|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1-858 |
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: 1397.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 1 MNIEKMTTTLQEAIAEAQQIAVTRKHQDIDIAHVWKIFL-QPNHFGRNFYTDAGLDVESFEHEIDRLLDEYPVVSGGNVQ 79
Cdd:COG0542 1 MNFEKFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLeQGEGLAAKLLRKLGVDLDALREELEEALGRLPKVSGSSGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 80 ygQNLSQNFFRLLNEADQIRESFGDEFLSTEVVILALMKLKNYPLTVYLNKNGLSEKELRKNIEEMRGGERVTSQNQEEQ 159
Cdd:COG0542 81 --PYLSPRLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITLEALREALEELRGGSRVTSQNPESK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 160 YKALEKYGVDLVQQVKSGKMDPIIGRDEEIRDVIRILSRKTKNNPVLIGEPGVGKTAIVEGLAQRIVRKDVPENLKDKTI 239
Cdd:COG0542 159 TPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDKRV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 240 FSLDMGALIAGAKFRGEFEERLKAVLKEVKKSDGRILLFIDEIHNIVGAGKTEGSMDAGNLLKPMLARGELHLIGATTLD 319
Cdd:COG0542 239 LSLDLGALVAGAKYRGEFEERLKAVLDEVKKSEGNIILFIDELHTLVGAGGAEGAMDAANLLKPALARGELRCIGATTLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 320 EYRQYMEKDKALERRFQKVLVKEPTVEDTISILRGLKERFEIHHGVNIHDNALVAAATLSDRYITDRFLPDKAIDLIDEA 399
Cdd:COG0542 319 EYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAIDLIDEA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 400 SATIRVEMNSMPTELDQVTRRLMQLEIEEAALKKESDDASKKRLKNLQEELAELREEANAMKMQWETEKEEVNSVSAKRA 479
Cdd:COG0542 399 AARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 480 EIDKakheledaennydleraavlRHGTIPQLEKELKELEAKAKDSEiKMVQESVTENEIAQVVGRLTGIPVTKLVEGER 559
Cdd:COG0542 479 ELEQ--------------------RYGKIPELEKELAELEEELAELA-PLLREEVTEEDIAEVVSRWTGIPVGKLLEGER 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 560 EKLIKLNETLHKRVIGQDEAVDAVSDAVIRSRAGLQDPNRPLGSFLFLGPTGVGKTELAKALAENLFDSEDHMVRIDMSE 639
Cdd:COG0542 538 EKLLNLEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSE 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 640 YMEKHAVSRLVGAPPGYVGYEEGGQLTEAVRRNPYTIVLLDEIEKAHPDVFNILLQVLDDGRLTDSKGRVVDFKNTVLIM 719
Cdd:COG0542 618 YMEKHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIM 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 720 TSNIGSQLLLEGvTADGTIPEAVAEQVNTLLRGNFKPEFLNRIDDTILFTPLSLDNVKGIVDKMVAQLAQRLEHQEILLT 799
Cdd:COG0542 698 TSNIGSELILDL-AEDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLE 776
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 488230346 800 ISDEAKTWIAENAYEPAYGARPLKRFITKEVETPLAKEIVAGHVMPKSKVTITLLDGQL 858
Cdd:COG0542 777 LTDAAKDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGEL 835
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
6-858 |
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: 1344.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 6 MTTTLQEAIAEAQQIAVTRKHQDIDIAHVWKIFL-QPNHFGRNFYTDAGLDVESFEHEIDRLLDEYPVVSG--GNVQYGQ 82
Cdd:TIGR03346 1 LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLdQEGGLARPLLQKAGVNVGALRQALEKELERLPKVSGpgGQVYLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 83 NLSqnffRLLNEADQIRESFGDEFLSTEVVILALMKLKNyPLTVYLNKNGLSEKELRKNIEEMRGGERVTSQNQEEQYKA 162
Cdd:TIGR03346 81 DLN----RLLNLAEKLAQKRGDEFISSEHLLLALLDDKG-TLGKLLKEAGATADALEAAINAVRGGQKVTDANAEDQYEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 163 LEKYGVDLVQQVKSGKMDPIIGRDEEIRDVIRILSRKTKNNPVLIGEPGVGKTAIVEGLAQRIVRKDVPENLKDKTIFSL 242
Cdd:TIGR03346 156 LEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 243 DMGALIAGAKFRGEFEERLKAVLKEVKKSDGRILLFIDEIHNIVGAGKTEGSMDAGNLLKPMLARGELHLIGATTLDEYR 322
Cdd:TIGR03346 236 DMGALIAGAKYRGEFEERLKAVLNEVTKSEGQIILFIDELHTLVGAGKAEGAMDAGNMLKPALARGELHCIGATTLDEYR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 323 QYMEKDKALERRFQKVLVKEPTVEDTISILRGLKERFEIHHGVNIHDNALVAAATLSDRYITDRFLPDKAIDLIDEASAT 402
Cdd:TIGR03346 316 KYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAAR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 403 IRVEMNSMPTELDQVTRRLMQLEIEEAALKKESDDASKKRLKNLQEELAELREEANAMKMQWETEKEEVNSVSAKRAEID 482
Cdd:TIGR03346 396 IRMEIDSKPEELDELDRRIIQLEIEREALKKEKDEASKKRLEDLEKELADLEEEYAELEEQWKAEKASIQGIQQIKEEIE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 483 KAKHELEDAENNYDLERAAVLRHGTIPQLEKELKELEAKAKDSEIKMVQESVTENEIAQVVGRLTGIPVTKLVEGEREKL 562
Cdd:TIGR03346 476 QVRLELEQAEREGDLAKAAELQYGKLPELEKQLQAAEQKLGEEQNRLLREEVTAEEIAEVVSRWTGIPVSKMLEGEREKL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 563 IKLNETLHKRVIGQDEAVDAVSDAVIRSRAGLQDPNRPLGSFLFLGPTGVGKTELAKALAENLFDSEDHMVRIDMSEYME 642
Cdd:TIGR03346 556 LHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRIDMSEYME 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 643 KHAVSRLVGAPPGYVGYEEGGQLTEAVRRNPYTIVLLDEIEKAHPDVFNILLQVLDDGRLTDSKGRVVDFKNTVLIMTSN 722
Cdd:TIGR03346 636 KHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMTSN 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 723 IGSQLLLEGvtADGTIPEAVAEQVNTLLRGNFKPEFLNRIDDTILFTPLSLDNVKGIVDKMVAQLAQRLEHQEILLTISD 802
Cdd:TIGR03346 716 LGSDFIQEL--AGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKITLELSD 793
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 488230346 803 EAKTWIAENAYEPAYGARPLKRFITKEVETPLAKEIVAGHVMPKSKVTITLLDGQL 858
Cdd:TIGR03346 794 AALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGRL 849
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
1-858 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 1005.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 1 MNIEKMTTTLQEAIAEAQQIAVTRKHQDIDIAHVWKIFL-QPNHFGRNFYTDAGLDVESFEHEIDRLLDEYPVV--SGGN 77
Cdd:PRK10865 1 MRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLnQEGGSVRPLLTSAGINAGQLRTDINQALSRLPQVegTGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 78 VQygqnLSQNFFRLLNEADQIRESFGDEFLSTEVVILALMKLKNyPLTVYLNKNGLSEKELRKNIEEMRGGERVTSQNQE 157
Cdd:PRK10865 81 VQ----PSQDLVRVLNLCDKLAQKRGDNFISSELFVLAALESRG-TLADILKAAGATTANITQAIEQMRGGESVNDQGAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 158 EQYKALEKYGVDLVQQVKSGKMDPIIGRDEEIRDVIRILSRKTKNNPVLIGEPGVGKTAIVEGLAQRIVRKDVPENLKDK 237
Cdd:PRK10865 156 DQRQALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 238 TIFSLDMGALIAGAKFRGEFEERLKAVLKEVKKSDGRILLFIDEIHNIVGAGKTEGSMDAGNLLKPMLARGELHLIGATT 317
Cdd:PRK10865 236 RVLALDMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 318 LDEYRQYMEKDKALERRFQKVLVKEPTVEDTISILRGLKERFEIHHGVNIHDNALVAAATLSDRYITDRFLPDKAIDLID 397
Cdd:PRK10865 316 LDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLID 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 398 EASATIRVEMNSMPTELDQVTRRLMQLEIEEAALKKESDDASKKRLKNLQEELAELREEANAMKMQWETEKEEVNSVSAK 477
