|
Name |
Accession |
Description |
Interval |
E-value |
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
11-856 |
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: 1087.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 11 LNPYCARAMEGAASLCQTRAHAEILPEHWLLKLLEQGEGDLTVLARRYEWDMDTIWQDMLGFLDSLPRSVRSRPQLSEGV 90
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLARALDKLPRGNTRTPVFSPHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 91 QSLMQDAWLHASL-AEEEHIRSIHLLMALVEKPKLLRcdglwpLLTLAQSQLERL-RGLLDAQSDErpEVQQEAELTQGD 168
Cdd:TIGR03345 81 VELLQEAWLLASLeLGDGRIRSGHLLLALLTDPELRR------LLGSISPELAKIdREALREALPA--LVEGSAEASAAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 169 EVEFVGRPVNAdikgelnPALQNALDRFTLDVTARAREGRIDPVYGRDNEIRQMVDILSRRRKNNPILVGEPGVGKTALV 248
Cdd:TIGR03345 153 ADAAPAGAAAG-------AAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 249 EELALRIHKGNVPDALKPVSVRTLDLGLLQAGAGVKGEFEQRLKNIIDAVQQSPQPVLLFIDEAHTIIGAGNQAGGADAA 328
Cdd:TIGR03345 226 EGLALRIAAGDVPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPIILFIDEAHTLIGAGGQAGQGDAA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 329 NLLKPALARGELRTIAATTWSEYKQYFERDAALERRFQMVKVDEPDDDTACLMLRGLKSRYAEHHGVHITDEAVKAAVTL 408
Cdd:TIGR03345 306 NLLKPALARGELRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVEL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 409 SRRYLTGRQLPDKAVDLLDTASARVRMSLDTVPEPLTRMKAQLTALTMEKQALLEDIAVSnTAHGERLAAIGEEEVAIIL 488
Cdd:TIGR03345 386 SHRYIPGRQLPDKAVSLLDTACARVALSQNATPAALEDLRRRIAALELELDALEREAALG-ADHDERLAELRAELAALEA 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 489 QLDEREAQYGQELKLTEELLACRTDI------------SRQGEIADLQMQLTAVQQNTPLLGLDVDARTVATVIADWTGV 556
Cdd:TIGR03345 465 ELAALEARWQQEKELVEAILALRAELeadadapaddddALRAQLAELEAALASAQGEEPLVFPEVDAQAVAEVVADWTGI 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 557 PLSSLMKDEQTELLSLEHSLAKRVVGQDSALNAIAQRLRASKTGLAPENGPQGVFLLVGPSGTGKTETALALADELFGGE 636
Cdd:TIGR03345 545 PVGRMVRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGE 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 637 KSLITINLSEYQEPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDRGVMRDGEGRE 716
Cdd:TIGR03345 625 QNLITINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGRE 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 717 IDFRNTVILMTSNLGSDLIMQMLEEQPEATEPD-LHELLRPVLRDHFQPALLARFQTVIYRPLAQAAMRTIVEMKLAQVS 795
Cdd:TIGR03345 705 IDFKNTVILLTSNAGSDLIMALCADPETAPDPEaLLEALRPELLKVFKPAFLGRMTVIPYLPLDDDVLAAIVRLKLDRIA 784
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 838691170 796 KRLNRHYGMKTDIHESLYDALTDACLLPDTGARNIDSLLNQQILPVLSQQLLTHMAAKQKP 856
Cdd:TIGR03345 785 RRLKENHGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQILERLAAGEPI 845
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
8-867 |
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: 1086.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 8 LRRLNPYCARAMEGAASLCQTRAHAEILPEHWLLKLLEQGEGDLTVLARRYEWDMDTIWQDMLGFLDSLPR--SVRSRPQ 85
Cdd:COG0542 3 FEKFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGRLPKvsGSSGQPY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 86 LSEGVQSLMQDAWLHASLAEEEHIRSIHLLMALVEKP-----KLLRCDGLwplltlaqsQLERLRGLLDAQSDERPEVQQ 160
Cdd:COG0542 83 LSPRLKRVLELAELEARKLGDEYISTEHLLLALLREGegvaaRILKKLGI---------TLEALREALEELRGGSRVTSQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 161 EAELTQgdevefvgrpvnadikgelnpalqNALDRFTLDVTARAREGRIDPVYGRDNEIRQMVDILSRRRKNNPILVGEP 240
Cdd:COG0542 154 NPESKT------------------------PALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 241 GVGKTALVEELALRIHKGNVPDALKPVSVRTLDLGLLQAGAGVKGEFEQRLKNIIDAVQQSPQPVLLFIDEAHTIIGAGN 320
Cdd:COG0542 210 GVGKTAIVEGLAQRIVNGDVPESLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKSEGNIILFIDELHTLVGAGG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 321 QAGGADAANLLKPALARGELRTIAATTWSEYKQYFERDAALERRFQMVKVDEPDDDTACLMLRGLKSRYAEHHGVHITDE 400
Cdd:COG0542 290 AEGAMDAANLLKPALARGELRCIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 401 AVKAAVTLSRRYLTGRQLPDKAVDLLDTASARVRMSLDTVPEPLTRMKAQLTALTMEKQALLEDiavSNTAHGERLAAIG 480
Cdd:COG0542 370 ALVAAVRLSDRYITDRFLPDKAIDLIDEAAARVRMEIDSKPEELDELERRLEQLEIEKEALKKE---QDEASFERLAELR 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 481 EEEVAIILQLDEREAQYGQELKLTEELLACRTDISRQ-GEIADLQMQLTAVQQ----NTPLLGLDVDARTVATVIADWTG 555
Cdd:COG0542 447 DELAELEEELEALKARWEAEKELIEEIQELKEELEQRyGKIPELEKELAELEEelaeLAPLLREEVTEEDIAEVVSRWTG 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 556 VPLSSLMKDEQTELLSLEHSLAKRVVGQDSALNAIAQRLRASKTGLAPENGPQGVFLLVGPSGTGKTETALALADELFGG 635
