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Conserved domains on  [gi|568938972|ref|XP_006504875|]
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mismatch repair endonuclease PMS2 isoform X9 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MutL_Trans_hPMS_2_like cd03484
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 40-181 2.60e-65

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: 211.74  E-value: 2.60e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972  40 MKENIGSVFGQKQLQSLIPFVQLPPSDAVCEEYgLSTSRTPQNLFYVSGFISQCTHGAGRSATDRQFFFINQRPCDPAKV 119
Cdd:cd03484    2 IKDNIINVFGGKVIKGLIPINLELDVNPTKEEL-DSDEDLADSEVKITGYISKPSHGCGRSSSDRQFFYINGRPVDLKKV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568938972 120 SKLVNEVYHMYNRHQYPFVVLNVSVDSECVDINVTPDKRQILLQEEKLLLAVLKTSLIGMFD 181
Cdd:cd03484   81 AKLINEVYKSFNSRQYPFFILNISLPTSLYDVNVTPDKRTVLLHDEDRLIDTLKTSLSELFE 142
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
 492-635 4.50e-41

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: 4.50e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972   492 ILGQFNLGFIVTKLKEDLFLVDQHAADEKYNFEMLQQHTV-LQAQRLITPQTLNLTAVNEAVLIENLEIFRKNGFDFVID 570
Cdd:smart00853   1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQAGgLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELEIF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568938972   571 EDAPVTerakLISLPTSKNWTFGPQDIDELIFMLSDSPGVMCrPSRVRQMFASRACRKSVMIGTA 635
Cdd:smart00853  81 GPQSLI----LRSVPALLRQQNLQKLIPELLDLLSDEEENAR-PSRLEALLASLACRSAIRAGDA 140
mutL super family cl35064
DNA mismatch repair endonuclease MutL;
379-667 6.20e-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: 100.29  E-value: 6.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972 379 ALPLARLSPTNAKRFKTEERPSNVNISQR-LPGPQSTSAAEVDVAIKMNKRIVLLEFSLSSLAKRMKQLQHLKAQNKHEL 457
Cdd:PRK00095 326 AQSGLIPAAAGANQVLEPAEPEPLPLQQTpLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSEAAAAASA 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972 458 SYRKFRAKICPGENQAAEDELRkeisksmFAEMEILGQFNLGFIVTKLKEDLFLVDQHAADEKYNFEMLQQH---TVLQA 534
Cdd:PRK00095 406 EAAAAAPAAAPEPAEAAEEADS-------FPLGYALGQLHGTYILAENEDGLYLVDQHAAHERLLYEQLKDKlaeVGLAS 478

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972 535 QRLITPQTLNLTAVNEAVLIENLEIFRKNGFDFvidedAPVTERAKLI-SLPTsknWtFGPQDIDELIF----MLSDSPG 609
Cdd:PRK00095 479 QPLLIPLVLELSEDEADRLEEHKELLARLGLEL-----EPFGPNSFAVrEVPA---L-LGQQELEELIRdlldELAEEGD 549

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568938972 610 VmcRPSRVRQMFASRACRKSVMIGTALNASEMKKLITHMGEMDHPWNCPHGRPTMRHV 667
Cdd:PRK00095 550 S--DTLKERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIEL 605
 
Name Accession Description Interval E-value
MutL_Trans_hPMS_2_like cd03484
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 40-181 2.60e-65

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: 211.74  E-value: 2.60e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972  40 MKENIGSVFGQKQLQSLIPFVQLPPSDAVCEEYgLSTSRTPQNLFYVSGFISQCTHGAGRSATDRQFFFINQRPCDPAKV 119
Cdd:cd03484    2 IKDNIINVFGGKVIKGLIPINLELDVNPTKEEL-DSDEDLADSEVKITGYISKPSHGCGRSSSDRQFFYINGRPVDLKKV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568938972 120 SKLVNEVYHMYNRHQYPFVVLNVSVDSECVDINVTPDKRQILLQEEKLLLAVLKTSLIGMFD 181
Cdd:cd03484   81 AKLINEVYKSFNSRQYPFFILNISLPTSLYDVNVTPDKRTVLLHDEDRLIDTLKTSLSELFE 142
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 1-161 4.34e-42

