|
Name |
Accession |
Description |
Interval |
E-value |
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
6-852 |
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: 1577.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 6 LTSKLQLALSDSQSLAVGLDHPAIEPAHLMQALLEQQGGSIKPLLMQVGFDVNSLRKELSKELDQLPKIQNPTGDVNMSQ 85
Cdd:TIGR03346 1 LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEKELERLPKVSGPGGQVYLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 86 DLARLLNQADRLAQQKGDQFISSELVLLAAMDENSKLGKLLLGQGVSKKALENAINNLRGGDAVNDPNHEESRQALDKYT 165
Cdd:TIGR03346 81 DLNRLLNLAEKLAQKRGDEFISSEHLLLALLDDKGTLGKLLKEAGATADALEAAINAVRGGQKVTDANAEDQYEALEKYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 166 VDLTKRAEEGKLDPVIGRDDEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIAEGLAQRIINGEVPDGLKGKRLLSLDMGSL 245
Cdd:TIGR03346 161 RDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLALDMGAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 246 IAGAKFRGEFEERLKSLLNELSKQEGQIILFIDELHTMVGAGKGEGSMDAGNMLKPALARGELHCVGATTLNEYRQYIEK 325
Cdd:TIGR03346 241 IAGAKYRGEFEERLKAVLNEVTKSEGQIILFIDELHTLVGAGKAEGAMDAGNMLKPALARGELHCIGATTLDEYRKYIEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 326 DAALERRFQKVLVEEPSEEDTIAILRGLKERYEVHHKVAITDGAIIAAAKLSHRYITDRQLPDKAIDLIDEAASRIRMEI 405
Cdd:TIGR03346 321 DAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAARIRMEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 406 DSKPEVLDRLDRRLIQLKVESQALKKEEDDAAKKRLEKLQEEIVRLEREYSDLEEIWTSEKAEVQGSAQIQQKIEQSRQE 485
Cdd:TIGR03346 401 DSKPEELDELDRRIIQLEIEREALKKEKDEASKKRLEDLEKELADLEEEYAELEEQWKAEKASIQGIQQIKEEIEQVRLE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 486 LEAARRKGDLNRMAELQYGVIPDLERSLQMVDQHGKSE-NQLLRSKVTEEEIAEVVSKWTGIPVSKMLEGERDKLLKMES 564
Cdd:TIGR03346 481 LEQAEREGDLAKAAELQYGKLPELEKQLQAAEQKLGEEqNRLLREEVTAEEIAEVVSRWTGIPVSKMLEGEREKLLHMEE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 565 LLHQRVIGQEEAVVAVSNAVRRSRAGLSDPNRPSGSFMFLGPTGVGKTELCKALAEFLFDTEEAMVRIDMSEFMEKHSVA 644
Cdd:TIGR03346 561 ELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRIDMSEYMEKHSVA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 645 RLIGAPPGYVGYEEGGYLTEAVRRKPYSVILLDEVEKAHPDVFNILLQVLEDGRLTDSHGRTVDFRNTVIVMTSNLGSAQ 724
Cdd:TIGR03346 641 RLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDF 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 725 IQELVG--DREAQRAAVMDALTTHFRPEFINRVDEVVIFEPLARDQIAGITEIQLGRLRGRLTERELSLDLSQEALDKLI 802
Cdd:TIGR03346 721 IQELAGgdDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKITLELSDAALDFLA 800
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 502155646 803 AVGYDPVYGARPLKRAIQRWIENPLAQLILSGSFMPGTSVTATVENDEIV 852
Cdd:TIGR03346 801 EAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGRLV 850
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1-852 |
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: 1471.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 1 MRIDRLTSKLQLALSDSQSLAVGLDHPAIEPAHLMQALLEQQGGSIKPLLMQVGFDVNSLRKELSKELDQLPKIQNPTGD 80
Cdd:COG0542 1 MNFEKFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGRLPKVSGSSGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 81 VNMSQDLARLLNQADRLAQQKGDQFISSELVLLAAM-DENSKLGKLLLGQGVSKKALENAINNLRGGDAVNDPNHEESRQ 159
Cdd:COG0542 81 PYLSPRLKRVLELAELEARKLGDEYISTEHLLLALLrEGEGVAARILKKLGITLEALREALEELRGGSRVTSQNPESKTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 160 ALDKYTVDLTKRAEEGKLDPVIGRDDEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIAEGLAQRIINGEVPDGLKGKRLLS 239
Cdd:COG0542 161 ALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDKRVLS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 240 LDMGSLIAGAKFRGEFEERLKSLLNELSKQEGQIILFIDELHTMVGAGKGEGSMDAGNMLKPALARGELHCVGATTLNEY 319
Cdd:COG0542 241 LDLGALVAGAKYRGEFEERLKAVLDEVKKSEGNIILFIDELHTLVGAGGAEGAMDAANLLKPALARGELRCIGATTLDEY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 320 RQYIEKDAALERRFQKVLVEEPSEEDTIAILRGLKERYEVHHKVAITDGAIIAAAKLSHRYITDRQLPDKAIDLIDEAAS 399
Cdd:COG0542 321 RKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAIDLIDEAAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 400 RIRMEIDSKPEVLDRLDRRLIQLKVESQALKKEEDDAAKKRLEKLQEEIVRLEREYSDLEEIWTSEKAEVQGSAQIQQKI 479
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 480 EQsrqeleaarrkgdlnrmaelQYGVIPDLERSLQMVDQHGKSENQLLRSKVTEEEIAEVVSKWTGIPVSKMLEGERDKL 559
Cdd:COG0542 481 EQ--------------------RYGKIPELEKELAELEEELAELAPLLREEVTEEDIAEVVSRWTGIPVGKLLEGEREKL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 560 LKMESLLHQRVIGQEEAVVAVSNAVRRSRAGLSDPNRPSGSFMFLGPTGVGKTELCKALAEFLFDTEEAMVRIDMSEFME 639
Cdd:COG0542 541 LNLEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYME 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 640 KHSVARLIGAPPGYVGYEEGGYLTEAVRRKPYSVILLDEVEKAHPDVFNILLQVLEDGRLTDSHGRTVDFRNTVIVMTSN 719
Cdd:COG0542 621 KHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSN 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 720 LGSAQIQELVGDR---EAQRAAVMDALTTHFRPEFINRVDEVVIFEPLARDQIAGITEIQLGRLRGRLTERELSLDLSQE 796
Cdd:COG0542 701 IGSELILDLAEDEpdyEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDA 780
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 502155646 797 ALDKLIAVGYDPVYGARPLKRAIQRWIENPLAQLILSGSFMPGTSVTATVENDEIV 852
Cdd:COG0542 781 AKDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGELV 836
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
1-854 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 1315.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 1 MRIDRLTSKLQLALSDSQSLAVGLDHPAIEPAHLMQALLEQQGGSIKPLLMQVGFDVNSLRKELSKELDQLPKIQNPTGD 80
Cdd:PRK10865 1 MRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVRPLLTSAGINAGQLRTDINQALSRLPQVEGTGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 81 VNMSQDLARLLNQADRLAQQKGDQFISSELVLLAAMDENSKLGKLLLGQGVSKKALENAINNLRGGDAVNDPNHEESRQA 160
Cdd:PRK10865 81 VQPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAALESRGTLADILKAAGATTANITQAIEQMRGGESVNDQGAEDQRQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 161 LDKYTVDLTKRAEEGKLDPVIGRDDEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIAEGLAQRIINGEVPDGLKGKRLLSL 240
Cdd:PRK10865 161 LKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 241 DMGSLIAGAKFRGEFEERLKSLLNELSKQEGQIILFIDELHTMVGAGKGEGSMDAGNMLKPALARGELHCVGATTLNEYR 320
Cdd:PRK10865 241 DMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 321 QYIEKDAALERRFQKVLVEEPSEEDTIAILRGLKERYEVHHKVAITDGAIIAAAKLSHRYITDRQLPDKAIDLIDEAASR 400
Cdd:PRK10865 321 QYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 401 IRMEIDSKPEVLDRLDRRLIQLKVESQALKKEEDDAAKKRLEKLQEEIVRLEREYSDLEEIWTSEKAEVQGSAQIQQKIE 480
