|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1-855 |
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: 1344.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 1 MNAERLTTKSREVITGAVAIASQRGHATVEPWHLLLSLLDTGGSTAGGLLRAVGANPVEVRRAAARAVENLPAARGSSvA 80
Cdd:COG0542 1 MNFEKFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGRLPKVSGSS-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 81 EPSLAREFANAIGAAEQIARPLGDEYTSTEHLLAGLARVG-GAVAQALKAAGATEENLVAAFPAVRGGdRRVTTADPEQT 159
Cdd:COG0542 80 QPYLSPRLKRVLELAELEARKLGDEYISTEHLLLALLREGeGVAARILKKLGITLEALREALEELRGG-SRVTSQNPESK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 160 YQALEKYGVDLTASARDGKIDPVIGRDSEIRRVIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVAGDVPESLRDKKL 239
Cdd:COG0542 159 TPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDKRV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 240 VSLDLGAMVAGAQYRGQFEERLKSVLEEIRGSDGQVITFLDELHTVVGAGKGEGSMDAGNMLKPMLARGELRMVGATTLD 319
Cdd:COG0542 239 LSLDLGALVAGAKYRGEFEERLKAVLDEVKKSEGNIILFIDELHTLVGAGGAEGAMDAANLLKPALARGELRCIGATTLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 320 EYRAHIEKDPALERRFQPVLVGEPTVEDTIGILRGLKERYEVHHGVRITDAALVAAASLSDRYITDRFLPDKAIDLVDES 399
Cdd:COG0542 319 EYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAIDLIDEA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 400 ASRLRMEIDSRPVEVDEIERAVRRLEIEEMALAKEPDVASAERLERLRKELADRREQLTALSDRWHLEKDHITRISTAKE 479
Cdd:COG0542 399 AARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 480 ELERlggeaeraerdgeleraaelRYGRIPTLQGELKRAETElvgLQADGAMLKEEVGADDIAAVVASWTGIPAGRLLEG 559
Cdd:COG0542 479 ELEQ--------------------RYGKIPELEKELAELEEE---LAELAPLLREEVTEEDIAEVVSRWTGIPVGKLLEG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 560 ETAKLLRMEESLGERVIGQREAVTAVSDAVRRARTGIADPDRPTGSFLFLGPTGVGKTELGKALAEFLFDDERAMVRIDM 639
Cdd:COG0542 536 EREKLLNLEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDM 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 640 SEYGEKHSVARLVGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEVEKAHPDVFDVLLQVLDDGRLTDGQGRTVDFRNAIL 719
Cdd:COG0542 616 SEYMEKHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTII 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 720 ILTSNLGSAMIADPT---LTEEQRREEVLAVVRTHFKPEFLNRLDDIVVFSSLTGDELRSIVDIQLTRMRRRLADRRLTL 796
Cdd:COG0542 696 IMTSNIGSELILDLAedePDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITL 775
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 2039925203 797 DVSDDARTWLADHGYDPIYGARPLRRLVQSAIGDRLAKALLAGAVRDGDTVRVDLAESK 855
Cdd:COG0542 776 ELTDAAKDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGE 834
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
6-851 |
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: 1298.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 6 LTTKSREVITGAVAIASQRGHATVEPWHLLLSLLDTGGSTAGGLLRAVGANPVEVRRAAARAVENLPAARGSsVAEPSLA 85
Cdd:TIGR03346 1 LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEKELERLPKVSGP-GGQVYLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 86 REFANAIGAAEQIARPLGDEYTSTEHLLAGLARVGGAVAQALKAAGATEENLVAAFPAVRGGdRRVTTADPEQTYQALEK 165
Cdd:TIGR03346 80 PDLNRLLNLAEKLAQKRGDEFISSEHLLLALLDDKGTLGKLLKEAGATADALEAAINAVRGG-QKVTDANAEDQYEALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 166 YGVDLTASARDGKIDPVIGRDSEIRRVIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVAGDVPESLRDKKLVSLDLG 245
Cdd:TIGR03346 159 YARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLALDMG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 246 AMVAGAQYRGQFEERLKSVLEEIRGSDGQVITFLDELHTVVGAGKGEGSMDAGNMLKPMLARGELRMVGATTLDEYRAHI 325
Cdd:TIGR03346 239 ALIAGAKYRGEFEERLKAVLNEVTKSEGQIILFIDELHTLVGAGKAEGAMDAGNMLKPALARGELHCIGATTLDEYRKYI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 326 EKDPALERRFQPVLVGEPTVEDTIGILRGLKERYEVHHGVRITDAALVAAASLSDRYITDRFLPDKAIDLVDESASRLRM 405
Cdd:TIGR03346 319 EKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAARIRM 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 406 EIDSRPVEVDEIERAVRRLEIEEMALAKEPDVASAERLERLRKELADRREQLTALSDRWHLEKDHITRISTAKEELERLG 485
Cdd:TIGR03346 399 EIDSKPEELDELDRRIIQLEIEREALKKEKDEASKKRLEDLEKELADLEEEYAELEEQWKAEKASIQGIQQIKEEIEQVR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 486 GEAERAERDGELERAAELRYGRIPTLQGELKRAETELVglQADGAMLKEEVGADDIAAVVASWTGIPAGRLLEGETAKLL 565
