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Conserved domains on  [gi|91992162|ref|NP_001035197|]
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DNA mismatch repair protein Mlh3 isoform 1 [Homo sapiens]

Protein Classification

DNA mismatch repair MutL family protein( domain architecture ID 13014530)

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_Trans_MLH3 cd03486
MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 206-349 1.03e-68

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: 227.20  E-value: 1.03e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162  206 DVCSRFCQIYGLGKSQKLREISFKYKEFELSGYISSEAHYNKNMQFLFVNKRLVLRTKLHKLIDFLLRKESIICKPKNGP 285
Cdd:cd03486    1 SILSVFKQIYGLVLAQKLKEVSAKFQEYEVSGYISSEGHYSKSFQFIYVNGRLYLKTRFHKLINKLFRKTSAVAKNKSSP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91992162  286 TSRQMnssLRHRSTPELYGIYVINVQCQFCEYDVCMEPAKTLIEFQNWDTLLFCIQEGVKMFLK 349
Cdd:cd03486   81 QSKSS---RRGKRSQESYPVFVLNITCPASEYDLSQEPSKTIIEFKDWKTLLPLILEVVKSFLK 141
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 9-192 2.65e-63

Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.


:

Pssm-ID: 340403 [Multi-domain]  Cd Length: 188  Bit Score: 213.45  E-value: 2.65e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162    9 VQAKLRSGLAISSLGQCVEELALNSIDAEAKCVAVRVNMETFQ-VQVIDNGFGMGSDDVEKVGNRYFTSKCHSVQDLENP 87
Cdd:cd16926    1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKlIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162   88 RFYGFRGEALANIADMaSAVEISSKKNRTMKTFVKLFQSGKALKACEAdvTRASAGTTVTVYNLFYQLPVRRKCM-DPRL 166
Cdd:cd16926   81 TTLGFRGEALASIASV-SRLTITTRTADDDVGTRLVVDGGGIIEEVKP--AAAPVGTTVTVRDLFYNTPARRKFLkSPKT 157

                        170       180
                 ....*....|....*....|....*.
gi 91992162  167 EFEKVRQRIEALSLMHPSISFSLRND 192
Cdd:cd16926  158 ELSKILDLVQRLALAHPDVSFSLTHD 183
MutL super family cl33837
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
1194-1409 2.75e-30

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


The actual alignment was detected with superfamily member COG0323:

Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 127.08  E-value: 2.75e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162 1194 QVDNKFIAClmstkteENGEAggnlLVLVDQHAAHERIRLEQLiidsyeKQQAqgsGRKKLLSSTLIPPLEITVTEEQRR 1273
Cdd:COG0323  333 QLHGTYILA-------ENEDG----LVLIDQHAAHERILYERL------KKAL---AEGGVASQPLLIPETLELSPAEAA 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162 1274 LLWCYHKNLEDLGLEF-VFPDTSdslVLVGKVPLCFVEREanelrrgrstvtksiVEEFIREQLELLQTTGGIQGTLPLt 1352
Cdd:COG0323  393 LLEEHLEELARLGFEIePFGPNT---VAVRAVPALLGEGD---------------AEELLRDLLDELAEEGSSESLEEL- 453

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 91992162 1353 VQKVLASQACHGAIKFNDGLSLQESCRLIEALSSCQLPFQCAHGRPSM--LPLADIDHL 1409
Cdd:COG0323  454 REELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTWieLSLEELEKL 512
 
Name Accession Description Interval E-value
MutL_Trans_MLH3 cd03486
MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 206-349 1.03e-68

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: 227.20  E-value: 1.03e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162  206 DVCSRFCQIYGLGKSQKLREISFKYKEFELSGYISSEAHYNKNMQFLFVNKRLVLRTKLHKLIDFLLRKESIICKPKNGP 285
Cdd:cd03486    1 SILSVFKQIYGLVLAQKLKEVSAKFQEYEVSGYISSEGHYSKSFQFIYVNGRLYLKTRFHKLINKLFRKTSAVAKNKSSP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91992162  286 TSRQMnssLRHRSTPELYGIYVINVQCQFCEYDVCMEPAKTLIEFQNWDTLLFCIQEGVKMFLK 349
Cdd:cd03486   81 QSKSS---RRGKRSQESYPVFVLNITCPASEYDLSQEPSKTIIEFKDWKTLLPLILEVVKSFLK 141
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 9-192 2.65e-63

Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.


