|
Name |
Accession |
Description |
Interval |
E-value |
| mutL |
PRK00095 |
DNA mismatch repair endonuclease MutL; |
3-668 |
0e+00 |
|
DNA mismatch repair endonuclease MutL;
Pssm-ID: 234630 [Multi-domain] Cd Length: 617 Bit Score: 823.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 3 KIKELQTSLANKIAAGEVVERPSSVVKELLENAIDAGATEISIEVEESGVQSIRVVDNGSGIEAEDLGLVFHRHATSKLD 82
Cdd:PRK00095 2 PIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 83 QDEDLFHIRTLGFRGEALASISSVAKVTLKTCTDNAN-GNEIYVENGEILNHKPAKAKKGTDILVESLFYNTPARLKYIK 161
Cdd:PRK00095 82 SLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAeGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKFLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 162 SLYTELGKITDIVNRMAMSHPDIRIALISDGKTMLSTNGSGRTNEVMAEIYGMKVARDLVHISGDTSDYHIEGFVAKPEH 241
Cdd:PRK00095 162 SEKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPTL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 242 SRSNKHYISIFINGRYIKNFMLNKAILEGYHTLLTIGRFPICYINIEMDPILVDVNVHPTKLEVRLSKEEQLYQLIVSKI 321
Cdd:PRK00095 242 SRANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDLIVQAI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 322 QEAFKDRILIPKnnldyVPKKNKVLHSFEQQKIEFEQRQNTENNQEKTFSSEESNSKPFMEENQNDEIVIKEDSYNPFVT 401
Cdd:PRK00095 322 QEALAQSGLIPA-----AAGANQVLEPAEPEPLPLQQTPLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 402 KTSESLIADDESSGYNNTREKDEDyfkkqqeilqemdqtfdsndgttvqnyenkasddyydvndikgtkSKDPKRRIPYM 481
Cdd:PRK00095 397 SEAAAAASAEAAAAAPAAAPEPAE---------------------------------------------AAEEADSFPLG 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 482 EIVGQVHGTYIIAQNEFGMYMIDQHAAQERIKYEYFRDKIGEVTNEVQDLLIPLTFHFSKDEQLVIDQYKNELQQVGIML 561
Cdd:PRK00095 432 YALGQLHGTYILAENEDGLYLVDQHAAHERLLYEQLKDKLAEVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLEL 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 562 EHFGGHDYIVSSYPVWFPKDEVEEIIKDMIELILEEKKVDIKKLREdVAIMMSCKKSIKANHYLQKHEMSDLIDQLREAE 641
Cdd:PRK00095 512 EPFGPNSFAVREVPALLGQQELEELIRDLLDELAEEGDSDTLKERE-LLATMACHGAIRAGRRLTLEEMNALLRQLEATE 590
|
650 660
....*....|....*....|....*..
gi 446438406 642 DPFTCPHGRPIIINFSKYELEKLFKRV 668
Cdd:PRK00095 591 NPGTCPHGRPTYIELSLSDLEKLFKRI 617
|
|
| MutL |
COG0323 |
DNA mismatch repair ATPase MutL [Replication, recombination and repair]; |
1-667 |
0e+00 |
|
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
Pssm-ID: 440092 [Multi-domain] Cd Length: 515 Bit Score: 735.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 1 MGKIKELQTSLANKIAAGEVVERPSSVVKELLENAIDAGATEISIEVEESGVQSIRVVDNGSGIEAEDLGLVFHRHATSK 80
Cdd:COG0323 1 MPKIRLLPDELANQIAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLPLAFERHATSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 81 LDQDEDLFHIRTLGFRGEALASISSVAKVTLKTCT-DNANGNEIYVENGEILNHKPAKAKKGTDILVESLFYNTPARLKY 159
Cdd:COG0323 81 IRSAEDLFRIRTLGFRGEALASIASVSRLTLTTRTaGAELGTRIEVEGGKVVEVEPAAAPKGTTVEVRDLFFNTPARRKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 160 IKSLYTELGKITDIVNRMAMSHPDIRIALISDGKTMLSTNGSGRTNEVMAEIYGMKVARDLVHISGDTSDYHIEGFVAKP 239
Cdd:COG0323 161 LKSDATELAHITDVVRRLALAHPDIAFTLIHNGREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 240 EHSRSNKHYISIFINGRYIKNFMLNKAILEGYHTLLTIGRFPICYINIEMDPILVDVNVHPTKLEVRLSKEEQLYQLIVS 319
Cdd:COG0323 241 EFSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 320 KIQEAFKDrilipknnldyvpkknkvlhsfeqqkiefeqrqntennqektfsseesnskpfmeenqndeivikedsynpf 399
Cdd:COG0323 321 AVREALAQ------------------------------------------------------------------------ 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 400 vtktsesliaddessgynntrekdedyfkkqqeilqemdqtfdsndgttvqnyenkasddyydvndikgtkskdpkrrip 479
Cdd:COG0323 --------------------------------------------------------------------------------
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 480 ymEIVGQVHGTYIIAQNEFGMYMIDQHAAQERIKYEYFRDKIGEVTNEVQDLLIPLTFHFSKDEQLVIDQYKNELQQVGI 559
Cdd:COG0323 329 --AALGQLHGTYILAENEDGLVLIDQHAAHERILYERLKKALAEGGVASQPLLIPETLELSPAEAALLEEHLEELARLGF 406
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 560 MLEHFGGHDYIVSSYPVWFPKDEVEEIIKDMIELILEEKK-VDIKKLREDVAIMMSCKKSIKANHYLQKHEMSDLIDQLR 638
Cdd:COG0323 407 EIEPFGPNTVAVRAVPALLGEGDAEELLRDLLDELAEEGSsESLEELREELLATMACHGAIKAGRRLSLEEMNALLRDLE 486
|
650 660
....*....|....*....|....*....
