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Conserved domains on  [gi|564356589|ref|XP_006240374|]
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DNA mismatch repair protein Mlh3 isoform X2 [Rattus norvegicus]

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 1.23e-64

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: 215.26  E-value: 1.23e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  206 DICSRFCQIYGLGKSQKLREIHYKYKEFEFNGYISSEAHYNKNMQFLFVNRRLVLRTKLHKLIDFLLRKESIICRPKNGS 285
Cdd:cd03486     1 SILSVFKQIYGLVLAQKLKEVSAKFQEYEVSGYISSEGHYSKSFQFIYVNGRLYLKTRFHKLINKLFRKTSAVAKNKSSP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564356589  286 ASRQMnssPRHRSASELHGIYVINVQCPFCEYDVCIEPAKTLIEFQNWDTVLICVQEGIKKFLK 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 1.16e-60

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: 205.75  E-value: 1.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589    9 VQAKLRSGLALSSLGQCVEELTLNSIDAEATCVAIRVNMETFQ-VQVIDNGLGMAGDDVEKVGNRYFTSKCHSVRDLENP 87
Cdd:cd16926     1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKlIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589   88 TFYGFRGEALASIADMaSAVEISSKKSTTLKTFVKMFQNGKALAAREAdlTRPSVGTTVTVYNLFYQFPVRRKSM-DPRL 166
Cdd:cd16926    81 TTLGFRGEALASIASV-SRLTITTRTADDDVGTRLVVDGGGIIEEVKP--AAAPVGTTVTVRDLFYNTPARRKFLkSPKT 157

                         170       180
                  ....*....|....*....|....*.
gi 564356589  167 EFEKVRQRVEALSLMHPSISFSLRND 192
Cdd:cd16926   158 ELSKILDLVQRLALAHPDVSFSLTHD 183
MutL super family cl33837
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
1150-1365 2.23e-32

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: 133.63  E-value: 2.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589 1150 QVDNKFIAClmssrTDGSGqaggnlLVLVDQHAAHERVRLEQLItDSYEKQAPQSagrKKLLsstiiPPLAITVSEEQRR 1229
Cdd:COG0323   333 QLHGTYILA-----ENEDG------LVLIDQHAAHERILYERLK-KALAEGGVAS---QPLL-----IPETLELSPAEAA 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589 1230 LLRSYHKHLEDLGLEL-LFpdaSDSSILVGKVPLCFVEREanelrrgrspvtksiVEELIREQLELLQTTGGIQGTLPLt 1308
Cdd:COG0323   393 LLEEHLEELARLGFEIePF---GPNTVAVRAVPALLGEGD---------------AEELLRDLLDELAEEGSSESLEEL- 453

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564356589 1309 VQKVLASQACHGAIKFNDRLSLEESCRLIEALSLCQLPFQCAHGRPSM--LPLADLDHL 1365
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 1.23e-64

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: 215.26  E-value: 1.23e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  206 DICSRFCQIYGLGKSQKLREIHYKYKEFEFNGYISSEAHYNKNMQFLFVNRRLVLRTKLHKLIDFLLRKESIICRPKNGS 285
Cdd:cd03486     1 SILSVFKQIYGLVLAQKLKEVSAKFQEYEVSGYISSEGHYSKSFQFIYVNGRLYLKTRFHKLINKLFRKTSAVAKNKSSP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564356589  286 ASRQMnssPRHRSASELHGIYVINVQCPFCEYDVCIEPAKTLIEFQNWDTVLICVQEGIKKFLK 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 1.16e-60

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: 205.75  E-value: 1.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589    9 VQAKLRSGLALSSLGQCVEELTLNSIDAEATCVAIRVNMETFQ-VQVIDNGLGMAGDDVEKVGNRYFTSKCHSVRDLENP 87
Cdd:cd16926     1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKlIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589   88 TFYGFRGEALASIADMaSAVEISSKKSTTLKTFVKMFQNGKALAAREAdlTRPSVGTTVTVYNLFYQFPVRRKSM-DPRL 166
Cdd:cd16926    81 TTLGFRGEALASIASV-SRLTITTRTADDDVGTRLVVDGGGIIEEVKP--AAAPVGTTVTVRDLFYNTPARRKFLkSPKT 157

