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Conserved domains on  [gi|1868342801|ref|XP_035299904|]
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DNA mismatch repair protein Mlh1 isoform X2 [Cricetulus griseus]

Protein Classification

TopoII/MutL transducer domain-containing protein( domain architecture ID 10855691)

TopoII/MutL transducer domain-containing protein similar to the C-terminal domains of of type II DNA topoisomerases (Topo II) and DNA mismatch repair (MutL/MLH1/PMS2) proteins; the 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Mlh1_C pfam16413
DNA mismatch repair protein Mlh1 C-terminus; This is the C-terminal domain of DNA mismatch ...
 358-612 8.74e-137

DNA mismatch repair protein Mlh1 C-terminus; This is the C-terminal domain of DNA mismatch repair protein Mlh1, these proteins belong to the MutL family. This domain forms part of the endonuclease active site.


:

Pssm-ID: 465109  Cd Length: 260  Bit Score: 399.22  E-value: 8.74e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801 358 NLTSVLSLQEEINERGHETLREMLRNHSFVGCVNPQ--WALAQHQTKLYLLNTTKLSEELFYQILIYDFANFGVLRLSEP 435
Cdd:pfam16413   1 RLTSIKELRAEVEESMHKELTEIFANHTFVGCVDERrrLALIQHGTKLYLVDYGALSEELFYQIGLTDFGNFGRIRLSPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801 436 APLFDLAMLALDSPESGWTEEDGPKEGLAEYIVEFLKKKAEMLADYFSLEIDEEGNLIGLPLLIDNYVPPLEGLPLFILR 515
Cdd:pfam16413  81 LSLYELLELALESEESGWTEEDGPKEELAEKIVELLIEKAEMLEEYFSIEIDEDGNLESLPLLLKGYTPNLDKLPLFLLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801 516 LATEVNWDEEKECFESLSKECAVFYSVRKQYILEESTLSGQQSDMPGSTP----KPWKWTVEHIIYKAFRSHLLPPKHFT 591
Cdd:pfam16413 161 LATEVDWDDEKECFETFLRELALFYSPEPLPPPSNDESNDDEDEEEDEEIearrEEWKWVIEHVLFPAIKRRLLPPKSLL 240

                         250       260
                  ....*....|....*....|.
gi 1868342801 592 EDGnVLQLANLPDLYKVFERC 612
Cdd:pfam16413 241 KDT-VVQVANLPDLYKVFERC 260
MutL_Trans_MLH1 cd03483
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 72-196 8.54e-75

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: 234.44  E-value: 8.54e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801  72 TTVDNIRSIFGSAVSRELIEVGCEDKT--LAFKMNGYISNANYSVKKCIFLLFINHRLVESTALRKAIETVYAAYLPKNT 149
Cdd:cd03483     1 STKDNIRSVYGAAVANELIEVEISDDDddLGFKVKGLISNANYSKKKIIFILFINNRLVECSALRRAIENVYANYLPKGA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1868342801 150 HPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQHVEGKLL 196
Cdd:cd03483    81 HPFVYLSLEIPPENVDVNVHPTKREVHFLNEEEIIERIQKLVEDKLS 127
 
Name Accession Description Interval E-value
Mlh1_C pfam16413
DNA mismatch repair protein Mlh1 C-terminus; This is the C-terminal domain of DNA mismatch ...
 358-612 8.74e-137

DNA mismatch repair protein Mlh1 C-terminus; This is the C-terminal domain of DNA mismatch repair protein Mlh1, these proteins belong to the MutL family. This domain forms part of the endonuclease active site.


