|
Name |
Accession |
Description |
Interval |
E-value |
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
15-866 |
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: 1242.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 15 LDADTRRDLEGSAERCVARGGSKVLVEDLLLGLLERPQGLLARALQDAAVDAGELNAALQ---ARGEHSASRNPVFAPEL 91
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLAralDKLPRGNTRTPVFSPHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 92 VQWLQDALLLANLELGRSQIDQAALILALLRNP-LRYAGSRYQPLLARLDIERLKdFALSQPLEGAP------------- 157
Cdd:TIGR03345 81 VELLQEAWLLASLELGDGRIRSGHLLLALLTDPeLRRLLGSISPELAKIDREALR-EALPALVEGSAeasaaaadaapag 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 158 SGKPGGGESLLQRFTHNLTQQARDGKLDPVLCRDGAIRQMVDILARRRKNNPIVVGEAGVGKTAIVEGLASRIAAGEVPP 237
Cdd:TIGR03345 160 AAAGAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVPP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 238 ALRDVELLSLDMGLLQAGASVKGEFERRLKGVIDEVKAAPRPTILFIDEAHTLIGAGGQAGGSDAANLLKPALARGELRT 317
Cdd:TIGR03345 240 ALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPIILFIDEAHTLIGAGGQAGQGDAANLLKPALARGELRT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 318 IAATTWAEYKKYFEKDPALARRFQPVQLHEPSVAEAVTILRGLARVYEESHGIYLRDDAVVAAAELSARYLAGRQLPDKA 397
Cdd:TIGR03345 320 IAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLPDKA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 398 VDVLDTACARVRISLAAAPESLERLRGELAEGERQRQALRRDAEAGLPIDHdALQALEERLAQAESERHVQEDQWSRQRE 477
Cdd:TIGR03345 400 VSLLDTACARVALSQNATPAALEDLRRRIAALELELDALEREAALGADHDE-RLAELRAELAALEAELAALEARWQQEKE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 478 LAERLLALRQQLarareanreeqgsEADAEAFPADEHggveALEKALHETRQALADAQAQGRLVSFEVCPRLVAEVIGAW 557
Cdd:TIGR03345 479 LVEAILALRAEL-------------EADADAPADDDD----ALRAQLAELEAALASAQGEEPLVFPEVDAQAVAEVVADW 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 558 TGVPVEQLAREHNAKVMGFADDLRTRIRGQEQAVSALDRAMRATAAGLNKPDAPVGVFLLVGPSGVGKTETALALADLLY 637
Cdd:TIGR03345 542 TGIPVGRMVRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLY 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 638 GGERFITTINMSEFQEKHTVSRLIGAPPGYVGYGEGGMLTEAVRQKPYSVILLDEVEKADPDVLNLFYQIFDKGVANDGE 717
Cdd:TIGR03345 622 GGEQNLITINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGE 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 718 GREIDFRNTLILMTSNLASEHIAALCQDGAR-PSAELLEETIRPALSRHFKPALLARMRVVPYYPVGGPVLRELIEIKLQ 796
Cdd:TIGR03345 702 GREIDFKNTVILLTSNAGSDLIMALCADPETaPDPEALLEALRPELLKVFKPAFLGRMTVIPYLPLDDDVLAAIVRLKLD 781
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596859 797 RLGERLARR-QLAFDYSQALVGHLAERCTQSDSGARLIDHLLDTHLLPLVADRLLEAMARDERLERVHATL 866
Cdd:TIGR03345 782 RIARRLKENhGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQILERLAAGEPIERIHLDV 852
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
51-857 |
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: 996.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 51 PQGLLARALQDAAVDAGELNAALQAR-----GEHSASRNPVFAPELVQWLQDALLLANlELGRSQIDQAALILALLRNPL 125
Cdd:COG0542 42 GEGLAAKLLRKLGVDLDALREELEEAlgrlpKVSGSSGQPYLSPRLKRVLELAELEAR-KLGDEYISTEHLLLALLREGE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 126 RYAGSryqpLLARLDI--ERLKDfALSQPLEG--APSGKPGGGESLLQRFTHNLTQQARDGKLDPVLCRDGAIRQMVDIL 201
Cdd:COG0542 121 GVAAR----ILKKLGItlEALRE-ALEELRGGsrVTSQNPESKTPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQIL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 202 ARRRKNNPIVVGEAGVGKTAIVEGLASRIAAGEVPPALRDVELLSLDMGLLQAGASVKGEFERRLKGVIDEVKAAPRPTI 281
Cdd:COG0542 196 SRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKSEGNII 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 282 LFIDEAHTLIGAGGQAGGSDAANLLKPALARGELRTIAATTWAEYKKYFEKDPALARRFQPVQLHEPSVAEAVTILRGLA 361
Cdd:COG0542 276 LFIDELHTLVGAGGAEGAMDAANLLKPALARGELRCIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLK 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 362 RVYEESHGIYLRDDAVVAAAELSARYLAGRQLPDKAVDVLDTACARVRISLAAAPESLERLRGELAEGERQRQALRRDAE 441
Cdd:COG0542 356 ERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAIDLIDEAAARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQD 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 442 AGlpiDHDALQALEERLAQAESERHVQEDQWSRQRELAERLLALRQQLarareanreeqgseadaeafpADEHGGVEALE 521
Cdd:COG0542 436 EA---SFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL---------------------EQRYGKIPELE 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 522 KALHETRQALAdaqAQGRLVSFEVCPRLVAEVIGAWTGVPVEQLAREHNAKVMGFADDLRTRIRGQEQAVSALDRAMRAT 601
Cdd:COG0542 492 KELAELEEELA---ELAPLLREEVTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEEELHERVIGQDEAVEAVADAIRRS 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 602 AAGLNKPDAPVGVFLLVGPSGVGKTETALALADLLYGGERFITTINMSEFQEKHTVSRLIGAPPGYVGYGEGGMLTEAVR 681
Cdd:COG0542 569 RAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYMEKHSVSRLIGAPPGYVGYEEGGQLTEAVR 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 682 QKPYSVILLDEVEKADPDVLNLFYQIFDKGVANDGEGREIDFRNTLILMTSNLASEHIAALCQDGarPSAELLEETIRPA 761
Cdd:COG0542 649 RRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIGSELILDLAEDE--PDYEEMKEAVMEE 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 762 LSRHFKPALLARM-RVVPYYPVGGPVLRELIEIKLQRLGERLARRQLAFDYSQALVGHLAERCTQSDSGARLIDHLLDTH 840
Cdd:COG0542 727 LKKHFRPEFLNRIdEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAAKDFLAEKGYDPEYGARPLKRAIQRE 806
|
810
....*....|....*..
