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Conserved domains on  [gi|489706902|ref|WP_003611039|]
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DNA mismatch repair endonuclease MutL [Lactobacillus delbrueckii]

Protein Classification

DNA mismatch repair endonuclease MutL( domain architecture ID 11478033)

DNA mismatch repair endonuclease MutL is required for dam-dependent methyl-directed DNA mismatch repair; it mediates the interactions between MutH and MutS in the DNA repair system

CATH:  3.30.565.10|3.30.230.10
Gene Symbol:  mutL
Gene Ontology:  GO:0032300|GO:0005524|GO:0006298|GO:0016887|GO:0140664
PubMed:  32652606|19953589
SCOP:  4000168

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mutL PRK00095
DNA mismatch repair endonuclease MutL;
3-655 0e+00

DNA mismatch repair endonuclease MutL;


:

Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 682.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902   3 KIHELSENLTNQIAAGEVIERPASVVKELVENAIDAQASRIRVEVQHSGLKQISVQDNGSGIAPDQVDLAFMRHATSKIQ 82
Cdd:PRK00095   2 PIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902  83 DEHDLFNIATLGFRGEALASIAAVAHVEILTSTDGQT-ATRAAFAGGVKKFQEDAGSAKGTKITVGDIFYNTPARLKYLK 161
Cdd:PRK00095  82 SLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAeGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKFLK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 162 SPKTELLKIVDIVNRIALGHPEISLTLASDGKVLLRTPGNGNLKQDVANIYGRKVAEKMLTVENEDPDFTLYGLVSEANL 241
Cdd:PRK00095 162 SEKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPTL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 242 TRSSRNFISILLNGRYIKNYQLSSALLDGYGNKL-GGKYPIAVLAIEADPLLVDVNVHPTKEEVRLSKEKELSRLITSAV 320
Cdd:PRK00095 242 SRANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLpRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDLIVQAI 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 321 TEALMDEDEASPLfqltpfkdktqldqlefNLKPNVVDTRRPDDFQLEVSQVAEPEGKTDITNKKETESKETKETAEKKE 400
Cdd:PRK00095 322 QEALAQSGLIPAA-----------------AGANQVLEPAEPEPLPLQQTPLYASGSSPPASSPSSAPPEQSEESQEESS 384

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 401 NKQEEKEEKTSAPEyvdlnqvreddqyvltkswgqhvkEQTALPPFAGGEEAASPVTSKADQLLRQHLPALRLLGQMGG- 479
Cdd:PRK00095 385 AEKNPLQPNASQSE------------------------AAAAASAEAAAAAPAAAPEPAEAAEEADSFPLGYALGQLHGt 440

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 480 YLLAEHGGDLYLLDQVAARRRLEYDQILASLEKDENYQQGLLEPLVFDFSVYDYQKLKDQLPLLRQLGLEMEDFGQNTLL 559
Cdd:PRK00095 441 YILAENEDGLYLVDQHAAHERLLYEQLKDKLAEVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLELEPFGPNSFA 520

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 560 MHSYPTWL-KGEVTVQVRELLDQLLSSRENDGKSLLKLVAAKAAESNVSRRVNLTGAEAADLLLRLQTASDPYRDASGQV 638
Cdd:PRK00095 521 VREVPALLgQQELEELIRDLLDELAEEGDSDTLKERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRP 600

                        650
                 ....*....|....*..
gi 489706902 639 AVVRLSQNDLSKLFKKG 655
Cdd:PRK00095 601 TYIELSLSDLEKLFKRI 617
 
Name Accession Description Interval E-value
mutL PRK00095
DNA mismatch repair endonuclease MutL;
3-655 0e+00

