|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
107-735 |
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: 953.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 107 LGQYGLNLTDLAKQGKIDPVIGRDKEIERVIEILNRRTKNNPVLIGEAGVGKTAVVEGLAQRIVEGSVPQKLLNKQIIRL 186
Cdd:COG0542 162 LDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDKRVLSL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 187 DVVSLVQGTGIRGQFEQRMQELMKEVQN-NPDLIVFIDEIHEIVGAGNAEGGMDAGNVLKPALARGDFQLVGATTLKEFR 265
Cdd:COG0542 242 DLGALVAGAKYRGEFEERLKAVLDEVKKsEGNIILFIDELHTLVGAGGAEGAMDAANLLKPALARGELRCIGATTLDEYR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 266 D-IEKDAALARRLQPVQVDEPSEEEAIKILKGIQKKYEDYHHVHYTDDAIVAAVKLSKRYIQDRYLPDKAIDLLDEAGSK 344
Cdd:COG0542 322 KyIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAIDLIDEAAAR 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 345 KNLTINVADPE--TIQKKIDEAEAEKKKALESED---YEKAAYYRDQVSKLEKNKDGATNKEDE---------------- 403
Cdd:COG0542 402 VRMEIDSKPEEldELERRLEQLEIEKEALKKEQDeasFERLAELRDELAELEEELEALKARWEAekelieeiqelkeele 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 404 ----------------------------PTITAEDMEKIIESKTDIPVGDLQKQEQEQLQNLASNLKAHVIGQDEAVDKI 455
Cdd:COG0542 482 qrygkipelekelaeleeelaelapllrEEVTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEEELHERVIGQDEAVEAV 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 456 SRAIRRNRIGLNGTGRPIGSFLFVGPTGVGKTELAKQLADQLFGSKDAMIRFDMSEYMEPHSISKLIGSPPGYVGYEEAG 535
Cdd:COG0542 562 ADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYMEKHSVSRLIGAPPGYVGYEEGG 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 536 QLTEQVRRHPYSLILLDEVEKAHPDVMHMFLQILDDGRLTDSQGRTVSFKDTIIIMTSNAGSGDVEADVGFGAAMQGKTH 615
Cdd:COG0542 642 QLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIGSELILDLAEDEPDYEEMKE 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 616 SVLDKLGNYFKPEFLNRFDDIVEFHALTKDNLMQIVDLMIADVNKMLATQGLHVNVTKPVEERLVELGYDPKMGARPLRR 695
Cdd:COG0542 722 AVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAAKDFLAEKGYDPEYGARPLKR 801
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 2672004240 696 VIQEQIEDRIAdfyldhpseKQLIAR--IKDDKIEVAPEDKK 735
Cdd:COG0542 802 AIQRELEDPLA---------EEILAGeiKEGDTITVDVDDGE 834
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
107-734 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 780.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 107 LGQYGLNLTDLAKQGKIDPVIGRDKEIERVIEILNRRTKNNPVLIGEAGVGKTAVVEGLAQRIVEGSVPQKLLNKQIIRL 186
Cdd:CHL00095 162 LEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDKLVITL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 187 DVVSLVQGTGIRGQFEQRMQELMKEVQNNPDLIVFIDEIHEIVGAGNAEGGMDAGNVLKPALARGDFQLVGATTLKEFRD 266
Cdd:CHL00095 242 DIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLDEYRK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 267 -IEKDAALARRLQPVQVDEPSEEEAIKILKGIQKKYEDYHHVHYTDDAIVAAVKLSKRYIQDRYLPDKAIDLLDEAGSKK 345
Cdd:CHL00095 322 hIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLDEAGSRV 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 346 NLtINVADPETIQ---KKIDEAEAEKKKALESEDYEKAAYYRD-------QVSKLEKNKDGATNKEDE-PTITAEDMEKI 414
Cdd:CHL00095 402 RL-INSRLPPAAReldKELREILKDKDEAIREQDFETAKQLRDremevraQIAAIIQSKKTEEEKRLEvPVVTEEDIAEI 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 415 IESKTDIPVGDLQKQEQEQLQNLASNLKAHVIGQDEAVDKISRAIRRNRIGLNGTGRPIGSFLFVGPTGVGKTELAKQLA 494
Cdd:CHL00095 481 VSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 495 DQLFGSKDAMIRFDMSEYMEPHSISKLIGSPPGYVGYEEAGQLTEQVRRHPYSLILLDEVEKAHPDVMHMFLQILDDGRL 574
Cdd:CHL00095 561 SYFFGSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRL 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 575 TDSQGRTVSFKDTIIIMTSNAGSGDVE---ADVGFGAAMQGKTHS--------VLDKLGNYFKPEFLNRFDDIVEFHALT 643
Cdd:CHL00095 641 TDSKGRTIDFKNTLIIMTSNLGSKVIEtnsGGLGFELSENQLSEKqykrlsnlVNEELKQFFRPEFLNRLDEIIVFRQLT 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 644 KDNLMQIVDLMIADVNKMLATQGLHVNVTKPVEERLVELGYDPKMGARPLRRVIQEQIEDRIADFYLDHPSEKQLIARI- 722
Cdd:CHL00095 721 KNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVd 800
|
650
....*....|....
