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Conserved domains on  [gi|255958238|ref|NP_081086.2|]
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DNA mismatch repair protein Mlh1 isoform 1 [Mus musculus]

Protein Classification

MutL_Trans_MLH1 and Mlh1_C domain-containing protein (domain architecture ID 10892065)

protein containing domains HATPase_c, MutL_Trans_MLH1, and Mlh1_C

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Mlh1_C pfam16413
DNA mismatch repair protein Mlh1 C-terminus; This is the C-terminal domain of DNA mismatch ...
505-760 3.15e-146

DNA mismatch repair protein Mlh1 C-terminus; This is the C-terminal domain of DNA mismatch repair protein Mlh1, these proteins belong to the MutL family. This domain forms part of the endonuclease active site.


:

Pssm-ID: 293022  Cd Length: 254  Bit Score: 431.14  E-value: 3.15e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238  505 INLTSVLSLQEEISERCHETLREMLRNHSFVGCVNPQWALAQHQTKLYLLNTTKLSEELFYQILIYDFANFGVLRLSEPA 584
Cdd:pfam16413   2 VRLTSVKELRAEVEENMHKGLTEIFRNHTFVGCVDERLALIQHGTKLYLVNYGALSEELFYQLGLRDFGNFGRIRLSPPL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238  585 PLFDLAMLALDSPESGWTEDDGPKEGLAEYIVEFLKKKAEMLADYFSVEIDEEGNLIGLPLLIDSYVPPLEGLPIFILRL 664
Cdd:pfam16413  82 PLRELLLLALESEESGWTEEDGPKEELAEKIVELLIEKAEMLEEYFSIEIDEDGNLESLPLLLKGYTPNLDKLPLFLLRL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238  665 ATEVNWDEEKECFESLSKECAMFYSIRKQYILEESTlsGQQSDMPGSTSKPWKWTVEHIIYKAFRSHLLPPKHFTEDGnV 744
Cdd:pfam16413 162 ATEVDWEDEKECFETILRELALFYAPEPLPSPDPSD--DEEDEEIEARRESWKWVIEHVLFPAIKRRLLPPKSLADDT-V 238
                         250
                  ....*....|....*.
gi 255958238  745 LQLANLPDLYKVFERC 760
Cdd:pfam16413 239 VQVASLPDLYKVFERC 254
MutL_Trans_MLH1 cd03483
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
211-335 4.50e-73

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  Cd Length: 127  Bit Score: 235.21  E-value: 4.50e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 211 TTVDNIRSIFGNAVSRELIEVGCEDKT--LAFKMNGYISNANYSVKKCIFLLFINHRLVESAALRKAIETVYAAYLPKNT 288
Cdd:cd03483    1 STKDNIRSVYGAAVANELIEVEISDDDddLGFKVKGLISNANYSKKKIIFILFINNRLVECSALRRAIENVYANYLPKGA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 255958238 289 HPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILQRVQQHIESKLL 335
Cdd:cd03483   81 HPFVYLSLEIPPENVDVNVHPTKREVHFLNEEEIIERIQKLVEDKLS 127
HATPase_c super family cl00075
Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: ...
31-132 2.08e-10

Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: histidine kinase, DNA gyrase B, topoisomerases, heat shock protein HSP90, phytochrome-like ATPases and DNA mismatch repair proteins


The actual alignment was detected with superfamily member pfam13589:

Pssm-ID: 294057  Cd Length: 135  Bit Score: 59.24  E-value: 2.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238   31 AIKEMIENCLDAKSTNIQVVVKEGGLKLIQIQDNGTGIRKEDLDIVCeRFTTSKLQTFEDLASISTYGFrGEALASISHV 110
Cdd:pfam13589   6 ALAELVDNSYDADATNVKIEVNKNPGGEIVIEDDGHGMSEEELINAL-RLATPDKEAERDSTDLGRKGI-GMKLASLSLG 83
                          90       100
                  ....*....|....*....|..
gi 255958238  111 AHVTITTKTADGKCAYRASYSD 132
Cdd:pfam13589  84 RKLTVTTKKEGESSTLTLDVDW 105
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
6-315 3.34e-139

