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Conserved domains on  [gi|2545606437|gb|WKF25444|]
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MUTL-like protein 1, partial [Rorippa islandica]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TopoII_MutL_Trans super family cl02783
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 60-153 1.13e-43

MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the C-terminal domain of type II DNA topoisomerases (Topo II) and DNA mismatch repair (MutL/MLH1/PMS2) proteins. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. The GyrB dimerizes in response to ATP binding, and is homologous to the N-terminal half of eukaryotic Topo II and the ATPase fragment of MutL. Type II DNA topoisomerases catalyze the ATP-dependent transport of one DNA duplex through another, in the process generating transient double strand breaks via covalent attachments to both DNA strands at the 5' positions. Included in this group are proteins similar to human MLH1 and PMS2. MLH1 forms a heterodimer with PMS2 which functions in meiosis and in DNA mismatch repair (MMR). Cells lacking either hMLH1 or hPMS2 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hMLH1 accounts for a large fraction of Lynch syndrome (HNPCC) families.


The actual alignment was detected with superfamily member cd03483:

Pssm-ID: 445919 [Multi-domain]  Cd Length: 127  Bit Score: 140.45  E-value: 1.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545606437  60 SRLDSIRSVYGVSVAKNLMKVEVSSCDSsGCTFDMDGFISNSNYVAKKTILVLFINDRLVECSTLKRAIEIVYAATLPKA 139
Cdd:cd03483     1 STKDNIRSVYGAAVANELIEVEISDDDD-DLGFKVKGLISNANYSKKKIIFILFINNRLVECSALRRAIENVYANYLPKG 79

                          90
                  ....*....|....*
gi 2545606437 140 SKPFVYMSINL-PQN 153
Cdd:cd03483    80 AHPFVYLSLEIpPEN 94
HATPase super family cl00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
 1-47 1.63e-14

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.


The actual alignment was detected with superfamily member cd16926:

Pssm-ID: 469604 [Multi-domain]  Cd Length: 188  Bit Score: 67.08  E-value: 1.63e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2545606437   1 VENLFYNMIARRKTLQNSADDYGKIVDLLSRMAIHHNKVSFSCRKHG 47
Cdd:cd16926   138 VRDLFYNTPARRKFLKSPKTELSKILDLVQRLALAHPDVSFSLTHDG 184
 
Name Accession Description Interval E-value
MutL_Trans_MLH1 cd03483
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 60-153 1.13e-43

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: 140.45  E-value: 1.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545606437  60 SRLDSIRSVYGVSVAKNLMKVEVSSCDSsGCTFDMDGFISNSNYVAKKTILVLFINDRLVECSTLKRAIEIVYAATLPKA 139
Cdd:cd03483     1 STKDNIRSVYGAAVANELIEVEISDDDD-DLGFKVKGLISNANYSKKKIIFILFINNRLVECSALRRAIENVYANYLPKG 79

                          90
                  ....*....|....*
gi 2545606437 140 SKPFVYMSINL-PQN 153
Cdd:cd03483    80 AHPFVYLSLEIpPEN 94
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 1-151 5.62e-30

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: 110.42  E-value: 5.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545606437   1 VENLFYNMIARRKTLQNSADDYGKIVDLLSRMAIHHNKVSFSCRKHGAVKADVHSVVSSS-RLDSIRSVYGVSVAKNLMK 79
Cdd:TIGR00585 147 VRDLFYNLPVRRKFLKSPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLQLSTKPNQStKENRIRSVFGTAVLRKLIP 226

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545606437  80 VEvsscDSSGCTFDMDGFISNSNY--VAKKTILVLFINDRLVECSTLKRAIEIVYAATLPKASKPFVYMSINLP 151
Cdd:TIGR00585 227 LD----EWEDLDLQLEGFISQPNVtrSRRSGWQFLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEID 296
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
1-151 2.03e-19