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 682.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902   3 KIHELSENLTNQIAAGEVIERPASVVKELVENAIDAQASRIRVEVQHSGLKQISVQDNGSGIAPDQVDLAFMRHATSKIQ 82
Cdd:PRK00095   2 PIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902  83 DEHDLFNIATLGFRGEALASIAAVAHVEILTSTDGQT-ATRAAFAGGVKKFQEDAGSAKGTKITVGDIFYNTPARLKYLK 161
Cdd:PRK00095  82 SLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAeGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKFLK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 162 SPKTELLKIVDIVNRIALGHPEISLTLASDGKVLLRTPGNGNLKQDVANIYGRKVAEKMLTVENEDPDFTLYGLVSEANL 241
Cdd:PRK00095 162 SEKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPTL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 242 TRSSRNFISILLNGRYIKNYQLSSALLDGYGNKL-GGKYPIAVLAIEADPLLVDVNVHPTKEEVRLSKEKELSRLITSAV 320
Cdd:PRK00095 242 SRANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLpRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDLIVQAI 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 321 TEALMDEDEASPLfqltpfkdktqldqlefNLKPNVVDTRRPDDFQLEVSQVAEPEGKTDITNKKETESKETKETAEKKE 400
Cdd:PRK00095 322 QEALAQSGLIPAA-----------------AGANQVLEPAEPEPLPLQQTPLYASGSSPPASSPSSAPPEQSEESQEESS 384

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 401 NKQEEKEEKTSAPEyvdlnqvreddqyvltkswgqhvkEQTALPPFAGGEEAASPVTSKADQLLRQHLPALRLLGQMGG- 479
Cdd:PRK00095 385 AEKNPLQPNASQSE------------------------AAAAASAEAAAAAPAAAPEPAEAAEEADSFPLGYALGQLHGt 440

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 480 YLLAEHGGDLYLLDQVAARRRLEYDQILASLEKDENYQQGLLEPLVFDFSVYDYQKLKDQLPLLRQLGLEMEDFGQNTLL 559
Cdd:PRK00095 441 YILAENEDGLYLVDQHAAHERLLYEQLKDKLAEVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLELEPFGPNSFA 520

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 560 MHSYPTWL-KGEVTVQVRELLDQLLSSRENDGKSLLKLVAAKAAESNVSRRVNLTGAEAADLLLRLQTASDPYRDASGQV 638
Cdd:PRK00095 521 VREVPALLgQQELEELIRDLLDELAEEGDSDTLKERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRP 600

                        650
                 ....*....|....*..
gi 489706902 639 AVVRLSQNDLSKLFKKG 655
Cdd:PRK00095 601 TYIELSLSDLEKLFKRI 617
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
1-653 0e+00

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 577.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902   1 MAKIHELSENLTNQIAAGEVIERPASVVKELVENAIDAQASRIRVEVQHSGLKQISVQDNGSGIAPDQVDLAFMRHATSK 80
Cdd:COG0323    1 MPKIRLLPDELANQIAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLPLAFERHATSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902  81 IQDEHDLFNIATLGFRGEALASIAAVAHVEILTSTDGQ-TATRAAFAGGVKKFQEDAGSAKGTKITVGDIFYNTPARLKY 159
Cdd:COG0323   81 IRSAEDLFRIRTLGFRGEALASIASVSRLTLTTRTAGAeLGTRIEVEGGKVVEVEPAAAPKGTTVEVRDLFFNTPARRKF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 160 LKSPKTELLKIVDIVNRIALGHPEISLTLASDGKVLLRTPGNGNLKQDVANIYGRKVAEKMLTVENEDPDFTLYGLVSEA 239
Cdd:COG0323  161 LKSDATELAHITDVVRRLALAHPDIAFTLIHNGREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 240 NLTRSSRNFISILLNGRYIKNYQLSSALLDGYGNKL-GGKYPIAVLAIEADPLLVDVNVHPTKEEVRLSKEKELSRLITS 318
Cdd:COG0323  241 EFSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRDLLpKGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRS 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 319 AVTEALmdedeasplfqltpfkdktqldqlefnlkpnvvdtrrpddfqlevsqvaepegktditnkketesketketaek 398
Cdd:COG0323  321 AVREAL-------------------------------------------------------------------------- 326

