|
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: 1735.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 1 MRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVSPLLTSAGINAGQLRTDINQALNRLPQVEGTGGD 80
Cdd:PRK10865 1 MRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVRPLLTSAGINAGQLRTDINQALSRLPQVEGTGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 81 VQPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAALESRGTLADILKAAGATTANITQAIEQMRGGESVNDQGAEDQRQA 160
Cdd:PRK10865 81 VQPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAALESRGTLADILKAAGATTANITQAIEQMRGGESVNDQGAEDQRQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 161 LKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLAL 240
Cdd:PRK10865 161 LKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 241 DMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYR 320
Cdd:PRK10865 241 DMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 321 QYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASS 400
Cdd:PRK10865 321 QYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 401 IRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKAELE 480
Cdd:PRK10865 401 IRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKAELE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 481 QAKIAIEQARRVGDLARMSELQYGKIPELEKQLEAATQLEGKTMRLLRNKVTDAEIAEVLARWTGIPVSRMMESEREKLL 560
Cdd:PRK10865 481 QAKIAIEQARRVGDLARMSELQYGKIPELEKQLAAATQLEGKTMRLLRNKVTDAEIAEVLARWTGIPVSRMLESEREKLL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 561 RMEQELHHRVIGQNEAVDAVSNAIRRSRAGLADPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDEAMVRIDMSEFMEK 640
Cdd:PRK10865 561 RMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEK 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 641 HSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNL 720
Cdd:PRK10865 641 HSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNL 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 721 GSDLIQERFGELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLKRLYKRLEERGYEIHISDEAL 800
Cdd:PRK10865 721 GSDLIQERFGELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYEIHISDEAL 800
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 447157846 801 KLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNEDRIVAVQ 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: 1632.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVSPLLTSAGINAGQLRTDINQALNRLPQVEGTGGDVQPSQ 85
Cdd:TIGR03346 1 LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEKELERLPKVSGPGGQVYLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 86 DLVRVLNLCDKLAQKRGDNFISSELFVLAALESRGTLADILKAAGATTANITQAIEQMRGGESVNDQGAEDQRQALKKYT 165
Cdd:TIGR03346 81 DLNRLLNLAEKLAQKRGDEFISSEHLLLALLDDKGTLGKLLKEAGATADALEAAINAVRGGQKVTDANAEDQYEALEKYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 166 IDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLALDMGAL 245
Cdd:TIGR03346 161 RDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLALDMGAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 246 VAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYRQYIEK 325
Cdd:TIGR03346 241 IAGAKYRGEFEERLKAVLNEVTKSEGQIILFIDELHTLVGAGKAEGAMDAGNMLKPALARGELHCIGATTLDEYRKYIEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 326 DAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASSIRMQI 405
Cdd:TIGR03346 321 DAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAARIRMEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 406 DSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKAELEQAKIA 485
Cdd:TIGR03346 401 DSKPEELDELDRRIIQLEIEREALKKEKDEASKKRLEDLEKELADLEEEYAELEEQWKAEKASIQGIQQIKEEIEQVRLE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 486 IEQARRVGDLARMSELQYGKIPELEKQLEAATQLEGKTM-RLLRNKVTDAEIAEVLARWTGIPVSRMMESEREKLLRMEQ 564
Cdd:TIGR03346 481 LEQAEREGDLAKAAELQYGKLPELEKQLQAAEQKLGEEQnRLLREEVTAEEIAEVVSRWTGIPVSKMLEGEREKLLHMEE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 565 ELHHRVIGQNEAVDAVSNAIRRSRAGLADPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDEAMVRIDMSEFMEKHSVS 644
Cdd:TIGR03346 561 ELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRIDMSEYMEKHSVA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 645 RLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNLGSDL 724
Cdd:TIGR03346 641 RLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDF 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 725 IQERFGELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLKRLYKRLEERGYEIHISDEALKLLS 804
Cdd:TIGR03346 721 IQELAGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKITLELSDAALDFLA 800
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 447157846 805 ENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNEDRIV 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: 1507.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 1 MRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVSPLLTSAGINAGQLRTDINQALNRLPQVEGTGGD 80
Cdd:COG0542 1 MNFEKFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGRLPKVSGSSGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 81 VQPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAAL-ESRGTLADILKAAGATTANITQAIEQMRGGESVNDQGAEDQRQ 159
Cdd:COG0542 81 PYLSPRLKRVLELAELEARKLGDEYISTEHLLLALLrEGEGVAARILKKLGITLEALREALEELRGGSRVTSQNPESKTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 160 ALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLA 239
Cdd:COG0542 161 ALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDKRVLS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 240 LDMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEY 319
Cdd:COG0542 241 LDLGALVAGAKYRGEFEERLKAVLDEVKKSEGNIILFIDELHTLVGAGGAEGAMDAANLLKPALARGELRCIGATTLDEY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 320 RQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAAS 399
Cdd:COG0542 321 RKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAIDLIDEAAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 400 SIRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKAEL 479
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 480 EQakiaieqarrvgdlarmselQYGKIPELEKQLEAATQLEGKTMRLLRNKVTDAEIAEVLARWTGIPVSRMMESEREKL 559
Cdd:COG0542 481 EQ--------------------RYGKIPELEKELAELEEELAELAPLLREEVTEEDIAEVVSRWTGIPVGKLLEGEREKL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 560 LRMEQELHHRVIGQNEAVDAVSNAIRRSRAGLADPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDEAMVRIDMSEFME 639
Cdd:COG0542 541 LNLEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYME 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 640 KHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSN 719