gi 15596859 841 LLPLVADRLLEAMARDE 857
Cdd:COG0542 807 LEDPLAEEILAGEIKEG 823
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
52-850 |
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: 682.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 52 QGLLARALQDAAVDAGELNAALQARGEH-----SASRNPVFAPELVQWLQDALLLANlELGRSQIDQAALILALLRNP-- 124
Cdd:TIGR03346 38 GGLARPLLQKAGVNVGALRQALEKELERlpkvsGPGGQVYLSPDLNRLLNLAEKLAQ-KRGDEFISSEHLLLALLDDKgt 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 125 ----LRYAGSRYQPLLARLDIERLKDFALSQPLEGApsgkpgggESLLQRFTHNLTQQARDGKLDPVLCRDGAIRQMVDI 200
Cdd:TIGR03346 117 lgklLKEAGATADALEAAINAVRGGQKVTDANAEDQ--------YEALEKYARDLTERAREGKLDPVIGRDEEIRRTIQV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 201 LARRRKNNPIVVGEAGVGKTAIVEGLASRIAAGEVPPALRDVELLSLDMGLLQAGASVKGEFERRLKGVIDEVKAAPRPT 280
Cdd:TIGR03346 189 LSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLALDMGALIAGAKYRGEFEERLKAVLNEVTKSEGQI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 281 ILFIDEAHTLIGAGGQAGGSDAANLLKPALARGELRTIAATTWAEYKKYFEKDPALARRFQPVQLHEPSVAEAVTILRGL 360
Cdd:TIGR03346 269 ILFIDELHTLVGAGKAEGAMDAGNMLKPALARGELHCIGATTLDEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 361 ARVYEESHGIYLRDDAVVAAAELSARYLAGRQLPDKAVDVLDTACARVRISLAAAPESLERLRGELAEGERQRQALRRDA 440
Cdd:TIGR03346 349 KERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAARIRMEIDSKPEELDELDRRIIQLEIEREALKKEK 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 441 EAGlpiDHDALQALEERLAQAESERHVQEDQWSRQRELAERLLALRQQLARAR---EANREEQGSEADAEAfpadEHGGV 517
Cdd:TIGR03346 429 DEA---SKKRLEDLEKELADLEEEYAELEEQWKAEKASIQGIQQIKEEIEQVRlelEQAEREGDLAKAAEL----QYGKL 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 518 EALEKALHETRQALAdaQAQGRLVSFEVCPRLVAEVIGAWTGVPVEQLAREHNAKVMGFADDLRTRIRGQEQAVSALDRA 597
Cdd:TIGR03346 502 PELEKQLQAAEQKLG--EEQNRLLREEVTAEEIAEVVSRWTGIPVSKMLEGEREKLLHMEEELHERVVGQDEAVEAVSDA 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 598 MRATAAGLNKPDAPVGVFLLVGPSGVGKTETALALADLLYGGERFITTINMSEFQEKHTVSRLIGAPPGYVGYGEGGMLT 677
Cdd:TIGR03346 580 IRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLT 659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 678 EAVRQKPYSVILLDEVEKADPDVLNLFYQIFDKGVANDGEGREIDFRNTLILMTSNLASEHIAALCQDGARpsaELLEET 757
Cdd:TIGR03346 660 EAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDFIQELAGGDDY---EEMREA 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 758 IRPALSRHFKPALLARM-RVVPYYPVGGPVLRELIEIKLQRLGERLARRQLAFDYSQALVGHLAERCTQSDSGARLIDHL 836
Cdd:TIGR03346 737 VMEVLRAHFRPEFLNRIdEIVVFHPLGREQIARIVEIQLGRLRKRLAERKITLELSDAALDFLAEAGYDPVYGARPLKRA 816
|
810
....*....|....
gi 15596859 837 LDTHLLPLVADRLL 850
Cdd:TIGR03346 817 IQREIENPLAKKIL 830
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
87-831 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 583.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 87 FAPELVQWLQDALLLANlELGRSQIDQAALILALLRNPLRYAGSRYQPLlaRLDIERLKDFA---LSQPLEGAPSGKPGG 163
Cdd:CHL00095 80 FTPRAKRVLEMSLEEAR-DLGHNYIGTEHLLLALLEEGEGVAARVLENL--GVDLSKIRSLIlnlIGEIIEAILGAEQSR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 164 GE-SLLQRFTHNLTQQARDGKLDPVLCRDGAIRQMVDILARRRKNNPIVVGEAGVGKTAIVEGLASRIAAGEVPPALRDV 242
Cdd:CHL00095 157 SKtPTLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 243 ELLSLDMGLLQAGASVKGEFERRLKGVIDEVKAApRPTILFIDEAHTLIGAGGQAGGSDAANLLKPALARGELRTIAATT 322
Cdd:CHL00095 237 LVITLDIGLLLAGTKYRGEFEERLKRIFDEIQEN-NNIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 323 WAEYKKYFEKDPALARRFQPVQLHEPSVAEAVTILRGLARVYEESHGIYLRDDAVVAAAELSARYLAGRQLPDKAVDVLD 402
Cdd:CHL00095 316 LDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLD 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 403 TACARVRISLAAAPESLERLRGELaegerqrqalrrdaeaglpidhdalqaleeRLAQAESERHVQEDQWSRQRELAERL 482
Cdd:CHL00095 396 EAGSRVRLINSRLPPAARELDKEL------------------------------REILKDKDEAIREQDFETAKQLRDRE 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 483 LALRQQLARAREANREEqgseadaeafpadehggvealekalhetrqalaDAQAQGRLVsfeVCPRLVAEVIGAWTGVPV 562
Cdd:CHL00095 446 MEVRAQIAAIIQSKKTE---------------------------------EEKRLEVPV---VTEEDIAEIVSAWTGIPV 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 563 EQLAREHNAKVMGFADDLRTRIRGQEQAVSALDRAMRATAAGLNKPDAPVGVFLLVGPSGVGKTETALALADLLYGGERF 642
Cdd:CHL00095 490 NKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALASYFFGSEDA 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 643 ITTINMSEFQEKHTVSRLIGAPPGYVGYGEGGMLTEAVRQKPYSVILLDEVEKADPDVLNLFYQIFDKGVANDGEGREID 722
Cdd:CHL00095 570 MIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTID 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 723 FRNTLILMTSNLASEHIAALCQD-GARPSAELLEET--------IRPALSRHFKPALLARM-RVVPYYPVGGPVLRELIE 792
Cdd:CHL00095 650 FKNTLIIMTSNLGSKVIETNSGGlGFELSENQLSEKqykrlsnlVNEELKQFFRPEFLNRLdEIIVFRQLTKNDVWEIAE 729
|
730 740 750
....*....|....*....|....*....|....*....
