13401 90 IDEAQHL----SLEALEELRdlLNLSSKLLQLI 118
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
189-353 |
4.24e-04 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 42.95 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 189 REEEIRSTIRVLARRIksnpCLIGEPGIGKTAIIEGVAQRIiddDVPtilqgakLFSLDLAALTAgaKYKGDFEERFKGV 268
Cdd:COG1223 23 RRENLRKFGLWPPRKI----LFYGPPGTGKTMLAEALAGEL---KLP-------LLTVRLDSLIG--SYLGETARNLRKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 269 LKEIEESKTliVLFIDEIHMLmGNGKDDAA---------NILKPALS--RGQLKVIGATtnNEYRSIvekDGAFERRFQ- 336
Cdd:COG1223 87 FDFARRAPC--VIFFDEFDAI-AKDRGDQNdvgevkrvvNALLQELDglPSGSVVIAAT--NHPELL---DSALWRRFDe 158
|
170
....*....|....*..
gi 1346246 337 KIEVAEPSVRQTVAILR 353
Cdd:COG1223 159 VIEFPLPDKEERKEILE 175
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
202-337 |
4.40e-04 |
|
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: 41.89 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 202 RRIKSNPCLIGEPGIGKTAIIEGVAQRIidddvptilqGAKLFSLDLAALTagAKYKGDfEERFKGVLKEIEESKTLIVL 281
Cdd:cd19522 30 RRPWKGVLMVGPPGTGKTLLAKAVATEC----------GTTFFNVSSSTLT--SKYRGE-SEKLVRLLFEMARFYAPTTI 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 282 FIDEIHMLM----GNGKDDAANILKPALSRGQLKVIGATTNNEYRSIV----------EKDGAFERRFQK 337
Cdd:cd19522 97 FIDEIDSICsrrgTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVmvlaatnfpwDIDEALRRRLEK 166
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
413-588 |
5.39e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 413 ELDSKERQLQLIQVEIKAL----ERDEDA-------DSTTKDRLKLARQKEASLQEELEPLRQRYnEEKHGHEELTQA-K 480
Cdd:PRK04778 276 DLDEAEEKNEEIQERIDQLydilEREVKArkyveknSDTLPDFLEHAKEQNKELKEEIDRVKQSY-TLNESELESVRQlE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 481 KKLDELENKALDAERRYDTATAAdlrYFAIPD-----------IKKQIEKLEDQVA---EEERRagANSMIQNVVdsDTI 546
Cdd:PRK04778 355 KQLESLEKQYDEITERIAEQEIA---YSELQEeleeilkqleeIEKEQEKLSEMLQglrKDELE--AREKLERYR--NKL 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1346246 547 SET-----AARLTGIP-------------VKKLSESENEKLIHMER--DLSSEVVGQMDAIK 588
Cdd:PRK04778 428 HEIkryleKSNLPGLPedylemffevsdeIEALAEELEEKPINMEAvnRLLEEATEDVETLE 489
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
418-533 |
5.80e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 418 ERQLQLIQveiKALERDEDADSTTKDRLKLARQKEASLQEELEPLRQRYNEekHGHEELTQAKKKLDELENKALDAERRY 497
Cdd:COG4913 287 QRRLELLE---AELEELRAELARLEAELERLEARLDALREELDELEAQIRG--NGGDRLEQLEREIERLERELEERERRR 361
|
90 100 110
....*....|....*....|....*....|....*...
gi 1346246 498 DT--ATAADLRyFAIPDIKKQIEKLEDQVAEEERRAGA 533
Cdd:COG4913 362 ARleALLAALG-LPLPASAEEFAALRAEAAALLEALEE 398
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
414-589 |
6.53e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 414 LDSKERQLQLIQVEIKALER-----DEDADSTTKDRLKLARQKE--------ASLQEELEPLRQRYNEEKHGHEELTQAK 480
Cdd:COG4913 612 LAALEAELAELEEELAEAEErlealEAELDALQERREALQRLAEyswdeidvASAEREIAELEAELERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 481 KKLDELENKALDAERRYDTATAadlryfAIPDIKKQIEKLEDQVAEEERRAGANSMIQNVVDSDTISETAARLTGIPV-K 559
Cdd:COG4913 692 EQLEELEAELEELEEELDELKG------EIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVeR 765
|
170 180 190
....*....|....*....|....*....|...