                         170       180
                  ....*....|....*....|....*.
gi 564356589  167 EFEKVRQRVEALSLMHPSISFSLRND 192
Cdd:cd16926   158 ELSKILDLVQRLALAHPDVSFSLTHD 183
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 1-326 5.74e-53

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: 188.62  E-value: 5.74e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589     1 MIRCLSDEVQAKLRSGLALSSLGQCVEELTLNSIDAEATcvAIRVNMETF---QVQVIDNGLGMAGDDVEKVGNRYFTSK 77
Cdd:TIGR00585    2 TIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGAT--RIDVEIEEGglkLIEVSDNGSGIDKEDLPLACERHATSK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589    78 CHSVRDLENPTFYGFRGEALASIADmASAVEISSKKSTTLKTFVKMFQNGKALAAREADlTRPsVGTTVTVYNLFYQFPV 157
Cdd:TIGR00585   80 IQSFEDLERIETLGFRGEALASISS-VSRLTITTKTSAADGLAYQALLEGGMIESIKPA-PRP-VGTTVEVRDLFYNLPV 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589   158 RRKSM-DPRLEFEKVRQRVEALSLMHPSISFSLRNDvsGSMILQLPK-----TKDicSRFCQIYGLGKSQKLREIHY-KY 230
Cdd:TIGR00585  157 RRKFLkSPKKEFRKILDVLQRYALIHPDISFSLTHD--GKKVLQLSTkpnqsTKE--NRIRSVFGTAVLRKLIPLDEwED 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589   231 KEFEFNGYISSEAH---YNKNMQFLFVNRRLVLRTKLHKLIDfllrkesiicrpkngSASRQMNssPRHRsaselHGIYV 307
Cdd:TIGR00585  233 LDLQLEGFISQPNVtrsRRSGWQFLFINGRPVELKLLLKAIR---------------EVYHEYL--PKGQ-----YPVFV 290

                          330
                   ....*....|....*....
gi 564356589   308 INVQCPFCEYDVCIEPAKT 326
Cdd:TIGR00585  291 LNLEIDPELVDVNVHPDKK 309
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
26-354 9.64e-50

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 185.25  E-value: 9.64e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589   26 VEELTLNSIDAEATcvAIRVNME----TFqVQVIDNGLGMAGDDVEKVGNRYFTSKCHSVRDLENPTFYGFRGEALASIA 101
Cdd:COG0323    28 VKELVENAIDAGAT--RIEVEIEeggkSL-IRVTDNGCGMSPEDLPLAFERHATSKIRSAEDLFRIRTLGFRGEALASIA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  102 dmA-SAVEISSK-KSTTLKTFVKMfQNGKALAAREADLtrpSVGTTVTVYNLFYQFPVRRKSMD-PRLEFEKVRQRVEAL 178
Cdd:COG0323   105 --SvSRLTLTTRtAGAELGTRIEV-EGGKVVEVEPAAA---PKGTTVEVRDLFFNTPARRKFLKsDATELAHITDVVRRL 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  179 SLMHPSISFSLRNDvsGSMILQLPKTKDICSRFCQIYGLGKSQKLREIHYKYKEFEFNGYISSEAHY--NKNMQFLFVNR 256
Cdd:COG0323   179 ALAHPDIAFTLIHN--GREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKPEFSrsNRDYQYFFVNG 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  257 RLVlRtklhkliDFLLRK------ESIIcrpkngsasrqmnssPRHRsaselHGIYVINVQCPFCEYDVCIEPAKTLIEF 330
Cdd:COG0323   257 RPV-R-------DKLLSHavreayRDLL---------------PKGR-----YPVAVLFLELDPELVDVNVHPTKTEVRF 308