Cdd:COG0542 527 IPVGKLLEGEREKLLNLEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGD 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 636 EKSLITINLSEYQEPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDRGVMRDGEGR 715
Cdd:COG0542 607 EDALIRIDMSEYMEKHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGR 686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 716 EIDFRNTVILMTSNLGSDLIMQMLEEQPEATEpdLHELLRPVLRDHFQPALLARF-QTVIYRPLAQAAMRTIVEMKLAQV 794
Cdd:COG0542 687 TVDFRNTIIIMTSNIGSELILDLAEDEPDYEE--MKEAVMEELKKHFRPEFLNRIdEIIVFHPLSKEELRKIVDLQLKRL 764
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 838691170 795 SKRLNRHyGMKTDIHESLYDALTDACLLPDTGARNIDSLLNQQILPVLSQQLLTHMAAKQKphTLTLGWSDEE 867
Cdd:COG0542 765 RKRLAER-GITLELTDAAKDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGD--TITVDVDDGE 834
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
18-847 |
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: 719.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 18 AMEGAASLCQTRAHAEILPEHWLLKLLEQGEGDLTVLARRYEWDMDTIWQDMLGFLDSLPR--SVRSRPQLSEGVQSLMQ 95
Cdd:TIGR03346 8 ALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEKELERLPKvsGPGGQVYLSPDLNRLLN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 96 DAWLHASLAEEEHIRSIHLLMALVEKPkllrcDGLWPLLTLAQSQLERLRGLLDAQSDERPEVQQEAELTQGdevefvgr 175
Cdd:TIGR03346 88 LAEKLAQKRGDEFISSEHLLLALLDDK-----GTLGKLLKEAGATADALEAAINAVRGGQKVTDANAEDQYE-------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 176 pvnadikgelnpalqnALDRFTLDVTARAREGRIDPVYGRDNEIRQMVDILSRRRKNNPILVGEPGVGKTALVEELALRI 255
Cdd:TIGR03346 155 ----------------ALEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 256 HKGNVPDALKPVSVRTLDLGLLQAGAGVKGEFEQRLKNIIDAVQQSPQPVLLFIDEAHTIIGAGNQAGGADAANLLKPAL 335
Cdd:TIGR03346 219 VNGDVPEGLKNKRLLALDMGALIAGAKYRGEFEERLKAVLNEVTKSEGQIILFIDELHTLVGAGKAEGAMDAGNMLKPAL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 336 ARGELRTIAATTWSEYKQYFERDAALERRFQMVKVDEPDDDTACLMLRGLKSRYAEHHGVHITDEAVKAAVTLSRRYLTG 415
Cdd:TIGR03346 299 ARGELHCIGATTLDEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 416 RQLPDKAVDLLDTASARVRMSLDTVPEPLTRMKAQLTALTMEKQALLEDiavSNTAHGERLAAIGEEEVAIILQLDEREA 495
Cdd:TIGR03346 379 RFLPDKAIDLIDEAAARIRMEIDSKPEELDELDRRIIQLEIEREALKKE---KDEASKKRLEDLEKELADLEEEYAELEE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 496 QYGQE-------LKLTEELLACRTDI---SRQ-----------GEIADLQMQLTAVQQ-----NTPLLGLDVDARTVATV 549
Cdd:TIGR03346 456 QWKAEkasiqgiQQIKEEIEQVRLELeqaEREgdlakaaelqyGKLPELEKQLQAAEQklgeeQNRLLREEVTAEEIAEV 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 550 IADWTGVPLSSLMKDEQTELLSLEHSLAKRVVGQDSALNAIAQRLRASKTGLAPENGPQGVFLLVGPSGTGKTETALALA 629
Cdd:TIGR03346 536 VSRWTGIPVSKMLEGEREKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALA 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 630 DELFGGEKSLITINLSEYQEPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDRGVM 709
Cdd:TIGR03346 616 EFLFDSEDAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRL 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 710 RDGEGREIDFRNTVILMTSNLGSDLIMQMLE-EQPEATEPDLHEllrpVLRDHFQPALLARF-QTVIYRPLAQAAMRTIV 787
Cdd:TIGR03346 696 TDGQGRTVDFRNTVIIMTSNLGSDFIQELAGgDDYEEMREAVME----VLRAHFRPEFLNRIdEIVVFHPLGREQIARIV 771
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 788 EMKLAQVSKRLnRHYGMKTDIHESLYDALTDACLLPDTGARNIDSLLNQQILPVLSQQLL 847
Cdd:TIGR03346 772 EIQLGRLRKRL-AERKITLELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKIL 830
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
190-861 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 595.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 190 QNALDRFTLDVTARAREGRIDPVYGRDNEIRQMVDILSRRRKNNPILVGEPGVGKTALVEELALRIHKGNVPDALKPVSV 269
Cdd:PRK10865 158 RQALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 270 RTLDLGLLQAGAGVKGEFEQRLKNIIDAVQQSPQPVLLFIDEAHTIIGAGNQAGGADAANLLKPALARGELRTIAATTWS 349
Cdd:PRK10865 238 LALDMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLD 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 350 EYKQYFERDAALERRFQMVKVDEPDDDTACLMLRGLKSRYAEHHGVHITDEAVKAAVTLSRRYLTGRQLPDKAVDLLDTA 429
Cdd:PRK10865 318 EYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEA 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 430 SARVRMSLDTVPEPLTRMKAQLTALTMEKQALLEDiavSNTAHGERLAAIGEEevaiilqLDEREAQYGQelkLTEELLA 509
Cdd:PRK10865 398 ASSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKE---SDEASKKRLDMLNEE-------LSDKERQYSE---LEEEWKA 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 510 CRTDIS--------------------RQGEIA-----------DLQMQLTAVQQ----NTPLLGLDVDARTVATVIADWT 554
