NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2093194996|gb|UAJ81857|]
View 

MutL, partial [Bacillus altitudinis]

Protein Classification

DNA mismatch repair MutL family protein( domain architecture ID 1001088)

DNA mismatch repair MutL family protein is required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage, or recombination events

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
mutL super family cl35064
DNA mismatch repair endonuclease MutL;
1-276 8.99e-165

DNA mismatch repair endonuclease MutL;


The actual alignment was detected with superfamily member PRK00095:

Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 470.47  E-value: 8.99e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996   1 IAAGEVVERPASVVKELVENAIDASSTVIEIDVEEAGLSSIRIIDNGVGIDAEDCKLAFQRHATSKIKDENDLFRVRTLG 80
Cdd:PRK00095   14 IAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIASLDDLEAIRTLG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996  81 FRGEALPSIASVSHLEMKTSTGEGA-GTHLALQGGKIISEKKTSGRRGTEIVVTNLFYNTPARLKYMKTVHTELGNISDV 159
Cdd:PRK00095   94 FRGEALPSIASVSRLTLTSRTADAAeGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKFLKSEKTELGHIDDV 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996 160 VNRIALAHPEVSIRLRHQGKVLLQTNGNGDVRHVLAAIYGTAVAKKMLPLHVQSLDFEVKGYISLPEVTRASRNYMSSVV 239
Cdd:PRK00095  174 VNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPTLSRANRDYQYLFV 253

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2093194996 240 NGRYVKHFPLVKAIHEGYHTLLPIGRHPITFIEMKMD 276
Cdd:PRK00095  254 NGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELD 290
 
Name Accession Description Interval E-value
mutL PRK00095
DNA mismatch repair endonuclease MutL;
1-276 8.99e-165

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 470.47  E-value: 8.99e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996   1 IAAGEVVERPASVVKELVENAIDASSTVIEIDVEEAGLSSIRIIDNGVGIDAEDCKLAFQRHATSKIKDENDLFRVRTLG 80
Cdd:PRK00095   14 IAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIASLDDLEAIRTLG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996  81 FRGEALPSIASVSHLEMKTSTGEGA-GTHLALQGGKIISEKKTSGRRGTEIVVTNLFYNTPARLKYMKTVHTELGNISDV 159
Cdd:PRK00095   94 FRGEALPSIASVSRLTLTSRTADAAeGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKFLKSEKTELGHIDDV 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996 160 VNRIALAHPEVSIRLRHQGKVLLQTNGNGDVRHVLAAIYGTAVAKKMLPLHVQSLDFEVKGYISLPEVTRASRNYMSSVV 239
Cdd:PRK00095  174 VNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPTLSRANRDYQYLFV 253

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2093194996 240 NGRYVKHFPLVKAIHEGYHTLLPIGRHPITFIEMKMD 276
Cdd:PRK00095  254 NGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELD 290
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
1-276 1.21e-161

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 458.74  E-value: 1.21e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996   1 IAAGEVVERPASVVKELVENAIDASSTVIEIDVEEAGLSSIRIIDNGVGIDAEDCKLAFQRHATSKIKDENDLFRVRTLG 80
Cdd:COG0323    15 IAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLPLAFERHATSKIRSAEDLFRIRTLG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996  81 FRGEALPSIASVSHLEMKTST-GEGAGTHLALQGGKIISEKKTSGRRGTEIVVTNLFYNTPARLKYMKTVHTELGNISDV 159
Cdd:COG0323    95 FRGEALASIASVSRLTLTTRTaGAELGTRIEVEGGKVVEVEPAAAPKGTTVEVRDLFFNTPARRKFLKSDATELAHITDV 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996 160 VNRIALAHPEVSIRLRHQGKVLLQTNGNGDVRHVLAAIYGTAVAKKMLPLHVQSLDFEVKGYISLPEVTRASRNYMSSVV 239
Cdd:COG0323   175 VRRLALAHPDIAFTLIHNGREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKPEFSRSNRDYQYFFV 254

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2093194996 240 NGRYVKHFPLVKAIHEGYHTLLPIGRHPITFIEMKMD 276
Cdd:COG0323   255 NGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELD 291
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 1-276 6.73e-118