Cdd:PRK10865 401 IRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKAELE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 481 QSRQELEAARRKGDLNRMAELQYGVIPDLERSLQMVDQHGKSENQLLRSKVTEEEIAEVVSKWTGIPVSKMLEGERDKLL 560
Cdd:PRK10865 481 QAKIAIEQARRVGDLARMSELQYGKIPELEKQLAAATQLEGKTMRLLRNKVTDAEIAEVLARWTGIPVSRMLESEREKLL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 561 KMESLLHQRVIGQEEAVVAVSNAVRRSRAGLSDPNRPSGSFMFLGPTGVGKTELCKALAEFLFDTEEAMVRIDMSEFMEK 640
Cdd:PRK10865 561 RMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEK 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 641 HSVARLIGAPPGYVGYEEGGYLTEAVRRKPYSVILLDEVEKAHPDVFNILLQVLEDGRLTDSHGRTVDFRNTVIVMTSNL 720
Cdd:PRK10865 641 HSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNL 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 721 GSAQIQELVGDRE--AQRAAVMDALTTHFRPEFINRVDEVVIFEPLARDQIAGITEIQLGRLRGRLTERELSLDLSQEAL 798
Cdd:PRK10865 721 GSDLIQERFGELDyaHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYEIHISDEAL 800
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 502155646 799 DKLIAVGYDPVYGARPLKRAIQRWIENPLAQLILSGSFMPGTSVTATVENDEIVFH 854
Cdd:PRK10865 801 KLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDDRIVAV 856
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
3-849 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 868.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 3 IDRLTSKLQLALSDSQSLAVGLDHPAIEPAHLMQALLEQQGGSIKPLLMQVGFDVNSLRKE-----------LSKELDQL 71
Cdd:CHL00095 2 FERFTEKAIKVIMLSQEEARRLGHNFVGTEQILLGLIGEGTGIAARALKSMGVTLKDARIEvekiigrgtgfVAVEIPFT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 72 PKIQnptgdvnmsqdlaRLLNQADRLAQQKGDQFISSELVLLAAMDENSKLGKLLLGQ-GVSKKALENAINNLRGG--DA 148
Cdd:CHL00095 82 PRAK-------------RVLEMSLEEARDLGHNYIGTEHLLLALLEEGEGVAARVLENlGVDLSKIRSLILNLIGEiiEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 149 VNDPNHEESRQ-ALDKYTVDLTKRAEEGKLDPVIGRDDEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIAEGLAQRIINGE 227
Cdd:CHL00095 149 ILGAEQSRSKTpTLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 228 VPDGLKGKRLLSLDMGSLIAGAKFRGEFEERLKSLLNELsKQEGQIILFIDELHTMVGAGKGEGSMDAGNMLKPALARGE 307
Cdd:CHL00095 229 VPDILEDKLVITLDIGLLLAGTKYRGEFEERLKRIFDEI-QENNNIILVIDEVHTLIGAGAAEGAIDAANILKPALARGE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 308 LHCVGATTLNEYRQYIEKDAALERRFQKVLVEEPSEEDTIAILRGLKERYEVHHKVAITDGAIIAAAKLSHRYITDRQLP 387
Cdd:CHL00095 308 LQCIGATTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 388 DKAIDLIDEAASRIRMEIDSKPEVLDRLDRRLiqlkvesqalkkeeddaakKRLEKLQEEIVRLEreysDLEEIWTSEKA 467
Cdd:CHL00095 388 DKAIDLLDEAGSRVRLINSRLPPAARELDKEL-------------------REILKDKDEAIREQ----DFETAKQLRDR 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 468 EVQGSAQIQQKIEQSRqeleaarrkgdlnrmaelqygvipdlerslqmvdqhGKSENQLLRSKVTEEEIAEVVSKWTGIP 547
Cdd:CHL00095 445 EMEVRAQIAAIIQSKK------------------------------------TEEEKRLEVPVVTEEDIAEIVSAWTGIP 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 548 VSKMLEGERDKLLKMESLLHQRVIGQEEAVVAVSNAVRRSRAGLSDPNRPSGSFMFLGPTGVGKTELCKALAEFLFDTEE 627
Cdd:CHL00095 489 VNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALASYFFGSED 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 628 AMVRIDMSEFMEKHSVARLIGAPPGYVGYEEGGYLTEAVRRKPYSVILLDEVEKAHPDVFNILLQVLEDGRLTDSHGRTV 707
Cdd:CHL00095 569 AMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTI 648
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 708 DFRNTVIVMTSNLGSAQIQ--------ELVGDREAQ------RAAVMDALTTHFRPEFINRVDEVVIFEPLARDQIAGIT 773
Cdd:CHL00095 649 DFKNTLIIMTSNLGSKVIEtnsgglgfELSENQLSEkqykrlSNLVNEELKQFFRPEFLNRLDEIIVFRQLTKNDVWEIA 728
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502155646 774 EIQLGRLRGRLTERELSLDLSQEALDKLIAVGYDPVYGARPLKRAIQRWIENPLAQLILSGSFMPGTSVTATVEND 849
Cdd:CHL00095 729 EIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVDVNDE 804
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
6-833 |
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: 792.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 6 LTSKLQLALSDSQSLAVGLDHPAIEPAHLMQALLEQQGGSIKPLLMQVGFDVNSLRKELSKELDQLPKIQNPTGDVnmSQ 85
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLARALDKLPRGNTRTPVF--SP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 86 DLARLLNQADRLAQ-QKGDQFISSELVLLAAMDENSKLGKLL----LGQGVSKKALENAINNLRGGDA-----------V 149
Cdd:TIGR03345 79 HLVELLQEAWLLASlELGDGRIRSGHLLLALLTDPELRRLLGsispELAKIDREALREALPALVEGSAeasaaaadaapA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 150 NDPNHEESRQALDKYTVDLTKRAEEGKLDPVIGRDDEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIAEGLAQRIINGEVP 229
Cdd:TIGR03345 159 GAAAGAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 230 DGLKGKRLLSLDMGSLIAGAKFRGEFEERLKSLLNELSKQEGQIILFIDELHTMVGAGKGEGSMDAGNMLKPALARGELH 309
Cdd:TIGR03345 239 PALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPIILFIDEAHTLIGAGGQAGQGDAANLLKPALARGELR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 310 CVGATTLNEYRQYIEKDAALERRFQKVLVEEPSEEDTIAILRGLKERYEVHHKVAITDGAIIAAAKLSHRYITDRQLPDK 389
Cdd:TIGR03345 319 TIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLPDK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 390 AIDLIDEAASRIRMEIDSKPEVLDRLDRRLIQLKVESQALKKEE----DDAAkkRLEKLQEEIVRLEREYSDLEEIWTSE 465
Cdd:TIGR03345 399 AVSLLDTACARVALSQNATPAALEDLRRRIAALELELDALEREAalgaDHDE--RLAELRAELAALEAELAALEARWQQE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 466 KAEVQGSAQIQQKIEQSrQELEAARRKGDLNRMAElqygvipdLERSLQMVDQhgksENQLLRSKVTEEEIAEVVSKWTG 545
Cdd:TIGR03345 477 KELVEAILALRAELEAD-ADAPADDDDALRAQLAE--------LEAALASAQG----EEPLVFPEVDAQAVAEVVADWTG 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 546 IPVSKMLEGERDKLLKMESLLHQRVIGQEEAVVAVSNAVRRSRAGLSDPNRPSGSFMFLGPTGVGKTELCKALAEFLFDT 625
Cdd:TIGR03345 544 IPVGRMVRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGG 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 626 EEAMVRIDMSEFMEKHSVARLIGAPPGYVGYEEGGYLTEAVRRKPYSVILLDEVEKAHPDVFNILLQVLEDGRLTDSHGR 705
Cdd:TIGR03345 624 EQNLITINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGR 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 706 TVDFRNTVIVMTSNLGSAQIQELVGDR------EAQRAAVMDALTTHFRPEFINRVdEVVIFEPLARDQIAGITEIQLGR 779
Cdd:TIGR03345 704 EIDFKNTVILLTSNAGSDLIMALCADPetapdpEALLEALRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDR 782
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 502155646 780 LRGRLTER-ELSLDLSQEALDKLIAVGYDPVYGARPLKRAIQRWIENPLAQLILS 833
Cdd:TIGR03345 783 IARRLKENhGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQILE 837
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