                         330       340
                  ....*....|....*....|....
gi 564356589  331 QNWDTVLICVQEGIKKFLKQEKLF 354
Cdd:COG0323   309 RDEREVYDLVRSAVREALAQAALG 332
mutL PRK00095
DNA mismatch repair endonuclease MutL;
26-351 4.13e-42

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 164.62  E-value: 4.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589   26 VEELTLNSIDAEATcvAIRVNME----TfQVQVIDNGLGMAGDDVEKVGNRYFTSKCHSVRDLENPTFYGFRGEALASIA 101
Cdd:PRK00095   27 VKELVENALDAGAT--RIDIEIEegglK-LIRVRDNGCGISKEDLALALARHATSKIASLDDLEAIRTLGFRGEALPSIA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  102 DMaSAVEISSKKSTTLKTFVKMFQNGKALAAREADLtrpSVGTTVTVYNLFYQFPVRRKSM-DPRLEFEKVRQRVEALSL 180
Cdd:PRK00095  104 SV-SRLTLTSRTADAAEGWQIVYEGGEIVEVKPAAH---PVGTTIEVRDLFFNTPARRKFLkSEKTELGHIDDVVNRLAL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  181 MHPSISFSLRNDvsGSMILQLPKTKDICSRFCQIYGLGKSQKLREIHYKYKEFEFNGYISS-EAHY-NKNMQFLFVNRRL 258
Cdd:PRK00095  180 AHPDVAFTLTHN--GKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLpTLSRaNRDYQYLFVNGRY 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  259 VlRtklhkliDFLLrkesiicrpkNGsASRQ--MNSSPRHRsaselHGIYVINVQCPFCEYDVCIEPAKTLIEFQNWDTV 336
Cdd:PRK00095  258 V-R-------DKLL----------NH-AIRQayHDLLPRGR-----YPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLV 313

                         330
                  ....*....|....*
gi 564356589  337 LICVQEGIKKFLKQE 351
Cdd:PRK00095  314 HDLIVQAIQEALAQS 328
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
1150-1365 2.23e-32

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 133.63  E-value: 2.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589 1150 QVDNKFIAClmssrTDGSGqaggnlLVLVDQHAAHERVRLEQLItDSYEKQAPQSagrKKLLsstiiPPLAITVSEEQRR 1229
Cdd:COG0323   333 QLHGTYILA-----ENEDG------LVLIDQHAAHERILYERLK-KALAEGGVAS---QPLL-----IPETLELSPAEAA 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589 1230 LLRSYHKHLEDLGLEL-LFpdaSDSSILVGKVPLCFVEREanelrrgrspvtksiVEELIREQLELLQTTGGIQGTLPLt 1308
Cdd:COG0323   393 LLEEHLEELARLGFEIePF---GPNTVAVRAVPALLGEGD---------------AEELLRDLLDELAEEGSSESLEEL- 453

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564356589 1309 VQKVLASQACHGAIKFNDRLSLEESCRLIEALSLCQLPFQCAHGRPSM--LPLADLDHL 1365
Cdd:COG0323   454 REELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTWieLSLEELEKL 512
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
 1147-1327 2.12e-29

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: 114.37  E-value: 2.12e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589   1147 VLQQVDNKFIACLMssrtdgsgqagGNLLVLVDQHAAHERVRLEQLITDsyekqapqsagRKKLLSSTIIPPLAITVSEE 1226
Cdd:smart00853    1 ALGQVAGTYILAER-----------EDGLYLLDQHAAHERILYEQLLKQ-----------AGGLESQPLLIPVRLELSPQ 58

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589   1227 QRRLLRSYHKHLEDLGLELLFPdaSDSSILVGKVPLCFVEREanelrrgrspvtksiVEELIREQLELLQTTGGIQgtLP 1306
Cdd:smart00853   59 EAALLEEHLELLRQLGFELEIF--GPQSLILRSVPALLRQQN---------------LQKLIPELLDLLSDEEENA--RP 119

                           170       180
                    ....*....|....*....|.
gi 564356589   1307 LTVQKVLASQACHGAIKFNDR 1327
Cdd:smart00853  120 SRLEALLASLACRSAIRAGDA 140
mutL PRK00095
DNA mismatch repair endonuclease MutL;
1175-1365 1.51e-27