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: 340.39  E-value: 6.73e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996   1 IAAGEVVERPASVVKELVENAIDASSTVIEIDVEEAGLSSIRIIDNGVGIDAEDCKLAFQRHATSKIKDENDLFRVRTLG 80
Cdd:TIGR00585  14 IAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKIQSFEDLERIETLG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996  81 FRGEALPSIASVSHLEMKTSTGEGAGT--HLALQGGKIISEKKTSGRRGTEIVVTNLFYNTPARLKYMKTVHTELGNISD 158
Cdd:TIGR00585  94 FRGEALASISSVSRLTITTKTSAADGLayQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRKFLKSPKKEFRKILD 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996 159 VVNRIALAHPEVSIRLRHQGKVLLQ--TNGNGDVRH-VLAAIYGTAVAKKMLPLH-VQSLDFEVKGYISLPEVTRASRNY 234
Cdd:TIGR00585 174 VLQRYALIHPDISFSLTHDGKKVLQlsTKPNQSTKEnRIRSVFGTAVLRKLIPLDeWEDLDLQLEGFISQPNVTRSRRSG 253

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2093194996 235 -MSSVVNGRYVKHFPLVKAIHEGYHTLLPIGRHPITFIEMKMD 276
Cdd:TIGR00585 254 wQFLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEID 296
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 1-182 1.00e-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: 297.04  E-value: 1.00e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996   1 IAAGEVVERPASVVKELVENAIDASSTVIEIDVEEAGLSSIRIIDNGVGIDAEDCKLAFQRHATSKIKDENDLFRVRTLG 80
Cdd:cd16926     5 IAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSITTLG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996  81 FRGEALPSIASVSHLEMKTST--GEGAGTHLALQGGKIISEKKTSGRRGTEIVVTNLFYNTPARLKYMKTVHTELGNISD 158
Cdd:cd16926    85 FRGEALASIASVSRLTITTRTadDDVGTRLVVDGGGIIEEVKPAAAPVGTTVTVRDLFYNTPARRKFLKSPKTELSKILD 164

                         170       180
                  ....*....|....*....|....
gi 2093194996 159 VVNRIALAHPEVSIRLRHQGKVLL 182
Cdd:cd16926   165 LVQRLALAHPDVSFSLTHDGKLVL 188
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 195-276 8.90e-27

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: 100.65  E-value: 8.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996 195 AAIYGTAVAKKMLPLHVQSLDFEVKGYISLPEVTRASRNYMSSVVNGRYVKHFPLVKAIHEGYHTLLPIGRHPITFIEMK 274
Cdd:pfam01119   1 AAIYGKEFAENLLPIEKEDDGLRLSGYISKPTLSRSNRDYQYLFVNGRPVRDKLLSHAIREAYRDLLPKGRYPVAVLFLE 80


                  ..
gi 2093194996 275 MD 276
Cdd:pfam01119  81 ID 82
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 13-61 3.48e-07

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 47.64  E-value: 3.48e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2093194996   13 VVKELVENAIDASSTVIEIDVE---EAGLSSIRIIDNGVGIDAEDCKLAFQR 61
Cdd:smart00387   9 VLSNLLDNAIKYTPEGGRITVTlerDGDHVEITVEDNGPGIPPEDLEKIFEP 60
 
Name Accession Description Interval E-value
mutL PRK00095
DNA mismatch repair endonuclease MutL;
1-276 8.99e-165

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 470.47  E-value: 8.99e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996   1 IAAGEVVERPASVVKELVENAIDASSTVIEIDVEEAGLSSIRIIDNGVGIDAEDCKLAFQRHATSKIKDENDLFRVRTLG 80
Cdd:PRK00095   14 IAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIASLDDLEAIRTLG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996  81 FRGEALPSIASVSHLEMKTSTGEGA-GTHLALQGGKIISEKKTSGRRGTEIVVTNLFYNTPARLKYMKTVHTELGNISDV 159
Cdd:PRK00095   94 FRGEALPSIASVSRLTLTSRTADAAeGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKFLKSEKTELGHIDDV 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996 160 VNRIALAHPEVSIRLRHQGKVLLQTNGNGDVRHVLAAIYGTAVAKKMLPLHVQSLDFEVKGYISLPEVTRASRNYMSSVV 239
Cdd:PRK00095  174 VNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPTLSRANRDYQYLFV 253

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2093194996 240 NGRYVKHFPLVKAIHEGYHTLLPIGRHPITFIEMKMD 276
Cdd:PRK00095  254 NGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELD 290
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
1-276 1.21e-161

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 458.74  E-value: 1.21e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996   1 IAAGEVVERPASVVKELVENAIDASSTVIEIDVEEAGLSSIRIIDNGVGIDAEDCKLAFQRHATSKIKDENDLFRVRTLG 80
Cdd:COG0323    15 IAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLPLAFERHATSKIRSAEDLFRIRTLG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996  81 FRGEALPSIASVSHLEMKTST-GEGAGTHLALQGGKIISEKKTSGRRGTEIVVTNLFYNTPARLKYMKTVHTELGNISDV 159
Cdd:COG0323    95 FRGEALASIASVSRLTLTTRTaGAELGTRIEVEGGKVVEVEPAAAPKGTTVEVRDLFFNTPARRKFLKSDATELAHITDV 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996 160 VNRIALAHPEVSIRLRHQGKVLLQTNGNGDVRHVLAAIYGTAVAKKMLPLHVQSLDFEVKGYISLPEVTRASRNYMSSVV 239
Cdd:COG0323   175 VRRLALAHPDIAFTLIHNGREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKPEFSRSNRDYQYFFV 254

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2093194996 240 NGRYVKHFPLVKAIHEGYHTLLPIGRHPITFIEMKMD 276
Cdd:COG0323   255 NGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELD 291
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 1-276 6.73e-118

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: 340.39  E-value: 6.73e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996   1 IAAGEVVERPASVVKELVENAIDASSTVIEIDVEEAGLSSIRIIDNGVGIDAEDCKLAFQRHATSKIKDENDLFRVRTLG 80
Cdd:TIGR00585  14 IAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKIQSFEDLERIETLG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996  81 FRGEALPSIASVSHLEMKTSTGEGAGT--HLALQGGKIISEKKTSGRRGTEIVVTNLFYNTPARLKYMKTVHTELGNISD 158
Cdd:TIGR00585  94 FRGEALASISSVSRLTITTKTSAADGLayQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRKFLKSPKKEFRKILD 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996 159 VVNRIALAHPEVSIRLRHQGKVLLQ--TNGNGDVRH-VLAAIYGTAVAKKMLPLH-VQSLDFEVKGYISLPEVTRASRNY 234
Cdd:TIGR00585 174 VLQRYALIHPDISFSLTHDGKKVLQlsTKPNQSTKEnRIRSVFGTAVLRKLIPLDeWEDLDLQLEGFISQPNVTRSRRSG 253

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2093194996 235 -MSSVVNGRYVKHFPLVKAIHEGYHTLLPIGRHPITFIEMKMD 276
Cdd:TIGR00585 254 wQFLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEID 296
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 1-182 1.00e-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: 297.04  E-value: 1.00e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996   1 IAAGEVVERPASVVKELVENAIDASSTVIEIDVEEAGLSSIRIIDNGVGIDAEDCKLAFQRHATSKIKDENDLFRVRTLG 80
Cdd:cd16926     5 IAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSITTLG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996  81 FRGEALPSIASVSHLEMKTST--GEGAGTHLALQGGKIISEKKTSGRRGTEIVVTNLFYNTPARLKYMKTVHTELGNISD 158
Cdd:cd16926    85 FRGEALASIASVSRLTITTRTadDDVGTRLVVDGGGIIEEVKPAAAPVGTTVTVRDLFYNTPARRKFLKSPKTELSKILD 164

                         170       180
                  ....*....|....*....|....
gi 2093194996 159 VVNRIALAHPEVSIRLRHQGKVLL 182
Cdd:cd16926   165 LVQRLALAHPDVSFSLTHDGKLVL 188
MutL_Trans cd00782
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 190-276 1.07e-27