gi 446438406 639 EAEDPFTCPHGRPIIINFSKYELEKLFKR 667
Cdd:COG0323 487 ATENPYTCPHGRPTWIELSLEELEKLFKR 515
|
|
| mutl |
TIGR00585 |
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ... |
2-306 |
1.05e-122 |
|
DNA mismatch repair protein MutL; All proteins in this family for which the functions are known are involved in the process of generalized mismatch repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273155 [Multi-domain] Cd Length: 312 Bit Score: 366.97 E-value: 1.05e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 2 GKIKELQTSLANKIAAGEVVERPSSVVKELLENAIDAGATEISIEVEESGVQSIRVVDNGSGIEAEDLGLVFHRHATSKL 81
Cdd:TIGR00585 1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 82 DQDEDLFHIRTLGFRGEALASISSVAKVTLKTCTDNANG--NEIYVENGEILNHKPAKAKKGTDILVESLFYNTPARLKY 159
Cdd:TIGR00585 81 QSFEDLERIETLGFRGEALASISSVSRLTITTKTSAADGlaYQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 160 IKSLYTELGKITDIVNRMAMSHPDIRIALISDGKTML--STNGSGRTNEVMA-EIYGMKVARDLVHI-SGDTSDYHIEGF 235
Cdd:TIGR00585 161 LKSPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLqlSTKPNQSTKENRIrSVFGTAVLRKLIPLdEWEDLDLQLEGF 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446438406 236 VAKPEHSRS-NKHYISIFINGRYIKNFMLNKAILEGYHTLLTIGRFPICYINIEMDPILVDVNVHPTKLEVR 306
Cdd:TIGR00585 241 ISQPNVTRSrRSGWQFLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
|
|
| HATPase_MutL-MLH-PMS-like |
cd16926 |
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ... |
11-196 |
4.10e-102 |
|
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.
Pssm-ID: 340403 [Multi-domain] Cd Length: 188 Bit Score: 309.37 E-value: 4.10e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 11 LANKIAAGEVVERPSSVVKELLENAIDAGATEISIEVEESGVQSIRVVDNGSGIEAEDLGLVFHRHATSKLDQDEDLFHI 90
Cdd:cd16926 1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 91 RTLGFRGEALASISSVAKVTLKTCT-DNANGNEIYVENGEILNH-KPAKAKKGTDILVESLFYNTPARLKYIKSLYTELG 168
Cdd:cd16926 81 TTLGFRGEALASIASVSRLTITTRTaDDDVGTRLVVDGGGIIEEvKPAAAPVGTTVTVRDLFYNTPARRKFLKSPKTELS 160
|
170 180
....*....|....*....|....*...
gi 446438406 169 KITDIVNRMAMSHPDIRIALISDGKTML 196
Cdd:cd16926 161 KILDLVQRLALAHPDVSFSLTHDGKLVL 188
|
|
| MutL_C |
pfam08676 |
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ... |
484-625 |
1.13e-57 |
|
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair machinery that corrects replication errors. MutS recognizes mispaired or unpaired bases in a DNA duplex and in the presence of ATP, recruits MutL to form a DNA signaling complex for repair. The N terminal region of MutL contains the ATPase domain and the C terminal is involved in dimerization.
Pssm-ID: 430147 Cd Length: 145 Bit Score: 191.28 E-value: 1.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 484 VGQVHGTYIIAQNEFGMYMIDQHAAQERIKYEYFRDKIGEVTNEVQDLLIPLTFHFSKDEQLVIDQYKNELQQVGIMLEH 563
Cdd:pfam08676 4 LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFELEE 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446438406 564 FGGHDYIVSSYPVWFPKDEVEEIIKDMIELILEEKKVDIKKLREDVAIMMSCKKSIKANHYL 625
Cdd:pfam08676 84 FGPNSVIVRSVPALLRQQNLQELIRELLDELAEKGGSSLEESLEELLATMACHSAVRAGRRL 145
|
|
| MutL_C |
smart00853 |
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ... |
483-624 |
3.25e-47 |
|
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair machinery that corrects replication errors. MutS recognises mispaired or unpaired bases in a DNA duplex and in the presence of ATP, recruits MutL to form a DNA signaling complex for repair. The N terminal region of MutL contains the ATPase domain and the C terminal is involved in dimerisation.