6-842 |
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: 744.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 6 LTSKLQLALSDSQSLAVGLDHPAIEPAHLMQALLEQQGGsiKPLLMQVGFDVNSLRKELSKELDQ-LPKI-QNPTGDVNM 83
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEA--IEILEECGGDVELLRKRLEDYLEEnLPVIpEDIDEEPEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 84 SQDLARLLNQADRLAQQKGDQFISSELVLLAAMDENSKLGKLLLG-QGVSKKALENAINNLRGGDAVNDP------NHEE 156
Cdd:TIGR02639 79 TVGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKsQGITRLDILNYISHGISKDDGKDQlgeeagKEEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 157 SRQ-ALDKYTVDLTKRAEEGKLDPVIGRDDEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIAEGLAQRIINGEVPDGLKGK 235
Cdd:TIGR02639 159 KGQdALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERLKNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 236 RLLSLDMGSLIAGAKFRGEFEERLKSLLNELSKQEGQIiLFIDELHTMVGAGK-GEGSMDAGNMLKPALARGELHCVGAT 314
Cdd:TIGR02639 239 KIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAI-LFIDEIHTIVGAGAtSGGSMDASNLLKPALSSGKIRCIGST 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 315 TLNEYRQYIEKDAALERRFQKVLVEEPSEEDTIAILRGLKERYEVHHKVAITDGAIIAAAKLSHRYITDRQLPDKAIDLI 394
Cdd:TIGR02639 318 TYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDVI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 395 DEAASRIRMEIDSKPevldrldrrliqlkvesqalkkeeddaakkrleklqeeivrlereysdleeiwtsekaevqgsaq 474
Cdd:TIGR02639 398 DEAGAAFRLRPKAKK----------------------------------------------------------------- 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 475 iqqkieqsrqeleaarrkgdlnrmaelqygvipdlerslqmvdqhgksenqllRSKVTEEEIAEVVSKWTGIPVSKMLEG 554
Cdd:TIGR02639 413 -----------------------------------------------------KANVNVKDIENVVAKMAKIPVKTVSSD 439
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 555 ERDKLLKMESLLHQRVIGQEEAVVAVSNAVRRSRAGLSDPNRPSGSFMFLGPTGVGKTELCKALAEFLfdtEEAMVRIDM 634
Cdd:TIGR02639 440 DREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEEL---GVHLLRFDM 516
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 635 SEFMEKHSVARLIGAPPGYVGYEEGGYLTEAVRRKPYSVILLDEVEKAHPDVFNILLQVLEDGRLTDSHGRTVDFRNTVI 714
Cdd:TIGR02639 517 SEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVIL 596
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 715 VMTSNLGSAQIQE----LVGDREAqrAAVMDALTTHFRPEFINRVDEVVIFEPLARDQIAGITEIQLGRLRGRLTERELS 790
Cdd:TIGR02639 597 IMTSNAGASEMSKppigFGGENRE--SKSLKAIKKLFSPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIE 674
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 502155646 791 LDLSQEALDKLIAVGYDPVYGARPLKRAIQRWIENPLAQLILSGSFMPGTSV 842
Cdd:TIGR02639 675 LELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEILFGKLKKGGSV 726
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
6-853 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 557.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 6 LTSKLQLALSDSQSLAVGLDHPAIEPAHLMQALLEQQggSIKPLLMQVGFDVNSLRKELSKELDQ----LPKiQNPTGDV 81
Cdd:PRK11034 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNP--SAREALEACSVDLVALRQELEAFIEQttpvLPA-SEEERDT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 82 NMSQDLARLLNQADRLAQQKGDQFISSELVLLAAMDEN-SKLGKLLLGQGVSKKALENAIN-------NLRGGDAVNDPN 153
Cdd:PRK11034 79 QPTLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQeSQAAYLLRKHEVSRLDVVNFIShgtrkdePSQSSDPGSQPN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 154 HEE---SRQALDKYTVDLTKRAEEGKLDPVIGRDDEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIAEGLAQRIINGEVPD 230
Cdd:PRK11034 159 SEEqagGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 231 GLKGKRLLSLDMGSLIAGAKFRGEFEERLKSLLNELsKQEGQIILFIDELHTMVGAGKGE-GSMDAGNMLKPALARGELH 309
Cdd:PRK11034 239 VMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQL-EQDTNSILFIDEIHTIIGAGAASgGQVDAANLIKPLLSSGKIR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 310 CVGATTLNEYRQYIEKDAALERRFQKVLVEEPSEEDTIAILRGLKERYEVHHKVAITDGAIIAAAKLSHRYITDRQLPDK 389
Cdd:PRK11034 318 VIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 390 AIDLIDEAASRIRMeidskpevldrldrrliqlkvesqalkkeeddaakkrleklqeeivrlereysdleeiwtsekaev 469
Cdd:PRK11034 398 AIDVIDEAGARARL------------------------------------------------------------------ 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 470 qgsaqiqqkieqsrqeLEAARRKGDLNrmaelqygvIPDLErslqmvdqhgksenqllrskvteeeiaEVVSKWTGIPVS 549
Cdd:PRK11034 412 ----------------MPVSKRKKTVN---------VADIE---------------------------SVVARIARIPEK 439
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 550 KMLEGERDKLLKMESLLHQRVIGQEEAVVAVSNAVRRSRAGLSDPNRPSGSFMFLGPTGVGKTELCKALAEFLfDTEeaM 629
Cdd:PRK11034 440 SVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL-GIE--L 516
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 630 VRIDMSEFMEKHSVARLIGAPPGYVGYEEGGYLTEAVRRKPYSVILLDEVEKAHPDVFNILLQVLEDGRLTDSHGRTVDF 709
Cdd:PRK11034 517 LRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADF 596
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 710 RNTVIVMTSNLGSAQIQE----LVGDREAQRAavMDALTTHFRPEFINRVDEVVIFEPLARDQIAGITEIQLGRLRGRLT 785
Cdd:PRK11034 597 RNVVLVMTTNAGVRETERksigLIHQDNSTDA--MEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLD 674
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502155646 786 ERELSLDLSQEALDKLIAVGYDPVYGARPLKRAIQRWIENPLAQLILSGSFMPGTSVTATVENDEIVF 853
Cdd:PRK11034 675 QKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKEKNEL 742
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
558-761 |
1.58e-110 |
|
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: 335.69 E-value: 1.58e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 558 KLLKMESLLHQRVIGQEEAVVAVSNAVRRSRAGLSDPNRPSGSFMFLGPTGVGKTELCKALAEFLFDTEEAMVRIDMSEF 637
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 638 MEKHSVARLIGAPPGYVGYEEGGYLTEAVRRKPYSVILLDEVEKAHPDVFNILLQVLEDGRLTDSHGRTVDFRNTVIVMT 717
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502155646 718 SNlgsaqiqelvgdreaqraavmdalttHFRPEFINRVDEVVIF 761
Cdd:cd19499 161 SN--------------------------HFRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
596-758 |
1.98e-92 |
|
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400187 [Multi-domain] Cd Length: 168 Bit Score: 287.94 E-value: 1.98e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 596 RPSGSFMFLGPTGVGKTELCKALAEFLFDTEEAMVRIDMSEFMEKHSVARLIGAPPGYVGYEEGGYLTEAVRRKPYSVIL 675
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 676 LDEVEKAHPDVFNILLQVLEDGRLTDSHGRTVDFRNTVIVMTSNLGSAQIQELVG-----DREAQRAAVMDALTTHFRPE 750
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRlgdspDYELLKEEVMDLLKKGFIPE 160
|
....*...
gi 502155646 751 FINRVDEV 758
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 |
4.92e-47 |
|
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: 162.66 E-value: 4.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 342 SEEDTIAILRGLKERYEVHHKVAITDGAIIAAAKLSHRYITDRQLPDKAIDLIDEAASRIRMEIDSKPEVLDRLDRRLIQ 421
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|....
gi 502155646 422 LKVESQALKKEEDDAAKKRLEKLQ 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, ... |
764-843 |
7.39e-26 |
|
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: 101.71 E-value: 7.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 764 LARDQIAGITEIQLGRLRGRLTERELSLDLSQEALDKLIAVGYDPVYGARPLKRAIQRWIENPLAQLILSGSFMPGTSVT 843
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
764-853 |
9.82e-26 |
|
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerisation, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilise the functional assembly. The domain is associated with two Clp_N at the N-terminus as well as AAA and AAA_2.
Pssm-ID: 198154 [Multi-domain] Cd Length: 90 Bit Score: 101.37 E-value: 9.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 764 LARDQIAGITEIQLGRLRGRLTERELSLDLSQEALDKLIAVGYDPVYGARPLKRAIQRWIENPLAQLILSGSFMPGTSVT 843
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
90
....*....|
gi 502155646 844 ATVENDEIVF 853
Cdd:smart01086 81 VDVDDGELVF 90
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
181-341 |
3.16e-21 |
|
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: 91.05 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 181 IGRDDEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIAEGLAQRIINgevpdglKGKRLLSLDMGSLIAGAKFRGEFEERLK 260
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFR-------PGAPFLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 261 SLLNELSKQEGQIILFIDELHTMvGAGKGEGSMDAGNMLKPALA-RGELHCVGATTLNEYRQyieKDAALERRFQKVLVE 339
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDSL-SRGAQNALLRVLETLNDLRIdRENVRVIGATNRPLLGD---LDRALYDRLDIRIVI 149
|
..
gi 502155646 340 EP 341
Cdd:cd00009 150 PL 151
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
571-725 |
8.79e-19 |
|
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: 83.73 E-value: 8.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 571 IGQEEAVVAVSNAVRRsraglsdpnRPSGSFMFLGPTGVGKTELCKALAEFLFDTEEAMVRIDMSEFMEKHSVARLIGAP 650
Cdd:cd00009 1 VGQEEAIEALREALEL---------PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502155646 651 PGYVgyeeggyLTEAVRRKPYSVILLDEVEKAHPDVFNILLQVLEDGRLTdshgrTVDFRNTVIVMTSNLGSAQI 725
Cdd:cd00009 72 LVRL-------LFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATNRPLLGD 134
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
597-732 |
3.91e-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: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 597 PSGSFMFLGPTGVGKTELCKALAEFLFDTEEAMVRIDMSEFMEKHSVARLIGAPPGYVGYEEGGY----LTEAVRRKPYS 672
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 673 VILLDEVEKAHPDVFNILLQVLEDGRLTDSHGRtvdFRNTVIVMTSNLGSAQIQELVGDR 732
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTNDEKDLGPALLRRR 137
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
600-728 |
3.44e-13 |
|
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: 67.32 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 600 SFMFLGPTGVGKTELCKALAEFLFDTEEAMVRidMSEFMEKhsvARLIGA--PPGYVGYEEGGYLTEAVRRKpySVILLD 677
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQ--LTRDTTE---EDLFGRrnIDPGGASWVDGPLVRAAREG--EIAVLD 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 502155646 678 EVEKAHPDVFNILLQVLEDGRL-TDSHGRTVDFRNT--VIVMTSNLGSAQIQEL 728
Cdd:pfam07728 74 EINRANPDVLNSLLSLLDERRLlLPDGGELVKAAPDgfRLIATMNPLDRGLNEL 127
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
204-337 |
9.14e-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: 66.08 E-value: 9.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 204 LIGEPGVGKTAIAEGLAQRIingevpdglkGKRLLSLDMGSLIagAKFRGEFEERLKSLLNELsKQEGQIILFIDELHTM 283
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELV--SKYVGESEKRLRELFEAA-KKLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502155646 284 VGA---GKGEGSMDAGNMLKPAL-----ARGELHCVGATTlneyrqYIEK-DAALERRFQKVL 337
Cdd:pfam00004 70 AGSrgsGGDSESRRVVNQLLTELdgftsSNSKVIVIAATN------RPDKlDPALLGRFDRII 126
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
38-423 |
3.26e-09 |
|
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: 59.92 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 38 LLEQQGGSIKPLLMQVGFDVNSLRKELSKELDQLPKIQNPTGDVNMSQDLARLLNQADRLAQQKGDQFISSELVLLAAMD 117
Cdd:COG0464 16 LLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 118 ENSKLGKLLLGQGVSKKALENAINNLRGGDAVNDPNHEESRQALDKYT-VDLTKRAEEGKLDPVIGRDD---EIRRTIQV 193
Cdd:COG0464 96 ELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGlEEELLELREAILDDLGGLEEvkeELRELVAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 194 LQRRTK-------NNP---VLIGEPGVGKTAIAEGLAQRIingevpdglkGKRLLSLDMGSLIagAKFRGEFEERLKSLL 263
Cdd:COG0464 176 PLKRPElreeyglPPPrglLLYGPPGTGKTLLARALAGEL----------GLPLIEVDLSDLV--SKYVGETEKNLREVF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 264 NELsKQEGQIILFIDELHTMVGAGKGEGSMDA----GNMLKpALA--RGELHCVGATtlneYRqyIEK-DAALERRFQKV 336
Cdd:COG0464 244 DKA-RGLAPCVLFIDEADALAGKRGEVGDGVGrrvvNTLLT-EMEelRSDVVVIAAT----NR--PDLlDPALLRRFDEI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 337 L-VEEPSEEDTIAILRGLKERYEVHHKVAITDgaiIAAAK--LSHRYItdRQLPDKAIDLideAASRIRMEIdSKPEVLD 413
Cdd:COG0464 316 IfFPLPDAEERLEIFRIHLRKRPLDEDVDLEE---LAEATegLSGADI--RNVVRRAALQ---ALRLGREPV-TTEDLLE 386
|