Pssm-ID: 340403 [Multi-domain]  Cd Length: 188  Bit Score: 213.45  E-value: 2.65e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162    9 VQAKLRSGLAISSLGQCVEELALNSIDAEAKCVAVRVNMETFQ-VQVIDNGFGMGSDDVEKVGNRYFTSKCHSVQDLENP 87
Cdd:cd16926    1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKlIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162   88 RFYGFRGEALANIADMaSAVEISSKKNRTMKTFVKLFQSGKALKACEAdvTRASAGTTVTVYNLFYQLPVRRKCM-DPRL 166
Cdd:cd16926   81 TTLGFRGEALASIASV-SRLTITTRTADDDVGTRLVVDGGGIIEEVKP--AAAPVGTTVTVRDLFYNTPARRKFLkSPKT 157

                        170       180
                 ....*....|....*....|....*.
gi 91992162  167 EFEKVRQRIEALSLMHPSISFSLRND 192
Cdd:cd16926  158 ELSKILDLVQRLALAHPDVSFSLTHD 183
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 1-269 9.45e-50

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: 179.37  E-value: 9.45e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162      1 MIKCLSVEVQAKLRSGLAISSLGQCVEELALNSIDAEAkcVAVRVNMETF---QVQVIDNGFGMGSDDVEKVGNRYFTSK 77
Cdd:TIGR00585    2 TIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGA--TRIDVEIEEGglkLIEVSDNGSGIDKEDLPLACERHATSK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162     78 CHSVQDLENPRFYGFRGEALANIADmASAVEISSKKNRTMKTFVKLFQSGKALKACEaDVTRASaGTTVTVYNLFYQLPV 157
Cdd:TIGR00585   80 IQSFEDLERIETLGFRGEALASISS-VSRLTITTKTSAADGLAYQALLEGGMIESIK-PAPRPV-GTTVEVRDLFYNLPV 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162    158 RRKCM-DPRLEFEKVRQRIEALSLMHPSISFSLRNDvsGSMVLQLPK-----TKDVcsRFCQIYGLGKSQKLreISFKYK 231
Cdd:TIGR00585  157 RRKFLkSPKKEFRKILDVLQRYALIHPDISFSLTHD--GKKVLQLSTkpnqsTKEN--RIRSVFGTAVLRKL--IPLDEW 230

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 91992162    232 E---FELSGYISSEAH---YNKNMQFLFVNKRLVLRTKLHKLID 269
Cdd:TIGR00585  231 EdldLQLEGFISQPNVtrsRRSGWQFLFINGRPVELKLLLKAIR 274
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
26-259 1.87e-42

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 163.68  E-value: 1.87e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162   26 VEELALNSIDAEAKCVAVRV-----NMetfqVQVIDNGFGMGSDDVEKVGNRYFTSKCHSVQDLENPRFYGFRGEALANI 100
Cdd:COG0323   28 VKELVENAIDAGATRIEVEIeeggkSL----IRVTDNGCGMSPEDLPLAFERHATSKIRSAEDLFRIRTLGFRGEALASI 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162  101 AdmA-SAVEISSK-KNRTMKTFVKLfQSGKALKACEADvtrASAGTTVTVYNLFYQLPVRRKCMD-PRLEFEKVRQRIEA 177
Cdd:COG0323  104 A--SvSRLTLTTRtAGAELGTRIEV-EGGKVVEVEPAA---APKGTTVEVRDLFFNTPARRKFLKsDATELAHITDVVRR 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162  178 LSLMHPSISFSLRNDvsGSMVLQLPKTKDVCSRFCQIYGLGKSQKLREISFKYKEFELSGYISSEAHY--NKNMQFLFVN 255
Cdd:COG0323  178 LALAHPDIAFTLIHN--GREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKPEFSrsNRDYQYFFVN 255


                 ....
gi 91992162  256 KRLV 259
Cdd:COG0323  256 GRPV 259
mutL PRK00095
DNA mismatch repair endonuclease MutL;
26-264 7.03e-39