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 83.55  E-value: 2.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545606437   1 VENLFYNMIARRKTLQNSADDYGKIVDLLSRMAIHHNKVSFSCRKHGAVKadVHSVVSSSRLDSIRSVYGVSVAKNLMKV 80
Cdd:COG0323   147 VRDLFFNTPARRKFLKSDATELAHITDVVRRLALAHPDIAFTLIHNGREV--FQLPGAGDLLQRIAAIYGREFAENLLPV 224

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545606437  81 EVSSCDssgctFDMDGFISNSNYvAKKTI--LVLFINDRLVECSTLKRAIEIVYAATLPKASKPFVYMSINLP 151
Cdd:COG0323   225 EAEREG-----LRLSGYIGKPEF-SRSNRdyQYFFVNGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELD 291
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 66-151 1.89e-16

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: 70.60  E-value: 1.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545606437  66 RSVYGVSVAKNLMKVEVSSCDssgctFDMDGFISNSNYV-AKKTILVLFINDRLVECSTLKRAIEIVYAATLPKASKPFV 144
Cdd:pfam01119   1 AAIYGKEFAENLLPIEKEDDG-----LRLSGYISKPTLSrSNRDYQYLFVNGRPVRDKLLSHAIREAYRDLLPKGRYPVA 75


                  ....*..
gi 2545606437 145 YMSINLP 151
Cdd:pfam01119  76 VLFLEID 82
mutL PRK00095
DNA mismatch repair endonuclease MutL;
1-151 2.54e-15

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 71.79  E-value: 2.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545606437   1 VENLFYNMIARRKTLQNSADDYGKIVDLLSRMAIHHNKVSFSCRKHGavKADVHSVVSSSRLDSIRSVYGVSVAKNLMKV 80
Cdd:PRK00095  146 VRDLFFNTPARRKFLKSEKTELGHIDDVVNRLALAHPDVAFTLTHNG--KLVLQTRGAGQLLQRLAAILGREFAENALPI 223

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545606437  81 EVSSCDssgctFDMDGFI-------SNSNYVAkktilvLFINDRLVECSTLKRAIEIVYAATLPKASKPFVYMSINLP 151
Cdd:PRK00095  224 DAEHGD-----LRLSGYVglptlsrANRDYQY------LFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELD 290
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 1-47 1.63e-14

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: 67.08  E-value: 1.63e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2545606437   1 VENLFYNMIARRKTLQNSADDYGKIVDLLSRMAIHHNKVSFSCRKHG 47
Cdd:cd16926   138 VRDLFYNTPARRKFLKSPKTELSKILDLVQRLALAHPDVSFSLTHDG 184
 
Name Accession Description Interval E-value
MutL_Trans_MLH1 cd03483
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 60-153 1.13e-43

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: 140.45  E-value: 1.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545606437  60 SRLDSIRSVYGVSVAKNLMKVEVSSCDSsGCTFDMDGFISNSNYVAKKTILVLFINDRLVECSTLKRAIEIVYAATLPKA 139
Cdd:cd03483     1 STKDNIRSVYGAAVANELIEVEISDDDD-DLGFKVKGLISNANYSKKKIIFILFINNRLVECSALRRAIENVYANYLPKG 79

                          90
                  ....*....|....*
gi 2545606437 140 SKPFVYMSINL-PQN 153
Cdd:cd03483    80 AHPFVYLSLEIpPEN 94
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 1-151 5.62e-30

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: 110.42  E-value: 5.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545606437   1 VENLFYNMIARRKTLQNSADDYGKIVDLLSRMAIHHNKVSFSCRKHGAVKADVHSVVSSS-RLDSIRSVYGVSVAKNLMK 79
Cdd:TIGR00585 147 VRDLFYNLPVRRKFLKSPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLQLSTKPNQStKENRIRSVFGTAVLRKLIP 226

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545606437  80 VEvsscDSSGCTFDMDGFISNSNY--VAKKTILVLFINDRLVECSTLKRAIEIVYAATLPKASKPFVYMSINLP 151
Cdd:TIGR00585 227 LD----EWEDLDLQLEGFISQPNVtrSRRSGWQFLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEID 296
MutL_Trans cd00782
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 62-151 2.21e-20

