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Conserved domains on  [gi|446438606|ref|WP_000516461|]
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MULTISPECIES: DNA mismatch repair endonuclease MutL [Bacillus cereus group]

Protein Classification

DNA mismatch repair endonuclease MutL( domain architecture ID 11478033)

DNA mismatch repair endonuclease MutL is required for dam-dependent methyl-directed DNA mismatch repair; it mediates the interactions between MutH and MutS in the DNA repair system

Gene Symbol:  mutL
PubMed:  32652606|19953589
SCOP:  4000168

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
mutL PRK00095
DNA mismatch repair endonuclease MutL;
3-646 0e+00

DNA mismatch repair endonuclease MutL;


:

Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 841.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606   3 KIRKLDDQLSNLIAAGEVVERPASVVKELVENSIDANSTSIEIHLEEAGLSKIRIIDNGDGIAEEDCIVAFERHATSKIK 82
Cdd:PRK00095   2 PIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606  83 DENDLFRIRTLGFRGEALPSIASVSELELITSTGDAP-GTHLIIKGGDIIKQEKTASRKGTDITVQNLFFNTPARLKYMK 161
Cdd:PRK00095  82 SLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAeGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKFLK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 162 TIHTELGNITDIVYRIAMSHPEVSLKLFHNEKKLLHTSGNGDVRQVLASIYSIQVAKKLVPIEAESLDFTIKGYVTLPEV 241
Cdd:PRK00095 162 SEKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPTL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 242 TRASRNYMSTIVNGRYVRNFVLMKAIQQGYHTLLPVGRYPIGFLSIEMDPMLVDVNVHPAKLEVRFSKEQELLKLIEETL 321
Cdd:PRK00095 242 SRANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDLIVQAI 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 322 QAAFKKIQLIPDAGVTTKKKEKDESVQEQFQFEHAKPKEPSMPDIILPTGMDEKQEEPQAVKQPAQLWQPPKQEWQPPQS 401
Cdd:PRK00095 322 QEALAQSGLIPAAAGANQVLEPAEPEPLPLQQTPLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSEAAA 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 402 LVREEQSWQPSTKSIIEEPIREEKswnsndedfeleeleeevqeieeiemngNDLPPLYPIGQMHGTYIFAQNDKGLYMI 481
Cdd:PRK00095 402 AASAEAAAAAPAAAPEPAEAAEEA----------------------------DSFPLGYALGQLHGTYILAENEDGLYLV 453
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 482 DQHAAQERINYEYFRDKVGRVAQEVQELLVPYRIDLSLTEFLRVEEQLEELKKVGLFLEQFGHQSFIVRSHPTWFPKGQE 561
Cdd:PRK00095 454 DQHAAHERLLYEQLKDKLAEVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLELEPFGPNSFAVREVPALLGQQEL 533
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 562 TEIIDEMMEQVVKLKKVDIKKLReEAAIMMSCKASIKANQYLTNDQIFALLEELRTTTNPYTCPHGRPILVHHSTYELEK 641
Cdd:PRK00095 534 EELIRDLLDELAEEGDSDTLKER-ELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIELSLSDLEK 612

                 ....*
gi 446438606 642 MFKRV 646
Cdd:PRK00095 613 LFKRI 617
 
Name Accession Description Interval E-value
mutL PRK00095
DNA mismatch repair endonuclease MutL;
3-646 0e+00