Cdd:TIGR03346 479 LELEQAEREGDLAKAAELQYGKLPELEKQLQAAEQKLG--EEQNRLLREEVTAEEIAEVVSRWTGIPVSKMLEGEREKLL 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 566 RMEESLGERVIGQREAVTAVSDAVRRARTGIADPDRPTGSFLFLGPTGVGKTELGKALAEFLFDDERAMVRIDMSEYGEK 645
Cdd:TIGR03346 557 HMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRIDMSEYMEK 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 646 HSVARLVGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEVEKAHPDVFDVLLQVLDDGRLTDGQGRTVDFRNAILILTSNL 725
Cdd:TIGR03346 637 HSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMTSNL 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 726 GSAMIADPTLTE--EQRREEVLAVVRTHFKPEFLNRLDDIVVFSSLTGDELRSIVDIQLTRMRRRLADRRLTLDVSDDAR 803
Cdd:TIGR03346 717 GSDFIQELAGGDdyEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKITLELSDAAL 796
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 2039925203 804 TWLADHGYDPIYGARPLRRLVQSAIGDRLAKALLAGAVRDGDTVRVDL 851
Cdd:TIGR03346 797 DFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDV 844
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
1-851 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 945.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 1 MNAERLTTKSREVITGAVAIASQRGHATVEPWHLLLSLLDTGGSTAGGLLRAVGANPVEVRRAAARAVENLPAARGSSvA 80
Cdd:PRK10865 1 MRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVRPLLTSAGINAGQLRTDINQALSRLPQVEGTG-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 81 EPSLAREFANAIGAAEQIARPLGDEYTSTEHLLAGLARVGGAVAQALKAAGATEENLVAAFPAVRGGDRrVTTADPEQTY 160
Cdd:PRK10865 80 DVQPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAALESRGTLADILKAAGATTANITQAIEQMRGGES-VNDQGAEDQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 161 QALEKYGVDLTASARDGKIDPVIGRDSEIRRVIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVAGDVPESLRDKKLV 240
Cdd:PRK10865 159 QALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 241 SLDLGAMVAGAQYRGQFEERLKSVLEEIRGSDGQVITFLDELHTVVGAGKGEGSMDAGNMLKPMLARGELRMVGATTLDE 320
Cdd:PRK10865 239 ALDMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 321 YRAHIEKDPALERRFQPVLVGEPTVEDTIGILRGLKERYEVHHGVRITDAALVAAASLSDRYITDRFLPDKAIDLVDESA 400
Cdd:PRK10865 319 YRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 401 SRLRMEIDSRPVEVDEIERAVRRLEIEEMALAKEPDVASAERLERLRKELADRREQLTALSDRWHLEKDHITRISTAKEE 480
Cdd:PRK10865 399 SSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 481 LERLGGEAERAERDGELERAAELRYGRIPTLQGELKRAEtelvglQADGA---MLKEEVGADDIAAVVASWTGIPAGRLL 557
Cdd:PRK10865 479 LEQAKIAIEQARRVGDLARMSELQYGKIPELEKQLAAAT------QLEGKtmrLLRNKVTDAEIAEVLARWTGIPVSRML 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 558 EGETAKLLRMEESLGERVIGQREAVTAVSDAVRRARTGIADPDRPTGSFLFLGPTGVGKTELGKALAEFLFDDERAMVRI 637
Cdd:PRK10865 553 ESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRI 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 638 DMSEYGEKHSVARLVGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEVEKAHPDVFDVLLQVLDDGRLTDGQGRTVDFRNA 717
Cdd:PRK10865 633 DMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNT 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 718 ILILTSNLGSAMIADP--TLTEEQRREEVLAVVRTHFKPEFLNRLDDIVVFSSLTGDELRSIVDIQLTRMRRRLADRRLT 795
Cdd:PRK10865 713 VVIMTSNLGSDLIQERfgELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYE 792
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 2039925203 796 LDVSDDARTWLADHGYDPIYGARPLRRLVQSAIGDRLAKALLAGAVRDGDTVRVDL 851
Cdd:PRK10865 793 IHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEV 848
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
4-856 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 832.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 4 ERLTTKSREVITGAVAIASQRGHATVEPWHLLLSLLDTGGSTAGGLLRAVGANPVEVRRAAAR---------AVENLPAA 74
Cdd:CHL00095 3 ERFTEKAIKVIMLSQEEARRLGHNFVGTEQILLGLIGEGTGIAARALKSMGVTLKDARIEVEKiigrgtgfvAVEIPFTP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 75 RGSSVAEPSLarefanaigaaeQIARPLGDEYTSTEHLLAGLarvggaVAQALKAAGATEENLVAAFPAVRG------GD 148
Cdd:CHL00095 83 RAKRVLEMSL------------EEARDLGHNYIGTEHLLLAL------LEEGEGVAARVLENLGVDLSKIRSlilnliGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 149 RRVTTADPEQTYQ---ALEKYGVDLTASARDGKIDPVIGRDSEIRRVIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRI 225
Cdd:CHL00095 145 IIEAILGAEQSRSktpTLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 226 VAGDVPESLRDKKLVSLDLGAMVAGAQYRGQFEERLKSVLEEIRgSDGQVITFLDELHTVVGAGKGEGSMDAGNMLKPML 305