Cdd:PRK10865 465 EKASLSgtqtikaeleqakiaieqarRVGDLArmselqygkipELEKQLAAATQlegkTMRLLRNKVTDAEIAEVLARWT 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 555 GVPLSSLMKDEQTELLSLEHSLAKRVVGQDSALNAIAQRLRASKTGLAPENGPQGVFLLVGPSGTGKTETALALADELFG 634
Cdd:PRK10865 545 GIPVSRMLESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFD 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 635 GEKSLITINLSEYQEPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDRGVMRDGEG 714
Cdd:PRK10865 625 SDDAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQG 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 715 REIDFRNTVILMTSNLGSDLIMqmlEEQPEATEPDLHELLRPVLRDHFQPALLARF-QTVIYRPLAQAAMRTIVEMKLAQ 793
Cdd:PRK10865 705 RTVDFRNTVVIMTSNLGSDLIQ---ERFGELDYAHMKELVLGVVSHNFRPEFINRIdEVVVFHPLGEQHIASIAQIQLQR 781
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 838691170 794 VSKRLNRHyGMKTDIHESLYDALTDACLLPDTGARNIDSLLNQQILPVLSQQLLTHMAAKQKPHTLTL 861
Cdd:PRK10865 782 LYKRLEER-GYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEV 848
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
193-847 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 578.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 193 LDRFTLDVTARAREGRIDPVYGRDNEIRQMVDILSRRRKNNPILVGEPGVGKTALVEELALRIHKGNVPDALKPVSVRTL 272
Cdd:CHL00095 162 LEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDKLVITL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 273 DLGLLQAGAGVKGEFEQRLKNIIDAVQQSpQPVLLFIDEAHTIIGAGNQAGGADAANLLKPALARGELRTIAATTWSEYK 352
Cdd:CHL00095 242 DIGLLLAGTKYRGEFEERLKRIFDEIQEN-NNIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLDEYR 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 353 QYFERDAALERRFQMVKVDEPDDDTACLMLRGLKSRYAEHHGVHITDEAVKAAVTLSRRYLTGRQLPDKAVDLLDTASAR 432
Cdd:CHL00095 321 KHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLDEAGSR 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 433 VRMSLDTVPEPLTRMKAQLTALTMEKQallediavsntahgerlAAIGEEEVAIILQLDEREaqygqelklteelLACRT 512
Cdd:CHL00095 401 VRLINSRLPPAARELDKELREILKDKD-----------------EAIREQDFETAKQLRDRE-------------MEVRA 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 513 DISrqgeiADLQMQLTAVQQNTPLlgLDVDARTVATVIADWTGVPLSSLMKDEQTELLSLEHSLAKRVVGQDSALNAIAQ 592
Cdd:CHL00095 451 QIA-----AIIQSKKTEEEKRLEV--PVVTEEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSK 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 593 RLRASKTGLAPENGPQGVFLLVGPSGTGKTETALALADELFGGEKSLITINLSEYQEPHTVSQLKGSPPGYVGYGQGGIL 672
Cdd:CHL00095 524 AIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALASYFFGSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 673 TEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDRGVMRDGEGREIDFRNTVILMTSNLGSDLI------MQMLEEQPEAT 746
Cdd:CHL00095 604 TEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSKVIetnsggLGFELSENQLS 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 747 EPD---LHELLRPVLRDHFQPALLARFQTVI-YRPLAQAAMRTIVEMKLAQVSKRLNRHyGMKTDIHESLYDALTDACLL 822
Cdd:CHL00095 684 EKQykrLSNLVNEELKQFFRPEFLNRLDEIIvFRQLTKNDVWEIAEIMLKNLFKRLNEQ-GIQLEVTERIKTLLIEEGYN 762
|
650 660
....*....|....*....|....*
gi 838691170 823 PDTGARNIDSLLNQQILPVLSQQLL 847
Cdd:CHL00095 763 PLYGARPLRRAIMRLLEDPLAEEVL 787
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
11-847 |
1.13e-128 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 404.22 E-value: 1.13e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 11 LNPYCARAMEGAASLCQTRAHAEILPEHWLLKLLEQGEGDLTVLARRYewDMDTIWQDMLGFLDS----LPRSVRSR--- 83
Cdd:PRK11034 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSV--DLVALRQELEAFIEQttpvLPASEEERdtq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 84 PQLSegVQSLMQDAWLHASLAEEEHIRSIHLLMALVEKPK-----LLRCDGLwplltlaqSQLERLRGLLDAQSDERPEv 158
Cdd:PRK11034 80 PTLS--FQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQEsqaayLLRKHEV--------SRLDVVNFISHGTRKDEPS- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 159 qqeaELTQGDEVEFVGRPVNADIKgelnpalqnaLDRFTLDVTARAREGRIDPVYGRDNEIRQMVDILSRRRKNNPILVG 238
Cdd:PRK11034 149 ----QSSDPGSQPNSEEQAGGEER----------MENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 239 EPGVGKTALVEELALRIHKGNVPDALKPVSVRTLDLGLLQAGAGVKGEFEQRLKNIIDAVQQSPQPVLlFIDEAHTIIGA 318
Cdd:PRK11034 215 ESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSIL-FIDEIHTIIGA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 319 GNQAGG-ADAANLLKPALARGELRTIAATTWSEYKQYFERDAALERRFQMVKVDEPDDDTACLMLRGLKSRYAEHHGVHI 397