Cdd:COG0542 621 KHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSN 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 720 LGSDLIQERFGE-LDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLKRLYKRLEERGYEIHISDE 798
Cdd:COG0542 701 IGSELILDLAEDePDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDA 780
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 447157846 799 ALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNEDRIV 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: 871.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 17 AQSLA--LGHDnqFIEPLHLMSALLNQEGGSVSPLLTSAGINAGQLRTDINQALNRlpqveGTG---GDVQPSQDLVRVL 91
Cdd:CHL00095 16 SQEEArrLGHN--FVGTEQILLGLIGEGTGIAARALKSMGVTLKDARIEVEKIIGR-----GTGfvaVEIPFTPRAKRVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 92 NLCDKLAQKRGDNFISSELFVLAAL-ESRGTLADILKAAGATTANITQAIEQMRGGESVNDQGAEDQRQ---ALKKYTID 167
Cdd:CHL00095 89 EMSLEEARDLGHNYIGTEHLLLALLeEGEGVAARVLENLGVDLSKIRSLILNLIGEIIEAILGAEQSRSktpTLEEFGTN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 168 LTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLALDMGALVA 247
Cdd:CHL00095 169 LTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDKLVITLDIGLLLA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 248 GAKYRGEFEERLKGVLNDLaKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYRQYIEKDA 327
Cdd:CHL00095 249 GTKYRGEFEERLKRIFDEI-QENNNIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLDEYRKHIEKDP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 328 ALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASSIRMQIDS 407
Cdd:CHL00095 328 ALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLDEAGSRVRLINSR 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 408 KPEELDRLDRriiqlklEQQALMKESDEASKkrldmlnEELSDKERQYSELEEEWKAEKASLsgtqtikaeleqakiaie 487
Cdd:CHL00095 408 LPPAARELDK-------ELREILKDKDEAIR-------EQDFETAKQLRDREMEVRAQIAAI------------------ 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 488 qarrvgdlarmselqygkipelekqleAATQLEGKTMRLLRNKVTDAEIAEVLARWTGIPVSRMMESEREKLLRMEQELH 567
Cdd:CHL00095 456 ---------------------------IQSKKTEEEKRLEVPVVTEEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLH 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 568 HRVIGQNEAVDAVSNAIRRSRAGLADPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDEAMVRIDMSEFMEKHSVSRLV 647
Cdd:CHL00095 509 KRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALASYFFGSEDAMIRLDMSEYMEKHTVSKLI 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 648 GAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNLGSDLIQE 727
Cdd:CHL00095 589 GSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSKVIET 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 728 RFGEL------------DYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLKRLYKRLEERGYEIHI 795
Cdd:CHL00095 669 NSGGLgfelsenqlsekQYKRLSNLVNEELKQFFRPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEV 748
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447157846 796 SDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNEDRIVAV 856
Cdd:CHL00095 749 TERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVDVNDEKEVKI 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: 784.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVSPLLTSAGINAGQLRTDINQALNRLPQveGTGGDVQPSQ 85
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLARALDKLPR--GNTRTPVFSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 86 DLVRVLNLCDKLAQKR-GDNFISSELFVLAALES---RGTLADILKA-AGATTANITQAIEQMRGGESVNDQGAED---- 156
Cdd:TIGR03345 79 HLVELLQEAWLLASLElGDGRIRSGHLLLALLTDpelRRLLGSISPElAKIDREALREALPALVEGSAEASAAAADaapa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 157 -------QRQALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVP 229
Cdd:TIGR03345 159 gaaagaaGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 230 EGLKGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELH 309
Cdd:TIGR03345 239 PALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPIILFIDEAHTLIGAGGQAGQGDAANLLKPALARGELR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 310 CVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDK 389
Cdd:TIGR03345 319 TIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLPDK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 390 AIDLIDEAASSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKES--DEASKKRLDMLNEELSDKERQYSELEEEWKAEKA 467
Cdd:TIGR03345 399 AVSLLDTACARVALSQNATPAALEDLRRRIAALELELDALEREAalGADHDERLAELRAELAALEAELAALEARWQQEKE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 468 SLSGTQTIKAELEQAkiaiEQARRVGDLARMSELQygkipELEKQLEAAtqleGKTMRLLRNKVTDAEIAEVLARWTGIP 547
Cdd:TIGR03345 479 LVEAILALRAELEAD----ADAPADDDDALRAQLA-----ELEAALASA----QGEEPLVFPEVDAQAVAEVVADWTGIP 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 548 VSRMMESEREKLLRMEQELHHRVIGQNEAVDAVSNAIRRSRAGLADPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDE 627
Cdd:TIGR03345 546 VGRMVRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGEQ 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 628 AMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTV 707
Cdd:TIGR03345 626 NLITINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREI 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 708 DFRNTVVIMTSNLGSDLIQERFGELDYA----HMKELVLGVVSHNFRPEFINRIdEVVVFHPLGEQHIASIAQIQLKRLY 783
Cdd:TIGR03345 706 DFKNTVILLTSNAGSDLIMALCADPETApdpeALLEALRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRIA 784
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 447157846 784 KRLEER-GYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILS 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: 756.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSvsPLLTSAGINAGQLRTDINQAL-NRLPQ-VEGTGGDVQP 83
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAI--EILEECGGDVELLRKRLEDYLeENLPViPEDIDEEPEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 84 SQDLVRVLNLCDKLAQKRGDNFISsELFVLAAL--ESRGTLADILKAAGATTANITQAI-EQMRGGESVNDQGA------ 154
Cdd:TIGR02639 79 TVGVQRVIQRALLHVKSAGKKEID-IGDLLVALfdEEDSHASYFLKSQGITRLDILNYIsHGISKDDGKDQLGEeagkee 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 155 EDQRQALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKG 234
Cdd:TIGR02639 158 EKGQDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERLKN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 235 RRVLALDMGALVAGAKYRGEFEERLKGVLNDLAKQEgNVILFIDELHTMVGAGK-ADGAMDAGNMLKPALARGELHCVGA 313
Cdd:TIGR02639 238 AKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEP-NAILFIDEIHTIVGAGAtSGGSMDASNLLKPALSSGKIRCIGS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 314 TTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDL 393
Cdd:TIGR02639 317 TTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 394 IDEAASSIRMQIDSKPEEldrldrriiqlkleqqalmkesdeaskkrldmlneelsdkerqyseleeewkaekaslsgtq 473
