|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
1-857 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 1742.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 1 MRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSIRPLLTSAGINAGQLRTAIDQALSRLPQVEGTGGD 80
Cdd:PRK10865 1 MRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVRPLLTSAGINAGQLRTDINQALSRLPQVEGTGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 81 VQPSSELVRVLNLCDKLAQKRGDNFISSELFVLAALESRGTLTDLLKSAGATTANITQAIEQMRGGESVNDQGAEDQRQA 160
Cdd:PRK10865 81 VQPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAALESRGTLADILKAAGATTANITQAIEQMRGGESVNDQGAEDQRQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 161 LKKYTVDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLAL 240
Cdd:PRK10865 161 LKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 241 DMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYR 320
Cdd:PRK10865 241 DMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 321 QYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASS 400
Cdd:PRK10865 321 QYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 401 IRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELDDKERQYSELEEEWKAEKASLSGTQTIKAELE 480
Cdd:PRK10865 401 IRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKAELE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 481 QAKIAIEQARRVGDLARMSELQYGKIPELEKQLEAATQSEGKTMRLLRNKVTDAEIAEVLARWTGIPVARMLEGEREKLL 560
Cdd:PRK10865 481 QAKIAIEQARRVGDLARMSELQYGKIPELEKQLAAATQLEGKTMRLLRNKVTDAEIAEVLARWTGIPVSRMLESEREKLL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 561 RMEQELHSRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEK 640
Cdd:PRK10865 561 RMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEK 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 641 HSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNL 720
Cdd:PRK10865 641 HSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNL 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 721 GSDLIQERFGELDYGRMKEMVLGVVSQNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYEIHISDEAL 800
Cdd:PRK10865 721 GSDLIQERFGELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYEIHISDEAL 800
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720980328 801 KLLSANGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEANDDRIVAVQ 857
Cdd:PRK10865 801 KLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDDRIVAVQ 857
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
6-854 |
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: 1625.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSIRPLLTSAGINAGQLRTAIDQALSRLPQVEGTGGDVQPSS 85
Cdd:TIGR03346 1 LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEKELERLPKVSGPGGQVYLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 86 ELVRVLNLCDKLAQKRGDNFISSELFVLAALESRGTLTDLLKSAGATTANITQAIEQMRGGESVNDQGAEDQRQALKKYT 165
Cdd:TIGR03346 81 DLNRLLNLAEKLAQKRGDEFISSEHLLLALLDDKGTLGKLLKEAGATADALEAAINAVRGGQKVTDANAEDQYEALEKYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 166 VDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLALDMGAL 245
Cdd:TIGR03346 161 RDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLALDMGAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 246 VAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYRQYIEK 325
Cdd:TIGR03346 241 IAGAKYRGEFEERLKAVLNEVTKSEGQIILFIDELHTLVGAGKAEGAMDAGNMLKPALARGELHCIGATTLDEYRKYIEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 326 DAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASSIRMQI 405
Cdd:TIGR03346 321 DAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAARIRMEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 406 DSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELDDKERQYSELEEEWKAEKASLSGTQTIKAELEQAKIA 485
Cdd:TIGR03346 401 DSKPEELDELDRRIIQLEIEREALKKEKDEASKKRLEDLEKELADLEEEYAELEEQWKAEKASIQGIQQIKEEIEQVRLE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 486 IEQARRVGDLARMSELQYGKIPELEKQLEAATQSEGKTM-RLLRNKVTDAEIAEVLARWTGIPVARMLEGEREKLLRMEQ 564
Cdd:TIGR03346 481 LEQAEREGDLAKAAELQYGKLPELEKQLQAAEQKLGEEQnRLLREEVTAEEIAEVVSRWTGIPVSKMLEGEREKLLHMEE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 565 ELHSRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEKHSVS 644
Cdd:TIGR03346 561 ELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRIDMSEYMEKHSVA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 645 RLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNLGSDL 724
Cdd:TIGR03346 641 RLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDF 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 725 IQERFGELDYGRMKEMVLGVVSQNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYEIHISDEALKLLS 804
Cdd:TIGR03346 721 IQELAGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKITLELSDAALDFLA 800
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 1720980328 805 ANGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEANDDRIV 854
Cdd:TIGR03346 801 EAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGRLV 850
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1-854 |
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: 1505.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 1 MRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSIRPLLTSAGINAGQLRTAIDQALSRLPQVEGTGGD 80
Cdd:COG0542 1 MNFEKFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGRLPKVSGSSGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 81 VQPSSELVRVLNLCDKLAQKRGDNFISSELFVLAAL-ESRGTLTDLLKSAGATTANITQAIEQMRGGESVNDQGAEDQRQ 159
Cdd:COG0542 81 PYLSPRLKRVLELAELEARKLGDEYISTEHLLLALLrEGEGVAARILKKLGITLEALREALEELRGGSRVTSQNPESKTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 160 ALKKYTVDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLA 239
Cdd:COG0542 161 ALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDKRVLS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 240 LDMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEY 319
Cdd:COG0542 241 LDLGALVAGAKYRGEFEERLKAVLDEVKKSEGNIILFIDELHTLVGAGGAEGAMDAANLLKPALARGELRCIGATTLDEY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 320 RQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAAS 399
Cdd:COG0542 321 RKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAIDLIDEAAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 400 SIRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELDDKERQYSELEEEWKAEKASLSGTQTIKAEL 479
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 480 EQakiaieqarrvgdlarmselQYGKIPELEKQLEAATQSEGKTMRLLRNKVTDAEIAEVLARWTGIPVARMLEGEREKL 559
Cdd:COG0542 481 EQ--------------------RYGKIPELEKELAELEEELAELAPLLREEVTEEDIAEVVSRWTGIPVGKLLEGEREKL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 560 LRMEQELHSRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFME 639
Cdd:COG0542 541 LNLEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYME 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 640 KHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSN 719