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 154.99  E-value: 7.03e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162    26 VEELALNSIDAEAKcvavRVNMETFQ-----VQVIDNGFGMGSDDVEKVGNRYFTSKCHSVQDLENPRFYGFRGEALANI 100
Cdd:PRK00095   27 VKELVENALDAGAT----RIDIEIEEgglklIRVRDNGCGISKEDLALALARHATSKIASLDDLEAIRTLGFRGEALPSI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162   101 ADMaSAVEISSK-KNRTMKTFVKlFQSGKALKaceadVTRASA--GTTVTVYNLFYQLPVRRKCM-DPRLEFEKVRQRIE 176
Cdd:PRK00095  103 ASV-SRLTLTSRtADAAEGWQIV-YEGGEIVE-----VKPAAHpvGTTIEVRDLFFNTPARRKFLkSEKTELGHIDDVVN 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162   177 ALSLMHPSISFSLRNDvsGSMVLQLPKTKDVCSRFCQIYGLGKSQKLREISFKYKEFELSGYISS-EAHY-NKNMQFLFV 254
Cdd:PRK00095  176 RLALAHPDVAFTLTHN--GKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLpTLSRaNRDYQYLFV 253

                         250
                  ....*....|
gi 91992162   255 NKRLVlRTKL 264
Cdd:PRK00095  254 NGRYV-RDKL 262
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
1194-1409 2.75e-30

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 127.08  E-value: 2.75e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162 1194 QVDNKFIAClmstkteENGEAggnlLVLVDQHAAHERIRLEQLiidsyeKQQAqgsGRKKLLSSTLIPPLEITVTEEQRR 1273
Cdd:COG0323  333 QLHGTYILA-------ENEDG----LVLIDQHAAHERILYERL------KKAL---AEGGVASQPLLIPETLELSPAEAA 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162 1274 LLWCYHKNLEDLGLEF-VFPDTSdslVLVGKVPLCFVEREanelrrgrstvtksiVEEFIREQLELLQTTGGIQGTLPLt 1352
Cdd:COG0323  393 LLEEHLEELARLGFEIePFGPNT---VAVRAVPALLGEGD---------------AEELLRDLLDELAEEGSSESLEEL- 453

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 91992162 1353 VQKVLASQACHGAIKFNDGLSLQESCRLIEALSSCQLPFQCAHGRPSM--LPLADIDHL 1409
Cdd:COG0323  454 REELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTWieLSLEELEKL 512
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
 1191-1370 5.26e-30

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: 116.30  E-value: 5.26e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162    1191 VLQQVDNKFIACLMstkteengeagGNLLVLVDQHAAHERIRLEQLIidsyekqqaqgSGRKKLLSSTLIPPLEITVTEE 1270
Cdd:smart00853    1 ALGQVAGTYILAER-----------EDGLYLLDQHAAHERILYEQLL-----------KQAGGLESQPLLIPVRLELSPQ 58

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162    1271 QRRLLWCYHKNLEDLGLEF-VFPDTSdslVLVGKVPLCFVEREanelrrgrstvtksiVEEFIREQLELLQTTGGIQgtL 1349
Cdd:smart00853   59 EAALLEEHLELLRQLGFELeIFGPQS---LILRSVPALLRQQN---------------LQKLIPELLDLLSDEEENA--R 118

                           170       180
                    ....*....|....*....|.
gi 91992162    1350 PLTVQKVLASQACHGAIKFND 1370
Cdd:smart00853  119 PSRLEALLASLACRSAIRAGD 139
mutL PRK00095
DNA mismatch repair endonuclease MutL;
1189-1409 7.51e-25

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 111.46  E-value: 7.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162  1189 MQVLQQVDNKFIacLMSTkteENGeaggnlLVLVDQHAAHERIRLEQLiidsyeKQQAQGSGRKkllSSTLIPPLEITVT 1268
Cdd:PRK00095  431 GYALGQLHGTYI--LAEN---EDG------LYLVDQHAAHERLLYEQL------KDKLAEVGLA---SQPLLIPLVLELS 490

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162  1269 EEQRRLLWCYHKNLEDLGLEF-VFPDTSdslVLVGKVPLCFVEREanelrrgrstvtksiVEEFIREQLELLQTTGGIQg 1347
Cdd:PRK00095  491 EDEADRLEEHKELLARLGLELePFGPNS---FAVREVPALLGQQE---------------LEELIRDLLDELAEEGDSD- 551

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91992162  1348 tlPLTVQKVLASQACHGAIKFNDGLSLQESCRLIEALSSCQLPFQCAHGRPSMLPL--ADIDHL 1409
Cdd:PRK00095  552 --TLKERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIELslSDLEKL 613
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
 1192-1370 2.17e-17

