|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
6-842 |
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: 1403.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 6 TTKTGEVLQEAMKAATSAGNPDIRPGHILVALLEQKEGIAAPLLEAAGVNPSGVLTRAKELVAGYPSASGANmANPQFNR 85
Cdd:COG0542 7 TEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGRLPKVSGSS-GQPYLSP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 86 DAVNALNAAEELAGELGDEYVSTEILLIG-VATGQSEAATVLQSAGATAEALKGALTSVRGSRKVTTENPEEQYQALEKY 164
Cdd:COG0542 86 RLKRVLELAELEARKLGDEYISTEHLLLAlLREGEGVAARILKKLGITLEALREALEELRGGSRVTSQNPESKTPALDKY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 165 ATDLTARAREGKIDPVIGRDAEIRRVVQVLSRRTKNNPVLIGEPGVGKTAIVEGLARRIVAGDVPESLKGKTLMSLDLGS 244
Cdd:COG0542 166 GRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDKRVLSLDLGA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 245 MVAGAKYRGEFEERLKAVLDEIKESDGQIITFIDEIHTIVGAGATgDGSMDAGNMIKPMLARGELRLVGATTLDEYRKYI 324
Cdd:COG0542 246 LVAGAKYRGEFEERLKAVLDEVKKSEGNIILFIDELHTLVGAGGA-EGAMDAANLLKPALARGELRCIGATTLDEYRKYI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 325 EKDAALERRFQQVFVGEPSVEDAIGILRGLKERYEVHHGVRIQDSALVAAATLSDRYITSRFLPDKAIDLVDEAASRLRM 404
Cdd:COG0542 325 EKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAIDLIDEAAARVRM 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 405 EIDSSPEEIDSAERIVRRLEIEEMALEKETDIASKERLDKLREELADEREKLNALKTRWQNEKSSIDDVRSVREELDAlr 484
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ-- 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 485 tesekaeregdygrvaelRYGRIPELEKKLEAAEEsvADAEENSMLKEEVTPQEVAEVVSAWTGIPAGKMMQGETEKLLE 564
Cdd:COG0542 483 ------------------RYGKIPELEKELAELEE--ELAELAPLLREEVTEEDIAEVVSRWTGIPVGKLLEGEREKLLN 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 565 MELNLGRRVVGQNAAVEAVSDAVRRSRAGVADPNRPTGSFLFLGPTGVGKTELAKALAEFLFDDERAMVRIDMSEYGEKH 644
Cdd:COG0542 543 LEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYMEKH 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 645 SVARLIGAPPGYVGYDAGGQLTEAVRRRPYTVVLFDEVEKAHPDVFDVLLQVLDEGRLTDGQGRTVDFRNTILILTSNLG 724
Cdd:COG0542 623 SVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIG 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 725 A-------------GGTHEQIMDAVKMAFKPEFINRLDDVVIFDPLTSEQLRGIVDIQVRNLAERLEARRLVLDVSDEAL 791
Cdd:COG0542 703 SelildlaedepdyEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAAK 782
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1092600816 792 DWLSERGYDPAYGARPLRRLVQKAIGDELARRLLAGDVRDGDRVEVTVADD 842
Cdd:COG0542 783 DFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDG 833
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
6-842 |
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: 1371.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 6 TTKTGEVLQEAMKAATSAGNPDIRPGHILVALLEQKEGIAAPLLEAAGVNPSGVLTRAKELVAGYPSASGANmANPQFNR 85
Cdd:TIGR03346 2 TEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEKELERLPKVSGPG-GQVYLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 86 DAVNALNAAEELAGELGDEYVSTEILLIGVATGQSEAATVLQSAGATAEALKGALTSVRGSRKVTTENPEEQYQALEKYA 165
Cdd:TIGR03346 81 DLNRLLNLAEKLAQKRGDEFISSEHLLLALLDDKGTLGKLLKEAGATADALEAAINAVRGGQKVTDANAEDQYEALEKYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 166 TDLTARAREGKIDPVIGRDAEIRRVVQVLSRRTKNNPVLIGEPGVGKTAIVEGLARRIVAGDVPESLKGKTLMSLDLGSM 245
Cdd:TIGR03346 161 RDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLALDMGAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 246 VAGAKYRGEFEERLKAVLDEIKESDGQIITFIDEIHTIVGAGATgDGSMDAGNMIKPMLARGELRLVGATTLDEYRKYIE 325
Cdd:TIGR03346 241 IAGAKYRGEFEERLKAVLNEVTKSEGQIILFIDELHTLVGAGKA-EGAMDAGNMLKPALARGELHCIGATTLDEYRKYIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 326 KDAALERRFQQVFVGEPSVEDAIGILRGLKERYEVHHGVRIQDSALVAAATLSDRYITSRFLPDKAIDLVDEAASRLRME 405
Cdd:TIGR03346 320 KDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAARIRME 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 406 IDSSPEEIDSAERIVRRLEIEEMALEKETDIASKERLDKLREELADEREKLNALKTRWQNEKSSIDDVRSVREELDALRT 485
Cdd:TIGR03346 400 IDSKPEELDELDRRIIQLEIEREALKKEKDEASKKRLEDLEKELADLEEEYAELEEQWKAEKASIQGIQQIKEEIEQVRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 486 ESEKAEREGDYGRVAELRYGRIPELEKKLEAAEESVADaEENSMLKEEVTPQEVAEVVSAWTGIPAGKMMQGETEKLLEM 565
Cdd:TIGR03346 480 ELEQAEREGDLAKAAELQYGKLPELEKQLQAAEQKLGE-EQNRLLREEVTAEEIAEVVSRWTGIPVSKMLEGEREKLLHM 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 566 ELNLGRRVVGQNAAVEAVSDAVRRSRAGVADPNRPTGSFLFLGPTGVGKTELAKALAEFLFDDERAMVRIDMSEYGEKHS 645
Cdd:TIGR03346 559 EEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRIDMSEYMEKHS 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 646 VARLIGAPPGYVGYDAGGQLTEAVRRRPYTVVLFDEVEKAHPDVFDVLLQVLDEGRLTDGQGRTVDFRNTILILTSNLGA 725
Cdd:TIGR03346 639 VARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGS 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 726 ------------GGTHEQIMDAVKMAFKPEFINRLDDVVIFDPLTSEQLRGIVDIQVRNLAERLEARRLVLDVSDEALDW 793
Cdd:TIGR03346 719 dfiqelaggddyEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKITLELSDAALDF 798
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 1092600816 794 LSERGYDPAYGARPLRRLVQKAIGDELARRLLAGDVRDGDRVEVTVADD 842
Cdd:TIGR03346 799 LAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGG 847
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
6-843 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 1001.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 6 TTKTGEVLQEAMKAATSAGNPDIRPGHILVALLEQKEGIAAPLLEAAGVNPSGVLTRAKELVAGYPSASGANmANPQFNR 85
Cdd:PRK10865 7 TNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVRPLLTSAGINAGQLRTDINQALSRLPQVEGTG-GDVQPSQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 86 DAVNALNAAEELAGELGDEYVSTEILLIGVATGQSEAATVLQSAGATAEALKGALTSVRGSRKVTTENPEEQYQALEKYA 165
Cdd:PRK10865 86 DLVRVLNLCDKLAQKRGDNFISSELFVLAALESRGTLADILKAAGATTANITQAIEQMRGGESVNDQGAEDQRQALKKYT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 166 TDLTARAREGKIDPVIGRDAEIRRVVQVLSRRTKNNPVLIGEPGVGKTAIVEGLARRIVAGDVPESLKGKTLMSLDLGSM 245
Cdd:PRK10865 166 IDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLALDMGAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 246 VAGAKYRGEFEERLKAVLDEIKESDGQIITFIDEIHTIVGAGaTGDGSMDAGNMIKPMLARGELRLVGATTLDEYRKYIE 325
Cdd:PRK10865 246 VAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAG-KADGAMDAGNMLKPALARGELHCVGATTLDEYRQYIE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 326 KDAALERRFQQVFVGEPSVEDAIGILRGLKERYEVHHGVRIQDSALVAAATLSDRYITSRFLPDKAIDLVDEAASRLRME 405
Cdd:PRK10865 325 KDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASSIRMQ 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 406 IDSSPEEIDSAERIVRRLEIEEMALEKETDIASKERLDKLREELADEREKLNALKTRWQNEKSSIDDVRSVREELDALRT 485
Cdd:PRK10865 405 IDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKAELEQAKI 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 486 ESEKAEREGDYGRVAELRYGRIPELEKKLEAAEEsvADAEENSMLKEEVTPQEVAEVVSAWTGIPAGKMMQGETEKLLEM 565
Cdd:PRK10865 485 AIEQARRVGDLARMSELQYGKIPELEKQLAAATQ--LEGKTMRLLRNKVTDAEIAEVLARWTGIPVSRMLESEREKLLRM 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 566 ELNLGRRVVGQNAAVEAVSDAVRRSRAGVADPNRPTGSFLFLGPTGVGKTELAKALAEFLFDDERAMVRIDMSEYGEKHS 645
Cdd:PRK10865 563 EQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEKHS 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 646 VARLIGAPPGYVGYDAGGQLTEAVRRRPYTVVLFDEVEKAHPDVFDVLLQVLDEGRLTDGQGRTVDFRNTILILTSNLGA 725
