|
Name |
Accession |
Description |
Interval |
E-value |
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
11-860 |
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: 1090.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 11 LNPCCARAMEGAASLCQTRAHAEILPEHWLLKLLEQGEGDLTVLARRYEWDMDALWQDLLNWLDKQPRSVRHRPQLSDHT 90
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLARALDKLPRGNTRTPVFSPHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 91 LRLMQEAWLIASL-SGEAQIRSVHLLMALVEKQNLiqcdglwplltlgQRQLERLRPLLDAQsderPPAQQEAALAQPHG 169
Cdd:TIGR03345 81 VELLQEAWLLASLeLGDGRIRSGHLLLALLTDPEL-------------RRLLGSISPELAKI----DREALREALPALVE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 170 GDVEFVGRPAGSELNADGLNPALQNALDKFTLDVTAKARDGQIDPVFGRDTEIRQMVDILSRRRKNNPILVGEPGVGKTA 249
Cdd:TIGR03345 144 GSAEASAAAADAAPAGAAAGAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 250 LVEGLALRIAEGNVPDALKPVSVRTLDLGLLQAGAGVKGEFEQRLKNIIEAVQQSPSPVLLFIDEAHTIIGAGNQAGGAD 329
Cdd:TIGR03345 224 VVEGLALRIAAGDVPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPIILFIDEAHTLIGAGGQAGQGD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 330 AANLLKPALARGELRTIAATTWSEYKQYFERDAALERRFQMVKVDEPDDDTACLMLRGLKSRYADHHGVHITDDAVRAAV 409
Cdd:TIGR03345 304 AANLLKPALARGELRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 410 TLSRRYLTGRQLPDKAVDLLDTASARLRMSLDTVPEPLTRMKAQLTVLAMEKQALLEDIALGnSARGDRLAAIEQEENRL 489
Cdd:TIGR03345 384 ELSHRYIPGRQLPDKAVSLLDTACARVALSQNATPAALEDLRRRIAALELELDALEREAALG-ADHDERLAELRAELAAL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 490 ILALDTLETQYGQELQLTEALLACRRDI------------SRQAEISDLQTALIAVQQGNPLLGLDVDVRTVATVIADWT 557
Cdd:TIGR03345 463 EAELAALEARWQQEKELVEAILALRAELeadadapaddddALRAQLAELEAALASAQGEEPLVFPEVDAQAVAEVVADWT 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 558 GVPLSSLMKDEQTELLSLEESLGKRVVGQEAALSAIARRLRAAKTGLTPENGPQGVFLLVGPSGTGKTETALALADALFG 637
Cdd:TIGR03345 543 GIPVGRMVRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYG 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 638 GEKALITINLSEYQEPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDRGVMRDGEG 717
Cdd:TIGR03345 623 GEQNLITINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEG 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 718 REIDFRNTVILMTANLGSDLLMQLLDEQPEASESD-LHELLRG----HFQPALLARFQTVIYRPLPAGALRAIVGMKLGQ 792
Cdd:TIGR03345 703 REIDFKNTVILLTSNAGSDLIMALCADPETAPDPEaLLEALRPellkVFKPAFLGRMTVIPYLPLDDDVLAAIVRLKLDR 782
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 835824986 793 VSQRLACHYGITTTLSESLFDALTEACLLPDTGARNVDSLLNQQILPALSQQLLSHMAAGQKPRQVTL 860
Cdd:TIGR03345 783 IARRLKENHGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQILERLAAGEPIERIHL 850
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
8-866 |
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: 1083.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 8 LRRLNPCCARAMEGAASLCQTRAHAEILPEHWLLKLLEQGEGDLTVLARRYEWDMDALWQDLLNWLDKQPR--SVRHRPQ 85
Cdd:COG0542 3 FEKFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGRLPKvsGSSGQPY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 86 LSDHTLRLMQEAWLIASLSGEAQIRSVHLLMALVEKQNLIQCDglwpLLTLGQRQLERLRPLLDAQSDERPPAQQEAALA 165
Cdd:COG0542 83 LSPRLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAAR----ILKKLGITLEALREALEELRGGSRVTSQNPESK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 166 QPhggdvefvgrpagselnadglnpalqnALDKFTLDVTAKARDGQIDPVFGRDTEIRQMVDILSRRRKNNPILVGEPGV 245
Cdd:COG0542 159 TP---------------------------ALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 246 GKTALVEGLALRIAEGNVPDALKPVSVRTLDLGLLQAGAGVKGEFEQRLKNIIEAVQQSPSPVLLFIDEAHTIIGAGNQA 325
Cdd:COG0542 212 GKTAIVEGLAQRIVNGDVPESLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKSEGNIILFIDELHTLVGAGGAE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 326 GGADAANLLKPALARGELRTIAATTWSEYKQYFERDAALERRFQMVKVDEPDDDTACLMLRGLKSRYADHHGVHITDDAV 405
Cdd:COG0542 292 GAMDAANLLKPALARGELRCIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEAL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 406 RAAVTLSRRYLTGRQLPDKAVDLLDTASARLRMSLDTVPEPLTRMKAQLTVLAMEKQALLEDIALGNSargDRLAAIEQE 485