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: 80.34  E-value: 2.17e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162   1192 LQQVDNKFIAClmstkteENGEAggnlLVLVDQHAAHERIRLEQLiidsYEKQQAQGSGRKKLLSstlipPLEITVTEEQ 1271
Cdd:pfam08676    4 LGQVHGTYILA-------ENEDG----LYLIDQHAAHERILYEKL----KRALAEGGLAAQPLLI-----PLVLELSPEE 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162   1272 RRLLWCYHKNLEDLGLEF-VFPDTSdslVLVGKVPLCFveREANelrrgrstvtksiVEEFIREQLELLQTTGGIqgTLP 1350
Cdd:pfam08676   64 AALLEEHKEELAQLGFELeEFGPNS---VIVRSVPALL--RQQN-------------LQELIRELLDELAEKGGS--SLE 123

                          170       180
                   ....*....|....*....|
gi 91992162   1351 LTVQKVLASQACHGAIKFND 1370
Cdd:pfam08676  124 ESLEELLATMACHSAVRAGR 143
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 213-348 2.98e-07

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: 50.57  E-value: 2.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162    213 QIYGLGKSQKLREISFKYKEFELSGYIS--SEAHYNKNMQFLFVNKRLVLRTKLHKLI-----DFLLRKEsiickpkngp 285
Cdd:pfam01119    2 AIYGKEFAENLLPIEKEDDGLRLSGYISkpTLSRSNRDYQYLFVNGRPVRDKLLSHAIreayrDLLPKGR---------- 71

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91992162    286 tsrqmnsslrhrstpelYGIYVINVQCQFCEYDVCMEPAKTLIEFQNWDTLLFCIQEGVKMFL 348
Cdd:pfam01119   72 -----------------YPVAVLFLEIDPELVDVNVHPTKREVRFRDEREVYDFIKEALREAL 117
 
Name Accession Description Interval E-value
MutL_Trans_MLH3 cd03486
MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 206-349 1.03e-68

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: 227.20  E-value: 1.03e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162  206 DVCSRFCQIYGLGKSQKLREISFKYKEFELSGYISSEAHYNKNMQFLFVNKRLVLRTKLHKLIDFLLRKESIICKPKNGP 285
Cdd:cd03486    1 SILSVFKQIYGLVLAQKLKEVSAKFQEYEVSGYISSEGHYSKSFQFIYVNGRLYLKTRFHKLINKLFRKTSAVAKNKSSP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91992162  286 TSRQMnssLRHRSTPELYGIYVINVQCQFCEYDVCMEPAKTLIEFQNWDTLLFCIQEGVKMFLK 349
Cdd:cd03486   81 QSKSS---RRGKRSQESYPVFVLNITCPASEYDLSQEPSKTIIEFKDWKTLLPLILEVVKSFLK 141
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 9-192 2.65e-63

Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.


Pssm-ID: 340403 [Multi-domain]  Cd Length: 188  Bit Score: 213.45  E-value: 2.65e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162    9 VQAKLRSGLAISSLGQCVEELALNSIDAEAKCVAVRVNMETFQ-VQVIDNGFGMGSDDVEKVGNRYFTSKCHSVQDLENP 87
Cdd:cd16926    1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKlIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162   88 RFYGFRGEALANIADMaSAVEISSKKNRTMKTFVKLFQSGKALKACEAdvTRASAGTTVTVYNLFYQLPVRRKCM-DPRL 166
Cdd:cd16926   81 TTLGFRGEALASIASV-SRLTITTRTADDDVGTRLVVDGGGIIEEVKP--AAAPVGTTVTVRDLFYNTPARRKFLkSPKT 157

                        170       180
                 ....*....|....*....|....*.
gi 91992162  167 EFEKVRQRIEALSLMHPSISFSLRND 192
Cdd:cd16926  158 ELSKILDLVQRLALAHPDVSFSLTHD 183
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 1-269 9.45e-50