Cdd:PRK10865 643 VSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNLGS 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 726 ------------GGTHEQIMDAVKMAFKPEFINRLDDVVIFDPLTSEQLRGIVDIQVRNLAERLEARRLVLDVSDEALDW 793
Cdd:PRK10865 723 dliqerfgeldyAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYEIHISDEALKL 802
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 1092600816 794 LSERGYDPAYGARPLRRLVQKAIGDELARRLLAGDVRDGDRVEVTVADDS 843
Cdd:PRK10865 803 LSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDDR 852
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
32-844 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 826.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 32 HILVALLEQKEGIAAPLLEAAGVNPSGVLTRAKELV---AGYPSAsganmaNPQFNRDAVNALNAAEELAGELGDEYVST 108
Cdd:CHL00095 32 QILLGLIGEGTGIAARALKSMGVTLKDARIEVEKIIgrgTGFVAV------EIPFTPRAKRVLEMSLEEARDLGHNYIGT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 109 EILLIG-VATGQSEAATVLQSAGA---------------TAEALKGALTSvrGSRKVTtenpeeqyqaLEKYATDLTARA 172
Cdd:CHL00095 106 EHLLLAlLEEGEGVAARVLENLGVdlskirslilnligeIIEAILGAEQS--RSKTPT----------LEEFGTNLTKEA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 173 REGKIDPVIGRDAEIRRVVQVLSRRTKNNPVLIGEPGVGKTAIVEGLARRIVAGDVPESLKGKTLMSLDLGSMVAGAKYR 252
Cdd:CHL00095 174 IDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDKLVITLDIGLLLAGTKYR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 253 GEFEERLKAVLDEIKESDgQIITFIDEIHTIVGAGATgDGSMDAGNMIKPMLARGELRLVGATTLDEYRKYIEKDAALER 332
Cdd:CHL00095 254 GEFEERLKRIFDEIQENN-NIILVIDEVHTLIGAGAA-EGAIDAANILKPALARGELQCIGATTLDEYRKHIEKDPALER 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 333 RFQQVFVGEPSVEDAIGILRGLKERYEVHHGVRIQDSALVAAATLSDRYITSRFLPDKAIDLVDEAASRLRMeidsspee 412
Cdd:CHL00095 332 RFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLDEAGSRVRL-------- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 413 idsaerIVRRLEIEEMALEKEtdiaskerldkLREELADEREklnalktrwqnekssiddvrsvreeldalrtesekAER 492
Cdd:CHL00095 404 ------INSRLPPAARELDKE-----------LREILKDKDE-----------------------------------AIR 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 493 EGDYGRVAELRyGRIPELEKKLEAAEESVADAEENSMLKEEVTPQEVAEVVSAWTGIPAGKMMQGETEKLLEMELNLGRR 572
Cdd:CHL00095 432 EQDFETAKQLR-DREMEVRAQIAAIIQSKKTEEEKRLEVPVVTEEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKR 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 573 VVGQNAAVEAVSDAVRRSRAGVADPNRPTGSFLFLGPTGVGKTELAKALAEFLFDDERAMVRIDMSEYGEKHSVARLIGA 652
Cdd:CHL00095 511 IIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALASYFFGSEDAMIRLDMSEYMEKHTVSKLIGS 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 653 PPGYVGYDAGGQLTEAVRRRPYTVVLFDEVEKAHPDVFDVLLQVLDEGRLTDGQGRTVDFRNTILILTSNLGA------- 725
Cdd:CHL00095 591 PPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSkvietns 670
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 726 -------GGTHEQ----------IMDAVKMAFKPEFINRLDDVVIFDPLTSEQLRGIVDIQVRNLAERLEARRLVLDVSD 788
Cdd:CHL00095 671 gglgfelSENQLSekqykrlsnlVNEELKQFFRPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTE 750
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092600816 789 EALDWLSERGYDPAYGARPLRRLVQKAIGDELARRLLAGDVRDGDRVEVTVADDSE 844
Cdd:CHL00095 751 RIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVDVNDEKE 806
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
4-825 |
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: 776.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 4 TPTTKTGevLQEAMKAATSAGNPDIRPGHILVALLEQKEGIAAPLLEAAGVNPSGVLTrakELVAGYPSASGANMANPQF 83
Cdd:TIGR03345 2 NPTSRRA--LEQAAALCVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKA---DLARALDKLPRGNTRTPVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 84 NRDAVNALNAAEELAG-ELGDEYVSTEILLIGVATGQSEAATVLQSAGATA----EALKGAL-----TSVRGSRKVTTEN 153
Cdd:TIGR03345 77 SPHLVELLQEAWLLASlELGDGRIRSGHLLLALLTDPELRRLLGSISPELAkidrEALREALpalveGSAEASAAAADAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 154 PEEQYQ------ALEKYATDLTARAREGKIDPVIGRDAEIRRVVQVLSRRTKNNPVLIGEPGVGKTAIVEGLARRIVAGD 227
Cdd:TIGR03345 157 PAGAAAgaagtsALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 228 VPESLKGKTLMSLDLGSMVAGAKYRGEFEERLKAVLDEIKESDGQIITFIDEIHTIVGAGATGdGSMDAGNMIKPMLARG 307
Cdd:TIGR03345 237 VPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPIILFIDEAHTLIGAGGQA-GQGDAANLLKPALARG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 308 ELRLVGATTLDEYRKYIEKDAALERRFQQVFVGEPSVEDAIGILRGLKERYEVHHGVRIQDSALVAAATLSDRYITSRFL 387
Cdd:TIGR03345 316 ELRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 388 PDKAIDLVDEAASRLRMEIDSSPEEIDSAERIVRRLEIEEMALEKE--TDIASKERLDKLREELADEREKLNALKTRWQN 465
Cdd:TIGR03345 396 PDKAVSLLDTACARVALSQNATPAALEDLRRRIAALELELDALEREaaLGADHDERLAELRAELAALEAELAALEARWQQ 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 466 EKSSIDDVRSVREELDAlrteSEKAEREGDYGRVAELRygripELEKKLEAAEEsvadaeENSMLKEEVTPQEVAEVVSA 545
Cdd:TIGR03345 476 EKELVEAILALRAELEA----DADAPADDDDALRAQLA-----ELEAALASAQG------EEPLVFPEVDAQAVAEVVAD 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 546 WTGIPAGKMMQGETEKLLEMELNLGRRVVGQNAAVEAVSDAVRRSRAGVADPNRPTGSFLFLGPTGVGKTELAKALAEFL 625
Cdd:TIGR03345 541 WTGIPVGRMVRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELL 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 626 FDDERAMVRIDMSEYGEKHSVARLIGAPPGYVGYDAGGQLTEAVRRRPYTVVLFDEVEKAHPDVFDVLLQVLDEGRLTDG 705
Cdd:TIGR03345 621 YGGEQNLITINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDG 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 706 QGRTVDFRNTILILTSNLGAggthEQIM------------DAVKMA--------FKPEFINRLdDVVIFDPLTSEQLRGI 765
Cdd:TIGR03345 701 EGREIDFKNTVILLTSNAGS----DLIMalcadpetapdpEALLEAlrpellkvFKPAFLGRM-TVIPYLPLDDDVLAAI 775
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092600816 766 VDIQVRNLAERLEAR-RLVLDVSDEALDWLSERGYDPAYGARPLRRLVQKAIGDELARRLL 825
Cdd:TIGR03345 776 VRLKLDRIARRLKENhGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQIL 836
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
11-839 |
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: 739.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 11 EVLQEAMKAATSAGNPDIRPGHILVALLEQKEGIAapLLEAAGVNPSGVLTRAKE-LVAGYPSASGANMANP----QFNR 85
Cdd:TIGR02639 7 RILSDALEEAKERRHEFVTLEHLLLALLDDNEAIE--ILEECGGDVELLRKRLEDyLEENLPVIPEDIDEEPeqtvGVQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 86 ---DAVNALNAAEELAGELGDEYVSTeilligVATGQSEAATVLQSAGATAEALKGALTSVRGSRKVTTENPEE------ 156
Cdd:TIGR02639 85 viqRALLHVKSAGKKEIDIGDLLVAL------FDEEDSHASYFLKSQGITRLDILNYISHGISKDDGKDQLGEEagkeee 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 157 -QYQALEKYATDLTARAREGKIDPVIGRDAEIRRVVQVLSRRTKNNPVLIGEPGVGKTAIVEGLARRIVAGDVPESLKGK 235
Cdd:TIGR02639 159 kGQDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERLKNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 236 TLMSLDLGSMVAGAKYRGEFEERLKAVLDEIKESDGQIItFIDEIHTIVGAGATGDGSMDAGNMIKPMLARGELRLVGAT 315
Cdd:TIGR02639 239 KIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAIL-FIDEIHTIVGAGATSGGSMDASNLLKPALSSGKIRCIGST 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 316 TLDEYRKYIEKDAALERRFQQVFVGEPSVEDAIGILRGLKERYEVHHGVRIQDSALVAAATLSDRYITSRFLPDKAIDLV 395
Cdd:TIGR02639 318 TYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDVI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 396 DEAASRLRMEIDSSPeeidsaerivrrleieemaleketdiaskerldklreeladereklnalktrwqnekssiddvrs 475
