|
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: 1571.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 6 LTSKLQLALSDAQSLAVGHDHPAIEPVHLLSALLEQQGGSIKPLLMQVGFDIAALRSGLNKELDALPKIQSPTGDVNLSQ 85
Cdd:TIGR03346 1 LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEKELERLPKVSGPGGQVYLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 86 DLARLLNQADRLAQQKGDQFISSELVLLAAMDENTRLGKLLLGQGVSRKALENAVANLRGGEAVNDPNVEESRQALDKYT 165
Cdd:TIGR03346 81 DLNRLLNLAEKLAQKRGDEFISSEHLLLALLDDKGTLGKLLKEAGATADALEAAINAVRGGQKVTDANAEDQYEALEKYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 166 VDMTKRAEEGKLDPVIGRDDEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPDGLKDKRLLALDMGAL 245
Cdd:TIGR03346 161 RDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLALDMGAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 246 IAGAKFRGEFEERLKAVLNELGKQEGRVILFIDELHTMVGAGKAEGAMDAGNMLKPALARGELHCVGATTLDEYRQYIEK 325
Cdd:TIGR03346 241 IAGAKYRGEFEERLKAVLNEVTKSEGQIILFIDELHTLVGAGKAEGAMDAGNMLKPALARGELHCIGATTLDEYRKYIEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 326 DAALERRFQKVLVDEPSEEDTIAILRGLKERYEVHHGVSITDGAIIAAAKLSHRYITDRQLPDKAIDLIDEAASRIRMEI 405
Cdd:TIGR03346 321 DAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAARIRMEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 406 DSKPEELDRLDRRLIQLKIEREALKKEDDEATRKRLAKLEEDIVKLEREYADLEEIWKSEKAEVQGSAQIQQKIEQAKQE 485
Cdd:TIGR03346 401 DSKPEELDELDRRIIQLEIEREALKKEKDEASKKRLEDLEKELADLEEEYAELEEQWKAEKASIQGIQQIKEEIEQVRLE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 486 MEAARRKGDLESMARIQYQTIPDLERSLQMVDQH-GKTENQLLRNKVTDEEIAEVVSKWTGIPVSKMLEGEREKLLRMEQ 564
Cdd:TIGR03346 481 LEQAEREGDLAKAAELQYGKLPELEKQLQAAEQKlGEEQNRLLREEVTAEEIAEVVSRWTGIPVSKMLEGEREKLLHMEE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 565 ELHRRVIGQDEAVVAVSNAVRRSRAGLADPNRPSGSFLFLGPTGVGKTELCKALAEFLFDTEEALVRIDMSEFMEKHSVA 644
Cdd:TIGR03346 561 ELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRIDMSEYMEKHSVA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 645 RLIGAPPGYVGFEEGGYLTEAIRRKPYSVVLLDEVEKAHPDVFNILLQVLEDGRLTDSHGRTVDFRNTVVVMTSNLGSAQ 724
Cdd:TIGR03346 641 RLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDF 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 725 IQELAG--DREAQRAAVMDAVNAHFRPEFINRIDEVVVFEPLAREQIAGIAEIQLGRLRKRLAERELSLELSQEALDKLI 802
Cdd:TIGR03346 721 IQELAGgdDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKITLELSDAALDFLA 800
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 15599738 803 AVGFDPVYGARPLKRAIQRWIENPLAQLILAGKFAPGASISAKVEGDEIV 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: 1468.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 1 MRIDRLTSKLQLALSDAQSLAVGHDHPAIEPVHLLSALLEQQGGSIKPLLMQVGFDIAALRSGLNKELDALPKIQSPTGD 80
Cdd:COG0542 1 MNFEKFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGRLPKVSGSSGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 81 VNLSQDLARLLNQADRLAQQKGDQFISSELVLLAAM-DENTRLGKLLLGQGVSRKALENAVANLRGGEAVNDPNVEESRQ 159
Cdd:COG0542 81 PYLSPRLKRVLELAELEARKLGDEYISTEHLLLALLrEGEGVAARILKKLGITLEALREALEELRGGSRVTSQNPESKTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 160 ALDKYTVDMTKRAEEGKLDPVIGRDDEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPDGLKDKRLLA 239
Cdd:COG0542 161 ALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDKRVLS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 240 LDMGALIAGAKFRGEFEERLKAVLNELGKQEGRVILFIDELHTMVGAGKAEGAMDAGNMLKPALARGELHCVGATTLDEY 319
Cdd:COG0542 241 LDLGALVAGAKYRGEFEERLKAVLDEVKKSEGNIILFIDELHTLVGAGGAEGAMDAANLLKPALARGELRCIGATTLDEY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 320 RQYIEKDAALERRFQKVLVDEPSEEDTIAILRGLKERYEVHHGVSITDGAIIAAAKLSHRYITDRQLPDKAIDLIDEAAS 399
Cdd:COG0542 321 RKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAIDLIDEAAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 400 RIRMEIDSKPEELDRLDRRLIQLKIEREALKKEDDEATRKRLAKLEEDIVKLEREYADLEEIWKSEKAEVQGSAQIQQKI 479
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 480 EQakqemeaarrkgdlesmariQYQTIPDLERSLQMVDQHGKTENQLLRNKVTDEEIAEVVSKWTGIPVSKMLEGEREKL 559
Cdd:COG0542 481 EQ--------------------RYGKIPELEKELAELEEELAELAPLLREEVTEEDIAEVVSRWTGIPVGKLLEGEREKL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 560 LRMEQELHRRVIGQDEAVVAVSNAVRRSRAGLADPNRPSGSFLFLGPTGVGKTELCKALAEFLFDTEEALVRIDMSEFME 639
Cdd:COG0542 541 LNLEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYME 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 640 KHSVARLIGAPPGYVGFEEGGYLTEAIRRKPYSVVLLDEVEKAHPDVFNILLQVLEDGRLTDSHGRTVDFRNTVVVMTSN 719
Cdd:COG0542 621 KHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSN 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 720 LGSAQIQELAGDR---EAQRAAVMDAVNAHFRPEFINRIDEVVVFEPLAREQIAGIAEIQLGRLRKRLAERELSLELSQE 796
Cdd:COG0542 701 IGSELILDLAEDEpdyEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDA 780
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599738 797 ALDKLIAVGFDPVYGARPLKRAIQRWIENPLAQLILAGKFAPGASISAKVEGDEIV 852
Cdd:COG0542 781 AKDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGELV 836
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
1-852 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 1318.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 1 MRIDRLTSKLQLALSDAQSLAVGHDHPAIEPVHLLSALLEQQGGSIKPLLMQVGFDIAALRSGLNKELDALPKIQSPTGD 80
Cdd:PRK10865 1 MRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVRPLLTSAGINAGQLRTDINQALSRLPQVEGTGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 81 VNLSQDLARLLNQADRLAQQKGDQFISSELVLLAAMDENTRLGKLLLGQGVSRKALENAVANLRGGEAVNDPNVEESRQA 160
Cdd:PRK10865 81 VQPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAALESRGTLADILKAAGATTANITQAIEQMRGGESVNDQGAEDQRQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 161 LDKYTVDMTKRAEEGKLDPVIGRDDEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPDGLKDKRLLAL 240
Cdd:PRK10865 161 LKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 241 DMGALIAGAKFRGEFEERLKAVLNELGKQEGRVILFIDELHTMVGAGKAEGAMDAGNMLKPALARGELHCVGATTLDEYR 320
Cdd:PRK10865 241 DMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 321 QYIEKDAALERRFQKVLVDEPSEEDTIAILRGLKERYEVHHGVSITDGAIIAAAKLSHRYITDRQLPDKAIDLIDEAASR 400
Cdd:PRK10865 321 QYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 401 IRMEIDSKPEELDRLDRRLIQLKIEREALKKEDDEATRKRLAKLEEDIVKLEREYADLEEIWKSEKAEVQGSAQIQQKIE 480
Cdd:PRK10865 401 IRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKAELE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 481 QAKQEMEAARRKGDLESMARIQYQTIPDLERSLQMVDQHGKTENQLLRNKVTDEEIAEVVSKWTGIPVSKMLEGEREKLL 560
Cdd:PRK10865 481 QAKIAIEQARRVGDLARMSELQYGKIPELEKQLAAATQLEGKTMRLLRNKVTDAEIAEVLARWTGIPVSRMLESEREKLL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 561 RMEQELHRRVIGQDEAVVAVSNAVRRSRAGLADPNRPSGSFLFLGPTGVGKTELCKALAEFLFDTEEALVRIDMSEFMEK 640
Cdd:PRK10865 561 RMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEK 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 641 HSVARLIGAPPGYVGFEEGGYLTEAIRRKPYSVVLLDEVEKAHPDVFNILLQVLEDGRLTDSHGRTVDFRNTVVVMTSNL 720
Cdd:PRK10865 641 HSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNL 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 721 GSAQIQELAGDRE--AQRAAVMDAVNAHFRPEFINRIDEVVVFEPLAREQIAGIAEIQLGRLRKRLAERELSLELSQEAL 798
Cdd:PRK10865 721 GSDLIQERFGELDyaHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYEIHISDEAL 800
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 15599738 799 DKLIAVGFDPVYGARPLKRAIQRWIENPLAQLILAGKFAPGASISAKVEGDEIV 852
Cdd:PRK10865 801 KLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDDRIV 854
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
89-849 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 863.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 89 RLLNQADRLAQQKGDQFISSELVLLAAMDENTRLGKLLLGQ-GVSRKALENAVANLRGG--EAVNDPNVEESRQ-ALDKY 164
Cdd:CHL00095 86 RVLEMSLEEARDLGHNYIGTEHLLLALLEEGEGVAARVLENlGVDLSKIRSLILNLIGEiiEAILGAEQSRSKTpTLEEF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 165 TVDMTKRAEEGKLDPVIGRDDEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPDGLKDKRLLALDMGA 244
Cdd:CHL00095 166 GTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDKLVITLDIGL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 245 LIAGAKFRGEFEERLKAVLNELgKQEGRVILFIDELHTMVGAGKAEGAMDAGNMLKPALARGELHCVGATTLDEYRQYIE 324
Cdd:CHL00095 246 LLAGTKYRGEFEERLKRIFDEI-QENNNIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLDEYRKHIE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 325 KDAALERRFQKVLVDEPSEEDTIAILRGLKERYEVHHGVSITDGAIIAAAKLSHRYITDRQLPDKAIDLIDEAASRIRME 404
Cdd:CHL00095 325 KDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLDEAGSRVRLI 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 405 IDSKPEELDRLDRRLiqlkieREALKkEDDEATRkrlakleedivklereyadleeiwksekaevqgsaqiQQKIEQAKQ 484
Cdd:CHL00095 405 NSRLPPAARELDKEL------REILK-DKDEAIR-------------------------------------EQDFETAKQ 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 485 EMEaarRKGDLESMARIQYQTIPDLERSLQMVDqhgktenqllrnKVTDEEIAEVVSKWTGIPVSKMLEGEREKLLRMEQ 564
Cdd:CHL00095 441 LRD---REMEVRAQIAAIIQSKKTEEEKRLEVP------------VVTEEDIAEIVSAWTGIPVNKLTKSESEKLLHMEE 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 565 ELHRRVIGQDEAVVAVSNAVRRSRAGLADPNRPSGSFLFLGPTGVGKTELCKALAEFLFDTEEALVRIDMSEFMEKHSVA 644
Cdd:CHL00095 506 TLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALASYFFGSEDAMIRLDMSEYMEKHTVS 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 645 RLIGAPPGYVGFEEGGYLTEAIRRKPYSVVLLDEVEKAHPDVFNILLQVLEDGRLTDSHGRTVDFRNTVVVMTSNLGSAQ 724
Cdd:CHL00095 586 KLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSKV 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 725 IQELAGD----------REAQ----RAAVMDAVNAHFRPEFINRIDEVVVFEPLAREQIAGIAEIQLGRLRKRLAERELS 790
Cdd:CHL00095 666 IETNSGGlgfelsenqlSEKQykrlSNLVNEELKQFFRPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQ 745
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599738 791 LELSQEALDKLIAVGFDPVYGARPLKRAIQRWIENPLAQLILAGKFAPGASISAKVEGD 849
Cdd:CHL00095 746 LEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVDVNDE 804
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
6-832 |
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: 789.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 6 LTSKLQLALSDAQSLAVGHDHPAIEPVHLLSALLEQQGGSIKPLLMQVGFDIAALRSGLNKELDALPKIQSPTGDvnLSQ 85
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLARALDKLPRGNTRTPV--FSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 86 DLARLLNQADRLAQ-QKGDQFISSELVLLAAMDENT------RLGKLLlgQGVSRKALENAVANLRGGEA---------- 148
Cdd:TIGR03345 79 HLVELLQEAWLLASlELGDGRIRSGHLLLALLTDPElrrllgSISPEL--AKIDREALREALPALVEGSAeasaaaadaa 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 149 -VNDPNVEESRQALDKYTVDMTKRAEEGKLDPVIGRDDEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGE 227
Cdd:TIGR03345 157 pAGAAAGAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 228 VPDGLKDKRLLALDMGALIAGAKFRGEFEERLKAVLNELGKQEGRVILFIDELHTMVGAGKAEGAMDAGNMLKPALARGE 307
Cdd:TIGR03345 237 VPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPIILFIDEAHTLIGAGGQAGQGDAANLLKPALARGE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 308 LHCVGATTLDEYRQYIEKDAALERRFQKVLVDEPSEEDTIAILRGLKERYEVHHGVSITDGAIIAAAKLSHRYITDRQLP 387
Cdd:TIGR03345 317 LRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 388 DKAIDLIDEAASRIRMEIDSKPEELDRLDRRLIQLKIEREALKKE------DDEatrkRLAKLEEDIVKLEREYADLEEI 461
Cdd:TIGR03345 397 DKAVSLLDTACARVALSQNATPAALEDLRRRIAALELELDALEREaalgadHDE----RLAELRAELAALEAELAALEAR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 462 WKSEKAEVQGSAQIQQKIEQAkQEMEAARRKGDLESMARiqyqtipdLERSLQMVDQhgktENQLLRNKVTDEEIAEVVS 541
Cdd:TIGR03345 473 WQQEKELVEAILALRAELEAD-ADAPADDDDALRAQLAE--------LEAALASAQG----EEPLVFPEVDAQAVAEVVA 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 542 KWTGIPVSKMLEGEREKLLRMEQELHRRVIGQDEAVVAVSNAVRRSRAGLADPNRPSGSFLFLGPTGVGKTELCKALAEF 621
Cdd:TIGR03345 540 DWTGIPVGRMVRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAEL 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 622 LFDTEEALVRIDMSEFMEKHSVARLIGAPPGYVGFEEGGYLTEAIRRKPYSVVLLDEVEKAHPDVFNILLQVLEDGRLTD 701
Cdd:TIGR03345 620 LYGGEQNLITINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMED 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 702 SHGRTVDFRNTVVVMTSNLGSAQIQELAGDR------EAQRAAVMDAVNAHFRPEFINRIdEVVVFEPLAREQIAGIAEI 775
Cdd:TIGR03345 700 GEGREIDFKNTVILLTSNAGSDLIMALCADPetapdpEALLEALRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRL 778
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 15599738 776 QLGRLRKRLAER-ELSLELSQEALDKLIAVGFDPVYGARPLKRAIQRWIENPLAQLIL 832
Cdd:TIGR03345 779 KLDRIARRLKENhGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQIL 836
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
6-846 |
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 15599738 6 LTSKLQLALSDAQSLAVGHDHPAIEPVHLLSALLEQQGGsiKPLLMQVGFDIAALRSGLNKELDA-LPKI-QSPTGDVNL 83
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEA--IEILEECGGDVELLRKRLEDYLEEnLPVIpEDIDEEPEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 84 SQDLARLLNQADRLAQQKGDQFISSELVLLAAMDENTRLGKLLLG-QGVSRKALENAVA------NLRGGEAVNDPNVEE 156
Cdd:TIGR02639 79 TVGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKsQGITRLDILNYIShgiskdDGKDQLGEEAGKEEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 157 SRQ-ALDKYTVDMTKRAEEGKLDPVIGRDDEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPDGLKDK 235
Cdd:TIGR02639 159 KGQdALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERLKNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 236 RLLALDMGALIAGAKFRGEFEERLKAVLNELGKQEGRvILFIDELHTMVGAGK-AEGAMDAGNMLKPALARGELHCVGAT 314
Cdd:TIGR02639 239 KIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNA-ILFIDEIHTIVGAGAtSGGSMDASNLLKPALSSGKIRCIGST 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 315 TLDEYRQYIEKDAALERRFQKVLVDEPSEEDTIAILRGLKERYEVHHGVSITDGAIIAAAKLSHRYITDRQLPDKAIDLI 394
Cdd:TIGR02639 318 TYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDVI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 395 DEAASRIRMEIDSKPEEldrldrrliqlkierealkkeddeatrkrlakleedivklereyadleeiwksekaevqgsaq 474
Cdd:TIGR02639 398 DEAGAAFRLRPKAKKKA--------------------------------------------------------------- 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 475 iqqkieqakqemeaarrkgdlesmariqyqtipdlerslqmvdqhgktenqllrnKVTDEEIAEVVSKWTGIPVSKMLEG 554
Cdd:TIGR02639 415 -------------------------------------------------------NVNVKDIENVVAKMAKIPVKTVSSD 439
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 555 EREKLLRMEQELHRRVIGQDEAVVAVSNAVRRSRAGLADPNRPSGSFLFLGPTGVGKTELCKALAEFLfdtEEALVRIDM 634
Cdd:TIGR02639 440 DREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEEL---GVHLLRFDM 516
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 635 SEFMEKHSVARLIGAPPGYVGFEEGGYLTEAIRRKPYSVVLLDEVEKAHPDVFNILLQVLEDGRLTDSHGRTVDFRNTVV 714
Cdd:TIGR02639 517 SEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVIL 596
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 715 VMTSNLGSAQIQE----LAGDREAqrAAVMDAVNAHFRPEFINRIDEVVVFEPLAREQIAGIAEIQLGRLRKRLAERELS 790
Cdd:TIGR02639 597 IMTSNAGASEMSKppigFGGENRE--SKSLKAIKKLFSPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIE 674
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599738 791 LELSQEALDKLIAVGFDPVYGARPLKRAIQRWIENPLAQLILAGKFAPGASISAKV 846
Cdd:TIGR02639 675 LELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEILFGKLKKGGSVKISL 730
|
|
| 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: 552.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 6 LTSKLQLALSDAQSLAVGHDHPAIEPVHLLSALLEQQggSIKPLLMQVGFDIAALRsglnKELDALPKIQSP-------T 78
Cdd:PRK11034 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNP--SAREALEACSVDLVALR----QELEAFIEQTTPvlpaseeE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 79 GDVNLSQDLARLLNQADRLAQQKGDQFISSELVLLAAMDEN-TRLGKLLLGQGVSRKALENAVA-------NLRGGEAVN 150
Cdd:PRK11034 76 RDTQPTLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQeSQAAYLLRKHEVSRLDVVNFIShgtrkdePSQSSDPGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 151 DPNVEE---SRQALDKYTVDMTKRAEEGKLDPVIGRDDEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGE 227
Cdd:PRK11034 156 QPNSEEqagGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 228 VPDGLKDKRLLALDMGALIAGAKFRGEFEERLKAVLNELgKQEGRVILFIDELHTMVGAGKAEGA-MDAGNMLKPALARG 306
Cdd:PRK11034 236 VPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQL-EQDTNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 307 ELHCVGATTLDEYRQYIEKDAALERRFQKVLVDEPSEEDTIAILRGLKERYEVHHGVSITDGAIIAAAKLSHRYITDRQL 386
Cdd:PRK11034 315 KIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 387 PDKAIDLIDEAASRIRMeidskpeeldrldrrliqlkierealkkeddeatrkrlakleedivklereyadleeiwksek 466
Cdd:PRK11034 395 PDKAIDVIDEAGARARL--------------------------------------------------------------- 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 467 aevqgsaqiqqkieqakqeMEAARRKgdlesmariqyqtipdlerslqmvdqhgKTENqllrnkVTDeeIAEVVSKWTGI 546
Cdd:PRK11034 412 -------------------MPVSKRK----------------------------KTVN------VAD--IESVVARIARI 436
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 547 PVSKMLEGEREKLLRMEQELHRRVIGQDEAVVAVSNAVRRSRAGLADPNRPSGSFLFLGPTGVGKTELCKALAEFLfDTE 626
Cdd:PRK11034 437 PEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL-GIE 515
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 627 eaLVRIDMSEFMEKHSVARLIGAPPGYVGFEEGGYLTEAIRRKPYSVVLLDEVEKAHPDVFNILLQVLEDGRLTDSHGRT 706
Cdd:PRK11034 516 --LLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRK 593
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 707 VDFRNTVVVMTSNlgsaqiqelAGDREAQRAAV-----------MDAVNAHFRPEFINRIDEVVVFEPLAREQIAGIAEI 775
Cdd:PRK11034 594 ADFRNVVLVMTTN---------AGVRETERKSIglihqdnstdaMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDK 664
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599738 776 QLGRLRKRLAERELSLELSQEALDKLIAVGFDPVYGARPLKRAIQRWIENPLAQLILAGKFAPGASISAKVEGDEIVF 853
Cdd:PRK11034 665 FIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKEKNEL 742
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
558-761 |
6.45e-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: 334.15 E-value: 6.45e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 558 KLLRMEQELHRRVIGQDEAVVAVSNAVRRSRAGLADPNRPSGSFLFLGPTGVGKTELCKALAEFLFDTEEALVRIDMSEF 637
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 638 MEKHSVARLIGAPPGYVGFEEGGYLTEAIRRKPYSVVLLDEVEKAHPDVFNILLQVLEDGRLTDSHGRTVDFRNTVVVMT 717
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15599738 718 SNlgsaqiqelagdreaqraavmdavnaHFRPEFINRIDEVVVF 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 |
3.47e-91 |
|
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400187 [Multi-domain] Cd Length: 168 Bit Score: 284.47 E-value: 3.47e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 596 RPSGSFLFLGPTGVGKTELCKALAEFLFDTEEALVRIDMSEFMEKHSVARLIGAPPGYVGFEEGGYLTEAIRRKPYSVVL 675
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 676 LDEVEKAHPDVFNILLQVLEDGRLTDSHGRTVDFRNTVVVMTSNLGSAQIQELAG-----DREAQRAAVMDAVNAHFRPE 750
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRlgdspDYELLKEEVMDLLKKGFIPE 160
|
....*...