Cdd:CHL00095 225 VNRDVPDILEDKLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQ-ENNNIILVIDEVHTLIGAGAAEGAIDAANILKPAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 306 ARGELRMVGATTLDEYRAHIEKDPALERRFQPVLVGEPTVEDTIGILRGLKERYEVHHGVRITDAALVAAASLSDRYITD 385
Cdd:CHL00095 304 ARGELQCIGATTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIAD 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 386 RFLPDKAIDLVDESASRLRMEIDSRPvevdeieRAVRRLEIEEMALAKEPDVASAERLERLRKELADRREQLTAlsdrwh 465
Cdd:CHL00095 384 RFLPDKAIDLLDEAGSRVRLINSRLP-------PAARELDKELREILKDKDEAIREQDFETAKQLRDREMEVRA------ 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 466 lekdHITRISTAKEelerlggeaeraerdgeleraaelrygRIPTLQGELKRaetelvglqadgamlkeeVGADDIAAVV 545
Cdd:CHL00095 451 ----QIAAIIQSKK---------------------------TEEEKRLEVPV------------------VTEEDIAEIV 481
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 546 ASWTGIPAGRLLEGETAKLLRMEESLGERVIGQREAVTAVSDAVRRARTGIADPDRPTGSFLFLGPTGVGKTELGKALAE 625
Cdd:CHL00095 482 SAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALAS 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 626 FLFDDERAMVRIDMSEYGEKHSVARLVGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEVEKAHPDVFDVLLQVLDDGRLT 705
Cdd:CHL00095 562 YFFGSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLT 641
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 706 DGQGRTVDFRNAILILTSNLGSAMIADPT------LTEEQRREE--------VLAVVRTHFKPEFLNRLDDIVVFSSLTG 771
Cdd:CHL00095 642 DSKGRTIDFKNTLIIMTSNLGSKVIETNSgglgfeLSENQLSEKqykrlsnlVNEELKQFFRPEFLNRLDEIIVFRQLTK 721
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 772 DELRSIVDIQLTRMRRRLADRRLTLDVSDDARTWLADHGYDPIYGARPLRRLVQSAIGDRLAKALLAGAVRDGDTVRVDL 851
Cdd:CHL00095 722 NDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVDV 801
|
....*
gi 2039925203 852 AESKD 856
Cdd:CHL00095 802 NDEKE 806
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
6-782 |
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: 727.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 6 LTTKSREVITGAVAIASQRGHATVEPWHLLLSLLDTGGSTAGGLLRAVGANPVEVRRAAARAVENLPaaRGSSvAEPSLA 85
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLARALDKLP--RGNT-RTPVFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 86 REFANAIGAAEQIAR-PLGDEYTSTEHLL------AGLARVGGAVAQALKAAGAteENLVAAFPAVRGGDR--RVTTADP 156
Cdd:TIGR03345 78 PHLVELLQEAWLLASlELGDGRIRSGHLLlalltdPELRRLLGSISPELAKIDR--EALREALPALVEGSAeaSAAAADA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 157 EQTYQ--------ALEKYGVDLTASARDGKIDPVIGRDSEIRRVIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVAG 228
Cdd:TIGR03345 156 APAGAaagaagtsALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 229 DVPESLRDKKLVSLDLGAMVAGAQYRGQFEERLKSVLEEIRGSDGQVITFLDELHTVVGAGKGEGSMDAGNMLKPMLARG 308
Cdd:TIGR03345 236 DVPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPIILFIDEAHTLIGAGGQAGQGDAANLLKPALARG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 309 ELRMVGATTLDEYRAHIEKDPALERRFQPVLVGEPTVEDTIGILRGLKERYEVHHGVRITDAALVAAASLSDRYITDRFL 388
Cdd:TIGR03345 316 ELRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 389 PDKAIDLVDESASRLRMEIDSRPVEVDEIERAVRRLEIEEMALAKEPDV--ASAERLERLRKELADRREQLTALSDRWHL 466
Cdd:TIGR03345 396 PDKAVSLLDTACARVALSQNATPAALEDLRRRIAALELELDALEREAALgaDHDERLAELRAELAALEAELAALEARWQQ 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 467 EKDHITRISTAKEELErlggEAERAERDGELERAAELRygriptlqgelkRAETELVGLQADGAMLKEEVGADDIAAVVA 546
Cdd:TIGR03345 476 EKELVEAILALRAELE----ADADAPADDDDALRAQLA------------ELEAALASAQGEEPLVFPEVDAQAVAEVVA 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 547 SWTGIPAGRLLEGETAKLLRMEESLGERVIGQREAVTAVSDAVRRARTGIADPDRPTGSFLFLGPTGVGKTELGKALAEF 626
Cdd:TIGR03345 540 DWTGIPVGRMVRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAEL 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 627 LFDDERAMVRIDMSEYGEKHSVARLVGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEVEKAHPDVFDVLLQVLDDGRLTD 706
Cdd:TIGR03345 620 LYGGEQNLITINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMED 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 707 GQGRTVDFRNAILILTSNLGSAMIADPTLTEEQRR--EEVLAVVR----THFKPEFLNRLdDIVVFSSLTGDELRSIVDI 780
Cdd:TIGR03345 700 GEGREIDFKNTVILLTSNAGSDLIMALCADPETAPdpEALLEALRpellKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRL 778
|
..