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: 155.11  E-value: 4.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972    1 MVQVLQAYCIISAGVRVSCTNQlgqGKRQPVVCTSGSSGMKEN-IGSVFGQKQLQSLIPFVQLPPSDavceeyglstsrt 79
Cdd:TIGR00585 171 ILDVLQRYALIHPDISFSLTHD---GKKVLQLSTKPNQSTKENrIRSVFGTAVLRKLIPLDEWEDLD------------- 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972   80 pqnlFYVSGFISQCTHGAGRSATDrQFFFINQRPCDPAKVSKLVNEVYHMYN-RHQYPFVVLNVSVDSECVDINVTPDKR 158
Cdd:TIGR00585 235 ----LQLEGFISQPNVTRSRRSGW-QFLFINGRPVELKLLLKAIREVYHEYLpKGQYPVFVLNLEIDPELVDVNVHPDKK 309


                  ...
gi 568938972  159 QIL 161
Cdd:TIGR00585 310 EVR 312
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
 492-635 4.50e-41

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: 4.50e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972   492 ILGQFNLGFIVTKLKEDLFLVDQHAADEKYNFEMLQQHTV-LQAQRLITPQTLNLTAVNEAVLIENLEIFRKNGFDFVID 570
Cdd:smart00853   1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQAGgLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELEIF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568938972   571 EDAPVTerakLISLPTSKNWTFGPQDIDELIFMLSDSPGVMCrPSRVRQMFASRACRKSVMIGTA 635
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 ...
 493-636 1.78e-32

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: 1.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972  493 LGQFNLGFIVTKLKEDLFLVDQHAADEKYNFEMLQQHT---VLQAQRLITPQTLNLTAVNEAVLIENLEIFRKNGFDFvi 569
Cdd:pfam08676   4 LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALaegGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFEL-- 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568938972  570 deDAPVTERAKLISLPTSKNWTFGPQDIDELIFMLSDSPGVMCrPSRVRQMFASRACRKSVMIGTAL 636
Cdd:pfam08676  82 --EEFGPNSVIVRSVPALLRQQNLQELIRELLDELAEKGGSSL-EESLEELLATMACHSAVRAGRRL 145
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
491-667 1.69e-29

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 122.85  E-value: 1.69e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972 491 EILGQFNLGFIVTKLKEDLFLVDQHAADEKYNFE-MLQQHTV--LQAQRLITPQTLNLTAVNEAVLIENLEIFRKNGFDF 567
Cdd:COG0323  329 AALGQLHGTYILAENEDGLVLIDQHAAHERILYErLKKALAEggVASQPLLIPETLELSPAEAALLEEHLEELARLGFEI 408

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972 568 videdAPVTERAKLI-SLPTSknwtFGPQDIDELIF----MLSDSPGVMCRPSRVRQMFASRACRKSVMIGTALNASEMK 642
Cdd:COG0323  409 -----EPFGPNTVAVrAVPAL----LGEGDAEELLRdlldELAEEGSSESLEELREELLATMACHGAIKAGRRLSLEEMN 479

                        170       180
                 ....*....|....*....|....*
gi 568938972 643 KLITHMGEMDHPWNCPHGRPTMRHV 667
Cdd:COG0323  480 ALLRDLEATENPYTCPHGRPTWIEL 504
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 46-176 2.18e-23

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: 95.64  E-value: 2.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972   46 SVFGQKQLQSLIPFVqlppsdavCEEYGLStsrtpqnlfyVSGFISQctHGAGRSATDRQFFFINQRPCDPAKVSKLVNE 125
Cdd:pfam01119   2 AIYGKEFAENLLPIE--------KEDDGLR----------LSGYISK--PTLSRSNRDYQYLFVNGRPVRDKLLSHAIRE 61

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568938972  126 VYHMY-NRHQYPFVVLNVSVDSECVDINVTPDKRQILLQEEKLLLAVLKTSL 176
Cdd:pfam01119  62 AYRDLlPKGRYPVAVLFLEIDPELVDVNVHPTKREVRFRDEREVYDFIKEAL 113
mutL PRK00095
DNA mismatch repair endonuclease MutL;
379-667 6.20e-22

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 100.29  E-value: 6.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972 379 ALPLARLSPTNAKRFKTEERPSNVNISQR-LPGPQSTSAAEVDVAIKMNKRIVLLEFSLSSLAKRMKQLQHLKAQNKHEL 457
Cdd:PRK00095 326 AQSGLIPAAAGANQVLEPAEPEPLPLQQTpLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSEAAAAASA 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972 458 SYRKFRAKICPGENQAAEDELRkeisksmFAEMEILGQFNLGFIVTKLKEDLFLVDQHAADEKYNFEMLQQH---TVLQA 534
Cdd:PRK00095 406 EAAAAAPAAAPEPAEAAEEADS-------FPLGYALGQLHGTYILAENEDGLYLVDQHAAHERLLYEQLKDKlaeVGLAS 478