gi 2672004240 723 --KDDKIEVAPEDK 734
Cdd:CHL00095 801 vnDEKEVKILLINK 814
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
107-706 |
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: 773.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 107 LGQYGLNLTDLAKQGKIDPVIGRDKEIERVIEILNRRTKNNPVLIGEAGVGKTAVVEGLAQRIVEGSVPQKLLNKQIIRL 186
Cdd:TIGR03346 156 LEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 187 DVVSLVQGTGIRGQFEQRMQELMKEVQN-NPDLIVFIDEIHEIVGAGNAEGGMDAGNVLKPALARGDFQLVGATTLKEFR 265
Cdd:TIGR03346 236 DMGALIAGAKYRGEFEERLKAVLNEVTKsEGQIILFIDELHTLVGAGKAEGAMDAGNMLKPALARGELHCIGATTLDEYR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 266 D-IEKDAALARRLQPVQVDEPSEEEAIKILKGIQKKYEDYHHVHYTDDAIVAAVKLSKRYIQDRYLPDKAIDLLDEAGSK 344
Cdd:TIGR03346 316 KyIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAAR 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 345 KNLTINvADPET--------IQKKI---------DEAEAEKKKALESE-------------------------------- 375
Cdd:TIGR03346 396 IRMEID-SKPEEldeldrriIQLEIerealkkekDEASKKRLEDLEKEladleeeyaeleeqwkaekasiqgiqqikeei 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 376 --------------DYEKAAYYR-DQVSKLEKNKDGATNKEDEPT-------ITAEDMEKIIESKTDIPVGDLQKQEQEQ 433
Cdd:TIGR03346 475 eqvrleleqaeregDLAKAAELQyGKLPELEKQLQAAEQKLGEEQnrllreeVTAEEIAEVVSRWTGIPVSKMLEGEREK 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 434 LQNLASNLKAHVIGQDEAVDKISRAIRRNRIGLNGTGRPIGSFLFVGPTGVGKTELAKQLADQLFGSKDAMIRFDMSEYM 513
Cdd:TIGR03346 555 LLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRIDMSEYM 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 514 EPHSISKLIGSPPGYVGYEEAGQLTEQVRRHPYSLILLDEVEKAHPDVMHMFLQILDDGRLTDSQGRTVSFKDTIIIMTS 593
Cdd:TIGR03346 635 EKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMTS 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 594 NAGSGDVEADVGfGAAMQGKTHSVLDKLGNYFKPEFLNRFDDIVEFHALTKDNLMQIVDLMIADVNKMLATQGLHVNVTK 673
Cdd:TIGR03346 715 NLGSDFIQELAG-GDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKITLELSD 793
|
650 660 670
....*....|....*....|....*....|...
gi 2672004240 674 PVEERLVELGYDPKMGARPLRRVIQEQIEDRIA 706
Cdd:TIGR03346 794 AALDFLAEAGYDPVYGARPLKRAIQREIENPLA 826
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
104-707 |
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: 674.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 104 SSLLGQYGLNLTDLAKQGKIDPVIGRDKEIERVIEILNRRTKNNPVLIGEAGVGKTAVVEGLAQRIVEGSVPQKLLNKQI 183
Cdd:TIGR02639 161 QDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERLKNAKI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 184 IRLDVVSLVQGTGIRGQFEQRMQELMKEVQNNPDLIVFIDEIHEIVGAGNAEGG-MDAGNVLKPALARGDFQLVGATTLK 262
Cdd:TIGR02639 241 YSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFIDEIHTIVGAGATSGGsMDASNLLKPALSSGKIRCIGSTTYE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 263 EFRDI-EKDAALARRLQPVQVDEPSEEEAIKILKGIQKKYEDYHHVHYTDDAIVAAVKLSKRYIQDRYLPDKAIDLLDEA 341
Cdd:TIGR02639 321 EYKNHfEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDVIDEA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 342 GSKKNLtinvadpetiqkkideAEAEKKKAlesedyekaayyrdqvskleknkdgatnkedepTITAEDMEKIIESKTDI 421
Cdd:TIGR02639 401 GAAFRL----------------RPKAKKKA---------------------------------NVNVKDIENVVAKMAKI 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 422 PVGDLQKQEQEQLQNLASNLKAHVIGQDEAVDKISRAIRRNRIGLNGTGRPIGSFLFVGPTGVGKTELAKQLADQLfgsK 501
Cdd:TIGR02639 432 PVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEEL---G 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 502 DAMIRFDMSEYMEPHSISKLIGSPPGYVGYEEAGQLTEQVRRHPYSLILLDEVEKAHPDVMHMFLQILDDGRLTDSQGRT 581
Cdd:TIGR02639 509 VHLLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRK 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 582 VSFKDTIIIMTSNAGSGDV-EADVGFGAamQGKTHSVLDKLGNYFKPEFLNRFDDIVEFHALTKDNLMQIVDLMIADVNK 660
Cdd:TIGR02639 589 ADFRNVILIMTSNAGASEMsKPPIGFGG--ENRESKSLKAIKKLFSPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQD 666
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 2672004240 661 MLATQGLHVNVTKPVEERLVELGYDPKMGARPLRRVIQEQIEDRIAD 707
Cdd:TIGR02639 667 QLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSD 713
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
107-706 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 626.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 107 LGQYGLNLTDLAKQGKIDPVIGRDKEIERVIEILNRRTKNNPVLIGEAGVGKTAVVEGLAQRIVEGSVPQKLLNKQIIRL 186
Cdd:PRK10865 161 LKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLAL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 187 DVVSLVQGTGIRGQFEQRMQELMKEV-QNNPDLIVFIDEIHEIVGAGNAEGGMDAGNVLKPALARGDFQLVGATTLKEFR 265
Cdd:PRK10865 241 DMGALVAGAKYRGEFEERLKGVLNDLaKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYR 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 266 D-IEKDAALARRLQPVQVDEPSEEEAIKILKGIQKKYEDYHHVHYTDDAIVAAVKLSKRYIQDRYLPDKAIDLLDEAGSK 344
Cdd:PRK10865 321 QyIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASS 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 345 KNLTINvADPETI-----------------QKKIDEAEAEKKKALESEDYEKAAYYRD---------------------- 385
Cdd:PRK10865 401 IRMQID-SKPEELdrldrriiqlkleqqalMKESDEASKKRLDMLNEELSDKERQYSEleeewkaekaslsgtqtikael 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 386 -------------------------QVSKLEKNKDGATNKEDEPT------ITAEDMEKIIESKTDIPVGDLQKQEQEQL 434
Cdd:PRK10865 480 eqakiaieqarrvgdlarmselqygKIPELEKQLAAATQLEGKTMrllrnkVTDAEIAEVLARWTGIPVSRMLESEREKL 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 435 QNLASNLKAHVIGQDEAVDKISRAIRRNRIGLNGTGRPIGSFLFVGPTGVGKTELAKQLADQLFGSKDAMIRFDMSEYME 514
Cdd:PRK10865 560 LRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFME 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 515 PHSISKLIGSPPGYVGYEEAGQLTEQVRRHPYSLILLDEVEKAHPDVMHMFLQILDDGRLTDSQGRTVSFKDTIIIMTSN 594
Cdd:PRK10865 640 KHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSN 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 595 AGSGDVEADVGfGAAMQGKTHSVLDKLGNYFKPEFLNRFDDIVEFHALTKDNLMQIVDLMIADVNKMLATQGLHVNVTKP 674
Cdd:PRK10865 720 LGSDLIQERFG-ELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYEIHISDE 798
|
650 660 670
....*....|....*....|....*....|..