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: 179.37  E-value: 9.45e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162      1 MIKCLSVEVQAKLRSGLAISSLGQCVEELALNSIDAEAkcVAVRVNMETF---QVQVIDNGFGMGSDDVEKVGNRYFTSK 77
Cdd:TIGR00585    2 TIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGA--TRIDVEIEEGglkLIEVSDNGSGIDKEDLPLACERHATSK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162     78 CHSVQDLENPRFYGFRGEALANIADmASAVEISSKKNRTMKTFVKLFQSGKALKACEaDVTRASaGTTVTVYNLFYQLPV 157
Cdd:TIGR00585   80 IQSFEDLERIETLGFRGEALASISS-VSRLTITTKTSAADGLAYQALLEGGMIESIK-PAPRPV-GTTVEVRDLFYNLPV 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162    158 RRKCM-DPRLEFEKVRQRIEALSLMHPSISFSLRNDvsGSMVLQLPK-----TKDVcsRFCQIYGLGKSQKLreISFKYK 231
Cdd:TIGR00585  157 RRKFLkSPKKEFRKILDVLQRYALIHPDISFSLTHD--GKKVLQLSTkpnqsTKEN--RIRSVFGTAVLRKL--IPLDEW 230

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 91992162    232 E---FELSGYISSEAH---YNKNMQFLFVNKRLVLRTKLHKLID 269
Cdd:TIGR00585  231 EdldLQLEGFISQPNVtrsRRSGWQFLFINGRPVELKLLLKAIR 274
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
26-259 1.87e-42

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 163.68  E-value: 1.87e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162   26 VEELALNSIDAEAKCVAVRV-----NMetfqVQVIDNGFGMGSDDVEKVGNRYFTSKCHSVQDLENPRFYGFRGEALANI 100
Cdd:COG0323   28 VKELVENAIDAGATRIEVEIeeggkSL----IRVTDNGCGMSPEDLPLAFERHATSKIRSAEDLFRIRTLGFRGEALASI 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162  101 AdmA-SAVEISSK-KNRTMKTFVKLfQSGKALKACEADvtrASAGTTVTVYNLFYQLPVRRKCMD-PRLEFEKVRQRIEA 177
Cdd:COG0323  104 A--SvSRLTLTTRtAGAELGTRIEV-EGGKVVEVEPAA---APKGTTVEVRDLFFNTPARRKFLKsDATELAHITDVVRR 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162  178 LSLMHPSISFSLRNDvsGSMVLQLPKTKDVCSRFCQIYGLGKSQKLREISFKYKEFELSGYISSEAHY--NKNMQFLFVN 255
Cdd:COG0323  178 LALAHPDIAFTLIHN--GREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKPEFSrsNRDYQYFFVN 255


                 ....
gi 91992162  256 KRLV 259
Cdd:COG0323  256 GRPV 259
mutL PRK00095
DNA mismatch repair endonuclease MutL;
26-264 7.03e-39

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 154.99  E-value: 7.03e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162    26 VEELALNSIDAEAKcvavRVNMETFQ-----VQVIDNGFGMGSDDVEKVGNRYFTSKCHSVQDLENPRFYGFRGEALANI 100
Cdd:PRK00095   27 VKELVENALDAGAT----RIDIEIEEgglklIRVRDNGCGISKEDLALALARHATSKIASLDDLEAIRTLGFRGEALPSI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162   101 ADMaSAVEISSK-KNRTMKTFVKlFQSGKALKaceadVTRASA--GTTVTVYNLFYQLPVRRKCM-DPRLEFEKVRQRIE 176
Cdd:PRK00095  103 ASV-SRLTLTSRtADAAEGWQIV-YEGGEIVE-----VKPAAHpvGTTIEVRDLFFNTPARRKFLkSEKTELGHIDDVVN 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162   177 ALSLMHPSISFSLRNDvsGSMVLQLPKTKDVCSRFCQIYGLGKSQKLREISFKYKEFELSGYISS-EAHY-NKNMQFLFV 254
Cdd:PRK00095  176 RLALAHPDVAFTLTHN--GKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLpTLSRaNRDYQYLFV 253

                         250
                  ....*....|
gi 91992162   255 NKRLVlRTKL 264
Cdd:PRK00095  254 NGRYV-RDKL 262
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
1194-1409 2.75e-30

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 127.08  E-value: 2.75e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162 1194 QVDNKFIAClmstkteENGEAggnlLVLVDQHAAHERIRLEQLiidsyeKQQAqgsGRKKLLSSTLIPPLEITVTEEQRR 1273
Cdd:COG0323  333 QLHGTYILA-------ENEDG----LVLIDQHAAHERILYERL------KKAL---AEGGVASQPLLIPETLELSPAEAA 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162 1274 LLWCYHKNLEDLGLEF-VFPDTSdslVLVGKVPLCFVEREanelrrgrstvtksiVEEFIREQLELLQTTGGIQGTLPLt 1352
Cdd:COG0323  393 LLEEHLEELARLGFEIePFGPNT---VAVRAVPALLGEGD---------------AEELLRDLLDELAEEGSSESLEEL- 453