gi 15596859 793 IKLQRLGERLARRQLAFDYSQALVGHLAERCTQSDSGAR 831
Cdd:CHL00095 730 IMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGAR 768
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
168-831 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 557.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 168 LQRFTHNLTQQARDGKLDPVLCRDGAIRQMVDILARRRKNNPIVVGEAGVGKTAIVEGLASRIAAGEVPPALRDVELLSL 247
Cdd:PRK10865 161 LKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLAL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 248 DMGLLQAGASVKGEFERRLKGVIDEVKAAPRPTILFIDEAHTLIGAGGQAGGSDAANLLKPALARGELRTIAATTWAEYK 327
Cdd:PRK10865 241 DMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYR 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 328 KYFEKDPALARRFQPVQLHEPSVAEAVTILRGLARVYEESHGIYLRDDAVVAAAELSARYLAGRQLPDKAVDVLDTACAR 407
Cdd:PRK10865 321 QYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASS 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 408 VRISLAAAPESLERLRGELAEGERQRQALRRDAEAGlpiDHDALQALEERLAQAESERHVQEDQWSRQRELAERLLALRQ 487
Cdd:PRK10865 401 IRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEA---SKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKA 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 488 QLARAREAnREEQGSEADAEAFPADEHGGVEALEKALHETRQALADAQaqgRLVSFEVCPRLVAEVIGAWTGVPVEQLAR 567
Cdd:PRK10865 478 ELEQAKIA-IEQARRVGDLARMSELQYGKIPELEKQLAAATQLEGKTM---RLLRNKVTDAEIAEVLARWTGIPVSRMLE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 568 EHNAKVMGFADDLRTRIRGQEQAVSALDRAMRATAAGLNKPDAPVGVFLLVGPSGVGKTETALALADLLYGGERFITTIN 647
Cdd:PRK10865 554 SEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRID 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 648 MSEFQEKHTVSRLIGAPPGYVGYGEGGMLTEAVRQKPYSVILLDEVEKADPDVLNLFYQIFDKGVANDGEGREIDFRNTL 727
Cdd:PRK10865 634 MSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTV 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 728 ILMTSNLASEHIAAlcQDGARPSAElLEETIRPALSRHFKPALLARM-RVVPYYPVGGPVLRELIEIKLQRLGERLARRQ 806
Cdd:PRK10865 714 VIMTSNLGSDLIQE--RFGELDYAH-MKELVLGVVSHNFRPEFINRIdEVVVFHPLGEQHIASIAQIQLQRLYKRLEERG 790
|
650 660
....*....|....*....|....*
gi 15596859 807 LAFDYSQALVGHLAERCTQSDSGAR 831
Cdd:PRK10865 791 YEIHISDEALKLLSENGYDPVYGAR 815
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
107-850 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 274241 [Multi-domain] Cd Length: 730 Bit Score: 541.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 107 GRSQIDQAALILALLRNPLRYAGsrY---QPLLARLDIERLKDFALSQPLEGAPSGKPGG-----GESLLQRFTHNLTQQ 178
Cdd:TIGR02639 97 GKKEIDIGDLLVALFDEEDSHAS--YflkSQGITRLDILNYISHGISKDDGKDQLGEEAGkeeekGQDALEKYTVDLTEK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 179 ARDGKLDPVLCRDGAIRQMVDILARRRKNNPIVVGEAGVGKTAIVEGLASRIAAGEVPPALRDVELLSLDMGLLQAGASV 258
Cdd:TIGR02639 175 AKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERLKNAKIYSLDMGTLLAGTKY 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 259 KGEFERRLKGVIDEVKAAPRPtILFIDEAHTLIGAGGQAGGS-DAANLLKPALARGELRTIAATTWAEYKKYFEKDPALA 337
Cdd:TIGR02639 255 RGDFEERLKAVVSEIEKEPNA-ILFIDEIHTIVGAGATSGGSmDASNLLKPALSSGKIRCIGSTTYEEYKNHFEKDRALS 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 338 RRFQPVQLHEPSVAEAVTILRGLARVYEESHGIYLRDDAVVAAAELSARYLAGRQLPDKAVDVLDTACARVRISLAAAPE 417
Cdd:TIGR02639 334 RRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDVIDEAGAAFRLRPKAKKK 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 418 SLERLRGelaegerqrqalrrdaeaglpidhdalqaleerlaqaeserhvqedqwsrqrelaerllalrqqlarareanr 497
Cdd:TIGR02639 414 ANVNVKD------------------------------------------------------------------------- 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 498 eeqgseadaeafpadehggvealekalhetrqaladaqaqgrlvsfevcprlVAEVIGAWTGVPVEQLAREHNAKVMGFA 577
Cdd:TIGR02639 421 ----------------------------------------------------IENVVAKMAKIPVKTVSSDDREQLKNLE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 578 DDLRTRIRGQEQAVSALDRAMRATAAGLNKPDAPVGVFLLVGPSGVGKTETALALADLLygG---ERFittiNMSEFQEK 654
Cdd:TIGR02639 449 KNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEEL--GvhlLRF----DMSEYMEK 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 655 HTVSRLIGAPPGYVGYGEGGMLTEAVRQKPYSVILLDEVEKADPDVLNLFYQIFDKGVANDGEGREIDFRNTLILMTSNL 734
Cdd:TIGR02639 523 HTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTSNA 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 735 asehiaalcqdGARPSA--------ELLEETIRPALSRHFKPALLARM-RVVPYYPVGGPVLRELIEIKLQRLGERLARR 805
Cdd:TIGR02639 603 -----------GASEMSkppigfggENRESKSLKAIKKLFSPEFRNRLdAIIHFNDLSEEMAEKIVKKFLDELQDQLNEK 671
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 15596859 806 QLAFDYSQALVGHLAERCTQSDSGARLIDHLLDTHLLPLVADRLL 850
Cdd:TIGR02639 672 NIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEIL 716
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
107-850 |
4.85e-127 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 399.98 E-value: 4.85e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 107 GRSQIDQAALILALLRNPLRYAGSryqpLLARLDIERL-------------KDFALSQPLEGAPSGKPGGGESLLQRFTH 173
Cdd:PRK11034 99 GRSEVTGANVLVAIFSEQESQAAY----LLRKHEVSRLdvvnfishgtrkdEPSQSSDPGSQPNSEEQAGGEERMENFTT 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 174 NLTQQARDGKLDPVLCRDGAIRQMVDILARRRKNNPIVVGEAGVGKTAIVEGLASRIAAGEVPPALRDVELLSLDMGLLQ 253
Cdd:PRK11034 175 NLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSLDIGSLL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 254 AGASVKGEFERRLKGVIDEVKAApRPTILFIDEAHTLIGAGGQAGGS-DAANLLKPALARGELRTIAATTWAEYKKYFEK 332