gi 15599738 751 FINRIDEV 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 |
6.14e-49 |
|
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: 168.05 E-value: 6.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 342 SEEDTIAILRGLKERYEVHHGVSITDGAIIAAAKLSHRYITDRQLPDKAIDLIDEAASRIRMEIDSKPEELDRLDRRLIQ 421
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|....
gi 15599738 422 LKIEREALKKEDDEATRKRLAKLE 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, ... |
764-842 |
8.69e-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, 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: 107.11 E-value: 8.69e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599738 764 LAREQIAGIAEIQLGRLRKRLAERELSLELSQEALDKLIAVGFDPVYGARPLKRAIQRWIENPLAQLILAGKFAPGASI 842
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTV 79
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
764-853 |
3.12e-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: 102.91 E-value: 3.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 764 LAREQIAGIAEIQLGRLRKRLAERELSLELSQEALDKLIAVGFDPVYGARPLKRAIQRWIENPLAQLILAGKFAPGASIS 843
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
90
....*....|
gi 15599738 844 AKVEGDEIVF 853
Cdd:smart01086 81 VDVDDGELVF 90
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
181-341 |
1.32e-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: 89.13 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 181 IGRDDEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINgevpdglKDKRLLALDMGALIAGAKFRGEFEERLK 260
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFR-------PGAPFLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 261 AVLNELGKQEGRVILFIDELHTMVGA--GKAEGAMDAGNMLKPalARGELHCVGATTLDEYRQyieKDAALERRFQKVLV 338
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDSLSRGaqNALLRVLETLNDLRI--DRENVRVIGATNRPLLGD---LDRALYDRLDIRIV 148
|
...
gi 15599738 339 DEP 341
Cdd:cd00009 149 IPL 151
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
571-763 |
8.29e-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: 84.12 E-value: 8.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 571 IGQDEAVVAVSNAVRRsragladpnRPSGSFLFLGPTGVGKTELCKALAEFLFDTEEALVRIDMSEFMEKHSVARLIGAP 650
Cdd:cd00009 1 VGQEEAIEALREALEL---------PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 651 PGYVgfeeggyLTEAIRRKPYSVVLLDEVEKAHPDVFNILLQVLEDGRLTdshgrTVDFRNTVVVMTSNLGSAQIqelag 730
Cdd:cd00009 72 LVRL-------LFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATNRPLLGD----- 134
|
170 180 190
....*....|....*....|....*....|...
gi 15599738 731 dreaqraavmdavnahFRPEFINRIDEVVVFEP 763
Cdd:cd00009 135 ----------------LDRALYDRLDIRIVIPL 151
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
597-732 |
1.26e-13 |
|
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: 68.94 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 597 PSGSFLFLGPTGVGKTELCKALAEFLFDTEEALVRIDMSEFMEKHSVARLIGAPPGYVGFEEGGY----LTEAIRRKPYS 672
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 673 VVLLDEVEKAHPDVFNILLQVLEDGRLTDSHGRtvdFRNTVVVMTSNLGSAQIQELAGDR 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 |
8.21e-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: 66.16 E-value: 8.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 600 SFLFLGPTGVGKTELCKALAEFLFDTEeaLVRIDMSEFMEKhsvARLIGA---PPGYVGFEEGGyLTEAIRRKpySVVLL 676
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRP--VFYVQLTRDTTE---EDLFGRrniDPGGASWVDGP-LVRAAREG--EIAVL 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15599738 677 DEVEKAHPDVFNILLQVLEDGRL-TDSHGRTVDFRNT--VVVMTSNLGSAQIQEL 728
Cdd:pfam07728 73 DEINRANPDVLNSLLSLLDERRLlLPDGGELVKAAPDgfRLIATMNPLDRGLNEL 127
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
204-337 |
9.17e-11 |
|
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: 60.30 E-value: 9.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 204 LIGEPGVGKTAIVEGLAQRIingevpdglkDKRLLALDMGALIagAKFRGEFEERLKAVLNELgKQEGRVILFIDELHTM 283
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELV--SKYVGESEKRLRELFEAA-KKLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599738 284 VGAGKAEG---AMDAGNMLKPAL-----ARGELHCVGATTldeyrqYIEK-DAALERRFQKVL 337
Cdd:pfam00004 70 AGSRGSGGdseSRRVVNQLLTELdgftsSNSKVIVIAATN------RPDKlDPALLGRFDRII 126
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
17-69 |
1.74e-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: 54.06 E-value: 1.74e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 15599738 17 AQSLAVGHDHPAIEPVHLLSALLEQQGGSIKPLLMQVGFDIAALRSGLNKELD 69
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
583-761 |
1.04e-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: 54.98 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 583 AVRRSRAGLADPNRPSGSFLFLGPTGVGKTELCKALAEFLFDTeeaLVRIDMSEFMEKHS--VARLIGAppgyvgfeegg 660
Cdd:cd19481 11 APRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLP---LIVVKLSSLLSKYVgeSEKNLRK----------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 661 yLTEAIRRKPYSVVLLDEVEKAHPD------------VFNILLQVLEDGRLTDshgrtvdfrNTVVVMTSNlgsaqiqel 728
Cdd:cd19481 77 -IFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAATN--------- 137
|
170 180 190
....*....|....*....|....*....|...
gi 15599738 729 agdreaqRAAVMDAvnAHFRPefiNRIDEVVVF 761
Cdd:cd19481 138 -------RPDLLDP--ALLRP---GRFDEVIEF 158
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
411-779 |
4.08e-08 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 56.46 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 411 ELDRLDRRLIQLKIEREALKKEDDEATRKRLAKLEEDIVKLEREYADLEEIWKSEKAEVQGSAQIQQKIEQAKQEMEAAR 490
Cdd:COG0464 7 LAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 491 RKGDLESMARIQYQTIPDLERSLQMVDQHGKTENQLLRNKVTDEEIAEVVSKWTGIPVSKMLEGEREKLL-------RME 563
Cdd:COG0464 87 SALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILddlggleEVK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 564 QELHRRVIGQDEavvavsNAVRRSRAGLadpnRPSGSFLFLGPTGVGKTELCKALAEFLfdtEEALVRIDMSEFMEKhsv 643
Cdd:COG0464 167 EELRELVALPLK------RPELREEYGL----PPPRGLLLYGPPGTGKTLLARALAGEL---GLPLIEVDLSDLVSK--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 644 arligappgYVGfEEGGYLTEAI---RRKPYSVVLLDEVEKAHPD-----------VFNILLQVLEDGRltdshgrtvdf 709
Cdd:COG0464 231 ---------YVG-ETEKNLREVFdkaRGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR----------- 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 710 RNTVVVMTSNLgsaqiqelagdreaqraavMDAVNahfrPEFINRIDEVVVFEPLAREQIAGIAEIQLGR 779
Cdd:COG0464 290 SDVVVIAATNR-------------------PDLLD----PALLRRFDEIIFFPLPDAEERLEIFRIHLRK 336
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
38-363 |