Cdd:PRK10865 396 EAASSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 478 RAEIDKAKHELEDAENNYDLERAAVLRHGTIPQLEKELkELEAKAKDSEIKMVQESVTENEIAQVVGRLTGIPVTKLVEG 557
Cdd:PRK10865 476 KAELEQAKIAIEQARRVGDLARMSELQYGKIPELEKQL-AAATQLEGKTMRLLRNKVTDAEIAEVLARWTGIPVSRMLES 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 558 EREKLIKLNETLHKRVIGQDEAVDAVSDAVIRSRAGLQDPNRPLGSFLFLGPTGVGKTELAKALAENLFDSEDHMVRIDM 637
Cdd:PRK10865 555 EREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDM 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 638 SEYMEKHAVSRLVGAPPGYVGYEEGGQLTEAVRRNPYTIVLLDEIEKAHPDVFNILLQVLDDGRLTDSKGRVVDFKNTVL 717
Cdd:PRK10865 635 SEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVV 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 718 IMTSNIGSQLLLE--GVTADGTIPEAVAEQVntllRGNFKPEFLNRIDDTILFTPLSLDNVKGIVDKMVAQLAQRLEHQE 795
Cdd:PRK10865 715 IMTSNLGSDLIQErfGELDYAHMKELVLGVV----SHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERG 790
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488230346 796 ILLTISDEAKTWIAENAYEPAYGARPLKRFITKEVETPLAKEIVAGHVMPKSKVTITLLDGQL 858
Cdd:PRK10865 791 YEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDDRI 853
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
102-852 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 808.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 102 FGDEFLSTEVVILALMKLKNYPLTVYLNKNGLSEKELRKNIEEMRGG---ERVTSQNQEEQYKALEKYGVDLVQQVKSGK 178
Cdd:CHL00095 98 LGHNYIGTEHLLLALLEEGEGVAARVLENLGVDLSKIRSLILNLIGEiieAILGAEQSRSKTPTLEEFGTNLTKEAIDGN 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 179 MDPIIGRDEEIRDVIRILSRKTKNNPVLIGEPGVGKTAIVEGLAQRIVRKDVPENLKDKTIFSLDMGALIAGAKFRGEFE 258
Cdd:CHL00095 178 LDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDKLVITLDIGLLLAGTKYRGEFE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 259 ERLKAVLKEVKKSDgRILLFIDEIHNIVGAGKTEGSMDAGNLLKPMLARGELHLIGATTLDEYRQYMEKDKALERRFQKV 338
Cdd:CHL00095 258 ERLKRIFDEIQENN-NIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLDEYRKHIEKDPALERRFQPV 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 339 LVKEPTVEDTISILRGLKERFEIHHGVNIHDNALVAAATLSDRYITDRFLPDKAIDLIDEASATIRVEMNSMPteldqvt 418
Cdd:CHL00095 337 YVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLDEAGSRVRLINSRLP------- 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 419 rrlmqleieeaalkkesdDASKKRLKNLQeelaelreeanamkmqwetekeevnsvsakraEIDKAKhelEDAENNYDLE 498
Cdd:CHL00095 410 ------------------PAARELDKELR--------------------------------EILKDK---DEAIREQDFE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 499 RAAVLRHGTIPQLEKELKELEAKAKDSEIKMVQESVTENEIAQVVGRLTGIPVTKLVEGEREKLIKLNETLHKRVIGQDE 578
Cdd:CHL00095 437 TAKQLRDREMEVRAQIAAIIQSKKTEEEKRLEVPVVTEEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDE 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 579 AVDAVSDAVIRSRAGLQDPNRPLGSFLFLGPTGVGKTELAKALAENLFDSEDHMVRIDMSEYMEKHAVSRLVGAPPGYVG 658
Cdd:CHL00095 517 AVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALASYFFGSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVG 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 659 YEEGGQLTEAVRRNPYTIVLLDEIEKAHPDVFNILLQVLDDGRLTDSKGRVVDFKNTVLIMTSNIGS----------QLL 728
Cdd:CHL00095 597 YNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSkvietnsgglGFE 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 729 LEGVTADGTIPEAVAEQVNTLLRGNFKPEFLNRIDDTILFTPLSLDNVKGIVDKMVAQLAQRLEHQEILLTISDEAKTWI 808
Cdd:CHL00095 677 LSENQLSEKQYKRLSNLVNEELKQFFRPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLL 756
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 488230346 809 AENAYEPAYGARPLKRFITKEVETPLAKEIVAGHVMPKSKVTIT 852
Cdd:CHL00095 757 IEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVD 800
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
9-838 |
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: 757.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 9 TLQEAIAEAQQIAVTRKHQDIDIAHVW-KIFLQPNHFGRNFYTDAGLDVESFEHEIDRLLDEYPVVSGGNVqygqNLSQN 87
Cdd:TIGR03345 4 TSRRALEQAAALCVARGHPEVELEHWLlALLDQPDSDLAAILRHFGVDLGRLKADLARALDKLPRGNTRTP----VFSPH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 88 FFRLLNEADQIRES-FGDEFLSTEVVILALMK---LKNYPLTVYLNKNGLSEKELRKNIEEMRGGE-----------RVT 152
Cdd:TIGR03345 80 LVELLQEAWLLASLeLGDGRIRSGHLLLALLTdpeLRRLLGSISPELAKIDREALREALPALVEGSaeasaaaadaaPAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 153 SQNQEEQYKALEKYGVDLVQQVKSGKMDPIIGRDEEIRDVIRILSRKTKNNPVLIGEPGVGKTAIVEGLAQRIVRKDVPE 232
Cdd:TIGR03345 160 AAAGAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVPP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 233 NLKDKTIFSLDMGALIAGAKFRGEFEERLKAVLKEVKKSDGRILLFIDEIHNIVGAGKTEGSMDAGNLLKPMLARGELHL 312
Cdd:TIGR03345 240 ALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPIILFIDEAHTLIGAGGQAGQGDAANLLKPALARGELRT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 313 IGATTLDEYRQYMEKDKALERRFQKVLVKEPTVEDTISILRGLKERFEIHHGVNIHDNALVAAATLSDRYITDRFLPDKA 392
Cdd:TIGR03345 320 IAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLPDKA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 393 IDLIDEASATIRVEMNSMPTELDQVTRRLMQLEIEEAALKKES--DDASKKRLKNLQEELAELREEANAMKMQWETEKEE 470
Cdd:TIGR03345 400 VSLLDTACARVALSQNATPAALEDLRRRIAALELELDALEREAalGADHDERLAELRAELAALEAELAALEARWQQEKEL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 471 VNSVSAKRAEIDkakhELEDAENNYDLERAAVLRhgtipQLEKELKELEAkakdsEIKMVQESVTENEIAQVVGRLTGIP 550
Cdd:TIGR03345 480 VEAILALRAELE----ADADAPADDDDALRAQLA-----ELEAALASAQG-----EEPLVFPEVDAQAVAEVVADWTGIP 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 551 VTKLVEGEREKLIKLNETLHKRVIGQDEAVDAVSDAVIRSRAGLQDPNRPLGSFLFLGPTGVGKTELAKALAENLFDSED 630
Cdd:TIGR03345 546 VGRMVRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGEQ 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 631 HMVRIDMSEYMEKHAVSRLVGAPPGYVGYEEGGQLTEAVRRNPYTIVLLDEIEKAHPDVFNILLQVLDDGRLTDSKGRVV 710
Cdd:TIGR03345 626 NLITINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREI 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 711 DFKNTVLIMTSNIGSQlLLEGVTADGTI---PEAVAEQVNTLLRGNFKPEFLNRIdDTILFTPLSLDNVKGIVDKMVAQL 787
Cdd:TIGR03345 706 DFKNTVILLTSNAGSD-LIMALCADPETapdPEALLEALRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRI 783
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 488230346 788 AQRL-EHQEILLTISDEAKTWIAENAYEPAYGARPLKRFITKEVETPLAKEI 838
Cdd:TIGR03345 784 ARRLkENHGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQI 835