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 119.94  E-value: 1.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589 1175 LVLVDQHAAHERVRLEQLitdsyeKQAPQSAGRKkllSSTIIPPLAITVSEEQRRLLRSYHKHLEDLGLELLfpDASDSS 1254
Cdd:PRK00095  450 LYLVDQHAAHERLLYEQL------KDKLAEVGLA---SQPLLIPLVLELSEDEADRLEEHKELLARLGLELE--PFGPNS 518

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589 1255 ILVGKVPLCFVEREanelrrgrspvtksiVEELIREQLELLQTTGGIQgtlPLTVQKVLASQACHGAIKFNDRLSLEESC 1334
Cdd:PRK00095  519 FAVREVPALLGQQE---------------LEELIRDLLDELAEEGDSD---TLKERELLATMACHGAIRAGRRLTLEEMN 580

                         170       180       190
                  ....*....|....*....|....*....|...
gi 564356589 1335 RLIEALSLCQLPFQCAHGRPSMLPL--ADLDHL 1365
Cdd:PRK00095  581 ALLRQLEATENPGTCPHGRPTYIELslSDLEKL 613
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
 1148-1328 1.26e-19

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: 86.89  E-value: 1.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  1148 LQQVDNKFIAClmsSRTDGsgqaggnlLVLVDQHAAHERVRLEQLitdsYEKQAPQSAGRKKLLSstiipPLAITVSEEQ 1227
Cdd:pfam08676    4 LGQVHGTYILA---ENEDG--------LYLIDQHAAHERILYEKL----KRALAEGGLAAQPLLI-----PLVLELSPEE 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  1228 RRLLRSYHKHLEDLGLEllFPDASDSSILVGKVPLCFveREANelrrgrspvtksiVEELIREQLELLQTTGGIqgTLPL 1307
Cdd:pfam08676   64 AALLEEHKEELAQLGFE--LEEFGPNSVIVRSVPALL--RQQN-------------LQELIRELLDELAEKGGS--SLEE 124

                          170       180
                   ....*....|....*....|.
gi 564356589  1308 TVQKVLASQACHGAIKFNDRL 1328
Cdd:pfam08676  125 SLEELLATMACHSAVRAGRRL 145
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 213-348 9.04e-12

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: 63.29  E-value: 9.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589   213 QIYGLGKSQKLREIHYKYKEFEFNGYIS--SEAHYNKNMQFLFVNRRLVLRTKLHKLIDfllrkesiicrpkngSASRqm 290
Cdd:pfam01119    2 AIYGKEFAENLLPIEKEDDGLRLSGYISkpTLSRSNRDYQYLFVNGRPVRDKLLSHAIR---------------EAYR-- 64

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 564356589   291 NSSPRHRsaselHGIYVINVQCPFCEYDVCIEPAKTLIEFQNWDTVLICVQEGIKKFL 348
Cdd:pfam01119   65 DLLPKGR-----YPVAVLFLEIDPELVDVNVHPTKREVRFRDEREVYDFIKEALREAL 117
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 22-80 6.59e-06

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 46.21  E-value: 6.59e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564356589    22 LGQCVEELTLNSIDAEATCVAIRVNME---TFQVQVIDNGLGMAGDDVEKVGNRYFTSKCHS 80
Cdd:pfam02518    6 LRQVLSNLLDNALKHAAKAGEITVTLSeggELTLTVEDNGIGIPPEDLPRIFEPFSTADKRG 67
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 22-77 4.77e-04

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 41.10  E-value: 4.77e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589     22 LGQCVEELTLNSIDAEATCVAIRVNMET----FQVQVIDNGLGMAGDDVEKVGNRYFTSK 77
Cdd:smart00387    6 LRQVLSNLLDNAIKYTPEGGRITVTLERdgdhVEITVEDNGPGIPPEDLEKIFEPFFRTD 65
 