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: 103.39  E-value: 1.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996 190 VRHVLAAIYGTAVAKKMLPLHVQSLDFEVKGYISLPEVTRASRNYMSSVVNGRYVKHFPLVKAIHEGYHTLLPIGRHPIT 269
Cdd:cd00782     1 LKDRIAQVYGKEVAKNLIEVELESGDFRISGYISKPDFGRSSKDRQFLFVNGRPVRDKLLSKAINEAYRSYLPKGRYPVF 80


                  ....*..
gi 2093194996 270 FIEMKMD 276
Cdd:cd00782    81 VLNLELP 87
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 195-276 8.90e-27

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: 100.65  E-value: 8.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996 195 AAIYGTAVAKKMLPLHVQSLDFEVKGYISLPEVTRASRNYMSSVVNGRYVKHFPLVKAIHEGYHTLLPIGRHPITFIEMK 274
Cdd:pfam01119   1 AAIYGKEFAENLLPIEKEDDGLRLSGYISKPTLSRSNRDYQYLFVNGRPVRDKLLSHAIREAYRDLLPKGRYPVAVLFLE 80


                  ..
gi 2093194996 275 MD 276
Cdd:pfam01119  81 ID 82
TopoII_MutL_Trans cd00329
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 190-276 3.60e-16

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: 72.29  E-value: 3.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996 190 VRHVLAAIYGTAVAKKMLPLHVQSLDFEVKGYISLPEVTRASRNYMSSVVNGRYV-KHFPLVKAIHEGYHTLL---PIGR 265
Cdd:cd00329     1 LKDRLAEILGDKVADKLIYVEGESDGFRVEGAISYPDSGRSSKDRQFSFVNGRPVrEGGTHVKAVREAYTRALngdDVRR 80

                          90
                  ....*....|.
gi 2093194996 266 HPITFIEMKMD 276
Cdd:cd00329    81 YPVAVLSLKIP 91
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 5-66 2.49e-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: 50.83  E-value: 2.49e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2093194996   5 EVVERPASVVKELVENAIDASS--TVIEIDVEEAGLSSIRIIDNGVGIDAEDCKLAFQRHATSK 66
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAkaGEITVTLSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTAD 64
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 13-61 3.48e-07

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 47.64  E-value: 3.48e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2093194996   13 VVKELVENAIDASSTVIEIDVE---EAGLSSIRIIDNGVGIDAEDCKLAFQR 61
Cdd:smart00387   9 VLSNLLDNAIKYTPEGGRITVTlerDGDHVEITVEDNGPGIPPEDLEKIFEP 60
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
 10-66 4.72e-07

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: 48.10  E-value: 4.72e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2093194996  10 PASVVKELVENAIDASSTVIEIDV--EEAGLSSIRIIDNGVGIDAEDCKLAFQRHATSK 66
Cdd:pfam13589   1 LEGALAELIDNSIDADATNIKIEVnkNRGGGTEIVIEDDGHGMSPEELINALRLATSAK 59
MutL_Trans_MutL cd03482
MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 194-267 5.87e-07

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: 47.58  E-value: 5.87e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2093194996 194 LAAIYGTAVAKKMLPLHVQSLDFEVKGYISLPEVTRASRNYMSSVVNGRYVKHFPLVKAIHEGYHTLLPIGRHP 267
Cdd:cd03482     5 LADILGEDFAEQALAIDEEAGGLRLSGWIALPTFARSQADIQYFYVNGRMVRDKLISHAVRQAYSDVLHGGRHP 78
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 14-61 3.41e-05

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: 42.01  E-value: 3.41e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2093194996  14 VKELVENAIDAS--STVIEIDVEEAGLSSIRIIDNGVGIDAEDCKLAFQR 61
Cdd:cd16940    18 LRNLVDNAVRYSpqGSRVEIKLSADDGAVIRVEDNGPGIDEEELEALFER 67
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
13-66 5.94e-05