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
6-853 |
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: 724.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 6 MTTTLQEAIAEAQQIAVTRKHQDIDIAHVWKIFLQPNHfGRNFYTDAGLDVESFEHEIDRLLDEYPVVSGGNVQYGQNLS 85
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNE-AIEILEECGGDVELLRKRLEDYLEENLPVIPEDIDEEPEQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 86 QNFFRLLNEADQIRESFGDEFLSTEVVILALMKLKNYPLTVYLNKNGLS-------------EKELRKNIEEMRGGErvt 152
Cdd:TIGR02639 80 VGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITrldilnyishgisKDDGKDQLGEEAGKE--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 153 sqnQEEQYKALEKYGVDLVQQVKSGKMDPIIGRDEEIRDVIRILSRKTKNNPVLIGEPGVGKTAIVEGLAQRIVRKDVPE 232
Cdd:TIGR02639 157 ---EEKGQDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 233 NLKDKTIFSLDMGALIAGAKFRGEFEERLKAVLKEVKKSDGRILlFIDEIHNIVGAGKT-EGSMDAGNLLKPMLARGELH 311
Cdd:TIGR02639 234 RLKNAKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAIL-FIDEIHTIVGAGATsGGSMDASNLLKPALSSGKIR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 312 LIGATTLDEYRQYMEKDKALERRFQKVLVKEPTVEDTISILRGLKERFEIHHGVNIHDNALVAAATLSDRYITDRFLPDK 391
Cdd:TIGR02639 313 CIGSTTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 392 AIDLIDEASATIRVEmnsmpteldqvtrrlmqleieeaalkkesdDASKKRlknlqeelaelreeanamkmqwetekeev 471
Cdd:TIGR02639 393 AIDVIDEAGAAFRLR------------------------------PKAKKK----------------------------- 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 472 nsvsakraeidkakheledaennydleraavlrhgtipqlekelkeleakakdseikmvqESVTENEIAQVVGRLTGIPV 551
Cdd:TIGR02639 414 ------------------------------------------------------------ANVNVKDIENVVAKMAKIPV 433
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 552 TKLVEGEREKLIKLNETLHKRVIGQDEAVDAVSDAVIRSRAGLQDPNRPLGSFLFLGPTGVGKTELAKALAENLfdsEDH 631
Cdd:TIGR02639 434 KTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEEL---GVH 510
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 632 MVRIDMSEYMEKHAVSRLVGAPPGYVGYEEGGQLTEAVRRNPYTIVLLDEIEKAHPDVFNILLQVLDDGRLTDSKGRVVD 711
Cdd:TIGR02639 511 LLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKAD 590
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 712 FKNTVLIMTSNIGSQLLLEGVT--ADGTIPEAVAEQVNTLlrgnFKPEFLNRIDDTILFTPLSLDNVKGIVDKMVAQLAQ 789
Cdd:TIGR02639 591 FRNVILIMTSNAGASEMSKPPIgfGGENRESKSLKAIKKL----FSPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQD 666
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488230346 790 RLEHQEILLTISDEAKTWIAENAYEPAYGARPLKRFITKEVETPLAKEIVAGHVMPKSKVTITL 853
Cdd:TIGR02639 667 QLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEILFGKLKKGGSVKISL 730
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
4-867 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 543.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 4 EKMTTTLQEAIAEAQQiavtRKHQDIDIAHVWKIFLQpNHFGRNFYTDAGLDVESFEHEIDRLLDEY-PVVSGGNVQYGQ 82
Cdd:PRK11034 4 QELELSLNMAFARARE----HRHEFMTVEHLLLALLS-NPSAREALEACSVDLVALRQELEAFIEQTtPVLPASEEERDT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 83 NLSQNFFRLLNEADQIRESFGDEFLSTEVVILALMKLKNYPLTVYLNKNGLSEKEL--------RKNIEEMRGGERVTSQ 154
Cdd:PRK11034 79 QPTLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVvnfishgtRKDEPSQSSDPGSQPN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 155 NQEEQ--YKALEKYGVDLVQQVKSGKMDPIIGRDEEIRDVIRILSRKTKNNPVLIGEPGVGKTAIVEGLAQRIVRKDVPE 232
Cdd:PRK11034 159 SEEQAggEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 233 NLKDKTIFSLDMGALIAGAKFRGEFEERLKAVLKEVKKSDGRILlFIDEIHNIVGAGKTEG-SMDAGNLLKPMLARGELH 311
Cdd:PRK11034 239 VMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSIL-FIDEIHTIIGAGAASGgQVDAANLIKPLLSSGKIR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 312 LIGATTLDEYRQYMEKDKALERRFQKVLVKEPTVEDTISILRGLKERFEIHHGVNIHDNALVAAATLSDRYITDRFLPDK 391
Cdd:PRK11034 318 VIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 392 AIDLIDEASATIRVemnsMPteldqVTRRlmqleieeaalkkesddaskkrlknlqeelaelreeanamkmqwetekeev 471
Cdd:PRK11034 398 AIDVIDEAGARARL----MP-----VSKR--------------------------------------------------- 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 472 nsvsakraeidkakheledaennydleraavlrhgtipqlekelkeleakakdseikmvQESVTENEIAQVVGRLTGIPV 551
Cdd:PRK11034 418 -----------------------------------------------------------KKTVNVADIESVVARIARIPE 438
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 552 TKLVEGEREKLIKLNETLHKRVIGQDEAVDAVSDAVIRSRAGLQDPNRPLGSFLFLGPTGVGKTELAKALAENLfDSEdh 631
Cdd:PRK11034 439 KSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL-GIE-- 515
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 632 MVRIDMSEYMEKHAVSRLVGAPPGYVGYEEGGQLTEAVRRNPYTIVLLDEIEKAHPDVFNILLQVLDDGRLTDSKGRVVD 711
Cdd:PRK11034 516 LLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKAD 595
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 712 FKNTVLIMTSNIGSQLLLE---GVTADGTIPEAVAEqvntlLRGNFKPEFLNRIDDTILFTPLSLDNVKGIVDKMVAQLA 788
Cdd:PRK11034 596 FRNVVLVMTTNAGVRETERksiGLIHQDNSTDAMEE-----IKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQ 670
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488230346 789 QRLEHQEILLTISDEAKTWIAENAYEPAYGARPLKRFITKEVETPLAKEIVAGHVMPKSKVTITLLDGQLHFKTEELEE 867
Cdd:PRK11034 671 AQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKEKNELTYGFQSA 749
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
561-768 |
1.19e-107 |
|
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: 328.37 E-value: 1.19e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 561 KLIKLNETLHKRVIGQDEAVDAVSDAVIRSRAGLQDPNRPLGSFLFLGPTGVGKTELAKALAENLFDSEDHMVRIDMSEY 640
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 641 MEKHAVSRLVGAPPGYVGYEEGGQLTEAVRRNPYTIVLLDEIEKAHPDVFNILLQVLDDGRLTDSKGRVVDFKNTVLIMT 720
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488230346 721 SNigsqlllegvtadgtipeavaeqvntllrgNFKPEFLNRIDDTILF 768
Cdd:cd19499 161 SN------------------------------HFRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
599-765 |
4.11e-92 |
|
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: 287.55 E-value: 4.11e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 599 RPLGSFLFLGPTGVGKTELAKALAENLFDSEDHMVRIDMSEYMEKHAVSRLVGAPPGYVGYEEGGQLTEAVRRNPYTIVL 678
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 679 LDEIEKAHPDVFNILLQVLDDGRLTDSKGRVVDFKNTVLIMTSNIGSQLLLEGV-TADGTIPEAVAEQVNTLLRGNFKPE 757
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASrLGDSPDYELLKEEVMDLLKKGFIPE 160
|
....*...