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: 415.50  E-value: 3.34e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238    6 GVIRRLDETVVNRIAAGEVIQRPANAIKEMIENCLDAKSTNIQVVVKEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSKL 85
Cdd:TIGR00585   1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238   86 QTFEDLASISTYGFRGEALASISHVAHVTITTKT-ADGKCAYRASYsDGKLQAPPKPCAGNQGTLITVEDLFYNIITRRK 164
Cdd:TIGR00585  81 QSFEDLERIETLGFRGEALASISSVSRLTITTKTsAADGLAYQALL-EGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238  165 ALKNPSEEYGKILEVVGRYSIHNSGISFSVKKQGETVSDVRTLPNATTVDN-IRSIFGNAVSRELIEVGcEDKTLAFKMN 243
Cdd:TIGR00585 160 FLKSPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLQLSTKPNQSTKENrIRSVFGTAVLRKLIPLD-EWEDLDLQLE 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255958238  244 GYISNANYSVKKCI--FLLFINHRLVESAALRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVH 315
Cdd:TIGR00585 239 GFISQPNVTRSRRSgwQFLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
 
Name Accession Description Interval E-value
Mlh1_C pfam16413
DNA mismatch repair protein Mlh1 C-terminus; This is the C-terminal domain of DNA mismatch ...
505-760 3.15e-146

DNA mismatch repair protein Mlh1 C-terminus; This is the C-terminal domain of DNA mismatch repair protein Mlh1, these proteins belong to the MutL family. This domain forms part of the endonuclease active site.


Pssm-ID: 293022  Cd Length: 254  Bit Score: 431.14  E-value: 3.15e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238  505 INLTSVLSLQEEISERCHETLREMLRNHSFVGCVNPQWALAQHQTKLYLLNTTKLSEELFYQILIYDFANFGVLRLSEPA 584
Cdd:pfam16413   2 VRLTSVKELRAEVEENMHKGLTEIFRNHTFVGCVDERLALIQHGTKLYLVNYGALSEELFYQLGLRDFGNFGRIRLSPPL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238  585 PLFDLAMLALDSPESGWTEDDGPKEGLAEYIVEFLKKKAEMLADYFSVEIDEEGNLIGLPLLIDSYVPPLEGLPIFILRL 664
Cdd:pfam16413  82 PLRELLLLALESEESGWTEEDGPKEELAEKIVELLIEKAEMLEEYFSIEIDEDGNLESLPLLLKGYTPNLDKLPLFLLRL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238  665 ATEVNWDEEKECFESLSKECAMFYSIRKQYILEESTlsGQQSDMPGSTSKPWKWTVEHIIYKAFRSHLLPPKHFTEDGnV 744
Cdd:pfam16413 162 ATEVDWEDEKECFETILRELALFYAPEPLPSPDPSD--DEEDEEIEARRESWKWVIEHVLFPAIKRRLLPPKSLADDT-V 238
                         250
                  ....*....|....*.
gi 255958238  745 LQLANLPDLYKVFERC 760
Cdd:pfam16413 239 VQVASLPDLYKVFERC 254
MutL_Trans_MLH1 cd03483
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
211-335 4.50e-73

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  Cd Length: 127  Bit Score: 235.21  E-value: 4.50e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 211 TTVDNIRSIFGNAVSRELIEVGCEDKT--LAFKMNGYISNANYSVKKCIFLLFINHRLVESAALRKAIETVYAAYLPKNT 288
Cdd:cd03483    1 STKDNIRSVYGAAVANELIEVEISDDDddLGFKVKGLISNANYSKKKIIFILFINNRLVECSALRRAIENVYANYLPKGA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 255958238 289 HPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILQRVQQHIESKLL 335
Cdd:cd03483   81 HPFVYLSLEIPPENVDVNVHPTKREVHFLNEEEIIERIQKLVEDKLS 127
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
217-334 9.82e-41

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: 279463  Cd Length: 117  Bit Score: 145.71  E-value: 9.82e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238  217 RSIFGNAVSRELIEVGCEDKTlaFKMNGYISNANYS-VKKCIFLLFINHRLVESAALRKAIETVYAAYLPKNTHPFLYLS 295
Cdd:pfam01119   1 AAIYGKEFAKNLLPIEGEDDD--LRLSGYISKPELTrSNRDYQYLFVNGRPVRDKLLSKAIREAYRDLLPKGRYPVAVLF 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 255958238  296 LEISPQNVDVNVHPTKHEVHFLHEESILQRVQQHIESKL 334
Cdd:pfam01119  79 LEIDPELVDVNVHPAKREVRFSDEREVYDFIYEAIREAL 117
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
31-132 2.08e-10