Cdd:COG0542 372 VAAVRLSDRYITDRFLPDKAIDLIDEAAARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASF---ERLAELRDE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 486 ENRLILALDTLETQYGQELQLTEALLACRRDISRQ-AEISDLQTALIAVQQ----GNPLLGLDVDVRTVATVIADWTGVP 560
Cdd:COG0542 449 LAELEEELEALKARWEAEKELIEEIQELKEELEQRyGKIPELEKELAELEEelaeLAPLLREEVTEEDIAEVVSRWTGIP 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 561 LSSLMKDEQTELLSLEESLGKRVVGQEAALSAIARRLRAAKTGLTPENGPQGVFLLVGPSGTGKTETALALADALFGGEK 640
Cdd:COG0542 529 VGKLLEGEREKLLNLEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDED 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 641 ALITINLSEYQEPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDRGVMRDGEGREI 720
Cdd:COG0542 609 ALIRIDMSEYMEKHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTV 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 721 DFRNTVILMTANLGSDLLMQLLDEQP--EASESDLHELLRGHFQPALLARF-QTVIYRPLPAGALRAIVGMKLGQVSQRL 797
Cdd:COG0542 689 DFRNTIIIMTSNIGSELILDLAEDEPdyEEMKEAVMEELKKHFRPEFLNRIdEIIVFHPLSKEELRKIVDLQLKRLRKRL 768
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 835824986 798 ACHyGITTTLSESLFDALTEACLLPDTGARNVDSLLNQQILPALSQQLLSHMAAGQKPrqVTLGYHEEE 866
Cdd:COG0542 769 AER-GITLELTDAAKDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDT--ITVDVDDGE 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: 722.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 18 AMEGAASLCQTRAHAEILPEHWLLKLLEQGEGDLTVLARRYEWDMDALWQDLLNWLDKQPR--SVRHRPQLSDHTLRLMQ 95
Cdd:TIGR03346 8 ALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEKELERLPKvsGPGGQVYLSPDLNRLLN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 96 EAWLIASLSGEAQIRSVHLLMALVEkqnliqcdglwplltlGQRQLERLrpLLDAQSDerpPAQQEAALAQPHGGDvefv 175
Cdd:TIGR03346 88 LAEKLAQKRGDEFISSEHLLLALLD----------------DKGTLGKL--LKEAGAT---ADALEAAINAVRGGQ---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 176 grpagselNADGLNPALQ-NALDKFTLDVTAKARDGQIDPVFGRDTEIRQMVDILSRRRKNNPILVGEPGVGKTALVEGL 254
Cdd:TIGR03346 143 --------KVTDANAEDQyEALEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 255 ALRIAEGNVPDALKPVSVRTLDLGLLQAGAGVKGEFEQRLKNIIEAVQQSPSPVLLFIDEAHTIIGAGNQAGGADAANLL 334
Cdd:TIGR03346 215 AQRIVNGDVPEGLKNKRLLALDMGALIAGAKYRGEFEERLKAVLNEVTKSEGQIILFIDELHTLVGAGKAEGAMDAGNML 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 335 KPALARGELRTIAATTWSEYKQYFERDAALERRFQMVKVDEPDDDTACLMLRGLKSRYADHHGVHITDDAVRAAVTLSRR 414
Cdd:TIGR03346 295 KPALARGELHCIGATTLDEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 415 YLTGRQLPDKAVDLLDTASARLRMSLDTVPEPLTRMKAQLTVLAMEKQALLEDialGNSARGDRLAAIEQEENRLILALD 494
Cdd:TIGR03346 375 YITDRFLPDKAIDLIDEAAARIRMEIDSKPEELDELDRRIIQLEIEREALKKE---KDEASKKRLEDLEKELADLEEEYA 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 495 TLETQYGQELQLTEALLACRRDISR------QAE---------------ISDLQTALIAVQQG-----NPLLGLDVDVRT 548
Cdd:TIGR03346 452 ELEEQWKAEKASIQGIQQIKEEIEQvrleleQAEregdlakaaelqygkLPELEKQLQAAEQKlgeeqNRLLREEVTAEE 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 549 VATVIADWTGVPLSSLMKDEQTELLSLEESLGKRVVGQEAALSAIARRLRAAKTGLTPENGPQGVFLLVGPSGTGKTETA 628
Cdd:TIGR03346 532 IAEVVSRWTGIPVSKMLEGEREKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELA 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 629 LALADALFGGEKALITINLSEYQEPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFD 708
Cdd:TIGR03346 612 KALAEFLFDSEDAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLD 691
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 709 RGVMRDGEGREIDFRNTVILMTANLGSDLLMQLL-DEQPEASESDLHELLRGHFQPALLARF-QTVIYRPLPAGALRAIV 786
Cdd:TIGR03346 692 DGRLTDGQGRTVDFRNTVIIMTSNLGSDFIQELAgGDDYEEMREAVMEVLRAHFRPEFLNRIdEIVVFHPLGREQIARIV 771
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 835824986 787 GMKLGQVSQRLAcHYGITTTLSESLFDALTEACLLPDTGARNVDSLLNQQILPALSQQLLS 847
Cdd:TIGR03346 772 EIQLGRLRKRLA-ERKITLELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILA 831
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
193-847 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 584.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 193 QNALDKFTLDVTAKARDGQIDPVFGRDTEIRQMVDILSRRRKNNPILVGEPGVGKTALVEGLALRIAEGNVPDALKPVSV 272