Cdd:COG0542 621 KHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSN 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 720 LGSDLIQERFGE-LDYGRMKEMVLGVVSQNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYEIHISDE 798
Cdd:COG0542 701 IGSELILDLAEDePDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDA 780
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720980328 799 ALKLLSANGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEANDDRIV 854
Cdd:COG0542 781 AKDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGELV 836
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
17-856 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 870.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 17 AQSLA--LGHDnqFIEPLHLMSALLNQEGGSIRPLLTSAGINAGQLRTAIDQALSRlpqvegtgGDVQPSSEL------V 88
Cdd:CHL00095 16 SQEEArrLGHN--FVGTEQILLGLIGEGTGIAARALKSMGVTLKDARIEVEKIIGR--------GTGFVAVEIpftpraK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 89 RVLNLCDKLAQKRGDNFISSELFVLAAL-ESRGTLTDLLKSAGATTANITQAIEQMRGGESVNDQGAEDQRQ---ALKKY 164
Cdd:CHL00095 86 RVLEMSLEEARDLGHNYIGTEHLLLALLeEGEGVAARVLENLGVDLSKIRSLILNLIGEIIEAILGAEQSRSktpTLEEF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 165 TVDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLALDMGA 244
Cdd:CHL00095 166 GTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDKLVITLDIGL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 245 LVAGAKYRGEFEERLKGVLNDLaKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYRQYIE 324
Cdd:CHL00095 246 LLAGTKYRGEFEERLKRIFDEI-QENNNIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLDEYRKHIE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 325 KDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASSIRMQ 404
Cdd:CHL00095 325 KDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLDEAGSRVRLI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 405 IDSKPEELDRLDRriiqlklEQQALMKESDEASKKRLDMLNEELDDKERqyseleeewkaekaslsgtqtikaeleqaki 484
Cdd:CHL00095 405 NSRLPPAARELDK-------ELREILKDKDEAIREQDFETAKQLRDREM------------------------------- 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 485 aieqarrvgdlarmselqygkipELEKQLEAATQS--EGKTMRLLRNKVTDAEIAEVLARWTGIPVARMLEGEREKLLRM 562
Cdd:CHL00095 447 -----------------------EVRAQIAAIIQSkkTEEEKRLEVPVVTEEDIAEIVSAWTGIPVNKLTKSESEKLLHM 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 563 EQELHSRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEKHS 642
Cdd:CHL00095 504 EETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALASYFFGSEDAMIRLDMSEYMEKHT 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 643 VSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNLGS 722
Cdd:CHL00095 584 VSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGS 663
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 723 DLIQERFGEL------------DYGRMKEMVLGVVSQNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERG 790
Cdd:CHL00095 664 KVIETNSGGLgfelsenqlsekQYKRLSNLVNEELKQFFRPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQG 743
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720980328 791 YEIHISDEALKLLSANGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEANDDRIVAV 856
Cdd:CHL00095 744 IQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVDVNDEKEVKI 809
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
6-835 |
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: 786.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSIRPLLTSAGINAGQLRTAIDQALSRLPQveGTGGDVQPSS 85
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLARALDKLPR--GNTRTPVFSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 86 ELVRVLNLCDKLAQKR-GDNFISSELFVLAALES---RGTLTDLLKS-AGATTANITQAIEQMRGGESVNDQGAED---- 156
Cdd:TIGR03345 79 HLVELLQEAWLLASLElGDGRIRSGHLLLALLTDpelRRLLGSISPElAKIDREALREALPALVEGSAEASAAAADaapa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 157 -------QRQALKKYTVDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVP 229
Cdd:TIGR03345 159 gaaagaaGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 230 EGLKGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELH 309
Cdd:TIGR03345 239 PALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPIILFIDEAHTLIGAGGQAGQGDAANLLKPALARGELR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 310 CVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDK 389
Cdd:TIGR03345 319 TIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLPDK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 390 AIDLIDEAASSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKES--DEASKKRLDMLNEELDDKERQYSELEEEWKAEKA 467
Cdd:TIGR03345 399 AVSLLDTACARVALSQNATPAALEDLRRRIAALELELDALEREAalGADHDERLAELRAELAALEAELAALEARWQQEKE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 468 SLSGTQTIKAELEQAkiaiEQARRVGDLARMSELQygkipELEKQLEAATQSEgktmRLLRNKVTDAEIAEVLARWTGIP 547
Cdd:TIGR03345 479 LVEAILALRAELEAD----ADAPADDDDALRAQLA-----ELEAALASAQGEE----PLVFPEVDAQAVAEVVADWTGIP 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 548 VARMLEGEREKLLRMEQELHSRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDD 627
Cdd:TIGR03345 546 VGRMVRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGEQ 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 628 AMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTV 707
Cdd:TIGR03345 626 NLITINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREI 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 708 DFRNTVVIMTSNLGSDLIQERFGELDYG----RMKEMVLGVVSQNFRPEFINRIdEVVVFHPLGEQHIASIAQIQLQRLY 783
Cdd:TIGR03345 706 DFKNTVILLTSNAGSDLIMALCADPETApdpeALLEALRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRIA 784
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1720980328 784 KRLEER-GYEIHISDEALKLLSANGYDPVYGARPLKRAIQQQIENPLAQQILS 835
Cdd:TIGR03345 785 RRLKENhGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQILE 837
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
6-848 |
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: 761.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGsiRPLLTSAGINAGQLRTAIDQALS-RLPQ-VEGTGGDVQP 83
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEA--IEILEECGGDVELLRKRLEDYLEeNLPViPEDIDEEPEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 84 SSELVRVLNLCDKLAQKRGDNFISsELFVLAAL--ESRGTLTDLLKSAGATTANITQAI-EQMRGGESVNDQGA------ 154
Cdd:TIGR02639 79 TVGVQRVIQRALLHVKSAGKKEID-IGDLLVALfdEEDSHASYFLKSQGITRLDILNYIsHGISKDDGKDQLGEeagkee 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 155 EDQRQALKKYTVDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKG 234
Cdd:TIGR02639 158 EKGQDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERLKN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 235 RRVLALDMGALVAGAKYRGEFEERLKGVLNDLAKQEgNVILFIDELHTMVGAGK-ADGAMDAGNMLKPALARGELHCVGA 313
Cdd:TIGR02639 238 AKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEP-NAILFIDEIHTIVGAGAtSGGSMDASNLLKPALSSGKIRCIGS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 314 TTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDL 393