Cdd:TIGR02639 397 IDEAGAAFRLRPKAKKKA-------------------------------------------------------------- 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 474 tikaeleqakiaieqarrvgdlarmselqygkipelekqleaatqlegktmrllrnKVTDAEIAEVLARWTGIPVSRMME 553
Cdd:TIGR02639 415 --------------------------------------------------------NVNVKDIENVVAKMAKIPVKTVSS 438
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 554 SEREKLLRMEQELHHRVIGQNEAVDAVSNAIRRSRAGLADPNRPIGSFLFLGPTGVGKTELCKALANFMfdsDEAMVRID 633
Cdd:TIGR02639 439 DDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEEL---GVHLLRFD 515
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 634 MSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTV 713
Cdd:TIGR02639 516 MSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVI 595
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 714 VIMTSNLGSD--------LIQERFGELDyahmkelvLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLKRLYKR 785
Cdd:TIGR02639 596 LIMTSNAGASemskppigFGGENRESKS--------LKAIKKLFSPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQ 667
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447157846 786 LEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEV 848
Cdd:TIGR02639 668 LNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEILFGKLKKGGSVKISL 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: 557.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLnqEGGSVSPLLTSAGINAGQLRTD----INQALNRLPQVEGTGgDV 81
Cdd:PRK11034 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALL--SNPSAREALEACSVDLVALRQEleafIEQTTPVLPASEEER-DT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 82 QPSQDLVRVLNLCDKLAQKRGDNFISSElFVLAAL--ESRGTLADILKAAGATTANITQAI-------EQMRGGESVNDQ 152
Cdd:PRK11034 79 QPTLSFQRVLQRAVFHVQSSGRSEVTGA-NVLVAIfsEQESQAAYLLRKHEVSRLDVVNFIshgtrkdEPSQSSDPGSQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 153 GAEDQRQA---LKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVP 229
Cdd:PRK11034 158 NSEEQAGGeerMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 230 EGLKGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLaKQEGNVILFIDELHTMVGAGKADGA-MDAGNMLKPALARGEL 308
Cdd:PRK11034 238 EVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQL-EQDTNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSGKI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 309 HCVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPD 388
Cdd:PRK11034 317 RVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 389 KAIDLIDEAASSIRMQidskpeeldrldrriiqlkleqqalmkesdEASKKRldmlneelsdkerqyseleeewkaekas 468
Cdd:PRK11034 397 KAIDVIDEAGARARLM------------------------------PVSKRK---------------------------- 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 469 lsgtqtikaeleqakiaieqarrvgdlarmselqygkipelekqleaatqlegKTmrllrnkVTDAEIAEVLARWTGIPV 548
Cdd:PRK11034 419 -----------------------------------------------------KT-------VNVADIESVVARIARIPE 438
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 549 SRMMESEREKLLRMEQELHHRVIGQNEAVDAVSNAIRRSRAGLADPNRPIGSFLFLGPTGVGKTELCKALANFMfdsDEA 628
Cdd:PRK11034 439 KSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL---GIE 515
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 629 MVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVD 708
Cdd:PRK11034 516 LLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKAD 595
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 709 FRNTVVIMTSNLGSDLIQER---FGELDYAH--MKElvlgvVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLKRLY 783
Cdd:PRK11034 596 FRNVVLVMTTNAGVRETERKsigLIHQDNSTdaMEE-----IKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQ 670
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447157846 784 KRLEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNEDR 852
Cdd:PRK11034 671 AQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKEK 739
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
558-763 |
1.28e-111 |
|
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: 338.38 E-value: 1.28e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 558 KLLRMEQELHHRVIGQNEAVDAVSNAIRRSRAGLADPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDEAMVRIDMSEF 637
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 638 MEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMT 717
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447157846 718 SNlgsdliqerfgeldyahmkelvlgvvshNFRPEFINRIDEVVVF 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 |
1.73e-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: 293.33 E-value: 1.73e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 596 RPIGSFLFLGPTGVGKTELCKALANFMFDSDEAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVIL 675
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 676 LDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNLGSDLIQERFG---ELDYAHMKELVLGVVSHNFRPE 752
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRlgdSPDYELLKEEVMDLLKKGFIPE 160
|
....*...
gi 447157846 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 |
1.43e-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: 1.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 342 SVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASSIRMQIDSKPEELDRLDRRIIQ 421
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|....
gi 447157846 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 |
2.30e-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: 117.12 E-value: 2.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 766 LGEQHIASIAQIQLKRLYKRLEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIR 845
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 447157846 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 |
1.22e-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: 109.84 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 766 LGEQHIASIAQIQLKRLYKRLEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIR 845
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
....*....
gi 447157846 846 LEVNEDRIV 854
Cdd:smart01086 81 VDVDDGELV 89
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
181-341 |
1.96e-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: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 181 IGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINgevpeglKGRRVLALDMGALVAGAKYRGEFEERLK 260
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFR-------PGAPFLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 261 GVLNDLAKQEGNVILFIDELHTMVGAGKADG--AMDAGNMLKPalARGELHCVGATTLDEYRQyieKDAALERRFQKVFV 338
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDSLSRGAQNALlrVLETLNDLRI--DRENVRVIGATNRPLLGD---LDRALYDRLDIRIV 148
|
...