Cdd:PRK10865 158 RQALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 273 RTLDLGLLQAGAGVKGEFEQRLKNIIEAVQQSPSPVLLFIDEAHTIIGAGNQAGGADAANLLKPALARGELRTIAATTWS 352
Cdd:PRK10865 238 LALDMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLD 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 353 EYKQYFERDAALERRFQMVKVDEPDDDTACLMLRGLKSRYADHHGVHITDDAVRAAVTLSRRYLTGRQLPDKAVDLLDTA 432
Cdd:PRK10865 318 EYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEA 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 433 SARLRMSLDTVPEPLTRMKAQLTVLAMEKQALLEDialGNSARGDRLAAIEQEENRLILALDTLETQYGQE--------- 503
Cdd:PRK10865 398 ASSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKE---SDEASKKRLDMLNEELSDKERQYSELEEEWKAEkaslsgtqt 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 504 --LQLTEALLA---CRR--DISRQAE-----ISDLQTALIAVQQGN----PLLGLDVDVRTVATVIADWTGVPLSSLMKD 567
Cdd:PRK10865 475 ikAELEQAKIAieqARRvgDLARMSElqygkIPELEKQLAAATQLEgktmRLLRNKVTDAEIAEVLARWTGIPVSRMLES 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 568 EQTELLSLEESLGKRVVGQEAALSAIARRLRAAKTGLTPENGPQGVFLLVGPSGTGKTETALALADALFGGEKALITINL 647
Cdd:PRK10865 555 EREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDM 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 648 SEYQEPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDRGVMRDGEGREIDFRNTVI 727
Cdd:PRK10865 635 SEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVV 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 728 LMTANLGSDLLMQLLDEQPEASESDL-HELLRGHFQPALLARF-QTVIYRPLPAGALRAIVGMKLGQVSQRLAcHYGITT 805
Cdd:PRK10865 715 IMTSNLGSDLIQERFGELDYAHMKELvLGVVSHNFRPEFINRIdEVVVFHPLGEQHIASIAQIQLQRLYKRLE-ERGYEI 793
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 835824986 806 TLSESLFDALTEACLLPDTGARNVDSLLNQQILPALSQQLLS 847
Cdd:PRK10865 794 HISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILS 835
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
196-847 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 583.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 196 LDKFTLDVTAKARDGQIDPVFGRDTEIRQMVDILSRRRKNNPILVGEPGVGKTALVEGLALRIAEGNVPDALKPVSVRTL 275
Cdd:CHL00095 162 LEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDKLVITL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 276 DLGLLQAGAGVKGEFEQRLKNIIEAVQQSpSPVLLFIDEAHTIIGAGNQAGGADAANLLKPALARGELRTIAATTWSEYK 355
Cdd:CHL00095 242 DIGLLLAGTKYRGEFEERLKRIFDEIQEN-NNIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLDEYR 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 356 QYFERDAALERRFQMVKVDEPDDDTACLMLRGLKSRYADHHGVHITDDAVRAAVTLSRRYLTGRQLPDKAVDLLDTASAR 435
Cdd:CHL00095 321 KHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLDEAGSR 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 436 LRMSLDTVPEpltrmkaQLTVLAMEKQALLEDIalgnsargdRLAAIEQEENRLILALDtletqygqelqlteallacrr 515
Cdd:CHL00095 401 VRLINSRLPP-------AARELDKELREILKDK---------DEAIREQDFETAKQLRD--------------------- 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 516 disRQAEISDLQTALIAVQQGNPLLGLDVDV---RTVATVIADWTGVPLSSLMKDEQTELLSLEESLGKRVVGQEAALSA 592
Cdd:CHL00095 444 ---REMEVRAQIAAIIQSKKTEEEKRLEVPVvteEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVA 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 593 IARRLRAAKTGLTPENGPQGVFLLVGPSGTGKTETALALADALFGGEKALITINLSEYQEPHTVSQLKGSPPGYVGYGQG 672
Cdd:CHL00095 521 VSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALASYFFGSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEG 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 673 GILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDRGVMRDGEGREIDFRNTVILMTANLGSDLL------MQLLDEQP 746
Cdd:CHL00095 601 GQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSKVIetnsggLGFELSEN 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 747 EASESDLHEL-------LRGHFQPALLARFQTVI-YRPLPAGALRAIVGMKLGQVSQRLAcHYGITTTLSESLFDALTEA 818
Cdd:CHL00095 681 QLSEKQYKRLsnlvneeLKQFFRPEFLNRLDEIIvFRQLTKNDVWEIAEIMLKNLFKRLN-EQGIQLEVTERIKTLLIEE 759
|
650 660
....*....|....*....|....*....