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: 80.66  E-value: 2.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545606437  62 LDSIRSVYGVSVAKNLMKVEVSSCDssgctFDMDGFISNSN-YVAKKTILVLFINDRLVECSTLKRAIEIVYAATLPKAS 140
Cdd:cd00782     2 KDRIAQVYGKEVAKNLIEVELESGD-----FRISGYISKPDfGRSSKDRQFLFVNGRPVRDKLLSKAINEAYRSYLPKGR 76

                          90
                  ....*....|.
gi 2545606437 141 KPFVYMSINLP 151
Cdd:cd00782    77 YPVFVLNLELP 87
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
1-151 2.03e-19

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 83.55  E-value: 2.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545606437   1 VENLFYNMIARRKTLQNSADDYGKIVDLLSRMAIHHNKVSFSCRKHGAVKadVHSVVSSSRLDSIRSVYGVSVAKNLMKV 80
Cdd:COG0323   147 VRDLFFNTPARRKFLKSDATELAHITDVVRRLALAHPDIAFTLIHNGREV--FQLPGAGDLLQRIAAIYGREFAENLLPV 224

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545606437  81 EVSSCDssgctFDMDGFISNSNYvAKKTI--LVLFINDRLVECSTLKRAIEIVYAATLPKASKPFVYMSINLP 151
Cdd:COG0323   225 EAEREG-----LRLSGYIGKPEF-SRSNRdyQYFFVNGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELD 291
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 66-151 1.89e-16

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: 70.60  E-value: 1.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545606437  66 RSVYGVSVAKNLMKVEVSSCDssgctFDMDGFISNSNYV-AKKTILVLFINDRLVECSTLKRAIEIVYAATLPKASKPFV 144
Cdd:pfam01119   1 AAIYGKEFAENLLPIEKEDDG-----LRLSGYISKPTLSrSNRDYQYLFVNGRPVRDKLLSHAIREAYRDLLPKGRYPVA 75


                  ....*..
gi 2545606437 145 YMSINLP 151
Cdd:pfam01119  76 VLFLEID 82
mutL PRK00095
DNA mismatch repair endonuclease MutL;
1-151 2.54e-15

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 71.79  E-value: 2.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545606437   1 VENLFYNMIARRKTLQNSADDYGKIVDLLSRMAIHHNKVSFSCRKHGavKADVHSVVSSSRLDSIRSVYGVSVAKNLMKV 80
Cdd:PRK00095  146 VRDLFFNTPARRKFLKSEKTELGHIDDVVNRLALAHPDVAFTLTHNG--KLVLQTRGAGQLLQRLAAILGREFAENALPI 223

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545606437  81 EVSSCDssgctFDMDGFI-------SNSNYVAkktilvLFINDRLVECSTLKRAIEIVYAATLPKASKPFVYMSINLP 151
Cdd:PRK00095  224 DAEHGD-----LRLSGYVglptlsrANRDYQY------LFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELD 290
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 1-47 1.63e-14

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: 67.08  E-value: 1.63e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2545606437   1 VENLFYNMIARRKTLQNSADDYGKIVDLLSRMAIHHNKVSFSCRKHG 47
Cdd:cd16926   138 VRDLFYNTPARRKFLKSPKTELSKILDLVQRLALAHPDVSFSLTHDG 184
MutL_Trans_hPMS_2_like cd03484
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 62-153 4.71e-03

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: 35.32  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545606437  62 LDSIRSVYGVSVAKNLMKVEVSSCDSSGCT------------FDMDGFISNSNY---VAKKTILVLFINDRLVECSTLKR 126
Cdd:cd03484     3 KDNIINVFGGKVIKGLIPINLELDVNPTKEeldsdedladseVKITGYISKPSHgcgRSSSDRQFFYINGRPVDLKKVAK 82

                          90       100
                  ....*....|....*....|....*..
gi 2545606437 127 AIEIVYaATLPKASKPFVYMSINLPQN 153
Cdd:cd03484    83 LINEVY-KSFNSRQYPFFILNISLPTS 108
 
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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