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 841.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606   3 KIRKLDDQLSNLIAAGEVVERPASVVKELVENSIDANSTSIEIHLEEAGLSKIRIIDNGDGIAEEDCIVAFERHATSKIK 82
Cdd:PRK00095   2 PIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606  83 DENDLFRIRTLGFRGEALPSIASVSELELITSTGDAP-GTHLIIKGGDIIKQEKTASRKGTDITVQNLFFNTPARLKYMK 161
Cdd:PRK00095  82 SLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAeGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKFLK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 162 TIHTELGNITDIVYRIAMSHPEVSLKLFHNEKKLLHTSGNGDVRQVLASIYSIQVAKKLVPIEAESLDFTIKGYVTLPEV 241
Cdd:PRK00095 162 SEKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPTL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 242 TRASRNYMSTIVNGRYVRNFVLMKAIQQGYHTLLPVGRYPIGFLSIEMDPMLVDVNVHPAKLEVRFSKEQELLKLIEETL 321
Cdd:PRK00095 242 SRANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDLIVQAI 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 322 QAAFKKIQLIPDAGVTTKKKEKDESVQEQFQFEHAKPKEPSMPDIILPTGMDEKQEEPQAVKQPAQLWQPPKQEWQPPQS 401
Cdd:PRK00095 322 QEALAQSGLIPAAAGANQVLEPAEPEPLPLQQTPLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSEAAA 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 402 LVREEQSWQPSTKSIIEEPIREEKswnsndedfeleeleeevqeieeiemngNDLPPLYPIGQMHGTYIFAQNDKGLYMI 481
Cdd:PRK00095 402 AASAEAAAAAPAAAPEPAEAAEEA----------------------------DSFPLGYALGQLHGTYILAENEDGLYLV 453
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 482 DQHAAQERINYEYFRDKVGRVAQEVQELLVPYRIDLSLTEFLRVEEQLEELKKVGLFLEQFGHQSFIVRSHPTWFPKGQE 561
Cdd:PRK00095 454 DQHAAHERLLYEQLKDKLAEVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLELEPFGPNSFAVREVPALLGQQEL 533
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 562 TEIIDEMMEQVVKLKKVDIKKLReEAAIMMSCKASIKANQYLTNDQIFALLEELRTTTNPYTCPHGRPILVHHSTYELEK 641
Cdd:PRK00095 534 EELIRDLLDELAEEGDSDTLKER-ELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIELSLSDLEK 612

                 ....*
gi 446438606 642 MFKRV 646
Cdd:PRK00095 613 LFKRI 617
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
1-645 0e+00

DNA mismatch repair ATPase MutL [Replication, recombination and repair];


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 769.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606   1 MGKIRKLDDQLSNLIAAGEVVERPASVVKELVENSIDANSTSIEIHLEEAGLSKIRIIDNGDGIAEEDCIVAFERHATSK 80
Cdd:COG0323    1 MPKIRLLPDELANQIAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLPLAFERHATSK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606  81 IKDENDLFRIRTLGFRGEALPSIASVSELELITSTGDAP-GTHLIIKGGDIIKQEKTASRKGTDITVQNLFFNTPARLKY 159
Cdd:COG0323   81 IRSAEDLFRIRTLGFRGEALASIASVSRLTLTTRTAGAElGTRIEVEGGKVVEVEPAAAPKGTTVEVRDLFFNTPARRKF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 160 MKTIHTELGNITDIVYRIAMSHPEVSLKLFHNEKKLLHTSGNGDVRQVLASIYSIQVAKKLVPIEAESLDFTIKGYVTLP 239
Cdd:COG0323  161 LKSDATELAHITDVVRRLALAHPDIAFTLIHNGREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 240 EVTRASRNYMSTIVNGRYVRNFVLMKAIQQGYHTLLPVGRYPIGFLSIEMDPMLVDVNVHPAKLEVRFSKEQELLKLIEE 319
Cdd:COG0323  241 EFSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRS 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 320 TLQAAFKKiqlipdagvttkkkekdesvqeqfqfehakpkepsmpdiilptgmdekqeepqavkqpaqlwqppkqewqpp 399
Cdd:COG0323  321 AVREALAQ------------------------------------------------------------------------ 328
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 400 qslvreeqswqpstksiieepireekswnsndedfeleeleeevqeieeiemngndlpplYPIGQMHGTYIFAQNDKGLY 479
Cdd:COG0323  329 ------------------------------------------------------------AALGQLHGTYILAENEDGLV 348
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 480 MIDQHAAQERINYEYFRDKVGRVAQEVQELLVPYRIDLSLTEFLRVEEQLEELKKVGLFLEQFGHQSFIVRSHPTWFPKG 559
Cdd:COG0323  349 LIDQHAAHERILYERLKKALAEGGVASQPLLIPETLELSPAEAALLEEHLEELARLGFEIEPFGPNTVAVRAVPALLGEG 428
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 560 QETEIIDEMMEQVVKLKK-VDIKKLREEAAIMMSCKASIKANQYLTNDQIFALLEELRTTTNPYTCPHGRPILVHHSTYE 638
Cdd:COG0323  429 DAEELLRDLLDELAEEGSsESLEELREELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTWIELSLEE 508