gi 835824986 819 CLLPDTGARNVDSLLNQQILPALSQQLLS 847
Cdd:CHL00095 760 GYNPLYGARPLRRAIMRLLEDPLAEEVLS 788
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
11-734 |
2.34e-133 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 416.93 E-value: 2.34e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 11 LNPCCARAMEgaaslcqtRAHAEILPEHWLLKLLEQGEGDLTVLARRYewDMDALWQDLLNWLDKQ----PRSVRHR--- 83
Cdd:PRK11034 10 LNMAFARARE--------HRHEFMTVEHLLLALLSNPSAREALEACSV--DLVALRQELEAFIEQTtpvlPASEEERdtq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 84 PQLSDHtlRLMQEAWLIASLSGEAQIRSVHLLMALVEKQNlIQCDGLwplltLGQRQLERLrpllDAQSDERPPAQQEAA 163
Cdd:PRK11034 80 PTLSFQ--RVLQRAVFHVQSSGRSEVTGANVLVAIFSEQE-SQAAYL-----LRKHEVSRL----DVVNFISHGTRKDEP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 164 LAQPHGGDVEFVGRPAGSElnadglnpalqNALDKFTLDVTAKARDGQIDPVFGRDTEIRQMVDILSRRRKNNPILVGEP 243
Cdd:PRK11034 148 SQSSDPGSQPNSEEQAGGE-----------ERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGES 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 244 GVGKTALVEGLALRIAEGNVPDALKPVSVRTLDLGLLQAGAGVKGEFEQRLKNIIEAVQQSPSPVLlFIDEAHTIIGAGN 323
Cdd:PRK11034 217 GVGKTAIAEGLAWRIVQGDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSIL-FIDEIHTIIGAGA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 324 QAGG-ADAANLLKPALARGELRTIAATTWSEYKQYFERDAALERRFQMVKVDEPDDDTACLMLRGLKSRYADHHGVHITD 402
Cdd:PRK11034 296 ASGGqVDAANLIKPLLSSGKIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 403 DAVRAAVTLSRRYLTGRQLPDKAVDLLDTASARLRMSldtvpePLTRMKAQLTVlamekqalledialgnsargdrlAAI 482
Cdd:PRK11034 376 KAVRAAVELAVKYINDRHLPDKAIDVIDEAGARARLM------PVSKRKKTVNV-----------------------ADI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 483 EqeenrlilaldtletqygqelqlteallacrrdisrqaeisdlqtaliavqqgnpllgldvdvrtvaTVIADWTGVPLS 562
Cdd:PRK11034 427 E-------------------------------------------------------------------SVVARIARIPEK 439
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 563 SLMKDEQTELLSLEESLGKRVVGQEAALSAIARRLRAAKTGLTPENGPQGVFLLVGPSGTGKTETALALADALfGGEkaL 642
Cdd:PRK11034 440 SVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL-GIE--L 516
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 643 ITINLSEYQEPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDRGVMRDGEGREIDF 722
Cdd:PRK11034 517 LRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADF 596
|
730
....*....|..
gi 835824986 723 RNTVILMTANLG 734
Cdd:PRK11034 597 RNVVLVMTTNAG 608
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
572-774 |
2.61e-89 |
|
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: 280.60 E-value: 2.61e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 572 LLSLEESLGKRVVGQEAALSAIARRLRAAKTGLTPENGPQGVFLLVGPSGTGKTETALALADALFGGEKALITINLSEYQ 651
Cdd:cd19499 2 LLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 652 EPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDRGVMRDGEGREIDFRNTVILMTA 731
Cdd:cd19499 82 EKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTS 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 835824986 732 NlgsdllmqlldeqpeasesdlhellrgHFQPALLARFQTVIY 774
Cdd:cd19499 162 N---------------------------HFRPEFLNRIDEIVV 177
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
610-769 |
2.84e-69 |
|
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400187 [Multi-domain] Cd Length: 168 Bit Score: 226.69 E-value: 2.84e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 610 PQGVFLLVGPSGTGKTETALALADALFGGEKALITINLSEYQEPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLL 689
Cdd:pfam07724 2 PIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 690 DEVEKAHRDVMNLFYQVFDRGVMRDGEGREIDFRNTVILMTANLGSDLLMQLLDEQPEASESDLHE----LLRGHFQPAL 765
Cdd:pfam07724 82 DEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRLGDSPDYELLKEevmdLLKKGFIPEF 161
|
....
gi 835824986 766 LARF 769
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 ... |
377-483 |
2.53e-40 |
|
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: 143.78 E-value: 2.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 377 DDDTACLMLRGLKSRYADHHGVHITDDAVRAAVTLSRRYLTGRQLPDKAVDLLDTASARLRMSLDTVPEPLTRMKAQLTV 456
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|....*..
gi 835824986 457 LAMEKQALLEDialGNSARGDRLAAIE 483
Cdd:pfam17871 81 LEIEKEALERE---QDFEKAERLAKLE 104
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
216-376 |
8.09e-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: 75.26 E-value: 8.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 216 FGRDTEIRQMVDILSRRRKNNPILVGEPGVGKTALVEGLALRIAEGNVPdalkpvsVRTLDLGLLQAGAGVKGEFEQRLK 295
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 296 NIIEAVQQSPSPVLLFIDEAHTiIGAGNQAGGADAANLLKPALA-RGELRTIAATTwseYKQYFERDAALERRFQMVKVD 374
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDS-LSRGAQNALLRVLETLNDLRIdRENVRVIGATN---RPLLGDLDRALYDRLDIRIVI 149
|
..
gi 835824986 375 EP 376
Cdd:cd00009 150 PL 151
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
584-777 |
2.55e-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: 74.10 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 584 VGQEAALSAIARRLraaktgltpENGPQGVFLLVGPSGTGKTETALALADALFGGEKALITINLSEYQEPHTVSqlkgsp 663
Cdd:cd00009 1 VGQEEAIEALREAL---------ELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVA------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 664 pGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDrgvmrDGEGREIDFRNTVILMTANLGSDllmqlld 743
Cdd:cd00009 66 -ELFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLE-----TLNDLRIDRENVRVIGATNRPLL------- 132
|
170 180 190
....*....|....*....|....*....|....