Pssm-ID: 465109  Cd Length: 260  Bit Score: 399.22  E-value: 8.74e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801 358 NLTSVLSLQEEINERGHETLREMLRNHSFVGCVNPQ--WALAQHQTKLYLLNTTKLSEELFYQILIYDFANFGVLRLSEP 435
Cdd:pfam16413   1 RLTSIKELRAEVEESMHKELTEIFANHTFVGCVDERrrLALIQHGTKLYLVDYGALSEELFYQIGLTDFGNFGRIRLSPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801 436 APLFDLAMLALDSPESGWTEEDGPKEGLAEYIVEFLKKKAEMLADYFSLEIDEEGNLIGLPLLIDNYVPPLEGLPLFILR 515
Cdd:pfam16413  81 LSLYELLELALESEESGWTEEDGPKEELAEKIVELLIEKAEMLEEYFSIEIDEDGNLESLPLLLKGYTPNLDKLPLFLLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801 516 LATEVNWDEEKECFESLSKECAVFYSVRKQYILEESTLSGQQSDMPGSTP----KPWKWTVEHIIYKAFRSHLLPPKHFT 591
Cdd:pfam16413 161 LATEVDWDDEKECFETFLRELALFYSPEPLPPPSNDESNDDEDEEEDEEIearrEEWKWVIEHVLFPAIKRRLLPPKSLL 240

                         250       260
                  ....*....|....*....|.
gi 1868342801 592 EDGnVLQLANLPDLYKVFERC 612
Cdd:pfam16413 241 KDT-VVQVANLPDLYKVFERC 260
MutL_Trans_MLH1 cd03483
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 72-196 8.54e-75

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: 234.44  E-value: 8.54e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801  72 TTVDNIRSIFGSAVSRELIEVGCEDKT--LAFKMNGYISNANYSVKKCIFLLFINHRLVESTALRKAIETVYAAYLPKNT 149
Cdd:cd03483     1 STKDNIRSVYGAAVANELIEVEISDDDddLGFKVKGLISNANYSKKKIIFILFINNRLVECSALRRAIENVYANYLPKGA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1868342801 150 HPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQHVEGKLL 196
Cdd:cd03483    81 HPFVYLSLEIPPENVDVNVHPTKREVHFLNEEEIIERIQKLVEDKLS 127
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 78-195 2.80e-41

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: 145.33  E-value: 2.80e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801  78 RSIFGSAVSRELIEVGCEDKTlaFKMNGYISNANYS-VKKCIFLLFINHRLVESTALRKAIETVYAAYLPKNTHPFLYLS 156
Cdd:pfam01119   1 AAIYGKEFAENLLPIEKEDDG--LRLSGYISKPTLSrSNRDYQYLFVNGRPVRDKLLSHAIREAYRDLLPKGRYPVAVLF 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1868342801 157 LEISPQNVDVNVHPTKHEVHFLHEESILERVQQHVEGKL 195
Cdd:pfam01119  79 LEIDPELVDVNVHPTKREVRFRDEREVYDFIKEALREAL 117
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 43-176 1.92e-39

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: 147.02  E-value: 1.92e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801  43 RYSIHNSGISFSVKKQGETVADIRTLPNATTVDN-IRSIFGSAVSRELIEVGcEDKTLAFKMNGYISNANYSVKKCI--F 119
Cdd:TIGR00585 177 RYALIHPDISFSLTHDGKKVLQLSTKPNQSTKENrIRSVFGTAVLRKLIPLD-EWEDLDLQLEGFISQPNVTRSRRSgwQ 255

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1868342801 120 LLFINHRLVESTALRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVH 176
Cdd:TIGR00585 256 FLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
43-189 3.03e-30

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 124.77  E-value: 3.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801  43 RYSIHNSGISFSVKKQGETVadIRTLPNATTVDNIRSIFGSAVSRELIEVgcEDKTLAFKMNGYISNANY--SVKKCIFL 120
Cdd:COG0323   177 RLALAHPDIAFTLIHNGREV--FQLPGAGDLLQRIAAIYGREFAENLLPV--EAEREGLRLSGYIGKPEFsrSNRDYQYF 252