Cdd:PRK11034 294 GAASGGqVDAANLIKPLLSSGKIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRY 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 398 TDEAVKAAVTLSRRYLTGRQLPDKAVDLLDTASARVRMSldtvpePLTRMKAQLTaltmekqallediavsntahgerla 477
Cdd:PRK11034 374 TAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGARARLM------PVSKRKKTVN------------------------- 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 478 aigeeevaiilqldereaqygqelklteellacrtdisrqgeIADLQmqltavqqntpllgldvdartvaTVIADWTGVP 557
Cdd:PRK11034 423 ------------------------------------------VADIE-----------------------SVVARIARIP 437
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 558 LSSLMKDEQTELLSLEHSLAKRVVGQDSALNAIAQRLRASKTGLAPENGPQGVFLLVGPSGTGKTETALALADELfggEK 637
Cdd:PRK11034 438 EKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL---GI 514
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 638 SLITINLSEYQEPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDRGVMRDGEGREI 717
Cdd:PRK11034 515 ELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKA 594
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 718 DFRNTVILMTSNLG-SDLIMQMLEEQPEATEPDLHELLRPVlrdhFQPALLARFQTVI-YRPLAQAAMRTIVEMKLAQVS 795
Cdd:PRK11034 595 DFRNVVLVMTTNAGvRETERKSIGLIHQDNSTDAMEEIKKI----FTPEFRNRLDNIIwFDHLSTDVIHQVVDKFIVELQ 670
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 838691170 796 KRLNRHyGMKTDIHESLYDALTDACLLPDTGARNIDSLLNQQILPVLSQQLL 847
Cdd:PRK11034 671 AQLDQK-GVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELL 721
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
569-775 |
1.28e-87 |
|
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: 275.98 E-value: 1.28e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 569 LLSLEHSLAKRVVGQDSALNAIAQRLRASKTGLAPENGPQGVFLLVGPSGTGKTETALALADELFGGEKSLITINLSEYQ 648
Cdd:cd19499 2 LLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 649 EPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDRGVMRDGEGREIDFRNTVILMTS 728
Cdd:cd19499 82 EKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTS 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 838691170 729 NlgsdlimqmleeqpeatepdlhellrpvlrdHFQPALLARFQTVIY 775
Cdd:cd19499 162 N-------------------------------HFRPEFLNRIDEIVV 177
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
607-770 |
1.36e-72 |
|
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: 235.55 E-value: 1.36e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 607 PQGVFLLVGPSGTGKTETALALADELFGGEKSLITINLSEYQEPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLL 686
Cdd:pfam07724 2 PIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 687 DEVEKAHRDVMNLFYQVFDRGVMRDGEGREIDFRNTVILMTSNLGSDLIMQMLEEQPEATEPDLHELLRPVLRDHFQPAL 766
Cdd:pfam07724 82 DEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRLGDSPDYELLKEEVMDLLKKGFIPEF 161
|
....
gi 838691170 767 LARF 770
Cdd:pfam07724 162 LGRL 165
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
374-479 |
2.31e-41 |
|
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: 146.48 E-value: 2.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 374 DDDTACLMLRGLKSRYAEHHGVHITDEAVKAAVTLSRRYLTGRQLPDKAVDLLDTASARVRMSLDTVPEPLTRMKAQLTA 453
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|....*.
gi 838691170 454 LTMEKQALLEDiavSNTAHGERLAAI 479
Cdd:pfam17871 81 LEIEKEALERE---QDFEKAERLAKL 103
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
581-738 |
9.53e-17 |
|
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: 77.96 E-value: 9.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 581 VGQDSALNAIAQRLrasktglapENGPQGVFLLVGPSGTGKTETALALADELFGGEKSLITINLSEYQEPHTVSqlkgsp 660
Cdd:cd00009 1 VGQEEAIEALREAL---------ELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVA------ 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 838691170 661 pGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDrgvmrDGEGREIDFRNTVILMTSNLGSDLIMQM 738
Cdd:cd00009 66 -ELFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLE-----TLNDLRIDRENVRVIGATNRPLLGDLDR 137
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
213-373 |
4.78e-16 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 76.03 E-value: 4.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 213 YGRDNEIRQMVDILSRRRKNNPILVGEPGVGKTALVEELALRIHKGNVPdalkpvsVRTLDLGLLQAGAGVKGEFEQRLK 292
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 293 NIIDAVQQSPQPVLLFIDEAHTiIGAGNQAGGADAANLLKPALA-RGELRTIAATTwseYKQYFERDAALERRFQMVKVD 371
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDS-LSRGAQNALLRVLETLNDLRIdRENVRVIGATN---RPLLGDLDRALYDRLDIRIVI 149
|
..
