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Conserved domains on  [gi|1720412469|ref|XP_030110063|]
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mismatch repair endonuclease PMS2 isoform X14 [Mus musculus]

Protein Classification

DNA mismatch repair MutL family protein( domain architecture ID 1001448)

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

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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 ...
314-457 6.21e-42

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: 146.35  E-value: 6.21e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412469  314 ILGQFNLGFIVTKLKEDLFLVDQHAADEKYNFEMLQQHTV-LQAQRLITPQTLNLTAVNEAVLIENLEIFRKNGFDFVID 392
Cdd:smart00853   1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQAGgLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELEIF 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720412469  393 EDAPVTerakLISLPTSKNWTFGPQDIDELIFMLSDSPGVMCrPSRVRQMFASRACRKSVMIGTA 457
Cdd:smart00853  81 GPQSLI----LRSVPALLRQQNLQKLIPELLDLLSDEEENAR-PSRLEALLASLACRSAIRAGDA 140
mutL super family cl35064
DNA mismatch repair endonuclease MutL;
201-489 3.77e-22

DNA mismatch repair endonuclease MutL;


The actual alignment was detected with superfamily member PRK00095:

Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 99.91  E-value: 3.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412469 201 ALPLARLSPTNAKRFKTEERPSNVNISQR-LPGPQSTSAAEVDVAIKMNKRIVLLEFSLSSLAKRMKQLQHLKAQNKHEL 279
Cdd:PRK00095  326 AQSGLIPAAAGANQVLEPAEPEPLPLQQTpLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSEAAAAASA 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412469 280 SYRKFRAKICPGENQAAEDELRkeisksmFAEMEILGQFNLGFIVTKLKEDLFLVDQHAADEKYNFEMLQQH---TVLQA 356
Cdd:PRK00095  406 EAAAAAPAAAPEPAEAAEEADS-------FPLGYALGQLHGTYILAENEDGLYLVDQHAAHERLLYEQLKDKlaeVGLAS 478
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412469 357 QRLITPQTLNLTAVNEAVLIENLEIFRKNGFDFvidedAPVTERAKLI-SLPTsknWtFGPQDIDELIF----MLSDSPG 431
Cdd:PRK00095  479 QPLLIPLVLELSEDEADRLEEHKELLARLGLEL-----EPFGPNSFAVrEVPA---L-LGQQELEELIRdlldELAEEGD 549
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412469 432 VmcRPSRVRQMFASRACRKSVMIGTALNASEMKKLITHMGEMDHPWNCPHGRPTMRHV 489
Cdd:PRK00095  550 S--DTLKERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIEL 605
 
Name Accession Description Interval E-value
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
314-457 6.21e-42

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: 146.35  E-value: 6.21e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412469  314 ILGQFNLGFIVTKLKEDLFLVDQHAADEKYNFEMLQQHTV-LQAQRLITPQTLNLTAVNEAVLIENLEIFRKNGFDFVID 392
Cdd:smart00853   1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQAGgLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELEIF 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720412469  393 EDAPVTerakLISLPTSKNWTFGPQDIDELIFMLSDSPGVMCrPSRVRQMFASRACRKSVMIGTA 457
Cdd:smart00853  81 GPQSLI----LRSVPALLRQQNLQKLIPELLDLLSDEEENAR-PSRLEALLASLACRSAIRAGDA 140
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
315-458 5.41e-33

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: 122.33  E-value: 5.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412469 315 LGQFNLGFIVTKLKEDLFLVDQHAADEKYNFEMLQQHT---VLQAQRLITPQTLNLTAVNEAVLIENLEIFRKNGFDFvi 391
Cdd:pfam08676   4 LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALaegGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFEL-- 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412469 392 deDAPVTERAKLISLPTSKNWTFGPQDIDELIFMLSDSPGVMCrPSRVRQMFASRACRKSVMIGTAL 458
Cdd:pfam08676  82 --EEFGPNSVIVRSVPALLRQQNLQELIRELLDELAEKGGSSL-EESLEELLATMACHSAVRAGRRL 145
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
313-489 5.28e-30

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 122.85  E-value: 5.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412469 313 EILGQFNLGFIVTKLKEDLFLVDQHAADEKYNFE-MLQQHTV--LQAQRLITPQTLNLTAVNEAVLIENLEIFRKNGFDF 389
Cdd:COG0323   329 AALGQLHGTYILAENEDGLVLIDQHAAHERILYErLKKALAEggVASQPLLIPETLELSPAEAALLEEHLEELARLGFEI 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412469 390 videdAPVTERAKLI-SLPTSknwtFGPQDIDELIF----MLSDSPGVMCRPSRVRQMFASRACRKSVMIGTALNASEMK 464
Cdd:COG0323   409 -----EPFGPNTVAVrAVPAL----LGEGDAEELLRdlldELAEEGSSESLEELREELLATMACHGAIKAGRRLSLEEMN 479
                         170       180
                  ....*....|....*....|....*
gi 1720412469 465 KLITHMGEMDHPWNCPHGRPTMRHV 489
Cdd:COG0323   480 ALLRDLEATENPYTCPHGRPTWIEL 504
mutL PRK00095
DNA mismatch repair endonuclease MutL;
201-489 3.77e-22

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 99.91  E-value: 3.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412469 201 ALPLARLSPTNAKRFKTEERPSNVNISQR-LPGPQSTSAAEVDVAIKMNKRIVLLEFSLSSLAKRMKQLQHLKAQNKHEL 279
Cdd:PRK00095  326 AQSGLIPAAAGANQVLEPAEPEPLPLQQTpLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSEAAAAASA 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412469 280 SYRKFRAKICPGENQAAEDELRkeisksmFAEMEILGQFNLGFIVTKLKEDLFLVDQHAADEKYNFEMLQQH---TVLQA 356
Cdd:PRK00095  406 EAAAAAPAAAPEPAEAAEEADS-------FPLGYALGQLHGTYILAENEDGLYLVDQHAAHERLLYEQLKDKlaeVGLAS 478
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412469 357 QRLITPQTLNLTAVNEAVLIENLEIFRKNGFDFvidedAPVTERAKLI-SLPTsknWtFGPQDIDELIF----MLSDSPG 431
Cdd:PRK00095  479 QPLLIPLVLELSEDEADRLEEHKELLARLGLEL-----EPFGPNSFAVrEVPA---L-LGQQELEELIRdlldELAEEGD 549
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412469 432 VmcRPSRVRQMFASRACRKSVMIGTALNASEMKKLITHMGEMDHPWNCPHGRPTMRHV 489
Cdd:PRK00095  550 S--DTLKERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIEL 605
 
Name Accession Description Interval E-value
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
314-457 6.21e-42

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: 146.35  E-value: 6.21e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412469  314 ILGQFNLGFIVTKLKEDLFLVDQHAADEKYNFEMLQQHTV-LQAQRLITPQTLNLTAVNEAVLIENLEIFRKNGFDFVID 392
Cdd:smart00853   1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQAGgLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELEIF 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720412469  393 EDAPVTerakLISLPTSKNWTFGPQDIDELIFMLSDSPGVMCrPSRVRQMFASRACRKSVMIGTA 457
Cdd:smart00853  81 GPQSLI----LRSVPALLRQQNLQKLIPELLDLLSDEEENAR-PSRLEALLASLACRSAIRAGDA 140
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
315-458 5.41e-33

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: 122.33  E-value: 5.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412469 315 LGQFNLGFIVTKLKEDLFLVDQHAADEKYNFEMLQQHT---VLQAQRLITPQTLNLTAVNEAVLIENLEIFRKNGFDFvi 391
Cdd:pfam08676   4 LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALaegGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFEL-- 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412469 392 deDAPVTERAKLISLPTSKNWTFGPQDIDELIFMLSDSPGVMCrPSRVRQMFASRACRKSVMIGTAL 458
Cdd:pfam08676  82 --EEFGPNSVIVRSVPALLRQQNLQELIRELLDELAEKGGSSL-EESLEELLATMACHSAVRAGRRL 145
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
313-489 5.28e-30

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 122.85  E-value: 5.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412469 313 EILGQFNLGFIVTKLKEDLFLVDQHAADEKYNFE-MLQQHTV--LQAQRLITPQTLNLTAVNEAVLIENLEIFRKNGFDF 389
Cdd:COG0323   329 AALGQLHGTYILAENEDGLVLIDQHAAHERILYErLKKALAEggVASQPLLIPETLELSPAEAALLEEHLEELARLGFEI 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412469 390 videdAPVTERAKLI-SLPTSknwtFGPQDIDELIF----MLSDSPGVMCRPSRVRQMFASRACRKSVMIGTALNASEMK 464
Cdd:COG0323   409 -----EPFGPNTVAVrAVPAL----LGEGDAEELLRdlldELAEEGSSESLEELREELLATMACHGAIKAGRRLSLEEMN 479
                         170       180
                  ....*....|....*....|....*
gi 1720412469 465 KLITHMGEMDHPWNCPHGRPTMRHV 489
Cdd:COG0323   480 ALLRDLEATENPYTCPHGRPTWIEL 504
mutL PRK00095
DNA mismatch repair endonuclease MutL;
201-489 3.77e-22

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 99.91  E-value: 3.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412469 201 ALPLARLSPTNAKRFKTEERPSNVNISQR-LPGPQSTSAAEVDVAIKMNKRIVLLEFSLSSLAKRMKQLQHLKAQNKHEL 279
Cdd:PRK00095  326 AQSGLIPAAAGANQVLEPAEPEPLPLQQTpLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSEAAAAASA 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412469 280 SYRKFRAKICPGENQAAEDELRkeisksmFAEMEILGQFNLGFIVTKLKEDLFLVDQHAADEKYNFEMLQQH---TVLQA 356
Cdd:PRK00095  406 EAAAAAPAAAPEPAEAAEEADS-------FPLGYALGQLHGTYILAENEDGLYLVDQHAAHERLLYEQLKDKlaeVGLAS 478
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412469 357 QRLITPQTLNLTAVNEAVLIENLEIFRKNGFDFvidedAPVTERAKLI-SLPTsknWtFGPQDIDELIF----MLSDSPG 431
Cdd:PRK00095  479 QPLLIPLVLELSEDEADRLEEHKELLARLGLEL-----EPFGPNSFAVrEVPA---L-LGQQELEELIRdlldELAEEGD 549
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412469 432 VmcRPSRVRQMFASRACRKSVMIGTALNASEMKKLITHMGEMDHPWNCPHGRPTMRHV 489
Cdd:PRK00095  550 S--DTLKERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIEL 605
 
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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