410
....*....|
gi 502155646 414 RLDRRLIQLK 423
Cdd:COG0464 387 ALEREDIFLK 396
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
574-761 |
3.17e-08 |
|
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: 53.83 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 574 EEAVVAVSNAVRRSRAGLsdpNRPSGsFMFLGPTGVGKTELCKALAEFLFDTeeaMVRIDMSEFMEKHSvarligappgY 653
Cdd:cd19481 6 REAVEAPRRGSRLRRYGL---GLPKG-ILLYGPPGTGKTLLAKALAGELGLP---LIVVKLSSLLSKYV----------G 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 654 VGYEEGGYLTEAVRRKPYSVILLDEVEKAHPD------------VFNILLQVLEDGRLTDshgrtvdfrNTVIVMTSNlg 721
Cdd:cd19481 69 ESEKNLRKIFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAATN-- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502155646 722 saqiqelvgdreaqRAAVMDaltthfrPEFI--NRVDEVVIF 761
Cdd:cd19481 138 --------------RPDLLD-------PALLrpGRFDEVIEF 158
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
17-69 |
3.44e-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: 50.60 E-value: 3.44e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 502155646 17 SQSLAVGLDHPAIEPAHLMQALLEQQGGSIKPLLMQVGFDVNSLRKELSKELD 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 |
1.05e-07 |
|
Clp amino terminal domain, pathogenicity island component; This short domain is found in one or two copies at the amino terminus of ClpA and ClpB proteins from bacteria and eukaryotes. The function of these domains is uncertain but they may form a protein binding site. In many bacterial species, including E.coli, this region represents the N-terminus of one of the key components of the pathogenicity island complex that injects toxin from one bacterium into another.
Pssm-ID: 460724 [Multi-domain] Cd Length: 53 Bit Score: 49.06 E-value: 1.05e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 502155646 94 ADRLAQQKGDQFISSELVLLAAMDE-NSKLGKLLLGQGVSKKALENAINNLRG 145
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEdDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
198-343 |
3.68e-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: 50.45 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 198 TKNNPVLIGEPGVGKTAIAEGLAQRI---------INGEVPDglkgKRLLSLDMGSLIAGAKFRGEFEERLKsLLNELSK 268
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELgppgggviyIDGEDIL----EEVLDQLLLIIVGGKKASGSGELRLR-LALALAR 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502155646 269 QEGQIILFIDELHTMVGAG--KGEGSMDAGNMLKPALARGELHCVGATTLNEyrqyIEKDAALERRFQKVLVEEPSE 343
Cdd:smart00382 76 KLKPDVLILDEITSLLDAEqeALLLLLEELRLLLLLKSEKNLTVILTTNDEK----DLGPALLRRRFDRRIVLLLIL 148
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
602-719 |
4.67e-07 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 49.51 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 602 MFLGPTGVGKTELCKALAEFLFDTeeaMVRIDMSEFMEKHsvarlIGAPPGYVgyeeGGYLTEAVRRKPySVILLDEVEK 681
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAP---FIEISGSELVSKY-----VGESEKRL----RELFEAAKKLAP-CVIFIDEIDA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 502155646 682 AHP-----------DVFNILLQVLEdgrltdshGRTVDFRNTVIVMTSN 719
Cdd:pfam00004 69 LAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
177-381 |
2.90e-06 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 49.50 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 177 LDPVIGrDDEIRRTIQVL---QRRTKN----------NPVLIGEPGVGKTAIAEGLAQRIingevpdglkGKRLLSLDMG 243
Cdd:COG1223 1 LDDVVG-QEEAKKKLKLIikeLRRRENlrkfglwpprKILFYGPPGTGKTMLAEALAGEL----------KLPLLTVRLD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 244 SLIAgaKFRGEFEERLKSLLNELSKQEGqiILFIDELHTMvgagkgegsmdagnmlkpALARGELHCVG--ATTLNEYRQ 321
Cdd:COG1223 70 SLIG--SYLGETARNLRKLFDFARRAPC--VIFFDEFDAI------------------AKDRGDQNDVGevKRVVNALLQ 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502155646 322 YIEK-----------------DAALERRFQKVL-VEEPSEEDTIAILRGLKERYEVhhKVAITDGAIIAAAK-LSHRYI 381
Cdd:COG1223 128 ELDGlpsgsvviaatnhpellDSALWRRFDEVIeFPLPDKEERKEILELNLKKFPL--PFELDLKKLAKKLEgLSGADI 204
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
410-779 |
3.90e-06 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 50.29 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 410 EVLDRLDRRLIQLKVESQALKKEEDDAAKKRLEKLQEEIVRLEREYSDLEEIWTSEKAEVQGSAQIQQKIEQSRQELEAA 489
Cdd:COG0464 5 LALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 490 RRKGDLNRMAELQYGVIPDLERSLQMVDQHGKSENQLLRSKVTEEEIAEVVSKWTGIPVSKMLEGERDKLLKMESLLHQR 569
Cdd:COG0464 85 LLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 570 VIGQ-EEAVVAVS-NAVRRSRAGLsdpnRPSGSFMFLGPTGVGKTELCKALAEFLfdtEEAMVRIDMSEFMEKhsvarli 647
Cdd:COG0464 165 VKEElRELVALPLkRPELREEYGL----PPPRGLLLYGPPGTGKTLLARALAGEL---GLPLIEVDLSDLVSK------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 648 gappgYVGyEEGGYLTEAV---RRKPYSVILLDEVEKAHPD-----------VFNILLQVLEDGRltdshgrtvdfRNTV 713
Cdd:COG0464 231 -----YVG-ETEKNLREVFdkaRGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR-----------SDVV 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502155646 714 IVMTSNLgsaqiqelvgdreaqraavMDALTthfrPEFINRVDEVVIFEPLARDQIAGITEIQLGR 779
Cdd:COG0464 294 VIAATNR-------------------PDLLD----PALLRRFDEIIFFPLPDAEERLEIFRIHLRK 336
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
596-691 |
1.29e-05 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 45.41 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 596 RPSGSFMFL-GPTGVGKTELCKALAEFLFDTEEAMVRIDMSEFMEK----HSVARLIGAPPGYVGYEEG--GYLTEAV-R 667
Cdd:pfam13401 2 RFGAGILVLtGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPkdllRALLRALGLPLSGRLSKEEllAALQQLLlA 81
|
90 100
....*....|....*....|....