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 1.23e-64

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: 215.26  E-value: 1.23e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  206 DICSRFCQIYGLGKSQKLREIHYKYKEFEFNGYISSEAHYNKNMQFLFVNRRLVLRTKLHKLIDFLLRKESIICRPKNGS 285
Cdd:cd03486     1 SILSVFKQIYGLVLAQKLKEVSAKFQEYEVSGYISSEGHYSKSFQFIYVNGRLYLKTRFHKLINKLFRKTSAVAKNKSSP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564356589  286 ASRQMnssPRHRSASELHGIYVINVQCPFCEYDVCIEPAKTLIEFQNWDTVLICVQEGIKKFLK 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 1.16e-60

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: 205.75  E-value: 1.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589    9 VQAKLRSGLALSSLGQCVEELTLNSIDAEATCVAIRVNMETFQ-VQVIDNGLGMAGDDVEKVGNRYFTSKCHSVRDLENP 87
Cdd:cd16926     1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKlIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589   88 TFYGFRGEALASIADMaSAVEISSKKSTTLKTFVKMFQNGKALAAREAdlTRPSVGTTVTVYNLFYQFPVRRKSM-DPRL 166
Cdd:cd16926    81 TTLGFRGEALASIASV-SRLTITTRTADDDVGTRLVVDGGGIIEEVKP--AAAPVGTTVTVRDLFYNTPARRKFLkSPKT 157

                         170       180
                  ....*....|....*....|....*.
gi 564356589  167 EFEKVRQRVEALSLMHPSISFSLRND 192
Cdd:cd16926   158 ELSKILDLVQRLALAHPDVSFSLTHD 183
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 1-326 5.74e-53

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: 188.62  E-value: 5.74e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589     1 MIRCLSDEVQAKLRSGLALSSLGQCVEELTLNSIDAEATcvAIRVNMETF---QVQVIDNGLGMAGDDVEKVGNRYFTSK 77
Cdd:TIGR00585    2 TIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGAT--RIDVEIEEGglkLIEVSDNGSGIDKEDLPLACERHATSK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589    78 CHSVRDLENPTFYGFRGEALASIADmASAVEISSKKSTTLKTFVKMFQNGKALAAREADlTRPsVGTTVTVYNLFYQFPV 157
Cdd:TIGR00585   80 IQSFEDLERIETLGFRGEALASISS-VSRLTITTKTSAADGLAYQALLEGGMIESIKPA-PRP-VGTTVEVRDLFYNLPV 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589   158 RRKSM-DPRLEFEKVRQRVEALSLMHPSISFSLRNDvsGSMILQLPK-----TKDicSRFCQIYGLGKSQKLREIHY-KY 230
Cdd:TIGR00585  157 RRKFLkSPKKEFRKILDVLQRYALIHPDISFSLTHD--GKKVLQLSTkpnqsTKE--NRIRSVFGTAVLRKLIPLDEwED 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589   231 KEFEFNGYISSEAH---YNKNMQFLFVNRRLVLRTKLHKLIDfllrkesiicrpkngSASRQMNssPRHRsaselHGIYV 307
Cdd:TIGR00585  233 LDLQLEGFISQPNVtrsRRSGWQFLFINGRPVELKLLLKAIR---------------EVYHEYL--PKGQ-----YPVFV 290

                          330
                   ....*....|....*....
gi 564356589   308 INVQCPFCEYDVCIEPAKT 326
Cdd:TIGR00585  291 LNLEIDPELVDVNVHPDKK 309
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
26-354 9.64e-50