gi 838691170 372 EP 373
Cdd:cd00009 150 PL 151
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
607-735 |
6.45e-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: 6.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 607 PQGVFLLVGPSGTGKTETALALADELFGGEKSLITINLSEYQEPHTVSQLKGSPPGYVGYGQGG----ILTEAVRKRPYS 682
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGElrlrLALALARKLKPD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 838691170 683 VVLLDEVEKAHRDVMNLFYQVFDRGVMRDGEGREidfRNTVILMTSNLGSDLI 735
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSE---KNLTVILTTNDEKDLG 130
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
611-729 |
1.33e-10 |
|
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: 60.00 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 611 FLLVGPSGTGKTETALALADELFGgeKSLITINLSEYQEPhtvSQLKGS--PPGYVGYGQGGILTEAVRKRpySVVLLDE 688
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSN--RPVFYVQLTRDTTE---EDLFGRrnIDPGGASWVDGPLVRAAREG--EIAVLDE 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 838691170 689 VEKAHRDVMNLFYQVFDRGVMRDGEGREID---FRNTVILMTSN 729
Cdd:pfam07728 75 INRANPDVLNSLLSLLDERRLLLPDGGELVkaaPDGFRLIATMN 118
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
778-853 |
2.54e-10 |
|
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: 57.42 E-value: 2.54e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 838691170 778 LAQAAMRTIVEMKLAQVSKRLNRHyGMKTDIHESLYDALTDACLLPDTGARNIDSLLNQQILPVLSQQLLTHMAAK 853
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAER-GITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKE 75
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
584-695 |
2.81e-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: 59.60 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 584 DSALNAIAQRLRASKTGLAPENGPQGVfLLVGPSGTGKTETALALADELfggEKSLITINLSEYQEPhtvsqlkgsppgY 663
Cdd:cd19481 3 ASLREAVEAPRRGSRLRRYGLGLPKGI-LLYGPPGTGKTLLAKALAGEL---GLPLIVVKLSSLLSK------------Y 66
|
90 100 110
....*....|....*....|....*....|....
gi 838691170 664 VGYGQGGI--LTEAVRKRPYSVVLLDEVEKAHRD 695
Cdd:cd19481 67 VGESEKNLrkIFERARRLAPCILFIDEIDAIGRK 100
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
612-778 |
3.48e-09 |
|
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: 55.68 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 612 LLVGPSGTGKTETALALADELFGgekSLITINLSEyqephTVSQLKGSPPGYVgygqGGILTEAVRKRPySVVLLDEVEK 691
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGA---PFIEISGSE-----LVSKYVGESEKRL----RELFEAAKKLAP-CVIFIDEIDA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 692 -----------AHRDVMNLFYQVFDrgvmrdgeGREIDFRNTVILMTSNlgsdlimqmleeqpeatepdlhellRPvlrD 760
Cdd:pfam00004 69 lagsrgsggdsESRRVVNQLLTELD--------GFTSSNSKVIVIAATN-------------------------RP---D 112
|
170
....*....|....*...
gi 838691170 761 HFQPALLARFQTVIYRPL 778
Cdd:pfam00004 113 KLDPALLGRFDRIIEFPL 130
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
778-862 |
3.51e-09 |
|
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: 54.37 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 778 LAQAAMRTIVEMKLAQVSKRLNRHyGMKTDIHESLYDALTDACLLPDTGARNIDSLLNQQILPVLSQQLLTHMAAKQKPH 857
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEK-GITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTV 79
|
....*
gi 838691170 858 TLTLG 862
Cdd:smart01086 80 VVDVD 84
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
235-368 |
3.80e-09 |
|
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: 55.68 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 235 ILVGEPGVGKTALVEELAlrihkgnvpDALKpVSVRTLDLGLLqaGAGVKGEFEQRLKNIIDAVqQSPQPVLLFIDEAHT 314
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVA---------KELG-APFIEISGSEL--VSKYVGESEKRLRELFEAA-KKLAPCVIFIDEIDA 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 838691170 315 IIGAGNQAG---GADAANLLKPALARGELRT-----IAATTwseykQYFERDAALERRFQMV 368
Cdd:pfam00004 69 LAGSRGSGGdseSRRVVNQLLTELDGFTSSNskvivIAATN-----RPDKLDPALLGRFDRI 125
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
230-365 |
1.99e-08 |
|
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: 54.30 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 230 RKNNPILVGEPGVGKTALVEELALRIHKGNVP-----DALKPVSVRTLDLGLLQAGAGVKGEFEQRLKNIIDAVQQsPQP 304
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGviyidGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARK-LKP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 838691170 305 VLLFIDEAHTIIGAGNQAGGADAA--NLLKPALARGELRTIAATTWSEykqyFERDAALERRF 365
Cdd:smart00382 80 DVLILDEITSLLDAEQEALLLLLEelRLLLLLKSEKNLTVILTTNDEK----DLGPALLRRRF 138
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
580-778 |
4.74e-08 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 54.89 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 580 VVGQDSALNAIAQ-------RLRASKTGLAPengPQGVfLLVGPSGTGKTETALALADELfggEKSLITINLSEyqepht 652
Cdd:COG1223 4 VVGQEEAKKKLKLiikelrrRENLRKFGLWP---PRKI-LFYGPPGTGKTMLAEALAGEL---KLPLLTVRLDS------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 653 vsqLKGSppgYVGYGQGGI--LTEAVRKRPySVVLLDEVE--KAHRDVMNLfyqvfdrgvmrDGEGREIdfRNTVILMTS 728
Cdd:COG1223 71 ---LIGS---YLGETARNLrkLFDFARRAP-CVIFFDEFDaiAKDRGDQND-----------VGEVKRV--VNALLQELD 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 838691170 729 NLGSDLIMQMLEEQPeatepdlhELLrpvlrDhfqPALLARFQTVIYRPL 778