gi 488230346 758 FLNRIDDT 765
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 |
1.77e-44 |
|
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: 155.34 E-value: 1.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 344 TVEDTISILRGLKERFEIHHGVNIHDNALVAAATLSDRYITDRFLPDKAIDLIDEASATIRVEMNSMPTELDQVTRRLMQ 423
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|....
gi 488230346 424 LEIEEAALKKESDDASKKRLKNLQ 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, ... |
771-851 |
5.24e-27 |
|
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: 104.79 E-value: 5.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 771 LSLDNVKGIVDKMVAQLAQRLEHQEILLTISDEAKTWIAENAYEPAYGARPLKRFITKEVETPLAKEIVAGHVMPKSKVT 850
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 488230346 851 I 851
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, ... |
771-860 |
1.07e-25 |
|
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: 101.37 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 771 LSLDNVKGIVDKMVAQLAQRLEHQEILLTISDEAKTWIAENAYEPAYGARPLKRFITKEVETPLAKEIVAGHVMPKSKVT 850
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
90
....*....|
gi 488230346 851 ITLLDGQLHF 860
Cdd:smart01086 81 VDVDDGELVF 90
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
183-343 |
6.41e-22 |
|
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: 92.98 E-value: 6.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 183 IGRDEEIRDVIRILSRKTKNNPVLIGEPGVGKTAIVEGLAQRIVRKDVPenlkdktIFSLDMGALIAGAKFRGEFEERLK 262
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 263 AVLKEVKKSDGRILLFIDEIHNIvGAGKTEGSMDA-GNLLKPMLARGELHLIGATTLDEYRQymeKDKALERRFQKVLVK 341
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDSL-SRGAQNALLRVlETLNDLRIDRENVRVIGATNRPLLGD---LDRALYDRLDIRIVI 149
|
..
gi 488230346 342 EP 343
Cdd:cd00009 150 PL 151
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
574-729 |
4.30e-20 |
|
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: 87.59 E-value: 4.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 574 IGQDEAVDAVSDAVirsraglqdPNRPLGSFLFLGPTGVGKTELAKALAENLFDSEDHMVRIDMSEYMEKHAVSRLvgap 653
Cdd:cd00009 1 VGQEEAIEALREAL---------ELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAEL---- 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488230346 654 pgyVGYEEGGQLTEAVRRNPYTIVLLDEIEKAHPDVFNILLQVLDDGRLTdskgrVVDFKNTVLIMTSNIGSQLLL 729
Cdd:cd00009 68 ---FGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATNRPLLGDL 135
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
603-728 |
7.80e-15 |
|
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: 71.94 E-value: 7.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 603 SFLFLGPTGVGKTELAKALAENLFDSEDHMVRidMSEYMEKhavSRLVGA--PPGYVGYEEGGQLTEAVRRNpyTIVLLD 680
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQ--LTRDTTE---EDLFGRrnIDPGGASWVDGPLVRAAREG--EIAVLD 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 488230346 681 EIEKAHPDVFNILLQVLDDGRL-TDSKGRVVDFKNT--VLIMTSNIGSQLL 728
Cdd:pfam07728 74 EINRANPDVLNSLLSLLDERRLlLPDGGELVKAAPDgfRLIATMNPLDRGL 124
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
600-728 |
1.08e-14 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 72.02 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 600 PLGSFLFLGPTGVGKTELAKALAENLFDSEDHMVRIDMSEYMEKHAVSRLVGAPPGYVGYEEGGQ----LTEAVRRNPYT 675
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 488230346 676 IVLLDEIEKAHPDVFNILLQVLDDGRLTDSKGRvvdFKNTVLIMTSNIGSQLL 728
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTNDEKDLG 130
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
206-339 |
1.57e-13 |
|
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: 68.00 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 206 LIGEPGVGKTAIVEGLAQRIvrkdvpenlkDKTIFSLDMGALIagAKFRGEFEERLKAVLKEVKKSDGRIlLFIDEIHNI 285
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELV--SKYVGESEKRLRELFEAAKKLAPCV-IFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488230346 286 VGAGKTEGSMDAGNLLKPMLA--------RGELHLIGATTldeyrqYMEK-DKALERRFQKVL 339
Cdd:pfam00004 70 AGSRGSGGDSESRRVVNQLLTeldgftssNSKVIVIAATN------RPDKlDPALLGRFDRII 126
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
579-722 |
8.96e-09 |
|
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: 55.37 E-value: 8.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 579 AVDAVSDAVIRSRAGLQDPNRPLG---SFLFLGPTGVGKTELAKALAEnlfDSEDHMVRIDMSEYMEKhavsrlvgappg 655
Cdd:cd19481 1 LKASLREAVEAPRRGSRLRRYGLGlpkGILLYGPPGTGKTLLAKALAG---ELGLPLIVVKLSSLLSK------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 656 YVGYEEG--GQLTEAVRRNPYTIVLLDEIEKAHPD------------VFNILLQVLDDGRLTDskgrvvdfkNTVLIMTS 721
Cdd:cd19481 66 YVGESEKnlRKIFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAAT 136
|
.
gi 488230346 722 N 722
Cdd:cd19481 137 N 137
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
486-683 |
1.23e-08 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 57.71 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 486 HELEDAENNYDLERAAVLRHGTIPQLEKELKELEAKAkdseikmvQESVTENEIAQVVGRLTGIPVTKLVEGEREKLIKL 565
Cdd:COG1222 2 NDLLTIDENIKALLALIDALQERLGVELALLLQPVKA--------LELLEEAPALLLNDANLTQKRLGTPRGTAVPAESP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 566 NETLHKrVIGQDEAVDAVSDAVIRSragLQDPN-------RPLGSFLFLGPTGVGKTELAKALAENLfdsEDHMVRIDMS 638
Cdd:COG1222 74 DVTFDD-IGGLDEQIEEIREAVELP---LKNPElfrkygiEPPKGVLLYGPPGTGKTLLAKAVAGEL---GAPFIRVRGS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488230346 639 EYMEKhavsrlvgappgYVGyeEGGQLT----EAVRRNPYTIVLLDEIE 683
Cdd:COG1222 147 ELVSK------------YIG--EGARNVrevfELAREKAPSIIFIDEID 181
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
605-722 |
3.22e-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: 52.98 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 605 LFLGPTGVGKTELAKALAENLFdseDHMVRIDMSEYMEKHavsrlVGAPPGYVgyeegGQLTEAVRRNPYTIVLLDEIEK 684
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELG---APFIEISGSELVSKY-----VGESEKRL-----RELFEAAKKLAPCVIFIDEIDA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 488230346 685 AHP-----------DVFNILLQVLDDgrLTDSKGRVvdfkntVLIMTSN 722
Cdd:pfam00004 69 LAGsrgsggdsesrRVVNQLLTELDG--FTSSNSKV------IVIAATN 109
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
50-367 |
4.97e-08 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 56.07 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 50 TDAGLDVESFEHEIDRLLDEYPVVSGGNVQYGQNLSQNFFRLLNEADQIRESFGDEFLSTEVVILALMKLKNYPLTVYLN 129
Cdd:COG0464 27 LLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 130 KNGLSEKELRKNIEEMRGGERVTSQNQEEQYKALEKYGVDLVQQVKSGKMDPIIGRDEEIRDVIRILSRKTKNNPV---- 205