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 43.36  E-value: 5.94e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2093194996  13 VVKELVENAIDASS--TVIEIDVEEAGLS-SIRIIDNGVGIDAEDCKLAFQRHATSK 66
Cdd:COG2205   136 VLANLLDNAIKYSPpgGTITISARREGDGvRISVSDNGPGIPEEELERIFERFYRGD 192
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 17-66 1.03e-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: 43.03  E-value: 1.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2093194996  17 LVENAIDASSTVIEIDVE---EAGLSSIRIIDNGVGIDAEDCKLAFQRHATSK 66
Cdd:COG5000   325 LLKNAIEAIEEGGEIEVStrrEDGRVRIEVSDNGPGIPEEVLERIFEPFFTTK 377
MutL_Trans_MLH1 cd03483
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 190-273 1.21e-04

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: 41.07  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996 190 VRHVLAAIYGTAVAKKMLPLHVQSLD----FEVKGYISLPevtrasrNYMSS------VVNGRYVKHFPLVKAIHEGYHT 259
Cdd:cd03483     2 TKDNIRSVYGAAVANELIEVEISDDDddlgFKVKGLISNA-------NYSKKkiifilFINNRLVECSALRRAIENVYAN 74

                          90
                  ....*....|....
gi 2093194996 260 LLPIGRHPitFIEM 273
Cdd:cd03483    75 YLPKGAHP--FVYL 86
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
13-66 1.31e-04

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 42.59  E-value: 1.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2093194996  13 VVKELVENAIDASS--TVIEIDVE-EAGLSSIRIIDNGVGIDAEDCKLAFQRHATSK 66
Cdd:COG0642   227 VLLNLLSNAIKYTPegGTVTVSVRrEGDRVRISVEDTGPGIPPEDLERIFEPFFRTD 283
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 11-69 1.71e-04

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 42.53  E-value: 1.71e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2093194996  11 ASVVKELVENAIDASSTV------IEIDV-EEAGLSSIRIIDNGVGIDAEDCKLAFQRHATSKIKD 69
Cdd:COG3290   283 VTILGNLLDNAIEAVEKLpeeerrVELSIrDDGDELVIEVEDSGPGIPEELLEKIFERGFSTKLGE 348
HATPase_TopVIB-like cd16933
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family ...
 13-61 6.35e-04

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: 6.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2093194996  13 VVKELVENAIDASSTV-----IEIDVEEAGLS--SIRIIDNGVGIDAEDCKLAFQR 61
Cdd:cd16933    23 TVRELVENSLDATEEAgilpdIKVEIEEIGKDhyKVIVEDNGPGIPEEQIPKVFGK 78
PRK04184 PRK04184
DNA topoisomerase VI subunit B; Validated
 13-59 2.12e-03

DNA topoisomerase VI subunit B; Validated


Pssm-ID: 235246 [Multi-domain]  Cd Length: 535  Bit Score: 39.10  E-value: 2.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2093194996  13 VVKELVENAIDASSTV-----IEIDVEEAGLS----SIRIIDNGVGIDAEDCKLAF 59
Cdd:PRK04184   40 TVKELVDNSLDACEEAgilpdIKIEIKRVDEGkdhyRVTVEDNGPGIPPEEIPKVF 95
MutL_Trans_hPMS_2_like cd03484
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 189-276 4.68e-03

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: 36.48  E-value: 4.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093194996 189 DVRHVLAAIYGTAVAKKMLPLHV-----------------QSLDFEVKGYISLPE--VTRASRNYMSSVVNGRYVKHFPL 249
Cdd:cd03484     1 DIKDNIINVFGGKVIKGLIPINLeldvnptkeeldsdedlADSEVKITGYISKPShgCGRSSSDRQFFYINGRPVDLKKV 80

                          90       100
                  ....*....|....*....|....*....
gi 2093194996 250 VKAIHEGYHTLlpiGRH--PITFIEMKMD 276
Cdd:cd03484    81 AKLINEVYKSF---NSRqyPFFILNISLP 106
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 13-66 8.67e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds.


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 35.34  E-value: 8.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2093194996  13 VVKELVENAIDASSTV--IEIDVEEAGLSSI-RIIDNGVGIDAEDCKLAFQRHATSK 66
Cdd:cd16948     9 IIGQIVSNALKYSKQGgkIEIYSETNEQGVVlSIKDFGIGIPEEDLPRVFDKGFTGE 65
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH