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Conserved domains on  [gi|2462614864|ref|XP_054214416|]
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mismatch repair endonuclease PMS2 isoform X12 [Homo sapiens]

Protein Classification

MutL_C domain-containing protein( domain architecture ID 10252393)

MutL_C domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
 367-521 5.23e-36

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: 131.32  E-value: 5.23e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462614864  367 IIGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQHTV-LQGQRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDFVID 445
Cdd:smart00853   1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQAGgLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELEIF 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462614864  446 ENvmdfsqncillapvtERAKLISLPTSKNWTFGPQDVDELIFMLSDSPGVMCrPSRVKQMFASRACRKSVMIGTA 521
Cdd:smart00853  81 GP---------------QSLILRSVPALLRQQNLQKLIPELLDLLSDEEENAR-PSRLEALLASLACRSAIRAGDA 140
TopoII_MutL_Trans super family cl02783
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 1-53 1.46e-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.


The actual alignment was detected with superfamily member cd03484:

Pssm-ID: 445919 [Multi-domain]  Cd Length: 142  Bit Score: 93.87  E-value: 1.46e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462614864   1 MYNRHQYPFVVLNISVDSECVDINVTPDKRQILLQEEKLLLAVLKTSLIGMFD 53
Cdd:cd03484    90 SFNSRQYPFFILNISLPTSLYDVNVTPDKRTVLLHDEDRLIDTLKTSLSELFE 142
 
Name Accession Description Interval E-value
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
 367-521 5.23e-36

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: 131.32  E-value: 5.23e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462614864  367 IIGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQHTV-LQGQRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDFVID 445
Cdd:smart00853   1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQAGgLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELEIF 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462614864  446 ENvmdfsqncillapvtERAKLISLPTSKNWTFGPQDVDELIFMLSDSPGVMCrPSRVKQMFASRACRKSVMIGTA 521
Cdd:smart00853  81 GP---------------QSLILRSVPALLRQQNLQKLIPELLDLLSDEEENAR-PSRLEALLASLACRSAIRAGDA 140
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
 368-522 3.43e-28

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: 109.62  E-value: 3.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462614864 368 IGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQHTVLQG---QRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDFVi 444
Cdd:pfam08676   4 LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGlaaQPLLIPLVLELSPEEAALLEEHKEELAQLGFELE- 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462614864 445 denvmDFSQNcillapvteRAKLISLPTSKNWTFGPQDVDELIFMLSDSPGVMCrPSRVKQMFASRACRKSVMIGTAL 522
Cdd:pfam08676  83 -----EFGPN---------SVIVRSVPALLRQQNLQELIRELLDELAEKGGSSL-EESLEELLATMACHSAVRAGRRL 145
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
366-553 1.25e-27

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 116.68  E-value: 1.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462614864 366 EIIGQFNLGFIITKLNEDIFIVDQHATDEKYNFE-MLQQHTV--LQGQRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDF 442
Cdd:COG0323   329 AALGQLHGTYILAENEDGLVLIDQHAAHERILYErLKKALAEggVASQPLLIPETLELSPAEAALLEEHLEELARLGFEI 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462614864 443 VidenvmDFSQNCILLapvteRAklisLPTSknwtFGPQDVDELIF----MLSDSPGVMCRPSRVKQMFASRACRKSVMI 518
Cdd:COG0323   409 E------PFGPNTVAV-----RA----VPAL----LGEGDAEELLRdlldELAEEGSSESLEELREELLATMACHGAIKA 469

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462614864 519 GTALNTSEMKKLITHMGEMDHPWNCPHGRPTMRHI 553
Cdd:COG0323   470 GRRLSLEEMNALLRDLEATENPYTCPHGRPTWIEL 504
MutL_Trans_hPMS_2_like cd03484
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 1-53 1.46e-22