                 ....*..
gi 446438606 639 LEKMFKR 645
Cdd:COG0323  509 LEKLFKR 515
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
2-306 7.06e-126

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: 374.67  E-value: 7.06e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606    2 GKIRKLDDQLSNLIAAGEVVERPASVVKELVENSIDANSTSIEIHLEEAGLSKIRIIDNGDGIAEEDCIVAFERHATSKI 81
Cdd:TIGR00585   1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606   82 KDENDLFRIRTLGFRGEALPSIASVSELELITSTGDAPGT--HLIIKGGDIIKQEKTASRKGTDITVQNLFFNTPARLKY 159
Cdd:TIGR00585  81 QSFEDLERIETLGFRGEALASISSVSRLTITTKTSAADGLayQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRKF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606  160 MKTIHTELGNITDIVYRIAMSHPEVSLKLFHNEKKLLHTSG--NGDVRQ-VLASIYSIQVAKKLVPI-EAESLDFTIKGY 235
Cdd:TIGR00585 161 LKSPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLQLSTkpNQSTKEnRIRSVFGTAVLRKLIPLdEWEDLDLQLEGF 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446438606  236 VTLPEVTRASRNY-MSTIVNGRYVRNFVLMKAIQQGYHTLLPVGRYPIGFLSIEMDPMLVDVNVHPAKLEVR 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 6.99e-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: 307.83  E-value: 6.99e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606  11 LSNLIAAGEVVERPASVVKELVENSIDANSTSIEIHLEEAGLSKIRIIDNGDGIAEEDCIVAFERHATSKIKDENDLFRI 90
Cdd:cd16926    1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606  91 RTLGFRGEALPSIASVSELELITSTGDAP-GTHLIIKGGDIIKQEKTASR-KGTDITVQNLFFNTPARLKYMKTIHTELG 168
Cdd:cd16926   81 TTLGFRGEALASIASVSRLTITTRTADDDvGTRLVVDGGGIIEEVKPAAApVGTTVTVRDLFYNTPARRKFLKSPKTELS 160
                        170       180
                 ....*....|....*....|....*...
gi 446438606 169 NITDIVYRIAMSHPEVSLKLFHNEKKLL 196
Cdd:cd16926  161 KILDLVQRLALAHPDVSFSLTHDGKLVL 188
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
462-603 1.44e-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: 190.89  E-value: 1.44e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606  462 IGQMHGTYIFAQNDKGLYMIDQHAAQERINYEYFRDKVGRVAQEVQELLVPYRIDLSLTEFLRVEEQLEELKKVGLFLEQ 541
Cdd:pfam08676   4 LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFELEE 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446438606  542 FGHQSFIVRSHPTWFPKGQETEIIDEMMEQVVKLKKVDIKKLREEAAIMMSCKASIKANQYL 603
Cdd:pfam08676  84 FGPNSVIVRSVPALLRQQNLQELIRELLDELAEKGGSSLEESLEELLATMACHSAVRAGRRL 145
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
461-602 4.93e-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: 162.14  E-value: 4.93e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606   461 PIGQMHGTYIFAQNDKGLYMIDQHAAQERINYEYFRDKVGRVAQevQELLVPYRIDLSLTEFLRVEEQLEELKKVGLFLE 540
Cdd:smart00853   1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQAGGLES--QPLLIPVRLELSPQEAALLEEHLELLRQLGFELE 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446438606   541 QFGHQSFIVRSHPTWFPKGQETEIIDEMMEQVVKLKKVDIKKLREEAAIMMSCKASIKANQY 602
Cdd:smart00853  79 IFGPQSLILRSVPALLRQQNLQKLIPELLDLLSDEEENARPSRLEALLASLACRSAIRAGDA 140
 
Name Accession Description Interval E-value
mutL PRK00095
DNA mismatch repair endonuclease MutL;
3-646 0e+00