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 185.25  E-value: 9.64e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589   26 VEELTLNSIDAEATcvAIRVNME----TFqVQVIDNGLGMAGDDVEKVGNRYFTSKCHSVRDLENPTFYGFRGEALASIA 101
Cdd:COG0323    28 VKELVENAIDAGAT--RIEVEIEeggkSL-IRVTDNGCGMSPEDLPLAFERHATSKIRSAEDLFRIRTLGFRGEALASIA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  102 dmA-SAVEISSK-KSTTLKTFVKMfQNGKALAAREADLtrpSVGTTVTVYNLFYQFPVRRKSMD-PRLEFEKVRQRVEAL 178
Cdd:COG0323   105 --SvSRLTLTTRtAGAELGTRIEV-EGGKVVEVEPAAA---PKGTTVEVRDLFFNTPARRKFLKsDATELAHITDVVRRL 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  179 SLMHPSISFSLRNDvsGSMILQLPKTKDICSRFCQIYGLGKSQKLREIHYKYKEFEFNGYISSEAHY--NKNMQFLFVNR 256
Cdd:COG0323   179 ALAHPDIAFTLIHN--GREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKPEFSrsNRDYQYFFVNG 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  257 RLVlRtklhkliDFLLRK------ESIIcrpkngsasrqmnssPRHRsaselHGIYVINVQCPFCEYDVCIEPAKTLIEF 330
Cdd:COG0323   257 RPV-R-------DKLLSHavreayRDLL---------------PKGR-----YPVAVLFLELDPELVDVNVHPTKTEVRF 308

                         330       340
                  ....*....|....*....|....
gi 564356589  331 QNWDTVLICVQEGIKKFLKQEKLF 354
Cdd:COG0323   309 RDEREVYDLVRSAVREALAQAALG 332
mutL PRK00095
DNA mismatch repair endonuclease MutL;
26-351 4.13e-42

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 164.62  E-value: 4.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589   26 VEELTLNSIDAEATcvAIRVNME----TfQVQVIDNGLGMAGDDVEKVGNRYFTSKCHSVRDLENPTFYGFRGEALASIA 101
Cdd:PRK00095   27 VKELVENALDAGAT--RIDIEIEegglK-LIRVRDNGCGISKEDLALALARHATSKIASLDDLEAIRTLGFRGEALPSIA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  102 DMaSAVEISSKKSTTLKTFVKMFQNGKALAAREADLtrpSVGTTVTVYNLFYQFPVRRKSM-DPRLEFEKVRQRVEALSL 180
Cdd:PRK00095  104 SV-SRLTLTSRTADAAEGWQIVYEGGEIVEVKPAAH---PVGTTIEVRDLFFNTPARRKFLkSEKTELGHIDDVVNRLAL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  181 MHPSISFSLRNDvsGSMILQLPKTKDICSRFCQIYGLGKSQKLREIHYKYKEFEFNGYISS-EAHY-NKNMQFLFVNRRL 258
Cdd:PRK00095  180 AHPDVAFTLTHN--GKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLpTLSRaNRDYQYLFVNGRY 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  259 VlRtklhkliDFLLrkesiicrpkNGsASRQ--MNSSPRHRsaselHGIYVINVQCPFCEYDVCIEPAKTLIEFQNWDTV 336
Cdd:PRK00095  258 V-R-------DKLL----------NH-AIRQayHDLLPRGR-----YPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLV 313

                         330
                  ....*....|....*
gi 564356589  337 LICVQEGIKKFLKQE 351
Cdd:PRK00095  314 HDLIVQAIQEALAQS 328
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
1150-1365 2.23e-32

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 133.63  E-value: 2.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589 1150 QVDNKFIAClmssrTDGSGqaggnlLVLVDQHAAHERVRLEQLItDSYEKQAPQSagrKKLLsstiiPPLAITVSEEQRR 1229
Cdd:COG0323   333 QLHGTYILA-----ENEDG------LVLIDQHAAHERILYERLK-KALAEGGVAS---QPLL-----IPETLELSPAEAA 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589 1230 LLRSYHKHLEDLGLEL-LFpdaSDSSILVGKVPLCFVEREanelrrgrspvtksiVEELIREQLELLQTTGGIQGTLPLt 1308
Cdd:COG0323   393 LLEEHLEELARLGFEIePF---GPNTVAVRAVPALLGEGD---------------AEELLRDLLDELAEEGSSESLEEL- 453

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564356589 1309 VQKVLASQACHGAIKFNDRLSLEESCRLIEALSLCQLPFQCAHGRPSM--LPLADLDHL 1365
Cdd:COG0323   454 REELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTWieLSLEELEKL 512
MutL_Trans cd00782
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 209-348 4.18e-32