Pssm-ID: 214857 [Multi-domain] Cd Length: 140 Bit Score: 162.91 E-value: 3.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 483 IVGQVHGTYIIAQNEFGMYMIDQHAAQERIKYEYFRDKigEVTNEVQDLLIPLTFHFSKDEQLVIDQYKNELQQVGIMLE 562
Cdd:smart00853 1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQ--AGGLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446438406 563 HFGGHDYIVSSYPVWFPKDEVEEIIKDMIELILEEKKVDIKKLREDVAIMMSCKKSIKANHY 624
Cdd:smart00853 79 IFGPQSLILRSVPALLRQQNLQKLIPELLDLLSDEEENARPSRLEALLASLACRSAIRAGDA 140
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| mutL |
PRK00095 |
DNA mismatch repair endonuclease MutL; |
3-668 |
0e+00 |
|
DNA mismatch repair endonuclease MutL;
Pssm-ID: 234630 [Multi-domain] Cd Length: 617 Bit Score: 823.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 3 KIKELQTSLANKIAAGEVVERPSSVVKELLENAIDAGATEISIEVEESGVQSIRVVDNGSGIEAEDLGLVFHRHATSKLD 82
Cdd:PRK00095 2 PIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 83 QDEDLFHIRTLGFRGEALASISSVAKVTLKTCTDNAN-GNEIYVENGEILNHKPAKAKKGTDILVESLFYNTPARLKYIK 161
Cdd:PRK00095 82 SLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAeGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKFLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 162 SLYTELGKITDIVNRMAMSHPDIRIALISDGKTMLSTNGSGRTNEVMAEIYGMKVARDLVHISGDTSDYHIEGFVAKPEH 241
Cdd:PRK00095 162 SEKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPTL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 242 SRSNKHYISIFINGRYIKNFMLNKAILEGYHTLLTIGRFPICYINIEMDPILVDVNVHPTKLEVRLSKEEQLYQLIVSKI 321
Cdd:PRK00095 242 SRANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDLIVQAI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 322 QEAFKDRILIPKnnldyVPKKNKVLHSFEQQKIEFEQRQNTENNQEKTFSSEESNSKPFMEENQNDEIVIKEDSYNPFVT 401
Cdd:PRK00095 322 QEALAQSGLIPA-----AAGANQVLEPAEPEPLPLQQTPLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 402 KTSESLIADDESSGYNNTREKDEDyfkkqqeilqemdqtfdsndgttvqnyenkasddyydvndikgtkSKDPKRRIPYM 481
Cdd:PRK00095 397 SEAAAAASAEAAAAAPAAAPEPAE---------------------------------------------AAEEADSFPLG 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 482 EIVGQVHGTYIIAQNEFGMYMIDQHAAQERIKYEYFRDKIGEVTNEVQDLLIPLTFHFSKDEQLVIDQYKNELQQVGIML 561
Cdd:PRK00095 432 YALGQLHGTYILAENEDGLYLVDQHAAHERLLYEQLKDKLAEVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLEL 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 562 EHFGGHDYIVSSYPVWFPKDEVEEIIKDMIELILEEKKVDIKKLREdVAIMMSCKKSIKANHYLQKHEMSDLIDQLREAE 641
Cdd:PRK00095 512 EPFGPNSFAVREVPALLGQQELEELIRDLLDELAEEGDSDTLKERE-LLATMACHGAIRAGRRLTLEEMNALLRQLEATE 590
|
650 660
....*....|....*....|....*..
gi 446438406 642 DPFTCPHGRPIIINFSKYELEKLFKRV 668
Cdd:PRK00095 591 NPGTCPHGRPTYIELSLSDLEKLFKRI 617
|
|
| MutL |
COG0323 |
DNA mismatch repair ATPase MutL [Replication, recombination and repair]; |
1-667 |
0e+00 |
|
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
Pssm-ID: 440092 [Multi-domain] Cd Length: 515 Bit Score: 735.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 1 MGKIKELQTSLANKIAAGEVVERPSSVVKELLENAIDAGATEISIEVEESGVQSIRVVDNGSGIEAEDLGLVFHRHATSK 80
Cdd:COG0323 1 MPKIRLLPDELANQIAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLPLAFERHATSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 81 LDQDEDLFHIRTLGFRGEALASISSVAKVTLKTCT-DNANGNEIYVENGEILNHKPAKAKKGTDILVESLFYNTPARLKY 159
Cdd:COG0323 81 IRSAEDLFRIRTLGFRGEALASIASVSRLTLTTRTaGAELGTRIEVEGGKVVEVEPAAAPKGTTVEVRDLFFNTPARRKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 160 IKSLYTELGKITDIVNRMAMSHPDIRIALISDGKTMLSTNGSGRTNEVMAEIYGMKVARDLVHISGDTSDYHIEGFVAKP 239
Cdd:COG0323 161 LKSDATELAHITDVVRRLALAHPDIAFTLIHNGREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 240 EHSRSNKHYISIFINGRYIKNFMLNKAILEGYHTLLTIGRFPICYINIEMDPILVDVNVHPTKLEVRLSKEEQLYQLIVS 319
Cdd:COG0323 241 EFSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 320 KIQEAFKDrilipknnldyvpkknkvlhsfeqqkiefeqrqntennqektfsseesnskpfmeenqndeivikedsynpf 399
Cdd:COG0323 321 AVREALAQ------------------------------------------------------------------------ 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 400 vtktsesliaddessgynntrekdedyfkkqqeilqemdqtfdsndgttvqnyenkasddyydvndikgtkskdpkrrip 479
Cdd:COG0323 --------------------------------------------------------------------------------
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 480 ymEIVGQVHGTYIIAQNEFGMYMIDQHAAQERIKYEYFRDKIGEVTNEVQDLLIPLTFHFSKDEQLVIDQYKNELQQVGI 559
Cdd:COG0323 329 --AALGQLHGTYILAENEDGLVLIDQHAAHERILYERLKKALAEGGVASQPLLIPETLELSPAEAALLEEHLEELARLGF 406
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 560 MLEHFGGHDYIVSSYPVWFPKDEVEEIIKDMIELILEEKK-VDIKKLREDVAIMMSCKKSIKANHYLQKHEMSDLIDQLR 638
Cdd:COG0323 407 EIEPFGPNTVAVRAVPALLGEGDAEELLRDLLDELAEEGSsESLEELREELLATMACHGAIKAGRRLSLEEMNALLRDLE 486
|
650 660
....*....|....*....|....*....