gi 447157846 339 AEP 341
Cdd:cd00009 149 IPL 151
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
571-765 |
5.14e-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: 5.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 571 IGQNEAVDAVSNAIRRsragladpnRPIGSFLFLGPTGVGKTELCKALANFMFDSDEAMVRIDMSEFMEKHSVSRLVGAP 650
Cdd:cd00009 1 VGQEEAIEALREALEL---------PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 651 PGYVgyeeggyLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTdgqgrTVDFRNTVVIMTSNLGSDLIqerfg 730
Cdd:cd00009 72 LVRL-------LFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATNRPLLGD----- 134
|
170 180 190
....*....|....*....|....*....|....*
gi 447157846 731 eldyahmkelvlgvvshnFRPEFINRIDEVVVFHP 765
Cdd:cd00009 135 ------------------LDRALYDRLDIRIVIPL 151
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
602-725 |
2.44e-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: 71.25 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 602 LFLGPTGVGKTELCKALANFMFDSDEAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGY----LTEAVRRRPYSVILLD 677
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 447157846 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 |
1.37e-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: 68.39 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 204 LIGEPGVGKTAIVEGLAQRIingevpeglkGRRVLALDMGALVagAKYRGEFEERLKGVLnDLAKQEGNVILFIDELHTM 283
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELV--SKYVGESEKRLRELF-EAAKKLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447157846 284 VGAGKADG---AMDAGNMLKPAL-----ARGELHCVGATTldeyrqYIEK-DAALERRFQKVF 337
Cdd:pfam00004 70 AGSRGSGGdseSRRVVNQLLTELdgftsSNSKVIVIAATN------RPDKlDPALLGRFDRII 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
600-719 |
1.34e-11 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 62.70 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 600 SFLFLGPTGVGKTELCKALAnFMFDSDEAMVrIDMSEFMEKhsvSRLVGA--PPGYVGYEEGGYLTEAVRRRpySVILLD 677
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLA-AALSNRPVFY-VQLTRDTTE---EDLFGRrnIDPGGASWVDGPLVRAAREG--EIAVLD 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 447157846 678 EVEKAHPDVFNILLQVLDDGRLTDGQGRT---VDFRNTVVIMTSN 719
Cdd:pfam07728 74 EINRANPDVLNSLLSLLDERRLLLPDGGElvkAAPDGFRLIATMN 118
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
37-382 |
1.64e-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: 67.24 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 37 ALLNQEGGSVSPLLTSAGINAGQLRTDINQALNRLPQVEGTGGDVQPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAAL 116
Cdd:COG0464 16 LLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 117 ESRGTLADILKAAGATTANITQAIEQMRGGESVNDQGAEDQRQALKKYTIDLTERAEQGKLDPVIGRDE---EIRRTIQV 193
Cdd:COG0464 96 ELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEvkeELRELVAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 194 LQRRTK-------NNP---VLIGEPGVGKTAIVEGLAQRIingevpeglkGRRVLALDMGALVagAKYRGEFEERLKGVL 263
Cdd:COG0464 176 PLKRPElreeyglPPPrglLLYGPPGTGKTLLARALAGEL----------GLPLIEVDLSDLV--SKYVGETEKNLREVF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 264 nDLAKQEGNVILFIDELHTMVGA--GKADGAMDA--GNMLKpALA--RGELHCVGATtldeYRqyIEK-DAALERRFQ-K 335
Cdd:COG0464 244 -DKARGLAPCVLFIDEADALAGKrgEVGDGVGRRvvNTLLT-EMEelRSDVVVIAAT----NR--PDLlDPALLRRFDeI 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 447157846 336 VFVAEPSVEDTIAILRGLKERYELHHHVqitDPAIVAAAT--LSHRYIA 382
Cdd:COG0464 316 IFFPLPDAEERLEIFRIHLRKRPLDEDV---DLEELAEATegLSGADIR 361
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
575-733 |
7.07e-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: 61.53 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 575 EAVDAVSNAIRRSRAGLadpNRPIGsFLFLGPTGVGKTELCKALANfmfDSDEAMVRIDMSEFMEKHSvsrlvgappgYV 654
Cdd:cd19481 7 EAVEAPRRGSRLRRYGL---GLPKG-ILLYGPPGTGKTLLAKALAG---ELGLPLIVVKLSSLLSKYV----------GE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 655 GYEEGGYLTEAVRRRPYSVILLDEVEKAHPD------------VFNILLQVLDDGRLTDgqgrtvdfrNTVVIMTSNLGS 722
Cdd:cd19481 70 SEKNLRKIFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAATNRPD 140
|
170
....*....|...
gi 447157846 723 DLIQE--RFGELD 733
Cdd:cd19481 141 LLDPAllRPGRFD 153
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
602-735 |
6.19e-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: 57.99 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 602 LFLGPTGVGKTELCKALANfmfDSDEAMVRIDMSEFMEKHsvsrlVGAPPGYVgyeeGGYLTEAVRRRPySVILLDEVEK 681
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAK---ELGAPFIEISGSELVSKY-----VGESEKRL----RELFEAAKKLAP-CVIFIDEIDA 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447157846 682 AHP-----------DVFNILLQVLDdgrltdgqGRTVDFRNTVVIMTSNlgsdliqeRFGELDYA 735
Cdd:pfam00004 69 LAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN--------RPDKLDPA 117
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
17-69 |
7.36e-10 |
|
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: 55.22 E-value: 7.36e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 447157846 17 AQSLALGHDNQFIEPLHLMSALLNQEGGSVSPLLTSAGINAGQLRTDINQALN 69
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
94-145 |
4.59e-09 |
|
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: 52.91 E-value: 4.59e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 447157846 94 CDKLAQKRGDNFISSELFVLAAL-ESRGTLADILKAAGATTANITQAIEQMRG 145
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLeEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
393-781 |
1.58e-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: 57.61 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 393 LIDEAASSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGT 472
Cdd:COG0464 1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 473 QTIKAELEQAKIAIEQARRVGDLARMSELQYGKIPELEKQLEAATQLEGKTMRLLRNKVTDAEIAEVLARWTGIPVSRMM 552
Cdd:COG0464 81 LLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 553 ESEREKllrmeQELHHRVIGQNEAVDAvsnairRSRAGLadpnRPIGSFLFLGPTGVGKTELCKALANfmfDSDEAMVRI 632
Cdd:COG0464 161 GLEEVK-----EELRELVALPLKRPEL------REEYGL----PPPRGLLLYGPPGTGKTLLARALAG---ELGLPLIEV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 633 DMSEFMEKhsvsrlvgappgYVGyEEGGYLTEAV---RRRPYSVILLDEVEKAHPD-----------VFNILLQVLDDGR 698
Cdd:COG0464 223 DLSDLVSK------------YVG-ETEKNLREVFdkaRGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 699 ltdgqgrtvdfRNTVVIMTSNlgsdliqeRFGELDyahmkelvlgvvshnfrPEFINRIDEVVVFHPLGEQHIASIAQIQ 778
Cdd:COG0464 290 -----------SDVVVIAATN--------RPDLLD-----------------PALLRRFDEIIFFPLPDAEERLEIFRIH 333
|
...