Cdd:PRK11034 255 AGTKYRGDFEKRFKALLKQLEQD-TNSILFIDEIHTIIGAGAASGGQvDAANLIKPLLSSGKIRVIGSTTYQEFSNIFEK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 333 DPALARRFQPVQLHEPSVAEAVTILRGLARVYEESHGIYLRDDAVVAAAELSARYLAGRQLPDKAVDVLDTACARVRIsl 412
Cdd:PRK11034 334 DRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGARARL-- 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 413 aaAPESLERLRGELAEGERQRQALRRDAEAGLPI-DHDALQALEERLaqaeserhvqedqwsrqrelaerllalrqqlar 491
Cdd:PRK11034 412 --MPVSKRKKTVNVADIESVVARIARIPEKSVSQsDRDTLKNLGDRL--------------------------------- 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 492 areanreeqgseadaeafpadehggvealekalhetrqaladaqaqgrlvsfevcprlvaevigawtgvpveqlarehna 571
Cdd:PRK11034 --------------------------------------------------------------------------------
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 572 KVMGFaddlrtrirGQEQAVSALDRAMRATAAGLNKPDAPVGVFLLVGPSGVGKTETALALADLLyGGE--RFittiNMS 649
Cdd:PRK11034 457 KMLVF---------GQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL-GIEllRF----DMS 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 650 EFQEKHTVSRLIGAPPGYVGYGEGGMLTEAVRQKPYSVILLDEVEKADPDVLNLFYQIFDKGVANDGEGREIDFRNTLIL 729
Cdd:PRK11034 523 EYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLV 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 730 MTSNlasehiaALCQDGARPSAELLEETIRP----ALSRHFKPALLARM-RVVPYYPVGGPVLRELIEIKLQRLGERLAR 804
Cdd:PRK11034 603 MTTN-------AGVRETERKSIGLIHQDNSTdameEIKKIFTPEFRNRLdNIIWFDHLSTDVIHQVVDKFIVELQAQLDQ 675
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 15596859 805 RQLAFDYSQALVGHLAERCTQSDSGARLIDHLLDTHLLPLVADRLL 850
Cdd:PRK11034 676 KGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELL 721
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
578-780 |
6.10e-82 |
|
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: 260.96 E-value: 6.10e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 578 DDLRTRIRGQEQAVSALDRAMRATAAGLNKPDAPVGVFLLVGPSGVGKTETALALADLLYGGERFITTINMSEFQEKHTV 657
Cdd:cd19499 7 ERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEYMEKHSV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 658 SRLIGAPPGYVGYGEGGMLTEAVRQKPYSVILLDEVEKADPDVLNLFYQIFDKGVANDGEGREIDFRNTLILMTSNlase 737
Cdd:cd19499 87 SRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTSN---- 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15596859 738 hiaalcqdgarpsaelleetirpalsrHFKPALLARMRVVPYY 780
Cdd:cd19499 163 ---------------------------HFRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
611-777 |
7.86e-79 |
|
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: 252.50 E-value: 7.86e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 611 PVGVFLLVGPSGVGKTETALALADLLYGGERFITTINMSEFQEKHTVSRLIGAPPGYVGYGEGGMLTEAVRQKPYSVILL 690
Cdd:pfam07724 2 PIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 691 DEVEKADPDVLNLFYQIFDKGVANDGEGREIDFRNTLILMTSNLASEHIAALCQDGARPSAELLEETIRPALSRHFKPAL 770
Cdd:pfam07724 82 DEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRLGDSPDYELLKEEVMDLLKKGFIPEF 161
|
....*..
gi 15596859 771 LARMRVV 777
Cdd:pfam07724 162 LGRLPII 168
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
349-452 |
1.63e-35 |
|
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: 129.91 E-value: 1.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 349 SVAEAVTILRGLARVYEESHGIYLRDDAVVAAAELSARYLAGRQLPDKAVDVLDTACARVRISLAAAPESLERLRGELAE 428
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|....
gi 15596859 429 GERQRQALRRDAEAGLPIDHDALQ 452
Cdd:pfam17871 81 LEIEKEALEREQDFEKAERLAKLE 104
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
190-341 |
1.69e-14 |
|
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: 71.79 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 190 RDGAIRQMVDILARRRKNNPIVVGEAGVGKTAIVEGLASRIaagevppALRDVELLSLDMGLLQAGASVKGEFERRLKGV 269
Cdd:cd00009 3 QEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANEL-------FRPGAPFLYLNASDLLEGLVVAELFGHFLVRL 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596859 270 IDEVKAAPRPTILFIDEAHTLiGAGGQAGGSDAANLLKPALA-RGELRTIAATTwaeYKKYFEKDPALARRFQ 341
Cdd:cd00009 76 LFELAEKAKPGVLFIDEIDSL-SRGAQNALLRVLETLNDLRIdRENVRVIGATN---RPLLGDLDRALYDRLD 144
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
586-739 |
3.72e-14 |
|
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: 70.64 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 586 GQEQAVSALDRAMRataaglNKPDAPVgvfLLVGPSGVGKTETALALADLLYGGERFITTINMSEFQEKHTVSRLIgapp 665
Cdd:cd00009 2 GQEEAIEALREALE------LPPPKNL---LLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELF---- 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596859 666 gyvGYGEGGMLTEAVRQKPYSVILLDEVEKADPDVLNLFYQIFDkgvanDGEGREIDFRNTLILMTSNLASEHI 739
Cdd:cd00009 69 ---GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLE-----TLNDLRIDRENVRVIGATNRPLLGD 134
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
613-742 |
1.23e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 63.55 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 613 GVFLLVGPSGVGKTETALALADLLYGGERFITTINMSEFQEKHTVSRLIGAPPGYVGYGEGGM----LTEAVRQKPYSVI 688
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPDVL 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15596859 689 LLDEVEKADPDVLNLFYQIFDKGVANDGEGREidfRNTLILMTSNLASEHIAAL 742
Cdd:smart00382 83 ILDEITSLLDAEQEALLLLLEELRLLLLLKSE---KNLTVILTTNDEKDLGPAL 133
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
786-868 |
2.62e-11 |
|
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: 60.54 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 786 VLRELIEIKLQRLGERLARRQLAFDYSQALVGHLAERCTQSDSGARLIDHLLDTHLLPLVADRLLEAMARDERLERVHAT 865
Cdd:smart01086 5 DLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVVVDVD 84
|
...