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 841.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606   3 KIRKLDDQLSNLIAAGEVVERPASVVKELVENSIDANSTSIEIHLEEAGLSKIRIIDNGDGIAEEDCIVAFERHATSKIK 82
Cdd:PRK00095   2 PIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606  83 DENDLFRIRTLGFRGEALPSIASVSELELITSTGDAP-GTHLIIKGGDIIKQEKTASRKGTDITVQNLFFNTPARLKYMK 161
Cdd:PRK00095  82 SLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAeGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKFLK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 162 TIHTELGNITDIVYRIAMSHPEVSLKLFHNEKKLLHTSGNGDVRQVLASIYSIQVAKKLVPIEAESLDFTIKGYVTLPEV 241
Cdd:PRK00095 162 SEKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPTL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 242 TRASRNYMSTIVNGRYVRNFVLMKAIQQGYHTLLPVGRYPIGFLSIEMDPMLVDVNVHPAKLEVRFSKEQELLKLIEETL 321
Cdd:PRK00095 242 SRANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDLIVQAI 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 322 QAAFKKIQLIPDAGVTTKKKEKDESVQEQFQFEHAKPKEPSMPDIILPTGMDEKQEEPQAVKQPAQLWQPPKQEWQPPQS 401
Cdd:PRK00095 322 QEALAQSGLIPAAAGANQVLEPAEPEPLPLQQTPLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSEAAA 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 402 LVREEQSWQPSTKSIIEEPIREEKswnsndedfeleeleeevqeieeiemngNDLPPLYPIGQMHGTYIFAQNDKGLYMI 481
Cdd:PRK00095 402 AASAEAAAAAPAAAPEPAEAAEEA----------------------------DSFPLGYALGQLHGTYILAENEDGLYLV 453
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 482 DQHAAQERINYEYFRDKVGRVAQEVQELLVPYRIDLSLTEFLRVEEQLEELKKVGLFLEQFGHQSFIVRSHPTWFPKGQE 561
Cdd:PRK00095 454 DQHAAHERLLYEQLKDKLAEVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLELEPFGPNSFAVREVPALLGQQEL 533
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 562 TEIIDEMMEQVVKLKKVDIKKLReEAAIMMSCKASIKANQYLTNDQIFALLEELRTTTNPYTCPHGRPILVHHSTYELEK 641
Cdd:PRK00095 534 EELIRDLLDELAEEGDSDTLKER-ELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIELSLSDLEK 612

                 ....*
gi 446438606 642 MFKRV 646
Cdd:PRK00095 613 LFKRI 617
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
1-645 0e+00

DNA mismatch repair ATPase MutL [Replication, recombination and repair];


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 769.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606   1 MGKIRKLDDQLSNLIAAGEVVERPASVVKELVENSIDANSTSIEIHLEEAGLSKIRIIDNGDGIAEEDCIVAFERHATSK 80
Cdd:COG0323    1 MPKIRLLPDELANQIAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLPLAFERHATSK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606  81 IKDENDLFRIRTLGFRGEALPSIASVSELELITSTGDAP-GTHLIIKGGDIIKQEKTASRKGTDITVQNLFFNTPARLKY 159
Cdd:COG0323   81 IRSAEDLFRIRTLGFRGEALASIASVSRLTLTTRTAGAElGTRIEVEGGKVVEVEPAAAPKGTTVEVRDLFFNTPARRKF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 160 MKTIHTELGNITDIVYRIAMSHPEVSLKLFHNEKKLLHTSGNGDVRQVLASIYSIQVAKKLVPIEAESLDFTIKGYVTLP 239
Cdd:COG0323  161 LKSDATELAHITDVVRRLALAHPDIAFTLIHNGREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 240 EVTRASRNYMSTIVNGRYVRNFVLMKAIQQGYHTLLPVGRYPIGFLSIEMDPMLVDVNVHPAKLEVRFSKEQELLKLIEE 319
Cdd:COG0323  241 EFSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRS 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 320 TLQAAFKKiqlipdagvttkkkekdesvqeqfqfehakpkepsmpdiilptgmdekqeepqavkqpaqlwqppkqewqpp 399
Cdd:COG0323  321 AVREALAQ------------------------------------------------------------------------ 328
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 400 qslvreeqswqpstksiieepireekswnsndedfeleeleeevqeieeiemngndlpplYPIGQMHGTYIFAQNDKGLY 479
Cdd:COG0323  329 ------------------------------------------------------------AALGQLHGTYILAENEDGLV 348
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 480 MIDQHAAQERINYEYFRDKVGRVAQEVQELLVPYRIDLSLTEFLRVEEQLEELKKVGLFLEQFGHQSFIVRSHPTWFPKG 559
Cdd:COG0323  349 LIDQHAAHERILYERLKKALAEGGVASQPLLIPETLELSPAEAALLEEHLEELARLGFEIEPFGPNTVAVRAVPALLGEG 428
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 560 QETEIIDEMMEQVVKLKK-VDIKKLREEAAIMMSCKASIKANQYLTNDQIFALLEELRTTTNPYTCPHGRPILVHHSTYE 638
Cdd:COG0323  429 DAEELLRDLLDELAEEGSsESLEELREELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTWIELSLEE 508

                 ....*..
gi 446438606 639 LEKMFKR 645
Cdd:COG0323  509 LEKLFKR 515
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
2-306 7.06e-126

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: 374.67  E-value: 7.06e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606    2 GKIRKLDDQLSNLIAAGEVVERPASVVKELVENSIDANSTSIEIHLEEAGLSKIRIIDNGDGIAEEDCIVAFERHATSKI 81
Cdd:TIGR00585   1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606   82 KDENDLFRIRTLGFRGEALPSIASVSELELITSTGDAPGT--HLIIKGGDIIKQEKTASRKGTDITVQNLFFNTPARLKY 159
Cdd:TIGR00585  81 QSFEDLERIETLGFRGEALASISSVSRLTITTKTSAADGLayQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRKF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606  160 MKTIHTELGNITDIVYRIAMSHPEVSLKLFHNEKKLLHTSG--NGDVRQ-VLASIYSIQVAKKLVPI-EAESLDFTIKGY 235
Cdd:TIGR00585 161 LKSPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLQLSTkpNQSTKEnRIRSVFGTAVLRKLIPLdEWEDLDLQLEGF 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446438606  236 VTLPEVTRASRNY-MSTIVNGRYVRNFVLMKAIQQGYHTLLPVGRYPIGFLSIEMDPMLVDVNVHPAKLEVR 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 6.99e-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: 307.83  E-value: 6.99e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606  11 LSNLIAAGEVVERPASVVKELVENSIDANSTSIEIHLEEAGLSKIRIIDNGDGIAEEDCIVAFERHATSKIKDENDLFRI 90
Cdd:cd16926    1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606  91 RTLGFRGEALPSIASVSELELITSTGDAP-GTHLIIKGGDIIKQEKTASR-KGTDITVQNLFFNTPARLKYMKTIHTELG 168
Cdd:cd16926   81 TTLGFRGEALASIASVSRLTITTRTADDDvGTRLVVDGGGIIEEVKPAAApVGTTVTVRDLFYNTPARRKFLKSPKTELS 160
                        170       180
                 ....*....|....*....|....*...
gi 446438606 169 NITDIVYRIAMSHPEVSLKLFHNEKKLL 196
Cdd:cd16926  161 KILDLVQRLALAHPDVSFSLTHDGKLVL 188
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
462-603 1.44e-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: 190.89  E-value: 1.44e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606  462 IGQMHGTYIFAQNDKGLYMIDQHAAQERINYEYFRDKVGRVAQEVQELLVPYRIDLSLTEFLRVEEQLEELKKVGLFLEQ 541
Cdd:pfam08676   4 LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFELEE 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446438606  542 FGHQSFIVRSHPTWFPKGQETEIIDEMMEQVVKLKKVDIKKLREEAAIMMSCKASIKANQYL 603
Cdd:pfam08676  84 FGPNSVIVRSVPALLRQQNLQELIRELLDELAEKGGSSLEESLEELLATMACHSAVRAGRRL 145
MutL_Trans cd00782
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
204-325 1.20e-48

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: 165.79  E-value: 1.20e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 204 VRQVLASIYSIQVAKKLVPIEAESLDFTIKGYVTLPEVTRASRNYMSTIVNGRYVRNFVLMKAIQQGYHTLLPVGRYPIG 283
Cdd:cd00782    1 LKDRIAQVYGKEVAKNLIEVELESGDFRISGYISKPDFGRSSKDRQFLFVNGRPVRDKLLSKAINEAYRSYLPKGRYPVF 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446438606 284 FLSIEMDPMLVDVNVHPAKLEVRFSKEQELLKLIEETLQAAF 325
Cdd:cd00782   81 VLNLELPPELVDVNVHPTKREVRFSDEEEVLELIREALRSAL 122
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
209-324 1.76e-48

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: 165.36  E-value: 1.76e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606  209 ASIYSIQVAKKLVPIEAESLDFTIKGYVTLPEVTRASRNYMSTIVNGRYVRNFVLMKAIQQGYHTLLPVGRYPIGFLSIE 288
Cdd:pfam01119   1 AAIYGKEFAENLLPIEKEDDGLRLSGYISKPTLSRSNRDYQYLFVNGRPVRDKLLSHAIREAYRDLLPKGRYPVAVLFLE 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 446438606  289 MDPMLVDVNVHPAKLEVRFSKEQELLKLIEETLQAA 324
Cdd:pfam01119  81 IDPELVDVNVHPTKREVRFRDEREVYDFIKEALREA 116
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
461-602 4.93e-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: 162.14  E-value: 4.93e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606   461 PIGQMHGTYIFAQNDKGLYMIDQHAAQERINYEYFRDKVGRVAQevQELLVPYRIDLSLTEFLRVEEQLEELKKVGLFLE 540
Cdd:smart00853   1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQAGGLES--QPLLIPVRLELSPQEAALLEEHLELLRQLGFELE 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446438606   541 QFGHQSFIVRSHPTWFPKGQETEIIDEMMEQVVKLKKVDIKKLREEAAIMMSCKASIKANQY 602
Cdd:smart00853  79 IFGPQSLILRSVPALLRQQNLQKLIPELLDLLSDEEENARPSRLEALLASLACRSAIRAGDA 140
TopoII_MutL_Trans cd00329
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
204-306 3.92e-27

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: 105.81  E-value: 3.92e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 204 VRQVLASIYSIQVAKKLVPIEAESLDFTIKGYVTLPEVTRASRNYMSTIVNGRYVR-NFVLMKAIQQGYHTLL---PVGR 279
Cdd:cd00329    1 LKDRLAEILGDKVADKLIYVEGESDGFRVEGAISYPDSGRSSKDRQFSFVNGRPVReGGTHVKAVREAYTRALngdDVRR 80
                         90       100
                 ....*....|....*....|....*..
gi 446438606 280 YPIGFLSIEMDPMLVDVNVHPAKLEVR 306
Cdd:cd00329   81 YPVAVLSLKIPPSLVDVNVHPTKEEVR 107
MutL_Trans_MutL cd03482
MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
208-307 6.42e-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: 94.19  E-value: 6.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 208 LASIYSIQVAKKLVPIEAESLDFTIKGYVTLPEVTRASRNYMSTIVNGRYVRNFVLMKAIQQGYHTLLPVGRYPIGFLSI 287
Cdd:cd03482    5 LADILGEDFAEQALAIDEEAGGLRLSGWIALPTFARSQADIQYFYVNGRMVRDKLISHAVRQAYSDVLHGGRHPAYVLYL 84
                         90       100
                 ....*....|....*....|
gi 446438606 288 EMDPMLVDVNVHPAKLEVRF 307
Cdd:cd03482   85 ELDPAQVDVNVHPAKHEVRF 104
MutL_Trans_MLH1 cd03483
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
204-322 1.70e-16