1.04e-07 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 54.92 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 38 LLEQQGGSIKPLLMQVGFDIAALRSGLNKELDALPKIQSPTGDVNLSQDLARLLNQADRLAQQKGDQFISSELVLLAAMD 117
Cdd:COG0464 16 LLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 118 ENTRLGKLLLGQGVSRKALENAVANLRGGEAVNDPNVEESRQALDKYTVDM-TKRAEEGKLDPVIGRDD---EIRRTIQV 193
Cdd:COG0464 96 ELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEeLLELREAILDDLGGLEEvkeELRELVAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 194 LQRRTKNNP----------VLIGEPGVGKTAIVEGLAQRIingevpdglkDKRLLALDMGALIagAKFRGEFEERLKAVL 263
Cdd:COG0464 176 PLKRPELREeyglppprglLLYGPPGTGKTLLARALAGEL----------GLPLIEVDLSDLV--SKYVGETEKNLREVF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 264 NELgKQEGRVILFIDELHTmvGAGKAEGAMDA------GNMLKpALA--RGELHCVGATtldeYRqyIEK-DAALERRFQ 334
Cdd:COG0464 244 DKA-RGLAPCVLFIDEADA--LAGKRGEVGDGvgrrvvNTLLT-EMEelRSDVVVIAAT----NR--PDLlDPALLRRFD 313
|
330 340 350
....*....|....*....|....*....|
gi 15599738 335 KVL-VDEPSEEDTIAILRGLKERYEVHHGV 363
Cdd:COG0464 314 EIIfFPLPDAEERLEIFRIHLRKRPLDEDV 343
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
602-719 |
3.06e-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: 50.28 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 602 LFLGPTGVGKTELCKALAEFLFDTeeaLVRIDMSEFMEKHsvarlIGAPPGYVgfeeGGYLTEAIRRKPySVVLLDEVEK 681
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAP---FIEISGSELVSKY-----VGESEKRL----RELFEAAKKLAP-CVIFIDEIDA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 15599738 682 AHP-----------DVFNILLQVLEdgrltdshGRTVDFRNTVVVMTSN 719
Cdd:pfam00004 69 LAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
94-145 |
4.40e-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: 47.13 E-value: 4.40e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 15599738 94 ADRLAQQKGDQFISSELVLLAAMDENTRLG-KLLLGQGVSRKALENAVANLRG 145
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAaRLLKKAGVDLDALREAIEKLLG 53
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
564-681 |
1.42e-06 |
|
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410906 [Multi-domain] Cd Length: 183 Bit Score: 49.30 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 564 QELHRRVIGQDEA----VVAVSNAVRRSR--AGLADPNRPSgSFLFLGPTGVGKTELCKALAEFlfdTEEALVRIDMSEF 637
Cdd:cd19498 7 SELDKYIIGQDEAkravAIALRNRWRRMQlpEELRDEVTPK-NILMIGPTGVGKTEIARRLAKL---AGAPFIKVEATKF 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15599738 638 MEKhsvarligappGYVGFEeggylTEAIRRKPYS-VVLLDEVEK 681
Cdd:cd19498 83 TEV-----------GYVGRD-----VESIIRDLVEgIVFIDEIDK 111
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
399-568 |
2.37e-06 |
|
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: 51.61 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 399 SRIRMEIDSKPEELDRLDRRLIQLKIEREALK------KEDDEATRKRLAKLEEDIVKLEREYADL----EEIWKSEKAE 468
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLaeieelEREIEEERKRRDKLTEEYAELKEELEDLraelEEVDKEFAET 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 469 VQGSAQIQQKIEQAKQEMEAARRKGDlesmaRIQYQTIPDLERSLQMVDQHGKTENQLLRNKVTDEEIAEVVSK--WTGI 546
Cdd:TIGR02169 384 RDELKDYREKLEKLKREINELKRELD-----RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKqeWKLE 458
|
170 180
....*....|....*....|..
gi 15599738 547 PVSKMLEGEREKLLRMEQELHR 568
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDR 480
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
198-343 |
2.97e-06 |
|
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: 47.75 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 198 TKNNPVLIGEPGVGKTAIVEGLAQRI---------INGEVpdglKDKRLLALDMGALIAGAKFRGEFEERLKaVLNELGK 268
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELgppgggviyIDGED----ILEEVLDQLLLIIVGGKKASGSGELRLR-LALALAR 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599738 269 QEGRVILFIDELHTMVGAG--KAEGAMDAGNMLKPALARGELHCVGATTLDEyrqyIEKDAALERRFQKVLVDEPSE 343
Cdd:smart00382 76 KLKPDVLILDEITSLLDAEqeALLLLLEELRLLLLLKSEKNLTVILTTNDEK----DLGPALLRRRFDRRIVLLLIL 148
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
596-691 |
9.97e-06 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 45.80 E-value: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 596 RPSGSFLFL-GPTGVGKTELCKALAEFLFDTEEALVRIDMSEFMEK----HSVARLIGAPPGYVGFEEG--GYLTEAI-R 667
Cdd:pfam13401 2 RFGAGILVLtGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPkdllRALLRALGLPLSGRLSKEEllAALQQLLlA 81
|
90 100
....*....|....*....|....
gi 15599738 668 RKPYSVVLLDEVEKAHPDVFNILL 691
Cdd:pfam13401 82 LAVAVVLIIDEAQHLSLEALEELR 105
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
595-695 |
1.43e-05 |
|
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required for, along with delta' subunit, the assembly of the processivity factor beta(2) onto primed DNA in the DNA polymerase III holoenzyme-catalyzed reaction. The delta subunit is also known as HolA.
Pssm-ID: 433013 [Multi-domain] Cd Length: 161 Bit Score: 46.05 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 595 NRPSGSFLFLGPTGVGKTELCKALAEFLFDTEEalvriDMSEFMEKHSVARLI--GAPPGYVGFEEGG---------YLT 663
Cdd:pfam13177 16 GRLSHAYLFSGPEGVGKLELALAFAKALFCEEP-----GDDLPCGQCRSCRRIesGNHPDLVIIEPEGqsikidqirELQ 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 15599738 664 EAIRRKPY----SVVLLDEVEKAHPDVFNILLQVLE 695
Cdd:pfam13177 91 KEFSKSPYegkkKVYIIEDAEKMTASAANSLLKFLE 126
|
|
| PRK14956 |
PRK14956 |
DNA polymerase III subunits gamma and tau; Provisional |
552-696 |
4.74e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184920 [Multi-domain] Cd Length: 484 Bit Score: 46.86 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 552 LEGEREKLLRMEQ-ELHRRVIGQDEAVVAVSNAVRRSRAGLAdpnrpsgsFLFLGPTGVGKTELCKALAEFL-----FDT 625
Cdd:PRK14956 1 MSGTHEVLSRKYRpQFFRDVIHQDLAIGALQNALKSGKIGHA--------YIFFGPRGVGKTTIARILAKRLncenpIGN 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599738 626 EEALVRIDMSEFMEKHSVARLIGAPPGYVGFEEGGYLTEAIRRKP----YSVVLLDEVEKAHPDVFNILLQVLED 696
Cdd:PRK14956 73 EPCNECTSCLEITKGISSDVLEIDAASNRGIENIRELRDNVKFAPmggkYKVYIIDEVHMLTDQSFNALLKTLEE 147
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
318-589 |
5.69e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 318 EYRQYIEKDAALERRFQKVLVDEPSEEDTIAILRGLKER-YEVHHGVSITdgaiiaaakLSH--RYITDRQLPDKAIDLI 394
Cdd:pfam15921 364 ERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRlWDRDTGNSIT---------IDHlrRELDDRNMEVQRLEAL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 395 DEAAS---RIRME-----IDSKPEELDRLDRRLIQLKIEREALKKEDDEATRKRLAkLEEDivklEREYADL-EEIWKSE 465
Cdd:pfam15921 435 LKAMKsecQGQMErqmaaIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMT-LESS----ERTVSDLtASLQEKE 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 466 KAEVQGSAQI---QQKIEQAKQEMEAARRKGDLESMARIQYQTI---------------PDLERSLQMVDQHGKTENQLL 527