Cdd:COG0464 107 LLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELreey 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 206 ---------LIGEPGVGKTAIVEGLAQRIvrkdvpenlkDKTIFSLDMGALIagAKFRGEFEERLKAVLKEVKKSdGRIL 276
Cdd:COG0464 187 glppprgllLYGPPGTGKTLLARALAGEL----------GLPLIEVDLSDLV--SKYVGETEKNLREVFDKARGL-APCV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 277 LFIDEIHNIvgAGKTEGSMDA------GNLLKPM-LARGELHLIGATtldeYRqyMEK-DKALERRFQKVL-VKEPTVED 347
Cdd:COG0464 254 LFIDEADAL--AGKRGEVGDGvgrrvvNTLLTEMeELRSDVVVIAAT----NR--PDLlDPALLRRFDEIIfFPLPDAEE 325
|
330 340
....*....|....*....|
gi 488230346 348 TISILRGLKERFEIHHGVNI 367
Cdd:COG0464 326 RLEIFRIHLRKRPLDEDVDL 345
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
200-340 |
7.85e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 52.38 E-value: 7.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 200 TKNNPVLIGEPGVGKTAIVEGLAQRIVRKDV------PENLKDKTIFSLdMGALIAGAKFRGEFEERLKAVLKEVKKSDG 273
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGgviyidGEDILEEVLDQL-LLIIVGGKKASGSGELRLRLALALARKLKP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488230346 274 RIlLFIDEIHNIVGAG--KTEGSMDAGNLLKPMLARGELHLIGATTLDEyrqyMEKDKALERRFQKVLV 340
Cdd:smart00382 80 DV-LILDEITSLLDAEqeALLLLLEELRLLLLLKSEKNLTVILTTNDEK----DLGPALLRRRFDRRIV 143
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
487-786 |
1.45e-07 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 54.53 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 487 ELEDAENNYDLERAAVLRHGTIPQLEKELKELEAKAKDSEIKMVQESVTENEIAQVVGRLTGIPVTKLVEGEREKLIKLN 566
Cdd:COG0464 73 LLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 567 ETLHKRVIGQDEAVDAVSDAV--------IRSRAGLQDPNRplgsFLFLGPTGVGKTELAKALAENLfdsEDHMVRIDMS 638
Cdd:COG0464 153 EAILDDLGGLEEVKEELRELValplkrpeLREEYGLPPPRG----LLLYGPPGTGKTLLARALAGEL---GLPLIEVDLS 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 639 EymekhavsrLVGappGYVGYEEGG--QLTEAVRRNPYTIVLLDEIEKAHPD-----------VFNILLQVLDDGRltds 705
Cdd:COG0464 226 D---------LVS---KYVGETEKNlrEVFDKARGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR---- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 706 kgrvvdfKNTVLIMTSNigsqlllegvtadgtipeavaeqvntlLRGNFKPEFLNRIDDTILFTPLSLDNVKGIVDKMVA 785
Cdd:COG0464 290 -------SDVVVIAATN---------------------------RPDLLDPALLRRFDEIIFFPLPDAEERLEIFRIHLR 335
|
.
gi 488230346 786 Q 786
Cdd:COG0464 336 K 336
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
567-684 |
3.48e-06 |
|
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: 48.14 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 567 ETLHKRVIGQDEAVDAVSDAvIRSR-------AGLQDPNRPlGSFLFLGPTGVGKTELAKALAEnLFDSEdhMVRIDMSE 639
Cdd:cd19498 7 SELDKYIIGQDEAKRAVAIA-LRNRwrrmqlpEELRDEVTP-KNILMIGPTGVGKTEIARRLAK-LAGAP--FIKVEATK 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 488230346 640 YMEKhavsrlvgappGYVGYEeggqlTEAVRRNPYT-IVLLDEIEK 684
Cdd:cd19498 82 FTEV-----------GYVGRD-----VESIIRDLVEgIVFIDEIDK 111
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
208-380 |
6.20e-06 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 49.70 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 208 GEPGVGKTAIVEGLAQRIvrkdvpenlkDKTIFSLDmgALIAGAKfrgefeeRLKAVLKEVKK---SDGRILLFIDEIH- 283
Cdd:PRK13342 43 GPPGTGKTTLARIIAGAT----------DAPFEALS--AVTSGVK-------DLREVIEEARQrrsAGRRTILFIDEIHr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 284 -NivgagKTEgsMDAgnLLkPMLARGELHLIGATTldEyRQYMEKDKALERRFQkVLVKEP-TVEDTISIL-RGLKERFE 360
Cdd:PRK13342 104 fN-----KAQ--QDA--LL-PHVEDGTITLIGATT--E-NPSFEVNPALLSRAQ-VFELKPlSEEDIEQLLkRALEDKER 169
|
170 180
....*....|....*....|
gi 488230346 361 IHhgVNIHDNALVAAATLSD 380
Cdd:PRK13342 170 GL--VELDDEALDALARLAN 187
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
603-701 |
1.19e-05 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 45.41 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 603 SFLFL-GPTGVGKTELAKALAENLFDSEDHMVRIDMSEYMEK----HAVSRLVGAPPGYVGYEEG--GQLTEAV-RRNPY 674
Cdd:pfam13401 6 GILVLtGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPkdllRALLRALGLPLSGRLSKEEllAALQQLLlALAVA 85
|
90 100
....*....|....*....|....*..
gi 488230346 675 TIVLLDEIEKAHPDVFNILLQVLDDGR 701
Cdd:pfam13401 86 VVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
573-699 |
1.50e-05 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 47.19 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 573 VIGQDEAVDAVSDAV-------IRSRAGLQDPNRplgsFLFLGPTGVGKTELAKALAENLfDSEDHMVRID--MSEYMEK 643
Cdd:COG1223 4 VVGQEEAKKKLKLIIkelrrreNLRKFGLWPPRK----ILFYGPPGTGKTMLAEALAGEL-KLPLLTVRLDslIGSYLGE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488230346 644 hAVSRLvgappgyvgyeegGQLTEAVRRNPyTIVLLDEIE---------KAHPD---VFNILLQVLDD 699
Cdd:COG1223 79 -TARNL-------------RKLFDFARRAP-CVIFFDEFDaiakdrgdqNDVGEvkrVVNALLQELDG 131
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
205-380 |
2.07e-05 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 47.74 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 205 VLIGEPGVGKTAIVEGLAQRivrkdvpenlkdktifsldmgaliAGAKFrgefeERLKAVL---KEVKK----------S 271
Cdd:COG2256 53 ILWGPPGTGKTTLARLIANA------------------------TDAEF-----VALSAVTsgvKDIREvieearerraY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 272 DGRILLFIDEIH--NivgagKTEgsMDAgnLLkPMLARGELHLIGATTldEyRQYMEKDKALERRFQkVLVKEP-TVEDT 348
Cdd:COG2256 104 GRRTILFVDEIHrfN-----KAQ--QDA--LL-PHVEDGTITLIGATT--E-NPSFEVNSALLSRCR-VFVLKPlSEEDL 169
|
170 180 190
....*....|....*....|....*....|....*
gi 488230346 349 ISIL-RGL--KERFEIHHGVNIHDNALVAAATLSD 380
Cdd:COG2256 170 EQLLeRALadDERGLGGYKLELDDEALEALARLAD 204
|
|
| Sigma54_activat |
pfam00158 |
Sigma-54 interaction domain; |
182-285 |
2.68e-05 |
|
Sigma-54 interaction domain;
Pssm-ID: 425491 [Multi-domain] Cd Length: 168 Bit Score: 45.47 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 182 IIGRDEEIRDVIRILSRKTKNN-PVLI-GEPGVGKTAIVEGLAQRIVRKD----------VPENLKDKTIFSLDMGALiA 249
Cdd:pfam00158 1 IIGESPAMQEVLEQAKRVAPTDaPVLItGESGTGKELFARAIHQLSPRADgpfvavncaaIPEELLESELFGHEKGAF-T 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 488230346 250 GAKFR--GEFEerlkavlkevkKSDGRIlLFIDEIHNI 285
Cdd:pfam00158 80 GADSDrkGLFE-----------LADGGT-LFLDEIGEL 105
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
95-147 |
2.71e-05 |
|
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: 42.12 E-value: 2.71e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488230346 95 ADQIRESFGDEFLSTEVVILALMKLKNYPLTVYLNKNGLSEKELRKNIEEMRG 147
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
194-334 |
3.01e-05 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 47.74 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 194 RILSRKTK----NNPVLIGEPGVGKTAivegLAQRIVRKDVPEnlkdktiFSlDMGALIAGAKfrgEFEERLKAVLKEVK 269