gi 2672004240 675 VEERLVELGYDPKMGARPLRRVIQEQIEDRIA 706
Cdd:PRK10865 799 ALKLLSENGYDPVYGARPLKRAIQQQIENPLA 830
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
105-722 |
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: 608.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 105 SLLGQYGLNLTDLAKQGKIDPVIGRDKEIERVIEILNRRTKNNPVLIGEAGVGKTAVVEGLAQRIVEGSVPQKLLNKQII 184
Cdd:TIGR03345 168 SALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVPPALRNVRLL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 185 RLDVVSLVQGTGIRGQFEQRMQELMKEVQNNPD-LIVFIDEIHEIVGAGNAEGGMDAGNVLKPALARGDFQLVGATTLKE 263
Cdd:TIGR03345 248 SLDLGLLQAGASVKGEFENRLKSVIDEVKASPQpIILFIDEAHTLIGAGGQAGQGDAANLLKPALARGELRTIAATTWAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 264 FRD-IEKDAALARRLQPVQVDEPSEEEAIKILKGIQKKYEDYHHVHYTDDAIVAAVKLSKRYIQDRYLPDKAIDLLDEAG 342
Cdd:TIGR03345 328 YKKyFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLPDKAVSLLDTAC 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 343 SKKNLTINvADPETIQ---KKIDEAEAE-----------------------KKKALESEDYEKAAYYRDQ---VSKL--- 390
Cdd:TIGR03345 408 ARVALSQN-ATPAALEdlrRRIAALELEldalereaalgadhderlaelraELAALEAELAALEARWQQEkelVEAIlal 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 391 -EKNKDGATNKEDE--------------------------PTITAEDMEKIIESKTDIPVGDLQKQEQEQLQNLASNLKA 443
Cdd:TIGR03345 487 rAELEADADAPADDddalraqlaeleaalasaqgeeplvfPEVDAQAVAEVVADWTGIPVGRMVRDEIEAVLSLPDRLAE 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 444 HVIGQDEAVDKISRAIRRNRIGLNGTGRPIGSFLFVGPTGVGKTELAKQLADQLFGSKDAMIRFDMSEYMEPHSISKLIG 523
Cdd:TIGR03345 567 RVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGEQNLITINMSEFQEAHTVSRLKG 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 524 SPPGYVGYEEAGQLTEQVRRHPYSLILLDEVEKAHPDVMHMFLQILDDGRLTDSQGRTVSFKDTIIIMTSNAGSGDVEAd 603
Cdd:TIGR03345 647 SPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVILLTSNAGSDLIMA- 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 604 vgfgAAMQGKTHSVLDK--------LGNYFKPEFLNRFdDIVEFHALTKDNLMQIVDLMIADVNKMLATQ-GLHVNVTKP 674
Cdd:TIGR03345 726 ----LCADPETAPDPEAllealrpeLLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRIARRLKENhGAELVYSEA 800
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2672004240 675 VEERLVELGYDPKMGARPLRRVIQEQIEDRIADFYLDHPSEKQLIARI 722
Cdd:TIGR03345 801 LVEHIVARCTEVESGARNIDAILNQTLLPELSRQILERLAAGEPIERI 848
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
107-707 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 544.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 107 LGQYGLNLTDLAKQGKIDPVIGRDKEIERVIEILNRRTKNNPVLIGEAGVGKTAVVEGLAQRIVEGSVPQKLLNKQIIRL 186
Cdd:PRK11034 169 MENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 187 DVVSLVQGTGIRGQFEQRMQELMKEVQNNPDLIVFIDEIHEIVGAGNAEGG-MDAGNVLKPALARGDFQLVGATTLKEFR 265
Cdd:PRK11034 249 DIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSGKIRVIGSTTYQEFS 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 266 DI-EKDAALARRLQPVQVDEPSEEEAIKILKGIQKKYEDYHHVHYTDDAIVAAVKLSKRYIQDRYLPDKAIDLLDEAGSK 344
Cdd:PRK11034 329 NIfEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 345 KNLTinvadPETIQKKideaeaekkkalesedyekaayyrdqvskleknkdgatnkedepTITAEDMEKIIESKTDIPVG 424
Cdd:PRK11034 409 ARLM-----PVSKRKK--------------------------------------------TVNVADIESVVARIARIPEK 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 425 DLQKQEQEQLQNLASNLKAHVIGQDEAVDKISRAIRRNRIGLNGTGRPIGSFLFVGPTGVGKTELAKQLAdQLFGSKdaM 504
Cdd:PRK11034 440 SVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLS-KALGIE--L 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 505 IRFDMSEYMEPHSISKLIGSPPGYVGYEEAGQLTEQVRRHPYSLILLDEVEKAHPDVMHMFLQILDDGRLTDSQGRTVSF 584
Cdd:PRK11034 517 LRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADF 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 585 KDTIIIMTSNAGSGDVEADvGFGAAMQGKTHSVLDKLGNYFKPEFLNRFDDIVEFHALTKDNLMQIVDLMIADVNKMLAT 664
Cdd:PRK11034 597 RNVVLVMTTNAGVRETERK-SIGLIHQDNSTDAMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQ 675
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2672004240 665 QGLHVNVTKPVEERLVELGYDPKMGARPLRRVIQEQIEDRIAD 707
Cdd:PRK11034 676 KGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLAN 718
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
436-639 |
1.56e-96 |
|
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: 296.40 E-value: 1.56e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 436 NLASNLKAHVIGQDEAVDKISRAIRRNRIGLNGTGRPIGSFLFVGPTGVGKTELAKQLADQLFGSKDAMIRFDMSEYMEP 515
Cdd:cd19499 4 NLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEYMEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 516 HSISKLIGSPPGYVGYEEAGQLTEQVRRHPYSLILLDEVEKAHPDVMHMFLQILDDGRLTDSQGRTVSFKDTIIIMTSna 595
Cdd:cd19499 84 HSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTS-- 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2672004240 596 gsgdveadvgfgaamqgkthsvldklgNYFKPEFLNRFDDIVEF 639
Cdd:cd19499 162 ---------------------------NHFRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
471-636 |
7.69e-87 |
|
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: 270.61 E-value: 7.69e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 471 RPIGSFLFVGPTGVGKTELAKQLADQLFGSKDAMIRFDMSEYMEPHSISKLIGSPPGYVGYEEAGQLTEQVRRHPYSLIL 550
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 551 LDEVEKAHPDVMHMFLQILDDGRLTDSQGRTVSFKDTIIIMTSNAGSGDVEADVGFGA--AMQGKTHSVLDKLGNYFKPE 628
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRLGDspDYELLKEEVMDLLKKGFIPE 160
|
....*...