gi 447157846 779 LKR 781
Cdd:COG0464 334 LRK 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 447157846 198 TKNNPVLIGEPGVGKTAIVEGLAQRI---------INGEVPEglkgRRVLALDMGALVAGAKYRGEFEERLKGVLnDLAK 268
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELgppgggviyIDGEDIL----EEVLDQLLLIIVGGKKASGSGELRLRLAL-ALAR 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447157846 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 |
1.14e-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: 49.69 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 564 QELHHRVIGQNEAVDAVS----NAIRRSR--AGLADPNRPiGSFLFLGPTGVGKTELCKALANFMfdsDEAMVRIDMSEF 637
Cdd:cd19498 7 SELDKYIIGQDEAKRAVAialrNRWRRMQlpEELRDEVTP-KNILMIGPTGVGKTEIARRLAKLA---GAPFIKVEATKF 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 447157846 638 MEKhsvsrlvgappGYVGYEeggyLTEAVRRRPYSVILLDEVEK 681
Cdd:cd19498 83 TEV-----------GYVGRD----VESIIRDLVEGIVFIDEIDK 111
|
|
| AtoC |
COG2204 |
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ... |
548-803 |
1.08e-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: 48.81 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 548 VSRMMESEReklLRMEQELHHRVIGQNEAVDAVSNAIRRsragLADPNRPIgsfLFLGPTGVGKTELCKALANFMFDSDE 627
Cdd:COG2204 114 VERALERRR---LRRENAEDSGLIGRSPAMQEVRRLIEK----VAPSDATV---LITGESGTGKELVARAIHRLSPRADG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 628 AMVRIDMSEFMEKHSVSRLVGAppgyvgyeEGGYLTEAVRRRPYSV-------ILLDEVEKAHPDVFNILLQVLDDG--- 697
Cdd:COG2204 184 PFVAVNCAAIPEELLESELFGH--------EKGAFTGAVARRIGKFeladggtLFLDEIGEMPLALQAKLLRVLQERefe 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 698 RLTDGQGRTVDFRntvVIMTSNLgsDLIQErfgeldyahmkelvlgVVSHNFRPEFINRIDEVVVFHP-LGEQH--IASI 774
Cdd:COG2204 256 RVGGNKPIPVDVR---VIAATNR--DLEEL----------------VEEGRFREDLYYRLNVFPIELPpLRERRedIPLL 314
|
250 260
....*....|....*....|....*....
gi 447157846 775 AQIQLKRLYKRLeerGYEIHISDEALKLL 803
Cdd:COG2204 315 ARHFLARFAAEL---GKPVKLSPEALEAL 340
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
388-593 |
1.24e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 388 DKAIDLIDEAASSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEAsKKRLDMLNEELSDKERQYSELEEEWKAEKA 467
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL-EEELEELEEELEELEEELEEAEEELEEAEA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 468 SLSGTQTIKAELEQAKIAIEQARRVGDLARMSELQyGKIPELEKQLEAATQLEGKTMRLLRNKVTDAEIAEVLARwtgip 547
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALR-AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE----- 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447157846 548 vSRMMESEREKLLRMEQELHHRVIGQNEAVDAVSNAIRRSRAGLAD 593
Cdd:COG1196 433 -LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
203-333 |
1.43e-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: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 203 VLIGEPGVGKTAIVEGLAQRIINGEV----------PEGLKGRRVLALDMGALVAGAKYRgEFEERLKGVLNDLAKQEGN 272
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSNRPVfyvqltrdttEEDLFGRRNIDPGGASWVDGPLVR-AAREGEIAVLDEINRANPD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447157846 273 VilfIDELHTmvgagkadgAMDAGNMLKPALaRGELHC------VGATTLDEYRQYIEKDAALERRF 333
Cdd:pfam07728 82 V---LNSLLS---------LLDERRLLLPDG-GELVKAapdgfrLIATMNPLDRGLNELSPALRSRF 135
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
596-782 |
1.83e-04 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 44.61 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 596 RPIGSFLFLGPTGVGKTELCKALANfmfDSDEAMVRIDMSEFMEKhsvsrlvgappgYVGyeEGGYL-----TEAVRRRP 670
Cdd:COG1222 110 EPPKGVLLYGPPGTGKTLLAKAVAG---ELGAPFIRVRGSELVSK------------YIG--EGARNvrevfELAREKAP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 671 ySVILLDEVE----KAHPD--------VFNILLQVLDDgrltdgqgrtVDFRNTVVIM-TSNlgsdliqeRFGELDYAhm 737
Cdd:COG1222 173 -SIIFIDEIDaiaaRRTDDgtsgevqrTVNQLLAELDG----------FESRGDVLIIaATN--------RPDLLDPA-- 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447157846 738 kelVLgvvshnfRPefiNRIDEVVVFHPLGEQHIASIAQIQLKRL 782
Cdd:COG1222 232 ---LL-------RP---GRFDRVIEVPLPDEEAREEILKIHLRDM 263
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
179-281 |
1.88e-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: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 179 PVIGRDEEIRRTIQVLQRRTKNNP---VLIGEPGVGKTAIVEGLAQR----------------IINGEVPEGLKGRRVLA 239
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRAlerdggyflrgkcdenLPYSPLLEALTREGLLR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447157846 240 --LDMGALVAGAKYRGEFEERLKGV------------------LNDLAKQEGNVILFIDELH 281
Cdd:pfam13191 81 qlLDELESSLLEAWRAALLEALAPVpelpgdlaerlldlllrlLDLLARGERPLVLVLDDLQ 142
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
415-516 |
1.92e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 415 LDRRIIQ----------LKLEQqalMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGT-QTIKAELEQ-A 482
Cdd:PRK00409 499 LPENIIEeakkligedkEKLNE---LIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEeDKLLEEAEKeA 575
|
90 100 110
....*....|....*....|....*....|....*..
gi 447157846 483 KIAIEQARRVGD--LARMSELQYGKIPEL-EKQLEAA 516
Cdd:PRK00409 576 QQAIKEAKKEADeiIKELRQLQKGGYASVkAHELIEA 612
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
204-283 |
1.95e-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: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 204 LIGEPGVGKTAIVEGLAQRIingevpeglkGRRVLALDMGALVagAKYRGEFEERLKGVLnDLAKQEGNVILFIDELHTM 283
Cdd:cd19481 31 LYGPPGTGKTLLAKALAGEL----------GLPLIVVKLSSLL--SKYVGESEKNLRKIF-ERARRLAPCILFIDEIDAI 97
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
347-551 |
2.25e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 347 IAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRqlpdkAIDLIDEAASSIRMQIDSKPEELDRLDRRIIQLKLEQ 426
Cdd:COG4913 251 IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR-----RLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 427 QALMKESDEASKKRLDMLNEELSDKERQYSELEEEWK-----AEKASLSGTQTIKAELEQAKIAIEQARRVGD-LARMSE 500
Cdd:COG4913 326 DELEAQIRGNGGDRLEQLEREIERLERELEERERRRArlealLAALGLPLPASAEEFAALRAEAAALLEALEEeLEALEE 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447157846 501 LQYGKIPELEKQLEAATQLEGKTMRLLRNKVT-DAEIAEV---LARWTGIPVSRM 551
Cdd:COG4913 406 ALAEAEAALRDLRRELRELEAEIASLERRKSNiPARLLALrdaLAEALGLDEAEL 460
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
410-592 |
2.27e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 410 EELDRLDRRIIQLKLEQQALMKESDEAS------KKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKAELEQAK 483
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEaqleelESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 484 IAIE-----QARRVGDLARMSELQYGKIPELEKQLEaatQLEGKTMRL------LRNKVTDAEIAEVLARWTGIpvsrmm 552
Cdd:TIGR02168 375 EELEeqletLRSKVAQLELQIASLNNEIERLEARLE---RLEDRRERLqqeieeLLKKLEEAELKELQAELEEL------ 445
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447157846 553 ESEREKLLRMEQELHHRVIGQNEAVDAVSNAIRRSRAGLA 592
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
600-698 |
4.08e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 41.17 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 600 SFLFL-GPTGVGKTELCKALANFMFDSDEAMVRIDMSEFMEK----HSVSRLVGAPPGYVGYEEG--GYLTEAVRRRP-Y 671
Cdd:pfam13401 6 GILVLtGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPkdllRALLRALGLPLSGRLSKEEllAALQQLLLALAvA 85
|
90 100
....*....|....*....|....*..
gi 447157846 672 SVILLDEVEKAHPDVFNILLQVLDDGR 698
Cdd:pfam13401 86 VVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| 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 |
5.43e-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: 5.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447157846 204 LIGEPGVGKTAIVEGLAQRIingevpeglkGRRVLALDMGALVagAKYRGEFEERLKGVLNDlAKQEGNVILFIDEL 280
Cdd:cd19503 39 LHGPPGTGKTLLARAVANEA----------GANFLSISGPSIV--SKYLGESEKNLREIFEE-ARSHAPSIIFIDEI 102
|
|
| Sigma54_activat |
pfam00158 |
Sigma-54 interaction domain; |
570-729 |
5.78e-04 |
|
Sigma-54 interaction domain;
Pssm-ID: 425491 [Multi-domain] Cd Length: 168 Bit Score: 41.62 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 570 VIGQNEAVDAVSNAIRRsragLADPNRPIgsfLFLGPTGVGKTELCKALANFMFDSDEAMVRIDMsefmekhsvsrlvGA 649
Cdd:pfam00158 1 IIGESPAMQEVLEQAKR----VAPTDAPV---LITGESGTGKELFARAIHQLSPRADGPFVAVNC-------------AA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 650 -PPGYV-----GYEEGGYlTEAVRRRP-------YSVILLDEVEKAHPDVFNILLQVLDDG---RLTDGQGRTVDFRntv 713
Cdd:pfam00158 61 iPEELLeselfGHEKGAF-TGADSDRKglfeladGGTLFLDEIGELPLELQAKLLRVLQEGefeRVGGTKPIKVDVR--- 136
|
170
....*....|....*...
gi 447157846 714 VI--MTSNLGSDLIQERF 729
Cdd:pfam00158 137 IIaaTNRDLEEAVAEGRF 154
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
323-533 |
6.19e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 323 IEKDAALERR----FQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLsHRYIADRQlpdkaidliDEaa 398
Cdd:COG4913 609 RAKLAALEAElaelEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA-EREIAELE---------AE-- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 399 ssiRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRlDMLNEELSDKERQYSELEEEwkAEKASLSGTQTIKAE 478
Cdd:COG4913 677 ---LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEI-GRLEKELEQAEEELDELQDR--LEAAEDLARLELRAL 750
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447157846 479 LEQAKIAIEQARRVGDLARmselqygkipELEKQLEAATQLEGKTMRLLRNKVTD 533
Cdd:COG4913 751 LEERFAAALGDAVERELRE----------NLEERIDALRARLNRAEEELERAMRA 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
401-592 |
1.10e-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: 42.75 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 401 IRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKrldmLNEELSDKERQYSELEEEWKAEKASLSGTQTIKA-EL 479
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK----IKDLGEEEQLRVKEKIGELEAEIASLERSIAEKErEL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 480 EQA--KIAIEQARRVGDLARMSELQyGKIPELEK---QLEAATQLEGKTMRLLRNKVtdAEIAEVLARWTGIPVSR---- 550
Cdd:TIGR02169 318 EDAeeRLAKLEAEIDKLLAEIEELE-REIEEERKrrdKLTEEYAELKEELEDLRAEL--EEVDKEFAETRDELKDYrekl 394
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447157846 551 -MMESEREKLLRMEQELHHRVIGQNEAVDAVSNAIRRSRAGLA 592
Cdd:TIGR02169 395 eKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN 437
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
391-491 |
1.24e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 391 IDLIDEAASSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASK------KRLDMLNEELSDKERQYSELEEEWKA 464
Cdd:COG1340 169 LKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKeiveaqEKADELHEEIIELQKELRELRKELKK 248
|
90 100 110
....*....|....*....|....*....|
gi 447157846 465 --EKASLSGTQTIKAEL-EQAKIAIEQARR 491
Cdd:COG1340 249 lrKKQRALKREKEKEELeEKAEEIFEKLKK 278
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
570-619 |
1.32e-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: 1.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 447157846 570 VIGQNEAVDAVSNAIRRSRAGLAdpnrpigsFLFLGPTGVGKTELCKALA 619
Cdd:COG2812 12 VVGQEHVVRTLKNALASGRLAHA--------YLFTGPRGVGKTTLARILA 53
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
570-696 |
1.40e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 41.41 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 570 VIGQNEAVDAVSNAIR-------RSRAGLADPNRpigsFLFLGPTGVGKTELCKALANfmfdsdEAM-----VRID--MS 635
Cdd:COG1223 4 VVGQEEAKKKLKLIIKelrrrenLRKFGLWPPRK----ILFYGPPGTGKTMLAEALAG------ELKlplltVRLDslIG 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447157846 636 EFMEKhSVSRLVGappgyvgyeeggyLTEAVRRRPySVILLDEVE---------KAHPD---VFNILLQVLDD 696
Cdd:COG1223 74 SYLGE-TARNLRK-------------LFDFARRAP-CVIFFDEFDaiakdrgdqNDVGEvkrVVNALLQELDG 131
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
98-375 |
1.79e-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: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 98 AQKRGDNFISSELFVLAALESRG-TLADILKAAGATTANITQAIEqmrggESVNDQGAEDQRQALKKYTIDLTERAEQgK 176
Cdd:COG1222 3 DLLTIDENIKALLALIDALQERLgVELALLLQPVKALELLEEAPA-----LLLNDANLTQKRLGTPRGTAVPAESPDV-T 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 177 LDPVIGRDEEIRRTIQVLQRRTKNN---------PV----LIGEPGVGKTaivegLAQRIINGEVpeglkGRRVLALDMG 243
Cdd:COG1222 77 FDDIGGLDEQIEEIREAVELPLKNPelfrkygiePPkgvlLYGPPGTGKT-----LLAKAVAGEL-----GAPFIRVRGS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 244 ALVAgaKYRGEFEERLKGVLnDLAKQEGNVILFIDELHTMvgAGKADGAMDAG--NMLKPAL--------ARGELHCVGA 313
Cdd:COG1222 147 ELVS--KYIGEGARNVREVF-ELAREKAPSIIFIDEIDAI--AARRTDDGTSGevQRTVNQLlaeldgfeSRGDVLIIAA 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447157846 314 TtldeyrQYIEK-DAALER--RF-QKVFVAEPSVEDTIAILRGLKERYELHHHVqitDPAIVAAAT 375
Cdd:COG1222 222 T------NRPDLlDPALLRpgRFdRVIEVPLPDEEAREEILKIHLRDMPLADDV---DLDKLAKLT 278
|
|
| PRK14970 |
PRK14970 |
DNA polymerase III subunits gamma and tau; Provisional |
570-696 |
4.34e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184934 [Multi-domain] Cd Length: 367 Bit Score: 40.24 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 570 VIGQNEAVDAVSNAIRRsragladpNRPIGSFLFLGPTGVGKTELCKALANFMFDSDeamvrIDMSEFMEKHSVSRLVGA 649
Cdd:PRK14970 19 VVGQSHITNTLLNAIEN--------NHLAQALLFCGPRGVGKTTCARILARKINQPG-----YDDPNEDFSFNIFELDAA 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 447157846 650 PPGYVgyEEGGYLTEAVRRRP----YSVILLDEVEKAHPDVFNILLQVLDD 696
Cdd:PRK14970 86 SNNSV--DDIRNLIDQVRIPPqtgkYKIYIIDEVHMLSSAAFNAFLKTLEE 134
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
404-516 |
4.72e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 404 QIDSKPEELDRLDRRIIQLKLEQQALMKESDEaSKKRLDMLNEELSDKERQYSELE------------------------ 459