gi 1346246 560 KLSE---SENEKLIHMERDLSSEVVGQMDAIKA 589
Cdd:COG4913 766 ELREnleERIDALRARLNRAEEELERAMRAFNR 798
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
412-533 |
8.65e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 412 EELDSKERQLQL------IQVEIKALERDEDADSTTKDRLKL--ARQKEASLQEELEPLRQRYNEEKhghEELTQAKKKL 483
Cdd:COG4913 242 EALEDAREQIELlepireLAERYAAARERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARLE---AELERLEARL 318
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1346246 484 DELENKALDAERRYDTATAADLRyfaipDIKKQIEKLEDQVAEEERRAGA 533
Cdd:COG4913 319 DALREELDELEAQIRGNGGDRLE-----QLEREIERLERELEERERRRAR 363
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
412-602 |
9.82e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 412 EELDSKERQLQLIQVEIKALERDEDADSTTKDRLK---------LARQKE--ASLQEELEPLRQRYNEEKHGHEELTQAK 480
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELEskldelaeeLAELEEklEELKEELESLEAELEELEAELEELESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 481 KKLDEL---ENKALDAERRYDTATAADLRYfaipdIKKQIEKLEDQVAEEERRAGANSMIQNVVDSDTISETAARLtgip 557
Cdd:TIGR02168 375 EELEEQletLRSKVAQLELQIASLNNEIER-----LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL---- 445
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1346246 558 vkklsESENEKLIHMERDLSSEVVGQMDAIKAVSNAVRLSRSGLA 602
Cdd:TIGR02168 446 -----EEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
413-539 |
1.03e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 413 ELDSKERQLQLIQVEIKALERDEDADSTTKDRLKLARQKEASLQEELEPLRQRYNEEKhghEELTQAKKKLDELENKALD 492
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE---KELEQAEEELDELQDRLEA 738
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1346246 493 AERRYDTATAADL-RYFAIPDIKKQIEKLEDQVaeEERRAGANSMIQN 539
Cdd:COG4913 739 AEDLARLELRALLeERFAAALGDAVERELRENL--EERIDALRARLNR 784
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
580-690 |
1.28e-03 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410905 [Multi-domain] Cd Length: 251 Bit Score: 41.43 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 580 VVGQMDAIKAVSNAV-----RLsRSGLANPRQPASF-----LFLGLSGSGKTELAKKVAGFLfnDEDMMIrVDCSELSEk 649
Cdd:cd19497 14 VIGQERAKKVLSVAVynhykRI-RNNLKQKDDDVELeksniLLIGPTGSGKTLLAQTLAKIL--DVPFAI-ADATTLTE- 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1346246 650 yavskllgttAGYVGYDEGGFLTNQLQYKPYSV-------LLFDEVEK 690
Cdd:cd19497 89 ----------AGYVGEDVENILLKLLQAADYDVeraqrgiVYIDEIDK 126
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
409-554 |
1.38e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 409 SKPEELDSKERQLQLIQVEIKALERdedadsttkdRLKLARQKEASLQEELEPLRQRyneekhgheeLTQAKKKLDELEN 488
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEK----------ELAALKKEEKALLKQLAALERR----------IAALARRIRALEQ 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1346246 489 KALDAERRYDTATAadlryfAIPDIKKQIEKLEDQVAEEER---RAGANSMIQNVVDSDTISETAARLT 554
Cdd:COG4942 77 ELAALEAELAELEK------EIAELRAELEAQKEELAELLRalyRLGRQPPLALLLSPEDFLDAVRRLQ 139
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
210-286 |
1.63e-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: 40.35 E-value: 1.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1346246 210 LIGEPGIGKTAIIEGVAQRIidddvptilqGAKLFSLDLAALTagAKYKGDFEERFKGVLKEIEESKTLIvLFIDEI 286
Cdd:cd19503 39 LHGPPGTGKTLLARAVANEA----------GANFLSISGPSIV--SKYLGESEKNLREIFEEARSHAPSI-IFIDEI 102
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
605-708 |
1.78e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 39.25 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 605 RQPASFLFL-GLSGSGKTELAKKVAGFLFNDEDMMIRVDCSELSEKYAVSKLL--GTTAGYVGYDEGGFLTNQLQ----- 676
Cdd:pfam13401 2 RFGAGILVLtGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRALlrALGLPLSGRLSKEELLAALQqllla 81
|
90 100 110
....*....|....*....|....*....|..