gi 2672004240 629 FLNRFDDI 636
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 ... |
286-386 |
1.14e-42 |
|
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: 149.94 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 286 SEEEAIKILKGIQKKYEDYHHVHYTDDAIVAAVKLSKRYIQDRYLPDKAIDLLDEAGSKKNLTINV--ADPETIQKKIDE 363
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESkpEELEDLERELAK 80
|
90 100
....*....|....*....|...
gi 2672004240 364 AEAEKKKALESEDYEKAAYYRDQ 386
Cdd:pfam17871 81 LEIEKEALEREQDFEKAERLAKL 103
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
642-716 |
2.78e-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: 96.71 E-value: 2.78e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2672004240 642 LTKDNLMQIVDLMIADVNKMLATQGLHVNVTKPVEERLVELGYDPKMGARPLRRVIQEQIEDRIADFYLDHPSEK 716
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKE 75
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
642-729 |
7.63e-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) 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: 95.97 E-value: 7.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 642 LTKDNLMQIVDLMIADVNKMLATQGLHVNVTKPVEERLVELGYDPKMGARPLRRVIQEQIEDRIADFYL--DHPSEKQLI 719
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILsgELKDGDTVV 80
|
90
....*....|
gi 2672004240 720 ARIKDDKIEV 729
Cdd:smart01086 81 VDVDDGELVF 90
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
446-594 |
2.87e-18 |
|
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: 82.19 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 446 IGQDEAVDKISRAIRRNriglngtgrPIGSFLFVGPTGVGKTELAKQLADQLFGSKDAMIRFDMSEYMEPHSISKLIgsp 525
Cdd:cd00009 1 VGQEEAIEALREALELP---------PPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELF--- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2672004240 526 pgyvGYEEAGQLTEQVRRHPYSLILLDEVEKAHPDVMHMFLQILDDGRLTdsqgrTVSFKDTIIIMTSN 594
Cdd:cd00009 69 ----GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATN 128
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
127-278 |
1.12e-15 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 74.88 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 127 IGRDKEIERVIEILNRRTKNNPVLIGEAGVGKTAVVEGLAQRIVEGSVPqkllnkqIIRLDVVSLVQGTGIRGQFEQRMQ 206
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2672004240 207 ELMKEVQNNPDL-IVFIDEIHEIvGAGNAEGGMDAGNVLKPALA-RGDFQLVGATTLKEFRDIekDAALARRLQ 278
Cdd:cd00009 74 RLLFELAEKAKPgVLFIDEIDSL-SRGAQNALLRVLETLNDLRIdRENVRVIGATNRPLLGDL--DRALYDRLD 144
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
477-594 |
4.00e-14 |
|
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: 70.09 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 477 LFVGPTGVGKTELAKQLADQLFGSKDAMIRFDMSEYMEPHSISKLI----GSPPGYVGYEEAGQLTEQVRRHPYSLILLD 552
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLiivgGKKASGSGELRLRLALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2672004240 553 EVEKAHPDVMHMFLQILDDGRLTDsqgRTVSFKDTIIIMTSN 594
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLL---LLKSEKNLTVILTTN 124
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
475-633 |
8.51e-11 |
|
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: 60.38 E-value: 8.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 475 SFLFVGPTGVGKTELAKQLADQLFGSKDAMIRfdMSEYMEPhsiSKLIGS--PPGYVGYEEAGQLTEQVRRHpySLILLD 552
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQ--LTRDTTE---EDLFGRrnIDPGGASWVDGPLVRAAREG--EIAVLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 553 EVEKAHPDVMHMFLQILDDGRLTDSQGRT---VSFKDTIIIMTSNagsgdveadvgfgaamqgkthsVLDKLGNYFKPEF 629
Cdd:pfam07728 74 EINRANPDVLNSLLSLLDERRLLLPDGGElvkAAPDGFRLIATMN----------------------PLDRGLNELSPAL 131
|
....
gi 2672004240 630 LNRF 633
Cdd:pfam07728 132 RSRF 135
|
|
| McsA |
COG3880 |
Protein-arginine kinase activator protein McsA [Posttranslational modification, protein ... |
1-32 |
1.00e-10 |
|
Protein-arginine kinase activator protein McsA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443088 [Multi-domain] Cd Length: 173 Bit Score: 61.06 E-value: 1.00e-10
10 20 30
....*....|....*....|....*....|..