Cdd:TIGR02639 317 TTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 394 IDEAASSIRMQIDSKPEEldrldrriiqlkleqqalmkesdeaskkrldmlneelddkerqyseleeewkaekaslsgtq 473
Cdd:TIGR02639 397 IDEAGAAFRLRPKAKKKA-------------------------------------------------------------- 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 474 tikaeleqakiaieqarrvgdlarmselqygkipelekqleaatqsegktmrllrnKVTDAEIAEVLARWTGIPVARMLE 553
Cdd:TIGR02639 415 --------------------------------------------------------NVNVKDIENVVAKMAKIPVKTVSS 438
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 554 GEREKLLRMEQELHSRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMfdsDDAMVRID 633
Cdd:TIGR02639 439 DDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEEL---GVHLLRFD 515
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 634 MSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTV 713
Cdd:TIGR02639 516 MSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVI 595
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 714 VIMTSNLGSDLIQERFGELDYGRMKEMVLGVVSQNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYEI 793
Cdd:TIGR02639 596 LIMTSNAGASEMSKPPIGFGGENRESKSLKAIKKLFSPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIEL 675
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 1720980328 794 HISDEALKLLSANGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEA 848
Cdd:TIGR02639 676 ELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEILFGKLKKGGSVKISL 730
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
6-852 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 552.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLnqEGGSIRPLLTSAGINAGQLRTA----IDQALSRLPQVEGTGgDV 81
Cdd:PRK11034 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALL--SNPSAREALEACSVDLVALRQEleafIEQTTPVLPASEEER-DT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 82 QPSSELVRVLNLCDKLAQKRGDNFISSElFVLAAL--ESRGTLTDLLK-------------SAGATTANITQAIEQMRGG 146
Cdd:PRK11034 79 QPTLSFQRVLQRAVFHVQSSGRSEVTGA-NVLVAIfsEQESQAAYLLRkhevsrldvvnfiSHGTRKDEPSQSSDPGSQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 147 ESVNDQGAEDQrqaLKKYTVDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIING 226
Cdd:PRK11034 158 NSEEQAGGEER---MENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 227 EVPEGLKGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLaKQEGNVILFIDELHTMVGAGKADGA-MDAGNMLKPALAR 305
Cdd:PRK11034 235 DVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQL-EQDTNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 306 GELHCVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQ 385
Cdd:PRK11034 314 GKIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 386 LPDKAIDLIDEAASSIRMQidskpeeldrldrriiqlkleqqalmkesdEASKKRldmlneelddkerqyseleeewkae 465
Cdd:PRK11034 394 LPDKAIDVIDEAGARARLM------------------------------PVSKRK------------------------- 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 466 kaslsgtqtikaeleqakiaieqarrvgdlarmselqygkipelekqleaatqsegKTmrllrnkVTDAEIAEVLARWTG 545
Cdd:PRK11034 419 --------------------------------------------------------KT-------VNVADIESVVARIAR 435
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 546 IPVARMLEGEREKLLRMEQELHSRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMfds 625
Cdd:PRK11034 436 IPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL--- 512
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 626 DDAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGR 705
Cdd:PRK11034 513 GIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGR 592
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 706 TVDFRNTVVIMTSNLGSDLIQERFGELDYGRMKEMVLGVVSQNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKR 785
Cdd:PRK11034 593 KADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQ 672
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720980328 786 LEERGYEIHISDEALKLLSANGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEANDDR 852
Cdd:PRK11034 673 LDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKEK 739
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
558-763 |
1.81e-112 |
|
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: 340.69 E-value: 1.81e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 558 KLLRMEQELHSRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEF 637
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 638 MEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMT 717
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720980328 718 SNlgsdliqerfgeldygrmkemvlgvvsqNFRPEFINRIDEVVVF 763
Cdd:cd19499 161 SN----------------------------HFRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
596-760 |
2.35e-94 |
|
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: 292.95 E-value: 2.35e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 596 RPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVIL 675
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 676 LDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNLGSDLIQERFG---ELDYGRMKEMVLGVVSQNFRPE 752
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRlgdSPDYELLKEEVMDLLKKGFIPE 160
|
....*...
gi 1720980328 753 FINRIDEV 760
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 ... |
342-445 |
1.13e-46 |
|
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: 161.50 E-value: 1.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 342 SVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASSIRMQIDSKPEELDRLDRRIIQ 421
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|....
gi 1720980328 422 LKLEQQALMKESDEASKKRLDMLN 445
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, ... |
766-846 |
7.59e-31 |
|
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: 115.97 E-value: 7.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 766 LGEQHIASIAQIQLQRLYKRLEERGYEIHISDEALKLLSANGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIR 845
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 1720980328 846 L 846
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, ... |
766-854 |
3.87e-28 |
|
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: 108.30 E-value: 3.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 766 LGEQHIASIAQIQLQRLYKRLEERGYEIHISDEALKLLSANGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIR 845
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
....*....
gi 1720980328 846 LEANDDRIV 854
Cdd:smart01086 81 VDVDDGELV 89
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
181-341 |
1.69e-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: 94.52 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 181 IGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINgevpeglKGRRVLALDMGALVAGAKYRGEFEERLK 260
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFR-------PGAPFLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 261 GVLNDLAKQEGNVILFIDELHTMVGAGKADG--AMDAGNMLKPalARGELHCVGATTLDEYRQyieKDAALERRFQKVFV 338
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDSLSRGAQNALlrVLETLNDLRI--DRENVRVIGATNRPLLGD---LDRALYDRLDIRIV 148
|
...