gi 446438406 639 EAEDPFTCPHGRPIIINFSKYELEKLFKR 667
Cdd:COG0323 487 ATENPYTCPHGRPTWIELSLEELEKLFKR 515
|
|
| mutl |
TIGR00585 |
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ... |
2-306 |
1.05e-122 |
|
DNA mismatch repair protein MutL; All proteins in this family for which the functions are known are involved in the process of generalized mismatch repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273155 [Multi-domain] Cd Length: 312 Bit Score: 366.97 E-value: 1.05e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 2 GKIKELQTSLANKIAAGEVVERPSSVVKELLENAIDAGATEISIEVEESGVQSIRVVDNGSGIEAEDLGLVFHRHATSKL 81
Cdd:TIGR00585 1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 82 DQDEDLFHIRTLGFRGEALASISSVAKVTLKTCTDNANG--NEIYVENGEILNHKPAKAKKGTDILVESLFYNTPARLKY 159
Cdd:TIGR00585 81 QSFEDLERIETLGFRGEALASISSVSRLTITTKTSAADGlaYQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 160 IKSLYTELGKITDIVNRMAMSHPDIRIALISDGKTML--STNGSGRTNEVMA-EIYGMKVARDLVHI-SGDTSDYHIEGF 235
Cdd:TIGR00585 161 LKSPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLqlSTKPNQSTKENRIrSVFGTAVLRKLIPLdEWEDLDLQLEGF 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446438406 236 VAKPEHSRS-NKHYISIFINGRYIKNFMLNKAILEGYHTLLTIGRFPICYINIEMDPILVDVNVHPTKLEVR 306
Cdd:TIGR00585 241 ISQPNVTRSrRSGWQFLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
|
|
| HATPase_MutL-MLH-PMS-like |
cd16926 |
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ... |
11-196 |
4.10e-102 |
|
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.
Pssm-ID: 340403 [Multi-domain] Cd Length: 188 Bit Score: 309.37 E-value: 4.10e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 11 LANKIAAGEVVERPSSVVKELLENAIDAGATEISIEVEESGVQSIRVVDNGSGIEAEDLGLVFHRHATSKLDQDEDLFHI 90
Cdd:cd16926 1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 91 RTLGFRGEALASISSVAKVTLKTCT-DNANGNEIYVENGEILNH-KPAKAKKGTDILVESLFYNTPARLKYIKSLYTELG 168
Cdd:cd16926 81 TTLGFRGEALASIASVSRLTITTRTaDDDVGTRLVVDGGGIIEEvKPAAAPVGTTVTVRDLFYNTPARRKFLKSPKTELS 160
|
170 180
....*....|....*....|....*...
gi 446438406 169 KITDIVNRMAMSHPDIRIALISDGKTML 196
Cdd:cd16926 161 KILDLVQRLALAHPDVSFSLTHDGKLVL 188
|
|
| MutL_C |
pfam08676 |
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ... |
484-625 |
1.13e-57 |
|
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair machinery that corrects replication errors. MutS recognizes mispaired or unpaired bases in a DNA duplex and in the presence of ATP, recruits MutL to form a DNA signaling complex for repair. The N terminal region of MutL contains the ATPase domain and the C terminal is involved in dimerization.
Pssm-ID: 430147 Cd Length: 145 Bit Score: 191.28 E-value: 1.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 484 VGQVHGTYIIAQNEFGMYMIDQHAAQERIKYEYFRDKIGEVTNEVQDLLIPLTFHFSKDEQLVIDQYKNELQQVGIMLEH 563
Cdd:pfam08676 4 LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFELEE 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446438406 564 FGGHDYIVSSYPVWFPKDEVEEIIKDMIELILEEKKVDIKKLREDVAIMMSCKKSIKANHYL 625
Cdd:pfam08676 84 FGPNSVIVRSVPALLRQQNLQELIRELLDELAEKGGSSLEESLEELLATMACHSAVRAGRRL 145
|
|
| MutL_C |
smart00853 |
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ... |
483-624 |
3.25e-47 |
|
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair machinery that corrects replication errors. MutS recognises mispaired or unpaired bases in a DNA duplex and in the presence of ATP, recruits MutL to form a DNA signaling complex for repair. The N terminal region of MutL contains the ATPase domain and the C terminal is involved in dimerisation.