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


Pssm-ID: 290321  Cd Length: 135  Bit Score: 59.24  E-value: 2.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238   31 AIKEMIENCLDAKSTNIQVVVKEGGLKLIQIQDNGTGIRKEDLDIVCeRFTTSKLQTFEDLASISTYGFrGEALASISHV 110
Cdd:pfam13589   6 ALAELVDNSYDADATNVKIEVNKNPGGEIVIEDDGHGMSEEELINAL-RLATPDKEAERDSTDLGRKGI-GMKLASLSLG 83
                          90       100
                  ....*....|....*....|..
gi 255958238  111 AHVTITTKTADGKCAYRASYSD 132
Cdd:pfam13589  84 RKLTVTTKKEGESSTLTLDVDW 105
HATPase_c cd00075
Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: ...
31-122 3.85e-08

Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: histidine kinase, DNA gyrase B, topoisomerases, heat shock protein HSP90, phytochrome-like ATPases and DNA mismatch repair proteins


Pssm-ID: 238030  Cd Length: 103  Bit Score: 51.88  E-value: 3.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238  31 AIKEMIENCLDA---KSTNIQVVVKEGGLKL-IQIQDNGTGIRKEDLDIVCERfttsklqtFEDLASISTYGFRGEALAS 106
Cdd:cd00075    4 VLLNLLSNAIKHtpeGGGRITISVERDGDHLeIRVEDNGPGIPEEDLERIFER--------FSDGSRSRKGGGTGLGLSI 75
                         90       100
                 ....*....|....*....|.
gi 255958238 107 ISHVA-----HVTITTKTADG 122
Cdd:cd00075   76 VKKLVelhggRIEVESEPGGG 96
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
31-84 6.54e-05

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


Pssm-ID: 214643  Cd Length: 111  Bit Score: 41.87  E-value: 6.54e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 255958238    31 AIKEMIENCLDAKSTNIQVVV---KEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSK 84
Cdd:smart00387   9 VLSNLLDNAIKYTPEGGRITVtleRDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTD 65
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
6-315 3.34e-139

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: 415.50  E-value: 3.34e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238    6 GVIRRLDETVVNRIAAGEVIQRPANAIKEMIENCLDAKSTNIQVVVKEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSKL 85
Cdd:TIGR00585   1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238   86 QTFEDLASISTYGFRGEALASISHVAHVTITTKT-ADGKCAYRASYsDGKLQAPPKPCAGNQGTLITVEDLFYNIITRRK 164
Cdd:TIGR00585  81 QSFEDLERIETLGFRGEALASISSVSRLTITTKTsAADGLAYQALL-EGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238  165 ALKNPSEEYGKILEVVGRYSIHNSGISFSVKKQGETVSDVRTLPNATTVDN-IRSIFGNAVSRELIEVGcEDKTLAFKMN 243
Cdd:TIGR00585 160 FLKSPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLQLSTKPNQSTKENrIRSVFGTAVLRKLIPLD-EWEDLDLQLE 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255958238  244 GYISNANYSVKKCI--FLLFINHRLVESAALRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVH 315
Cdd:TIGR00585 239 GFISQPNVTRSRRSgwQFLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
8-691 9.68e-134