Cdd:TIGR02639 398 DEAGAAFRLRPKAKK----------------------------------------------------------------- 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 476 vreeldalrtesekaeregdygrvaelrygripelekkleaaeesvadaeensmlKEEVTPQEVAEVVSAWTGIPAGKMM 555
Cdd:TIGR02639 413 -------------------------------------------------------KANVNVKDIENVVAKMAKIPVKTVS 437
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 556 QGETEKLLEMELNLGRRVVGQNAAVEAVSDAVRRSRAGVADPNRPTGSFLFLGPTGVGKTELAKALAEFLfddERAMVRI 635
Cdd:TIGR02639 438 SDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEEL---GVHLLRF 514
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 636 DMSEYGEKHSVARLIGAPPGYVGYDAGGQLTEAVRRRPYTVVLFDEVEKAHPDVFDVLLQVLDEGRLTDGQGRTVDFRNT 715
Cdd:TIGR02639 515 DMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNV 594
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 716 ILILTSNLGA------------GGTHEQIMDAVKMAFKPEFINRLDDVVIFDPLTSEQLRGIVDIQVRNLAERLEARRLV 783
Cdd:TIGR02639 595 ILIMTSNAGAsemskppigfggENRESKSLKAIKKLFSPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIE 674
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092600816 784 LDVSDEALDWLSERGYDPAYGARPLRRLVQKAIGDELARRLLAGDVRDGDRVEVTV 839
Cdd:TIGR02639 675 LELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEILFGKLKKGGSVKISL 730
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
161-847 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 554.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 161 LEKYATDLTARAREGKIDPVIGRDAEIRRVVQVLSRRTKNNPVLIGEPGVGKTAIVEGLARRIVAGDVPESLKGKTLMSL 240
Cdd:PRK11034 169 MENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 241 DLGSMVAGAKYRGEFEERLKAVLDEIkESDGQIITFIDEIHTIVGAGATGDGSMDAGNMIKPMLARGELRLVGATTLDEY 320
Cdd:PRK11034 249 DIGSLLAGTKYRGDFEKRFKALLKQL-EQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVIGSTTYQEF 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 321 RKYIEKDAALERRFQQVFVGEPSVEDAIGILRGLKERYEVHHGVRIQDSALVAAATLSDRYITSRFLPDKAIDLVDEAAS 400
Cdd:PRK11034 328 SNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 401 RLRMeidsSPeeidsaerivrrleieemaleketdiaskerldklreelADEREKlnalktrwqneKSSIDDVRSVreel 480
Cdd:PRK11034 408 RARL----MP---------------------------------------VSKRKK-----------TVNVADIESV---- 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 481 dalrtesekaeregdygrVAelRYGRIPelEKKLEAAEESVADAEENSMlkeevtpqevaevvsawtgipagKMMqgete 560
Cdd:PRK11034 430 ------------------VA--RIARIP--EKSVSQSDRDTLKNLGDRL-----------------------KML----- 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 561 kllemelnlgrrVVGQNAAVEAVSDAVRRSRAGVADPNRPTGSFLFLGPTGVGKTELAKALAEFLfddERAMVRIDMSEY 640
Cdd:PRK11034 460 ------------VFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL---GIELLRFDMSEY 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 641 GEKHSVARLIGAPPGYVGYDAGGQLTEAVRRRPYTVVLFDEVEKAHPDVFDVLLQVLDEGRLTDGQGRTVDFRNTILILT 720
Cdd:PRK11034 525 MERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMT 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 721 SNLGAGGTHEQ------------IMDAVKMAFKPEFINRLDDVVIFDPLTSEQLRGIVDIQVRNLAERLEARRLVLDVSD 788
Cdd:PRK11034 605 TNAGVRETERKsiglihqdnstdAMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQ 684
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1092600816 789 EALDWLSERGYDPAYGARPLRRLVQKAIGDELARRLLAGDVRDGDRVEVTVADDSESLK 847
Cdd:PRK11034 685 EARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKEKNELT 743
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
561-754 |
1.92e-103 |
|
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: 317.20 E-value: 1.92e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 561 KLLEMELNLGRRVVGQNAAVEAVSDAVRRSRAGVADPNRPTGSFLFLGPTGVGKTELAKALAEFLFDDERAMVRIDMSEY 640
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 641 GEKHSVARLIGAPPGYVGYDAGGQLTEAVRRRPYTVVLFDEVEKAHPDVFDVLLQVLDEGRLTDGQGRTVDFRNTILILT 720
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190
....*....|....*....|....*....|....
gi 1092600816 721 SNlgaggtheqimdavkmAFKPEFINRLDDVVIF 754
Cdd:cd19499 161 SN----------------HFRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
599-751 |
1.69e-86 |
|
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: 272.53 E-value: 1.69e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 599 RPTGSFLFLGPTGVGKTELAKALAEFLFDDERAMVRIDMSEYGEKHSVARLIGAPPGYVGYDAGGQLTEAVRRRPYTVVL 678
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 679 FDEVEKAHPDVFDVLLQVLDEGRLTDGQGRTVDFRNTILILTSNLGA---------------GGTHEQIMDAVKMAFKPE 743
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSekisdasrlgdspdyELLKEEVMDLLKKGFIPE 160
|
....*...
gi 1092600816 744 FINRLDDV 751
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 ... |
343-446 |
1.28e-46 |
|
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.
Pssm-ID: 465544 [Multi-domain] Cd Length: 104 Bit Score: 161.50 E-value: 1.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 343 SVEDAIGILRGLKERYEVHHGVRIQDSALVAAATLSDRYITSRFLPDKAIDLVDEAASRLRMEIDSSPEEIDSAERIVRR 422
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|....
gi 1092600816 423 LEIEEMALEKETDIASKERLDKLR 446
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, ... |
757-837 |
4.73e-30 |
|
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: 113.65 E-value: 4.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 757 LTSEQLRGIVDIQVRNLAERLEARRLVLDVSDEALDWLSERGYDPAYGARPLRRLVQKAIGDELARRLLAGDVRDGDRVE 836
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 1092600816 837 V 837
Cdd:pfam10431 81 V 81
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
757-846 |
8.28e-27 |
|
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA) 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: 104.45 E-value: 8.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 757 LTSEQLRGIVDIQVRNLAERLEARRLVLDVSDEALDWLSERGYDPAYGARPLRRLVQKAIGDELARRLLAGDVRDGDRVE 836
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
90
....*....|
gi 1092600816 837 VTVADDSESL 846
Cdd:smart01086 81 VDVDDGELVF 90
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
574-756 |
6.96e-20 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 87.20 E-value: 6.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 574 VGQNAAVEAVSDAVRRsragvadpnRPTGSFLFLGPTGVGKTELAKALAEFLFDDERAMVRIDMSEYGEKHSVARLIgap 653
Cdd:cd00009 1 VGQEEAIEALREALEL---------PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELF--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 654 pgyvGYDAGGQLTEAVRRRPYTVVLFDEVEKAHPDVFDVLLQVLDEGRLTdgqgrTVDFRNTILILTSNLGAGGTheqim 733
Cdd:cd00009 69 ----GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATNRPLLGD----- 134
|
170 180
....*....|....*....|...
gi 1092600816 734 davkmaFKPEFINRLDDVVIFDP 756
Cdd:cd00009 135 ------LDRALYDRLDIRIVIPL 151
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
181-342 |
1.46e-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: 86.05 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 181 IGRDAEIRRVVQVLSRRTKNNPVLIGEPGVGKTAIVEGLARRIVagdvpesLKGKTLMSLDLGSMVAGAKYRGEFEERLK 260
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELF-------RPGAPFLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 261 AVLDEIKESDGQIITFIDEIHTI-VGAGATGDGSMDAGNMikPMLARGELRLVGATTLDEYRKyieKDAALERRFQQVFV 339
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDSLsRGAQNALLRVLETLND--LRIDRENVRVIGATNRPLLGD---LDRALYDRLDIRIV 148
|
...