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 399 kenkqeekeektsapeyvdlnqvreddqyvltkswGQHVkeqtalppfaggeeaaspvtskadqllrqhlpalrlLGQMG 478
Cdd:COG0323  327 -----------------------------------AQAA------------------------------------LGQLH 335

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 479 G-YLLAEHGGDLYLLDQVAARRRLEYDQILASLEKDENYQQGLLEPLVFDFSVYDYQKLKDQLPLLRQLGLEMEDFGQNT 557
Cdd:COG0323  336 GtYILAENEDGLVLIDQHAAHERILYERLKKALAEGGVASQPLLIPETLELSPAEAALLEEHLEELARLGFEIEPFGPNT 415

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 558 LLMHSYPTWLK-GEVTVQVRELLDQLLSSRENDGKS-----LLKLVAAKAAesnVSRRVNLTGAEAADLLLRLQTASDPY 631
Cdd:COG0323  416 VAVRAVPALLGeGDAEELLRDLLDELAEEGSSESLEelreeLLATMACHGA---IKAGRRLSLEEMNALLRDLEATENPY 492

                        650       660
                 ....*....|....*....|..
gi 489706902 632 RDASGQVAVVRLSQNDLSKLFK 653
Cdd:COG0323  493 TCPHGRPTWIELSLEELEKLFK 514
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 3-305 9.94e-121

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: 361.57  E-value: 9.94e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902    3 KIHELSENLTNQIAAGEVIERPASVVKELVENAIDAQASRIRVEVQHSGLKQISVQDNGSGIAPDQVDLAFMRHATSKIQ 82
Cdd:TIGR00585   2 TIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKIQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902   83 DEHDLFNIATLGFRGEALASIAAVAHVEILTST--DGQTATRAAFAGGVKKFQEDAGSAKGTKITVGDIFYNTPARLKYL 160
Cdd:TIGR00585  82 SFEDLERIETLGFRGEALASISSVSRLTITTKTsaADGLAYQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRKFL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902  161 KSPKTELLKIVDIVNRIALGHPEISLTLASDGKVLL--RTPGNGNLKQD-VANIYGRKVAEKML-TVENEDPDFTLYGLV 236
Cdd:TIGR00585 162 KSPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLqlSTKPNQSTKENrIRSVFGTAVLRKLIpLDEWEDLDLQLEGFI 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489706902  237 SEANLTRSSR-NFISILLNGRYIKNYQLSSALLDGYGNKLG-GKYPIAVLAIEADPLLVDVNVHPTKEEVR 305
Cdd:TIGR00585 242 SQPNVTRSRRsGWQFLFINGRPVELKLLLKAIREVYHEYLPkGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 11-196 6.66e-100

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: 303.20  E-value: 6.66e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902  11 LTNQIAAGEVIERPASVVKELVENAIDAQASRIRVEVQHSGLKQISVQDNGSGIAPDQVDLAFMRHATSKIQDEHDLFNI 90
Cdd:cd16926    1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902  91 ATLGFRGEALASIAAVAHVEILTSTDGQ-TATRAAFA-GGVKKFQEDAGSAKGTKITVGDIFYNTPARLKYLKSPKTELL 168
Cdd:cd16926   81 TTLGFRGEALASIASVSRLTITTRTADDdVGTRLVVDgGGIIEEVKPAAAPVGTTVTVRDLFYNTPARRKFLKSPKTELS 160

                        170       180
                 ....*....|....*....|....*...
gi 489706902 169 KIVDIVNRIALGHPEISLTLASDGKVLL 196
Cdd:cd16926  161 KILDLVQRLALAHPDVSFSLTHDGKLVL 188
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 209-324 8.82e-43