gi 1346246 677 YKPYSVLLFDEVEKAHPDVLTVMLQMLDDGRI 708
Cdd:pfam13401 82 LAVAVVLIIDEAQHLSLEALEELRDLLNLSSK 113
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
412-531 |
2.77e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 412 EELDSKERQLQLIQVEIKALERDEDADSTTKDRLKLARQKeasLQEELEPLRQRYNEEKHGHEELTQAKKKLDELENKAL 491
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEE---LELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1346246 492 DAERRYDTATAAdlryfaipdIKKQIEKLEDQVAEEERRA 531
Cdd:COG1196 316 ERLEELEEELAE---------LEEELEELEEELEELEEEL 346
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
210-289 |
2.77e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 40.54 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 210 LIGEPGIGKTAIIEGVAQRIIDDDVPTILQGAKLFSLDLAA-------LTAGAKYKGDFEERFKGVLKEIEESKTLIVLF 282
Cdd:COG3267 48 LTGEVGTGKTTLLRRLLERLPDDVKVAYIPNPQLSPAELLRaiadelgLEPKGASKADLLRQLQEFLLELAAAGRRVVLI 127
|
....*..
gi 1346246 283 IDEIHML 289
Cdd:COG3267 128 IDEAQNL 134
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
412-528 |
3.25e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 412 EELDSKERQLQLIQVEIKALERDEDADSTTKDRLKLARQKEASLQEELEPLRQRYNEEKHGHEELTQAKKKLDELENKAL 491
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348
|
90 100 110
....*....|....*....|....*....|....*..
gi 1346246 492 DAERRYDTATAADLRYFAIPDIKKQIEKLEDQVAEEE 528
Cdd:PRK03918 349 ELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLT 385
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
332-526 |
5.37e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 332 ERRFQKIEVAEPSVRQTVAILRGLQPKYEIHHGVRILDSALVTAAQLAKRYLPYRRLPDSALDLVDISCAGvAVARDSKP 411
Cdd:COG1196 583 RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG-EGGSAGGS 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 412 EELDSKERQLQLIQVEIKALERDEDADSTTKDRLKLARQKEASLQEELEPLRQRYNEEKHGHEELTQAKKKLDELENKAL 491
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
170 180 190
....*....|....*....|....*....|....*..
gi 1346246 492 DAERRYDTATAA--DLRYFAIPDIKKQIEKLEDQVAE 526
Cdd:COG1196 742 LEEEELLEEEALeeLPEPPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
401-531 |
5.41e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 401 AGVAVARDSKPEELDSKERQLQLIQVEIKALERDEDADSTTKDRLKLARQKEASLQEELEPLRQRYNEEKhghEELTQAK 480
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE---AELAEAE 364
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1346246 481 KKLDELENKALDAERRYDTATAADLRYF-AIPDIKKQIEKLEDQVAEEERRA 531
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALrAAAELAAQLEELEEAEEALLERL 416
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
419-530 |
5.53e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 419 RQLQLIQVEIKALERDEDADSTTKDRLKLARQKEASLQEELEPLRQRYNEEKHGHEELTQAK------KKLDELENKALD 492
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplyQELEALEAELAE 143
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1346246 493 AERRYDTATAADLRY----FAIPDIKKQIEKLEDQVAEEERR 530
Cdd:COG4717 144 LPERLEELEERLEELreleEELEELEAELAELQEELEELLEQ 185
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
178-237 |
7.52e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 40.23 E-value: 7.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1346246 178 ARQGKLDPVIGREEEIRSTIRVLARRIKSNP---CLIGEPGIGKTAIIEGVAQRIIDDDVPTI 237
Cdd:COG3899 281 ARRLIPQPLVGREAELAALLAALERARAGRGelvLVSGEAGIGKSRLVRELARRARARGGRVL 343
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
412-531 |
7.86e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 412 EELDSKERQLQLIQVEIKALERDEDAdstTKDRLKLARQKEASLQEELEPLRQRYN----EEKHGHEELTQAKKKLDELE 487
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIAR---LEERRRELEERLEELEEELAELEEELEeleeELEELEEELEEAEEELEEAE 357
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1346246 488 NKALDAERRYDTATAADLryfaipDIKKQIEKLEDQVAEEERRA 531
Cdd:COG1196 358 AELAEAEEALLEAEAELA------EAEEELEELAEELLEALRAA 395
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
574-666 |
9.20e-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: 38.13 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346246 574 RDLSSEVVGQMDAIKAVSNAV--RLSRSGLANPRQ----PASFLFLGLSGSGKTELAKKVAGFLfndEDMMIRVDCSELS 647
Cdd:cd19498 7 SELDKYIIGQDEAKRAVAIALrnRWRRMQLPEELRdevtPKNILMIGPTGVGKTEIARRLAKLA---GAPFIKVEATKFT 83
|
90
....*....|....*....
gi 1346246 648 EkyavskllgttAGYVGYD 666
Cdd:cd19498 84 E-----------VGYVGRD 91
|
|
| |