gi 1092600816 340 GEP 342
Cdd:cd00009 149 IPL 151
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
204-338 |
4.24e-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: 66.85 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 204 LIGEPGVGKTAIVEGLARRIvagdvpeslkGKTLMSLDLGSMVagAKYRGEFEERLKAVLDEIKESDGQIItFIDEIHTI 283
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELV--SKYVGESEKRLRELFEAAKKLAPCVI-FIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092600816 284 VGAGATGDGSMDAG--NMIKPML-----ARGELRLVGATTldeyrkYIEK-DAALERRFQQVF 338
Cdd:pfam00004 70 AGSRGSGGDSESRRvvNQLLTELdgftsSNSKVIVIAATN------RPDKlDPALLGRFDRII 126
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
605-724 |
4.30e-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: 67.40 E-value: 4.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 605 LFLGPTGVGKTELAKALAEFLFDDERAMVRIDMSEYGEKHSVARLIGAPPGYVGYDAGGQ----LTEAVRRRPYTVVLFD 680
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1092600816 681 EVEKAHPDVFDVLLQVLDEGRLTDGQGRtvdFRNTILILTSNLG 724
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTNDE 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
603-731 |
4.20e-12 |
|
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: 64.24 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 603 SFLFLGPTGVGKTELAKALAEFLFDDERAMVRI--DMSEygekhsvARLIGA--PPGYVGYDAGGQLTEAVRRRpyTVVL 678
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLtrDTTE-------EDLFGRrnIDPGGASWVDGPLVRAAREG--EIAV 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092600816 679 FDEVEKAHPDVFDVLLQVLDEGRLTDGQGRT---VDFRNTILILTSNLGAGGTHEQ 731
Cdd:pfam07728 72 LDEINRANPDVLNSLLSLLDERRLLLPDGGElvkAAPDGFRLIATMNPLDRGLNEL 127
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
586-754 |
1.84e-10 |
|
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: 59.99 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 586 AVRRSRAGVADPNRPTGSFLFLGPTGVGKTELAKALAEFLfddERAMVRIDMSEYGEKHSvarligappgYVGYDAGGQL 665
Cdd:cd19481 11 APRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGEL---GLPLIVVKLSSLLSKYV----------GESEKNLRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 666 TEAVRRRPYTVVLFDEVEKA---------HPDVFDVLLQVLDEgrlTDGQGRTVDFrntILILTSNlgaggtHEQIMDav 736
Cdd:cd19481 78 FERARRLAPCILFIDEIDAIgrkrdssgeSGELRRVLNQLLTE---LDGVNSRSKV---LVIAATN------RPDLLD-- 143
|
170 180
....*....|....*....|
gi 1092600816 737 kmafkPEFI--NRLDDVVIF 754
Cdd:cd19481 144 -----PALLrpGRFDEVIEF 158
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
33-368 |
1.99e-10 |
|
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: 63.78 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 33 ILVALLEQKEGIAAPLLEAAGVNPSGVLTRAKELVAGYPSASGANMANPQFNRDAVNALNAAEELAGELGDEYVSTEILL 112
Cdd:COG0464 12 ALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 113 IGVATGQSEAATVLQSAGATAEALKGALTSVRGSRKVTTENPEEQYQALEKYATDLTARAREGKIDPVIGRD---AEIRR 189
Cdd:COG0464 92 LLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEevkEELRE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 190 VVQVLSRRTKNNP----------VLIGEPGVGKTAIVEGLARRIvagdvpeslkGKTLMSLDLGSMVagAKYRGEFEERL 259
Cdd:COG0464 172 LVALPLKRPELREeyglppprglLLYGPPGTGKTLLARALAGEL----------GLPLIEVDLSDLV--SKYVGETEKNL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 260 KAVLDEIKESDGQIItFIDEIHTIVGA-GATGDGSMDA--GNMIKPM-LARGELRLVGATtldeYRKyIEKDAALERRFQ 335
Cdd:COG0464 240 REVFDKARGLAPCVL-FIDEADALAGKrGEVGDGVGRRvvNTLLTEMeELRSDVVVIAAT----NRP-DLLDPALLRRFD 313
|
330 340 350
....*....|....*....|....*....|....
gi 1092600816 336 -QVFVGEPSVEDAIGILRGLKERYEVHHGVRIQD 368
Cdd:COG0464 314 eIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEE 347
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
411-833 |
1.89e-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: 60.70 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 411 EEIDSAERIVRRLEIEEMALEKETDIASKERLDKLREELADEREKLNALKTRWQNEKSSIDDVRSVREELDALRTESEKA 490
Cdd:COG0464 3 ELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 491 EREGDYGRVAELRYGRIPELEKKLEAAEESVADAEENSMLKEEVTPQEVAEVVSAWTGIPAGKMmqgETEKLLEMELNlg 570
Cdd:COG0464 83 AALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEE---ELLELREAILD-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 571 rRVVGQNAAVEAVSDAV--------RRSRAGVadpnRPTGSFLFLGPTGVGKTELAKALAEFLfddERAMVRIDMSEyge 642
Cdd:COG0464 158 -DLGGLEEVKEELRELValplkrpeLREEYGL----PPPRGLLLYGPPGTGKTLLARALAGEL---GLPLIEVDLSD--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 643 khsvarLIGappGYVGyDAGGQLTEAV---RRRPYTVVLFDEVEKAHPD-----------VFDVLLQVLDEGRltdgqgr 708
Cdd:COG0464 227 ------LVS---KYVG-ETEKNLREVFdkaRGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 709 tvdfRNTILILTSNlgaggtHEQIMDavkmafkPEFINRLDDVVIFDPLTSEQLRGIVDIqvrnlaeRLEARRLVLDVSD 788
Cdd:COG0464 290 ----SDVVVIAATN------RPDLLD-------PALLRRFDEIIFFPLPDAEERLEIFRI-------HLRKRPLDEDVDL 345
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1092600816 789 EALDWLSErGYDPAYgarpLRRLVQKAIgdELARRLLAGDVRDGD 833
Cdd:COG0464 346 EELAEATE-GLSGAD----IRNVVRRAA--LQALRLGREPVTTED 383
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
123-376 |
1.90e-08 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 56.94 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 123 ATVLQSAGATAEALKGALTSVRGSRKVTTENPEEQYQALEKYATDLTARAREGKIDP-------------VIGRDAEIRR 189
Cdd:COG1222 10 NIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTavpaespdvtfddIGGLDEQIEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 190 VVQVLSRRTKNN---------PV----LIGEPGVGKTaivegLARRIVAGDVpeslkGKTLMSLDLGSMVagAKYRGEFE 256
Cdd:COG1222 90 IREAVELPLKNPelfrkygiePPkgvlLYGPPGTGKT-----LLAKAVAGEL-----GAPFIRVRGSELV--SKYIGEGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 257 ERLKAVLDEIKESDGQIItFIDEIHTIvGAGATGDGSMDAGNMIKPML--------ARGELRLVGATTldeyrkYIEK-D 327
Cdd:COG1222 158 RNVREVFELAREKAPSII-FIDEIDAI-AARRTDDGTSGEVQRTVNQLlaeldgfeSRGDVLIIAATN------RPDLlD 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1092600816 328 AALER--RF-QQVFVGEPSVEDAIGILRGLKERYEVHHGVriqDSALVAAAT 376
Cdd:COG1222 230 PALLRpgRFdRVIEVPLPDEEAREEILKIHLRDMPLADDV---DLDKLAKLT 278
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
198-339 |
4.12e-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: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 198 TKNNPVLIGEPGVGKTAIVEGLAR-------RIVAGDVPESLKGktLMSLDLGSMVAGAKYRGEFEERLKAVLDEIKESD 270
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARelgppggGVIYIDGEDILEE--VLDQLLLIIVGGKKASGSGELRLRLALALARKLK 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 271 GQIItFIDEIHTIVGAGATGDG-SMDAGNMIKPMLARGELRLVGATTLDEyrkyIEKDAALERRFQQVFV 339
Cdd:smart00382 79 PDVL-ILDEITSLLDAEQEALLlLLEELRLLLLLKSEKNLTVILTTNDEK----DLGPALLRRRFDRRIV 143
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
573-816 |
5.95e-07 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 51.42 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 573 VVGQNAAVEAVSDAVR-------RSRAGVADPNRptgsFLFLGPTGVGKTELAKALAeflfddERAMVRIDMSEYGEkhs 645
Cdd:COG1223 4 VVGQEEAKKKLKLIIKelrrrenLRKFGLWPPRK----ILFYGPPGTGKTMLAEALA------GELKLPLLTVRLDS--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 646 varLIGAppgYVGyDAGGQLT---EAVRRRPyTVVLFDEVE---------KAHPD---VFDVLLQVLDEGRltdgqgrtv 710
Cdd:COG1223 71 ---LIGS---YLG-ETARNLRklfDFARRAP-CVIFFDEFDaiakdrgdqNDVGEvkrVVNALLQELDGLP--------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 711 dfRNTILILTSNlgaggtHEQIMDavkmafkPEFINRLDDVVIFDPLTSEQLRGIvdiqvrnLAERLEARRLVLDVSDEA 790
Cdd:COG1223 134 --SGSVVIAATN------HPELLD-------SALWRRFDEVIEFPLPDKEERKEI-------LELNLKKFPLPFELDLKK 191
|
250 260
....*....|....*....|....*.
gi 1092600816 791 LDWLSErGYDPAYGARPLRRLVQKAI 816
Cdd:COG1223 192 LAKKLE-GLSGADIEKVLKTALKKAI 216
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
94-145 |
7.01e-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: 46.75 E-value: 7.01e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1092600816 94 AEELAGELGDEYVSTEILLIGVAT-GQSEAATVLQSAGATAEALKGALTSVRG 145
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEeDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
185-283 |
9.58e-07 |
|
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: 49.59 E-value: 9.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 185 AEIRRVVQVLSRRTKNNPV---------LIGEPGVGKTAIVEGLARRIvagdvpeslkGKTLMSLDLGSMVagAKYRGEF 255
Cdd:cd19481 3 ASLREAVEAPRRGSRLRRYglglpkgilLYGPPGTGKTLLAKALAGEL----------GLPLIVVKLSSLL--SKYVGES 70
|
90 100
....*....|....*....|....*...
gi 1092600816 256 EERLKAVLDEIKESDGQIItFIDEIHTI 283
Cdd:cd19481 71 EKNLRKIFERARRLAPCIL-FIDEIDAI 97
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
16-68 |
3.24e-06 |
|
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: 44.82 E-value: 3.24e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1092600816 16 AMKAATSAGNPDIRPGHILVALLEQKEGIAAPLLEAAGVNPSGVLTRAKELVA 68
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
605-722 |
6.01e-06 |
|
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: 46.43 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 605 LFLGPTGVGKTELAKALAEFLFddeRAMVRIDMSEYGEKHsvarlIGAPPGYVgydagGQLTEAVRRRPYTVVLFDEVEK 684
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELG---APFIEISGSELVSKY-----VGESEKRL-----RELFEAAKKLAPCVIFIDEIDA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1092600816 685 AHP-----------DVFDVLLQVLDegrltdgqGRTVDFRNTILILTSN 722
Cdd:pfam00004 69 LAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
203-334 |
7.11e-06 |
|
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: 46.52 E-value: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 203 VLIGEPGVGKTAIVEGLARRIVAGDV----------PESLKGKTLMSLDLGSMVAGAKYRgEFEERLKAVLDEIKESDGQ 272
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSNRPVfyvqltrdttEEDLFGRRNIDPGGASWVDGPLVR-AAREGEIAVLDEINRANPD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092600816 273 II----TFIDEIHTIVGAGATgdgsmdagnmikPMLARGELRLVGATTLDEYRKYIEKDAALERRF 334
Cdd:pfam07728 82 VLnsllSLLDERRLLLPDGGE------------LVKAAPDGFRLIATMNPLDRGLNELSPALRSRF 135
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
401-552 |
1.54e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 401 RLRMEIDSSPEEIDSAERIVRRLEIEEMALEKETDIASK-ERLDKLREELADEREKLNALKTRWQNEKSSIDDVRSVREE 479
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyQELEALEAELAELPERLEELEERLEELRELEEELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 480 LDALRTESEKAEREGDYGRVAELRY---------GRIPELEKKLEAAEESVADAEEN-SMLKEEVTPQEVAEVVSAWTGI 549
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEELQDlaeeleelqQRLAELEEELEEAQEELEELEEElEQLENELEAAALEERLKEARLL 251
|
...
gi 1092600816 550 PAG 552
Cdd:COG4717 252 LLI 254
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
598-725 |
2.53e-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: 45.28 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 598 NRPTGSFLFLGPTGVGKTELAKALAEFLFDDERamvriDMSEYGEKHSVARLI--GAPPGYVGYDAGGQ---------LT 666
Cdd:pfam13177 16 GRLSHAYLFSGPEGVGKLELALAFAKALFCEEP-----GDDLPCGQCRSCRRIesGNHPDLVIIEPEGQsikidqireLQ 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092600816 667 EAVRRRPYT----VVLFDEVEKAHPDVFDVLLQVLDEgrltdGQGRTVdfrntILILTSNLGA 725
Cdd:pfam13177 91 KEFSKSPYEgkkkVYIIEDAEKMTASAANSLLKFLEE-----PPGNTV-----IILLTENPSR 143
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
204-315 |
5.28e-05 |
|
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: 44.59 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 204 LIGEPGVGKTAIVEGLARriVAGDVPESLKGKTLMSldlgsmvagaKYRGEFEERLKAVLDEIKESDGQIItFIDEIHTI 283
Cdd:cd19503 39 LHGPPGTGKTLLARAVAN--EAGANFLSISGPSIVS----------KYLGESEKNLREIFEEARSHAPSII-FIDEIDAL 105
|
90 100 110
....*....|....*....|....*....|....*...
gi 1092600816 284 VGAGATGDGSMDAG------NMIKPMLARGELRLVGAT 315
Cdd:cd19503 106 APKREEDQREVERRvvaqllTLMDGMSSRGKVVVIAAT 143
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
573-626 |
6.06e-05 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 45.95 E-value: 6.06e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1092600816 573 VVGQNAAVEAVSDAVRRsragvadpNRPTGSFLFLGPTGVGKTELAKALAEFLF 626
Cdd:COG2812 12 VVGQEHVVRTLKNALAS--------GRLAHAYLFTGPRGVGKTTLARILAKALN 57
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
564-722 |
9.48e-05 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 45.16 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 564 EMELNLGRRVVGQNAAVEAVSDAVRrsrAGvadpnrptGSFLFLGPTGVGKTELAKALAEFLfddERAMVRI----DMSE 639
Cdd:COG0714 5 RLRAEIGKVYVGQEELIELVLIALL---AG--------GHLLLEGVPGVGKTTLAKALARAL---GLPFIRIqftpDLLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 640 ygekhsvARLIGAppgyvgYDAGGQLTE-AVRRRPY--TVVLFDEVEKAHPDVFDVLLQVLDEGRLTDGqGRTVDFRNT- 715
Cdd:COG0714 71 -------SDILGT------YIYDQQTGEfEFRPGPLfaNVLLADEINRAPPKTQSALLEAMEERQVTIP-GGTYKLPEPf 136
|
....*..
gi 1092600816 716 ILILTSN 722
Cdd:COG0714 137 LVIATQN 143
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
395-526 |
1.20e-04 |
|
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: 44.53 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 395 VDEAASRLRMEIDSSPEEIDSAERIVRRLEIEEMALEKETDIASKErLDKLREELADEREKLNALKTRwqnekssIDDVR 474
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKE-IKRLELEIEEVEARIKKYEEQ-------LGNVR 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1092600816 475 SVReELDALRTESEKAERegdygRVAELRYgRIPELEKKLEAAEESVADAEE 526
Cdd:COG1579 87 NNK-EYEALQKEIESLKR-----RISDLED-EILELMERIEELEEELAELEA 131
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
605-698 |
1.62e-04 |
|
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410908 [Multi-domain] Cd Length: 182 Bit Score: 43.32 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 605 LFLGPTGVGKTELAKALAEFLfddERAMVRIDMseyGEKHSVARLIGAPPGYVGyDAGGQLTEAVRR----RPytVVLFD 680
Cdd:cd19500 41 CLVGPPGVGKTSLGKSIARAL---GRKFVRISL---GGVRDEAEIRGHRRTYVG-AMPGRIIQALKKagtnNP--VFLLD 111
|
90 100
....*....|....*....|..
gi 1092600816 681 EVEK----AHPDVFDVLLQVLD 698
Cdd:cd19500 112 EIDKigssFRGDPASALLEVLD 133
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
400-526 |
1.72e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 400 SRLRMEIDSSPEEIDSAERIVRRLEIEEMALEKEtdiaskerLDKLREELADEREKLNALKTRWQNEKSSIDDVRSVREE 479
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQE--------EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1092600816 480 LDALRTESEKAEREGDygrvAELRYGRIPELEKKLEAAEESVADAEE 526
Cdd:TIGR02169 770 LEEDLHKLEEALNDLE----ARLSHSRIPEIQAELSKLEEEVSRIEA 812
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
576-722 |
1.76e-04 |
|
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
Pssm-ID: 440238 [Multi-domain] Cd Length: 289 Bit Score: 44.58 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 576 QNAAVEAVSDAVRRSRAGVAdpnrptgsFLFLGPTGVGKTELAKALAEFLFDDERAmvriDMSEYGEKHSVARLIGAPPG 655
Cdd:COG0470 1 QEEAWEQLLAAAESGRLPHA--------LLLHGPPGIGKTTLALALARDLLCENPE----GGKACGQCHSRLMAAGNHPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 656 YV-----------GYDAGGQLTEAVRRRPYT----VVLFDEVEKAHPDVFDVLLQVLDEGRltdgqgrtvdfRNTILILT 720
Cdd:COG0470 69 LLelnpeeksdqiGIDQIRELGEFLSLTPLEggrkVVIIDEADAMNEAAANALLKTLEEPP-----------KNTPFILI 137
|
..
gi 1092600816 721 SN 722
Cdd:COG0470 138 AN 139
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
203-447 |
1.81e-04 |
|
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.
Pssm-ID: 273521 [Multi-domain] Cd Length: 733 Bit Score: 45.28 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 203 VLIGEPGVGKTAIVEGLARRIVAGDVpeSLKGKTLMSldlgsmvagaKYRGEFEERLKAVLDEIKESDGQIItFIDEIHT 282
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANEAGAYFI--SINGPEIMS----------KYYGESEERLREIFKEAEENAPSII-FIDEIDA 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 283 IVGAGATGDGSMDAG------NMIKPMLARGELRLVGATTLDEyrkyiEKDAALER--RF-QQVFVGEPSVEDAIGILR- 352
Cdd:TIGR01243 283 IAPKREEVTGEVEKRvvaqllTLMDGLKGRGRVIVIGATNRPD-----ALDPALRRpgRFdREIVIRVPDKRARKEILKv 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 353 -----------GLKERYEVHHGVRIQDsaLVAAATLSDRYITSRFLPDKAIDL-VDEAASRLRMEIDSSPEEIDSAERIV 420
Cdd:TIGR01243 358 htrnmplaedvDLDKLAEVTHGFVGAD--LAALAKEAAMAALRRFIREGKINFeAEEIPAEVLKELKVTMKDFMEALKMV 435
|
250 260 270
....*....|....*....|....*....|..
gi 1092600816 421 RRLEIEEMALE----KETDIASKERLDK-LRE 447
Cdd:TIGR01243 436 EPSAIREVLVEvpnvRWSDIGGLEEVKQeLRE 467
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
344-526 |
1.87e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 344 VEDA---IGILRGLKERYEVHHGVRIQDSALVAAATLSDRYITSRflpdkAIDLVDEAASRLRMEIDSSPEEIDSAERIV 420
Cdd:COG4913 244 LEDAreqIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR-----RLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 421 RRLEIEEMALEKETDIASKERLDKLREELADEREKLNALKTRWQNEKSSIDDVR----SVREELDALRTE--SEKAEREG 494
Cdd:COG4913 319 DALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEaaALLEALEE 398
|
170 180 190
....*....|....*....|....*....|..
gi 1092600816 495 DYGRVAELRYgripELEKKLEAAEESVADAEE 526
Cdd:COG4913 399 ELEALEEALA----EAEAALRDLRRELRELEA 426
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
179-228 |
1.95e-04 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 42.88 E-value: 1.95e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1092600816 179 PVIGRDAEIRRVVQVLSRRTKNNP---VLIGEPGVGKTAIVEGLARRIVAGDV 228
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERDGG 53
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
599-690 |
2.15e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 41.94 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 599 RPTGSFLFL-GPTGVGKTELAKALAEFLFDDERAMVRIDMSEYGEK----HSVARLIGAPPGYVG--YDAGGQLTEAVRR 671
Cdd:pfam13401 2 RFGAGILVLtGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPkdllRALLRALGLPLSGRLskEELLAALQQLLLA 81
|
90 100
....*....|....*....|
gi 1092600816 672 RPYTVVL-FDEVEKAHPDVF 690
Cdd:pfam13401 82 LAVAVVLiIDEAQHLSLEAL 101
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
393-526 |
2.19e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 393 DLVDEAASRLRMEIDSSPEEIdsAERIVR-RLEIEEMALEKETdiaSKERLDKLREELADEREKLNALKTRWQNEKSSID 471
Cdd:PRK02224 306 DADAEAVEARREELEDRDEEL--RDRLEEcRVAAQAHNEEAES---LREDADDLEERAEELREEAAELESELEEAREAVE 380
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092600816 472 DVRSVREELDALRTESEKA------EREGDYGRVAELR------YGRIPELEKKLEAAEESVADAEE 526
Cdd:PRK02224 381 DRREEIEELEEEIEELRERfgdapvDLGNAEDFLEELReerdelREREAELEATLRTARERVEEAEA 447
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
569-684 |
2.67e-04 |
|
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: 42.75 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 569 LGRRVVGQNAAVEAVSDAVR----RSR--AGVADPNRPTgSFLFLGPTGVGKTELAKALAEFLfddERAMVRIDMSEYGE 642
Cdd:cd19498 9 LDKYIIGQDEAKRAVAIALRnrwrRMQlpEELRDEVTPK-NILMIGPTGVGKTEIARRLAKLA---GAPFIKVEATKFTE 84
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1092600816 643 KhsvarligappGYVGYDaggqLTEAVRRRPYTVVLFDEVEK 684
Cdd:cd19498 85 V-----------GYVGRD----VESIIRDLVEGIVFIDEIDK 111
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
405-527 |
3.99e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 405 EIDSSPEEIDSAERIVRRLEIEEMALEKETDiASKERLDKLREELADEREKLNALKTRWQNEKSSIDDVRSVREELdaLR 484
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEERKRRDKLTEEYA-ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL--KR 406
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1092600816 485 TESEKAER-EGDYGRVAELR------YGRIPELEKKLEAAEESVADAEEN 527
Cdd:TIGR02169 407 ELDRLQEElQRLSEELADLNaaiagiEAKINELEEEKEDKALEIKKQEWK 456
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
393-533 |
6.05e-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: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 393 DLVDEAASRLRMEIDSSPEEIDSAERIVR-RLEIEEMALEKETdiaSKERLDKLREELADEREKLNALKTRWQNEKSSID 471
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEElEAQIEQLKEELKA---LREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092600816 472 DVRSVREELDAlRTESEKAEREGDYGRVAELRYgRIPELEKKLEAAEESVADAEENSMLKEE 533
Cdd:TIGR02168 835 ATERRLEDLEE-QIEELSEDIESLAAEIEELEE-LIEELESELEALLNERASLEEALALLRS 894
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
401-543 |
6.58e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 401 RLRMEIDSSPEEIDSAERIVRRLEIEEMALEKETDIASKERLD----KLREELADEREKLNALKTRWQNEKSSIDDVRSV 476
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELReeylELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092600816 477 REELDALRTESEKAEREGDygRVAELRyGRIPELekKLEAAEESVADAEE-NSMLKEEVTPQEVAEVV 543
Cdd:PRK03918 703 LEEREKAKKELEKLEKALE--RVEELR-EKVKKY--KALLKERALSKVGEiASEIFEELTEGKYSGVR 765
|
|
| PRK14970 |
PRK14970 |
DNA polymerase III subunits gamma and tau; Provisional |
573-699 |
1.07e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184934 [Multi-domain] Cd Length: 367 Bit Score: 42.17 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 573 VVGQNAAVEAVSDAVRRsragvadpNRPTGSFLFLGPTGVGKTELAKALAEFLfdDERAmvrIDMSEYGEKHSVARLIGA 652
Cdd:PRK14970 19 VVGQSHITNTLLNAIEN--------NHLAQALLFCGPRGVGKTTCARILARKI--NQPG---YDDPNEDFSFNIFELDAA 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1092600816 653 PPGYVgyDAGGQLTEAVRRRP----YTVVLFDEVEKAHPDVFDVLLQVLDE 699
Cdd:PRK14970 86 SNNSV--DDIRNLIDQVRIPPqtgkYKIYIIDEVHMLSSAAFNAFLKTLEE 134
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
403-526 |
1.20e-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: 42.74 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 403 RMEIDSSPEEIDSAERIVRRLEIEEMALEKETDiASKERLDKLREELADEREKLNALKTRWQNEKSSIDDVRSVREELDA 482
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1092600816 483 LRTESEkAEREGDYGRVAELRyGRIPELEKKLEAAEESVADAEE 526
Cdd:TIGR02168 755 ELTELE-AEIEELEERLEEAE-EELAEAEAEIEELEAQIEQLKE 796
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
203-336 |
1.24e-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: 40.41 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 203 VLIGEPGVGKTAIVEGLARRIvagdvpeslkGKTLMSLDLGSMVagAKYRGEFEERLKAVLDEIKESDGQIItFIDEIHT 282
Cdd:cd19509 36 LLYGPPGTGKTLLARAVASES----------GSTFFSISASSLV--SKWVGESEKIVRALFALARELQPSII-FIDEIDS 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092600816 283 IVgaGATGDGSMDAGNMIKPMLArgeLRLVGATTLDEYRKYI--------EKDAALERRFQQ 336
Cdd:cd19509 103 LL--SERGSGEHEASRRVKTEFL---VQMDGVLNKPEDRVLVlgatnrpwELDEAFLRRFEK 159
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
424-544 |
1.27e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 424 EIEEMALEKETDiASKERLDKLREELADEREKLNALKTrwqnekssidDVRSVREELDALRtESEKAEREgdygRVAELR 503
Cdd:PRK04778 83 DIEEQLFEAEEL-NDKFRFRKAKHEINEIESLLDLIEE----------DIEQILEELQELL-ESEEKNRE----EVEQLK 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092600816 504 ----------------YGR-IPELEKKLEAAEESVADAEEnsmLKEEVTPQEVAEVVS 544
Cdd:PRK04778 147 dlyrelrksllanrfsFGPaLDELEKQLENLEEEFSQFVE---LTESGDYVEAREILD 201
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
196-336 |
1.29e-03 |
|
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: 40.35 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 196 RRTKNNPVLIGEPGVGKTAIVEGLARRIvagdvpeslkGKTLMSLDLGSMVagAKYRGEfEERLKAVLDEIKESDGQIIT 275
Cdd:cd19522 30 RRPWKGVLMVGPPGTGKTLLAKAVATEC----------GTTFFNVSSSTLT--SKYRGE-SEKLVRLLFEMARFYAPTTI 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092600816 276 FIDEIHTIVGAGATGDgSMDAGNMIKPMLARGELRLVGATTLDEYRKYI----------EKDAALERRFQQ 336
Cdd:cd19522 97 FIDEIDSICSRRGTSE-EHEASRRVKSELLVQMDGVGGASENDDPSKMVmvlaatnfpwDIDEALRRRLEK 166
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
389-526 |
1.32e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 389 DKAIDLVDEAASRLRMEIDSSPEEID--SAERIVRRLEIEEMALEKETDI--ASKERLDKLREELADEREKLNALKTRWQ 464
Cdd:COG4913 637 EAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAELERLDASSDDlaALEEQLEELEAELEELEEELDELKGEIG 716
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092600816 465 NEKSSIDDVRSVREELDALRTESEKAEREGDYGRVAELRYGRIPE---------LEKKLEAAEESVADAEE 526
Cdd:COG4913 717 RLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDaverelrenLEERIDALRARLNRAEE 787
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
396-538 |
1.54e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 396 DEAASRLRMEIDSSPEEIDSAERIvrRLEIEEMALEKEtDIASKERLDK-----LREELADEREKLNALKtRWQNEKSSI 470
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEEL--KKAEEENKIKAA-EEAKKAEEDKkkaeeAKKAEEDEKKAAEALK-KEAEEAKKA 1704
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092600816 471 DDVRSVREElDALRTESEKAEREGDYGRVAELRygRIPELEKKleAAEESVADAEENSMLKEEVTPQE 538
Cdd:PTZ00121 1705 EELKKKEAE-EKKKAEELKKAEEENKIKAEEAK--KEAEEDKK--KAEEAKKDEEEKKKIAHLKKEEE 1767
|
|
| RecA-like_CDC48_r1-like |
cd19519 |
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ... |
203-283 |
1.88e-03 |
|
first of two ATPase domains of CDC48 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. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like 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: 410927 [Multi-domain] Cd Length: 166 Bit Score: 40.11 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 203 VLIGEPGVGKTAIVEGLARRIVAGDVPesLKGKTLMSldlgsmvagaKYRGEFEERLKAVLDEIKESDGQIItFIDEIHT 282
Cdd:cd19519 38 LLYGPPGTGKTLIARAVANETGAFFFL--INGPEIMS----------KLAGESESNLRKAFEEAEKNAPAII-FIDEIDA 104
|
.
gi 1092600816 283 I 283
Cdd:cd19519 105 I 105
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
600-736 |
1.97e-03 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 40.67 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 600 PTGSF-LFLGPTGVGKTELA-----KALAE------FLFDDERAMVRIDMSEYG------EKHSVARLIGAPPGYVGYDA 661
Cdd:COG0467 18 PRGSStLLSGPPGTGKTTLAlqflaEGLRRgekglyVSFEESPEQLLRRAESLGldleeyIESGLLRIIDLSPEELGLDL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 662 GG---QLTEAVRRRPYTVVLFD---EVEKAHPDVFDVLLQVLdegRLTdgqgRTVDFRNTILILTSNLGAGGTH------ 729
Cdd:COG0467 98 EEllaRLREAVEEFGAKRVVIDslsGLLLALPDPERLREFLH---RLL----RYLKKRGVTTLLTSETGGLEDEateggl 170
|
....*..
gi 1092600816 730 EQIMDAV 736
Cdd:COG0467 171 SYLADGV 177
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
196-281 |
2.09e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 39.25 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 196 RRTKNNPVLIGEPGVGKTAIVEGLARRIVAG-------DVPESLKGKTLMSLDLGSMVAGAKYRGEFEERLKAVLDEIKE 268
Cdd:pfam13401 2 RFGAGILVLTGESGTGKTTLLRRLLEQLPEVrdsvvfvDLPSGTSPKDLLRALLRALGLPLSGRLSKEELLAALQQLLLA 81
|
90
....*....|...
gi 1092600816 269 SDGQIITFIDEIH 281
Cdd:pfam13401 82 LAVAVVLIIDEAQ 94
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
166-221 |
2.15e-03 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 40.92 E-value: 2.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092600816 166 TDLTARAREGKIdpVIGRDAEIRRV-VQVLSRRtknnPVLI-GEPGVGKTAIVEGLAR 221
Cdd:COG0714 2 TEARLRAEIGKV--YVGQEELIELVlIALLAGG----HLLLeGVPGVGKTTLAKALAR 53
|
|
| RecA-like_Figl-1 |
cd19525 |
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ... |
203-336 |
2.34e-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: 39.97 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 203 VLIGEPGVGKTAIveglarrivaGDVPESLKGKTLMSLDLGSMVagAKYRGEFEERLKAVLDEIKESDGQIItFIDEIHT 282
Cdd:cd19525 59 LLFGPPGTGKTLI----------GKCIASQSGATFFSISASSLT--SKWVGEGEKMVRALFSVARCKQPAVI-FIDEIDS 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092600816 283 IVgaGATGDGSMDAGNMIKPMLArgeLRLVGATTLDEYRKYI--------EKDAALERRFQQ 336
Cdd:cd19525 126 LL--SQRGEGEHESSRRIKTEFL---VQLDGATTSSEDRILVvgatnrpqEIDEAARRRLVK 182
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
412-491 |
2.76e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 412 EIDSAERIVRRLEIEEMALEketdiaskERLDKLREELADEREKLNALKTRWQNEKSSIDD-VRSVREELDALRTESEKA 490
Cdd:COG1579 97 EIESLKRRISDLEDEILELM--------ERIEELEEELAELEAELAELEAELEEKKAELDEeLAELEAELEELEAEREEL 168
|
.
gi 1092600816 491 E 491
Cdd:COG1579 169 A 169
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
429-622 |
3.12e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 41.03 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 429 ALEKETDIASKERLDKLREELADEREKLNALKTRWQNEKSSIDDVRSVREELDALRTESEKAERegdygrvaelrygriP 508
Cdd:PRK05703 50 AVDEDETPKKNPVLREEKRKPAKSILSLQALLEKRPSRTNSQDALLQAENALPEWKKELEKPSE---------------P 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 509 ELEKKLEAAEESVADAEENSMLKE-----EVTPQEVAEVVSAWTGIPAGKMMQgetEKLLEMELN------LGRRV---- 573
Cdd:PRK05703 115 KEEEPKAAAESKVVQKELDELRDElkelkNLLEDQLSGLRQVERIPPEFAELY---KRLKRSGLSpeiaekLLKLLlehm 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1092600816 574 -VGQNAAVEAVSDAVRRS-RAGVADPNRPTGSFLFLGPTGVGK-TELAKaLA 622
Cdd:PRK05703 192 pPRERTAWRYLLELLANMiPVRVEDILKQGGVVALVGPTGVGKtTTLAK-LA 242
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
573-625 |
3.65e-03 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410905 [Multi-domain] Cd Length: 251 Bit Score: 39.89 E-value: 3.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092600816 573 VVGQNAAVEAVSDAV----RRSRAGVADPNRPT----GSFLFLGPTGVGKTELAKALAEFL 625
Cdd:cd19497 14 VIGQERAKKVLSVAVynhyKRIRNNLKQKDDDVelekSNILLIGPTGSGKTLLAQTLAKIL 74
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
400-530 |
4.07e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 38.39 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 400 SRLRMEIDSSPEEIDSAERIVRRLEIEemaLEKETDIAsKERLDKLREEL---ADEREKLNALKTRWQNEKSSIDDVRSV 476
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEAQLQKLQED---LEKQAEIA-REAQQNYERELvlhAEDIKALQALREELNELKAEIAELKAE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092600816 477 REELDALRTESEK--AEREGdygrvaelrygripELEKKLEAAEESVADAEE-NSML 530
Cdd:pfam07926 80 AESAKAELEESEEswEEQKK--------------ELEKELSELEKRIEDLNEqNKLL 122
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
298-515 |
4.23e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 298 NMIKPMLARGELRLVGATTL-DEYRKYIEKDAALERRFQQVFVGEPSVEDAIGILRGLKERYEvhhGVRIQDSALVAAAT 376
Cdd:TIGR00606 587 NQTRDRLAKLNKELASLEQNkNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIE---KSSKQRAMLAGATA 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 377 LSDRYITSrfLPDKAIDL-------------VDEAASRLRMEIDSSPEEIDSAERIVRRLEIEEMALEKETDIASKErLD 443
Cdd:TIGR00606 664 VYSQFITQ--LTDENQSCcpvcqrvfqteaeLQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSI-ID 740
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092600816 444 KLREELADEREKLNALKTRWQNEKSSIDDVRSvreELDALRTESEKAEREGDYGRVAELRYGRIPELEKKLE 515
Cdd:TIGR00606 741 LKEKEIPELRNKLQKVNRDIQRLKNDIEEQET---LLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIA 809
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
420-533 |
4.85e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.73 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 420 VRRLEIEEMALEKETDIASKERLDKLREELADEREKLNALKTRWQNEKssiddvRSVREELDALRTESEKAEREGDYGRV 499
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQEL------KLKEQAKKALEYYQLKEKLELEEEYL 226
|
90 100 110
....*....|....*....|....*....|....*...
gi 1092600816 500 AELRY----GRIPELEKKLEAAEESVADAEENSMLKEE 533
Cdd:pfam02463 227 LYLDYlklnEERIDLLQELLRDEQEEIESSKQEIEKEE 264
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
253-533 |
5.35e-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: 40.44 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 253 GEFEERLKAVLDEIKE-SDGQIITFIDEIHTIVGAGATGDGSMDAGNMIKPMLARGElrlvgATTLDEYRKYIEKDAALE 331
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL-----AKLEAEIDKLLAEIEELE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 332 RRFQQVFVGEPSVEDAIgilRGLKERYEVHHgVRIQDSALVAAATlsdryitsrflpdkaidlVDEAASRlRMEIDSSPE 411
Cdd:TIGR02169 343 REIEEERKRRDKLTEEY---AELKEELEDLR-AELEEVDKEFAET------------------RDELKDY-REKLEKLKR 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 412 EIDSAERIVRRLEIEEMALEketdiaskERLDKLREELADEREKLNALKTRW-----------QNEKSSIDDVRSVREEL 480
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLS--------EELADLNAAIAGIEAKINELEEEKedkaleikkqeWKLEQLAADLSKYEQEL 471
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1092600816 481 DALRTESEKAEREgdygrVAELRYgRIPELEKKLEAAEESVADAEENSMLKEE 533
Cdd:TIGR02169 472 YDLKEEYDRVEKE-----LSKLQR-ELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
421-533 |
6.21e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 421 RRLEIEEMALEKEtdiASKERLDKLREELADEREKLNALKTRWQNEKSSIDDVRSVREELDALRTESEKAEREGDyGRVA 500
Cdd:COG1196 223 KELEAELLLLKLR---ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL-AELA 298
|
90 100 110
....*....|....*....|....*....|...
gi 1092600816 501 ELRYGRIPELEKKLEAAEESVADAEENSMLKEE 533
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
|
| CDC6 |
COG1474 |
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]; |
572-841 |
6.55e-03 |
|
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
Pssm-ID: 441083 [Multi-domain] Cd Length: 389 Bit Score: 39.83 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 572 RVVGQNAAVEAVSDAVRrsraGVADPNRPTGSFLFlGPTGVGKTELAKALAEFL------FDDERAMVRIDMSEYGEKHS 645
Cdd:COG1474 27 RLPHREEEIEELASALR----PALRGERPSNVLIY-GPTGTGKTAVAKYVLEELeeeaeeRGVDVRVVYVNCRQASTRYR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 646 VARLI------GAPPGYVGYDAG---GQLTEAVRRRPYTVVL-FDEV----EKAHPDVFDVLLQVLDEgrltdgqgrtVD 711
Cdd:COG1474 102 VLSRIleelgsGEDIPSTGLSTDelfDRLYEALDERDGVLVVvLDEIdylvDDEGDDLLYQLLRANEE----------LE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 712 FRNTILILTSNlgaggtheqimdavkmafKPEFINRLDD---------VVIFDPLTSEQLRGIvdiqvrnlaerLEARR- 781
Cdd:COG1474 172 GARVGVIGISN------------------DLEFLENLDPrvksslgeeEIVFPPYDADELRDI-----------LEDRAe 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092600816 782 --LVLDV-SDEALDWLSERGYDPAYGARplrrlvqKAIgdELARRllAGDV--RDGDRvEVTVAD 841
Cdd:COG1474 223 laFYDGVlSDEVIPLIAALAAQEHGDAR-------KAI--DLLRV--AGEIaeREGSD-RVTEEH 275
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
390-532 |
7.24e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 390 KAIDLVDEAASRLRMEIDSSPEEIDSAERIVRRLEIEEMALEKETDIASK-------------ERLDKLREELADEREKL 456
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgdapvdlgnaeDFLEELREERDELRERE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 457 NALKTRWQNEKssiDDVRSVREELDALR--------TESEKAEREGDY-GRVAELRYGR------IPELEKKLEAAEESV 521
Cdd:PRK02224 429 AELEATLRTAR---ERVEEAEALLEAGKcpecgqpvEGSPHVETIEEDrERVEELEAELedleeeVEEVEERLERAEDLV 505
|
170
....*....|.
gi 1092600816 522 ADAEENSMLKE 532
Cdd:PRK02224 506 EAEDRIERLEE 516
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
402-586 |
7.37e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 402 LRMEIDSSPEEIDSAERIVRRL-EIEEMALEKETdiaSKERLDKLREELADEREKLNALKTRWQNEKSSIDDVRSVREEL 480
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKELkELKEKAEEYIK---LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 481 DALRTESEKAERegdygrvaelrygRIPELEKKLEAAEESVADAEENSMLKEEVTPQEVAEVVSAWTGIP-AGKMMQGET 559
Cdd:PRK03918 341 EELKKKLKELEK-------------RLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEkAKEEIEEEI 407
|
170 180
....*....|....*....|....*..
gi 1092600816 560 EKLLEMELNLGRRVVGQNAAVEAVSDA 586
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKA 434
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
401-541 |
7.45e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 401 RLRMEIDSSPEEIDSAERIVRRleIEEMALEKETDIASKERLDKLREELADEREKLNALKTRWQNEKSSI-DDVRSVREE 479
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRER--LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLeQEEEKLKER 738
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092600816 480 LDALRT--ESEKAEREGDYGRVAELRyGRIPELEKKLEAAEESVADAEEnsMLKEEVTPQEVAE 541
Cdd:TIGR02169 739 LEELEEdlSSLEQEIENVKSELKELE-ARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAE 799
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
405-533 |
8.44e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 405 EIDSSPEEIDSAERIVRRL-----------------------------------EIEEMALEKETDIASKER-LDKLREE 448
Cdd:PRK03918 136 EIDAILESDESREKVVRQIlglddyenayknlgevikeikrrierlekfikrteNIEELIKEKEKELEEVLReINEISSE 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600816 449 LADEREKLNALKTRWQnekssidDVRSVREELDALRTESEKaeREGDYGRVAELRYG---RIPELEKKLEAAEESVADAE 525
Cdd:PRK03918 216 LPELREELEKLEKEVK-------ELEELKEEIEELEKELES--LEGSKRKLEEKIREleeRIEELKKEIEELEEKVKELK 286
|
....*...
gi 1092600816 526 ENSMLKEE 533
Cdd:PRK03918 287 ELKEKAEE 294
|
|
| PRK07399 |
PRK07399 |
DNA polymerase III subunit delta'; Validated |
568-635 |
9.97e-03 |
|
DNA polymerase III subunit delta'; Validated
Pssm-ID: 236011 [Multi-domain] Cd Length: 314 Bit Score: 39.11 E-value: 9.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092600816 568 NLGRRVVGQNAAVEAVSDAVRRsragvadpNRPTGSFLFLGPTGVGKTELAKALAEFLFDDERAMVRI 635
Cdd:PRK07399 1 NLFANLIGQPLAIELLTAAIKQ--------NRIAPAYLFAGPEGVGRKLAALCFIEGLLSQGSPSKNI 60
|
|
| |