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: 149.96  E-value: 8.82e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902  209 ANIYGRKVAEKMLTVENEDPDFTLYGLVSEANLTRSSRNFISILLNGRYIKNYQLSSALLDGYGNKL-GGKYPIAVLAIE 287
Cdd:pfam01119   1 AAIYGKEFAENLLPIEKEDDGLRLSGYISKPTLSRSNRDYQYLFVNGRPVRDKLLSHAIREAYRDLLpKGRYPVAVLFLE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 489706902  288 ADPLLVDVNVHPTKEEVRLSKEKELSRLITSAVTEAL 324
Cdd:pfam01119  81 IDPELVDVNVHPTKREVRFRDEREVYDFIKEALREAL 117
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
 474-602 2.23e-27

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: 107.83  E-value: 2.23e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902   474 LGQM-GGYLLAEHGGDLYLLDQVAARRRLEYDQILAslEKDENYQQGLLEPLVFDFSVYDYQKLKDQLPLLRQLGLEMED 552
Cdd:smart00853   2 LGQVaGTYILAEREDGLYLLDQHAAHERILYEQLLK--QAGGLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELEI 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 489706902   553 FGQNTLLMHSYPTWLK-GEVTVQVRELLDQLLSSRENDGKSLLKLVAAKAA 602
Cdd:smart00853  80 FGPQSLILRSVPALLRqQNLQKLIPELLDLLSDEEENARPSRLEALLASLA 130
 
Name Accession Description Interval E-value
mutL PRK00095
DNA mismatch repair endonuclease MutL;
3-655 0e+00

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 682.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902   3 KIHELSENLTNQIAAGEVIERPASVVKELVENAIDAQASRIRVEVQHSGLKQISVQDNGSGIAPDQVDLAFMRHATSKIQ 82
Cdd:PRK00095   2 PIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902  83 DEHDLFNIATLGFRGEALASIAAVAHVEILTSTDGQT-ATRAAFAGGVKKFQEDAGSAKGTKITVGDIFYNTPARLKYLK 161
Cdd:PRK00095  82 SLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAeGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKFLK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 162 SPKTELLKIVDIVNRIALGHPEISLTLASDGKVLLRTPGNGNLKQDVANIYGRKVAEKMLTVENEDPDFTLYGLVSEANL 241
Cdd:PRK00095 162 SEKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPTL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 242 TRSSRNFISILLNGRYIKNYQLSSALLDGYGNKL-GGKYPIAVLAIEADPLLVDVNVHPTKEEVRLSKEKELSRLITSAV 320
Cdd:PRK00095 242 SRANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLpRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDLIVQAI 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 321 TEALMDEDEASPLfqltpfkdktqldqlefNLKPNVVDTRRPDDFQLEVSQVAEPEGKTDITNKKETESKETKETAEKKE 400
Cdd:PRK00095 322 QEALAQSGLIPAA-----------------AGANQVLEPAEPEPLPLQQTPLYASGSSPPASSPSSAPPEQSEESQEESS 384

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 401 NKQEEKEEKTSAPEyvdlnqvreddqyvltkswgqhvkEQTALPPFAGGEEAASPVTSKADQLLRQHLPALRLLGQMGG- 479
Cdd:PRK00095 385 AEKNPLQPNASQSE------------------------AAAAASAEAAAAAPAAAPEPAEAAEEADSFPLGYALGQLHGt 440

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 480 YLLAEHGGDLYLLDQVAARRRLEYDQILASLEKDENYQQGLLEPLVFDFSVYDYQKLKDQLPLLRQLGLEMEDFGQNTLL 559
Cdd:PRK00095 441 YILAENEDGLYLVDQHAAHERLLYEQLKDKLAEVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLELEPFGPNSFA 520

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 560 MHSYPTWL-KGEVTVQVRELLDQLLSSRENDGKSLLKLVAAKAAESNVSRRVNLTGAEAADLLLRLQTASDPYRDASGQV 638
Cdd:PRK00095 521 VREVPALLgQQELEELIRDLLDELAEEGDSDTLKERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRP 600