gi 15596859 866 LGE 868
Cdd:smart01086 85 DGE 87
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
210-341 |
3.95e-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: 58.37 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 210 IVVGEAGVGKTAIVEGLASRIaagevppalrDVELLSLDMGLLqaGASVKGEFERRLKGVIDEVKAaPRPTILFIDEAHT 289
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSEL--VSKYVGESEKRLRELFEAAKK-LAPCVIFIDEIDA 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596859 290 LIGAGGQAGGS---DAANLLKPALARGELRT-----IAATTwaeykkYFEK-DPALARRFQ 341
Cdd:pfam00004 69 LAGSRGSGGDSesrRVVNQLLTELDGFTSSNskvivIAATN------RPDKlDPALLGRFD 123
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
786-856 |
5.29e-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: 56.65 E-value: 5.29e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596859 786 VLRELIEIKLQRLGERLARRQLAFDYSQALVGHLAERCTQSDSGARLIDHLLDTHLLPLVADRLLEAMARD 856
Cdd:pfam10431 5 ELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKE 75
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
615-733 |
3.38e-09 |
|
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: 55.76 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 615 FLLVGPSGVGKTETALALADLLYGGERFitTINMSEFQekhTVSRLIGA--PPGYVGYGEGGMLTEAVRQKpySVILLDE 692
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRPVF--YVQLTRDT---TEEDLFGRrnIDPGGASWVDGPLVRAAREG--EIAVLDE 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 15596859 693 VEKADPDVLNLFYQIFDKGVANDGEGREID---FRNTLILMTSN 733
Cdd:pfam07728 75 INRANPDVLNSLLSLLDERRLLLPDGGELVkaaPDGFRLIATMN 118
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
352-537 |
7.24e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 7.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 352 EAVTILRGLARVYEESHGIYLRDDAVVAAAELSARYLAGRQLpdkavDVLDTACARVRISLAAAPESLERLRGELAEGER 431
Cdd:COG4913 249 EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRL-----ELLEAELEELRAELARLEAELERLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 432 QRQALRRDAEAglpIDHDALQALEERLAQAESERHVQEDQWSRQRELAERLLALRQQLARAREANREEqgseadAEAFPA 511
Cdd:COG4913 324 ELDELEAQIRG---NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE------AAALLE 394
|
170 180
....*....|....*....|....*.
gi 15596859 512 DEHGGVEALEKALHETRQALADAQAQ 537
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRE 420
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
616-742 |
4.28e-07 |
|
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: 49.90 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 616 LLVGPSGVGKTETALALADLLygGERFItTINMSEFQEKhtvsrligappgYVGYGEG---GMLTEAVRQKPySVILLDE 692
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKEL--GAPFI-EISGSELVSK------------YVGESEKrlrELFEAAKKLAP-CVIFIDE 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596859 693 VEK-----------ADPDVLNLFYQIFDkgvandgeGREIDFRNTLILMTSNLASEHIAAL 742
Cdd:pfam00004 66 IDAlagsrgsggdsESRRVVNQLLTELD--------GFTSSNSKVIVIAATNRPDKLDPAL 118
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
205-340 |
2.57e-06 |
|
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: 48.14 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 205 RKNNPIVVGEAGVGKTAIVEGLasriaAGEVPPALRDVELLSLDMGLLQAGASVK----------GEFERRLKGVIDEVK 274
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL-----ARELGPPGGGVIYIDGEDILEEVLDQLLliivggkkasGSGELRLRLALALAR 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596859 275 aAPRPTILFIDEAHTLIGAGGQAGGSDAA--NLLKPALARGELRTIAATTWAEykkyFEKDPALARRF 340
Cdd:smart00382 76 -KLKPDVLILDEITSLLDAEQEALLLLLEelRLLLLLKSEKNLTVILTTNDEK----DLGPALLRRRF 138
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
54-389 |
3.16e-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: 50.29 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 54 LLARALQDAAVDAGELNAALQARGEHSASRNPVFAPELVQWLQDALLLANLELGRSQIDQAALILALLRNPLRYAGSRYQ 133
Cdd:COG0464 26 LLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 134 PLLARLDIERLKDFALSQPLEGAPSGKPGGGESLLQRFTHNLTQQARDGKLDPVLCRDGAIRQMVDILARRRKNNP---- 209
Cdd:COG0464 106 LLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRPElree 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 210 ---------IVVGEAGVGKTAIVEGLASRIaagevppalrDVELLSLDMGLLQAGASvkGEFERRLKGVIDEVKAApRPT 280
Cdd:COG0464 186 yglppprglLLYGPPGTGKTLLARALAGEL----------GLPLIEVDLSDLVSKYV--GETEKNLREVFDKARGL-APC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 281 ILFIDEAHTLIGAGGQAGGSDA----ANLLKpALA--RGELRTIAATTWAEykkyfEKDPALARRFQ-PVQLHEPSVAEA 353
Cdd:COG0464 253 VLFIDEADALAGKRGEVGDGVGrrvvNTLLT-EMEelRSDVVVIAATNRPD-----LLDPALLRRFDeIIFFPLPDAEER 326
|
330 340 350
....*....|....*....|....*....|....*.
gi 15596859 354 VTILRGLARVYEESHGIYLrDDAVVAAAELSARYLA 389
Cdd:COG0464 327 LEIFRIHLRKRPLDEDVDL-EELAEATEGLSGADIR 361
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
588-696 |
1.68e-05 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 45.74 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 588 EQAVSALDRAMRATAAGLNKPdapVGVfLLVGPSGVGKTETALALADLLygGERFItTINMSEFQEKhtvsrligappgY 667
Cdd:cd19481 6 REAVEAPRRGSRLRRYGLGLP---KGI-LLYGPPGTGKTLLAKALAGEL--GLPLI-VVKLSSLLSK------------Y 66
|
90 100 110
....*....|....*....|....*....|.
gi 15596859 668 VGYGEGGM--LTEAVRQKPYSVILLDEVEKA 696
Cdd:cd19481 67 VGESEKNLrkIFERARRLAPCILFIDEIDAI 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
395-607 |
3.94e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 395 DKAVDVLDTACARVRISLAAAPESLERLRGE---LAEGERQRQALRRDAEAGLPIDHDALQALEERLAQAESERhvqEDQ 471
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEveqLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI---EEL 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 472 WSRQRELAERLLALRQQLARAREANREEQGSEADAEAFPADEHGGVEALEKALHETRQALADAQAQGRlvsfevcpRLVA 551
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE--------SLAA 859
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596859 552 EVIGAWTGVPVEQLAREHNAKVMGFA-----------DDLRTRIRGQEQAVSALDRAMRATAAGLNK 607
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLeealallrselEELSEELRELESKRSELRRELEELREKLAQ 926
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
372-537 |
5.71e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 372 LRDDAVVAAAELSARYLAGRQLPDKAvdvldTACARVRiSLAAAPESLERLRGELAEGERQRQALRRDaeaglpidHDAL 451
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERR-----EALQRLA-EYSWDEIDVASAEREIAELEAELERLDAS--------SDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 452 QALEERLAQAESERHVQEDQW----SRQRELAERLLALRQQLARAREANREEQGSEADAEAFPADEHGGVEALEKALHET 527
Cdd:COG4913 688 AALEEQLEELEAELEELEEELdelkGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170
....*....|
gi 15596859 528 RQALADAQAQ 537
Cdd:COG4913 768 RENLEERIDA 777
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
613-709 |
5.76e-05 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 43.48 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 613 GVFLLVGPSGVGKTETALALADLLYGGERFITTINMSEFQEK----HTVSRLIGAPPgyVGYGEGGMLTEAVRQ-----K 683
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPkdllRALLRALGLPL--SGRLSKEELLAALQQlllalA 83
|
90 100
....*....|....*....|....*.
gi 15596859 684 PYSVILLDEVEKADPDVLNLFYQIFD 709
Cdd:pfam13401 84 VAVVLIIDEAQHLSLEALEELRDLLN 109
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
406-695 |
7.63e-05 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 46.06 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 406 ARVRISLAAAPESLERLRGELAEGERQRQALRRDAEAGLPIDHDALQALEERLAQAESERHVQEDQWSRQRELAERLLAL 485
Cdd:COG0464 1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 486 RQQLARAREANREEQGSEADAEAFPADEHGGVEALEKALHETRQALADAQAQGRLVSFEVCPRLVAEVigawtgvpveQL 565
Cdd:COG0464 81 LLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEEL----------LE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 566 AREHNAKVMGFADDLRTRIRGQEQAVSALDRAMRAtaAGLnkpDAPVGVfLLVGPSGVGKTETALALADLLygGERFITT 645
Cdd:COG0464 151 LREAILDDLGGLEEVKEELRELVALPLKRPELREE--YGL---PPPRGL-LLYGPPGTGKTLLARALAGEL--GLPLIEV 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15596859 646 inmsefqekhTVSRLIGappGYVGYGEGGM--LTEAVRQKPYSVILLDEVEK 695
Cdd:COG0464 223 ----------DLSDLVS---KYVGETEKNLreVFDKARGLAPCVLFIDEADA 261
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
211-290 |
1.08e-04 |
|
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: 44.78 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 211 VVGEAGVGKTAIVEGLASRIAAGEVP-----PALRDVELLS---LDMGLLQAGASvKGEFERRLKGVIDEVKAAPRPTIL 282
Cdd:COG3267 48 LTGEVGTGKTTLLRRLLERLPDDVKVayipnPQLSPAELLRaiaDELGLEPKGAS-KADLLRQLQEFLLELAAAGRRVVL 126
|
....*...
gi 15596859 283 FIDEAHTL 290
Cdd:COG3267 127 IIDEAQNL 134
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
406-537 |
1.17e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 406 ARVRISLAAAPESLERLRGELAEGERQRQALRRDAEAGLpidhDALQALEERLAQAESERHVQEDQWSRQRELAERLLAL 485
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELE----EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15596859 486 RQQLARAREANREEQGSEADAEAFPADEHGGVEALEKALHETRQALADAQAQ 537
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
397-537 |
1.36e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 397 AVDVLDTACARVRISLAAAPESLERLRGELAEGERQRQALRRDAEAglpiDHDALQALEERLAQAESERHVQEDQWSRQR 476
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE----LELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596859 477 ELAERLLALRQQLARAREANREEQGSEADAEafpADEHGGVEALEKALHETRQALADAQAQ 537
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEEL---EELEEELEEAEEELEEAEAELAEAEEA 366
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
372-532 |
1.81e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 372 LRDDAVVAAAELSARYLAGRQLPDKAVDVLDTACARVRISLAAAPESLERLRGELAEGE--------------------R 431
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEggsaggsltggsrrellaalL 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 432 QRQALRRDAEAGLPIDHDALQALEERLAQAESERHVQEDQWSRQRELAERLL-ALRQQLARAREANREEQGSEADAEAFP 510
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEeQLEAEREELLEELLEEEELLEEEALEE 755
|
170 180
....*....|....*....|..