Cdd:COG1223 131 GLPSGSVVIAATNHP--------ELL-----D---SALWRRFDEVIEFPL 164
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
211-313 |
2.98e-07 |
|
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: 50.97 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 211 PVYGRDNEIRQMVDILSRRRKNNP---ILVGEPGVGKTALVEELALRIHKGNV----------------PDALKPVSV-- 269
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERDGGyflrgkcdenlpysplLEALTREGLlr 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 838691170 270 --------------RTLDLGLLQAGAGVKGEFEQR----LKNIIDAVQQSPQPVLLFIDEAH 313
Cdd:pfam13191 81 qlldelesslleawRAALLEALAPVPELPGDLAERlldlLLRLLDLLARGERPLVLVLDDLQ 142
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
90-376 |
9.81e-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: 52.22 E-value: 9.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 90 VQSLMQDAWLHASLAEEEHIRSIHLLMALVEKPKLLRCDGLWPLLTLAQSQLERLRGLLDAQSDERPEVQQEAELTQGDE 169
Cdd:COG0464 37 LLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLER 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 170 VEFVGRPVNADIKGELNPALQNALDRFTLDVTARAREGRIDPVYGRDN---EIRQMVDILSRRRK-------NNP---IL 236
Cdd:COG0464 117 ALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEvkeELRELVALPLKRPElreeyglPPPrglLL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 237 VGEPGVGKTALVEELAlriHKGNVPdalkpvsVRTLDLGLLqAGAGVkGEFEQRLKNIIDAVQQSpQPVLLFIDEAHTII 316
Cdd:COG0464 197 YGPPGTGKTLLARALA---GELGLP-------LIEVDLSDL-VSKYV-GETEKNLREVFDKARGL-APCVLFIDEADALA 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 838691170 317 GAGNQAGGADA----ANLLKpALA--RGELRTIAATTwseykqYFER-DAALERRFQ-MVKVDEPDDD 376
Cdd:COG0464 264 GKRGEVGDGVGrrvvNTLLT-EMEelRSDVVVIAATN------RPDLlDPALLRRFDeIIFFPLPDAE 324
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
228-313 |
1.26e-06 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 48.49 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 228 RRRKNNPILVGEPGVGKTALVEELALRIHKGNVP----DALKPVSVRTLDLGLLQAgAGVKGEFEQRLKNIIDAVQQ--- 300
Cdd:pfam13401 2 RFGAGILVLTGESGTGKTTLLRRLLEQLPEVRDSvvfvDLPSGTSPKDLLRALLRA-LGLPLSGRLSKEELLAALQQlll 80
|
90
....*....|....
gi 838691170 301 -SPQPVLLFIDEAH 313
Cdd:pfam13401 81 aLAVAVVLIIDEAQ 94
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
605-705 |
3.84e-05 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 44.25 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 605 NGPQGVFLLVGPSGTGKTETALALADELFGGEKSLITINLSEYQEPHTVSQ--LKGSPPGYVGYGQGGILTEAV-----R 677
Cdd:pfam13401 2 RFGAGILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRalLRALGLPLSGRLSKEELLAALqqlllA 81
|
90 100
....*....|....*....|....*...
gi 838691170 678 KRPYSVVLLDEVEKAHRDVMNLFYQVFD 705
Cdd:pfam13401 82 LAVAVVLIIDEAQHLSLEALEELRDLLN 109
|
|
| CDC6 |
COG1474 |
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]; |
559-702 |
1.74e-04 |
|
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
Pssm-ID: 441083 [Multi-domain] Cd Length: 389 Bit Score: 44.84 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 559 SSLMKDEqtELLSLEHsLAKRVVGQDSALNAIAQRLRASKTGLAPENGpqgvfLLVGPSGTGKTETALALADEL------ 632
Cdd:COG1474 10 ESIFRDR--EVLSPDY-VPDRLPHREEEIEELASALRPALRGERPSNV-----LIYGPTGTGKTAVAKYVLEELeeeaee 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 633 FGGEKSLITINLSEYQEPHTV-----SQLK-GSPPGYVGYGQG---GILTEAVRKRPYSVVL-LDEVEKAHRDVMN-LFY 701
Cdd:COG1474 82 RGVDVRVVYVNCRQASTRYRVlsrilEELGsGEDIPSTGLSTDelfDRLYEALDERDGVLVVvLDEIDYLVDDEGDdLLY 161
|
.
gi 838691170 702 Q 702
Cdd:COG1474 162 Q 162
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
431-784 |
2.88e-04 |
|
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: 44.13 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 431 ARVRMSLDTVPEPLTRMKAQLTALTMEKQALLEDIAVSNTAHGERLAAIGEEEVAIILQLDEREAQYGQELKLTEELLAC 510
Cdd:COG0464 1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 511 RTDISRQGEIADLQMQLTAVQQNTPLLGLDVDARTVATVIADWTGVPLSSLMKDEQTELLSLEHSLAKR---------VV 581
Cdd:COG0464 81 LLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLelreailddLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 582 GQDSALNAIAQRLRA--------SKTGLAPENGpqgvFLLVGPSGTGKTETALALADELfggEKSLITINLSEyqephTV 653
Cdd:COG0464 161 GLEEVKEELRELVALplkrpelrEEYGLPPPRG----LLLYGPPGTGKTLLARALAGEL---GLPLIEVDLSD-----LV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 654 SQlkgsppgYVGYGQGGI---LTEAVRKRPySVVLLDEVEKAHRdvmnlfyqvfDRGVMRDGEGREI---------DFRN 721
Cdd:COG0464 229 SK-------YVGETEKNLrevFDKARGLAP-CVLFIDEADALAG----------KRGEVGDGVGRRVvntlltemeELRS 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 838691170 722 TVILM-TSNLGSDLimqmleeqpeatepDlhellrpvlrdhfqPALLARFQTVIYRPLAQAAMR 784
Cdd:COG0464 291 DVVVIaATNRPDLL--------------D--------------PALLRRFDEIIFFPLPDAEER 326
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
471-632 |
2.93e-04 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 44.30 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 471 AHGERLAAIGEEEVAIILQLDEREAQYGQELKLTEELLACRTDISRQGEIADLQMQLTAVQQNTPLLGLDVDARTVATVI 550
Cdd:COG1203 11 GALALAALLLLLLALLLAALLLLLLAALLLALLLALLLLAALELALLLLLLLLLLLLLLLLLLDLLLDDLAFLFLLLLID 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 551 ADWTGVPLSSLMKDeqtellSLEHSLAKRV---VGQDSALNAIAQRLR--ASKTGLAPENGPQGVFLLVGPSGTGKTETA 625
Cdd:COG1203 91 ADWLDSANFDMARQ------ALDHLLAERLerlLPKKSKPRTPINPLQneALELALEAAEEEPGLFILTAPTGGGKTEAA 164
|
....*..