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


Pssm-ID: 223400 [Multi-domain]  Cd Length: 638  Bit Score: 413.27  E-value: 9.68e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238   8 IRRLDETVVNRIAAGEVIQRPANAIKEMIENCLDAKSTNIQVVVKEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSKLQT 87
Cdd:COG0323    4 IRQLPPDLVNQIAAGEVIERPASVVKELVENSLDAGATRIDIEVEGGGLKLIRVRDNGSGIDKEDLPLALLRHATSKIAS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238  88 FEDLASISTYGFRGEALASISHVAHVTITTKTADGKCAYRASYSDGKLQAPPKPCAGNQGTLITVEDLFYNIITRRKALK 167
Cdd:COG0323   84 LEDLFRIRTLGFRGEALASIASVSRLTITSRTAEASEGTQIYAEGGGMEVTVKPAAHPVGTTVEVRDLFYNTPARRKFLK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 168 NPSEEYGKILEVVGRYSIHNSGISFSVKKQGETVSDVRTLPNATTVDN-IRSIFGNAVSRELIEVgcEDKTLAFKMNGYI 246
Cdd:COG0323  164 SEKTEFGHITELINRYALAHPDISFSLSHNGKLRIELLKLPGTGDLEErIAAVYGTEFLKNALPI--ENEHEDLRLSGYV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 247 SNANYSVKKCIFL-LFINHRLVESAALRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILQR 325
Cdd:COG0323  242 SLPEFTRASRDYQyLFVNGRPVRDKLLNHALREAYADYLPRGRYPVFVLFLELDPELVDVNVHPAKKEVRFSDERLVHDL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 326 VQQHIESkllgsnssrmYFTQTllpglagpsgEAARPTTGVASSSTSGsgdkvyAYQMVRTDSREQKLDAFLQPVSSLGP 405
Cdd:COG0323  322 IYEAIKE----------ALAQQ----------GLIPPASVEAPKSASQ------PLPAFQEPSPLPESRIQKSKVAKSGS 375
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 406 SQPqdPAPVRGARTEGSperatredeemlalpapaeaaaeSENLERESLMETSDAAQKAAPTSSPGSSRKRHREDSDVEM 485
Cdd:COG0323  376 SKS--DAPSIAEPASGA-----------------------SPSPASPSIRPLSKNILPESSPGSLKNEDRSYDDLLEEPA 430
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 486 VENASGKEMTaacyprrriinltsvlslQEEISERCHETLRemlrnhsFVGCVNPQWALAQHQTKLYLLNTTKLSEELFY 565
Cdd:COG0323  431 ESEDKQEEAE------------------QKAISEDVFPLGE-------AIGQVHGTYILAEHEDGLVLVDQHAAHERILY 485
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 566 QILIYDFANFGVL-RLSEPApLFDLamlaldspesgwTEDDgpkeglAEYIVEFLKKKAEMladYFSVEIDEEGNLI--G 642
Cdd:COG0323  486 EKLKNELGNVGELqPLLIPI-RLEL------------SPEE------ADVLEEHKEELEKL---GFEIESFGENSVAvrS 543
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*....
gi 255958238 643 LPLLIDSYvpPLEGLPIFILRLATEVNWDEEKECFESLSKECAMFYSIR 691
Cdd:COG0323  544 VPAMLGKA--EVQELIRELLDDLLEGKLKDLKELLEELAATMACRSAVK 590
mutL PRK00095
DNA mismatch repair protein; Reviewed
8-433 4.77e-113

DNA mismatch repair protein; Reviewed


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 358.37  E-value: 4.77e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238   8 IRRLDETVVNRIAAGEVIQRPANAIKEMIENCLDAKSTNIQVVVKEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSKLQT 87
Cdd:PRK00095   3 IQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIAS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238  88 FEDLASISTYGFRGEALASISHVAHVTITTKTADGKCAYRASYSDGKLQaPPKPCAGNQGTLITVEDLFYNIITRRKALK 167
Cdd:PRK00095  83 LDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAEGWQIVYEGGEIV-EVKPAAHPVGTTIEVRDLFFNTPARRKFLK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 168 NPSEEYGKILEVVGRYSIHNSGISFSVKKQGETVsdVRTLPNATTVDNIRSIFGNAVSRELIEVGCEDktLAFKMNGYI- 246
Cdd:PRK00095 162 SEKTELGHIDDVVNRLALAHPDVAFTLTHNGKLV--LQTRGAGQLLQRLAAILGREFAENALPIDAEH--GDLRLSGYVg 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 247 ------SNANYsvkkcIFlLFINHRLVESAALRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEE 320
Cdd:PRK00095 238 lptlsrANRDY-----QY-LFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDER 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 321 SILQRVQQHIESKLLGSNSSRMYFTQTLLPGLAGPSGEAARPTTGVASSSTSGSGDKVYAYQMVRTDSREQKLDAFLQPV 400
Cdd:PRK00095 312 LVHDLIVQAIQEALAQSGLIPAAAGANQVLEPAEPEPLPLQQTPLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPLQ 391
                        410       420       430
                 ....*....|....*....|....*....|...
gi 255958238 401 SSLGPSQPQDPAPVRGARTEGSPERATREDEEM 433
Cdd:PRK00095 392 PNASQSEAAAAASAEAAAAAPAAAPEPAEAAEE 424
 
Name Accession Description Interval E-value
Mlh1_C pfam16413
DNA mismatch repair protein Mlh1 C-terminus; This is the C-terminal domain of DNA mismatch ...
505-760 3.15e-146

DNA mismatch repair protein Mlh1 C-terminus; This is the C-terminal domain of DNA mismatch repair protein Mlh1, these proteins belong to the MutL family. This domain forms part of the endonuclease active site.