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 91992162 1353 VQKVLASQACHGAIKFNDGLSLQESCRLIEALSSCQLPFQCAHGRPSM--LPLADIDHL 1409
Cdd:COG0323  454 REELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTWieLSLEELEKL 512
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
 1191-1370 5.26e-30

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: 116.30  E-value: 5.26e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162    1191 VLQQVDNKFIACLMstkteengeagGNLLVLVDQHAAHERIRLEQLIidsyekqqaqgSGRKKLLSSTLIPPLEITVTEE 1270
Cdd:smart00853    1 ALGQVAGTYILAER-----------EDGLYLLDQHAAHERILYEQLL-----------KQAGGLESQPLLIPVRLELSPQ 58

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162    1271 QRRLLWCYHKNLEDLGLEF-VFPDTSdslVLVGKVPLCFVEREanelrrgrstvtksiVEEFIREQLELLQTTGGIQgtL 1349
Cdd:smart00853   59 EAALLEEHLELLRQLGFELeIFGPQS---LILRSVPALLRQQN---------------LQKLIPELLDLLSDEEENA--R 118

                           170       180
                    ....*....|....*....|.
gi 91992162    1350 PLTVQKVLASQACHGAIKFND 1370
Cdd:smart00853  119 PSRLEALLASLACRSAIRAGD 139
MutL_Trans cd00782
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 209-348 9.96e-30

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: 114.95  E-value: 9.96e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162  209 SRFCQIYGLGKSQKLREISFKYKEFELSGYISSEAHY--NKNMQFLFVNKRLVLRTKLHKLIDFLLRkesiickpkngpt 286
Cdd:cd00782    3 DRIAQVYGKEVAKNLIEVELESGDFRISGYISKPDFGrsSKDRQFLFVNGRPVRDKLLSKAINEAYR------------- 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91992162  287 srqmnSSLRHRStpelYGIYVINVQCQFCEYDVCMEPAKTLIEFQNWDTLLFCIQEGVKMFL 348
Cdd:cd00782   70 -----SYLPKGR----YPVFVLNLELPPELVDVNVHPTKREVRFSDEEEVLELIREALRSAL 122
mutL PRK00095
DNA mismatch repair endonuclease MutL;
1189-1409 7.51e-25

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 111.46  E-value: 7.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162  1189 MQVLQQVDNKFIacLMSTkteENGeaggnlLVLVDQHAAHERIRLEQLiidsyeKQQAQGSGRKkllSSTLIPPLEITVT 1268
Cdd:PRK00095  431 GYALGQLHGTYI--LAEN---EDG------LYLVDQHAAHERLLYEQL------KDKLAEVGLA---SQPLLIPLVLELS 490

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162  1269 EEQRRLLWCYHKNLEDLGLEF-VFPDTSdslVLVGKVPLCFVEREanelrrgrstvtksiVEEFIREQLELLQTTGGIQg 1347
Cdd:PRK00095  491 EDEADRLEEHKELLARLGLELePFGPNS---FAVREVPALLGQQE---------------LEELIRDLLDELAEEGDSD- 551

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91992162  1348 tlPLTVQKVLASQACHGAIKFNDGLSLQESCRLIEALSSCQLPFQCAHGRPSMLPL--ADIDHL 1409
Cdd:PRK00095  552 --TLKERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIELslSDLEKL 613
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
 1192-1370 2.17e-17

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: 80.34  E-value: 2.17e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162   1192 LQQVDNKFIAClmstkteENGEAggnlLVLVDQHAAHERIRLEQLiidsYEKQQAQGSGRKKLLSstlipPLEITVTEEQ 1271
Cdd:pfam08676    4 LGQVHGTYILA-------ENEDG----LYLIDQHAAHERILYEKL----KRALAEGGLAAQPLLI-----PLVLELSPEE 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162   1272 RRLLWCYHKNLEDLGLEF-VFPDTSdslVLVGKVPLCFveREANelrrgrstvtksiVEEFIREQLELLQTTGGIqgTLP 1350
Cdd:pfam08676   64 AALLEEHKEELAQLGFELeEFGPNS---VIVRSVPALL--RQQN-------------LQELIRELLDELAEKGGS--SLE 123