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972 535 QRLITPQTLNLTAVNEAVLIENLEIFRKNGFDFvidedAPVTERAKLI-SLPTsknWtFGPQDIDELIF----MLSDSPG 609
Cdd:PRK00095 479 QPLLIPLVLELSEDEADRLEEHKELLARLGLEL-----EPFGPNSFAVrEVPA---L-LGQQELEELIRdlldELAEEGD 549

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568938972 610 VmcRPSRVRQMFASRACRKSVMIGTALNASEMKKLITHMGEMDHPWNCPHGRPTMRHV 667
Cdd:PRK00095 550 S--DTLKERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIEL 605
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
34-176 9.53e-15

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 77.39  E-value: 9.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972  34 TSGSSGMKENIGSVFGQKQLQSLIPFvqlppsDAVCEEYGLStsrtpqnlfyvsGFISQCTHGagRSATDRQFFFINQRP 113
Cdd:COG0323  199 LPGAGDLLQRIAAIYGREFAENLLPV------EAEREGLRLS------------GYIGKPEFS--RSNRDYQYFFVNGRP 258

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568938972 114 CDPAKVSKLVNEVYH---MYNRHqyPFVVLNVSVDSECVDINVTPDKRQILLQEEKLLLAVLKTSL 176
Cdd:COG0323  259 VRDKLLSHAVREAYRdllPKGRY--PVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRSAV 322
 
Name Accession Description Interval E-value
MutL_Trans_hPMS_2_like cd03484
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 40-181 2.60e-65

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: 211.74  E-value: 2.60e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972  40 MKENIGSVFGQKQLQSLIPFVQLPPSDAVCEEYgLSTSRTPQNLFYVSGFISQCTHGAGRSATDRQFFFINQRPCDPAKV 119
Cdd:cd03484    2 IKDNIINVFGGKVIKGLIPINLELDVNPTKEEL-DSDEDLADSEVKITGYISKPSHGCGRSSSDRQFFYINGRPVDLKKV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568938972 120 SKLVNEVYHMYNRHQYPFVVLNVSVDSECVDINVTPDKRQILLQEEKLLLAVLKTSLIGMFD 181
Cdd:cd03484   81 AKLINEVYKSFNSRQYPFFILNISLPTSLYDVNVTPDKRTVLLHDEDRLIDTLKTSLSELFE 142
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 1-161 4.34e-42

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: 155.11  E-value: 4.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972    1 MVQVLQAYCIISAGVRVSCTNQlgqGKRQPVVCTSGSSGMKEN-IGSVFGQKQLQSLIPFVQLPPSDavceeyglstsrt 79
Cdd:TIGR00585 171 ILDVLQRYALIHPDISFSLTHD---GKKVLQLSTKPNQSTKENrIRSVFGTAVLRKLIPLDEWEDLD------------- 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972   80 pqnlFYVSGFISQCTHGAGRSATDrQFFFINQRPCDPAKVSKLVNEVYHMYN-RHQYPFVVLNVSVDSECVDINVTPDKR 158
Cdd:TIGR00585 235 ----LQLEGFISQPNVTRSRRSGW-QFLFINGRPVELKLLLKAIREVYHEYLpKGQYPVFVLNLEIDPELVDVNVHPDKK 309


                  ...
gi 568938972  159 QIL 161
Cdd:TIGR00585 310 EVR 312
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
 492-635 4.50e-41

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: 4.50e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972   492 ILGQFNLGFIVTKLKEDLFLVDQHAADEKYNFEMLQQHTV-LQAQRLITPQTLNLTAVNEAVLIENLEIFRKNGFDFVID 570
Cdd:smart00853   1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQAGgLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELEIF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568938972   571 EDAPVTerakLISLPTSKNWTFGPQDIDELIFMLSDSPGVMCrPSRVRQMFASRACRKSVMIGTA 635
Cdd:smart00853  81 GPQSLI----LRSVPALLRQQNLQKLIPELLDLLSDEEENAR-PSRLEALLASLACRSAIRAGDA 140
MutL_Trans cd00782
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 40-176 1.19e-35

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: 130.35  E-value: 1.19e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972  40 MKENIGSVFGQKQLQSLIPFVQlppsdavceeyglstsrtPQNLFYVSGFISQCTHGagRSATDRQFFFINQRPCDPAKV 119
Cdd:cd00782    1 LKDRIAQVYGKEVAKNLIEVEL------------------ESGDFRISGYISKPDFG--RSSKDRQFLFVNGRPVRDKLL 60

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568938972 120 SKLVNEVYHMYN-RHQYPFVVLNVSVDSECVDINVTPDKRQILLQEEKLLLAVLKTSL 176
Cdd:cd00782   61 SKAINEAYRSYLpKGRYPVFVLNLELPPELVDVNVHPTKREVRFSDEEEVLELIREAL 118
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
 493-636 1.78e-32

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: 1.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972  493 LGQFNLGFIVTKLKEDLFLVDQHAADEKYNFEMLQQHT---VLQAQRLITPQTLNLTAVNEAVLIENLEIFRKNGFDFvi 569
Cdd:pfam08676   4 LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALaegGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFEL-- 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568938972  570 deDAPVTERAKLISLPTSKNWTFGPQDIDELIFMLSDSPGVMCrPSRVRQMFASRACRKSVMIGTAL 636
Cdd:pfam08676  82 --EEFGPNSVIVRSVPALLRQQNLQELIRELLDELAEKGGSSL-EESLEELLATMACHSAVRAGRRL 145
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
491-667 1.69e-29

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 122.85  E-value: 1.69e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972 491 EILGQFNLGFIVTKLKEDLFLVDQHAADEKYNFE-MLQQHTV--LQAQRLITPQTLNLTAVNEAVLIENLEIFRKNGFDF 567
Cdd:COG0323  329 AALGQLHGTYILAENEDGLVLIDQHAAHERILYErLKKALAEggVASQPLLIPETLELSPAEAALLEEHLEELARLGFEI 408

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972 568 videdAPVTERAKLI-SLPTSknwtFGPQDIDELIF----MLSDSPGVMCRPSRVRQMFASRACRKSVMIGTALNASEMK 642
Cdd:COG0323  409 -----EPFGPNTVAVrAVPAL----LGEGDAEELLRdlldELAEEGSSESLEELREELLATMACHGAIKAGRRLSLEEMN 479

                        170       180
                 ....*....|....*....|....*
gi 568938972 643 KLITHMGEMDHPWNCPHGRPTMRHV 667
Cdd:COG0323  480 ALLRDLEATENPYTCPHGRPTWIEL 504
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 46-176 2.18e-23

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: 95.64  E-value: 2.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972   46 SVFGQKQLQSLIPFVqlppsdavCEEYGLStsrtpqnlfyVSGFISQctHGAGRSATDRQFFFINQRPCDPAKVSKLVNE 125
Cdd:pfam01119   2 AIYGKEFAENLLPIE--------KEDDGLR----------LSGYISK--PTLSRSNRDYQYLFVNGRPVRDKLLSHAIRE 61

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568938972  126 VYHMY-NRHQYPFVVLNVSVDSECVDINVTPDKRQILLQEEKLLLAVLKTSL 176
Cdd:pfam01119  62 AYRDLlPKGRYPVAVLFLEIDPELVDVNVHPTKREVRFRDEREVYDFIKEAL 113
mutL PRK00095
DNA mismatch repair endonuclease MutL;
379-667 6.20e-22

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 100.29  E-value: 6.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972 379 ALPLARLSPTNAKRFKTEERPSNVNISQR-LPGPQSTSAAEVDVAIKMNKRIVLLEFSLSSLAKRMKQLQHLKAQNKHEL 457
Cdd:PRK00095 326 AQSGLIPAAAGANQVLEPAEPEPLPLQQTpLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSEAAAAASA 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972 458 SYRKFRAKICPGENQAAEDELRkeisksmFAEMEILGQFNLGFIVTKLKEDLFLVDQHAADEKYNFEMLQQH---TVLQA 534
Cdd:PRK00095 406 EAAAAAPAAAPEPAEAAEEADS-------FPLGYALGQLHGTYILAENEDGLYLVDQHAAHERLLYEQLKDKlaeVGLAS 478

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972 535 QRLITPQTLNLTAVNEAVLIENLEIFRKNGFDFvidedAPVTERAKLI-SLPTsknWtFGPQDIDELIF----MLSDSPG 609
Cdd:PRK00095 479 QPLLIPLVLELSEDEADRLEEHKELLARLGLEL-----EPFGPNSFAVrEVPA---L-LGQQELEELIRdlldELAEEGD 549

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568938972 610 VmcRPSRVRQMFASRACRKSVMIGTALNASEMKKLITHMGEMDHPWNCPHGRPTMRHV 667
Cdd:PRK00095 550 S--DTLKERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIEL 605
TopoII_MutL_Trans cd00329
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 40-161 1.89e-18