gi 838691170 626 LALADEL 632
Cdd:COG1203 165 LLFALRL 171
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
600-690 |
3.73e-04 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 43.46 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 600 GLAPengPQGVfLLVGPSGTGKTETALALADELfggEKSLITINLSEYQEPhtvsqlkgsppgYVgyGQGG-----ILTE 674
Cdd:COG1222 108 GIEP---PKGV-LLYGPPGTGKTLLAKAVAGEL---GAPFIRVRGSELVSK------------YI--GEGArnvreVFEL 166
|
90
....*....|....*.
gi 838691170 675 AVRKRPySVVLLDEVE 690
Cdd:COG1222 167 AREKAP-SIIFIDEID 181
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
580-689 |
5.44e-04 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 43.37 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 580 VVGQDSALNAIAQRLRASKTGlapenGPQGVFLLVGPSGTGKTETALALADElFGGEksLITINLSEYQephTVSQLKgs 659
Cdd:PRK04195 16 VVGNEKAKEQLREWIESWLKG-----KPKKALLLYGPPGVGKTSLAHALAND-YGWE--VIELNASDQR---TADVIE-- 82
|
90 100 110
....*....|....*....|....*....|.
gi 838691170 660 ppGYVGYG-QGGILTEAVRKrpysVVLLDEV 689
Cdd:PRK04195 83 --RVAGEAaTSGSLFGARRK----LILLDEV 107
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
235-315 |
5.50e-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: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 235 ILVGEPGVGKTALVEELALRIHkgnvpdalkpVSVRTLDLGLLQAGAgvKGEFEQRLKNIIDAVQQSpQPVLLFIDEAHT 314
Cdd:cd19481 30 LLYGPPGTGKTLLAKALAGELG----------LPLIVVKLSSLLSKY--VGESEKNLRKIFERARRL-APCILFIDEIDA 96
|
.
gi 838691170 315 I 315
Cdd:cd19481 97 I 97
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
583-699 |
7.08e-04 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 42.97 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 583 QDSALNAIAQRLRASKTgLAPENGPQgVFLLVGPSGTGKTETALALAD--ELFGGEKSL----ITIN---LSEYQEPHTV 653
Cdd:PRK12723 151 RDSVIIYIAKTIKCSGS-IIDNLKKR-VFILVGPTGVGKTTTIAKLAAiyGINSDDKSLnikiITIDnyrIGAKKQIQTY 228
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 838691170 654 SQLKGSPPGYVGYGQgGILTEAVRKRPYSVVLLDEVEKAHRDVMNL 699
Cdd:PRK12723 229 GDIMGIPVKAIESFK-DLKEEITQSKDFDLVLVDTIGKSPKDFMKL 273
|
|
| PulE-GspE-like |
cd01129 |
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ... |
605-642 |
9.15e-04 |
|
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II secretory pathway, the main terminal branch of the general secretory pathway (GSP). PulE is a cytoplasmic protein of the GSP, which contains an ATP binding site and a tetracysteine motif. This subgroup also includes PilB, a type IV pilus assembly ATPase, DotB, an ATPase of the type IVb secretion system, also known as the dot/icm system, Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ, and HofB.
Pssm-ID: 410873 [Multi-domain] Cd Length: 159 Bit Score: 40.55 E-value: 9.15e-04
10 20 30
....*....|....*....|....*....|....*...
gi 838691170 605 NGPQGVFLLVGPSGTGKTETALALADELFGGEKSLITI 642
Cdd:cd01129 8 KRPHGLILVTGPTGSGKTTTLYAMLRELNGPERNIITI 45
|
|
| TIP49 |
COG1224 |
DNA helicase TIP49, TBP-interacting protein [Transcription]; |
573-678 |
1.06e-03 |
|
DNA helicase TIP49, TBP-interacting protein [Transcription];
Pssm-ID: 440837 [Multi-domain] Cd Length: 452 Bit Score: 42.65 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 573 EHSLAKRV----VGQDSALNA---IAQRLRASKTGlapengPQGVfLLVGPSGTGKTETALALADELfGGEKSLITINLS 645
Cdd:COG1224 29 ENGKAKFVadglVGQVEAREAagiVVKMIKEGKMA------GKGI-LIVGPPGTGKTALAVAIAREL-GEDTPFVAISGS 100
|
90 100 110
....*....|....*....|....*....|....