gi 835824986 744 eqpeasesdlhellrGHFQPALLARFQTVIYRPL 777
Cdd:cd00009 133 ---------------GDLDRALYDRLDIRIVIPL 151
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
610-738 |
8.94e-13 |
|
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: 66.63 E-value: 8.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 610 PQGVFLLVGPSGTGKTETALALADALFGGEKALITINLSEYQEPHTVSQLKGSPPGYVGYGQGG----ILTEAVRKRPYS 685
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGElrlrLALALARKLKPD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 835824986 686 VVLLDEVEKAHRDVMNLFYQVFDRGVMRDGEGREidfRNTVILMTANLGSDLL 738
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSE---KNLTVILTTNDEKDLG 130
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
614-742 |
1.27e-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: 62.70 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 614 FLLVGPSGTGKTETALALADALFGGEkaLITINLSEYQEPhtvSQLKGS--PPGYVGYGQGGILTEAVRKRpySVVLLDE 691
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRP--VFYVQLTRDTTE---EDLFGRrnIDPGGASWVDGPLVRAAREG--EIAVLDE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 835824986 692 VEKAHRDVMNLFYQVFDRGVMRDGEGREID---FRNTVILMTANLGSDLLMQLL 742
Cdd:pfam07728 75 INRANPDVLNSLLSLLDERRLLLPDGGELVkaaPDGFRLIATMNPLDRGLNELS 128
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
777-849 |
2.76e-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: 2.76e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 835824986 777 LPAGALRAIVGMKLGQVSQRLACHyGITTTLSESLFDALTEACLLPDTGARNVDSLLNQQILPALSQQLLSHM 849
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAER-GITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGE 72
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
781-869 |
2.87e-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) 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: 57.45 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 781 ALRAIVGMKLGQVSQRLAcHYGITTTLSESLFDALTEACLLPDTGARNVDSLLNQQILPALSQQLLSHMAAGQKPRQVTL 860
Cdd:smart01086 5 DLVRIVDLPLNALQKRLA-EKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVVVDV 83
|
....*....
gi 835824986 861 GyhEEEGVV 869
Cdd:smart01086 84 D--DGELVF 90
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
583-791 |
3.70e-10 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 61.05 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 583 VVGQEAALSAIAR-------RLRAAKTGLTPengPQGVfLLVGPSGTGKTETALALADALfggEKALITINLSEyqepht 655
Cdd:COG1223 4 VVGQEEAKKKLKLiikelrrRENLRKFGLWP---PRKI-LFYGPPGTGKTMLAEALAGEL---KLPLLTVRLDS------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 656 vsqLKGSppgYVGYGQGGI--LTEAVRKRPySVVLLDEVE--KAHRDVMNLfyqvfdrgvmrDGEGREIdfRNTVILMTA 731
Cdd:COG1223 71 ---LIGS---YLGETARNLrkLFDFARRAP-CVIFFDEFDaiAKDRGDQND-----------VGEVKRV--VNALLQELD 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 835824986 732 NLGSDLLM-------QLLDeqpeasesdlhellrghfqPALLARFQTVIYRPLP-AGALRAIVGMKLG 791
Cdd:COG1223 131 GLPSGSVViaatnhpELLD-------------------SALWRRFDEVIEFPLPdKEERKEILELNLK 179
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
238-371 |
9.76e-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: 9.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 238 ILVGEPGVGKTALVEGLAlriAEGNVPdalkpvsVRTLDLGLLqaGAGVKGEFEQRLKNIIEAVqQSPSPVLLFIDEAHT 317
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVA---KELGAP-------FIEISGSEL--VSKYVGESEKRLRELFEAA-KKLAPCVIFIDEIDA 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 835824986 318 IIGAGNQAG---GADAANLLKPALARGELRT-----IAATTwseykQYFERDAALERRFQMV 371
Cdd:pfam00004 69 LAGSRGSGGdseSRRVVNQLLTELDGFTSSNskvivIAATN-----RPDKLDPALLGRFDRI 125
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
615-777 |
1.88e-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: 56.45 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 615 LLVGPSGTGKTETALALADALFGgekALITINLSEyqephTVSQLKGSPPGYVgygqGGILTEAVRKRPySVVLLDEVEK 694
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGA---PFIEISGSE-----LVSKYVGESEKRL----RELFEAAKKLAP-CVIFIDEIDA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 695 -----------AHRDVMNLFYQVFDrgvmrdgeGREIDFRNTVILMTANlgsdlLMQLLDeqpeasesdlhellrghfqP 763
Cdd:pfam00004 69 lagsrgsggdsESRRVVNQLLTELD--------GFTSSNSKVIVIAATN-----RPDKLD-------------------P 116
|
170
....*....|....
gi 835824986 764 ALLARFQTVIYRPL 777
Cdd:pfam00004 117 ALLGRFDRIIEFPL 130
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
233-368 |
2.52e-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: 53.92 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 233 RKNNPILVGEPGVGKTALVEGLALRIAEGNVP-----DALKPVSVRTLDLGLLQAGAGVKGEFEQRLKNIIEAVQQSPsP 307
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGviyidGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLK-P 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 835824986 308 VLLFIDEAHTIIGAGNQAGGADAA--NLLKPALARGELRTIAATTWSEykqyFERDAALERRF 368
Cdd:smart00382 80 DVLILDEITSLLDAEQEALLLLLEelRLLLLLKSEKNLTVILTTNDEK----DLGPALLRRRF 138
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
587-698 |
2.64e-07 |
|
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: 51.13 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 587 EAALSAIARRLRAAKTGLTPENGPQGVfLLVGPSGTGKTETALALAdalfgGE--KALITINLSEYQEPhtvsqlkgspp 664
Cdd:cd19481 3 ASLREAVEAPRRGSRLRRYGLGLPKGI-LLYGPPGTGKTLLAKALA-----GElgLPLIVVKLSSLLSK----------- 65
|
90 100 110
....*....|....*....|....*....|....*.
gi 835824986 665 gYVGYGQGGI--LTEAVRKRPYSVVLLDEVEKAHRD 698
Cdd:cd19481 66 -YVGESEKNLrkIFERARRLAPCILFIDEIDAIGRK 100
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
32-379 |
3.91e-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: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 32 AEILPEHWLLKLLEQGEGDLTVLARRYEWDMDALWQDLLNWLDKQPRSVRHRPQLSDHTLRLMQEAWLIASLSGEAQIRS 111
Cdd:COG0464 5 LALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 112 VHLLMALVEKQNLIQCDGLWPLLTLGQRQLERLRPLLDAQSDERPPAQQEAALAQPHGGDVEFVGRPAGSELNADGLNPA 191
Cdd:COG0464 85 LLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 192 LQNALDKFTLdvtakardgqidpvfgrdtEIRQMVDILSRRRKNNP---ILVGEPGVGKTALVEGLAlRIAEGNVpdalk 268
Cdd:COG0464 165 VKEELRELVA-------------------LPLKRPELREEYGLPPPrglLLYGPPGTGKTLLARALA-GELGLPL----- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 269 pVSVRTLDLgllqAGAGVkGEFEQRLKNIIEAVQQSpSPVLLFIDEAHTIIGAGNQAGGADA----ANLLKpALA--RGE 342
Cdd:COG0464 220 -IEVDLSDL----VSKYV-GETEKNLREVFDKARGL-APCVLFIDEADALAGKRGEVGDGVGrrvvNTLLT-EMEelRSD 291
|
330 340 350
....*....|....*....|....*....|....*....
gi 835824986 343 LRTIAATTwseykqYFER-DAALERRFQ-MVKVDEPDDD 379
Cdd:COG0464 292 VVVIAATN------RPDLlDPALLRRFDeIIFFPLPDAE 324
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
423-785 |
1.95e-06 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 51.07 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 423 DKAVDLLDTASARLRMSLDTVPEPLTRMKAQLTVLAMEKQALLEDIALGNSARGDRLAAIEQEENRLILALDTLETQYGQ 502
Cdd:COG0464 1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 503 ELQLTEALLACRRDISRQAEISDLQTALIAVqqGNPLLGLDVDVRTVATVIADWTGVPLSSLMKDEQTELLSLEESLGKR 582
Cdd:COG0464 81 LLAALLSALELLLLGELLLLLLLLLLLLLLL--LDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 583 VVGQEAALSAIARRLRAAKT--------GLTPENGpqgvFLLVGPSGTGKTETALALADALfggEKALITINLSEyqeph 654
Cdd:COG0464 159 LGGLEEVKEELRELVALPLKrpelreeyGLPPPRG----LLLYGPPGTGKTLLARALAGEL---GLPLIEVDLSD----- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 655 TVSQlkgsppgYVGYGQGGI---LTEAVRKRPySVVLLDEVEKAHRdvmnlfyqvfDRGVMRDGEGREI---------DF 722
Cdd:COG0464 227 LVSK-------YVGETEKNLrevFDKARGLAP-CVLFIDEADALAG----------KRGEVGDGVGRRVvntlltemeEL 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 835824986 723 RNTVILM-TANlgsdlLMQLLDeqpeasesdlhellrghfqPALLARFQTVIYRPLP-AGALRAI 785
Cdd:COG0464 289 RSDVVVIaATN-----RPDLLD-------------------PALLRRFDEIIFFPLPdAEERLEI 329
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
231-316 |
1.01e-05 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 45.80 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 231 RRRKNNPILVGEPGVGKTALVEGLALRIAEGNVP----DALKPVSVRTLDLGLLQAgAGVKGEFEQRLKNIIEAVQQ--- 303
Cdd:pfam13401 2 RFGAGILVLTGESGTGKTTLLRRLLEQLPEVRDSvvfvDLPSGTSPKDLLRALLRA-LGLPLSGRLSKEELLAALQQlll 80
|
90
....*....|....
gi 835824986 304 -SPSPVLLFIDEAH 316
Cdd:pfam13401 81 aLAVAVVLIIDEAQ 94
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
214-316 |
6.98e-05 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 44.03 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 214 PVFGRDTEIRQMVDILSRRRKNNP---ILVGEPGVGKTALVEGLALRIAEGNV--------------------------- 263
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERDGGyflrgkcdenlpyspllealtregllr 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 835824986 264 -----PDALKPVSVRTLDLGLLQAGAGVKGEFEQR----LKNIIEAVQQSPSPVLLFIDEAH 316
Cdd:pfam13191 81 qlldeLESSLLEAWRAALLEALAPVPELPGDLAERlldlLLRLLDLLARGERPLVLVLDDLQ 142
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
586-645 |
1.25e-04 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 45.24 E-value: 1.25e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 835824986 586 QEAALSAIARRLRAAKTgltPENGPQGVFLLVGPSGTGKTETA--LALADALFGGEK-ALITI 645
Cdd:COG1419 142 WRALLEALARRLPVAED---PLLDEGGVIALVGPTGVGKTTTIakLAARFVLRGKKKvALITT 201
|
|
| CDC6 |
COG1474 |
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]; |
582-705 |
1.69e-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: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 582 RVVGQEAALSAIARRLRAAKTGLTPENGpqgvfLLVGPSGTGKTETALALADAL------FGGEKALITINLSEYQEPHT 655
Cdd:COG1474 27 RLPHREEEIEELASALRPALRGERPSNV-----LIYGPTGTGKTAVAKYVLEELeeeaeeRGVDVRVVYVNCRQASTRYR 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 835824986 656 V-----SQLK-GSPPGYVGYGQG---GILTEAVRKRPYSVVL-LDEVEKAHRDVMN-LFYQ 705
Cdd:COG1474 102 VlsrilEELGsGEDIPSTGLSTDelfDRLYEALDERDGVLVVvLDEIDYLVDDEGDdLLYQ 162
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
577-714 |
2.09e-04 |
|
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410906 [Multi-domain] Cd Length: 183 Bit Score: 43.14 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 577 ESLGKRVVGQEAALSAIA-------RRLRAA---KTGLTPENgpqgvFLLVGPSGTGKTETA--LA-LADALFggekalI 643
Cdd:cd19498 7 SELDKYIIGQDEAKRAVAialrnrwRRMQLPeelRDEVTPKN-----ILMIGPTGVGKTEIArrLAkLAGAPF------I 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 835824986 644 TINLSEYQEphtvsqlkgspPGYVGYGQGGILTEAVRkrpySVVLLDEVEKAHRDVMNLFYQVFDRGVMRD 714
Cdd:cd19498 76 KVEATKFTE-----------VGYVGRDVESIIRDLVE----GIVFIDEIDKIAKRGGSSGPDVSREGVQRD 131
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
238-318 |
2.72e-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: 42.27 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 238 ILVGEPGVGKTALVEGLAlriAEGNVPdalkpvsVRTLDLGLLQAGAgvKGEFEQRLKNIIEAVQQSpSPVLLFIDEAHT 317
Cdd:cd19481 30 LLYGPPGTGKTLLAKALA---GELGLP-------LIVVKLSSLLSKY--VGESEKNLRKIFERARRL-APCILFIDEIDA 96
|
.
gi 835824986 318 I 318
Cdd:cd19481 97 I 97
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
586-643 |
6.67e-04 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 43.47 E-value: 6.67e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 835824986 586 QEAALSAIARRLRAAKtgltpengpqGVFLLVGPSGTGKTETALALADALFGGEKALI 643
Cdd:COG1061 85 QQEALEALLAALERGG----------GRGLVVAPTGTGKTVLALALAAELLRGKRVLV 132
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
600-785 |
6.80e-04 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 42.69 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 600 AKTGLTPengPQGVfLLVGPSGTGKTETALALADALfggEKALITINLSEYQEPhtvsqlkgsppgYVgyGQGG-----I 674
Cdd:COG1222 105 RKYGIEP---PKGV-LLYGPPGTGKTLLAKAVAGEL---GAPFIRVRGSELVSK------------YI--GEGArnvreV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 675 LTEAVRKRPySVVLLDEVEK--AHRD----------VMNLFYQVFDrgvmrdgegrEIDFRNTVILMTA-NlgsdlLMQL 741
Cdd:COG1222 164 FELAREKAP-SIIFIDEIDAiaARRTddgtsgevqrTVNQLLAELD----------GFESRGDVLIIAAtN-----RPDL 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 835824986 742 LDeqpeasesdlhellrghfqPALL--ARFQTVIYRPLP-AGALRAI 785
Cdd:COG1222 228 LD-------------------PALLrpGRFDRVIEVPLPdEEAREEI 255
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
608-708 |
8.22e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 40.40 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 608 NGPQGVFLLVGPSGTGKTETALALADALFGGEKALITINLSEYQEPHTVSQ--LKGSPPGYVGYGQGGILTEAV-----R 680
Cdd:pfam13401 2 RFGAGILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRalLRALGLPLSGRLSKEELLAALqqlllA 81
|
90 100
....*....|....*....|....*...
gi 835824986 681 KRPYSVVLLDEVEKAHRDVMNLFYQVFD 708
Cdd:pfam13401 82 LAVAVVLIIDEAQHLSLEALEELRDLLN 109
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
574-732 |
1.36e-03 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 42.22 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 574 SLEEslgkrVVGQEAALSAIARRLRAAKTGltpenGPQGVFLLVGPSGTGKTETALALA-DalFGGEkaLITINLSEYQe 652
Cdd:PRK04195 12 TLSD-----VVGNEKAKEQLREWIESWLKG-----KPKKALLLYGPPGVGKTSLAHALAnD--YGWE--VIELNASDQR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 653 phTVSQLKgsppGYVGYG-QGGILTEAVRKrpysVVLLDEVEkahrdvmNLFYQVfDRGVMrdgegREI-----DFRNTV 726
Cdd:PRK04195 77 --TADVIE----RVAGEAaTSGSLFGARRK----LILLDEVD-------GIHGNE-DRGGA-----RAIlelikKAKQPI 133
|
....*.