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: 81.15  E-value: 1.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972  40 MKENIGSVFGQKQLQSLIPFVQLPPSdavceeyglstsrtpqnlFYVSGFISQCTHGagRSATDRQFFFINQRPCDPAK- 118
Cdd:cd00329    1 LKDRLAEILGDKVADKLIYVEGESDG------------------FRVEGAISYPDSG--RSSKDRQFSFVNGRPVREGGt 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568938972 119 VSKLVNEVYHMY----NRHQYPFVVLNVSVDSECVDINVTPDKRQIL 161
Cdd:cd00329   61 HVKAVREAYTRAlngdDVRRYPVAVLSLKIPPSLVDVNVHPTKEEVR 107
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
34-176 9.53e-15

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 77.39  E-value: 9.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972  34 TSGSSGMKENIGSVFGQKQLQSLIPFvqlppsDAVCEEYGLStsrtpqnlfyvsGFISQCTHGagRSATDRQFFFINQRP 113
Cdd:COG0323  199 LPGAGDLLQRIAAIYGREFAENLLPV------EAEREGLRLS------------GYIGKPEFS--RSNRDYQYFFVNGRP 258

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568938972 114 CDPAKVSKLVNEVYH---MYNRHqyPFVVLNVSVDSECVDINVTPDKRQILLQEEKLLLAVLKTSL 176
Cdd:COG0323  259 VRDKLLSHAVREAYRdllPKGRY--PVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRSAV 322
MutL_Trans_hPMS_1_like cd03485
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 41-171 6.85e-11

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: 60.36  E-value: 6.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972  41 KENIGSVFGQKQLQSLIPFvqlppsdavceeyglsTSRTPQNLFYVSGFISQCTHGAGRSATDRQFFFINQRPCDPAK-V 119
Cdd:cd03485    3 KEALARVLGTAVAANMVPV----------------QSTDEDPQISLEGFLPKPGSDVSKTKSDGKFISVNSRPVSLGKdI 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568938972 120 SKLVNEVYHMYNRH----QYPFVVLNVSVDSECVDINVTPDKRQILLQ-EEKLLLAV 171
Cdd:cd03485   67 GKLLRQYYSSAYRKsslrRYPVFFLNILCPPGLVDVNIEPDKDDVLLQnKEAVLQAV 123
MutL_Trans_MLH1 cd03483
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 41-165 6.49e-09

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: 54.55  E-value: 6.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972  41 KENIGSVFGQKQLQSLIPFvqlppSDAVCEEYGLstsrtpqnlFYVSGFISQcthgAGRSATDRQF-FFINQR--PCDPA 117
Cdd:cd03483    3 KDNIRSVYGAAVANELIEV-----EISDDDDDLG---------FKVKGLISN----ANYSKKKIIFiLFINNRlvECSAL 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568938972 118 KvsKLVNEVYHMY-NRHQYPFVVLNVSVDSECVDINVTPDKRQI--LLQEE 165
Cdd:cd03483   65 R--RAIENVYANYlPKGAHPFVYLSLEIPPENVDVNVHPTKREVhfLNEEE 113
MutL_Trans_MutL cd03482
MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 86-160 1.85e-06

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: 47.19  E-value: 1.85e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568938972  86 VSGFISQctHGAGRSATDRQFFFINQRPCDPAKVSKLVNEVYHMYNRHQ-YPFVVLNVSVDSECVDINVTPDKRQI 160
Cdd:cd03482   29 LSGWIAL--PTFARSQADIQYFYVNGRMVRDKLISHAVRQAYSDVLHGGrHPAYVLYLELDPAQVDVNVHPAKHEV 102
MutL_Trans_MLH3 cd03486
MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 84-172 1.08e-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: 39.99  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938972  84 FYVSGFISQCTHGAgrsaTDRQFFFINQRPCDPAKVSKLVNE-------VYHMYN--------RHQ-----YPFVVLNVS 143
Cdd:cd03486   28 YEVSGYISSEGHYS----KSFQFIYVNGRLYLKTRFHKLINKlfrktsaVAKNKSspqskssrRGKrsqesYPVFVLNIT 103

                         90       100
                 ....*....|....*....|....*....
gi 568938972 144 VDSECVDINVTPDKRQILLQEEKLLLAVL 172
Cdd:cd03486  104 CPASEYDLSQEPSKTIIEFKDWKTLLPLI 132
 
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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