Cdd:pfam15921 510 RAIEATNAEItklRSRVDLKLQELQHLKNEGDHLRNVQTECEALklqmaekdkvieilrQQIENMTQLVGQHGRTAGAMQ 589
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599738 528 RNKVTDEEiaEVVSKWTGIPVSKMLEGEREKLLRmeqELHRRVIGQD-EAVVAVSNAVRRSRA 589
Cdd:pfam15921 590 VEKAQLEK--EINDRRLELQEFKILKDKKDAKIR---ELEARVSDLElEKVKLVNAGSERLRA 647
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
570-695 |
8.25e-05 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 45.57 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 570 VIGQDEAVVAVSNAVRRsragladpNRPSGSFLFLGPTGVGKTELCKALAEFLF----------DTEEALVRIDMSEFME 639
Cdd:COG2812 12 VVGQEHVVRTLKNALAS--------GRLAHAYLFTGPRGVGKTTLARILAKALNcengptgepcGECESCRAIAAGSHPD 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 640 KHsvarLIGAPPGYVGFEEGGYLTEAIRRKPYS----VVLLDEVEKAHPDVFNILLQVLE 695
Cdd:COG2812 84 VI----EIDAEASNIGVDDIRELIEKVSYAPVEgrykVYIIDEAHMLTTEAFNALLKTLE 139
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
570-622 |
1.97e-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: 1.97e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599738 570 VIGQDEA----VVAVSNAVRRSRAGLADPNR----PSGSFLFLGPTGVGKTELCKALAEFL 622
Cdd:cd19497 14 VIGQERAkkvlSVAVYNHYKRIRNNLKQKDDdvelEKSNILLIGPTGSGKTLLAQTLAKIL 74
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
378-575 |
2.24e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.73 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 378 HRYITDRQLPDKAIDLIDEaasRIRMEIDSKPEELDRlDRRLIQLKIEREAL--KKEDDEATRKRLA---KLEEDIVKLE 452
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQE---RLRQEKEEKAREVER-RRKLEEAEKARQAEmdRQAAIYAEQERMAmerERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 453 REYADLEEIWKSEKA-EVQGSAQI-------QQKIEQAKQEMEAARRKGDLE------------SMARIQYQTIPDLERS 512
Cdd:pfam17380 357 ERKRELERIRQEEIAmEISRMRELerlqmerQQKNERVRQELEAARKVKILEeerqrkiqqqkvEMEQIRAEQEEARQRE 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599738 513 LQMVDQHGKTENQLLRNKVTD-EEIAEVVSKWTGIPVSKMLEGEREKLLRMEQELHRRVIGQDE 575
Cdd:pfam17380 437 VRRLEEERAREMERVRLEEQErQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKE 500
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
177-381 |
3.18e-04 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 43.33 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 177 LDPVIGrDDEIRRTIQVL---QRRTKN----------NPVLIGEPGVGKTAIVEGLAQRIingevpdglkDKRLLALDMG 243
Cdd:COG1223 1 LDDVVG-QEEAKKKLKLIikeLRRRENlrkfglwpprKILFYGPPGTGKTMLAEALAGEL----------KLPLLTVRLD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 244 ALIAgaKFRGEFEERLKAVLNELgkQEGRVILFIDELHTMvgagkaegamdagnmlkpALARGELHCVGA---------T 314
Cdd:COG1223 70 SLIG--SYLGETARNLRKLFDFA--RRAPCVIFFDEFDAI------------------AKDRGDQNDVGEvkrvvnallQ 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599738 315 TLDEYRQYI----------EKDAALERRFQKVL-VDEPSEEDTIAILRGLKERYEVHhgVSITDGAIIAAAK-LSHRYI 381
Cdd:COG1223 128 ELDGLPSGSvviaatnhpeLLDSALWRRFDEVIeFPLPDKEERKEILELNLKKFPLP--FELDLKKLAKKLEgLSGADI 204
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
324-488 |
3.54e-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: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 324 EKDAALERRFQKVLVDEPSEEDTIAILRGLKERYEVHHGVSITDGAIIAAAKLSHRYITDRQLP-----DKAIDLIDEAA 398
Cdd:COG1196 609 READARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAalleaEAELEELAERL 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 399 SRIRMEIDSKPEELDRLDRRLIQLKIEREALKKEDDEATRKRLAKLEEDIVKLEREYADLEEIWKSEKAEVQGSAQIQQK 478
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
170
....*....|
gi 15599738 479 IEQAKQEMEA 488
Cdd:COG1196 769 LERLEREIEA 778
|
|
| PRK14959 |
PRK14959 |
DNA polymerase III subunits gamma and tau; Provisional |
573-696 |
5.61e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 43.52 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 573 QDEAVVAVSNAVRRSRAGLADPNRPSGSFLFLGPTGVGKTELCKALAEFL----------FDTEEALVRIDMSEFMEkhs 642
Cdd:PRK14959 13 QTFAEVAGQETVKAILSRAAQENRVAPAYLFSGTRGVGKTTIARIFAKALncetaptgepCNTCEQCRKVTQGMHVD--- 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15599738 643 VARLIGAppGYVGFEEGGYLTEAIRRKP----YSVVLLDEVEKAHPDVFNILLQVLED 696
Cdd:PRK14959 90 VVEIDGA--SNRGIDDAKRLKEAIGYAPmegrYKVFIIDEAHMLTREAFNALLKTLEE 145
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
404-502 |
5.69e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 404 EIDSKPEELDRLDRRLIQ----LKIEREALKKEDDE--ATRKRLAKLEEDIVKLEREYadlEEIWKSEKAEVQGSAQIQQ 477
Cdd:PRK12704 76 ELRERRNELQKLEKRLLQkeenLDRKLELLEKREEEleKKEKELEQKQQELEKKEEEL---EELIEEQLQELERISGLTA 152
|
90 100
....*....|....*....|....*.
gi 15599738 478 kiEQAKQE-MEAARRKGDLESMARIQ 502
Cdd:PRK12704 153 --EEAKEIlLEKVEEEARHEAAVLIK 176
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
445-569 |
6.14e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 42.00 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 445 EEDIVKLEREYADLEEIWKSEKAEVQGSAQIQQKIEQAKQEMEAARRK--------GDLESMARIQYQ--TIPDLERSLQ 514
Cdd:pfam13904 43 KLEGLKLERQPLEAYENWLAAKQRQRQKELQAQKEEREKEEQEAELRKrlakekyqEWLQRKARQQTKkrEESHKQKAAE 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15599738 515 mvdQHGKTENQLLRnKVTDEEIAEVVSKWtgipVSKMLEGEREKLLRMEQELHRR 569
Cdd:pfam13904 123 ---SASKSLAKPER-KVSQEEAKEVLQEW----ERKKLEQQQRKREEEQREQLKK 169
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
389-498 |
6.54e-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: 43.51 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 389 KAIDLIDEAASRIRMEIDSKPEELDRLDRRLIQLKIEREALKKEDDEATRK----RLAKLEEDIVKLEREYADLEEIWKS 464
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelqaELEELEEELEELQEELERLEEALEE 465
|
90 100 110
....*....|....*....|....*....|....*
gi 15599738 465 EKAEVqgsAQIQQKIEQAKQEMEAAR-RKGDLESM 498
Cdd:TIGR02168 466 LREEL---EEAEQALDAAERELAQLQaRLDSLERL 497
|
|
| AtoC |
COG2204 |
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ... |
548-803 |
1.48e-03 |
|
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: 41.87 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 548 VSKMLEGEReklLRMEQELHRRVIGQDEAVVAVSNAVRRsragLADPNRPsgsFLFLGPTGVGKTELCKALAEFLFDTEE 627
Cdd:COG2204 114 VERALERRR---LRRENAEDSGLIGRSPAMQEVRRLIEK----VAPSDAT---VLITGESGTGKELVARAIHRLSPRADG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 628 ALVRIDMSEFMEKHSVARLIGAppgyvgfeEGGYLTEAIRRKPYSV-------VLLDEVEKAHPDVFNILLQVLEDG--- 697
Cdd:COG2204 184 PFVAVNCAAIPEELLESELFGH--------EKGAFTGAVARRIGKFeladggtLFLDEIGEMPLALQAKLLRVLQERefe 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 698 RLTDSHGRTVDFRntvVVMTSNlgsaqiQELAGDREAQRaavmdavnahFRPEFINRIDEVVVFEPLAREQIAGIAEIQL 777
Cdd:COG2204 256 RVGGNKPIPVDVR---VIAATN------RDLEELVEEGR----------FREDLYYRLNVFPIELPPLRERREDIPLLAR 316
|
250 260
....*....|....*....|....*.
gi 15599738 778 GRLRKRLAERELSLELSQEALDKLIA 803
Cdd:COG2204 317 HFLARFAAELGKPVKLSPEALEALLA 342
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
399-534 |
1.61e-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: 42.36 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 399 SRIRMEIDSKPEELDRLDRRLIQLKIEREALKKEDDEATRKRLAKLEEDIVKLEREYADLEeiwksekAEVqgsAQIQQK 478
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELE-------AEI---ASLERS 309
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599738 479 IEQAKQEME-AARRKGDLESMARIQYQTIPDLERSLQmvdqhgktENQLLRNKVTDE 534
Cdd:TIGR02169 310 IAEKERELEdAEERLAKLEAEIDKLLAEIEELEREIE--------EERKRRDKLTEE 358
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
408-494 |
1.67e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 408 KPEELdRLDRRLIQLKIEREALKKEDDEATRKRLAKLEED-------IVKLEREYADLEEIWKSEKAEVQGSAQIQQ--- 477
Cdd:PTZ00121 1648 KAEEL-KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDekkaaeaLKKEAEEAKKAEELKKKEAEEKKKAEELKKaee 1726
|
90 100
....*....|....*....|.
gi 15599738 478 ----KIEQAKQEMEAARRKGD 494
Cdd:PTZ00121 1727 enkiKAEEAKKEAEEDKKKAE 1747
|
|
| clpX |
PRK05342 |
ATP-dependent Clp protease ATP-binding subunit ClpX; |
527-622 |
1.79e-03 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX;
Pssm-ID: 235422 [Multi-domain] Cd Length: 412 Bit Score: 41.68 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 527 LRNKVTDEEIAEVVSKWTGIPVSKmlegerekllrmeqELHRR----VIGQDEA----VVAVSNAVRRSRAG-------- 590
Cdd:PRK05342 40 LCNEIIREELKEEAVELKELPTPK--------------EIKAHldqyVIGQERAkkvlSVAVYNHYKRLRHGdkkdddve 105
|
90 100 110
....*....|....*....|....*....|..
gi 15599738 591 LADPNrpsgsFLFLGPTGVGKTELCKALAEFL 622
Cdd:PRK05342 106 LQKSN-----ILLIGPTGSGKTLLAQTLARIL 132
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
178-319 |
1.83e-03 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 41.96 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 178 DPVIGRDDEIRRTIQVLQRrtkNNPVLIGEPGVGKTAIVEGLAqRIINGEVpdglkdkrllaLDMGALIAGAKfrgEFEE 257
Cdd:PRK13341 34 DHILGEGRLLRRAIKADRV---GSLILYGPPGVGKTTLARIIA-NHTRAHF-----------SSLNAVLAGVK---DLRA 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599738 258 RLKAVLNELGKQEGRVILFIDELHTMvgaGKAEgaMDAgnmLKPALARGELHCVGATTLDEY 319
Cdd:PRK13341 96 EVDRAKERLERHGKRTILFIDEVHRF---NKAQ--QDA---LLPWVENGTITLIGATTENPY 149
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
204-283 |
2.25e-03 |
|
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: 39.57 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 204 LIGEPGVGKTAIVEGLAQRIingevpdGLKdkrLLALDMGALIagAKFRGEFEERLKAVLNELgKQEGRVILFIDELHTM 283
Cdd:cd19481 31 LYGPPGTGKTLLAKALAGEL-------GLP---LIVVKLSSLL--SKYVGESEKNLRKIFERA-RRLAPCILFIDEIDAI 97
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
389-492 |
2.46e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 389 KAIDLIDEAASRIRMEIDSKPEELDRLDRRLIQLKIEREALKKEDDEATRKRLAKLEEDIVKLEREYADLEEIWKSEKAE 468
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEAL 367
|
90 100
....*....|....*....|....
gi 15599738 469 VqgsAQIQQKIEQAKQEMEAARRK 492
Cdd:COG4913 368 L---AALGLPLPASAEEFAALRAE 388
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
179-281 |
3.00e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 39.41 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 179 PVIGRDDEIRRTIQVLQRRTKNNP---VLIGEPGVGKTAIVEGLAQRI---------------------INGEVPDGLKD 234
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALerdggyflrgkcdenlpysplLEALTREGLLR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599738 235 KRLLALDM-----------GALIAGAKFRGEFEERLKAVLNE----LGKQEGRVILFIDELH 281
Cdd:pfam13191 81 QLLDELESslleawraallEALAPVPELPGDLAERLLDLLLRlldlLARGERPLVLVLDDLQ 142
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
206-420 |
3.28e-03 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 40.84 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 206 GEPGVGKTAivegLAqRIINGEVpdglkDKRLLALDmgALIAGAKfrgefeeRLKAVLNE---LGKQEGRVILFIDELHT 282
Cdd:PRK13342 43 GPPGTGKTT----LA-RIIAGAT-----DAPFEALS--AVTSGVK-------DLREVIEEarqRRSAGRRTILFIDEIHR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 283 MvgaGKAEgaMDAgnmLKPALARGELHCVGATTldEyRQYIEKDAALERRFQkVLVDEP-SEEDTIAIL-RGLKERYEVH 360
Cdd:PRK13342 104 F---NKAQ--QDA---LLPHVEDGTITLIGATT--E-NPSFEVNPALLSRAQ-VFELKPlSEEDIEQLLkRALEDKERGL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599738 361 hgVSITDGAIIAAAKLSH---RyitdrqlpdKAIDLIdEAASRIRMEIDskPEEL-DRLDRRLI 420
Cdd:PRK13342 172 --VELDDEALDALARLANgdaR---------RALNLL-ELAALGVDSIT--LELLeEALQKRAA 221
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
389-496 |
3.51e-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: 41.21 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 389 KAIDLIDEAASRIRMEIDSKPEELDRLDRRLIQLKIEREALKKEDDEaTRKRLAKLEEDIVKLEREYADLE-----EIWK 463
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE-LEARIEELEEDLHKLEEALNDLEarlshSRIP 794
|
90 100 110
....*....|....*....|....*....|...
gi 15599738 464 SEKAEVQGSAQIQQKIEQAKQEMEAARRKGDLE 496
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
411-592 |
3.60e-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: 41.20 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 411 ELDRLDRRLIQLKIEREALKKEDDEATRkRLAKLEEDIVKLEREYADLEEIWKSEKAEVQGSAQIQQKIEQAKQEMEaAR 490
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTA-ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR-ER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 491 RKGDLESMARIQYQtipdlerslqmVDQHGKTENQLLRNKVTDEEIAEVVSKwtgipVSKMLEGEREKLLRMEQELHRRV 570
Cdd:TIGR02168 311 LANLERQLEELEAQ-----------LEELESKLDELAEELAELEEKLEELKE-----ELESLEAELEELEAELEELESRL 374
|
170 180
....*....|....*....|..