Pssm-ID: 214857 [Multi-domain] Cd Length: 140 Bit Score: 162.91 E-value: 3.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 483 IVGQVHGTYIIAQNEFGMYMIDQHAAQERIKYEYFRDKigEVTNEVQDLLIPLTFHFSKDEQLVIDQYKNELQQVGIMLE 562
Cdd:smart00853 1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQ--AGGLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446438406 563 HFGGHDYIVSSYPVWFPKDEVEEIIKDMIELILEEKKVDIKKLREDVAIMMSCKKSIKANHY 624
Cdd:smart00853 79 IFGPQSLILRSVPALLRQQNLQKLIPELLDLLSDEEENARPSRLEALLASLACRSAIRAGDA 140
|
|
| MutL_Trans |
cd00782 |
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ... |
206-325 |
4.58e-47 |
|
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the C-terminal domain of DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. Included in this group are proteins similar to human MLH1, hPMS2, hPMS1, hMLH3 and E. coli MutL, MLH1 forms heterodimers with PMS2, PMS1 and MLH3. These three complexes have distinct functions in meiosis. hMLH1-hPMS2 also participates in the repair of all DNA mismatch repair (MMR) substrates. Roles for hMLH1-hPMS1 or hMLH1-hMLH3 in MMR have not been established. Cells lacking either hMLH1 or hPMS2 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hMLH1 causes predisposition to HNPCC, Muir-Torre syndrome and Turcot syndrome (HNPCC variant). Mutation in hPMS2 causes predisposition to HPNCC and Turcot syndrome. Mutation in hMLH1 accounts for a large fraction of HNPCC families. There is no convincing evidence to support hPMS1 having a role in HNPCC predisposition. It has been suggested that hMLH3 may be a low risk gene for colorectal cancer; however there is little evidence to support it having a role in classical HNPCC. It has been suggested that during initiation of DNA mismatch repair in E. coli, the mismatch recognition protein MutS recruits MutL in the presence of ATP. The MutS(ATP)-MutL ternary complex formed, then recruits the latent endonuclease MutH.
Pssm-ID: 238405 [Multi-domain] Cd Length: 122 Bit Score: 161.94 E-value: 4.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 206 EVMAEIYGMKVARDLVHISGDTSDYHIEGFVAKPEHSRSNKHYISIFINGRYIKNFMLNKAILEGYHTLLTIGRFPICYI 285
Cdd:cd00782 3 DRIAQVYGKEVAKNLIEVELESGDFRISGYISKPDFGRSSKDRQFLFVNGRPVRDKLLSKAINEAYRSYLPKGRYPVFVL 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 446438406 286 NIEMDPILVDVNVHPTKLEVRLSKEEQLYQLIVSKIQEAF 325
Cdd:cd00782 83 NLELPPELVDVNVHPTKREVRFSDEEEVLELIREALRSAL 122
|
|
| DNA_mis_repair |
pfam01119 |
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ... |
209-324 |
3.25e-46 |
|
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain of the mutL/hexB/PMS1 family. This domain has a ribosomal S5 domain 2-like fold.
Pssm-ID: 426060 [Multi-domain] Cd Length: 117 Bit Score: 159.59 E-value: 3.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 209 AEIYGMKVARDLVHISGDTSDYHIEGFVAKPEHSRSNKHYISIFINGRYIKNFMLNKAILEGYHTLLTIGRFPICYINIE 288
Cdd:pfam01119 1 AAIYGKEFAENLLPIEKEDDGLRLSGYISKPTLSRSNRDYQYLFVNGRPVRDKLLSHAIREAYRDLLPKGRYPVAVLFLE 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 446438406 289 MDPILVDVNVHPTKLEVRLSKEEQLYQLIVSKIQEA 324
Cdd:pfam01119 81 IDPELVDVNVHPTKREVRFRDEREVYDFIKEALREA 116
|
|
| TopoII_MutL_Trans |
cd00329 |
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ... |
206-306 |
3.73e-28 |
|
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the C-terminal domain of type II DNA topoisomerases (Topo II) and DNA mismatch repair (MutL/MLH1/PMS2) proteins. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. The GyrB dimerizes in response to ATP binding, and is homologous to the N-terminal half of eukaryotic Topo II and the ATPase fragment of MutL. Type II DNA topoisomerases catalyze the ATP-dependent transport of one DNA duplex through another, in the process generating transient double strand breaks via covalent attachments to both DNA strands at the 5' positions. Included in this group are proteins similar to human MLH1 and PMS2. MLH1 forms a heterodimer with PMS2 which functions in meiosis and in DNA mismatch repair (MMR). Cells lacking either hMLH1 or hPMS2 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hMLH1 accounts for a large fraction of Lynch syndrome (HNPCC) families.
Pssm-ID: 238202 [Multi-domain] Cd Length: 107 Bit Score: 108.89 E-value: 3.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 206 EVMAEIYGMKVARDLVHISGDTSDYHIEGFVAKPEHSRSNKHYISIFINGRYI-KNFMLNKAILEGYHTLLT---IGRFP 281
Cdd:cd00329 3 DRLAEILGDKVADKLIYVEGESDGFRVEGAISYPDSGRSSKDRQFSFVNGRPVrEGGTHVKAVREAYTRALNgddVRRYP 82
|
90 100
....*....|....*....|....*
gi 446438406 282 ICYINIEMDPILVDVNVHPTKLEVR 306
Cdd:cd00329 83 VAVLSLKIPPSLVDVNVHPTKEEVR 107
|
|
| MutL_Trans_MutL |
cd03482 |
MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
208-326 |
2.17e-23 |
|
MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to Escherichia coli MutL. EcMutL belongs to the DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from the ATP-binding site to the DNA breakage/reunion regions of the enzymes. It has been suggested that during initiation of DNA mismatch repair in E. coli, the mismatch recognition protein MutS recruits MutL in the presence of ATP. The MutS(ATP)-MutL ternary complex formed, then recruits the latent endonuclease MutH. Prokaryotic MutS and MutL are homodimers.