Pssm-ID: 293022  Cd Length: 254  Bit Score: 431.14  E-value: 3.15e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238  505 INLTSVLSLQEEISERCHETLREMLRNHSFVGCVNPQWALAQHQTKLYLLNTTKLSEELFYQILIYDFANFGVLRLSEPA 584
Cdd:pfam16413   2 VRLTSVKELRAEVEENMHKGLTEIFRNHTFVGCVDERLALIQHGTKLYLVNYGALSEELFYQLGLRDFGNFGRIRLSPPL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238  585 PLFDLAMLALDSPESGWTEDDGPKEGLAEYIVEFLKKKAEMLADYFSVEIDEEGNLIGLPLLIDSYVPPLEGLPIFILRL 664
Cdd:pfam16413  82 PLRELLLLALESEESGWTEEDGPKEELAEKIVELLIEKAEMLEEYFSIEIDEDGNLESLPLLLKGYTPNLDKLPLFLLRL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238  665 ATEVNWDEEKECFESLSKECAMFYSIRKQYILEESTlsGQQSDMPGSTSKPWKWTVEHIIYKAFRSHLLPPKHFTEDGnV 744
Cdd:pfam16413 162 ATEVDWEDEKECFETILRELALFYAPEPLPSPDPSD--DEEDEEIEARRESWKWVIEHVLFPAIKRRLLPPKSLADDT-V 238
                         250
                  ....*....|....*.
gi 255958238  745 LQLANLPDLYKVFERC 760
Cdd:pfam16413 239 VQVASLPDLYKVFERC 254
MutL_Trans_MLH1 cd03483
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
211-335 4.50e-73

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  Cd Length: 127  Bit Score: 235.21  E-value: 4.50e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 211 TTVDNIRSIFGNAVSRELIEVGCEDKT--LAFKMNGYISNANYSVKKCIFLLFINHRLVESAALRKAIETVYAAYLPKNT 288
Cdd:cd03483    1 STKDNIRSVYGAAVANELIEVEISDDDddLGFKVKGLISNANYSKKKIIFILFINNRLVECSALRRAIENVYANYLPKGA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 255958238 289 HPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILQRVQQHIESKLL 335
Cdd:cd03483   81 HPFVYLSLEIPPENVDVNVHPTKREVHFLNEEEIIERIQKLVEDKLS 127
MutL_Trans cd00782
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
214-334 3.81e-44

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  Cd Length: 122  Bit Score: 155.01  E-value: 3.81e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 214 DNIRSIFGNAVSRELIEVGCEDKTlaFKMNGYISNANYSV-KKCIFLLFINHRLVESAALRKAIETVYAAYLPKNTHPFL 292
Cdd:cd00782    3 DRIAQVYGKEVAKNLIEVELESGD--FRISGYISKPDFGRsSKDRQFLFVNGRPVRDKLLSKAINEAYRSYLPKGRYPVF 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 255958238 293 YLSLEISPQNVDVNVHPTKHEVHFLHEESILQRVQQHIESKL 334
Cdd:cd00782   81 VLNLELPPELVDVNVHPTKREVRFSDEEEVLELIREALRSAL 122
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
217-334 9.82e-41

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: 279463  Cd Length: 117  Bit Score: 145.71  E-value: 9.82e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238  217 RSIFGNAVSRELIEVGCEDKTlaFKMNGYISNANYS-VKKCIFLLFINHRLVESAALRKAIETVYAAYLPKNTHPFLYLS 295
Cdd:pfam01119   1 AAIYGKEFAKNLLPIEGEDDD--LRLSGYISKPELTrSNRDYQYLFVNGRPVRDKLLSKAIREAYRDLLPKGRYPVAVLF 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 255958238  296 LEISPQNVDVNVHPTKHEVHFLHEESILQRVQQHIESKL 334
Cdd:pfam01119  79 LEIDPELVDVNVHPAKREVRFSDEREVYDFIYEAIREAL 117
TopoII_MutL_Trans cd00329
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
214-315 5.33e-22

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  Cd Length: 107  Bit Score: 92.32  E-value: 5.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 214 DNIRSIFGNAVSRELIEVGCEDKTlaFKMNGYISNANYSV-KKCIFLLFINHRLVESA-ALRKAIETVYAAYL---PKNT 288
Cdd:cd00329    3 DRLAEILGDKVADKLIYVEGESDG--FRVEGAISYPDSGRsSKDRQFSFVNGRPVREGgTHVKAVREAYTRALngdDVRR 80
                         90       100
                 ....*....|....*....|....*..
gi 255958238 289 HPFLYLSLEISPQNVDVNVHPTKHEVH 315
Cdd:cd00329   81 YPVAVLSLKIPPSLVDVNVHPTKEEVR 107
MutL_Trans_MutL cd03482
MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
216-334 2.11e-14

MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to Escherichia coli MutL. EcMutL belongs to the DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from the ATP-binding site to the DNA breakage/reunion regions of the enzymes. It has been suggested that during initiation of DNA mismatch repair in E. coli, the mismatch recognition protein MutS recruits MutL in the presence of ATP. The MutS(ATP)-MutL ternary complex formed, then recruits the latent endonuclease MutH. Prokaryotic MutS and MutL are homodimers.


Pssm-ID: 239564  Cd Length: 123  Bit Score: 70.69  E-value: 2.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 216 IRSIFGNAVSRELIEVGCEDKTLafKMNGYISNANYS-VKKCIFLLFINHRLVE----SAALRKAietvYAAYLPKNTHP 290
Cdd:cd03482    5 LADILGEDFAEQALAIDEEAGGL--RLSGWIALPTFArSQADIQYFYVNGRMVRdkliSHAVRQA----YSDVLHGGRHP 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 255958238 291 FLYLSLEISPQNVDVNVHPTKHEVHFLHEESILQRVQQHIESKL 334
Cdd:cd03482   79 AYVLYLELDPAQVDVNVHPAKHEVRFRDSRLVHDFIYHAVKKAL 122
MutL_Trans_hPMS_2_like cd03484
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
214-332 1.05e-12

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  Cd Length: 142  Bit Score: 66.14  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 214 DNIRSIFGNAVSRELIEV---------------GCEDKTLAFKMNGYISnanysvkKCIF----------LLFINHRLVE 268
Cdd:cd03484    4 DNIINVFGGKVIKGLIPInleldvnptkeeldsDEDLADSEVKITGYIS-------KPSHgcgrsssdrqFFYINGRPVD 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255958238 269 SAALRKAIETVYAAYlPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILQRVQQHIES 332
Cdd:cd03484   77 LKKVAKLINEVYKSF-NSRQYPFFILNISLPTSLYDVNVTPDKRTVLLHDEDRLIDTLKTSLSE 139
MutL_Trans_hPMS_1_like cd03485
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
218-332 1.27e-10

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  Cd Length: 132  Bit Score: 59.98  E-value: 1.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 218 SIFGNAVSRELIEVGCEDKTLAFKMNGYI--SNANYSVKKCIF-LLFINHRLVESA-ALRKAIETVYAAYLPKNT---HP 290
Cdd:cd03485    8 RVLGTAVAANMVPVQSTDEDPQISLEGFLpkPGSDVSKTKSDGkFISVNSRPVSLGkDIGKLLRQYYSSAYRKSSlrrYP 87
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 255958238 291 FLYLSLEISPQNVDVNVHPTKHEVHFLHEESILQRVQQHIES 332
Cdd:cd03485   88 VFFLNILCPPGLVDVNIEPDKDDVLLQNKEAVLQAVENLLES 129
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
31-132 2.08e-10

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


Pssm-ID: 290321  Cd Length: 135  Bit Score: 59.24  E-value: 2.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238   31 AIKEMIENCLDAKSTNIQVVVKEGGLKLIQIQDNGTGIRKEDLDIVCeRFTTSKLQTFEDLASISTYGFrGEALASISHV 110
Cdd:pfam13589   6 ALAELVDNSYDADATNVKIEVNKNPGGEIVIEDDGHGMSEEELINAL-RLATPDKEAERDSTDLGRKGI-GMKLASLSLG 83
                          90       100
                  ....*....|....*....|..
gi 255958238  111 AHVTITTKTADGKCAYRASYSD 132
Cdd:pfam13589  84 RKLTVTTKKEGESSTLTLDVDW 105
HATPase_c cd00075
Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: ...
31-122 3.85e-08

Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: histidine kinase, DNA gyrase B, topoisomerases, heat shock protein HSP90, phytochrome-like ATPases and DNA mismatch repair proteins


Pssm-ID: 238030  Cd Length: 103  Bit Score: 51.88  E-value: 3.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238  31 AIKEMIENCLDA---KSTNIQVVVKEGGLKL-IQIQDNGTGIRKEDLDIVCERfttsklqtFEDLASISTYGFRGEALAS 106
Cdd:cd00075    4 VLLNLLSNAIKHtpeGGGRITISVERDGDHLeIRVEDNGPGIPEEDLERIFER--------FSDGSRSRKGGGTGLGLSI 75
                         90       100
                 ....*....|....*....|.
gi 255958238 107 ISHVA-----HVTITTKTADG 122
Cdd:cd00075   76 VKKLVelhggRIEVESEPGGG 96
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
31-124 2.28e-07