gi 502155646 668 RKPYSVILLDEVEKAHPDVFNILL 691
Cdd:pfam13401 82 LAVAVVLIIDEAQHLSLEALEELR 105
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
566-681 |
3.58e-05 |
|
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: 45.45 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 566 LHQRVIGQEEA----VVAVSNAVRRSR--AGLSDPNRPSGSFMfLGPTGVGKTELCKALAEFlfdTEEAMVRIDMSEFME 639
Cdd:cd19498 9 LDKYIIGQDEAkravAIALRNRWRRMQlpEELRDEVTPKNILM-IGPTGVGKTEIARRLAKL---AGAPFIKVEATKFTE 84
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 502155646 640 KhsvarligappGYVGYEeggyLTEAVRRKPYSVILLDEVEK 681
Cdd:cd19498 85 V-----------GYVGRD----VESIIRDLVEGIVFIDEIDK 111
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
570-695 |
3.84e-05 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 46.72 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 570 VIGQEEAVVAVSNAVRRsraglsdpNRPSGSFMFLGPTGVGKTELCKALAEFLF----------DTEEAMVRIDMSEFME 639
Cdd:COG2812 12 VVGQEHVVRTLKNALAS--------GRLAHAYLFTGPRGVGKTTLARILAKALNcengptgepcGECESCRAIAAGSHPD 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 640 KHsvarLIGAPPGYVGYEEGGYLTEAVRRKPYS----VILLDEVEKAHPDVFNILLQVLE 695
Cdd:COG2812 84 VI----EIDAEASNIGVDDIRELIEKVSYAPVEgrykVYIIDEAHMLTTEAFNALLKTLE 139
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
196-335 |
4.09e-05 |
|
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410930 [Multi-domain] Cd Length: 170 Bit Score: 44.98 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 196 RRTKNNPVLIGEPGVGKTAIAEGLAQRIingevpdglkGKRLLSLDMGSLIagAKFRGEfEERLKSLLNELSKQEGQIIL 275
Cdd:cd19522 30 RRPWKGVLMVGPPGTGKTLLAKAVATEC----------GTTFFNVSSSTLT--SKYRGE-SEKLVRLLFEMARFYAPTTI 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502155646 276 FIDELHTMVGAGKGEGSMDAGNMLKPALARgELHCVGATTLNEYRQYI-----------EKDAALERRFQK 335
Cdd:cd19522 97 FIDEIDSICSRRGTSEEHEASRRVKSELLV-QMDGVGGASENDDPSKMvmvlaatnfpwDIDEALRRRLEK 166
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
391-591 |
4.71e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 391 IDLIDEAASRIRMEIDSKPEVLDRLDRRLIQLKVESQALKKEED------DAAKKRLEKLQEEIVRLEREYSDLEEIWTS 464
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEelkeelESLEAELEELEAELEELESRLEELEEQLET 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 465 EKAEVqgsAQIQQKIEQSRQELEAAR-RKGDLNRMAELQYGVIPDLERSLQmvdqhgKSENQLLRSKVTEEEIAEvvskw 543
Cdd:TIGR02168 384 LRSKV---AQLELQIASLNNEIERLEaRLERLEDRRERLQQEIEELLKKLE------EAELKELQAELEELEEEL----- 449
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502155646 544 tgipvsKMLEGERDKLLKMESLLHQRVIGQEEAVVAVSNAVRRSRAGL 591
Cdd:TIGR02168 450 ------EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
347-492 |
9.19e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 9.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 347 IAILRGLKERYEVHHKvAITDGAIIAAAKLSHRYITDRQlpdkAIDLIDEAASRIRMEIDSKPEVLDRLDRRLIQLKVES 426
Cdd:COG4913 251 IELLEPIRELAERYAA-ARERLAELEYLRAALRLWFAQR----RLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502155646 427 QALKKEEDDAAKKRLEKLQEEIVRLEREYSDLEEIWTSEKAEVqgsAQIQQKIEQSRQELEAARRK 492
Cdd:COG4913 326 DELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALL---AALGLPLPASAEEFAALRAE 388
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
147-403 |
1.10e-04 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 45.38 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 147 DAVNDPNHEESRQALDKYTVDLTKRAEEgKLDPVIGRDDEIRRTIQVLQRRTKNN---------PV----LIGEPGVGKT 213
Cdd:COG1222 48 LLLNDANLTQKRLGTPRGTAVPAESPDV-TFDDIGGLDEQIEEIREAVELPLKNPelfrkygiePPkgvlLYGPPGTGKT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 214 AIAEGLAQR----IINgevpdgLKGKRLLSldmgsliagaKFRGEFEERLKSLLnELSKQEGQIILFIDELHTMVGAGKG 289
Cdd:COG1222 127 LLAKAVAGElgapFIR------VRGSELVS----------KYIGEGARNVREVF-ELAREKAPSIIFIDEIDAIAARRTD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 290 EGSMDAGNMLKPAL--------ARGELHCVGATtlNeyrqYIEK-DAALER--RF-QKVLVEEPSEEDTIAILRGLKERY 357
Cdd:COG1222 190 DGTSGEVQRTVNQLlaeldgfeSRGDVLIIAAT--N----RPDLlDPALLRpgRFdRVIEVPLPDEEAREEILKIHLRDM 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502155646 358 EVHHKV------AITDG------------AIIAAAKLSHRYITDRQLpDKAIDLIDEAASRIRM 403
Cdd:COG1222 264 PLADDVdldklaKLTEGfsgadlkaivteAGMFAIREGRDTVTMEDL-EKAIEKVKKKTETATN 326
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
566-622 |
1.66e-04 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410905 [Multi-domain] Cd Length: 251 Bit Score: 44.13 E-value: 1.66e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502155646 566 LHQRVIGQEEA----VVAVSNAVRRSRAGLSDPNR----PSGSFMFLGPTGVGKTELCKALAEFL 622
Cdd:cd19497 10 LDKYVIGQERAkkvlSVAVYNHYKRIRNNLKQKDDdvelEKSNILLIGPTGSGKTLLAQTLAKIL 74
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
204-283 |
2.15e-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: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 204 LIGEPGVGKTAIAEGLAQRIingevpdglkGKRLLSLDMGSLIagAKFRGEFEERLKSLLNELsKQEGQIILFIDELHTM 283
Cdd:cd19481 31 LYGPPGTGKTLLAKALAGEL----------GLPLIVVKLSSLL--SKYVGESEKNLRKIFERA-RRLAPCILFIDEIDAI 97
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
388-502 |
2.89e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 388 DKAIDLIDEAASRIRMEIDSKPEVLDRLDRRLIQLKVESQALKKEEDdAAKKRLEKLQEEIVRLEREYSDLEEIWTSEKA 467
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA-ELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
90 100 110
....*....|....*....|....*....|....*
gi 502155646 468 EVQGSAQIQQKIEQSRQELEAARRKGDLNRMAELQ 502
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
405-612 |
7.18e-04 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 42.96 E-value: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 405 IDSKPEVLDRLDRRLIQLKVESQALKKEEDDAAKKRLEKLQEEIVRLEREYSDLEEIWTSEKAEVQGSAQIQQKIEQSRQ 484
Cdd:PRK05703 51 VDEDETPKKNPVLREEKRKPAKSILSLQALLEKRPSRTNSQDALLQAENALPEWKKELEKPSEPKEEEPKAAAESKVVQK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 485 ELEAARRKgdlnrMAELQyGVIPDLERSLQMVdQHGKSENQLLRSKVTEEEIAEVVskwtgipvskmlegeRDKLLKMes 564
Cdd:PRK05703 131 ELDELRDE-----LKELK-NLLEDQLSGLRQV-ERIPPEFAELYKRLKRSGLSPEI---------------AEKLLKL-- 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502155646 565 LLHQRVIGQEEAVVAVSNAVRRS-RAGLSDPNRPSGSFMFLGPTGVGKT 612
Cdd:PRK05703 187 LLEHMPPRERTAWRYLLELLANMiPVRVEDILKQGGVVALVGPTGVGKT 235
|
|
| RecA-like_Figl-1 |
cd19525 |
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ... |
203-337 |