gi 2672004240 1 MLCQNCHKNEATIHLYTNVNGRRTEVNLCQNC 32
Cdd:COG3880 1 MLCERCKKRPATVHLTQIINGEKTEVHLCEEC 32
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
450-639 |
6.68e-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: 58.45 E-value: 6.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 450 EAVDKISRAIRRNRIGLNGTGRPIGSFLFVGPTGVGKTELAKQLADQLfGSKdaMIRFDMSEYMEPhsiskligsppgYV 529
Cdd:cd19481 3 ASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGEL-GLP--LIVVKLSSLLSK------------YV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 530 GYEEA--GQLTEQVRRHPYSLILLDEVEKA---------HPDVMHMFLQILDdgrLTDSQGRTvsfKDTIIIMTSNagsg 598
Cdd:cd19481 68 GESEKnlRKIFERARRLAPCILFIDEIDAIgrkrdssgeSGELRRVLNQLLT---ELDGVNSR---SKVLVIAATN---- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2672004240 599 dveadvgfgaamqgkthsvldkLGNYFKPEFL--NRFDDIVEF 639
Cdd:cd19481 138 ----------------------RPDLLDPALLrpGRFDEVIEF 158
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
150-278 |
8.65e-10 |
|
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: 57.22 E-value: 8.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 150 LIGEAGVGKTAVVEGLAQRivegsvpqklLNKQIIRLDVVSLVQGtgIRGQFEQRMQELMKEVQNNPDLIVFIDEIHEIV 229
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKE----------LGAPFIEISGSELVSK--YVGESEKRLRELFEAAKKLAPCVIFIDEIDALA 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2672004240 230 GAGNAEGGMDAG---NVLKPAL-----ARGDFQLVGATTlkEFRDIekDAALARRLQ 278
Cdd:pfam00004 71 GSRGSGGDSESRrvvNQLLTELdgftsSNSKVIVIAATN--RPDKL--DPALLGRFD 123
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
144-277 |
4.73e-09 |
|
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: 55.84 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 144 TKNNPVLIGEAGVGKTAVVEGLAQRIVEGSVPQKLLNKQIIRLDVVSLVQGTGIR-----GQFEQRMQELMKEVQNNPDL 218
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGgkkasGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2672004240 219 IVFIDEIHEIVGAGNAEGGMDA--GNVLKPALARGDFQLVGATTLkefRDIEKDAALARRL 277
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLeeLRLLLLLKSEKNLTVILTTND---EKDLGPALLRRRF 138
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
445-657 |
3.71e-08 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 56.07 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 445 VIGQDEAVDKISRAI--------RRNRIGLngtgRPIGSFLFVGPTGVGKTELAKQLADQLFGSkdaMIRFDMSEymeph 516
Cdd:COG0464 159 LGGLEEVKEELRELValplkrpeLREEYGL----PPPRGLLLYGPPGTGKTLLARALAGELGLP---LIEVDLSD----- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 517 siskLIGsppGYVGyeEAGQLTEQV----RRHPYSLILLDEVEKAHPD-----------VMHMFLQILDDGRltdsqgrt 581
Cdd:COG0464 227 ----LVS---KYVG--ETEKNLREVfdkaRGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR-------- 289
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2672004240 582 vsfKDTIIIMTSNagsgDVEAdvgfgaamqgkthsvLDklgnyfkPEFLNRFDDIVEFHALTKDNLMQIVDLMIAD 657
Cdd:COG0464 290 ---SDVVVIAATN----RPDL---------------LD-------PALLRRFDEIIFFPLPDAEERLEIFRIHLRK 336
|
|
| UVR |
pfam02151 |
UvrB/uvrC motif; |
358-392 |
1.38e-07 |
|
UvrB/uvrC motif;
Pssm-ID: 308001 [Multi-domain] Cd Length: 36 Bit Score: 48.16 E-value: 1.38e-07
10 20 30
....*....|....*....|....*....|....*
gi 2672004240 358 QKKIDEAEAEKKKALESEDYEKAAYYRDQVSKLEK 392
Cdd:pfam02151 1 KKLIKELEEEMEEAAENEDFEKAAKLRDQINALKK 35
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
474-573 |
1.83e-07 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 50.42 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 474 GSFLFVGPTGVGKTELAKQLADQLFGSKDAMIRFDMSEYMEP----HSISKLIGSPPGYVGYEEA--GQLTEQVRRHP-Y 546
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPkdllRALLRALGLPLSGRLSKEEllAALQQLLLALAvA 85
|
90 100
....*....|....*....|....*..
gi 2672004240 547 SLILLDEVEKAHPDVMHMFLQILDDGR 573
Cdd:pfam13401 86 VVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
124-302 |
2.73e-07 |
|
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: 53.38 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 124 DPVIGRDKEIERVIEILNRRTKNNPV-------------LIGEAGVGKTAVVEGLAqrivegsvpqKLLNKQIIRLDVVS 190
Cdd:COG0464 157 DDLGGLEEVKEELRELVALPLKRPELreeyglppprgllLYGPPGTGKTLLARALA----------GELGLPLIEVDLSD 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 191 LVqgTGIRGQFEQRMQELMKEVQNNPDLIVFIDEIHEIVGAGNAEGGMDAGNV----LKpALA--RGDFQLVGATTLkeF 264
Cdd:COG0464 227 LV--SKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVvntlLT-EMEelRSDVVVIAATNR--P 301
|
170 180 190
....*....|....*....|....*....|....*....