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: 280651  Cd Length: 107  Bit Score: 49.60  E-value: 2.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238   31 AIKEMIENCLDAKSTNIQVVV---KEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSKlqtfedlasisTYGFRGEALASI 107
Cdd:pfam02518   9 VLSELLDNAIKHAPEGGEIEVrveKDGGRLEIEVEDNGPGIPEEDLPRIFEPFFRGS-----------SSGGTGLGLSIV 77
                          90       100
                  ....*....|....*....|..
gi 255958238  108 -----SHVAHVTITTKTADGKC 124
Cdd:pfam02518  78 rklveLMGGEIWVESEPGGGTT 99
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
31-84 6.54e-05

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


Pssm-ID: 214643  Cd Length: 111  Bit Score: 41.87  E-value: 6.54e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 255958238    31 AIKEMIENCLDAKSTNIQVVV---KEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSK 84
Cdd:smart00387   9 VLSNLLDNAIKYTPEGGRITVtleRDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTD 65
MutL_Trans_MLH3 cd03486
MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
217-334 3.73e-03

MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to yeast and human MLH3 (MutL homologue 3). MLH3 belongs to the DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. MLH1 forms heterodimers with MLH3. The MLH1-MLH3 complex plays a role in meiosis. A role for hMLH1-hMLH3 in DNA mismatch repair (MMR) has not been established. It has been suggested that hMLH3 may be a low risk gene for colorectal cancer; however there is little evidence to support it having a role in classical HNPCC.


Pssm-ID: 239568  Cd Length: 141  Bit Score: 37.30  E-value: 3.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 217 RSIFGNAVSRELIEVGCEDKTlaFKMNGYISNaNYSVKKCIFLLFINHRLVESAALRKAIETVY----AAYLPKNT---- 288
Cdd:cd03486    7 KQIYGLVLAQKLKEVSAKFQE--YEVSGYISS-EGHYSKSFQFIYVNGRLYLKTRFHKLINKLFrktsAVAKNKSSpqsk 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 255958238 289 -----------HPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILQRVQQHIESKL 334
Cdd:cd03486   84 ssrrgkrsqesYPVFVLNITCPASEYDLSQEPSKTIIEFKDWKTLLPLILEVVKSFL 140
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
6-315 3.34e-139

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: 415.50  E-value: 3.34e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238    6 GVIRRLDETVVNRIAAGEVIQRPANAIKEMIENCLDAKSTNIQVVVKEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSKL 85
Cdd:TIGR00585   1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238   86 QTFEDLASISTYGFRGEALASISHVAHVTITTKT-ADGKCAYRASYsDGKLQAPPKPCAGNQGTLITVEDLFYNIITRRK 164
Cdd:TIGR00585  81 QSFEDLERIETLGFRGEALASISSVSRLTITTKTsAADGLAYQALL-EGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238  165 ALKNPSEEYGKILEVVGRYSIHNSGISFSVKKQGETVSDVRTLPNATTVDN-IRSIFGNAVSRELIEVGcEDKTLAFKMN 243
Cdd:TIGR00585 160 FLKSPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLQLSTKPNQSTKENrIRSVFGTAVLRKLIPLD-EWEDLDLQLE 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255958238  244 GYISNANYSVKKCI--FLLFINHRLVESAALRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVH 315
Cdd:TIGR00585 239 GFISQPNVTRSRRSgwQFLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
8-691 9.68e-134