Cdd:PRK13341 41 RLLRRAIKadrvGSLILYGPPGVGKTT----LARIIANHTRAH-------FS-SLNAVLAGVK---DLRAEVDRAKERLE 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488230346 270 KSDGRILLFIDEIHNIVGAGKtegsmDAgnlLKPMLARGELHLIGATTLDEyrqYMEKDKALERR 334
Cdd:PRK13341 106 RHGKRTILFIDEVHRFNKAQQ-----DA---LLPWVENGTITLIGATTENP---YFEVNKALVSR 159
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
206-339 |
4.42e-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: 44.58 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 206 LIGEPGVGKTAIVEGLAQRIVRKdvpenlkdktIFSLDMGALIagAKFRGEFEERLKAVLKEVKKSDGRIlLFIDEIHNI 285
Cdd:cd19481 31 LYGPPGTGKTLLAKALAGELGLP----------LIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCI-LFIDEIDAI 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488230346 286 vgAGKTEGSMDAG----------NLLKPMLARGELHLIGATTLDEyrqymEKDKALER--RFQKVL 339
Cdd:cd19481 98 --GRKRDSSGESGelrrvlnqllTELDGVNSRSKVLVIAATNRPD-----LLDPALLRpgRFDEVI 156
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
181-230 |
9.40e-05 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 43.65 E-value: 9.40e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488230346 181 PIIGRDEEIRDVIRILSRKTKNNP---VLIGEPGVGKTAIVEGLAQRIVRKDV 230
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERDGG 53
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
564-722 |
1.13e-04 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 45.16 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 564 KLNETLHKRVIGQDEAVDAVSDAVIrsrAGlqdpnRPLgsfLFLGPTGVGKTELAKALAENLfDSEdhMVRI----DMse 639
Cdd:COG0714 5 RLRAEIGKVYVGQEELIELVLIALL---AG-----GHL---LLEGVPGVGKTTLAKALARAL-GLP--FIRIqftpDL-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 640 yMEkhavSRLVGAppgYVgYEEGGQlTEAVRRNPY--TIVLLDEIEKAHPDVFNILLQVLDDGRLTdSKGRVVDFKNTVL 717
Cdd:COG0714 69 -LP----SDILGT---YI-YDQQTG-EFEFRPGPLfaNVLLADEINRAPPKTQSALLEAMEERQVT-IPGGTYKLPEPFL 137
|
....*.
gi 488230346 718 IM-TSN 722
Cdd:COG0714 138 VIaTQN 143
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
134-377 |
1.29e-04 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 45.00 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 134 SEKELRKNIEEMRGGERVTSQNQEEQYKALEKYGVDLVQQVKSGKMDP-------------IIGRDEEIRDVIRILSRKT 200
Cdd:COG1222 19 DALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTavpaespdvtfddIGGLDEQIEEIREAVELPL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 201 KNN---------PV----LIGEPGVGKTAIVEGLAQRIvrkdvpenlkDKTIFSLDMGALIagAKFRGEFEERLKAVLKE 267
Cdd:COG1222 99 KNPelfrkygiePPkgvlLYGPPGTGKTLLAKAVAGEL----------GAPFIRVRGSELV--SKYIGEGARNVREVFEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 268 VKKSDgRILLFIDEIHNIvgAGKTEGSMDAG---NLLKPMLA-------RGELHLIGAT-TLDEYrqymekDKALER--R 334
Cdd:COG1222 167 AREKA-PSIIFIDEIDAI--AARRTDDGTSGevqRTVNQLLAeldgfesRGDVLIIAATnRPDLL------DPALLRpgR 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 488230346 335 F-QKVLVKEPTVEDTISILRGLKERFEIHHGVNIhdnALVAAAT 377
Cdd:COG1222 238 FdRVIEVPLPDEEAREEILKIHLRDMPLADDVDL---DKLAKLT 278
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
17-68 |
1.72e-04 |
|
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: 39.81 E-value: 1.72e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488230346 17 AQQIAVTRKHQDIDIAHVWKIFL-QPNHFGRNFYTDAGLDVESFEHEIDRLLD 68
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLeEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
206-316 |
2.13e-04 |
|
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410911 [Multi-domain] Cd Length: 165 Bit Score: 42.66 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 206 LIGEPGVGKTAIVEGLAqrivrkdvpeNLKDKTIFSLDmGALIAGaKFRGEFEERLKAVLKEVkKSDGRILLFIDEIHNI 285
Cdd:cd19503 39 LHGPPGTGKTLLARAVA----------NEAGANFLSIS-GPSIVS-KYLGESEKNLREIFEEA-RSHAPSIIFIDEIDAL 105
|
90 100 110
....*....|....*....|....*....|....*...
gi 488230346 286 VGA-GKTEGSMDAG------NLLKPMLARGELHLIGAT 316
Cdd:cd19503 106 APKrEEDQREVERRvvaqllTLMDGMSSRGKVVVIAAT 143
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
205-335 |
2.22e-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: 41.89 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 205 VLIGEPGVGKTAIVEGLAQRIVRKDVPENLkdktiFSLDMGA--LIAGAKFRGEFEERLKAVLKEVKKSdGRIlLFIDEI 282
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSNRPVFYVQ-----LTRDTTEedLFGRRNIDPGGASWVDGPLVRAARE-GEI-AVLDEI 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 283 H----NIVGAGKT---EGSMDAGNLLKPMLARGELHLIGATTLDEYRQYMEKDKALERRF 335
Cdd:pfam07728 76 NranpDVLNSLLSlldERRLLLPDGGELVKAAPDGFRLIATMNPLDRGLNELSPALRSRF 135
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
205-337 |
2.75e-04 |
|
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410930 [Multi-domain] Cd Length: 170 Bit Score: 42.66 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 205 VLIGEPGVGKTAIVEGLAQRIvrkdvpenlkDKTIFSLDMGALIAgaKFRGEfEERLKAVLKEVKKSDGRILLFIDEIHN 284
Cdd:cd19522 37 LMVGPPGTGKTLLAKAVATEC----------GTTFFNVSSSTLTS--KYRGE-SEKLVRLLFEMARFYAPTTIFIDEIDS 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488230346 285 IVGAGKTEGSMDAGNLLKPMLARGELHLIGATTLDEYRQYM----------EKDKALERRFQK 337
Cdd:cd19522 104 ICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVmvlaatnfpwDIDEALRRRLEK 166
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
198-285 |
2.82e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 41.56 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 198 RKTKNNPVLIGEPGVGKTAIVEGLAQRIVRKDV---------PENLKD--KTIFSldmgALIAGAKFRGEFEERLKAVLK 266
Cdd:pfam13401 2 RFGAGILVLTGESGTGKTTLLRRLLEQLPEVRDsvvfvdlpsGTSPKDllRALLR----ALGLPLSGRLSKEELLAALQQ 77
|
90
....*....|....*....
gi 488230346 267 EVKKSDGRILLFIDEIHNI 285
Cdd:pfam13401 78 LLLALAVAVVLIIDEAQHL 96
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
605-698 |
3.29e-04 |
|
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: 42.55 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 605 LFLGPTGVGKTELAKALAENLfdsEDHMVRI------DMSE-------YmekhavsrlVGAPPgyvgyeegGQLTEAVRR 671
Cdd:cd19500 41 CLVGPPGVGKTSLGKSIARAL---GRKFVRIslggvrDEAEirghrrtY---------VGAMP--------GRIIQALKK 100
|
90 100 110
....*....|....*....|....*....|....*
gi 488230346 672 ----NPytIVLLDEIEK----AHPDVFNILLQVLD 698
Cdd:cd19500 101 agtnNP--VFLLDEIDKigssFRGDPASALLEVLD 133
|
|
| AcoR |
COG3284 |
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription]; |
180-282 |
5.29e-04 |
|
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
Pssm-ID: 442514 [Multi-domain] Cd Length: 625 Bit Score: 43.74 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 180 DPIIGRDEEIRDVIRILSRKTKNN-PVLI-GEPGVGKTAIVEGLAQRIVRKD----------VPENLKDKTIFSLDMGAL 247
Cdd:COG3284 321 AALAGGDPAMRRALRRARRLADRDiPVLIlGETGTGKELFARAIHAASPRADgpfvavncaaIPEELIESELFGYEPGAF 400
|
90 100 110
....*....|....*....|....*....|....*...