Pssm-ID: 239564 [Multi-domain] Cd Length: 123 Bit Score: 95.73 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 208 MAEIYGMKVARDLVHISGDTSDYHIEGFVAKPEHSRSNKHYISIFINGRYIKNFMLNKAILEGYHTLLTIGRFPICYINI 287
Cdd:cd03482 5 LADILGEDFAEQALAIDEEAGGLRLSGWIALPTFARSQADIQYFYVNGRMVRDKLISHAVRQAYSDVLHGGRHPAYVLYL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 446438406 288 EMDPILVDVNVHPTKLEVRLSKEEQLYQLIVSKIQEAFK 326
Cdd:cd03482 85 ELDPAQVDVNVHPAKHEVRFRDSRLVHDFIYHAVKKALA 123
|
|
| MutL_Trans_MLH1 |
cd03483 |
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
211-324 |
1.27e-15 |
|
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to yeast and human MLH1 (MutL homologue 1). This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. MLH1 forms heterodimers with PMS2, PMS1 and MLH3. These three complexes have distinct functions in meiosis. hMLH1-hPMS2 also participates in the repair of all DNA mismatch repair (MMR) substrates. Roles for hMLH1-hPMS1 or hMLH1-hMLH3 in MMR have not been established. Cells lacking hMLH1 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hMLH1 causes predisposition to HNPCC, Muir-Torre syndrome and Turcot syndrome (HNPCC variant). Mutation in hMLH1 accounts for a large fraction of HNPCC families.
Pssm-ID: 239565 [Multi-domain] Cd Length: 127 Bit Score: 73.81 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 211 IYGMKVARDLVHISGDTSDYH----IEGFVAKPEHSRSNKHYIsIFINGRYIKNFMLNKAILEGYHTLLTIGRFPICYIN 286
Cdd:cd03483 9 VYGAAVANELIEVEISDDDDDlgfkVKGLISNANYSKKKIIFI-LFINNRLVECSALRRAIENVYANYLPKGAHPFVYLS 87
|
90 100 110
....*....|....*....|....*....|....*...
gi 446438406 287 IEMDPILVDVNVHPTKLEVRLSKEEQLYQLIVSKIQEA 324
Cdd:cd03483 88 LEIPPENVDVNVHPTKREVHFLNEEEIIERIQKLVEDK 125
|
|
| MutL_Trans_hPMS_2_like |
cd03484 |
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
227-325 |
9.34e-11 |
|
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to human PSM2 (hPSM2). hPSM2 belongs to the DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. Included in this group are proteins similar to yeast PMS1. The yeast MLH1-PMS1 and the human MLH1-PMS2 heterodimers play a role in meiosis. hMLH1-hPMS2 also participates in the repair of all DNA mismatch repair (MMR) substrates. Cells lacking hPMS2 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hPMS2 causes predisposition to HPNCC and Turcot syndrome.
Pssm-ID: 239566 [Multi-domain] Cd Length: 142 Bit Score: 60.36 E-value: 9.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 227 TSDYHIEGFVAKPEH--SRSNKHYISIFINGRYIKNFMLNKAILEGYHTLLTIgRFPICYINIEMDPILVDVNVHPTKLE 304
Cdd:cd03484 42 DSEVKITGYISKPSHgcGRSSSDRQFFYINGRPVDLKKVAKLINEVYKSFNSR-QYPFFILNISLPTSLYDVNVTPDKRT 120
|
90 100
....*....|....*....|.
gi 446438406 305 VRLSKEEQLYQLIVSKIQEAF 325
Cdd:cd03484 121 VLLHDEDRLIDTLKTSLSELF 141
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
27-80 |
1.96e-09 |
|
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.
Pssm-ID: 460579 [Multi-domain] Cd Length: 109 Bit Score: 55.45 E-value: 1.96e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 446438406 27 VVKELLENAID--AGATEISIEVEESGVQSIRVVDNGSGIEAEDLGLVFHRHATSK 80
Cdd:pfam02518 9 VLSNLLDNALKhaAKAGEITVTLSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTAD 64
|
|
| HATPase_c_3 |
pfam13589 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ... |
26-113 |
1.57e-08 |
|
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.
Pssm-ID: 433332 [Multi-domain] Cd Length: 135 Bit Score: 53.49 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 26 SVVKELLENAIDAGATEISIEV--EESGVQSIRVVDNGSGIEAEDLGLVFHRHATSKldqdEDLFHIRTLGFRG--EALA 101
Cdd:pfam13589 3 GALAELIDNSIDADATNIKIEVnkNRGGGTEIVIEDDGHGMSPEELINALRLATSAK----EAKRGSTDLGRYGigLKLA 78
|
90
....*....|..
gi 446438406 102 SISSVAKVTLKT 113
Cdd:pfam13589 79 SLSLGAKLTVTS 90
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
27-85 |
7.62e-08 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 51.11 E-value: 7.62e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446438406 27 VVKELLENAIDAG--ATEISIEVEESGVQ-SIRVVDNGSGIEAEDLGLVFHRHATSKLDQDE 85
Cdd:smart00387 9 VLSNLLDNAIKYTpeGGRITVTLERDGDHvEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRK 70
|
|
| MutL_Trans_hPMS_1_like |
cd03485 |
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
232-323 |
1.48e-07 |
|
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to human PSM1 (hPSM1) and yeast MLH2. hPSM1 and yMLH2 are members of the DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. PMS1 forms a heterodimer with MLH1. The MLH1-PMS1 complex functions in meiosis. Loss of yMLH2 results in a small but significant decrease in spore viability and a significant increase in gene conversion frequencies. A role for hMLH1-hPMS1 in DNA mismatch repair has not been established. Mutation in hMLH1 accounts for a large fraction of Lynch syndrome (HNPCC) families, however there is no convincing evidence to support hPMS1 having a role in HNPCC predisposition.