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1868342801 121 lFINHRLVESTALRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQ 189
Cdd:COG0323   253 -FVNGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRS 320
mutL PRK00095
DNA mismatch repair endonuclease MutL;
51-295 1.70e-23

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 104.91  E-value: 1.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801  51 ISFSVKKQGETVadIRTLPNATTVDNIRSIFGSAVSRELIEVGCEDktLAFKMNGYI-------SNANYsvkkcIFLlFI 123
Cdd:PRK00095  184 VAFTLTHNGKLV--LQTRGAGQLLQRLAAILGREFAENALPIDAEH--GDLRLSGYVglptlsrANRDY-----QYL-FV 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801 124 NHRLVESTALRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQHVEGKLLGSNSSRM 203
Cdd:PRK00095  254 NGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDLIVQAIQEALAQSGLIPA 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801 204 YFTQTLLPGLAGPSGEVVKSTVGVASSSASGSGDKVYAYQMVRTDSRDQKLDAFLQPVSKVLPSPPQEPVQEDRTDMQKD 283
Cdd:PRK00095  334 AAGANQVLEPAEPEPLPLQQTPLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSEAAAAASAEAAAAAPA 413

                         250
                  ....*....|..
gi 1868342801 284 VEMLELPIPSEA 295
Cdd:PRK00095  414 AAPEPAEAAEEA 425
 
Name Accession Description Interval E-value
Mlh1_C pfam16413
DNA mismatch repair protein Mlh1 C-terminus; This is the C-terminal domain of DNA mismatch ...
 358-612 8.74e-137

DNA mismatch repair protein Mlh1 C-terminus; This is the C-terminal domain of DNA mismatch repair protein Mlh1, these proteins belong to the MutL family. This domain forms part of the endonuclease active site.


Pssm-ID: 465109  Cd Length: 260  Bit Score: 399.22  E-value: 8.74e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801 358 NLTSVLSLQEEINERGHETLREMLRNHSFVGCVNPQ--WALAQHQTKLYLLNTTKLSEELFYQILIYDFANFGVLRLSEP 435
Cdd:pfam16413   1 RLTSIKELRAEVEESMHKELTEIFANHTFVGCVDERrrLALIQHGTKLYLVDYGALSEELFYQIGLTDFGNFGRIRLSPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801 436 APLFDLAMLALDSPESGWTEEDGPKEGLAEYIVEFLKKKAEMLADYFSLEIDEEGNLIGLPLLIDNYVPPLEGLPLFILR 515
Cdd:pfam16413  81 LSLYELLELALESEESGWTEEDGPKEELAEKIVELLIEKAEMLEEYFSIEIDEDGNLESLPLLLKGYTPNLDKLPLFLLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801 516 LATEVNWDEEKECFESLSKECAVFYSVRKQYILEESTLSGQQSDMPGSTP----KPWKWTVEHIIYKAFRSHLLPPKHFT 591
Cdd:pfam16413 161 LATEVDWDDEKECFETFLRELALFYSPEPLPPPSNDESNDDEDEEEDEEIearrEEWKWVIEHVLFPAIKRRLLPPKSLL 240

                         250       260
                  ....*....|....*....|.
gi 1868342801 592 EDGnVLQLANLPDLYKVFERC 612
Cdd:pfam16413 241 KDT-VVQVANLPDLYKVFERC 260
MutL_Trans_MLH1 cd03483
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 72-196 8.54e-75

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: 234.44  E-value: 8.54e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801  72 TTVDNIRSIFGSAVSRELIEVGCEDKT--LAFKMNGYISNANYSVKKCIFLLFINHRLVESTALRKAIETVYAAYLPKNT 149
Cdd:cd03483     1 STKDNIRSVYGAAVANELIEVEISDDDddLGFKVKGLISNANYSKKKIIFILFINNRLVECSALRRAIENVYANYLPKGA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1868342801 150 HPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQHVEGKLL 196
Cdd:cd03483    81 HPFVYLSLEIPPENVDVNVHPTKREVHFLNEEEIIERIQKLVEDKLS 127
MutL_Trans cd00782
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 75-195 6.66e-44