gi 1720980328 339 AEP 341
Cdd:cd00009 149 IPL 151
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
571-765 |
3.02e-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: 87.97 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 571 IGQNEAVEAVSNAIRRsraglsdpnRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEKHSVSRLVGAP 650
Cdd:cd00009 1 VGQEEAIEALREALEL---------PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 651 PGYVgyeeggyLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTdgqgrTVDFRNTVVIMTSNLGSDLIqerfg 730
Cdd:cd00009 72 LVRL-------LFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATNRPLLGD----- 134
|
170 180 190
....*....|....*....|....*....|....*
gi 1720980328 731 eldygrmkemvlgvvsqnFRPEFINRIDEVVVFHP 765
Cdd:cd00009 135 ------------------LDRALYDRLDIRIVIPL 151
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
602-725 |
3.85e-14 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 70.48 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 602 LFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGY----LTEAVRRRPYSVILLD 677
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1720980328 678 EVEKAHPDVFNILLQVLDDGRLTDGQGRtvdFRNTVVIMTSNLGSDLI 725
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTNDEKDLG 130
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
204-337 |
1.56e-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: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 204 LIGEPGVGKTAIVEGLAQRIingevpeglkGRRVLALDMGALVagAKYRGEFEERLKGVLnDLAKQEGNVILFIDELHTM 283
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELV--SKYVGESEKRLRELF-EAAKKLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720980328 284 VGAGKADG---AMDAGNMLKPAL-----ARGELHCVGATTldeyrqYIEK-DAALERRFQKVF 337
Cdd:pfam00004 70 AGSRGSGGdseSRRVVNQLLTELdgftsSNSKVIVIAATN------RPDKlDPALLGRFDRII 126
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
37-382 |
1.01e-11 |
|
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: 67.63 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 37 ALLNQEGGSIRPLLTSAGINAGQLRTAIDQALSRLPQVEGTGGDVQPSSELVRVLNLCDKLAQKRGDNFISSELFVLAAL 116
Cdd:COG0464 16 LLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 117 ESRGTLTDLLKSAGATTANITQAIEQMRGGESVNDQGAEDQRQALKKYTVDLTERAEQGKLDPVIGRDE---EIRRTIQV 193
Cdd:COG0464 96 ELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEvkeELRELVAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 194 LQRRTK-------NNP---VLIGEPGVGKTAIVEGLAQRIingevpeglkGRRVLALDMGALVagAKYRGEFEERLKGVL 263
Cdd:COG0464 176 PLKRPElreeyglPPPrglLLYGPPGTGKTLLARALAGEL----------GLPLIEVDLSDLV--SKYVGETEKNLREVF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 264 nDLAKQEGNVILFIDELHTMVGA--GKADGAMDA--GNMLKpALA--RGELHCVGATtldeYRqyIEK-DAALERRFQ-K 335
Cdd:COG0464 244 -DKARGLAPCVLFIDEADALAGKrgEVGDGVGRRvvNTLLT-EMEelRSDVVVIAAT----NR--PDLlDPALLRRFDeI 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1720980328 336 VFVAEPSVEDTIAILRGLKERYELHHHVqitDPAIVAAAT--LSHRYIA 382
Cdd:COG0464 316 IFFPLPDAEERLEIFRIHLRKRPLDEDV---DLEELAEATegLSGADIR 361
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
600-719 |
2.19e-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: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 600 SFLFLGPTGVGKTELCKALANFMFDSDDAMVRidMSEFMEKhsvSRLVGA--PPGYVGYEEGGYLTEAVRRRpySVILLD 677
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQ--LTRDTTE---EDLFGRrnIDPGGASWVDGPLVRAAREG--EIAVLD 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1720980328 678 EVEKAHPDVFNILLQVLDDGRLTDGQGRT---VDFRNTVVIMTSN 719
Cdd:pfam07728 74 EINRANPDVLNSLLSLLDERRLLLPDGGElvkAAPDGFRLIATMN 118
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
575-733 |
2.21e-11 |
|
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: 62.69 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 575 EAVEAVSNAIRRSRAGLsdpNRPIGsFLFLGPTGVGKTELCKALANfmfDSDDAMVRIDMSEFMEKHSvsrlvgappgYV 654
Cdd:cd19481 7 EAVEAPRRGSRLRRYGL---GLPKG-ILLYGPPGTGKTLLAKALAG---ELGLPLIVVKLSSLLSKYV----------GE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 655 GYEEGGYLTEAVRRRPYSVILLDEVEKAHPD------------VFNILLQVLDDGRLTDgqgrtvdfrNTVVIMTSNLGS 722
Cdd:cd19481 70 SEKNLRKIFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAATNRPD 140
|
170
....*....|...
gi 1720980328 723 DLIQE--RFGELD 733
Cdd:cd19481 141 LLDPAllRPGRFD 153
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
17-69 |
3.95e-11 |
|
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: 58.69 E-value: 3.95e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720980328 17 AQSLALGHDNQFIEPLHLMSALLNQEGGSIRPLLTSAGINAGQLRTAIDQALS 69
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
602-719 |
6.89e-10 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 57.60 E-value: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 602 LFLGPTGVGKTELCKALANfmfDSDDAMVRIDMSEFMEKHsvsrlVGAPPGYVgyeeGGYLTEAVRRRPySVILLDEVEK 681
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAK---ELGAPFIEISGSELVSKY-----VGESEKRL----RELFEAAKKLAP-CVIFIDEIDA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1720980328 682 AHP-----------DVFNILLQVLDdgrltdgqGRTVDFRNTVVIMTSN 719
Cdd:pfam00004 69 LAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
94-145 |
4.12e-08 |
|
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: 50.21 E-value: 4.12e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720980328 94 CDKLAQKRGDNFISSELFVLAAL-ESRGTLTDLLKSAGATTANITQAIEQMRG 145
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLeEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
410-781 |
4.36e-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: 56.46 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 410 EELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELDDKERQYSELEEEWKAEKASLSGTQTIKAELEQAKIAIEQA 489
Cdd:COG0464 4 LLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 490 RRVGDLARMSELqygkipELEKQLEAATQSEGKTMRLLRNKVTDAEIAEVLARWTGIPVARMLEGEREKLLRMEQELH-S 568
Cdd:COG0464 84 ALLSALELLLLG------ELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAIlD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 569 RVIGQNEAVEAVSNAI--------RRSRAGLsdpnRPIGSFLFLGPTGVGKTELCKALANfmfDSDDAMVRIDMSEFMEK 640
Cdd:COG0464 158 DLGGLEEVKEELRELValplkrpeLREEYGL----PPPRGLLLYGPPGTGKTLLARALAG---ELGLPLIEVDLSDLVSK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 641 hsvsrlvgappgYVGyEEGGYLTEAV---RRRPYSVILLDEVEKAHPD-----------VFNILLQVLDDGRltdgqgrt 706
Cdd:COG0464 231 ------------YVG-ETEKNLREVFdkaRGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR-------- 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720980328 707 vdfRNTVVIMTSNlgsdliqeRFGELDygrmkemvlgvvsqnfrPEFINRIDEVVVFHPLGEQHIASIAQIQLQR 781
Cdd:COG0464 290 ---SDVVVIAATN--------RPDLLD-----------------PALLRRFDEIIFFPLPDAEERLEIFRIHLRK 336
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
198-341 |
2.31e-07 |
|
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: 50.83 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 198 TKNNPVLIGEPGVGKTAIVEGLAQRI---------INGEVPEglkgRRVLALDMGALVAGAKYRGEFEERLKGVLnDLAK 268
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELgppgggviyIDGEDIL----EEVLDQLLLIIVGGKKASGSGELRLRLAL-ALAR 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720980328 269 QEGNVILFIDELHTMVGAG--KADGAMDAGNMLKPALARGELHCVGATTLDEyrqyIEKDAALERRFQKVFVAEP 341
Cdd:smart00382 76 KLKPDVLILDEITSLLDAEqeALLLLLEELRLLLLLKSEKNLTVILTTNDEK----DLGPALLRRRFDRRIVLLL 146
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
564-681 |
1.63e-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: 49.30 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 564 QELHSRVIGQNEAVEAVS----NAIRRSR--AGLSDPNRPiGSFLFLGPTGVGKTELCKALANFMfdsDDAMVRIDMSEF 637
Cdd:cd19498 7 SELDKYIIGQDEAKRAVAialrNRWRRMQlpEELRDEVTP-KNILMIGPTGVGKTEIARRLAKLA---GAPFIKVEATKF 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1720980328 638 MEKhsvsrlvgappGYVGYEeggyLTEAVRRRPYSVILLDEVEK 681
Cdd:cd19498 83 TEV-----------GYVGRD----VESIIRDLVEGIVFIDEIDK 111
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
388-591 |
7.25e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 388 DKAIDLIDEAASSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEAsKKRLDMLNEELDDKERQYSELEEEWKAEKA 467
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL-EEELEELEEELEELEEELEEAEEELEEAEA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 468 SLSGTQTIKAELEQAKIAIEQARRVGDLARMSELQyGKIPELEKQLEAATQSEGKTMRLLRNKVTDAEIAEVLARwtgip 547
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALR-AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE----- 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720980328 548 vARMLEGEREKLLRMEQELHSRVIGQNEAVEAVSNAIRRSRAGL 591
Cdd:COG1196 433 -LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
410-591 |
8.51e-06 |
|
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: 49.67 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 410 EELDRLDRRIIQLKLEQQALMKESDEAS------KKRLDMLNEELDDKERQYSELEEEWKAEKASLSGTQTIKAELEQAK 483
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEaqleelESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 484 IAIE-----QARRVGDLARMSELQYGKIPELEKQLEAATQSEGKT---MRLLRNKVTDAEIAEVLARWTGIpvARMLEGE 555
Cdd:TIGR02168 375 EELEeqletLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqqeIEELLKKLEEAELKELQAELEEL--EEELEEL 452
|
170 180 190
....*....|....*....|....*....|....*.
gi 1720980328 556 REKLLRMEQELHSrvigQNEAVEAVSNAIRRSRAGL 591
Cdd:TIGR02168 453 QEELERLEEALEE----LREELEEAEQALDAAEREL 484
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
203-333 |
1.64e-05 |
|
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: 45.36 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 203 VLIGEPGVGKTAIVEGLAQRIINGEV----------PEGLKGRRVLALDMGALVAGAKYRgEFEERLKGVLNDLAKQEGN 272
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSNRPVfyvqltrdttEEDLFGRRNIDPGGASWVDGPLVR-AAREGEIAVLDEINRANPD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720980328 273 VilfIDELHTmvgagkadgAMDAGNMLKPALaRGELHC------VGATTLDEYRQYIEKDAALERRF 333
Cdd:pfam07728 82 V---LNSLLS---------LLDERRLLLPDG-GELVKAapdgfrLIATMNPLDRGLNELSPALRSRF 135
|
|
| AtoC |
COG2204 |
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ... |
548-805 |
3.52e-05 |
|
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];
Pssm-ID: 441806 [Multi-domain] Cd Length: 418 Bit Score: 47.27 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 548 VARMLEGEReklLRMEQELHSRVIGQNEAVEAVSNAIRRsragLSDPNRPIgsfLFLGPTGVGKTELCKALANFMFDSDD 627
Cdd:COG2204 114 VERALERRR---LRRENAEDSGLIGRSPAMQEVRRLIEK----VAPSDATV---LITGESGTGKELVARAIHRLSPRADG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 628 AMVRIDMSEFMEKHSVSRLVGAppgyvgyeEGGYLTEAVRRRPYSV-------ILLDEVEKAHPDVFNILLQVLDDG--- 697
Cdd:COG2204 184 PFVAVNCAAIPEELLESELFGH--------EKGAFTGAVARRIGKFeladggtLFLDEIGEMPLALQAKLLRVLQERefe 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 698 RLTDGQGRTVDFRntvVIMTSNLgsDLIQErfgeldygrmkemvlgVVSQNFRPEFINRIDEVVVFHP-LGEQH--IASI 774
Cdd:COG2204 256 RVGGNKPIPVDVR---VIAATNR--DLEEL----------------VEEGRFREDLYYRLNVFPIELPpLRERRedIPLL 314
|
250 260 270
....*....|....*....|....*....|.
gi 1720980328 775 AQIQLQRLYKRLeerGYEIHISDEALKLLSA 805
Cdd:COG2204 315 ARHFLARFAAEL---GKPVKLSPEALEALLA 342
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
415-519 |
7.20e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 415 LDRRIIQ----------LKLEQqalMKESDEASKKRLDMLNEELDDKERQYSELEEEWKAEKASLSGT-QTIKAELEQ-A 482
Cdd:PRK00409 499 LPENIIEeakkligedkEKLNE---LIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEeDKLLEEAEKeA 575
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1720980328 483 KIAIEQARRVGD--LARMSELQYGKIPEL-EKQLEAATQS 519
Cdd:PRK00409 576 QQAIKEAKKEADeiIKELRQLQKGGYASVkAHELIEARKR 615
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
600-698 |
7.57e-05 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 43.10 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 600 SFLFL-GPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEK----HSVSRLVGAPPGYVGYEEG--GYLTEAVRRRP-Y 671
Cdd:pfam13401 6 GILVLtGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPkdllRALLRALGLPLSGRLSKEEllAALQQLLLALAvA 85
|
90 100
....*....|....*....|....*..
gi 1720980328 672 SVILLDEVEKAHPDVFNILLQVLDDGR 698
Cdd:pfam13401 86 VVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
401-591 |
1.67e-04 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 401 IRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKrldmLNEELDDKERQYSELEEEWKAEKASLSGTQTIKA-EL 479
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK----IKDLGEEEQLRVKEKIGELEAEIASLERSIAEKErEL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 480 EQA--KIAIEQARRVGDLARMSELQyGKIPELEK---QLEAATQSEGKTMRLLRNKVtdAEIAEVLARWTGIPVAR---- 550
Cdd:TIGR02169 318 EDAeeRLAKLEAEIDKLLAEIEELE-REIEEERKrrdKLTEEYAELKEELEDLRAEL--EEVDKEFAETRDELKDYrekl 394
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720980328 551 -MLEGEREKLLRMEQELHSRVIGQNEAVEAVSNAIRRSRAGL 591
Cdd:TIGR02169 395 eKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
204-283 |
2.04e-04 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 42.66 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 204 LIGEPGVGKTAIVEGLAQRIingevpeglkGRRVLALDMGALVagAKYRGEFEERLKGVLnDLAKQEGNVILFIDELHTM 283
Cdd:cd19481 31 LYGPPGTGKTLLAKALAGEL----------GLPLIVVKLSSLL--SKYVGESEKNLRKIF-ERARRLAPCILFIDEIDAI 97
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
179-281 |
2.20e-04 |
|
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: 42.88 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 179 PVIGRDEEIRRTIQVLQRRTKNNP---VLIGEPGVGKTAIVEGLAQR----------------IINGEVPEGLKGRRVLA 239
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRAlerdggyflrgkcdenLPYSPLLEALTREGLLR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720980328 240 --LDMGALVAGAKYRGEFEERLKGV------------------LNDLAKQEGNVILFIDELH 281
Cdd:pfam13191 81 qlLDELESSLLEAWRAALLEALAPVpelpgdlaerlldlllrlLDLLARGERPLVLVLDDLQ 142
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
391-491 |
2.85e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 391 IDLIDEAASSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASK------KRLDMLNEELDDKERQYSELEEEWKA 464
Cdd:COG1340 169 LKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKeiveaqEKADELHEEIIELQKELRELRKELKK 248
|
90 100 110
....*....|....*....|....*....|
gi 1720980328 465 --EKASLSGTQTIKAEL-EQAKIAIEQARR 491
Cdd:COG1340 249 lrKKQRALKREKEKEELeEKAEEIFEKLKK 278
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
323-533 |
4.33e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 323 IEKDAALERR----FQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLsHRYIADRQlpdkaidliDEaa 398
Cdd:COG4913 609 RAKLAALEAElaelEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA-EREIAELE---------AE-- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 399 ssiRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRlDMLNEELDDKERQYSELEEEwkAEKASLSGTQTIKAE 478
Cdd:COG4913 677 ---LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEI-GRLEKELEQAEEELDELQDR--LEAAEDLARLELRAL 750
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720980328 479 LEQAKIAIEQARRVGDLARmselqygkipELEKQLEAATQSEGKTMRLLRNKVTD 533
Cdd:COG4913 751 LEERFAAALGDAVERELRE----------NLEERIDALRARLNRAEEELERAMRA 795
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
204-280 |
5.74e-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: 41.51 E-value: 5.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720980328 204 LIGEPGVGKTAIVEGLAQRIingevpeglkGRRVLALDMGALVagAKYRGEFEERLKGVLNDlAKQEGNVILFIDEL 280
Cdd:cd19503 39 LHGPPGTGKTLLARAVANEA----------GANFLSISGPSIV--SKYLGESEKNLREIFEE-ARSHAPSIIFIDEI 102
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
508-680 |
9.95e-04 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 42.30 E-value: 9.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 508 ELEKQLEAATQSEGKTMRLLRNKVTDAEIAEVLARWTGIPVARMLEGEREKLlRMEQelhsrVIGQNEAVEAVSNAI--- 584
Cdd:COG1222 24 RLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDV-TFDD-----IGGLDEQIEEIREAVelp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 585 -----RRSRAGLsdpnRPIGSFLFLGPTGVGKTELCKALANfmfDSDDAMVRIDMSEFMEKhsvsrlvgappgYVGyeEG 659
Cdd:COG1222 98 lknpeLFRKYGI----EPPKGVLLYGPPGTGKTLLAKAVAG---ELGAPFIRVRGSELVSK------------YIG--EG 156
|
170 180
....*....|....*....|....*.
gi 1720980328 660 GYL-----TEAVRRRPySVILLDEVE 680
Cdd:COG1222 157 ARNvrevfELAREKAP-SIIFIDEID 181
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
347-551 |
9.96e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 347 IAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRqlpdkAIDLIDEAASSIRMQIDSKPEELDRLDRRIIQLKLEQ 426
Cdd:COG4913 251 IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR-----RLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 427 QALMKESDEASKKRLDMLNEELDDKERQYSELEEEWK-----AEKASLSGTQTIKAELEQAKIAIEQARRVGD-LARMSE 500
Cdd:COG4913 326 DELEAQIRGNGGDRLEQLEREIERLERELEERERRRArlealLAALGLPLPASAEEFAALRAEAAALLEALEEeLEALEE 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720980328 501 LQYGKIPELEKQLEAATQSEGKTMRLLRNKVT-DAEIAEV---LARWTGIPVARM 551
Cdd:COG4913 406 ALAEAEAALRDLRRELRELEAEIASLERRKSNiPARLLALrdaLAEALGLDEAEL 460
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
568-619 |
1.21e-03 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 42.10 E-value: 1.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720980328 568 SRVIGQNEAVEAVSNAIRRSRaglsdpnrpIG-SFLFLGPTGVGKTELCKALA 619
Cdd:COG2812 10 DDVVGQEHVVRTLKNALASGR---------LAhAYLFTGPRGVGKTTLARILA 53
|
|
| PRK08116 |
PRK08116 |
hypothetical protein; Validated |
601-752 |
1.65e-03 |
|
hypothetical protein; Validated
Pssm-ID: 236153 [Multi-domain] Cd Length: 268 Bit Score: 41.16 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 601 FLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMekhsvSRLVGAPPGYVGYEEGGYLTEAVRrrpYSVILLDE-- 678
Cdd:PRK08116 117 LLLWGSVGTGKTYLAACIANELIEKGVPVIFVNFPQLL-----NRIKSTYKSSGKEDENEIIRSLVN---ADLLILDDlg 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 679 VEK----AHPDVFNILlqvldDGRLTDGQGrtvdfrntvVIMTSNLGSDLIQERFGELDYGRMKEMVLGV--VSQNFRPE 752
Cdd:PRK08116 189 AERdtewAREKVYNII-----DSRYRKGLP---------TIVTTNLSLEELKNQYGKRIYDRILEMCTPVenEGKSYRKE 254
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
98-375 |
1.78e-03 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 41.53 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 98 AQKRGDNFISSELFVLAALESRG-TLTDLLKSAGATTANITQAIEqmrggESVNDQGAEDQRQALKKYTVDLTERAEQgK 176
Cdd:COG1222 3 DLLTIDENIKALLALIDALQERLgVELALLLQPVKALELLEEAPA-----LLLNDANLTQKRLGTPRGTAVPAESPDV-T 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 177 LDPVIGRDEEIRRTIQVLQRRTKNN---------PV----LIGEPGVGKTAIVEGLAQRIingevpeglkGRRVLALDMG 243
Cdd:COG1222 77 FDDIGGLDEQIEEIREAVELPLKNPelfrkygiePPkgvlLYGPPGTGKTLLAKAVAGEL----------GAPFIRVRGS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 244 ALVAgaKYRGEFEERLKGVLnDLAKQEGNVILFIDELHTMvgAGKADGAMDAG--NMLKPAL--------ARGELHCVGA 313
Cdd:COG1222 147 ELVS--KYIGEGARNVREVF-ELAREKAPSIIFIDEIDAI--AARRTDDGTSGevQRTVNQLlaeldgfeSRGDVLIIAA 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720980328 314 TtldeyrQYIEK-DAALER--RF-QKVFVAEPSVEDTIAILRGLKERYELHHHVqitDPAIVAAAT 375
Cdd:COG1222 222 T------NRPDLlDPALLRpgRFdRVIEVPLPDEEAREEILKIHLRDMPLADDV---DLDKLAKLT 278
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
570-696 |
1.78e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 41.02 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 570 VIGQNEAVEAVSNAIR-------RSRAGLSDPNRpigsFLFLGPTGVGKTELCKALAN---FMFdsddAMVRID--MSEF 637
Cdd:COG1223 4 VVGQEEAKKKLKLIIKelrrrenLRKFGLWPPRK----ILFYGPPGTGKTMLAEALAGelkLPL----LTVRLDslIGSY 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720980328 638 MEKhSVSRLVGappgyvgyeeggyLTEAVRRRPySVILLDEVE---------KAHPD---VFNILLQVLDD 696
Cdd:COG1223 76 LGE-TARNLRK-------------LFDFARRAP-CVIFFDEFDaiakdrgdqNDVGEvkrVVNALLQELDG 131
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
407-490 |
2.25e-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: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 407 SKPEELDRLDRRIIQLKLEQQALMKESDEAsKKRLDMLNEELDDKERQYSELEEEWKAEKASLsgtQTIKAELEQAKIAI 486
Cdd:COG1579 86 RNNKEYEALQKEIESLKRRISDLEDEILEL-MERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAELEEL 161
|
....
gi 1720980328 487 EQAR 490
Cdd:COG1579 162 EAER 165
|
|
| hslU |
PRK05201 |
ATP-dependent protease ATPase subunit HslU; |
564-619 |
2.40e-03 |
|
ATP-dependent protease ATPase subunit HslU;
Pssm-ID: 235364 [Multi-domain] Cd Length: 443 Bit Score: 41.22 E-value: 2.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720980328 564 QELHSRVIGQNEAVEAVSNAI----RRSRagLSDPNR----P--IgsfLFLGPTGVGKTELCKALA 619
Cdd:PRK05201 11 SELDKYIIGQDDAKRAVAIALrnrwRRMQ--LPEELRdevtPknI---LMIGPTGVGKTEIARRLA 71
|
|
| Sigma54_activat |
pfam00158 |
Sigma-54 interaction domain; |
570-729 |
2.75e-03 |
|
Sigma-54 interaction domain;
Pssm-ID: 425491 [Multi-domain] Cd Length: 168 Bit Score: 39.31 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 570 VIGQNEAVEAVSNAIRRsrAGLSDpnrpiGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMsefmekhsvsrlvGA 649
Cdd:pfam00158 1 IIGESPAMQEVLEQAKR--VAPTD-----APVLITGESGTGKELFARAIHQLSPRADGPFVAVNC-------------AA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 650 -PPGYV-----GYEEGGYlTEAVRRRP-------YSVILLDEVEKAHPDVFNILLQVLDDG---RLTDGQGRTVDFRntv 713
Cdd:pfam00158 61 iPEELLeselfGHEKGAF-TGADSDRKglfeladGGTLFLDEIGELPLELQAKLLRVLQEGefeRVGGTKPIKVDVR--- 136
|
170
....*....|....*...
gi 1720980328 714 VI--MTSNLGSDLIQERF 729
Cdd:pfam00158 137 IIaaTNRDLEEAVAEGRF 154
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
458-612 |
3.46e-03 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 40.62 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 458 LEEEwKAEKASLSGTQTIKAELEQAKIAIEQARRvgDLARMSELqygkIPELEKQLEAATQSEGKTMRLLRNKVTDAEIA 537
Cdd:COG1419 49 VDED-EAEKAPAAAAAPAAASAAAEEEELEELRR--ELAELKEL----LEEQLSGLAGESARLPPELAELLERLLEAGVS 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720980328 538 EVLARwtgipvaRMLEGEREKLlrmeqelhsrviGQNEAVEAVSNAIRRSragLSDPNRPIGS----FLFLGPTGVGKT 612
Cdd:COG1419 122 PELAR-------ELLEKLPEDL------------SAEEAWRALLEALARR---LPVAEDPLLDeggvIALVGPTGVGKT 178
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
389-593 |
4.95e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 389 KAIDLIDEAASSIRMQIDSKPEELDRLDRRIIQLKLE------QQALMKESDEASKKRLDMLNEELDDKERQYSELEEEW 462
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKEleelsrQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 463 KAEKASLSGTQTIKAELEqAKIAIEQARRVGDLARMSELQYgKIPELEKQL----EAATQSEGKTMRLLRNKVTDAEIAE 538
Cdd:TIGR02168 764 EELEERLEEAEEELAEAE-AEIEELEAQIEQLKEELKALRE-ALDELRAELtllnEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720980328 539 VLARWTGIPVARM--LEGEREKLLRMEQELHSRVIGQNEAVEAVSNAIRRSRAGLSD 593
Cdd:TIGR02168 842 DLEEQIEELSEDIesLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
570-684 |
5.89e-03 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 39.90 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 570 VIGQNEAVEAVSNAIRRSRAGlsDPNRPIgsfLFLGPTGVGKTELCKALANFM-FDsddaMVRIDMSEFMEKHSVSRLVG 648
Cdd:PRK04195 16 VVGNEKAKEQLREWIESWLKG--KPKKAL---LLYGPPGVGKTSLAHALANDYgWE----VIELNASDQRTADVIERVAG 86
|
90 100 110
....*....|....*....|....*....|....*.
gi 1720980328 649 AppgyvgyeegGYLTEAVRRRPYSVILLDEVEKAHP 684
Cdd:PRK04195 87 E----------AATSGSLFGARRKLILLDEVDGIHG 112
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
570-622 |
7.30e-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: 39.12 E-value: 7.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720980328 570 VIGQNEAVE----AVSNAIRRSRAGLSDPNRPI----GSFLFLGPTGVGKTELCKALANFM 622
Cdd:cd19497 14 VIGQERAKKvlsvAVYNHYKRIRNNLKQKDDDVelekSNILLIGPTGSGKTLLAQTLAKIL 74
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
203-283 |
7.35e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 39.00 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 203 VLIGEPGVGKTAIVEGLAQR---------IINGEV-PEGLkgRRVLALDMGALVAGAkYRGEFEERLKGVLNDLAKQEGN 272
Cdd:COG3267 47 VLTGEVGTGKTTLLRRLLERlpddvkvayIPNPQLsPAEL--LRAIADELGLEPKGA-SKADLLRQLQEFLLELAAAGRR 123
|
90
....*....|.
gi 1720980328 273 VILFIDELHTM 283
Cdd:COG3267 124 VVLIIDEAQNL 134
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
397-566 |
7.75e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 397 AASSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEAsKKRLDMLNEELDDKERQYSELEEEWKAEKASLSGTQTIK 476
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAL-LKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 477 AELEQAKIAIEQ--ARRVGDLARMSELQYGKI---PELEKQLEAATQSEGKTMRLLRNKVtdAEIAEVLARWTGipVARM 551
Cdd:COG4942 93 AELRAELEAQKEelAELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQA--EELRADLAELAA--LRAE 168
|
170
....*....|....*
gi 1720980328 552 LEGEREKLLRMEQEL 566
Cdd:COG4942 169 LEAERAELEALLAEL 183
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
410-515 |
7.75e-03 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 410 EELDRLDRRIIQLKLEQQALMKESDEASK------KRLDMLNEELDDKERQYSELEEEWKAEKASLSGTQTIKAELEQAK 483
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASRKIGEIEKeieqleQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL 774
|
90 100 110
....*....|....*....|....*....|..
gi 1720980328 484 IAIEQArrVGDLARMseLQYGKIPELEKQLEA 515
Cdd:TIGR02169 775 HKLEEA--LNDLEAR--LSHSRIPEIQAELSK 802
|
|
| HslU |
COG1220 |
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ... |
564-619 |
7.81e-03 |
|
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440833 [Multi-domain] Cd Length: 454 Bit Score: 39.65 E-value: 7.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720980328 564 QELHSRVIGQNEAVEAVS----NAIRRSRagLSDPNRP------IgsfLFLGPTGVGKTELCKALA 619
Cdd:COG1220 11 AELDKYIIGQDEAKRAVAialrNRWRRQQ--LPEELRDeitpknI---LMIGPTGVGKTEIARRLA 71
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
396-592 |
8.49e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 396 EAASSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASK--KRLDMLNEELDDKERQYSELEEEWKAEKASLSGTQ 473
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKevKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 474 TIKAEL-EQAKIAIEQARRVGDLaRMSELQYGKIPELEKQLEAATQSEGKTMRLLRNKVTD-----AEIAEVLARwtgip 547
Cdd:PRK03918 266 ERIEELkKEIEELEEKVKELKEL-KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGieeriKELEEKEER----- 339
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720980328 548 vARMLEGEREKLLRMEQELHSRVIGQNEAVEAVSNA--IRRSRAGLS 592
Cdd:PRK03918 340 -LEELKKKLKELEKRLEELEERHELYEEAKAKKEELerLKKRLTGLT 385
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
374-593 |
8.91e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 39.78 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 374 ATLSHRYIADRQ----LPDKAIDLI-DEAASSIRMQIDSKP--EELDRLDRRIiQLKLEQQALMKESDEASKKRLDMLNE 446
Cdd:PRK10246 383 RQWQQQLTHAEQklnaLPAITLTLTaDEVAAALAQHAEQRPlrQRLVALHGQI-VPQQKRLAQLQVAIQNVTQEQTQRNA 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 447 ELDDKERQYSELEEEWKAEKASLSGTQTIK------AELEQAK----------IAIE----------QARR------VGD 494
Cdd:PRK10246 462 ALNEMRQRYKEKTQQLADVKTICEQEARIKdleaqrAQLQAGQpcplcgstshPAVEayqalepgvnQSRLdalekeVKK 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720980328 495 LARMSELQYGKIPELEKQLEAATqSEGKTMRLLRNKVTDA------------EIAEVLARWtgipvarMLEGEREK---- 558
Cdd:PRK10246 542 LGEEGAALRGQLDALTKQLQRDE-SEAQSLRQEEQALTQQwqavcaslnitlQPQDDIQPW-------LDAQEEHErqlr 613
|
250 260 270
....*....|....*....|....*....|....*
gi 1720980328 559 LLRMEQELHSRVIGQNEAVEAVSNAIRRSRAGLSD 593
Cdd:PRK10246 614 LLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLT 648
|
|
| |