gi 15596859 511 ADEHGGVEALEKALHETRQALA 532
Cdd:COG1196 756 LPEPPDLEELERELERLEREIE 777
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
419-600 |
2.94e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 419 LERLRGELAEGERQRQALRRDAEAGlpidHDALQALEERLAQAeseRHVQEDQWSRQ--RELAERLLALRQQLARAREAN 496
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEAL----EAELDALQERREAL---QRLAEYSWDEIdvASAEREIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 497 R-----EEQGSEADAEAFPADEHGG-----VEALEKALHETRQALADAQAQGRLVSFEVCPRLVAEVIGAWTGVPVEQLA 566
Cdd:COG4913 685 DdlaalEEQLEELEAELEELEEELDelkgeIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180 190
....*....|....*....|....*....|....
gi 15596859 567 REHNAKvmgFADDLRTRIRGQEQAVSALDRAMRA 600
Cdd:COG4913 765 RELREN---LEERIDALRARLNRAEEELERAMRA 795
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
494-645 |
4.00e-04 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 43.70 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 494 EANREEQGSEADAEAFPADEHGGVEALEKALHETRQALADAQAQGRLVSFEVCPRLvAEVIgawtgvpvEQLARehnakv 573
Cdd:COG1419 53 EAEKAPAAAAAPAAASAAAEEEELEELRRELAELKELLEEQLSGLAGESARLPPEL-AELL--------ERLLE------ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 574 MGFADDLRTRIRGQEQAVSALDRAMRATAAGLNK----PDAPV----GVFLLVGPSGVGKTETA--LALADLLYGGER-- 641
Cdd:COG1419 118 AGVSPELARELLEKLPEDLSAEEAWRALLEALARrlpvAEDPLldegGVIALVGPTGVGKTTTIakLAARFVLRGKKKva 197
|
....
gi 15596859 642 FITT 645
Cdd:COG1419 198 LITT 201
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
373-537 |
7.54e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 373 RDDAVVAAAELSARYLAGRQlpdkAVDVLDTACARVRISLAAAPESLERLRGELA-EGERQRQALRRDAEAGLPIDHDA- 450
Cdd:COG1196 255 LEELEAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELARLEQDIArLEERRRELEERLEELEEELAELEe 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 451 -LQALEERLAQAESERHVQEDQWSRQRELAERLLALRQQLARAREANREEQGSEADAEAFPADEHGGVEALEKALHETRQ 529
Cdd:COG1196 331 eLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
....*...
gi 15596859 530 ALADAQAQ 537
Cdd:COG1196 411 ALLERLER 418
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
453-645 |
7.75e-04 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 42.32 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 453 ALEERLAQAESERHVQEDQWSRQRELAERLLALRQQLARAREANREEQGSEADAEAFPADEHGGVEALEKALHETRQALA 532
Cdd:TIGR03499 49 AIDEEEAAAASAEEEASKALEQADPKPLSATAEPLELPAPQEEPAAPAAQAAEPLLPEEELRKELEALRELLERLLAGLA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 533 DAQAQGRLVsfEVCPRLVAEvigawtGVPvEQLAREhnakVMGFADDLRTRIRGQEQAVSALDRAMRATAAGLNKPDAPv 612
Cdd:TIGR03499 129 WLQRPPERA--KLYERLLEA------GVS-EELARE----LLEKLPEDADAEDAWRWLREALEGMLPVKPEEDPILEQG- 194
|
170 180 190
....*....|....*....|....*....|....*....
gi 15596859 613 GVFLLVGPSGVGKTeTALA-LADLL---YGGER--FITT 645
Cdd:TIGR03499 195 GVIALVGPTGVGKT-TTLAkLAARFaleHGKKKvaLITT 232
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
401-607 |
1.02e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 401 LDTACARVRISLAAAPESLERLRGELAEGERQRQALRRDAEAglpidhDALQALEERLAQAESERHVQEDQwSRQRELAE 480
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE------LEEEEEEEEEALEEAAEEEAELE-EEEEALLE 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 481 RLLALRQQLARAREANREEQGSEADAeafpadehggvEALEKALHETRQALADAQAQGRLVSFEVCPRLVAEVIGAWTGV 560
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEA-----------AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15596859 561 PVEQLAREHNAKVMGFADDLRTRIRGQEQAVSAL--DRAMRATAAGLNK 607
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLkaAKAGRATFLPLDK 581
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
408-537 |
1.03e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 42.34 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 408 VRISLAAAPESLERLRGELAEGERQRQALRRDAEAglpidHDALQALEERLAQAESERHVQEDQWSRQRELAER------ 481
Cdd:COG1566 74 ARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGA-----EAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKgavsqq 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15596859 482 -LLALRQQLARAREANREEQGSEADAEAfPADEHGGVEALEKALHETRQALADAQAQ 537
Cdd:COG1566 149 eLDEARAALDAAQAQLEAAQAQLAQAQA-GLREEEELAAAQAQVAQAEAALAQAELN 204
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
385-537 |
1.11e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 385 ARYLAGRQLPDKAVDVLDTACARVRISLAAAPESLERLRGELAEGERQRQALRRdaeaglpidhdALQALEERLAQAESE 464
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES-----------RLEELEEQLETLRSK 387
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596859 465 RHVQEDQWSRQRELAERLLALRQQLARAREANREEQGSEADA--EAFPADEHGGVEALEKALHETRQALADAQAQ 537
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKleEAELKELQAELEELEEELEELQEELERLEEA 462
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
212-341 |
1.17e-03 |
|
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: 40.34 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 212 VGEAGVGKTAIVEGLASRIaagevppalrDVELLSLDMGLLQAGASvkGEFERRLKGVIDEVKAAPrPTILFIDEAHTLI 291
Cdd:cd19481 32 YGPPGTGKTLLAKALAGEL----------GLPLIVVKLSSLLSKYV--GESEKNLRKIFERARRLA-PCILFIDEIDAIG 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 292 GAGGQAGGSDAANLLKPAL--------ARGELRTIAATTWAEykkyfEKDPALAR--RFQ 341
Cdd:cd19481 99 RKRDSSGESGELRRVLNQLlteldgvnSRSKVLVIAATNRPD-----LLDPALLRpgRFD 153
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
409-544 |
1.50e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 409 RISLAAAPESLERLRGELAEGERQRQALRrdaeaglpidhDALQALEERLAQAESERHVQEDQWSRQRELAERLLALRQQ 488
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELR-----------KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15596859 489 LARAREANREEQGSEADAEAFPADEHGGVEALEKALHETRQALAD--AQAQGRLVSFE 544
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAqiEQLKEELKALR 802
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
212-443 |
1.87e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 41.02 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 212 VGEAGVGKTAIVEGLASRIaagevppalrDVELLSLDMGLLQAgaSVKGEFERRLKGVIDEvkAAPRPTILFIDEAHTlI 291
Cdd:COG1223 41 YGPPGTGKTMLAEALAGEL----------KLPLLTVRLDSLIG--SYLGETARNLRKLFDF--ARRAPCVIFFDEFDA-I 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 292 GA--GGQAGGSDAANLLKPALA-----RGELRTIAATTWAEykkyfEKDPALARRFQPV-QLHEPSVAEAVTILRGLARV 363
Cdd:COG1223 106 AKdrGDQNDVGEVKRVVNALLQeldglPSGSVVIAATNHPE-----LLDSALWRRFDEViEFPLPDKEERKEILELNLKK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 364 YEESHGIYLRddAVVAAAE-LSARYLagrqlpdkaVDVLDTAcarVRISLAAAPESLErlRGELAEGERQRQALRRDAEA 442
Cdd:COG1223 181 FPLPFELDLK--KLAKKLEgLSGADI---------EKVLKTA---LKKAILEDREKVT--KEDLEEALKQRKERKKEPKK 244
|
.