gi 488230346 248 iAGAK---FRGEFEErlkavlkevkkSDGRIlLFIDEI 282
Cdd:COG3284 401 -TGARrkgRPGKIEQ-----------ADGGT-LFLDEI 425
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
576-728 |
6.74e-04 |
|
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
Pssm-ID: 440238 [Multi-domain] Cd Length: 289 Bit Score: 42.65 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 576 QDEAVDAVSDAVIRsraglqdpNRPLGSFLFLGPTGVGKTELAKALAENLFDSEDHmvriDMSEYMEKHAVSRLVGAPPG 655
Cdd:COG0470 1 QEEAWEQLLAAAES--------GRLPHALLLHGPPGIGKTTLALALARDLLCENPE----GGKACGQCHSRLMAAGNHPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 656 YV---GYEEGGQLT-EAVRR-----------NPYTIVLLDEIEKAHPDVFNILLQVLDDGRltdskgrvvdfKNTVLIMT 720
Cdd:COG0470 69 LLelnPEEKSDQIGiDQIRElgeflsltpleGGRKVVIIDEADAMNEAAANALLKTLEEPP-----------KNTPFILI 137
|
....*...
gi 488230346 721 SNIGSQLL 728
Cdd:COG0470 138 ANDPSRLL 145
|
|
| PRK14956 |
PRK14956 |
DNA polymerase III subunits gamma and tau; Provisional |
573-699 |
6.87e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184920 [Multi-domain] Cd Length: 484 Bit Score: 43.01 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 573 VIGQDEAVDAVSDAVIRSRAGlqdpnrplGSFLFLGPTGVGKTELAKALA-----ENLFDSE--------DHMVRIDMSE 639
Cdd:PRK14956 20 VIHQDLAIGALQNALKSGKIG--------HAYIFFGPRGVGKTTIARILAkrlncENPIGNEpcnectscLEITKGISSD 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488230346 640 YMEKHAVSRlvgappgyVGYEEGGQLTEAVRRNP----YTIVLLDEIEKAHPDVFNILLQVLDD 699
Cdd:PRK14956 92 VLEIDAASN--------RGIENIRELRDNVKFAPmggkYKVYIIDEVHMLTDQSFNALLKTLEE 147
|
|
| RecA-like_FtsH |
cd19501 |
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ... |
571-683 |
8.19e-04 |
|
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410909 [Multi-domain] Cd Length: 171 Bit Score: 41.06 E-value: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 571 KRVIGQDEAVDAVSDAVirsrAGLQDPNR--------PLGsFLFLGPTGVGKTELAKALAenlfdSEDHMVRIDM--SEY 640
Cdd:cd19501 4 KDVAGCEEAKEELKEVV----EFLKNPEKftklgakiPKG-VLLVGPPGTGKTLLAKAVA-----GEAGVPFFSIsgSDF 73
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 488230346 641 MEKhavsrLVGappgyVGYEEGGQLTEAVRRNPYTIVLLDEIE 683
Cdd:cd19501 74 VEM-----FVG-----VGASRVRDLFEQAKKNAPCIVFIDEID 106
|
|
| RecA-like_Figl-1 |
cd19525 |
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ... |
205-339 |
9.03e-04 |
|
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410933 [Multi-domain] Cd Length: 186 Bit Score: 41.13 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 205 VLIGEPGVGKTAIVEGLAQRivrkdvpenlKDKTIFSLDMGALIagAKFRGEFEERLKAvLKEVKKSDGRILLFIDEIHN 284
Cdd:cd19525 59 LLFGPPGTGKTLIGKCIASQ----------SGATFFSISASSLT--SKWVGEGEKMVRA-LFSVARCKQPAVIFIDEIDS 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488230346 285 IVgAGKTEGSMDAGNLLKPMLArgeLHLIGATTLDEYR--------QYMEKDKALERRFQKVL 339
Cdd:cd19525 126 LL-SQRGEGEHESSRRIKTEFL---VQLDGATTSSEDRilvvgatnRPQEIDEAARRRLVKRL 184
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
564-625 |
9.29e-04 |
|
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: 41.82 E-value: 9.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 564 KLNETLHKRVIGQDEAVDAVSDAVI----RSRAGLQDPNRPL----GSFLFLGPTGVGKTELAKALAENL 625
Cdd:cd19497 5 EIKEHLDKYVIGQERAKKVLSVAVYnhykRIRNNLKQKDDDVelekSNILLIGPTGSGKTLLAQTLAKIL 74
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
182-282 |
1.24e-03 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 41.69 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 182 IIGRDEEIRDV-IRILSRKtknnPVLI-GEPGVGKTAIVEGLAQRIvrkdvpeNLKDKTI-FSLDM------GALIAGAK 252
Cdd:COG0714 14 YVGQEELIELVlIALLAGG----HLLLeGVPGVGKTTLAKALARAL-------GLPFIRIqFTPDLlpsdilGTYIYDQQ 82
|
90 100 110
....*....|....*....|....*....|
gi 488230346 253 FrGEFEERLKAVLKEVkksdgrilLFIDEI 282
Cdd:COG0714 83 T-GEFEFRPGPLFANV--------LLADEI 103
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
205-285 |
1.53e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 41.31 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 205 VLIGEPGVGKTAIVEGLAQRIvrkdvPENLKDKTIF--SLDMGALIA------GAKFRG----EFEERLKAVLKEVKKSD 272
Cdd:COG3267 47 VLTGEVGTGKTTLLRRLLERL-----PDDVKVAYIPnpQLSPAELLRaiadelGLEPKGaskaDLLRQLQEFLLELAAAG 121
|
90
....*....|...
gi 488230346 273 GRILLFIDEIHNI 285
Cdd:COG3267 122 RRVVLIIDEAQNL 134
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
573-622 |
1.53e-03 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 41.72 E-value: 1.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488230346 573 VIGQDEAVDAVSDAVIRSR---AglqdpnrplgsFLFLGPTGVGKTELAKALA 622
Cdd:COG2812 12 VVGQEHVVRTLKNALASGRlahA-----------YLFTGPRGVGKTTLARILA 53
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
181-230 |
1.93e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.15 E-value: 1.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488230346 181 PIIGRDEEIRDVIRILSRKTKNNP--VLI-GEPGVGKTAIVEGLAQRIVRKDV 230
Cdd:COG3899 288 PLVGREAELAALLAALERARAGRGelVLVsGEAGIGKSRLVRELARRARARGG 340
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
205-337 |
2.03e-03 |
|
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410917 [Multi-domain] Cd Length: 163 Bit Score: 39.64 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 205 VLIGEPGVGKTAIVEGLAQRIvrkdvpenlkDKTIFSLDMGALIagAKFRGEFEERLKAVLKEVKKSDGRIlLFIDEIHN 284
Cdd:cd19509 36 LLYGPPGTGKTLLARAVASES----------GSTFFSISASSLV--SKWVGESEKIVRALFALARELQPSI-IFIDEIDS 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488230346 285 IV---GAGKTEGSMDAGN-LLKPM-----LARGELHLIGATTLDEyrqymEKDKALERRFQK 337
Cdd:cd19509 103 LLserGSGEHEASRRVKTeFLVQMdgvlnKPEDRVLVLGATNRPW-----ELDEAFLRRFEK 159
|
|
| RecA-like_Yta7-like |
cd19517 |
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ... |
205-316 |
2.80e-03 |
|
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 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: 410925 [Multi-domain] Cd Length: 170 Bit Score: 39.41 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 205 VLIGEPGVGKTAIVEGLAQRIVRKDvpenlkDKTIFSLDMGALIAgAKFRGEFEERLKAVLKEVKKSDGRILLFiDEIHN 284
Cdd:cd19517 38 LFHGPPGTGKTLMARALAAECSKGG------QKVSFFMRKGADCL-SKWVGEAERQLRLLFEEAYRMQPSIIFF-DEIDG 109
|
90 100 110
....*....|....*....|....*....|....*....
gi 488230346 285 IVGAGKTEGSMDAGNLLKPMLA-------RGELHLIGAT 316
Cdd:cd19517 110 LAPVRSSKQEQIHASIVSTLLAlmdgldnRGQVVVIGAT 148
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
205-395 |
5.16e-03 |
|
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.