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: 76.12  E-value: 1.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 204 VRQVLASIYSIQVAKKLVPIEAESLD----FTIKGYVTLPevtrasrNYMST------IVNGRYVRNFVLMKAIQQGYHT 273
Cdd:cd03483    2 TKDNIRSVYGAAVANELIEVEISDDDddlgFKVKGLISNA-------NYSKKkiifilFINNRLVECSALRRAIENVYAN 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446438606 274 LLPVGRYPIGFLSIEMDPMLVDVNVHPAKLEVRFSKEQELLKLIEETLQ 322
Cdd:cd03483   75 YLPKGAHPFVYLSLEIPPENVDVNVHPTKREVHFLNEEEIIERIQKLVE 123
MutL_Trans_hPMS_2_like cd03484
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
203-325 6.00e-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: 60.74  E-value: 6.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 203 DVRQVLASIYSIQVAKKLVPIE-----------------AESLDFTIKGYVTLPE--VTRASRNYMSTIVNGRYVRNFVL 263
Cdd:cd03484    1 DIKDNIINVFGGKVIKGLIPINleldvnptkeeldsdedLADSEVKITGYISKPShgCGRSSSDRQFFYINGRPVDLKKV 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446438606 264 MKAIQQGYHTLLPVgRYPIGFLSIEMDPMLVDVNVHPAKLEVRFSKEQELLKLIEETLQAAF 325
Cdd:cd03484   81 AKLINEVYKSFNSR-QYPFFILNISLPTSLYDVNVTPDKRTVLLHDEDRLIDTLKTSLSELF 141
MutL_Trans_hPMS_1_like cd03485
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
203-323 2.53e-10

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: 58.82  E-value: 2.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 203 DVRQVLASIYSIQVAKKLVPIEAESLD--FTIKGYVTLPE----VTRASRNYMStiVNGRYV-RNFVLMKAIQQGYHTLL 275
Cdd:cd03485    1 DHKEALARVLGTAVAANMVPVQSTDEDpqISLEGFLPKPGsdvsKTKSDGKFIS--VNSRPVsLGKDIGKLLRQYYSSAY 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446438606 276 PVG---RYPIGFLSIEMDPMLVDVNVHPAKLEVRFSKEQELLKLIEETLQA 323
Cdd:cd03485   79 RKSslrRYPVFFLNILCPPGLVDVNIEPDKDDVLLQNKEAVLQAVENLLES 129
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
24-113 1.76e-09

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: 56.19  E-value: 1.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606   24 PASVVKELVENSIDANSTSIEIHL--EEAGLSKIRIIDNGDGIAEEDCIVAFERHATSKIKDendlFRIRTLGFRGEALP 101
Cdd:pfam13589   1 LEGALAELIDNSIDADATNIKIEVnkNRGGGTEIVIEDDGHGMSPEELINALRLATSAKEAK----RGSTDLGRYGIGLK 76
                          90
                  ....*....|..
gi 446438606  102 SiASVSELELIT 113
Cdd:pfam13589  77 L-ASLSLGAKLT 87
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
19-80 4.33e-08

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: 51.60  E-value: 4.33e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446438606   19 EVVERPASVVKELVENSIDANS--TSIEIHLEEAGLSKIRIIDNGDGIAEEDCIVAFERHATSK 80
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAkaGEITVTLSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTAD 64
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
27-126 2.76e-07

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.


Pssm-ID: 340391 [Multi-domain]  Cd Length: 102  Bit Score: 49.14  E-value: 2.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606  27 VVKELVENSIDANS--TSIEIHLEEAGLS-KIRIIDNGDGIAEEDCIVAFERHATSKIKdendlfriRTLGFRGEALPSI 103
Cdd:cd00075    4 VLSNLLDNALKYSPpgGTIEISLRQEGDGvVLEVEDNGPGIPEEDLERIFERFYRGDKS--------REGGGTGLGLAIV 75
                         90       100
                 ....*....|....*....|....*.
gi 446438606 104 ASVSEL---ELITSTGDAPGTHLIIK 126
Cdd:cd00075   76 RRIVEAhggRITVESEPGGGTTFTVT 101
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
27-75 3.09e-05

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 43.41  E-value: 3.09e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 446438606    27 VVKELVENSIDANSTSIEIHLE---EAGLSKIRIIDNGDGIAEEDCIVAFER 75
Cdd:smart00387   9 VLSNLLDNAIKYTPEGGRITVTlerDGDHVEITVEDNGPGIPPEDLEKIFEP 60
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
28-75 8.76e-04