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: 121.49  E-value: 4.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  209 SRFCQIYGLGKSQKLREIHYKYKEFEFNGYISSEAHY--NKNMQFLFVNRRLVLRTKLHKLIDFLLRkesiicrpkngsa 286
Cdd:cd00782     3 DRIAQVYGKEVAKNLIEVELESGDFRISGYISKPDFGrsSKDRQFLFVNGRPVRDKLLSKAINEAYR------------- 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564356589  287 srqmNSSPRHRsaselHGIYVINVQCPFCEYDVCIEPAKTLIEFQNWDTVLICVQEGIKKFL 348
Cdd:cd00782    70 ----SYLPKGR-----YPVFVLNLELPPELVDVNVHPTKREVRFSDEEEVLELIREALRSAL 122
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
 1147-1327 2.12e-29

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: 114.37  E-value: 2.12e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589   1147 VLQQVDNKFIACLMssrtdgsgqagGNLLVLVDQHAAHERVRLEQLITDsyekqapqsagRKKLLSSTIIPPLAITVSEE 1226
Cdd:smart00853    1 ALGQVAGTYILAER-----------EDGLYLLDQHAAHERILYEQLLKQ-----------AGGLESQPLLIPVRLELSPQ 58

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589   1227 QRRLLRSYHKHLEDLGLELLFPdaSDSSILVGKVPLCFVEREanelrrgrspvtksiVEELIREQLELLQTTGGIQgtLP 1306
Cdd:smart00853   59 EAALLEEHLELLRQLGFELEIF--GPQSLILRSVPALLRQQN---------------LQKLIPELLDLLSDEEENA--RP 119

                           170       180
                    ....*....|....*....|.
gi 564356589   1307 LTVQKVLASQACHGAIKFNDR 1327
Cdd:smart00853  120 SRLEALLASLACRSAIRAGDA 140
mutL PRK00095
DNA mismatch repair endonuclease MutL;
1175-1365 1.51e-27

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 119.94  E-value: 1.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589 1175 LVLVDQHAAHERVRLEQLitdsyeKQAPQSAGRKkllSSTIIPPLAITVSEEQRRLLRSYHKHLEDLGLELLfpDASDSS 1254
Cdd:PRK00095  450 LYLVDQHAAHERLLYEQL------KDKLAEVGLA---SQPLLIPLVLELSEDEADRLEEHKELLARLGLELE--PFGPNS 518

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589 1255 ILVGKVPLCFVEREanelrrgrspvtksiVEELIREQLELLQTTGGIQgtlPLTVQKVLASQACHGAIKFNDRLSLEESC 1334
Cdd:PRK00095  519 FAVREVPALLGQQE---------------LEELIRDLLDELAEEGDSD---TLKERELLATMACHGAIRAGRRLTLEEMN 580

                         170       180       190
                  ....*....|....*....|....*....|...
gi 564356589 1335 RLIEALSLCQLPFQCAHGRPSMLPL--ADLDHL 1365
Cdd:PRK00095  581 ALLRQLEATENPGTCPHGRPTYIELslSDLEKL 613
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
 1148-1328 1.26e-19

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: 86.89  E-value: 1.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  1148 LQQVDNKFIAClmsSRTDGsgqaggnlLVLVDQHAAHERVRLEQLitdsYEKQAPQSAGRKKLLSstiipPLAITVSEEQ 1227
Cdd:pfam08676    4 LGQVHGTYILA---ENEDG--------LYLIDQHAAHERILYEKL----KRALAEGGLAAQPLLI-----PLVLELSPEE 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  1228 RRLLRSYHKHLEDLGLEllFPDASDSSILVGKVPLCFveREANelrrgrspvtksiVEELIREQLELLQTTGGIqgTLPL 1307
Cdd:pfam08676   64 AALLEEHKEELAQLGFE--LEEFGPNSVIVRSVPALL--RQQN-------------LQELIRELLDELAEKGGS--SLEE 124