1.27e-03 |
|
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410933 [Multi-domain] Cd Length: 186 Bit Score: 40.74 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 203 VLIGEPGVGKTAIAEGLAQRiingevpdglKGKRLLSLDMGSLIagAKFRGEFEERLKSLLNELSKQEGQIIlFIDELHT 282
Cdd:cd19525 59 LLFGPPGTGKTLIGKCIASQ----------SGATFFSISASSLT--SKWVGEGEKMVRALFSVARCKQPAVI-FIDEIDS 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502155646 283 MVgAGKGEGSMDAGNMLKPALArgeLHCVGATTLNEYRQYI--------EKDAALERRFQKVL 337
Cdd:cd19525 126 LL-SQRGEGEHESSRRIKTEFL---VQLDGATTSSEDRILVvgatnrpqEIDEAARRRLVKRL 184
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
332-570 |
1.29e-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: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 332 RFQKVLVEEPSEEDTIAILRGLKERY-EVHHKVAITDGAIIAAAKLSHRyiTDRQLPDKAIDLIDEAASRIRMEIDSKPE 410
Cdd:TIGR02169 188 RLDLIIDEKRQQLERLRREREKAERYqALLKEKREYEGYELLKEKEALE--RQKEAIERQLASLEEELEKLTEEISELEK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 411 VLDRLDRRLIQLKVESQALKKEEDDAAKKRLEKLQEEIVRLER-------EYSDLEEiwTSEKAEVQGSAQiQQKIEQSR 483
Cdd:TIGR02169 266 RLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERsiaekerELEDAEE--RLAKLEAEIDKL-LAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 484 QELEAARRKGD--LNRMAELQyGVIPDLERSLQMVDqhgkSENQLLRSKVTE--EEIAEVVSKwtgipvSKMLEGERDKL 559
Cdd:TIGR02169 343 REIEEERKRRDklTEEYAELK-EELEDLRAELEEVD----KEFAETRDELKDyrEKLEKLKRE------INELKRELDRL 411
|
250
....*....|.
gi 502155646 560 LKMESLLHQRV 570
Cdd:TIGR02169 412 QEELQRLSEEL 422
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
389-492 |
1.35e-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: 41.06 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 389 KAIDLIDEAASRIRMEIDSKPEVLDRLDRRLIQLKV--ESQALKKEEDDAAKK-------------RLEKLQEEIVRLER 453
Cdd:COG1579 52 TELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKEIESLKRRisdledeilelmeRIEELEEELAELEA 131
|
90 100 110
....*....|....*....|....*....|....*....
gi 502155646 454 EYSDLEEIWTSEKAEVQgsaQIQQKIEQSRQELEAARRK 492
Cdd:COG1579 132 ELAELEAELEEKKAELD---EELAELEAELEELEAEREE 167
|
|
| RecA-like_VPS4 |
cd19521 |
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ... |
203-335 |
1.36e-03 |
|
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. 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: 410929 [Multi-domain] Cd Length: 170 Bit Score: 40.62 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 203 VLIGEPGVGKTAIAEGLAQRIingevpdglkGKRLLSLDMGSLIAgaKFRGEFEERLKSLLnELSKQEGQIILFIDELHT 282
Cdd:cd19521 44 LLYGPPGTGKSYLAKAVATEA----------NSTFFSVSSSDLVS--KWMGESEKLVKQLF-AMARENKPSIIFIDEVDS 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502155646 283 MVGAgKGEGSMDAGNMLKPAL----------ARGELhCVGATTLNeyrqyIEKDAALERRFQK 335
Cdd:cd19521 111 LCGT-RGEGESEASRRIKTELlvqmngvgndSQGVL-VLGATNIP-----WQLDSAIRRRFEK 166
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
203-333 |
1.47e-03 |
|
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: 39.58 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 203 VLIGEPGVGKTAIAEGLAQRIINGEV----------PDGLKGKRLLSLDMGSLIAGAkfrgefeerlksLLNELskQEGQ 272
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSNRPVfyvqltrdttEEDLFGRRNIDPGGASWVDGP------------LVRAA--REGE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502155646 273 IIlFIDELHtmvgagkgEGSMDAGNMLKPALARGELHC---------------VGATTLNEYRQYIEKDAALERRF 333
Cdd:pfam07728 69 IA-VLDEIN--------RANPDVLNSLLSLLDERRLLLpdggelvkaapdgfrLIATMNPLDRGLNELSPALRSRF 135
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
203-335 |
1.90e-03 |
|
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410917 [Multi-domain] Cd Length: 163 Bit Score: 40.03 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 203 VLIGEPGVGKTAIAEGLAQRIingevpdglkGKRLLSLDMGSLIagAKFRGEFEERLKSLLNELSKQEGQIIlFIDELHT 282
Cdd:cd19509 36 LLYGPPGTGKTLLARAVASES----------GSTFFSISASSLV--SKWVGESEKIVRALFALARELQPSII-FIDEIDS 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502155646 283 MVGAgKGEGSMDAGNMLKPALARgELHcvGATTLNEYRQYI--------EKDAALERRFQK 335
Cdd:cd19509 103 LLSE-RGSGEHEASRRVKTEFLV-QMD--GVLNKPEDRVLVlgatnrpwELDEAFLRRFEK 159
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
178-319 |
2.32e-03 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 41.58 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 178 DPVIGRDDEIRRTIQVLQRrtkNNPVLIGEPGVGKTAIAEGLAqRIINGEVpdglkgkrllsLDMGSLIAGAK-FRGEFE 256
Cdd:PRK13341 34 DHILGEGRLLRRAIKADRV---GSLILYGPPGVGKTTLARIIA-NHTRAHF-----------SSLNAVLAGVKdLRAEVD 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502155646 257 ERLKSLlnelsKQEGQ-IILFIDELHTMVGAgkgegSMDAgnmLKPALARGELHCVGATTLNEY 319
Cdd:PRK13341 99 RAKERL-----ERHGKrTILFIDEVHRFNKA-----QQDA---LLPWVENGTITLIGATTENPY 149
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
324-488 |
2.70e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 324 EKDAALERRFQKVLVEEPSEEDTIAILRGLKERYEVHHKVAITDGAIIAAAKLSHRYITDRQLP-----DKAIDLIDEAA 398
Cdd:COG1196 609 READARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAalleaEAELEELAERL 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 399 SRIRMEIDSKPEVLDRLDRRLIQLKVESQALKKEEDDAAKKRLEKLQEEIVRLEREYSDLEEIWTSEKAEVQGSAQIQQK 478
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
170
....*....|
gi 502155646 479 IEQSRQELEA 488
Cdd:COG1196 769 LERLEREIEA 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
404-542 |
2.81e-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: 41.59 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 404 EIDSKPEVLDRLDRRLIQLKVESQALKkEEDDAAKKRLEKLQEEIVRLEREYSDLEEiwTSEKAEVQGsAQIQQKIEQSR 483
Cdd:TIGR02169 358 EYAELKEELEDLRAELEEVDKEFAETR-DELKDYREKLEKLKREINELKRELDRLQE--ELQRLSEEL-ADLNAAIAGIE 433
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 502155646 484 QELEAARrkgdlNRMAELQYGVIPDLERSLQMVDQHGKSENQLLRSKVTEEEIAEVVSK 542
Cdd:TIGR02169 434 AKINELE-----EEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
|
| clpX |
PRK05342 |
ATP-dependent Clp protease ATP-binding subunit ClpX; |
533-622 |
2.88e-03 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX;
Pssm-ID: 235422 [Multi-domain] Cd Length: 412 Bit Score: 40.91 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 533 EEEIAEVVSKWTGIPVSKmlegerdkllKMESLLHQRVIGQEEA----VVAVSNAVRRSRAGLSDPNRPSGS---FMFLG 605
Cdd:PRK05342 46 REELKEEAVELKELPTPK----------EIKAHLDQYVIGQERAkkvlSVAVYNHYKRLRHGDKKDDDVELQksnILLIG 115
|
90
....*....|....*..