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: 93.87  E-value: 1.46e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462614864   1 MYNRHQYPFVVLNISVDSECVDINVTPDKRQILLQEEKLLLAVLKTSLIGMFD 53
Cdd:cd03484    90 SFNSRQYPFFILNISLPTSLYDVNVTPDKRTVLLHDEDRLIDTLKTSLSELFE 142
mutL PRK00095
DNA mismatch repair endonuclease MutL;
362-553 1.85e-19

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 92.20  E-value: 1.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462614864 362 FAEMEIIGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQH---TVLQGQRLIAPQTLNLTAVNEAVLIENLEIFRKN 438
Cdd:PRK00095  428 FPLGYALGQLHGTYILAENEDGLYLVDQHAAHERLLYEQLKDKlaeVGLASQPLLIPLVLELSEDEADRLEEHKELLARL 507

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462614864 439 GFDFVIdenvmdFSQNCILLapvteRakliSLPTsknWtFGPQDVDELIF----MLSDSPGVmcRPSRVKQMFASRACRK 514
Cdd:PRK00095  508 GLELEP------FGPNSFAV-----R----EVPA---L-LGQQELEELIRdlldELAEEGDS--DTLKERELLATMACHG 566

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462614864 515 SVMIGTALNTSEMKKLITHMGEMDHPWNCPHGRPTMRHI 553
Cdd:PRK00095  567 AIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIEL 605
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 4-48 5.72e-11

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: 59.82  E-value: 5.72e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462614864   4 RHQYPFVVLNISVDSECVDINVTPDKRQILLQEEKLLLAVLKTSL 48
Cdd:pfam01119  69 KGRYPVAVLFLEIDPELVDVNVHPTKREVRFRDEREVYDFIKEAL 113
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 4-33 1.36e-07

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: 53.41  E-value: 1.36e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462614864   4 RHQYPFVVLNISVDSECVDINVTPDKRQIL 33
Cdd:TIGR00585 283 KGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
4-48 4.13e-05

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 46.19  E-value: 4.13e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462614864   4 RHQYPFVVLNISVDSECVDINVTPDKRQILLQEEKLLLAVLKTSL 48
Cdd:COG0323   278 KGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRSAV 322
 
Name Accession Description Interval E-value
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
 367-521 5.23e-36

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: 131.32  E-value: 5.23e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462614864  367 IIGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQHTV-LQGQRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDFVID 445
Cdd:smart00853   1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQAGgLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELEIF 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462614864  446 ENvmdfsqncillapvtERAKLISLPTSKNWTFGPQDVDELIFMLSDSPGVMCrPSRVKQMFASRACRKSVMIGTA 521
Cdd:smart00853  81 GP---------------QSLILRSVPALLRQQNLQKLIPELLDLLSDEEENAR-PSRLEALLASLACRSAIRAGDA 140
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
 368-522 3.43e-28

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: 109.62  E-value: 3.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462614864 368 IGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQHTVLQG---QRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDFVi 444
Cdd:pfam08676   4 LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGlaaQPLLIPLVLELSPEEAALLEEHKEELAQLGFELE- 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462614864 445 denvmDFSQNcillapvteRAKLISLPTSKNWTFGPQDVDELIFMLSDSPGVMCrPSRVKQMFASRACRKSVMIGTAL 522
Cdd:pfam08676  83 -----EFGPN---------SVIVRSVPALLRQQNLQELIRELLDELAEKGGSSL-EESLEELLATMACHSAVRAGRRL 145
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
366-553 1.25e-27

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 116.68  E-value: 1.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462614864 366 EIIGQFNLGFIITKLNEDIFIVDQHATDEKYNFE-MLQQHTV--LQGQRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDF 442
Cdd:COG0323   329 AALGQLHGTYILAENEDGLVLIDQHAAHERILYErLKKALAEggVASQPLLIPETLELSPAEAALLEEHLEELARLGFEI 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462614864 443 VidenvmDFSQNCILLapvteRAklisLPTSknwtFGPQDVDELIF----MLSDSPGVMCRPSRVKQMFASRACRKSVMI 518
Cdd:COG0323   409 E------PFGPNTVAV-----RA----VPAL----LGEGDAEELLRdlldELAEEGSSESLEELREELLATMACHGAIKA 469