Pssm-ID: 239567 [Multi-domain] Cd Length: 132 Bit Score: 50.73 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 232 IEGFVAKPE--HSRSNKHYISIFINGR---YIKNFM-LNKAILEGYHTLLTIGRFPICYINIEMDPILVDVNVHPTKLEV 305
Cdd:cd03485 32 LEGFLPKPGsdVSKTKSDGKFISVNSRpvsLGKDIGkLLRQYYSSAYRKSSLRRYPVFFLNILCPPGLVDVNIEPDKDDV 111
|
90
....*....|....*...
gi 446438406 306 RLSKEEQLYQLIVSKIQE 323
Cdd:cd03485 112 LLQNKEAVLQAVENLLES 129
|
|
| KdpD |
COG2205 |
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
27-85 |
4.17e-06 |
|
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 48.36 E-value: 4.17e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446438406 27 VVKELLENAI----DAGATEISIEVEESGVQsIRVVDNGSGIEAEDLGLVFHRHATSKLDQDE 85
Cdd:COG2205 136 VLANLLDNAIkyspPGGTITISARREGDGVR-ISVSDNGPGIPEEELERIFERFYRGDNSRGE 197
|
|
| BaeS |
COG0642 |
Signal transduction histidine kinase [Signal transduction mechanisms]; |
27-80 |
4.26e-06 |
|
Signal transduction histidine kinase [Signal transduction mechanisms];
Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 49.14 E-value: 4.26e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446438406 27 VVKELLENAIDAGA--TEISIEVEESGVQ-SIRVVDNGSGIEAEDLGLVFHRHATSK 80
Cdd:COG0642 227 VLLNLLSNAIKYTPegGTVTVSVRREGDRvRISVEDTGPGIPPEDLERIFEPFFRTD 283
|
|
| WalK |
COG5002 |
Sensor histidine kinase WalK [Signal transduction mechanisms]; |
26-75 |
9.31e-05 |
|
Sensor histidine kinase WalK [Signal transduction mechanisms];
Pssm-ID: 444026 [Multi-domain] Cd Length: 390 Bit Score: 45.31 E-value: 9.31e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446438406 26 SVVKELLENAI----DAGATEISIEVEESGVQsIRVVDNGSGIEAEDLGLVFHR 75
Cdd:COG5002 284 QVLTNLLDNAIkytpEGGTITVSLREEDDQVR-ISVRDTGIGIPEEDLPRIFER 336
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
31-80 |
1.00e-04 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 45.34 E-value: 1.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446438406 31 LLENAIDAGAT----EISIEVEESGVQsIRVVDNGSGIEAEDLGLVFHRHATSK 80
Cdd:COG5000 325 LLKNAIEAIEEggeiEVSTRREDGRVR-IEVSDNGPGIPEEVLERIFEPFFTTK 377
|
|
| CitA |
COG3290 |
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ... |
26-84 |
2.62e-04 |
|
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];
Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 43.68 E-value: 2.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446438406 26 SVVKELLENAIDAGAT--------EISIEVEESGVqSIRVVDNGSGIEAEDLGLVFHRHATSKLDQD 84
Cdd:COG3290 284 TILGNLLDNAIEAVEKlpeeerrvELSIRDDGDEL-VIEVEDSGPGIPEELLEKIFERGFSTKLGEG 349
|
|
| COG4191 |
COG4191 |
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ... |
31-73 |
5.99e-04 |
|
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];
Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 42.48 E-value: 5.99e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 446438406 31 LLENAIDA------GATEISIEVEESGVQsIRVVDNGSGIEAEDLGLVF 73
Cdd:COG4191 264 LLINAIDAmeegegGRITISTRREGDYVV-ISVRDNGPGIPPEVLERIF 311
|
|
| PRK04184 |
PRK04184 |
DNA topoisomerase VI subunit B; Validated |
27-73 |
9.82e-04 |
|
DNA topoisomerase VI subunit B; Validated
Pssm-ID: 235246 [Multi-domain] Cd Length: 535 Bit Score: 42.19 E-value: 9.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 446438406 27 VVKELLENAIDAGAT-----EISIEVEESGVQ----SIRVVDNGSGIEAEDLGLVF 73
Cdd:PRK04184 40 TVKELVDNSLDACEEagilpDIKIEIKRVDEGkdhyRVTVEDNGPGIPPEEIPKVF 95
|
|
| HATPase_TopVIB-like |
cd16933 |
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family ... |
27-75 |
1.05e-03 |
|
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family includes the histidine kinase-like ATPase (HATPase) domain of the B subunit of topoisomerase VI (Topo VIB). Topo VI is a heterotetrameric complex composed of two TopVIA and two TopVIB subunits and is categorized as a type II B DNA topoisomerase. It is found in archaea and also in plants. Type II enzymes cleave both strands of a DNA duplex and pass a second duplex through the resulting break in an ATP-dependent mechanism. DNA cleavage by Topo VI generates two-nucleotide 5'-protruding ends.