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


Pssm-ID: 223400 [Multi-domain]  Cd Length: 638  Bit Score: 413.27  E-value: 9.68e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238   8 IRRLDETVVNRIAAGEVIQRPANAIKEMIENCLDAKSTNIQVVVKEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSKLQT 87
Cdd:COG0323    4 IRQLPPDLVNQIAAGEVIERPASVVKELVENSLDAGATRIDIEVEGGGLKLIRVRDNGSGIDKEDLPLALLRHATSKIAS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238  88 FEDLASISTYGFRGEALASISHVAHVTITTKTADGKCAYRASYSDGKLQAPPKPCAGNQGTLITVEDLFYNIITRRKALK 167
Cdd:COG0323   84 LEDLFRIRTLGFRGEALASIASVSRLTITSRTAEASEGTQIYAEGGGMEVTVKPAAHPVGTTVEVRDLFYNTPARRKFLK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 168 NPSEEYGKILEVVGRYSIHNSGISFSVKKQGETVSDVRTLPNATTVDN-IRSIFGNAVSRELIEVgcEDKTLAFKMNGYI 246
Cdd:COG0323  164 SEKTEFGHITELINRYALAHPDISFSLSHNGKLRIELLKLPGTGDLEErIAAVYGTEFLKNALPI--ENEHEDLRLSGYV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 247 SNANYSVKKCIFL-LFINHRLVESAALRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILQR 325
Cdd:COG0323  242 SLPEFTRASRDYQyLFVNGRPVRDKLLNHALREAYADYLPRGRYPVFVLFLELDPELVDVNVHPAKKEVRFSDERLVHDL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 326 VQQHIESkllgsnssrmYFTQTllpglagpsgEAARPTTGVASSSTSGsgdkvyAYQMVRTDSREQKLDAFLQPVSSLGP 405
Cdd:COG0323  322 IYEAIKE----------ALAQQ----------GLIPPASVEAPKSASQ------PLPAFQEPSPLPESRIQKSKVAKSGS 375
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 406 SQPqdPAPVRGARTEGSperatredeemlalpapaeaaaeSENLERESLMETSDAAQKAAPTSSPGSSRKRHREDSDVEM 485
Cdd:COG0323  376 SKS--DAPSIAEPASGA-----------------------SPSPASPSIRPLSKNILPESSPGSLKNEDRSYDDLLEEPA 430
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 486 VENASGKEMTaacyprrriinltsvlslQEEISERCHETLRemlrnhsFVGCVNPQWALAQHQTKLYLLNTTKLSEELFY 565
Cdd:COG0323  431 ESEDKQEEAE------------------QKAISEDVFPLGE-------AIGQVHGTYILAEHEDGLVLVDQHAAHERILY 485
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 566 QILIYDFANFGVL-RLSEPApLFDLamlaldspesgwTEDDgpkeglAEYIVEFLKKKAEMladYFSVEIDEEGNLI--G 642
Cdd:COG0323  486 EKLKNELGNVGELqPLLIPI-RLEL------------SPEE------ADVLEEHKEELEKL---GFEIESFGENSVAvrS 543
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*....
gi 255958238 643 LPLLIDSYvpPLEGLPIFILRLATEVNWDEEKECFESLSKECAMFYSIR 691
Cdd:COG0323  544 VPAMLGKA--EVQELIRELLDDLLEGKLKDLKELLEELAATMACRSAVK 590
mutL PRK00095
DNA mismatch repair protein; Reviewed
8-433 4.77e-113

DNA mismatch repair protein; Reviewed


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 358.37  E-value: 4.77e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238   8 IRRLDETVVNRIAAGEVIQRPANAIKEMIENCLDAKSTNIQVVVKEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSKLQT 87
Cdd:PRK00095   3 IQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIAS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238  88 FEDLASISTYGFRGEALASISHVAHVTITTKTADGKCAYRASYSDGKLQaPPKPCAGNQGTLITVEDLFYNIITRRKALK 167
Cdd:PRK00095  83 LDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAEGWQIVYEGGEIV-EVKPAAHPVGTTIEVRDLFFNTPARRKFLK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 168 NPSEEYGKILEVVGRYSIHNSGISFSVKKQGETVsdVRTLPNATTVDNIRSIFGNAVSRELIEVGCEDktLAFKMNGYI- 246
Cdd:PRK00095 162 SEKTELGHIDDVVNRLALAHPDVAFTLTHNGKLV--LQTRGAGQLLQRLAAILGREFAENALPIDAEH--GDLRLSGYVg 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 247 ------SNANYsvkkcIFlLFINHRLVESAALRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEE 320
Cdd:PRK00095 238 lptlsrANRDY-----QY-LFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDER 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238 321 SILQRVQQHIESKLLGSNSSRMYFTQTLLPGLAGPSGEAARPTTGVASSSTSGSGDKVYAYQMVRTDSREQKLDAFLQPV 400
Cdd:PRK00095 312 LVHDLIVQAIQEALAQSGLIPAAAGANQVLEPAEPEPLPLQQTPLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPLQ 391
                        410       420       430
                 ....*....|....*....|....*....|...
gi 255958238 401 SSLGPSQPQDPAPVRGARTEGSPERATREDEEM 433
Cdd:PRK00095 392 PNASQSEAAAAASAEAAAAAPAAAPEPAEAAEE 424
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
1-84 1.77e-03

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 223715 [Multi-domain]  Cd Length: 336  Bit Score: 39.74  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958238   1 MAFVAGVIRRLDETVVNRIAAGEviQRPANAIKEMIENCLDA-KSTNIQVVVKEGGLKL-IQIQDNGTGIRKEDLDIVCE 78
Cdd:COG0642  204 LAQEKGIELAVDLPELPYVLGDP--ERLRQVLVNLLSNAIKYtPGGEITISVRQDDEQVtISVEDTGPGIPEEELERIFE 281

                 ....*.
gi 255958238  79 RFTTSK 84
Cdd:COG0642  282 PFFRTD 287
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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