                          170       180
                   ....*....|....*....|
gi 91992162   1351 LTVQKVLASQACHGAIKFND 1370
Cdd:pfam08676  124 ESLEELLATMACHSAVRAGR 143
TopoII_MutL_Trans cd00329
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 209-328 2.62e-14

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: 70.37  E-value: 2.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162  209 SRFCQIYGLGKSQKLREISFKYKEFELSGYISS--EAHYNKNMQFLFVNKRLVLRTKLH-KLIDFLLRkesiickpkngp 285
Cdd:cd00329    3 DRLAEILGDKVADKLIYVEGESDGFRVEGAISYpdSGRSSKDRQFSFVNGRPVREGGTHvKAVREAYT------------ 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 91992162  286 tsRQMNSSLRHRstpelYGIYVINVQCQFCEYDVCMEPAKTLI 328
Cdd:cd00329   71 --RALNGDDVRR-----YPVAVLSLKIPPSLVDVNVHPTKEEV 106
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 213-348 2.98e-07

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: 50.57  E-value: 2.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162    213 QIYGLGKSQKLREISFKYKEFELSGYIS--SEAHYNKNMQFLFVNKRLVLRTKLHKLI-----DFLLRKEsiickpkngp 285
Cdd:pfam01119    2 AIYGKEFAENLLPIEKEDDGLRLSGYISkpTLSRSNRDYQYLFVNGRPVRDKLLSHAIreayrDLLPKGR---------- 71

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91992162    286 tsrqmnsslrhrstpelYGIYVINVQCQFCEYDVCMEPAKTLIEFQNWDTLLFCIQEGVKMFL 348
Cdd:pfam01119   72 -----------------YPVAVLFLEIDPELVDVNVHPTKREVRFRDEREVYDFIKEALREAL 117
MutL_Trans_hPMS_2_like cd03484
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 225-347 4.40e-05

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: 44.95  E-value: 4.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162  225 EISFKYKEFELSGYISSEAHY----NKNMQFLFVNKRLVLRTKLHKLIDfllrkesiickpkngptsrQMNSSLRHRSTP 300
Cdd:cd03484   37 DEDLADSEVKITGYISKPSHGcgrsSSDRQFFYINGRPVDLKKVAKLIN-------------------EVYKSFNSRQYP 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 91992162  301 elygIYVINVQCQFCEYDVCMEPAKTLIEFQNWDTLLFCIQEG-VKMF 347
Cdd:cd03484   98 ----FFILNISLPTSLYDVNVTPDKRTVLLHDEDRLIDTLKTSlSELF 141
MutL_Trans_MLH1 cd03483
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 213-269 9.61e-04

MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to yeast and human MLH1 (MutL homologue 1). This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. MLH1 forms heterodimers with PMS2, PMS1 and MLH3. These three complexes have distinct functions in meiosis. hMLH1-hPMS2 also participates in the repair of all DNA mismatch repair (MMR) substrates. Roles for hMLH1-hPMS1 or hMLH1-hMLH3 in MMR have not been established. Cells lacking hMLH1 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hMLH1 causes predisposition to HNPCC, Muir-Torre syndrome and Turcot syndrome (HNPCC variant). Mutation in hMLH1 accounts for a large fraction of HNPCC families.


Pssm-ID: 239565 [Multi-domain]  Cd Length: 127  Bit Score: 40.68  E-value: 9.61e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91992162  213 QIYGLGKSQKLREISFKYKE----FELSGYISSeAHYN--KNMQFLFVNKRLVLRTKLHKLID 269
Cdd:cd03483    8 SVYGAAVANELIEVEISDDDddlgFKVKGLISN-ANYSkkKIIFILFINNRLVECSALRRAIE 69
MutL_Trans_hPMS_1_like cd03485
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 250-341 1.20e-03

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: 40.72  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91992162  250 QFLFVNKRLVLRTK-LHKLIDFLLRKESiickpkngptsrqmnsslrHRSTPELYGIYVINVQCQFCEYDVCMEPAKTLI 328
Cdd:cd03485   51 KFISVNSRPVSLGKdIGKLLRQYYSSAY-------------------RKSSLRRYPVFFLNILCPPGLVDVNIEPDKDDV 111

                         90
                 ....*....|...
gi 91992162  329 EFQNWDTLLFCIQ 341
Cdd:cd03485  112 LLQNKEAVLQAVE 124
 
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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