gi 2039925203 781 QL 782
Cdd:TIGR03345 779 KL 780
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
11-851 |
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: 695.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 11 REVITGAVAIASQRGHATVEPWHLLLSLLDTggSTAGGLLRAVGANPVEVRRAAARAVE-NLPAARGSSVAEPSLAREFA 89
Cdd:TIGR02639 6 ERILSDALEEAKERRHEFVTLEHLLLALLDD--NEAIEILEECGGDVELLRKRLEDYLEeNLPVIPEDIDEEPEQTVGVQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 90 NAIGAAEQIARPLGDEYTSTEHLLAGLARVGGAVAQ-ALKAAGATEENLVA----AFPAVRGGDRRVTTADPEQTYQ--A 162
Cdd:TIGR02639 84 RVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASyFLKSQGITRLDILNyishGISKDDGKDQLGEEAGKEEEKGqdA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 163 LEKYGVDLTASARDGKIDPVIGRDSEIRRVIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVAGDVPESLRDKKLVSL 242
Cdd:TIGR02639 164 LEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERLKNAKIYSL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 243 DLGAMVAGAQYRGQFEERLKSVLEEIRGSDGQvITFLDELHTVVGAGK-GEGSMDAGNMLKPMLARGELRMVGATTLDEY 321
Cdd:TIGR02639 244 DMGTLLAGTKYRGDFEERLKAVVSEIEKEPNA-ILFIDEIHTIVGAGAtSGGSMDASNLLKPALSSGKIRCIGSTTYEEY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 322 RAHIEKDPALERRFQPVLVGEPTVEDTIGILRGLKERYEVHHGVRITDAALVAAASLSDRYITDRFLPDKAIDLVDESAS 401
Cdd:TIGR02639 323 KNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDVIDEAGA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 402 RLRMEIDSRPvevdeieravrrleieemalakepdvasaerlerlrkeladrreqltalsdrwhlekdhitristakeel 481
Cdd:TIGR02639 403 AFRLRPKAKK---------------------------------------------------------------------- 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 482 erlggeaeraerdgeleraaelrygriptlqgelkraetelvglqadgamlKEEVGADDIAAVVASWTGIPAGRLLEGET 561
Cdd:TIGR02639 413 ---------------------------------------------------KANVNVKDIENVVAKMAKIPVKTVSSDDR 441
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 562 AKLLRMEESLGERVIGQREAVTAVSDAVRRARTGIADPDRPTGSFLFLGPTGVGKTELGKALAEFLfddERAMVRIDMSE 641
Cdd:TIGR02639 442 EQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEEL---GVHLLRFDMSE 518
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 642 YGEKHSVARLVGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEVEKAHPDVFDVLLQVLDDGRLTDGQGRTVDFRNAILIL 721
Cdd:TIGR02639 519 YMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIM 598
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 722 TSNLGSAMIADPTL--TEEQRREEVLAVVRTHFKPEFLNRLDDIVVFSSLTGDELRSIVDIQLTRMRRRLADRRLTLDVS 799
Cdd:TIGR02639 599 TSNAGASEMSKPPIgfGGENRESKSLKAIKKLFSPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIELELT 678
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 2039925203 800 DDARTWLADHGYDPIYGARPLRRLVQSAIGDRLAKALLAGAVRDGDTVRVDL 851
Cdd:TIGR02639 679 DDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEILFGKLKKGGSVKISL 730
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
14-861 |
1.69e-170 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 512.85 E-value: 1.69e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 14 ITGAVAIASQRGHA--TVEpwHLLLSLLDTggSTAGGLLRAVGANPVEVRRAAARAVEN----LPAARGSSVAEPSLA-- 85
Cdd:PRK11034 10 LNMAFARAREHRHEfmTVE--HLLLALLSN--PSAREALEACSVDLVALRQELEAFIEQttpvLPASEEERDTQPTLSfq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 86 REFANAIGAAEQIARplgDEYTSTEHLLAGLARVGGAVAQALKAAGATEENLVA----AFPAVRGGDRRVTTADPEQTYQ 161
Cdd:PRK11034 86 RVLQRAVFHVQSSGR---SEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNfishGTRKDEPSQSSDPGSQPNSEEQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 162 A-----LEKYGVDLTASARDGKIDPVIGRDSEIRRVIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVAGDVPESLRD 236
Cdd:PRK11034 163 AggeerMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 237 KKLVSLDLGAMVAGAQYRGQFEERLKSVLEEIRgSDGQVITFLDELHTVVGAGKGE-GSMDAGNMLKPMLARGELRMVGA 315
Cdd:PRK11034 243 CTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLE-QDTNSILFIDEIHTIIGAGAASgGQVDAANLIKPLLSSGKIRVIGS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 316 TTLDEYRAHIEKDPALERRFQPVLVGEPTVEDTIGILRGLKERYEVHHGVRITDAALVAAASLSDRYITDRFLPDKAIDL 395
Cdd:PRK11034 322 TTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 396 VDESASRLRmeidsrpvevdeieravrrleieemalakepdvasaerlerlrkeladrreqLTALSDRwhlekdhitris 475
Cdd:PRK11034 402 IDEAGARAR----------------------------------------------------LMPVSKR------------ 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 476 takeelerlggeaeraerdgeleraaelrygriptlqgelkraetelvglqadgamlKEEVGADDIAAVVASWTGIPAGR 555
Cdd:PRK11034 418 ---------------------------------------------------------KKTVNVADIESVVARIARIPEKS 440
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 556 LLEGETAKLLRMEESLGERVIGQREAVTAVSDAVRRARTGIADPDRPTGSFLFLGPTGVGKTELGKALAEFLfddERAMV 635
Cdd:PRK11034 441 VSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL---GIELL 517
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 636 RIDMSEYGEKHSVARLVGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEVEKAHPDVFDVLLQVLDDGRLTDGQGRTVDFR 715
Cdd:PRK11034 518 RFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFR 597
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 716 NAILILTSNLGSAMIADPT--LTEEQRREEVLAVVRTHFKPEFLNRLDDIVVFSSLTGDELRSIVDIQLTRMRRRLADRR 793
Cdd:PRK11034 598 NVVLVMTTNAGVRETERKSigLIHQDNSTDAMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKG 677
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2039925203 794 LTLDVSDDARTWLADHGYDPIYGARPLRRLVQSAIGDRLAKALLAGAVRDGDTVRVDLAESKDGLTVE 861
Cdd:PRK11034 678 VSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKEKNELTYG 745
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
563-766 |
2.11e-104 |
|
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: 319.89 E-value: 2.11e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 563 KLLRMEESLGERVIGQREAVTAVSDAVRRARTGIADPDRPTGSFLFLGPTGVGKTELGKALAEFLFDDERAMVRIDMSEY 642
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 643 GEKHSVARLVGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEVEKAHPDVFDVLLQVLDDGRLTDGQGRTVDFRNAILILT 722
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2039925203 723 SNlgsamiadptlteeqrreevlavvrtHFKPEFLNRLDDIVVF 766
Cdd:cd19499 161 SN--------------------------HFRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
601-763 |
9.80e-91 |
|
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: 283.70 E-value: 9.80e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 601 RPTGSFLFLGPTGVGKTELGKALAEFLFDDERAMVRIDMSEYGEKHSVARLVGAPPGYVGYEEGGQLTEAVRRRPYSVVL 680
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 681 LDEVEKAHPDVFDVLLQVLDDGRLTDGQGRTVDFRNAILILTSNLGSAMIAD-----PTLTEEQRREEVLAVVRTHFKPE 755
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDasrlgDSPDYELLKEEVMDLLKKGFIPE 160
|
....*...