gi 502155646 606 PTGVGKTELCKALAEFL 622
Cdd:PRK05342 116 PTGSGKTLLAQTLARIL 132
|
|
| PRK14953 |
PRK14953 |
DNA polymerase III subunits gamma and tau; Provisional |
568-696 |
3.22e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237867 [Multi-domain] Cd Length: 486 Bit Score: 40.96 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 568 QRVIGQEEAVVAVSNAVRRsraglsdpNRPSGSFMFLGPTGVGKTELCKALAEFL-----FDTE-----EAMVRIDMSEF 637
Cdd:PRK14953 16 KEVIGQEIVVRILKNAVKL--------QRVSHAYIFAGPRGTGKTTIARILAKVLnclnpQEGEpcgkcENCVEIDKGSF 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502155646 638 MEKHSvarlIGAPPGYvGYEEGGYLTEAVRRKP----YSVILLDEVEKAHPDVFNILLQVLED 696
Cdd:PRK14953 88 PDLIE----IDAASNR-GIDDIRALRDAVSYTPikgkYKVYIIDEAHMLTKEAFNALLKTLEE 145
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
327-538 |
4.09e-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: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 327 AALERRFQKVLVEEPSEEDTIAILRglKERYEVHHKVAITDGAIIAAAKLSHRYITDRQLPDKAIDLIDEAASRIRMEID 406
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLS--KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 407 SKPEVLDRLDRRLIQLKVESQALKKEEDDAAK------KRLEKLQEEIVRLEREYSDLEEIWTSEKAEVQGSAQIQQKIE 480
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERrledleEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502155646 481 QSRQELEAARRK--GDLNRMAElqygVIPDLERSLQMV-DQHGKSENQLLRSKVTEEEIAE 538
Cdd:TIGR02168 887 EALALLRSELEElsEELRELES----KRSELRRELEELrEKLAQLELRLEGLEVRIDNLQE 943
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
382-492 |
4.38e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.00 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 382 TDRQLPDKAIDLIDEAASRIRmeidSKPEVLDRLDRRLIQLKVESQALKKEEDDAAKKRLEKLQEEIVRLEREYSDLEEI 461
Cdd:smart00787 158 EDYKLLMKELELLNSIKPKLR----DRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEE 233
|
90 100 110
....*....|....*....|....*....|.
gi 502155646 462 WTSEKAEVQGSAQIQQKIEQSRQELEAARRK 492
Cdd:smart00787 234 LQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| 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 |
4.57e-03 |
|
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: 38.81 E-value: 4.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502155646 204 LIGEPGVGKTAIAEGLAQRIingevpdglkGKRLLSLDMGSLIagAKFRGEFEERLKSLLNELSKQEGQIIlFIDEL 280
Cdd:cd19503 39 LHGPPGTGKTLLARAVANEA----------GANFLSISGPSIV--SKYLGESEKNLREIFEEARSHAPSII-FIDEI 102
|
|
| RecA-like_ATAD1 |
cd19520 |
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ... |
204-285 |
5.91e-03 |
|
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. 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: 410928 [Multi-domain] Cd Length: 166 Bit Score: 38.56 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 204 LIGEPGVGKTAIAEGLAQRiingevpdglKGKRLLSLDMGSLIagAKFRGEFEERLKSLLNELSKQEGQIIlFIDELHTM 283
Cdd:cd19520 40 LYGPPGCGKTMLAKATAKE----------AGARFINLQVSSLT--DKWYGESQKLVAAVFSLASKLQPSII-FIDEIDSF 106
|
..
gi 502155646 284 VG 285
Cdd:cd19520 107 LR 108
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
204-280 |
6.27e-03 |
|
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. 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: 410915 [Multi-domain] Cd Length: 161 Bit Score: 38.12 E-value: 6.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502155646 204 LIGEPGVGKTAIAEGLAqriingevpdGLKGKRLLSLDMGSLIAGakFRGEFEERLKSLLnELSKQEGQIILFIDEL 280
Cdd:cd19507 36 LVGIQGTGKSLTAKAIA----------GVWQLPLLRLDMGRLFGG--LVGESESRLRQMI-QTAEAIAPCVLWIDEI 99
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
179-281 |
7.57e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 38.25 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 179 PVIGRDDEIRRTIQVLQRRTKNNP---VLIGEPGVGKTAIAEGLAQRiINGEVPDGLKGKRLLSLDMGSLIAGAKFRGEF 255
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRA-LERDGGYFLRGKCDENLPYSPLLEALTREGLL 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502155646 256 E-------------------------------------ERLKSLLNELSKQEGQIILFIDELH 281
Cdd:pfam13191 80 RqlldelesslleawraallealapvpelpgdlaerllDLLLRLLDLLARGERPLVLVLDDLQ 142
|
|
| COG1672 |
COG1672 |
Predicted ATPase, archaeal AAA+ ATPase superfamily [General function prediction only]; |
595-734 |
7.66e-03 |
|
Predicted ATPase, archaeal AAA+ ATPase superfamily [General function prediction only];
Pssm-ID: 441278 [Multi-domain] Cd Length: 324 Bit Score: 39.51 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 595 NRPSGSFMFL-GPTGVGKTELCKALAE----FLFDTEEAMVRIDMSEFMEKhsVARLIGAPPGYVGYEEG----GYLTEA 665
Cdd:COG1672 17 ESDGGELVVVyGRRRVGKTSLIKEFLKekpaIYFDAREESERESLRDFSEA--LAEALGDPLSKKEFESWeeafEYLAEL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502155646 666 VRRKPYsVILLDEVE---KAHPDVFNILlqvledGRLTDSHGRTvdfRNTVIVMTsnlGSAQ--IQELVGDREA 734
Cdd:COG1672 95 AEGKRL-VIVIDEFQylvKLDPSLLSIL------QYLWDELLSD---SNVSLILC---GSSIgmMEELLLDYKS 155
|
|
| ClpX |
COG1219 |
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ... |
553-622 |
8.45e-03 |
|
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440832 [Multi-domain] Cd Length: 409 Bit Score: 39.65 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502155646 553 EGERDKLLK---MESLLHQRVIGQEEA----VVAVSNAVRRSRAGLSDP--------NrpsgsFMFLGPTGVGKTELCKA 617
Cdd:COG1219 54 EEELKKLPKpkeIKAFLDEYVIGQERAkkvlSVAVYNHYKRLNSGSKDDddveleksN-----ILLIGPTGSGKTLLAQT 128
|
....*
gi 502155646 618 LAEFL 622
Cdd:COG1219 129 LARIL 133
|
|
| |