                        650
                 ....*....|....*..
gi 489706902 639 AVVRLSQNDLSKLFKKG 655
Cdd:PRK00095 601 TYIELSLSDLEKLFKRI 617
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
1-653 0e+00

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 577.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902   1 MAKIHELSENLTNQIAAGEVIERPASVVKELVENAIDAQASRIRVEVQHSGLKQISVQDNGSGIAPDQVDLAFMRHATSK 80
Cdd:COG0323    1 MPKIRLLPDELANQIAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLPLAFERHATSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902  81 IQDEHDLFNIATLGFRGEALASIAAVAHVEILTSTDGQ-TATRAAFAGGVKKFQEDAGSAKGTKITVGDIFYNTPARLKY 159
Cdd:COG0323   81 IRSAEDLFRIRTLGFRGEALASIASVSRLTLTTRTAGAeLGTRIEVEGGKVVEVEPAAAPKGTTVEVRDLFFNTPARRKF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 160 LKSPKTELLKIVDIVNRIALGHPEISLTLASDGKVLLRTPGNGNLKQDVANIYGRKVAEKMLTVENEDPDFTLYGLVSEA 239
Cdd:COG0323  161 LKSDATELAHITDVVRRLALAHPDIAFTLIHNGREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 240 NLTRSSRNFISILLNGRYIKNYQLSSALLDGYGNKL-GGKYPIAVLAIEADPLLVDVNVHPTKEEVRLSKEKELSRLITS 318
Cdd:COG0323  241 EFSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRDLLpKGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRS 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 319 AVTEALmdedeasplfqltpfkdktqldqlefnlkpnvvdtrrpddfqlevsqvaepegktditnkketesketketaek 398
Cdd:COG0323  321 AVREAL-------------------------------------------------------------------------- 326

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 399 kenkqeekeektsapeyvdlnqvreddqyvltkswGQHVkeqtalppfaggeeaaspvtskadqllrqhlpalrlLGQMG 478
Cdd:COG0323  327 -----------------------------------AQAA------------------------------------LGQLH 335

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 479 G-YLLAEHGGDLYLLDQVAARRRLEYDQILASLEKDENYQQGLLEPLVFDFSVYDYQKLKDQLPLLRQLGLEMEDFGQNT 557
Cdd:COG0323  336 GtYILAENEDGLVLIDQHAAHERILYERLKKALAEGGVASQPLLIPETLELSPAEAALLEEHLEELARLGFEIEPFGPNT 415

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 558 LLMHSYPTWLK-GEVTVQVRELLDQLLSSRENDGKS-----LLKLVAAKAAesnVSRRVNLTGAEAADLLLRLQTASDPY 631
Cdd:COG0323  416 VAVRAVPALLGeGDAEELLRDLLDELAEEGSSESLEelreeLLATMACHGA---IKAGRRLSLEEMNALLRDLEATENPY 492

                        650       660
                 ....*....|....*....|..
gi 489706902 632 RDASGQVAVVRLSQNDLSKLFK 653
Cdd:COG0323  493 TCPHGRPTWIELSLEELEKLFK 514
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 3-305 9.94e-121

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: 361.57  E-value: 9.94e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902    3 KIHELSENLTNQIAAGEVIERPASVVKELVENAIDAQASRIRVEVQHSGLKQISVQDNGSGIAPDQVDLAFMRHATSKIQ 82
Cdd:TIGR00585   2 TIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKIQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902   83 DEHDLFNIATLGFRGEALASIAAVAHVEILTST--DGQTATRAAFAGGVKKFQEDAGSAKGTKITVGDIFYNTPARLKYL 160
Cdd:TIGR00585  82 SFEDLERIETLGFRGEALASISSVSRLTITTKTsaADGLAYQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRKFL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902  161 KSPKTELLKIVDIVNRIALGHPEISLTLASDGKVLL--RTPGNGNLKQD-VANIYGRKVAEKML-TVENEDPDFTLYGLV 236
Cdd:TIGR00585 162 KSPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLqlSTKPNQSTKENrIRSVFGTAVLRKLIpLDEWEDLDLQLEGFI 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489706902  237 SEANLTRSSR-NFISILLNGRYIKNYQLSSALLDGYGNKLG-GKYPIAVLAIEADPLLVDVNVHPTKEEVR 305
Cdd:TIGR00585 242 SQPNVTRSRRsGWQFLFINGRPVELKLLLKAIREVYHEYLPkGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 11-196 6.66e-100