gi 2672004240 265 RDIekDAALARRLQ-PVQVDEPSEEEAIKILKGIQKKYE 302
Cdd:COG0464 302 DLL--DPALLRRFDeIIFFPLPDAEERLEIFRIHLRKRP 338
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
443-494 |
5.74e-07 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 52.12 E-value: 5.74e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2672004240 443 AHVIGQDEAVDKISRAIRRNRIGlngtgrpiGSFLFVGPTGVGKTELAKQLA 494
Cdd:COG2812 10 DDVVGQEHVVRTLKNALASGRLA--------HAYLFTGPRGVGKTTLARILA 53
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
445-658 |
5.80e-07 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 51.42 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 445 VIGQDEAVDKISRAIR--RNRIGLNGTGR-PIGSFLFVGPTGVGKTELAKQLADQLfGSKDAMIRFDmseymephsisKL 521
Cdd:COG1223 4 VVGQEEAKKKLKLIIKelRRRENLRKFGLwPPRKILFYGPPGTGKTMLAEALAGEL-KLPLLTVRLD-----------SL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 522 IGSppgYVGyEEAGQLT---EQVRRHPySLILLDEVE---------KAHPD---VMHMFLQILDDGRltdsqgrtvsfKD 586
Cdd:COG1223 72 IGS---YLG-ETARNLRklfDFARRAP-CVIFFDEFDaiakdrgdqNDVGEvkrVVNALLQELDGLP-----------SG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2672004240 587 TIIIMTSNAGsgdveadvgfgaamqgkthSVLDklgnyfkPEFLNRFDDIVEFHALTKDNLMQIVDLMIADV 658
Cdd:COG1223 136 SVVIAATNHP-------------------ELLD-------SALWRRFDEVIEFPLPDKEERKEILELNLKKF 181
|
|
| PRK07399 |
PRK07399 |
DNA polymerase III subunit delta'; Validated |
440-506 |
2.38e-06 |
|
DNA polymerase III subunit delta'; Validated
Pssm-ID: 236011 [Multi-domain] Cd Length: 314 Bit Score: 50.28 E-value: 2.38e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2672004240 440 NLKAHVIGQDEAVDKISRAIRRNRIGlngtgrPigSFLFVGPTGVGKTELAKQLADQLF--GSKDAMIR 506
Cdd:PRK07399 1 NLFANLIGQPLAIELLTAAIKQNRIA------P--AYLFAGPEGVGRKLAALCFIEGLLsqGSPSKNIR 61
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
125-228 |
2.55e-06 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 48.27 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 125 PVIGRDKEIERVIEILNRRTKNNP---VLIGEAGVGKTAVVEGLAQRIVE----------------GSVPQKLLNKQIIR 185
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERdggyflrgkcdenlpySPLLEALTREGLLR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2672004240 186 ----------------LDVVSLVQGTGIRGQFEQRMQELMKEV-----QNNPDLIVFIDEIHEI 228
Cdd:pfam13191 81 qlldelesslleawraALLEALAPVPELPGDLAERLLDLLLRLldllaRGERPLVLVLDDLQWA 144
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
477-594 |
4.02e-06 |
|
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: 46.82 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 477 LFVGPTGVGKTELAKQLADQLfgsKDAMIRFDMSEymephSISKLIGSPPGYVgyeeaGQLTEQVRRHPYSLILLDEVEK 556
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKEL---GAPFIEISGSE-----LVSKYVGESEKRL-----RELFEAAKKLAPCVIFIDEIDA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2672004240 557 AHP-----------DVMHMFLQILDdgrltdsqGRTVSFKDTIIIMTSN 594
Cdd:pfam00004 69 LAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
149-277 |
7.26e-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: 46.13 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 149 VLIGEAGVGKTAVVEGLAQRIVEGSVPQKLLNKQIIRLDvvsLVQGTGIRGQ-FEQRMQELMKEVQNNpdLIVFIDEIH- 226
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSNRPVFYVQLTRDTTEED---LFGRRNIDPGgASWVDGPLVRAAREG--EIAVLDEINr 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 227 ---EIVGAGNA------EGGMDAGNVLKPALArgDFQLVGATTLKEFRDIEKDAALARRL 277
Cdd:pfam07728 78 anpDVLNSLLSllderrLLLPDGGELVKAAPD--GFRLIATMNPLDRGLNELSPALRSRF 135
|
|
| PRK05298 |
PRK05298 |
excinuclease ABC subunit UvrB; |
333-392 |
2.27e-05 |
|
excinuclease ABC subunit UvrB;
Pssm-ID: 235395 [Multi-domain] Cd Length: 652 Bit Score: 47.73 E-value: 2.27e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2672004240 333 KAI-DLLDEAGSKKNLTinvadPETIQKKIDEAEAEKKKALESEDYEKAAYYRDQVSKLEK 392
Cdd:PRK05298 591 KKIrDILDSVYKKDKLS-----KKELEKLIKELEKQMKEAAKNLEFEEAARLRDEIKELKE 646
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
437-594 |
3.94e-05 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 46.31 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 437 LASNLKAHVIGQDEAVDKISRAIRrnriglngTGRPIgsfLFVGPTGVGKTELAKQLADQLFGSkdaMIRFDMSEYMEPh 516
Cdd:COG0714 6 LRAEIGKVYVGQEELIELVLIALL--------AGGHL---LLEGVPGVGKTTLAKALARALGLP---FIRIQFTPDLLP- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 517 siSKLIGSppgyvgyEEAGQLTEQVRRHP----YSLILLDEVEKAHPDVMHMFLQILDDGRLTdSQGRTVSFKDT-IIIM 591
Cdd:COG0714 71 --SDILGT-------YIYDQQTGEFEFRPgplfANVLLADEINRAPPKTQSALLEAMEERQVT-IPGGTYKLPEPfLVIA 140
|
...