gi 2039925203 756 FLNRLDDI 763
Cdd:pfam07724 161 FLGRLPII 168
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
344-447 |
4.43e-37 |
|
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: 134.54 E-value: 4.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 344 TVEDTIGILRGLKERYEVHHGVRITDAALVAAASLSDRYITDRFLPDKAIDLVDESASRLRMEIDSRPVEVDEIERAVRR 423
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|....
gi 2039925203 424 LEIEEMALAKEPDVASAERLERLR 447
Cdd:pfam17871 81 LEIEKEALEREQDFEKAERLAKLE 104
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
769-849 |
2.36e-21 |
|
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: 88.62 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 769 LTGDELRSIVDIQLTRMRRRLADRRLTLDVSDDARTWLADHGYDPIYGARPLRRLVQSAIGDRLAKALLAGAVRDGDTVR 848
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 2039925203 849 V 849
Cdd:pfam10431 81 V 81
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
769-855 |
1.43e-18 |
|
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: 80.95 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 769 LTGDELRSIVDIQLTRMRRRLADRRLTLDVSDDARTWLADHGYDPIYGARPLRRLVQSAIGDRLAKALLAGAVRDGDTVR 848
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
....*..
gi 2039925203 849 VDLAESK 855
Cdd:smart01086 81 VDVDDGE 87
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
576-735 |
1.26e-17 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 80.65 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 576 IGQREAVTAVSDAVRRartgiadpdRPTGSFLFLGPTGVGKTELGKALAEFLFDDERAMVRIDMSEYGEKHSVARLvgap 655
Cdd:cd00009 1 VGQEEAIEALREALEL---------PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAEL---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 656 pgyVGYEEGGQLTEAVRRRPYSVVLLDEVEKAHPDVFDVLLQVLDDGRLTdgqgrTVDFRNAILILTSNLGSAMIADPTL 735
Cdd:cd00009 68 ---FGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATNRPLLGDLDRAL 139
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
183-343 |
3.04e-16 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 76.80 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 183 IGRDSEIRRVIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVagdvpesLRDKKLVSLDLGAMVAGAQYRGQFEERLK 262
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELF-------RPGAPFLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 263 SVLEEIRGSDGQVITFLDELHTvVGAGKGEGSMDAGNMLKPMLA-RGELRMVGATTLDEYrahIEKDPALERRFQPVLVG 341
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDS-LSRGAQNALLRVLETLNDLRIdRENVRVIGATNRPLL---GDLDRALYDRLDIRIVI 149
|
..
gi 2039925203 342 EP 343
Cdd:cd00009 150 PL 151
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
607-727 |
3.58e-12 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 64.70 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 607 LFLGPTGVGKTELGKALAEFLFDDERAMVRIDMSEYGEKHSVARLVGAPPGYVGYEEGGQ----LTEAVRRRPYSVVLLD 682
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2039925203 683 EVEKAHPDVFDVLLQVLDDGRLTDGQGRtvdFRNAILILTSNLGS 727
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTNDEK 127
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
605-724 |
1.73e-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: 62.31 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 605 SFLFLGPTGVGKTELGKALAEFLFDDERAMVRI--DMSEygekhsvARLVGA--PPGYVGYEEGGQLTEAVRRRpySVVL 680
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLtrDTTE-------EDLFGRrnIDPGGASWVDGPLVRAAREG--EIAV 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2039925203 681 LDEVEKAHPDVFDVLLQVLDDGRLTDGQGRT---VDFRNAILILTSN 724
Cdd:pfam07728 72 LDEINRANPDVLNSLLSLLDERRLLLPDGGElvkAAPDGFRLIATMN 118
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
588-747 |
4.02e-10 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 59.22 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 588 AVRRARTGIADPDRPTGSFLFLGPTGVGKTELGKALAEFLfddERAMVRIDMSEYGEKHSvarlvgappgYVGYEEGGQL 667
Cdd:cd19481 11 APRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGEL---GLPLIVVKLSSLLSKYV----------GESEKNLRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 668 TEAVRRRPYSVVLLDEVEKAHPD------------VFDVLLQVLDDGRLTDgqgrtvdfrNAILILTSNLGSAMiaDPTL 735
Cdd:cd19481 78 FERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAATNRPDLL--DPAL 146
|
170
....*....|..
gi 2039925203 736 TEEQRREEVLAV 747
Cdd:cd19481 147 LRPGRFDEVIEF 158
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
206-339 |
1.23e-08 |
|
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: 54.14 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 206 LIGEPGVGKTAIVEGLAQRIvagdvpeslrDKKLVSLDLGAMVagAQYRGQFEERLKSVLEEIRGSDGQVItFLDELHTV 285
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELV--SKYVGESEKRLRELFEAAKKLAPCVI-FIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2039925203 286 VGA---GKGEGSMDAGNMLKPML-----ARGELRMVGATTldeyraHIEK-DPALERRFQPVL 339
Cdd:pfam00004 70 AGSrgsGGDSESRRVVNQLLTELdgftsSNSKVIVIAATN------RPDKlDPALLGRFDRII 126
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
95-146 |
1.13e-07 |
|
Clp amino terminal domain, pathogenicity island component; This short domain is found in one or two copies at the amino terminus of ClpA and ClpB proteins from bacteria and eukaryotes. The function of these domains is uncertain but they may form a protein binding site. In many bacterial species, including E.coli, this region represents the N-terminus of one of the key components of the pathogenicity island complex that injects toxin from one bacterium into another.