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: 303.20  E-value: 6.66e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902  11 LTNQIAAGEVIERPASVVKELVENAIDAQASRIRVEVQHSGLKQISVQDNGSGIAPDQVDLAFMRHATSKIQDEHDLFNI 90
Cdd:cd16926    1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902  91 ATLGFRGEALASIAAVAHVEILTSTDGQ-TATRAAFA-GGVKKFQEDAGSAKGTKITVGDIFYNTPARLKYLKSPKTELL 168
Cdd:cd16926   81 TTLGFRGEALASIASVSRLTITTRTADDdVGTRLVVDgGGIIEEVKPAAAPVGTTVTVRDLFYNTPARRKFLKSPKTELS 160

                        170       180
                 ....*....|....*....|....*...
gi 489706902 169 KIVDIVNRIALGHPEISLTLASDGKVLL 196
Cdd:cd16926  161 KILDLVQRLALAHPDVSFSLTHDGKLVL 188
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 209-324 8.82e-43

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: 149.96  E-value: 8.82e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902  209 ANIYGRKVAEKMLTVENEDPDFTLYGLVSEANLTRSSRNFISILLNGRYIKNYQLSSALLDGYGNKL-GGKYPIAVLAIE 287
Cdd:pfam01119   1 AAIYGKEFAENLLPIEKEDDGLRLSGYISKPTLSRSNRDYQYLFVNGRPVRDKLLSHAIREAYRDLLpKGRYPVAVLFLE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 489706902  288 ADPLLVDVNVHPTKEEVRLSKEKELSRLITSAVTEAL 324
Cdd:pfam01119  81 IDPELVDVNVHPTKREVRFRDEREVYDFIKEALREAL 117
MutL_Trans cd00782
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 204-324 4.66e-39

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: 139.98  E-value: 4.66e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 204 LKQDVANIYGRKVAEKMLTVENEDPDFTLYGLVSEANLTRSSRNFISILLNGRYIKNYQLSSALLDGYGNKL-GGKYPIA 282
Cdd:cd00782    1 LKDRIAQVYGKEVAKNLIEVELESGDFRISGYISKPDFGRSSKDRQFLFVNGRPVRDKLLSKAINEAYRSYLpKGRYPVF 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489706902 283 VLAIEADPLLVDVNVHPTKEEVRLSKEKELSRLITSAVTEAL 324
Cdd:cd00782   81 VLNLELPPELVDVNVHPTKREVRFSDEEEVLELIREALRSAL 122
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
 473-602 1.52e-28

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: 111.16  E-value: 1.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902  473 LLGQM-GGYLLAEHGGDLYLLDQVAARRRLEYDQILASLEKDENYQQGLLEPLVFDFSVYDYQKLKDQLPLLRQLGLEME 551
Cdd:pfam08676   3 GLGQVhGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFELE 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489706902  552 DFGQNTLLMHSYPTWL-KGEVTVQVRELLDQLLSSRENDGKSLLKLVAAKAA 602
Cdd:pfam08676  83 EFGPNSVIVRSVPALLrQQNLQELIRELLDELAEKGGSSLEESLEELLATMA 134
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
 474-602 2.23e-27