Pssm-ID: 340410 [Multi-domain] Cd Length: 203 Bit Score: 40.79 E-value: 1.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 446438406 27 VVKELLENAIDAGAT-----EISIEVEESGVQ--SIRVVDNGSGIEAEDLGLVFHR 75
Cdd:cd16933 23 TVRELVENSLDATEEagilpDIKVEIEEIGKDhyKVIVEDNGPGIPEEQIPKVFGK 78
|
|
| HATPase_BasS-like |
cd16940 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
25-75 |
1.97e-03 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain.
Pssm-ID: 340417 [Multi-domain] Cd Length: 113 Bit Score: 38.54 E-value: 1.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446438406 25 SSVVKELLENAID---AGaTEISIEVEESGVQSIRVVDNGSGIEAEDLGLVFHR 75
Cdd:cd16940 15 FLLLRNLVDNAVRyspQG-SRVEIKLSADDGAVIRVEDNGPGIDEEELEALFER 67
|
|
| PRK14867 |
PRK14867 |
DNA topoisomerase VI subunit B; Provisional |
25-289 |
3.17e-03 |
|
DNA topoisomerase VI subunit B; Provisional
Pssm-ID: 237841 [Multi-domain] Cd Length: 659 Bit Score: 40.57 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 25 SSVVKELLENAIDAGAT-----EISIEVEESGVQSIRVV--DNGSGIEAEDLGLVFHRH-ATSKLDQdedlfHIRTLGFR 96
Cdd:PRK14867 38 TTIIHELVTNSLDACEEaeilpDIKVEIEKLGSDHYKVAveDNGPGIPPEFVPKVFGKMlAGSKMHR-----LIQSRGQQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 97 GEALASISSVAKVT----LKTCTDNANGNEIYVE--------NGEILNHKPAKAK-KGTDilVESLFyntparlKYIKSL 163
Cdd:PRK14867 113 GIGAAGVLLFSQITtgkpLKITTSTGDGKIHEMEikmsveknEGDIVSHKVREGFwRGTR--VEGEF-------KEVTYN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438406 164 YTELGKItDIVNRMAMSHPDIRIALISDGKTML----STNGSGRTNEVMAEIYGMKVaRDLVHISGDTSDYHIEGFVAKp 239
Cdd:PRK14867 184 RREQGPF-EYLRRISLSTPHAKITLKDPEETVVfdrtVDEIPEKPEEMKPHPYGLTT-DELLYIARKTDSSKVSSMLNS- 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446438406 240 EHSRSNKHYIsifingRYIKNFMLNKAILEGYHTLLTIGRFPICYINIEM 289
Cdd:PRK14867 261 ELSRVTTKRI------KELEEYVLRDLLLENYRDSVFWDTVVSCYLNFDF 304
|
|
| HATPase_GyrB-like |
cd16928 |
Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes ... |
28-64 |
3.38e-03 |
|
Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes histidine kinase-like ATPase domain of the B subunit of DNA gyrase. Bacterial DNA gyrase is a type II topoisomerase (type II as it transiently cleaves both strands of DNA) which catalyzes the introduction of negative supercoils into DNA, possibly by a mechanism in which one segment of the double-stranded DNA substrate is passed through a transient break in a second segment. It consists of GyrA and GyrB subunits in an A2B2 stoichiometry; GyrA subunits catalyze strand-breakage and reunion reactions, and GyrB subunits hydrolyze ATP. DNA gyrase is found in bacteria, plants and archaea, but as it is absent in humans it is a possible drug target for the treatment of bacterial and parasite infections.
Pssm-ID: 340405 [Multi-domain] Cd Length: 180 Bit Score: 39.06 E-value: 3.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 446438406 28 VKELLENAID---AG-ATEISIEVEESGvqSIRVVDNGSGI 64
Cdd:cd16928 5 VWEIVDNSIDealAGyATEIEVTLHEDN--SITVEDNGRGI 43
|
|
| ComP |
COG4585 |
Signal transduction histidine kinase ComP [Signal transduction mechanisms]; |
27-72 |
4.60e-03 |
|
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
Pssm-ID: 443642 [Multi-domain] Cd Length: 252 Bit Score: 39.22 E-value: 4.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446438406 27 VVKELLENAID-AGATEISIEVEESGVQ-SIRVVDNGSGIEAED-----LGLV 72
Cdd:COG4585 166 IVQEALTNALKhAGATRVTVTLEVDDGElTLTVRDDGVGFDPEAapgggLGLR 218
|
|
| gyrB |
PRK05644 |
DNA gyrase subunit B; Validated |
28-64 |
5.33e-03 |
|
DNA gyrase subunit B; Validated
Pssm-ID: 235542 [Multi-domain] Cd Length: 638 Bit Score: 40.08 E-value: 5.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 446438406 28 VKELLENAID---AG-ATEISIEVEESGvqSIRVVDNGSGI 64
Cdd:PRK05644 42 VYEIVDNSIDealAGyCDHIEVTINEDG--SITVTDNGRGI 80
|
|
| TOP2c |
smart00433 |
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE |
28-85 |
5.71e-03 |
|
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
Pssm-ID: 214659 [Multi-domain] Cd Length: 594 Bit Score: 39.85 E-value: 5.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446438406 28 VKELLENAID---AG-ATEISIEVEESGvqSIRVVDNGSGI-----EAED---LGLVF-HRHATSKLDQDE 85
Cdd:smart00433 6 VDEIVDNAADealAGyMDTIKVTIDKDN--SISVEDNGRGIpveihPKEKkyaPEVIFtVLHAGGKFDDDA 74
|
|
| |