Pssm-ID: 460724 [Multi-domain] Cd Length: 53 Bit Score: 49.06 E-value: 1.13e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2039925203 95 AEQIARPLGDEYTSTEHLLAGLARVG-GAVAQALKAAGATEENLVAAFPAVRG 146
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDdGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
410-782 |
1.02e-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: 51.84 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 410 RPVEVDEIERAVRRLEIEEMALAKEPDVASAERLERLRKELADRREQLTALSDRWHLEKDHITRISTAKEELERLGGEAE 489
Cdd:COG0464 10 ALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 490 RAERDGELERAAELRYGRIPTLQGELKRAETELVGLQADGAMLKEEVGADDIAAVVASwtgipAGRLLEGETAKLLRMEE 569
Cdd:COG0464 90 ELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEE-----LLELREAILDDLGGLEE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 570 sLGERVigqREAVTAVSDAVR-RARTGIadpdRPTGSFLFLGPTGVGKTELGKALAEFLfddERAMVRIDMSEygekhsv 648
Cdd:COG0464 165 -VKEEL---RELVALPLKRPElREEYGL----PPPRGLLLYGPPGTGKTLLARALAGEL---GLPLIEVDLSD------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 649 arLVGappGYVGYEEGG--QLTEAVRRRPYSVVLLDEVEKAHPD-----------VFDVLLQVLDDGRltdgqgrtvdfR 715
Cdd:COG0464 227 --LVS---KYVGETEKNlrEVFDKARGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR-----------S 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2039925203 716 NAILILTSNLGSAMiaDptlteeqrreevlavvrthfkPEFLNRLDDIVVFSSLTGDELRSIVDIQL 782
Cdd:COG0464 291 DVVVIAATNRPDLL--D---------------------PALLRRFDEIIFFPLPDAEERLEIFRIHL 334
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
27-367 |
1.53e-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: 51.45 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 27 ATVEPWHLLLSLLDTGGSTAGGLLRAVGANPVEVRRAAARAVENLPAARGSSVAEPSLAREFANAIGAAEQIARPLGDEY 106
Cdd:COG0464 5 LALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 107 TSTEHLLAGLARVGGAVAQALKAAGATEENLVAAFPAVRGGDRRVTTADPEQTYQALEKyGVDLTASARDGKIDPVIGRD 186
Cdd:COG0464 85 LLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGG-LEEELLELREAILDDLGGLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 187 S---EIRRVIQVLSRRTKNNP----------VLIGEPGVGKTAIVEGLAQRIvagdvpeslrDKKLVSLDLGAMVagAQY 253
Cdd:COG0464 164 EvkeELRELVALPLKRPELREeyglppprglLLYGPPGTGKTLLARALAGEL----------GLPLIEVDLSDLV--SKY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 254 RGQFEERLKSVLEEIRGSDGQVItFLDELHTVVGAGKGEGSMDAGNMLKPMLA-----RGELRMVGATTldeyraHIEK- 327
Cdd:COG0464 232 VGETEKNLREVFDKARGLAPCVL-FIDEADALAGKRGEVGDGVGRRVVNTLLTemeelRSDVVVIAATN------RPDLl 304
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2039925203 328 DPALERRFQPVL-VGEPTVEDTIGILRGLKERYEVHHGVRI 367
Cdd:COG0464 305 DPALLRRFDEIIfFPLPDAEERLEIFRIHLRKRPLDEDVDL 345
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
17-63 |
1.72e-06 |
|
Clp amino terminal domain, pathogenicity island component; This short domain is found in one or two copies at the amino terminus of ClpA and ClpB proteins from bacteria and eukaryotes. The function of these domains is uncertain but they may form a protein binding site. In many bacterial species, including E.coli, this region represents the N-terminus of one of the key components of the pathogenicity island complex that injects toxin from one bacterium into another.
Pssm-ID: 460724 [Multi-domain] Cd Length: 53 Bit Score: 45.59 E-value: 1.72e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2039925203 17 AVAIASQRGHATVEPWHLLLSLLDTGGSTAGGLLRAVGANPVEVRRA 63
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREA 47
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
607-700 |
1.49e-05 |
|
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410908 [Multi-domain] Cd Length: 182 Bit Score: 46.40 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 607 LFLGPTGVGKTELGKALAEFLfddERAMVRIDMseyGEKHSVARLVGAPPGYVGyEEGGQLTEAVRR----RPysVVLLD 682
Cdd:cd19500 41 CLVGPPGVGKTSLGKSIARAL---GRKFVRISL---GGVRDEAEIRGHRRTYVG-AMPGRIIQALKKagtnNP--VFLLD 111
|
90 100
....*....|....*....|..
gi 2039925203 683 EVEK----AHPDVFDVLLQVLD 700
Cdd:cd19500 112 EIDKigssFRGDPASALLEVLD 133
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
607-724 |
8.37e-05 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 42.97 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 607 LFLGPTGVGKTELGKALAEFLFddeRAMVRIDMSEYGEKHsvarlVGAPPGYVgyeegGQLTEAVRRRPYSVVLLDEVEK 686
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELG---APFIEISGSELVSKY-----VGESEKRL-----RELFEAAKKLAPCVIFIDEIDA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2039925203 687 AHP-----------DVFDVLLQVLDdgrltdgqGRTVDFRNAILILTSN 724
Cdd:pfam00004 69 LAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
12-598 |
1.10e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 46.02 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 12 EVITGAVAIASQRGHATVEPWHLLLSLLDTGGSTAGGLLRAVG---ANPVEVRRAAAravenLPAARGSSVAEPSLA--R 86
Cdd:COG3321 796 EVGPGPVLTGLVRQCLAAAGDAVVLPSLRRGEDELAQLLTALAqlwVAGVPVDWSAL-----YPGRGRRRVPLPTYPfqR 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 87 EFANAIGAAEQIARPLGDEYTSTEHLLAGLARVGGAVAQALKAAGATEENLVAAFPAVRGGDRRVTTADPEQTYQALEKY 166
Cdd:COG3321 871 EDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAA 950
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 167 GVDLTASARDGkIDPVIGRDSEIRRVIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVAGDVPESLRDKKLVSLDLGA 246
Cdd:COG3321 951 AAAAALAAAEA-GALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLA 1029
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 247 MVAGAQYRGQFEERLKSVLEEIRGSDGQVITFLDELHTVVGAGKGEGSMDAGNMLKPMLARGELRMVGATTLDEYRAHIE 326
Cdd:COG3321 1030 AAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLL 1109
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 327 KDPALERRF-QPVLVGEPTVEDTIGILRGLKERYEVHHGVRITDAALVAAASLSDRYITDRFLPDKAIDLVDESASRLRM 405
Cdd:COG3321 1110 ALLAALALAaAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAAL 1189
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 406 EIDSRPVEVDEIERAVRRLEIEEMALAKEPDVASAERLERLRKELADRREQLTALSDRWHLEKDHITRISTAKEELERLG 485
Cdd:COG3321 1190 AGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAA 1269
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 486 GEAERAERDGELERAAELRYGRIPTLQGELKRAETELVGLQADGAMLKEEVGADDIAAVVASWTGIPAGRLLEGETAKLL 565
Cdd:COG3321 1270 GLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAA 1349
|
570 580 590
....*....|....*....|....*....|...