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462614864 519 GTALNTSEMKKLITHMGEMDHPWNCPHGRPTMRHI 553
Cdd:COG0323   470 GRRLSLEEMNALLRDLEATENPYTCPHGRPTWIEL 504
MutL_Trans_hPMS_2_like cd03484
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 1-53 1.46e-22

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: 93.87  E-value: 1.46e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462614864   1 MYNRHQYPFVVLNISVDSECVDINVTPDKRQILLQEEKLLLAVLKTSLIGMFD 53
Cdd:cd03484    90 SFNSRQYPFFILNISLPTSLYDVNVTPDKRTVLLHDEDRLIDTLKTSLSELFE 142
mutL PRK00095
DNA mismatch repair endonuclease MutL;
362-553 1.85e-19

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 92.20  E-value: 1.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462614864 362 FAEMEIIGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQH---TVLQGQRLIAPQTLNLTAVNEAVLIENLEIFRKN 438
Cdd:PRK00095  428 FPLGYALGQLHGTYILAENEDGLYLVDQHAAHERLLYEQLKDKlaeVGLASQPLLIPLVLELSEDEADRLEEHKELLARL 507

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462614864 439 GFDFVIdenvmdFSQNCILLapvteRakliSLPTsknWtFGPQDVDELIF----MLSDSPGVmcRPSRVKQMFASRACRK 514
Cdd:PRK00095  508 GLELEP------FGPNSFAV-----R----EVPA---L-LGQQELEELIRdlldELAEEGDS--DTLKERELLATMACHG 566

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462614864 515 SVMIGTALNTSEMKKLITHMGEMDHPWNCPHGRPTMRHI 553
Cdd:PRK00095  567 AIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIEL 605
MutL_Trans cd00782
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 3-48 3.27e-13

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: 66.41  E-value: 3.27e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2462614864   3 NRHQYPFVVLNISVDSECVDINVTPDKRQILLQEEKLLLAVLKTSL 48
Cdd:cd00782    73 PKGRYPVFVLNLELPPELVDVNVHPTKREVRFSDEEEVLELIREAL 118
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 4-48 5.72e-11

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: 59.82  E-value: 5.72e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462614864   4 RHQYPFVVLNISVDSECVDINVTPDKRQILLQEEKLLLAVLKTSL 48
Cdd:pfam01119  69 KGRYPVAVLFLEIDPELVDVNVHPTKREVRFRDEREVYDFIKEAL 113
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 4-33 1.36e-07

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: 53.41  E-value: 1.36e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462614864   4 RHQYPFVVLNISVDSECVDINVTPDKRQIL 33
Cdd:TIGR00585 283 KGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
MutL_Trans_hPMS_1_like cd03485
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 7-43 2.61e-05

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: 44.18  E-value: 2.61e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2462614864   7 YPFVVLNISVDSECVDINVTPDKRQILLQ-EEKLLLAV 43
Cdd:cd03485    86 YPVFFLNILCPPGLVDVNIEPDKDDVLLQnKEAVLQAV 123
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
4-48 4.13e-05

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 46.19  E-value: 4.13e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462614864   4 RHQYPFVVLNISVDSECVDINVTPDKRQILLQEEKLLLAVLKTSL 48
Cdd:COG0323   278 KGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRSAV 322
TopoII_MutL_Trans cd00329
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 3-33 6.93e-05

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: 42.25  E-value: 6.93e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462614864   3 NRHQYPFVVLNISVDSECVDINVTPDKRQIL 33
Cdd:cd00329    77 DVRRYPVAVLSLKIPPSLVDVNVHPTKEEVR 107
 
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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