gi 835824986 727 IlMTAN 732
Cdd:PRK04195 134 I-LTAN 138
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
586-702 |
2.34e-03 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 41.43 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 586 QEAALSAIARRLRAAKTgLTPENGPQgVFLLVGPSGTGKTETALALAD--ALFGGEKAL----ITIN---LSEYQEPHTV 656
Cdd:PRK12723 151 RDSVIIYIAKTIKCSGS-IIDNLKKR-VFILVGPTGVGKTTTIAKLAAiyGINSDDKSLnikiITIDnyrIGAKKQIQTY 228
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 835824986 657 SQLKGSPPGYVGYGQgGILTEAVRKRPYSVVLLDEVEKAHRDVMNL 702
Cdd:PRK12723 229 GDIMGIPVKAIESFK-DLKEEITQSKDFDLVLVDTIGKSPKDFMKL 273
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
402-645 |
2.39e-03 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 41.29 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 402 DDAVRAAVTLSRRYLTGRQLPDKAvdllDTASARLRMSLDTVPEPLTRMKAQLTVLAMEKQALLEDIAlgnsargDRLAA 481
Cdd:COG1401 34 DDLRGAAELATRLAERLSEELLRA----DRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEA-------AVAIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 482 IEQEENRLILALDTLETQYGQELQLTEALLACRRDISRQAEISDLQTALIAVQQGNPLLGLDV---DVRTVATVIADWTG 558
Cdd:COG1401 103 ELYELEADSEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETEVLEALEAELEELlaaPEDLSADALAAELS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 559 VPLSSLMKDEQTELLSLEESLGKRvvgQEAALSAIARRLRAAKtgltpengpqgvFL-LVGPSGTGKTETALALADALFG 637
Cdd:COG1401 183 AAEELYSEDLESEDDYLKDLLREK---FEETLEAFLAALKTKK------------NViLAGPPGTGKTYLARRLAEALGG 247
|
....*...
gi 835824986 638 GEKALITI 645
Cdd:COG1401 248 EDNGRIEF 255
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
586-645 |
2.51e-03 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 40.78 E-value: 2.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 835824986 586 QEAALSAIARRLRAAKTGLTPENGPqGVFLLVGPSGTGKTeTALA-LAdALF----GGEK-ALITI 645
Cdd:TIGR03499 170 WRWLREALEGMLPVKPEEDPILEQG-GVIALVGPTGVGKT-TTLAkLA-ARFalehGKKKvALITT 232
|
|
| rfc |
PRK00440 |
replication factor C small subunit; Reviewed |
574-637 |
2.65e-03 |
|
replication factor C small subunit; Reviewed
Pssm-ID: 234763 [Multi-domain] Cd Length: 319 Bit Score: 41.01 E-value: 2.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 835824986 574 SLEEslgkrVVGQEAalsaIARRLRA-AKTGLTPEngpqgvFLLVGPSGTGKTETALALADALFG 637
Cdd:PRK00440 15 TLDE-----IVGQEE----IVERLKSyVKEKNMPH------LLFAGPPGTGKTTAALALARELYG 64
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
583-636 |
4.20e-03 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 40.17 E-value: 4.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 835824986 583 VVGQEAalsaIARRLR-AAKTG-LTPengpqgVFLLVGPSGTGKTETALALADALF 636
Cdd:COG2812 12 VVGQEH----VVRTLKnALASGrLAH------AYLFTGPRGVGKTTLARILAKALN 57
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
474-635 |
4.96e-03 |
|
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: 40.45 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 474 ARGDRLAAIEQEENRLILALDTLETQYGQELQLTEALLACRRDISRQAEISDLQTALIAVQQGNPLLGLDVDVRTVATVI 553
Cdd:COG1203 11 GALALAALLLLLLALLLAALLLLLLAALLLALLLALLLLAALELALLLLLLLLLLLLLLLLLLDLLLDDLAFLFLLLLID 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 554 ADWTGVPLSSLMKDEQTELLS--LEESLGKRvvgqeAALSAIARRLR--AAKTGLTPENGPQGVFLLVGPSGTGKTETAL 629
Cdd:COG1203 91 ADWLDSANFDMARQALDHLLAerLERLLPKK-----SKPRTPINPLQneALELALEAAEEEPGLFILTAPTGGGKTEAAL 165
|
....*.
gi 835824986 630 ALADAL 635
Cdd:COG1203 166 LFALRL 171
|
|
| TIP49 |
COG1224 |
DNA helicase TIP49, TBP-interacting protein [Transcription]; |
584-681 |
5.01e-03 |
|
DNA helicase TIP49, TBP-interacting protein [Transcription];
Pssm-ID: 440837 [Multi-domain] Cd Length: 452 Bit Score: 40.34 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 584 VGQEAALSA---IARRLRAAKTGltpengPQGVfLLVGPSGTGKTETALALADALfGGEKALITINLSE-YQephtvSQL 659
Cdd:COG1224 41 VGQVEAREAagiVVKMIKEGKMA------GKGI-LIVGPPGTGKTALAVAIAREL-GEDTPFVAISGSEiYS-----AEL 107
|
90 100
....*....|....*....|..
gi 835824986 660 KgsppgyvgygQGGILTEAVRK 681
Cdd:COG1224 108 K----------KTEFLMQALRK 119
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
239-316 |
5.12e-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: 39.77 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835824986 239 LVGEPGVGKTALVEGLALRIAEGNV----------PDALkpvsVRTL--DLGLLQAGAGvKGEFEQRLKNIIEAVQQSPS 306
Cdd:COG3267 48 LTGEVGTGKTTLLRRLLERLPDDVKvayipnpqlsPAEL----LRAIadELGLEPKGAS-KADLLRQLQEFLLELAAAGR 122
|
90
....*....|
gi 835824986 307 PVLLFIDEAH 316
Cdd:COG3267 123 RVVLIIDEAQ 132
|
|
| PulE-GspE-like |
cd01129 |
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ... |
608-645 |
7.82e-03 |
|
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: 37.85 E-value: 7.82e-03
10 20 30
....*....|....*....|....*....|....*...
gi 835824986 608 NGPQGVFLLVGPSGTGKTETALALADALFGGEKALITI 645
Cdd:cd01129 8 KRPHGLILVTGPTGSGKTTTLYAMLRELNGPERNIITI 45
|
|
| |