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: 152.70  E-value: 6.66e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801  75 DNIRSIFGSAVSRELIEVGCEDKTlaFKMNGYISNANYSV-KKCIFLLFINHRLVESTALRKAIETVYAAYLPKNTHPFL 153
Cdd:cd00782     3 DRIAQVYGKEVAKNLIEVELESGD--FRISGYISKPDFGRsSKDRQFLFVNGRPVRDKLLSKAINEAYRSYLPKGRYPVF 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1868342801 154 YLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQHVEGKL 195
Cdd:cd00782    81 VLNLELPPELVDVNVHPTKREVRFSDEEEVLELIREALRSAL 122
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 78-195 2.80e-41

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: 145.33  E-value: 2.80e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801  78 RSIFGSAVSRELIEVGCEDKTlaFKMNGYISNANYS-VKKCIFLLFINHRLVESTALRKAIETVYAAYLPKNTHPFLYLS 156
Cdd:pfam01119   1 AAIYGKEFAENLLPIEKEDDG--LRLSGYISKPTLSrSNRDYQYLFVNGRPVRDKLLSHAIREAYRDLLPKGRYPVAVLF 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1868342801 157 LEISPQNVDVNVHPTKHEVHFLHEESILERVQQHVEGKL 195
Cdd:pfam01119  79 LEIDPELVDVNVHPTKREVRFRDEREVYDFIKEALREAL 117
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 43-176 1.92e-39

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: 147.02  E-value: 1.92e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801  43 RYSIHNSGISFSVKKQGETVADIRTLPNATTVDN-IRSIFGSAVSRELIEVGcEDKTLAFKMNGYISNANYSVKKCI--F 119
Cdd:TIGR00585 177 RYALIHPDISFSLTHDGKKVLQLSTKPNQSTKENrIRSVFGTAVLRKLIPLD-EWEDLDLQLEGFISQPNVTRSRRSgwQ 255

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1868342801 120 LLFINHRLVESTALRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVH 176
Cdd:TIGR00585 256 FLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
43-189 3.03e-30

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 124.77  E-value: 3.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801  43 RYSIHNSGISFSVKKQGETVadIRTLPNATTVDNIRSIFGSAVSRELIEVgcEDKTLAFKMNGYISNANY--SVKKCIFL 120
Cdd:COG0323   177 RLALAHPDIAFTLIHNGREV--FQLPGAGDLLQRIAAIYGREFAENLLPV--EAEREGLRLSGYIGKPEFsrSNRDYQYF 252

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1868342801 121 lFINHRLVESTALRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQ 189
Cdd:COG0323   253 -FVNGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRS 320
mutL PRK00095
DNA mismatch repair endonuclease MutL;
51-295 1.70e-23

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 104.91  E-value: 1.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801  51 ISFSVKKQGETVadIRTLPNATTVDNIRSIFGSAVSRELIEVGCEDktLAFKMNGYI-------SNANYsvkkcIFLlFI 123
Cdd:PRK00095  184 VAFTLTHNGKLV--LQTRGAGQLLQRLAAILGREFAENALPIDAEH--GDLRLSGYVglptlsrANRDY-----QYL-FV 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801 124 NHRLVESTALRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQHVEGKLLGSNSSRM 203
Cdd:PRK00095  254 NGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDLIVQAIQEALAQSGLIPA 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801 204 YFTQTLLPGLAGPSGEVVKSTVGVASSSASGSGDKVYAYQMVRTDSRDQKLDAFLQPVSKVLPSPPQEPVQEDRTDMQKD 283
Cdd:PRK00095  334 AAGANQVLEPAEPEPLPLQQTPLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSEAAAAASAEAAAAAPA 413

                         250
                  ....*....|..
gi 1868342801 284 VEMLELPIPSEA 295
Cdd:PRK00095  414 AAPEPAEAAEEA 425
TopoII_MutL_Trans cd00329
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 75-176 1.28e-22

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: 92.71  E-value: 1.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801  75 DNIRSIFGSAVSRELIEVGCEDKTlaFKMNGYISNANYSV-KKCIFLLFINHRLV-ESTALRKAIETVYAAYL---PKNT 149
Cdd:cd00329     3 DRLAEILGDKVADKLIYVEGESDG--FRVEGAISYPDSGRsSKDRQFSFVNGRPVrEGGTHVKAVREAYTRALngdDVRR 80

                          90       100
                  ....*....|....*....|....*..
gi 1868342801 150 HPFLYLSLEISPQNVDVNVHPTKHEVH 176
Cdd:cd00329    81 YPVAVLSLKIPPSLVDVNVHPTKEEVR 107
MutL_Trans_MutL cd03482
MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 77-177 3.85e-14

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: 69.15  E-value: 3.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801  77 IRSIFGSAVSRELIEVGCEDKTLafKMNGYISNANYS-VKKCIFLLFINHRLVE----STALRKAietvYAAYLPKNTHP 151
Cdd:cd03482     5 LADILGEDFAEQALAIDEEAGGL--RLSGWIALPTFArSQADIQYFYVNGRMVRdkliSHAVRQA----YSDVLHGGRHP 78

                          90       100
                  ....*....|....*....|....*.
gi 1868342801 152 FLYLSLEISPQNVDVNVHPTKHEVHF 177
Cdd:cd03482    79 AYVLYLELDPAQVDVNVHPAKHEVRF 104
MutL_Trans_hPMS_2_like cd03484
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 75-189 9.29e-13

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: 65.75  E-value: 9.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801  75 DNIRSIFGSAVSRELIEV---------------GCEDKTLAFKMNGYISnanysvkKCIF----------LLFINHRLVE 129
Cdd:cd03484     4 DNIINVFGGKVIKGLIPInleldvnptkeeldsDEDLADSEVKITGYIS-------KPSHgcgrsssdrqFFYINGRPVD 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801 130 STALRKAIETVYAAYlPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQ 189
Cdd:cd03484    77 LKKVAKLINEVYKSF-NSRQYPFFILNISLPTSLYDVNVTPDKRTVLLHDEDRLIDTLKT 135
MutL_Trans_hPMS_1_like cd03485
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 79-192 8.50e-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: 56.89  E-value: 8.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801  79 SIFGSAVSRELIEVGCEDKTLAFKMNGYI--SNANYSVKKCIF-LLFINHRLVEST-ALRKAIETVYAAYLPKNT---HP 151
Cdd:cd03485     8 RVLGTAVAANMVPVQSTDEDPQISLEGFLpkPGSDVSKTKSDGkFISVNSRPVSLGkDIGKLLRQYYSSAYRKSSlrrYP 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1868342801 152 FLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQHVE 192
Cdd:cd03485    88 VFFLNILCPPGLVDVNIEPDKDDVLLQNKEAVLQAVENLLE 128
MutL_Trans_MLH3 cd03486
MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 78-189 3.24e-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: 38.45  E-value: 3.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342801  78 RSIFGSAVSRELIEVGCEDKTlaFKMNGYISNaNYSVKKCIFLLFINHRLVESTALRKAIETVY----AAYLPKNT---- 149
Cdd:cd03486     7 KQIYGLVLAQKLKEVSAKFQE--YEVSGYISS-EGHYSKSFQFIYVNGRLYLKTRFHKLINKLFrktsAVAKNKSSpqsk 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1868342801 150 -----------HPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQ 189
Cdd:cd03486    84 ssrrgkrsqesYPVFVLNITCPASEYDLSQEPSKTIIEFKDWKTLLPLILE 134
 
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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