gi 15596859 443 G 443
Cdd:COG1223 245 E 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
357-499 |
2.37e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 357 LRGLARVYEESHGIYLRDDAVVAAAELSARYLAGRQLPDKAVDVLDTACARVRISLAAAP-ESLERLRGELAEGERQRQA 435
Cdd:COG4913 277 LRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEE 356
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596859 436 LRRDAE--------AGLPIDHDAlQALEERLAQAESERHVQEDQWSRQRELAERLLALRQQLARAREANREE 499
Cdd:COG4913 357 RERRRArleallaaLGLPLPASA-EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
419-537 |
4.12e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 419 LERLRGELAEGERQRQALRRdaeagLPIDHDALQALEERLAQAESERHVQeDQWSRQRELA---ERLLALRQQLARAREA 495
Cdd:COG4913 237 LERAHEALEDAREQIELLEP-----IRELAERYAAARERLAELEYLRAAL-RLWFAQRRLElleAELEELRAELARLEAE 310
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15596859 496 NREEQGSEADAEAFPAD------EHGG--VEALEKALHETRQALADAQAQ 537
Cdd:COG4913 311 LERLEARLDALREELDEleaqirGNGGdrLEQLEREIERLERELEERERR 360
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
412-537 |
4.27e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 412 LAAAPESLERLRGELAEGERQRQALRRDAE-------------------AGLPID--HDALQALEERLAQAESERHVQED 470
Cdd:COG1196 181 LEATEENLERLEDILGELERQLEPLERQAEkaeryrelkeelkeleaelLLLKLRelEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596859 471 QwsrQRELAERLLALRQQLARAREANREEQGSEADAEAFPADEHGGVEALEKALHETRQALADAQAQ 537
Cdd:COG1196 261 E---LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
412-537 |
5.35e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 412 LAAAPESLERLRGELAEGERQRQALRRDAEA-----GLPIDHDALQALEERLAQAESERHVQEDQWSRQRELAERLLALR 486
Cdd:COG4717 90 YAELQEELEELEEELEELEAELEELREELEKlekllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELE 169
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15596859 487 QQLARAREA-NREEQGSEADAEAFPADEHGGVEALEKALHETRQALADAQAQ 537
Cdd:COG4717 170 AELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
417-512 |
6.65e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 417 ESLERLRGELAEGERQRQALRrDAEAGLPIDHDALQALEERLAQA-ESERHVQEDQWSRQRELAERLLALRQQLARAREA 495
Cdd:PRK09039 81 DSVANLRASLSAAEAERSRLQ-ALLAELAGAGAAAEGRAGELAQElDSEKQVSARALAQVELLNQQIAALRRQLAALEAA 159
|
90
....*....|....*..
gi 15596859 496 NREEQGSEADAEAFPAD 512
Cdd:PRK09039 160 LDASEKRDRESQAKIAD 176
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
411-536 |
7.14e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 411 SLAAAPESLERLRGELAEGER---QRQALRRDAEA---GLPIDHDALQALEERLAQAESERHVQEDQwsrQRELAERLLA 484
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQrlrQQQNAERLLEEfcqRIGQQLDAAEELEELLAELEAQLEELEEQ---AAEAVEQRSE 582
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15596859 485 LRQQLARAReANREEQGSEADAeafpadEHGGVEALEKALHETRQALADAQA 536
Cdd:COG3096 583 LRQQLEQLR-ARIKELAARAPA------WLAAQDALERLREQSGEALADSQE 627
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
349-537 |
8.97e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.94 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 349 SVAEAVTILRGL----ARVYEESHGIYLRD-DAVVAAAELSARYLagrQLPDKAVDVLDTACArvriSLAAAPESLERLR 423
Cdd:COG3096 868 QLKEQLQLLNKLlpqaNLLADETLADRLEElREELDAAQEAQAFI---QQHGKALAQLEPLVA----VLQSDPEQFEQLQ 940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 424 GELAEGERQRQALRR------------------DAEAGLPIDHDALQALEERLAQAESERHVQEDQWSRQRELAERLLAL 485
Cdd:COG3096 941 ADYLQAKEQQRRLKQqifalsevvqrrphfsyeDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQV 1020
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596859 486 RQQLARAREANRE----------EQGSEADAEAfPADEHGGVEALEKALHETRQALADAQAQ 537
Cdd:COG3096 1021 LASLKSSRDAKQQtlqeleqeleELGVQADAEA-EERARIRRDELHEELSQNRSRRSQLEKQ 1081
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
379-537 |
9.10e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 379 AAAELSARYLAGRQlpdkAVDVLDTACARVRISLAAAPESLERLRGELAEGERQRQAL---RRDAEAGLPIDHDALQALE 455
Cdd:PRK02224 238 EADEVLEEHEERRE----ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELeeeRDDLLAEAGLDDADAEAVE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596859 456 ERLAQAESERHVQEDQWSRQR-----------ELAERLLALRQQLARAREANREEQGSEADAEAFPADEHGGVEALEKAL 524
Cdd:PRK02224 314 ARREELEDRDEELRDRLEECRvaaqahneeaeSLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
170
....*....|...
gi 15596859 525 HETRQALADAQAQ 537
Cdd:PRK02224 394 EELRERFGDAPVD 406
|
|
| |