Pssm-ID: 273521 [Multi-domain] Cd Length: 733 Bit Score: 40.66 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 205 VLIGEPGVGKTAIVEGLAQRIvrkdvpenlkdKTIFSLDMGALIAgAKFRGEFEERLKAVLKEVKKSDGRIlLFIDEIHN 284
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANEA-----------GAYFISINGPEIM-SKYYGESEERLREIFKEAEENAPSI-IFIDEIDA 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 285 IV-----GAGKTEGSMDAG--NLLKPMLARGELHLIGATTLDEyrqymEKDKALER--RFQK-VLVKEPTVEDTISILR- 353
Cdd:TIGR01243 283 IApkreeVTGEVEKRVVAQllTLMDGLKGRGRVIVIGATNRPD-----ALDPALRRpgRFDReIVIRVPDKRARKEILKv 357
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488230346 354 -----------GLKERFEIHHGVNIHDNALVA--AATLSDRyitdRFLPDKAIDL 395
Cdd:TIGR01243 358 htrnmplaedvDLDKLAEVTHGFVGADLAALAkeAAMAALR----RFIREGKINF 408
|
|
| CDC6 |
COG1474 |
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]; |
182-286 |
5.68e-03 |
|
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
Pssm-ID: 441083 [Multi-domain] Cd Length: 389 Bit Score: 39.83 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 182 IIGRDEEIRDVIRILSRKTKNNP----VLIGEPGVGKTAIVEGLAQRIVRKDVPENLK----------DKTIFSLdMGAL 247
Cdd:COG1474 28 LPHREEEIEELASALRPALRGERpsnvLIYGPTGTGKTAVAKYVLEELEEEAEERGVDvrvvyvncrqASTRYRV-LSRI 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 488230346 248 IAGAKFRGEFEER-------LKAVLKEVKKSDGRILLFIDEIHNIV 286
Cdd:COG1474 107 LEELGSGEDIPSTglstdelFDRLYEALDERDGVLVVVLDEIDYLV 152
|
|
| RecA-like_Yta7-like |
cd19517 |
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ... |
605-710 |
5.70e-03 |
|
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 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: 410925 [Multi-domain] Cd Length: 170 Bit Score: 38.64 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 605 LFLGPTGVGKTELAKALAENLFDSEDhmvriDMSEYMEKHA--VSRLVGappgyvgyEEGGQLT---EAVRRNPYTIVLL 679
Cdd:cd19517 38 LFHGPPGTGKTLMARALAAECSKGGQ-----KVSFFMRKGAdcLSKWVG--------EAERQLRllfEEAYRMQPSIIFF 104
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 488230346 680 DEI-----------EKAHPDVFNILLQVLDDgrlTDSKGRVV 710
Cdd:cd19517 105 DEIdglapvrsskqEQIHASIVSTLLALMDG---LDNRGQVV 143
|
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
185-305 |
6.41e-03 |
|
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is involved in binding ATP. There are eukaryote members as well as archaeal members in this family.
Pssm-ID: 376582 [Multi-domain] Cd Length: 222 Bit Score: 39.23 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 185 RDEEIRDVIRILSRKTkNNPVLI-GEPGVGKTAIVEGLAQRI------------VRKDVPENLKDKTIFS-LDMGALIAG 250
Cdd:pfam01637 4 REKELKELEEWAERGP-NLIYVIyGPEGCGKTALLRESIENLldlgyyviyydpLRRYFISKLDRFEEVRrLAEALGIAV 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 488230346 251 AKFRGEF----EERLKAVLKEVKKSDGRILLFIDEIHNIVGAGKtegsmdAGNLLKPML 305
Cdd:pfam01637 83 PKAELEEsklaFLAIELLLEALKRRGKKIAIIIDEVQQAIGLNG------AELLVKELL 135
|
|
| ClpX |
COG1219 |
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ... |
556-622 |
6.43e-03 |
|
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440832 [Multi-domain] Cd Length: 409 Bit Score: 40.03 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 556 EGEREKLIK---LNETLHKRVIGQDEAVDAVSDAV------IRSRAG------LQDPNrplgsFLFLGPTGVGKTELAKA 620
Cdd:COG1219 54 EEELKKLPKpkeIKAFLDEYVIGQERAKKVLSVAVynhykrLNSGSKddddveLEKSN-----ILLIGPTGSGKTLLAQT 128
|
..
gi 488230346 621 LA 622
Cdd:COG1219 129 LA 130
|
|
| hslU |
PRK05201 |
ATP-dependent protease ATPase subunit HslU; |
569-622 |
7.55e-03 |
|
ATP-dependent protease ATPase subunit HslU;
Pssm-ID: 235364 [Multi-domain] Cd Length: 443 Bit Score: 39.68 E-value: 7.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488230346 569 LHKRVIGQDEAVDAVSDAvIRSR-------AGLQD---PNrplgSFLFLGPTGVGKTELAKALA 622
Cdd:PRK05201 13 LDKYIIGQDDAKRAVAIA-LRNRwrrmqlpEELRDevtPK----NILMIGPTGVGKTEIARRLA 71
|
|
| COG1672 |
COG1672 |
Predicted ATPase, archaeal AAA+ ATPase superfamily [General function prediction only]; |
182-290 |
7.82e-03 |
|
Predicted ATPase, archaeal AAA+ ATPase superfamily [General function prediction only];
Pssm-ID: 441278 [Multi-domain] Cd Length: 324 Bit Score: 39.51 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 182 IIGRDEEIRDVIRILSRKTKNNPVLIGEPGVGKTAIV-EGLAQRIV------RKDVPENLKDktiFSLDMGALIAGAKFR 254
Cdd:COG1672 2 FFDREEELEELEKLYESDGGELVVVYGRRRVGKTSLIkEFLKEKPAiyfdarEESERESLRD---FSEALAEALGDPLSK 78
|
90 100 110
....*....|....*....|....*....|....*...
gi 488230346 255 GEFEErLKAVLKEVKK--SDGRILLFIDEIHNIVGAGK 290
Cdd:COG1672 79 KEFES-WEEAFEYLAElaEGKRLVIVIDEFQYLVKLDP 115
|
|
| TIGR02928 |
TIGR02928 |
orc1/cdc6 family replication initiation protein; Members of this protein family are found ... |
180-289 |
8.84e-03 |
|
orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 274354 [Multi-domain] Cd Length: 365 Bit Score: 39.15 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488230346 180 DPIIGRDEEIRDVIRILSR----KTKNNPVLIGEPGVGKTAIVEGLAQRIVR--KDVPENL--------KDKTIFSLdMG 245
Cdd:TIGR02928 15 DRIVHRDEQIEELAKALRPilrgSRPSNVFIYGKTGTGKTAVTKYVMKELEEaaEDRDVRVvtvyvncqILDTLYQV-LV 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 488230346 246 ALIAGAKFRGE--------FEERLKAVLKEVKKSDGRILLFIDEIHNIVGAG 289
Cdd:TIGR02928 94 ELANQLRGSGEevpttglsTSEVFRRLYKELNERGDSLIIVLDEIDYLVGDD 145
|
|
| |