gi 15599738 571 IGQDEAVVAVSNAVRRSRAGLA 592
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIA 396
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
394-570 |
3.66e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 394 IDEAASRIRMEIDSKPEELdrldRRLIQLKIEREALKKEDDEatRKRLAKLEEdivKLEREYADLEEIWKSEKAEVQGSA 473
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEELKKAEEE--KKKVEQLKK---KEAEEKKKAEELKKAEEENKIKAA 1664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 474 QIQQKIEQAKQEMEAARRKGDLESMARIQYQTIPDLERSLQMVDQHGKTEnqllRNKVTDEEIAEVVSKWTGIPVSKMLE 553
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE----KKKAEELKKAEEENKIKAEEAKKEAE 1740
|
170
....*....|....*....
gi 15599738 554 GEREKL--LRMEQELHRRV 570
Cdd:PTZ00121 1741 EDKKKAeeAKKDEEEKKKI 1759
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
410-566 |
4.02e-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: 40.82 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 410 EELDRLDRRLIQLKIEREALKKEDDEATRKrLAKLEEDIVKLEREyadLEEIWKSEKAEVQGSAQIQQKIEQAKQEMEAA 489
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQE-LSDASRKIGEIEKE---IEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 490 RRKGDlESMARIQYQT---------IPDLERSLQMvDQHGKTENQLlrnkvtdEEIAEVVSKWTGIPVSkmLEGEREKLL 560
Cdd:TIGR02169 757 KSELK-ELEARIEELEedlhkleeaLNDLEARLSH-SRIPEIQAEL-------SKLEEEVSRIEARLRE--IEQKLNRLT 825
|
....*.
gi 15599738 561 RMEQEL 566
Cdd:TIGR02169 826 LEKEYL 831
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
517-680 |
4.84e-03 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 39.99 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 517 DQHGKTENQLLRNKVTDEEIAEVVSKWTGIPVSKMLEGEREKLlRMEQelhrrVIGQDEAVVAVSNAV--------RRSR 588
Cdd:COG1222 33 LQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDV-TFDD-----IGGLDEQIEEIREAVelplknpeLFRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 589 AGLadpnRPSGSFLFLGPTGVGKTELCKALAEflfDTEEALVRIDMSEFMEKhsvarligappgYVGfeEGGYLT----E 664
Cdd:COG1222 107 YGI----EPPKGVLLYGPPGTGKTLLAKAVAG---ELGAPFIRVRGSELVSK------------YIG--EGARNVrevfE 165
|
170
....*....|....*.
gi 15599738 665 AIRRKPYSVVLLDEVE 680
Cdd:COG1222 166 LAREKAPSIIFIDEID 181
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
391-495 |
5.10e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 391 IDLIDEAASRIRMEIDSKPEELDRLDRRLIQLKIEREALKKEDDEAT------RKRLAKLEEDIVKLEREYADLEEIWKS 464
Cdd:COG1340 169 LKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHkeiveaQEKADELHEEIIELQKELRELRKELKK 248
|
90 100 110
....*....|....*....|....*....|....
gi 15599738 465 --EKAEVQGSAQIQQKI-EQAKQEMEAARRKGDL 495
Cdd:COG1340 249 lrKKQRALKREKEKEELeEKAEEIFEKLKKGEKL 282
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
388-492 |
5.38e-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: 39.52 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 388 DKAIDLIDEAASRIRMEIDSKPEELDRLDRRLIQLKIEREALKKE------DDEATRKRLAKLEEDI--VKLEREYADLE 459
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEikrlelEIEEVEARIKKYEEQLgnVRNNKEYEALQ 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 15599738 460 --------EIWKSEKAEVQGSAQI---QQKIEQAKQEMEAARRK 492
Cdd:COG1579 96 keieslkrRISDLEDEILELMERIeelEEELAELEAELAELEAE 139
|
|
| hslU |
PRK05201 |
ATP-dependent protease ATPase subunit HslU; |
564-619 |
5.96e-03 |
|
ATP-dependent protease ATPase subunit HslU;
Pssm-ID: 235364 [Multi-domain] Cd Length: 443 Bit Score: 40.06 E-value: 5.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599738 564 QELHRRVIGQDEAVVAVSNAVR---RsRAGLADPNR----PSgSFLFLGPTGVGKTELCKALA 619
Cdd:PRK05201 11 SELDKYIIGQDDAKRAVAIALRnrwR-RMQLPEELRdevtPK-NILMIGPTGVGKTEIARRLA 71
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
405-573 |
7.35e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 405 IDSKPEELDRLDRRLIQLKIEREALKKEDDEATRKR--LAKLEE------DIVKLEREYADLEEiwksEKAEVQGS---- 472
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERReaLQRLAEyswdeiDVASAEREIAELEA----ELERLDASsddl 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 473 AQIQQKIEQAKQEMEAAR--------RKGDLES-MARIQYQtIPDLERSLQMVDQHGKTE-NQLLRNKVTDEEIAEVVSK 542
Cdd:COG4913 688 AALEEQLEELEAELEELEeeldelkgEIGRLEKeLEQAEEE-LDELQDRLEAAEDLARLElRALLEERFAAALGDAVERE 766
|
170 180 190
....*....|....*....|....*....|.
gi 15599738 543 wtgipVSKMLEGEREKLLRMEQELHRRVIGQ 573
Cdd:COG4913 767 -----LRENLEERIDALRARLNRAEEELERA 792
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
203-333 |
7.82e-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: 37.66 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 203 VLIGEPGVGKTAIVEGLAQRIINGEV----------PDGLKDKRLLALDMGALIAGAkFRGEFEERLKAVLNELGKQEGR 272
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSNRPVfyvqltrdttEEDLFGRRNIDPGGASWVDGP-LVRAAREGEIAVLDEINRANPD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599738 273 VilfIDELHTmvgagkaegAMDAGNMLKPALaRGELHC------VGATTLDEYRQYIEKDAALERRF 333
Cdd:pfam07728 82 V---LNSLLS---------LLDERRLLLPDG-GELVKAapdgfrLIATMNPLDRGLNELSPALRSRF 135
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
400-573 |
8.64e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 39.72 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 400 RIRMEIDS----KPEELDRlDRRLIQLKIEREALKKEDDEATRKRLAKLEEDIVKlEREYADLEEIWKSEKAEV---QGS 472
Cdd:pfam17380 393 RVRQELEAarkvKILEEER-QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR-EMERVRLEEQERQQQVERlrqQEE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 473 AQIQQKIE-----QAKQEMEAARRKgDLESMARIQYQTIPDLERSLQMVDQhgktENQLLRNKVTDEEiaevvskwtgip 547
Cdd:pfam17380 471 ERKRKKLElekekRDRKRAEEQRRK-ILEKELEERKQAMIEEERKRKLLEK----EMEERQKAIYEEE------------ 533
|
170 180
....*....|....*....|....*.
gi 15599738 548 vsKMLEGEREKLLRMEQELHRRVIGQ 573
Cdd:pfam17380 534 --RRREAEEERRKQQEMEERRRIQEQ 557
|
|
| PRK14953 |
PRK14953 |
DNA polymerase III subunits gamma and tau; Provisional |
568-696 |
9.12e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237867 [Multi-domain] Cd Length: 486 Bit Score: 39.42 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599738 568 RRVIGQDEAVVAVSNAVRRsragladpNRPSGSFLFLGPTGVGKTELCKALAEFL-----FDTE-----EALVRIDMSEF 637
Cdd:PRK14953 16 KEVIGQEIVVRILKNAVKL--------QRVSHAYIFAGPRGTGKTTIARILAKVLnclnpQEGEpcgkcENCVEIDKGSF 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599738 638 MEKHSvarlIGAPPGYvGFEEGGYLTEAIRRKP----YSVVLLDEVEKAHPDVFNILLQVLED 696
Cdd:PRK14953 88 PDLIE----IDAASNR-GIDDIRALRDAVSYTPikgkYKVYIIDEAHMLTKEAFNALLKTLEE 145
|
|
| |