gi 2039925203 566 RMEESLGERVIGQREAVTAVSDAVRRARTGIAD 598
Cdd:COG3321 1350 AAAAAAAAAAAAALAAAAGAAAAAAALALAALA 1382
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
409-540 |
1.22e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 409 SRPVEVDEIERAVRRLEIEEMALAKEpdvasaerLERLRKELADRREQLTALSDRWHlekDHITRISTAKEELERLGGEA 488
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKA--------LAELRKELEELEEELEQLRKELE---ELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 489 ERAER-----DGELERAAELRYG---RIPTLQGELKRAETELVGLQADGAMLKEEVGADD 540
Cdd:TIGR02168 743 EQLEEriaqlSKELTELEAEIEEleeRLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
413-536 |
1.62e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 413 EVDEIERAVRRLEIEEMALAKEPDVASA-ERLERLRKELADRREQLTALSDRWHLEKDHITRISTAKEELERLGGEAERA 491
Cdd:COG4717 103 ELEELEAELEELREELEKLEKLLQLLPLyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEEL 182
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2039925203 492 ERDGELERAAELRY--GRIPTLQGELKRAETELVGLQADGAMLKEEV 536
Cdd:COG4717 183 LEQLSLATEEELQDlaEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
200-340 |
1.64e-04 |
|
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: 42.75 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 200 TKNNPVLIGEPGVGKTAIVEGLAQ-------RIVAGDVPESLRDKKLVSLDLGAMVAGAQYRGqfEERLKSVLEEIRGSD 272
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARelgppggGVIYIDGEDILEEVLDQLLLIIVGGKKASGSG--ELRLRLALALARKLK 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 273 GQVItFLDELHTVVGAG--KGEGSMDAGNMLKPMLARGELRMVGATTLDEyrahIEKDPALERRFQPVLV 340
Cdd:smart00382 79 PDVL-ILDEITSLLDAEqeALLLLLEELRLLLLLKSEKNLTVILTTNDEK----DLGPALLRRRFDRRIV 143
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
600-727 |
2.31e-04 |
|
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required for, along with delta' subunit, the assembly of the processivity factor beta(2) onto primed DNA in the DNA polymerase III holoenzyme-catalyzed reaction. The delta subunit is also known as HolA.
Pssm-ID: 433013 [Multi-domain] Cd Length: 161 Bit Score: 42.58 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 600 DRPTGSFLFLGPTGVGKTELGKALAEFLFDDEramvRIDMSEYGEKHSVARLV-GAPPGYVGYEEGGQ---------LTE 669
Cdd:pfam13177 16 GRLSHAYLFSGPEGVGKLELALAFAKALFCEE----PGDDLPCGQCRSCRRIEsGNHPDLVIIEPEGQsikidqireLQK 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2039925203 670 AVRRRPY----SVVLLDEVEKAHPDVFDVLLQVLDdgrltDGQGRTVdfrnaILILTSNLGS 727
Cdd:pfam13177 92 EFSKSPYegkkKVYIIEDAEKMTASAANSLLKFLE-----EPPGNTV-----IILLTENPSR 143
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
601-703 |
2.88e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 41.56 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 601 RPTGSFLFL-GPTGVGKTELGKALAEFLFDDERAMVRIDMSEYGEK----HSVARLVGAPPGYVGYEEG--GQLTEAVRR 673
Cdd:pfam13401 2 RFGAGILVLtGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPkdllRALLRALGLPLSGRLSKEEllAALQQLLLA 81
|
90 100 110
....*....|....*....|....*....|.