gi 838691170 646 E-YQephtvSQLKgsppgyvgygQGGILTEAVRK 678
Cdd:COG1224 101 EiYS-----AELK----------KTEFLMQALRK 119
|
|
| rfc |
PRK00440 |
replication factor C small subunit; Reviewed |
580-634 |
1.30e-03 |
|
replication factor C small subunit; Reviewed
Pssm-ID: 234763 [Multi-domain] Cd Length: 319 Bit Score: 41.78 E-value: 1.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 838691170 580 VVGQDSalnaIAQRLRA-SKTGLAPEngpqgvFLLVGPSGTGKTETALALADELFG 634
Cdd:PRK00440 19 IVGQEE----IVERLKSyVKEKNMPH------LLFAGPPGTGKTTAALALARELYG 64
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
576-711 |
2.46e-03 |
|
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410906 [Multi-domain] Cd Length: 183 Bit Score: 40.06 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 576 LAKRVVGQDSALNAIA----QRLRASK--TGLAPENGPQGVfLLVGPSGTGKTETALALAdELFGGekSLITINLSEYQE 649
Cdd:cd19498 9 LDKYIIGQDEAKRAVAialrNRWRRMQlpEELRDEVTPKNI-LMIGPTGVGKTEIARRLA-KLAGA--PFIKVEATKFTE 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 838691170 650 phtvsqlkgspPGYVGYGQGGILTEAVRkrpySVVLLDEVEKAHRDVMNLFYQVFDRGVMRD 711
Cdd:cd19498 85 -----------VGYVGRDVESIIRDLVE----GIVFIDEIDKIAKRGGSSGPDVSREGVQRD 131
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
236-313 |
3.87e-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: 40.16 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 236 LVGEPGVGKT----ALVEELALRIHKGNVPDA-LKPVS-VRTL--DLGLLQAGAGvKGEFEQRLKNIIDAVQQSPQPVLL 307
Cdd:COG3267 48 LTGEVGTGKTtllrRLLERLPDDVKVAYIPNPqLSPAElLRAIadELGLEPKGAS-KADLLRQLQEFLLELAAAGRRVVL 126
|
....*.
gi 838691170 308 FIDEAH 313
Cdd:COG3267 127 IIDEAQ 132
|
|
| PRK12402 |
PRK12402 |
replication factor C small subunit 2; Reviewed |
575-645 |
6.45e-03 |
|
replication factor C small subunit 2; Reviewed
Pssm-ID: 237090 [Multi-domain] Cd Length: 337 Bit Score: 39.59 E-value: 6.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 838691170 575 SLAKRVVGQDSAlnaIAQRLRASKTGLAPEngpqgvFLLVGPSGTGKTETALALADELFG--GEKSLITINLS 645
Cdd:PRK12402 12 ALLEDILGQDEV---VERLSRAVDSPNLPH------LLVQGPPGSGKTAAVRALARELYGdpWENNFTEFNVA 75
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
612-718 |
7.08e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 38.50 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 612 LLVGPSGTGKTETALALADELFGGEkSLITINLSEYQE--PHTVSQLKGSPPGYVGYGQ--GGILTE----AVRKRPYSV 683
Cdd:pfam06414 15 LLGGQPGAGKTELARALLDELGRQG-NVVRIDPDDFRElhPHYRELQAADPKTASEYTQpdASRWVEkllqHAIENGYNI 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 838691170 684 VL------LDEVEKAHRDVMNLFYQV----------------FDRGVMRDGEGREID 718
Cdd:pfam06414 94 ILegtlrsPDVAKKIARALKAAGYRVevaavaappelswlgvLDRYEEEVAEGRYVP 150
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
596-632 |
7.30e-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: 38.04 E-value: 7.30e-03
10 20 30
....*....|....*....|....*....|....*..
gi 838691170 596 ASKTGLAPengPQGVfLLVGPSGTGKTETALALADEL 632
Cdd:cd19503 26 FRALGLKP---PRGV-LLHGPPGTGKTLLARAVANEA 58
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
212-341 |
7.43e-03 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 38.31 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 212 VYGRDNEIRQMVDILSR-----RRKNNPI----LVGEPGVGKTALVEELALRIHKGNvpDALKpvsvrTLDLGLLQ---A 279
Cdd:cd19499 13 VVGQDEAVKAVSDAIRRaraglSDPNRPIgsflFLGPTGVGKTELAKALAELLFGDE--DNLI-----RIDMSEYMekhS 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838691170 280 GAGVKGE------FEQRLKnIIDAVQQSPQPVLLF--IDEAHTiigagnqaggaDAANLLKPALARGELR 341
Cdd:cd19499 86 VSRLIGAppgyvgYTEGGQ-LTEAVRRKPYSVVLLdeIEKAHP-----------DVQNLLLQVLDDGRLT 143
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
187-255 |
7.84e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 40.23 E-value: 7.84e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 838691170 187 PALQNALDRFTLDVTARAREGRIDPVYGRDNEIRQMVDILSRRRKNNPILV---GEPGVGKTALVEELALRI 255
Cdd:COG3899 264 LLLLGLLAAAAAGRRLLARRLIPQPLVGREAELAALLAALERARAGRGELVlvsGEAGIGKSRLVRELARRA 335
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
583-640 |
7.95e-03 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 39.62 E-value: 7.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 838691170 583 QDSALNAIAQRLRASKtglapengpqGVFLLVGPSGTGKTETALALADELFGGEKSLI 640
Cdd:COG1061 85 QQEALEALLAALERGG----------GRGLVVAPTGTGKTVLALALAAELLRGKRVLV 132
|
|
| |