gi 2672004240 592 TSN 594
Cdd:COG0714 141 TQN 143
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
448-556 |
6.23e-05 |
|
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
Pssm-ID: 440238 [Multi-domain] Cd Length: 289 Bit Score: 45.35 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 448 QDEAVDKISRAIRRNRIGlngtgrpiGSFLFVGPTGVGKTELAKQLADQLFGSKDAmirfDMSEYMEPHSISKLIGSPPG 527
Cdd:COG0470 1 QEEAWEQLLAAAESGRLP--------HALLLHGPPGIGKTTLALALARDLLCENPE----GGKACGQCHSRLMAAGNHPD 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2672004240 528 YV---GYEEAGQLT-EQVRR-----------HPYSLILLDEVEK 556
Cdd:COG0470 69 LLelnPEEKSDQIGiDQIRElgeflsltpleGGRKVVIIDEADA 112
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
437-556 |
7.76e-05 |
|
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410906 [Multi-domain] Cd Length: 183 Bit Score: 43.91 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 437 LASNLKAHVIGQDEAVDKISRAIRrNRIGLNGTGRPI------GSFLFVGPTGVGKTELAKQLAdQLFGSkdAMIRFDMS 510
Cdd:cd19498 5 IVSELDKYIIGQDEAKRAVAIALR-NRWRRMQLPEELrdevtpKNILMIGPTGVGKTEIARRLA-KLAGA--PFIKVEAT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2672004240 511 EYMEphsiskligspPGYVGYEeagqlTEQVRRHPYS-LILLDEVEK 556
Cdd:cd19498 81 KFTE-----------VGYVGRD-----VESIIRDLVEgIVFIDEIDK 111
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
443-555 |
9.83e-05 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 45.00 E-value: 9.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 443 AHVIGQDEAVDKISRAI---RRN-----RIGLngtgRPIGSFLFVGPTGVGKTELAKQLADQLfgskDA-MIRFDMSEym 513
Cdd:COG1222 78 DDIGGLDEQIEEIREAVelpLKNpelfrKYGI----EPPKGVLLYGPPGTGKTLLAKAVAGEL----GApFIRVRGSE-- 147
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2672004240 514 ephSISKLIGsppgyvgyeEAGQLTEQV----RRHPYSLILLDEVE 555
Cdd:COG1222 148 ---LVSKYIG---------EGARNVREVfelaREKAPSIIFIDEID 181
|
|
| McsA |
COG3880 |
Protein-arginine kinase activator protein McsA [Posttranslational modification, protein ... |
357-392 |
1.15e-04 |
|
Protein-arginine kinase activator protein McsA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443088 [Multi-domain] Cd Length: 173 Bit Score: 43.35 E-value: 1.15e-04
10 20 30
....*....|....*....|....*....|....*.
gi 2672004240 357 IQKKIDEAEAEKKKALESEDYEKAAYYRDQVSKLEK 392
Cdd:COG3880 131 IKREIEELKEELQEAVEKEEYEEAAELRDEIRELEK 166
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
125-174 |
1.99e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 44.85 E-value: 1.99e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2672004240 125 PVIGRDKEIERVIEILNR--RTKNNPVLI-GEAGVGKTAVVEGLAQRIVEGSV 174
Cdd:COG3899 288 PLVGREAELAALLAALERarAGRGELVLVsGEAGIGKSRLVRELARRARARGG 340
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
447-498 |
2.18e-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: 42.20 E-value: 2.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2672004240 447 GQDEAVDKISRAIRRNRIGlngtgrpiGSFLFVGPTGVGKTELAKQLADQLF 498
Cdd:pfam13177 1 GQPEAIQLLQNSLENGRLS--------HAYLFSGPEGVGKLELALAFAKALF 44
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
150-276 |
3.92e-04 |
|
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: 41.50 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 150 LIGEAGVGKTAVVEGLAqrivegsvpqKLLNKQIIRLDVVSLVqgTGIRGQFEQRMQELMKEVQNNPDLIVFIDEIHEIV 229
Cdd:cd19481 31 LYGPPGTGKTLLAKALA----------GELGLPLIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDAIG 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2672004240 230 GAGNAEGGMDAGNVLKPAL--------ARGDFQLVGATTLKEfrdiEKDAALARR 276
Cdd:cd19481 99 RKRDSSGESGELRRVLNQLlteldgvnSRSKVLVIAATNRPD----LLDPALLRP 149
|
|
| TIGR02928 |
TIGR02928 |
orc1/cdc6 family replication initiation protein; Members of this protein family are found ... |
124-233 |
4.53e-04 |
|
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: 43.01 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 124 DPVIGRDKEIERVI----EILNRRTKNNPVLIGEAGVGKTAVVEGLAQRIvEGSVPQKLLNKQIIRLD----------VV 189
Cdd:TIGR02928 15 DRIVHRDEQIEELAkalrPILRGSRPSNVFIYGKTGTGKTAVTKYVMKEL-EEAAEDRDVRVVTVYVNcqildtlyqvLV 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2672004240 190 SLVQGTGIRGQ--------FEQRMQELMKEVQNNPDLIVFI-DEIHEIVGAGN 233
Cdd:TIGR02928 94 ELANQLRGSGEevpttglsTSEVFRRLYKELNERGDSLIIVlDEIDYLVGDDD 146
|
|
| UvrB |
COG0556 |
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair]; |
297-392 |
5.60e-04 |
|
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
Pssm-ID: 440322 [Multi-domain] Cd Length: 657 Bit Score: 43.46 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 297 IQKKYEDYHHVhyTDDAIVAAVK--LSKRYIQDRYLPDKAIDLLDEAGSKKNLtinvadpetiQKKIDEAEAEKKKALES 374
Cdd:COG0556 571 IQEAYNEEHGI--TPQTIKKSIRdiLEGTYEADEETEELVAEADAAKLSKEEL----------EKLIKELEKEMKEAAKN 638
|
90
....*....|....*...