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: 39.31  E-value: 8.76e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446438606  28 VKELVENSI--DANSTSIEIHLEEAGLSKIRIIDNGDGIAEEDCIVAFER 75
Cdd:cd16940   18 LRNLVDNAVrySPQGSRVEIKLSADDGAVIRVEDNGPGIDEEELEALFER 67
HATPase_TopVIB-like cd16933
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family ...
27-75 1.80e-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: 40.02  E-value: 1.80e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446438606  27 VVKELVENSIDANSTS-------IEIHLEEAGLSKIRIIDNGDGIAEEDCIVAFER 75
Cdd:cd16933   23 TVRELVENSLDATEEAgilpdikVEIEEIGKDHYKVIVEDNGPGIPEEQIPKVFGK 78
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
25-83 1.86e-03

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 40.99  E-value: 1.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446438606  25 ASVVKELVENSIDANST--------SIEIHLEEAGLSkIRIIDNGDGIAEEDCIVAFERHATSKIKD 83
Cdd:COG3290  283 VTILGNLLDNAIEAVEKlpeeerrvELSIRDDGDELV-IEVEDSGPGIPEELLEKIFERGFSTKLGE 348
PRK04184 PRK04184
DNA topoisomerase VI subunit B; Validated
27-68 5.88e-03

DNA topoisomerase VI subunit B; Validated


Pssm-ID: 235246 [Multi-domain]  Cd Length: 535  Bit Score: 39.49  E-value: 5.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446438606  27 VVKELVENSIDANST---------SIEIHLEEAGLSKIRIIDNGDGIAEED 68
Cdd:PRK04184  40 TVKELVDNSLDACEEagilpdikiEIKRVDEGKDHYRVTVEDNGPGIPPEE 90
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
7-80 6.20e-03

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 38.73  E-value: 6.20e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446438606   7 LDDQLSNLIAAGEVVERpasVVKELVENSIDANS--TSIEIHLEEAGLS-KIRIIDNGDGIAEEDCIVAFERHATSK 80
Cdd:COG2205  119 LPPELPLVYADPELLEQ---VLANLLDNAIKYSPpgGTITISARREGDGvRISVSDNGPGIPEEELERIFERFYRGD 192
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
31-80 6.78e-03

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: 39.17  E-value: 6.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446438606  31 LVENSIDANSTSIEIHLE---EAGLSKIRIIDNGDGIAEEDCIVAFERHATSK 80
Cdd:COG5000  325 LLKNAIEAIEEGGEIEVStrrEDGRVRIEVSDNGPGIPEEVLERIFEPFFTTK 377
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
25-80 7.74e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 36.50  E-value: 7.74e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446438606  25 ASVVKELVENSIDANSTS------IEIHL-EEAGLSKIRIIDNGDGIAEEDCIVAFERHATSK 80
Cdd:cd16915    2 ITIVGNLIDNALDALAATgapnkqVEVFLrDEGDDLVIEVRDTGPGIAPELRDKVFERGVSTK 64
MutL_Trans_MLH3 cd03486
MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
203-321 8.93e-03

MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to yeast and human MLH3 (MutL homologue 3). MLH3 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. MLH1 forms heterodimers with MLH3. The MLH1-MLH3 complex plays a role in meiosis. A role for hMLH1-hMLH3 in DNA mismatch repair (MMR) has not been established. 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.


Pssm-ID: 239568 [Multi-domain]  Cd Length: 141  Bit Score: 36.91  E-value: 8.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438606 203 DVRQVLASIYSIQVAKKLVPIEAESLDFTIKGYVTLPEVtrASRNYMSTIVNGRYVRNFVLMKAIQQGY----------- 271
Cdd:cd03486    1 SILSVFKQIYGLVLAQKLKEVSAKFQEYEVSGYISSEGH--YSKSFQFIYVNGRLYLKTRFHKLINKLFrktsavaknks 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446438606 272 ---HTLLPVGR-----YPIGFLSIEMDPMLVDVNVHPAKLEVRFSKEQELLKLIEETL 321
Cdd:cd03486   79 spqSKSSRRGKrsqesYPVFVLNITCPASEYDLSQEPSKTIIEFKDWKTLLPLILEVV 136
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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