Cdd:TIGR04523 490 ELKSKEKELKKLNEEKKELEEKVKDLTKKISS-LKEKIEKLESEKKEKESKISDLEdelnkddfelkkenlekeideknk 568
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 447157846 460 --EEWKAEKASLSGTQTIKAELEQAKiaieqARRVGDLARMSELQYGKIPELEKQLEAA 516
Cdd:TIGR04523 569 eiEELKQTQKSLKKKQEEKQELIDQK-----EKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
397-566 |
5.20e-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: 40.13 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 397 AASSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEAsKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIK 476
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAL-LKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 477 AELEQAKIAIEQ--ARRVGDLARMSELQYGKI---PELEKQLEAATQLEGKTMRLLRNKVtdAEIAEVLARWTGipVSRM 551
Cdd:COG4942 93 AELRAELEAQKEelAELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQA--EELRADLAELAA--LRAE 168
|
170
....*....|....*
gi 447157846 552 MESEREKLLRMEQEL 566
Cdd:COG4942 169 LEAERAELEALLAEL 183
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
458-612 |
6.83e-03 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 39.85 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 458 LEEEwKAEKASLSGTQTIKAELEQAKIAIEQARRvgDLARMSELQYGKIPELEKQLEAATQLEGKTMRLLRnkvtDAEIA 537
Cdd:COG1419 49 VDED-EAEKAPAAAAAPAAASAAAEEEELEELRR--ELAELKELLEEQLSGLAGESARLPPELAELLERLL----EAGVS 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447157846 538 EVLARwtgipvsRMMESEREKLlrmeqelhhrviGQNEAVDAVSNAIRRSragLADPNRPIGS----FLFLGPTGVGKT 612
Cdd:COG1419 122 PELAR-------ELLEKLPEDL------------SAEEAWRALLEALARR---LPVAEDPLLDeggvIALVGPTGVGKT 178
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
570-684 |
7.06e-03 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 39.90 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 570 VIGQNEAVDAVSNAIRRSRAGlaDPNRPIgsfLFLGPTGVGKTELCKALANFM-FDsdeaMVRIDMSEFMEKHSVSRLVG 648
Cdd:PRK04195 16 VVGNEKAKEQLREWIESWLKG--KPKKAL---LLYGPPGVGKTSLAHALANDYgWE----VIELNASDQRTADVIERVAG 86
|
90 100 110
....*....|....*....|....*....|....*.
gi 447157846 649 AppgyvgyeegGYLTEAVRRRPYSVILLDEVEKAHP 684
Cdd:PRK04195 87 E----------AATSGSLFGARRKLILLDEVDGIHG 112
|
|
| 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 447157846 203 VLIGEPGVGKTAIVEGLAQR---------IINGEV-PEGLkgRRVLALDMGALVAGAkYRGEFEERLKGVLNDLAKQEGN 272
Cdd:COG3267 47 VLTGEVGTGKTTLLRRLLERlpddvkvayIPNPQLsPAEL--LRAIADELGLEPKGA-SKADLLRQLQEFLLELAAAGRR 123
|
90
....*....|.
gi 447157846 273 VILFIDELHTM 283
Cdd:COG3267 124 VVLIIDEAQNL 134
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
410-515 |
7.43e-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: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 410 EELDRLDRRIIQLKLEQQALMKESDEASK------KRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKAELEQAK 483
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASRKIGEIEKeieqleQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL 774
|
90 100 110
....*....|....*....|....*....|..
gi 447157846 484 IAIEQArrVGDLARMseLQYGKIPELEKQLEA 515
Cdd:TIGR02169 775 HKLEEA--LNDLEAR--LSHSRIPEIQAELSK 802
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
391-568 |
8.03e-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: 40.04 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 391 IDLIDEAASSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASK------KRLDMLNEELSDKERQYSELEEEWKA 464
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEelesleAELEELEAELEELESRLEELEEQLET 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 465 EKASLSGTQ----TIKAELEQAKIAIEQ-ARRVGDLARMSELQYGKIPELEKQlEAATQLEGKTMRLLRNKVTDAEIAEV 539
Cdd:TIGR02168 384 LRSKVAQLElqiaSLNNEIERLEARLERlEDRRERLQQEIEELLKKLEEAELK-ELQAELEELEEELEELQEELERLEEA 462
|
170 180
....*....|....*....|....*....
gi 447157846 540 LARwtgipVSRMMESEREKLLRMEQELHH 568
Cdd:TIGR02168 463 LEE-----LREELEEAEQALDAAERELAQ 486
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
396-570 |
8.35e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 396 EAASSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASK--KRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQ 473
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKevKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447157846 474 TIKAELEQakiaieqarrvgdlarmselqygKIPELEKQLEAATQLEGK-----TMRLLRNKVTDA--EIAEVLARWTG- 545
Cdd:PRK03918 266 ERIEELKK-----------------------EIEELEEKVKELKELKEKaeeyiKLSEFYEEYLDElrEIEKRLSRLEEe 322
|
170 180 190
....*....|....*....|....*....|..
gi 447157846 546 -------IPVSRMMESEREKLLRMEQELHHRV 570
Cdd:PRK03918 323 ingieerIKELEEKEERLEELKKKLKELEKRL 354
|
|
| hslU |
PRK05201 |
ATP-dependent protease ATPase subunit HslU; |
564-619 |
9.37e-03 |
|
ATP-dependent protease ATPase subunit HslU;
Pssm-ID: 235364 [Multi-domain] Cd Length: 443 Bit Score: 39.29 E-value: 9.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447157846 564 QELHHRVIGQNEAVDAVSNAI----RRSRagLADPNR----P--IgsfLFLGPTGVGKTELCKALA 619
Cdd:PRK05201 11 SELDKYIIGQDDAKRAVAIALrnrwRRMQ--LPEELRdevtPknI---LMIGPTGVGKTEIARRLA 71
|
|
|