gi 2039925203 674 RP-YSVVLLDEVEKAHPDVFDVLLQVLDDGR 703
Cdd:pfam13401 82 LAvAVVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
413-525 |
6.27e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 413 EVDEIERAVRRLEIEEMALA------KEPDVASAERLERLRKELADRREQLTALSDRWHLEKDHIT-RISTAK------- 478
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLShlhfgyKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNgELSAADaavakdr 321
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2039925203 479 EELERLGGEAERAERDGELERAAELRygRIPTLQGELKRAETELVGL 525
Cdd:pfam12128 322 SELEALEDQHGAFLDADIETAAADQE--QLPSWQSELENLEERLKAL 366
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
404-594 |
8.19e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 404 RMEIDSRPVEVDEIERAVRRLEIEEMALAKEPDVASA--ERLERLRKELADRREQLTALSDRWHLEKDH----------- 470
Cdd:COG4913 595 RRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEErlEALEAELDALQERREALQRLAEYSWDEIDVasaereiaele 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 471 --ITRISTAKEELERLGGEAERAERDG-ELERAAELRYGRIPTLQGELKRAETELVGLQAdgamlkEEVGADDIAAVVAS 547
Cdd:COG4913 675 aeLERLDASSDDLAALEEQLEELEAELeELEEELDELKGEIGRLEKELEQAEEELDELQD------RLEAAEDLARLELR 748
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2039925203 548 WTGIPAgRLLEGETAKLLRMEESLGERVIGQREAVTAVSDAVRRART 594
Cdd:COG4913 749 ALLEER-FAAALGDAVERELRENLEERIDALRARLNRAEEELERAMR 794
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
205-335 |
8.85e-04 |
|
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: 40.35 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 205 VLIGEPGVGKTAIVEGLAQRIVAGDVPESLRDKKLVSLDLgamVAGAQYRGQFEERLKSVL-EEIRGSDgqvITFLDELH 283
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSNRPVFYVQLTRDTTEEDL---FGRRNIDPGGASWVDGPLvRAAREGE---IAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2039925203 284 T----VVGAGKG---EGSMDAGNMLKPMLARGELRMVGATTLDEYRAHIEKDPALERRF 335
Cdd:pfam07728 77 RanpdVLNSLLSlldERRLLLPDGGELVKAAPDGFRLIATMNPLDRGLNELSPALRSRF 135
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
569-686 |
1.21e-03 |
|
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410906 [Multi-domain] Cd Length: 183 Bit Score: 40.83 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 569 ESLGERVIGQREAVTAVSDAVR------RARTGIADPDRPTgSFLFLGPTGVGKTELGKALAEFLfddERAMVRIDMSEY 642
Cdd:cd19498 7 SELDKYIIGQDEAKRAVAIALRnrwrrmQLPEELRDEVTPK-NILMIGPTGVGKTEIARRLAKLA---GAPFIKVEATKF 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2039925203 643 GEKhsvarlvgappGYVGYEeggqLTEAVRRRPYSVVLLDEVEK 686
Cdd:cd19498 83 TEV-----------GYVGRD----VESIIRDLVEGIVFIDEIDK 111
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
390-528 |
1.34e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 390 DKAIDLVDESASRLRM--EIDSRPVEVDEIERAVRRLEIEEMALAKEPDVASA---------ERLERLRKELADRREQLT 458
Cdd:COG4913 637 EAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDASSDDLAAleeqleeleAELEELEEELDELKGEIG 716
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2039925203 459 ALSDRWHLEKDHITRISTAKEELERLGGEAERAERDGELERA------AELR---YGRIPTLQGELKRAETELVGLQAD 528
Cdd:COG4913 717 RLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAlgdaveRELRenlEERIDALRARLNRAEEELERAMRA 795
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
396-536 |
2.00e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 396 VDESASRLRMEIDSRPVEVDEIERAVRRLEiEEMALAKepdvasaERLERLRKELADRREQLTALSDRwhLEKD--HITR 473
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALE-ARLEAAK-------TELEDLEKEIKRLELEIEEVEAR--IKKYeeQLGN 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2039925203 474 ISTAKeELERLGGEAERAERD-GELERAAELRYGRIPTLQGELKRAETELVGLQADGAMLKEEV 536
Cdd:COG1579 85 VRNNK-EYEALQKEIESLKRRiSDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
187-353 |
2.65e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 40.25 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 187 SEIRRVIQVLSRR---------TKNNPVLIGEPGVGKTAIVEGLAQRIvagDVPeslrdkkLVSLDLGAMVAgaQYRGQF 257
Cdd:COG1223 12 KKLKLIIKELRRRenlrkfglwPPRKILFYGPPGTGKTMLAEALAGEL---KLP-------LLTVRLDSLIG--SYLGET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 258 EERLKSVLEEIRGSDGqvITFLDELHTVvgaGKGEGSMDAgnmlkpmlaRGEL-RMVGA--TTLDEYRAHI--------- 325
Cdd:COG1223 80 ARNLRKLFDFARRAPC--VIFFDEFDAI---AKDRGDQND---------VGEVkRVVNAllQELDGLPSGSvviaatnhp 145
|
170 180 190
....*....|....*....|....*....|
gi 2039925203 326 -EKDPALERRFQPVL-VGEPTVEDTIGILR 353
Cdd:COG1223 146 eLLDSALWRRFDEVIeFPLPDKEERKEILE 175
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
569-627 |
3.15e-03 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410905 [Multi-domain] Cd Length: 251 Bit Score: 40.28 E-value: 3.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2039925203 569 ESLGERVIGQREAVTAVSDAV----RRARTGIADPDRPT----GSFLFLGPTGVGKTELGKALAEFL 627
Cdd:cd19497 8 EHLDKYVIGQERAKKVLSVAVynhyKRIRNNLKQKDDDVelekSNILLIGPTGSGKTLLAQTLAKIL 74
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
573-628 |
3.63e-03 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 40.56 E-value: 3.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2039925203 573 ERVIGQREAVTAVSDAVRRartgiadpDRPTGSFLFLGPTGVGKTELGKALAEFLF 628
Cdd:COG2812 10 DDVVGQEHVVRTLKNALAS--------GRLAHAYLFTGPRGVGKTTLARILAKALN 57
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
181-230 |
4.49e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 39.02 E-value: 4.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2039925203 181 PVIGRDSEIRRVIQVLSRRTKNNP---VLIGEPGVGKTAIVEGLAQRIVAGDV 230
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERDGG 53
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
391-527 |
8.68e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039925203 391 KAIDLVDESASRLRMEIDSRPVEVDEIERAVRRLEIEEMALAKEPDVASAERLERLRKELADRREQLTALSDRWHLEKDH 470
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEAL 367
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2039925203 471 ITRI----STAKEELERLGGEAE--RAERDGELERAAELRY---GRIPTLQGELKRAETELVGLQA 527
Cdd:COG4913 368 LAALglplPASAEEFAALRAEAAalLEALEEELEALEEALAeaeAALRDLRRELRELEAEIASLER 433
|
|
| |