gi 2672004240 375 EDYEKAAYYRDQVSKLEK 392
Cdd:COG0556 639 LEFEEAARLRDEIKELKK 656
|
|
| COG2842 |
COG2842 |
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ... |
477-654 |
8.07e-04 |
|
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];
Pssm-ID: 442090 [Multi-domain] Cd Length: 254 Bit Score: 41.86 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 477 LFVGPTGVGKTELAKQLADQlfgSKDA-MIRfdMSEYMEPHSISKLI------GSPPGYVGyEEAGQLTEQVRRHPYsLI 549
Cdd:COG2842 54 VVYGESGVGKTTAAREYANR---NPNViYVT--ASPSWTSKELLEELaeelgiPAPPGTIA-DLRDRILERLAGTGR-LL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 550 LLDEVEKAHPDVMHMFLQILDdgrltdsqgrtvsfkdtiiimtsnagsgdvEADVGFgaAMQGkTHSVLDKLGNYfkPEF 629
Cdd:COG2842 127 IIDEADHLKPKALEELRDIHD------------------------------ETGVGV--VLIG-MERLPAKLKRY--EQL 171
|
170 180
....*....|....*....|....*
gi 2672004240 630 LNRFDDIVEFHALTKDNLMQIVDLM 654
Cdd:COG2842 172 YSRIGFWVEFKPLSLEDVRALAEAW 196
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
443-494 |
9.46e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 42.49 E-value: 9.46e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2672004240 443 AHVIGQDEAVDKISRAIRRNRIGlngtgrpiGSFLFVGPTGVGKTELAKQLA 494
Cdd:PRK14950 16 AELVGQEHVVQTLRNAIAEGRVA--------HAYLFTGPRGVGKTSTARILA 59
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
444-582 |
1.39e-03 |
|
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: 40.18 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 444 HVIGQDEAVDKISRAIRRNRiglngTGRPiGSFLFVGPTGVGKTELAKQLADQLFGSKDAMIRFDMSEYMEPHSISKLIG 523
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVR-----SGRP-PSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPLLEALT 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2672004240 524 SPPGYVGYEEAGQLTEQVRRHPYSLILLDEVEKAHPDVMHMFLQILDD--GRLTDSQGRTV 582
Cdd:pfam13191 75 REGLLRQLLDELESSLLEAWRAALLEALAPVPELPGDLAERLLDLLLRllDLLARGERPLV 135
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
142-228 |
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 2672004240 142 RRTKNNPVLIGEAGVGKTAVVEGLAQRIVEGSVPQKLLN-------KQIIRldvvSLVQGTGIRGQFEQRMQELMKEVQN 214
Cdd:pfam13401 2 RFGAGILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDlpsgtspKDLLR----ALLRALGLPLSGRLSKEELLAALQQ 77
|
90
....*....|....*....
gi 2672004240 215 N-----PDLIVFIDEIHEI 228
Cdd:pfam13401 78 LllalaVAVVLIIDEAQHL 96
|
|
| hslU |
PRK05201 |
ATP-dependent protease ATPase subunit HslU; |
441-494 |
2.42e-03 |
|
ATP-dependent protease ATPase subunit HslU;
Pssm-ID: 235364 [Multi-domain] Cd Length: 443 Bit Score: 40.83 E-value: 2.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2672004240 441 LKAHVIGQDEAvdKISRAI------RRNRigLNGTGR----P--IgsfLFVGPTGVGKTELAKQLA 494
Cdd:PRK05201 13 LDKYIIGQDDA--KRAVAIalrnrwRRMQ--LPEELRdevtPknI---LMIGPTGVGKTEIARRLA 71
|
|
| PRK06647 |
PRK06647 |
DNA polymerase III subunits gamma and tau; Validated |
444-497 |
3.66e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 235845 [Multi-domain] Cd Length: 563 Bit Score: 40.52 E-value: 3.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2672004240 444 HVIGQDEAVDKISRAIRRNRIGlngtgrpiGSFLFVGPTGVGKTELAKQLADQL 497
Cdd:PRK06647 17 SLEGQDFVVETLKHSIESNKIA--------NAYIFSGPRGVGKTSSARAFARCL 62
|
|
| PRK14956 |
PRK14956 |
DNA polymerase III subunits gamma and tau; Provisional |
445-497 |
3.72e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184920 [Multi-domain] Cd Length: 484 Bit Score: 40.31 E-value: 3.72e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2672004240 445 VIGQDEAVDKISRAIRRNRIGlngtgrpiGSFLFVGPTGVGKTELAKQLADQL 497
Cdd:PRK14956 20 VIHQDLAIGALQNALKSGKIG--------HAYIFFGPRGVGKTTIARILAKRL 64
|
|
| RecA-like_FtsH |
cd19501 |
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ... |
445-555 |
4.49e-03 |
|
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and 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: 410909 [Multi-domain] Cd Length: 171 Bit Score: 38.75 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2672004240 445 VIGQDEA-------VDKISRAIRRNRIGlngtGRPIGSFLFVGPTGVGKTELAKQLADQlfgskdAMIRF---DMSEYME 514
Cdd:cd19501 6 VAGCEEAkeelkevVEFLKNPEKFTKLG----AKIPKGVLLVGPPGTGKTLLAKAVAGE------AGVPFfsiSGSDFVE 75
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2672004240 515 phsisKLIGsppgyVGYEEAGQLTEQVRRHPYSLILLDEVE 555
Cdd:cd19501 76 -----MFVG-----VGASRVRDLFEQAKKNAPCIVFIDEID 106
|
|
| HslU |
COG1220 |
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ... |
444-494 |
5.36e-03 |
|
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440833 [Multi-domain] Cd Length: 454 Bit Score: 40.03 E-value: 5.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2672004240 444 HVIGQDEAvdKISRAIR-RNRIglngtgR-------------P--IgsfLFVGPTGVGKTELAKQLA 494
Cdd:COG1220 16 YIIGQDEA--KRAVAIAlRNRW------RrqqlpeelrdeitPknI---LMIGPTGVGKTEIARRLA 71
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
445-497 |
6.06e-03 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 39.68 E-value: 6.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2672004240 445 VIGQDEAVDK---ISRAIRRNRIGlngtgrpigSFLFVGPTGVGKTELAKQLADQL 497
Cdd:PRK13342 14 VVGQEHLLGPgkpLRRMIEAGRLS---------SMILWGPPGTGKTTLARIIAGAT 60
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
437-494 |
7.69e-03 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 39.08 E-value: 7.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2672004240 437 LASNLKAHvIGQDEAVDKISRAIRRNrigLNGTGRPIGS----FLFVGPTGVGKT-ELAKqLA 494
Cdd:COG1419 128 LLEKLPED-LSAEEAWRALLEALARR---LPVAEDPLLDeggvIALVGPTGVGKTtTIAK-LA 185
|
|
| |