                          170       180
                   ....*....|....*....|.
gi 564356589  1308 TVQKVLASQACHGAIKFNDRL 1328
Cdd:pfam08676  125 SLEELLATMACHSAVRAGRRL 145
TopoII_MutL_Trans cd00329
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 207-328 3.67e-15

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: 72.68  E-value: 3.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  207 ICSRFCQIYGLGKSQKLREIHYKYKEFEFNGYISS--EAHYNKNMQFLFVNRRLVLRTKLH-KLIDFLLRkesiicrpkn 283
Cdd:cd00329     1 LKDRLAEILGDKVADKLIYVEGESDGFRVEGAISYpdSGRSSKDRQFSFVNGRPVREGGTHvKAVREAYT---------- 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 564356589  284 gsasRQMNSSPRHRsaselHGIYVINVQCPFCEYDVCIEPAKTLI 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 9.04e-12

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: 63.29  E-value: 9.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589   213 QIYGLGKSQKLREIHYKYKEFEFNGYIS--SEAHYNKNMQFLFVNRRLVLRTKLHKLIDfllrkesiicrpkngSASRqm 290
Cdd:pfam01119    2 AIYGKEFAENLLPIEKEDDGLRLSGYISkpTLSRSNRDYQYLFVNGRPVRDKLLSHAIR---------------EAYR-- 64

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 564356589   291 NSSPRHRsaselHGIYVINVQCPFCEYDVCIEPAKTLIEFQNWDTVLICVQEGIKKFL 348
Cdd:pfam01119   65 DLLPKGR-----YPVAVLFLEIDPELVDVNVHPTKREVRFRDEREVYDFIKEALREAL 117
MutL_Trans_hPMS_1_like cd03485
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 250-349 3.81e-07

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: 50.73  E-value: 3.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  250 QFLFVNRRLVLRTK-LHKLIDFLLRKESiicrpkngsasrqmnssprHRSASELHGIYVINVQCPFCEYDVCIEPAKTLI 328
Cdd:cd03485    51 KFISVNSRPVSLGKdIGKLLRQYYSSAY-------------------RKSSLRRYPVFFLNILCPPGLVDVNIEPDKDDV 111

                          90       100
                  ....*....|....*....|.
gi 564356589  329 EFQNWDTVLICVQEGIKKFLK 349
Cdd:cd03485   112 LLQNKEAVLQAVENLLESLYG 132
MutL_Trans_hPMS_2_like cd03484
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 231-347 4.23e-06

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: 47.65  E-value: 4.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589  231 KEFEFNGYISSEAHY----NKNMQFLFVNRRLVLRTKLHKLIDFLLRKESiicrpkngsaSRQmnsSPrhrsaselhgIY 306
Cdd:cd03484    43 SEVKITGYISKPSHGcgrsSSDRQFFYINGRPVDLKKVAKLINEVYKSFN----------SRQ---YP----------FF 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 564356589  307 VINVQCPFCEYDVCIEPAKTLIEFQNWDTVLICVQEGIKKF 347
Cdd:cd03484   100 ILNISLPTSLYDVNVTPDKRTVLLHDEDRLIDTLKTSLSEL 140
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 22-80 6.59e-06

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 46.21  E-value: 6.59e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564356589    22 LGQCVEELTLNSIDAEATCVAIRVNME---TFQVQVIDNGLGMAGDDVEKVGNRYFTSKCHS 80
Cdd:pfam02518    6 LRQVLSNLLDNALKHAAKAGEITVTLSeggELTLTVEDNGIGIPPEDLPRIFEPFSTADKRG 67
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 22-77 4.77e-04

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 41.10  E-value: 4.77e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564356589     22 LGQCVEELTLNSIDAEATCVAIRVNMET----FQVQVIDNGLGMAGDDVEKVGNRYFTSK 77
Cdd:smart00387    6 LRQVLSNLLDNAIKYTPEGGRITVTLERdgdhVEITVEDNGPGIPPEDLEKIFEPFFRTD 65
 
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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