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: 107.83  E-value: 2.23e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902   474 LGQM-GGYLLAEHGGDLYLLDQVAARRRLEYDQILAslEKDENYQQGLLEPLVFDFSVYDYQKLKDQLPLLRQLGLEMED 552
Cdd:smart00853   2 LGQVaGTYILAEREDGLYLLDQHAAHERILYEQLLK--QAGGLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELEI 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 489706902   553 FGQNTLLMHSYPTWLK-GEVTVQVRELLDQLLSSRENDGKSLLKLVAAKAA 602
Cdd:smart00853  80 FGPQSLILRSVPALLRqQNLQKLIPELLDLLSDEEENARPSRLEALLASLA 130
TopoII_MutL_Trans cd00329
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 204-305 5.10e-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 [Multi-domain]  Cd Length: 107  Bit Score: 91.17  E-value: 5.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 204 LKQDVANIYGRKVAEKMLTVENEDPDFTLYGLVSEANLTRSSRNFISILLNGRYIK-NYQLSSALLDGYGNKLGG----K 278
Cdd:cd00329    1 LKDRLAEILGDKVADKLIYVEGESDGFRVEGAISYPDSGRSSKDRQFSFVNGRPVReGGTHVKAVREAYTRALNGddvrR 80

                         90       100
                 ....*....|....*....|....*..
gi 489706902 279 YPIAVLAIEADPLLVDVNVHPTKEEVR 305
Cdd:cd00329   81 YPVAVLSLKIPPSLVDVNVHPTKEEVR 107
MutL_Trans_MutL cd03482
MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 206-324 4.15e-20

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


Pssm-ID: 239564 [Multi-domain]  Cd Length: 123  Bit Score: 86.48  E-value: 4.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 206 QDVANIYGRKVAEKMLTVENEDPDFTLYGLVSEANLTRSSRNFISILLNGRYIKNYQLSSALLDGYGNKL-GGKYPIAVL 284
Cdd:cd03482    3 QRLADILGEDFAEQALAIDEEAGGLRLSGWIALPTFARSQADIQYFYVNGRMVRDKLISHAVRQAYSDVLhGGRHPAYVL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489706902 285 AIEADPLLVDVNVHPTKEEVRLSKEKELSRLITSAVTEAL 324
Cdd:cd03482   83 YLELDPAQVDVNVHPAKHEVRFRDSRLVHDFIYHAVKKAL 122
MutL_Trans_MLH1 cd03483
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 211-325 5.43e-15

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: 71.88  E-value: 5.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 211 IYGRKVAEKMLTVE-NEDPD---FTLYGLVSEANLTRSSRNFIsILLNGRYIKNYQLSSALLDGYGNKL-GGKYPIAVLA 285
Cdd:cd03483    9 VYGAAVANELIEVEiSDDDDdlgFKVKGLISNANYSKKKIIFI-LFINNRLVECSALRRAIENVYANYLpKGAHPFVYLS 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489706902 286 IEADPLLVDVNVHPTKEEVRLSKEKELSRLITSAVTEALM 325
Cdd:cd03483   88 LEIPPENVDVNVHPTKREVHFLNEEEIIERIQKLVEDKLS 127
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 19-80 1.12e-09

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: 56.22  E-value: 1.12e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489706902   19 EVIERPASVVKELVENAID--AQASRIRVEVQHSGLKQISVQDNGSGIAPDQVDLAFMRHATSK 80
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKhaAKAGEITVTLSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTAD 64
MutL_Trans_hPMS_1_like cd03485
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 203-316 1.58e-08

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: 53.43  E-value: 1.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 203 NLKQDVANIYGRKVAEKM--LTVENEDPDFTLYGLV----SEANLTRSSRNFISIllNGRYIKNYQ----LSSALLDGYG 272
Cdd:cd03485    1 DHKEALARVLGTAVAANMvpVQSTDEDPQISLEGFLpkpgSDVSKTKSDGKFISV--NSRPVSLGKdigkLLRQYYSSAY 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489706902 273 NKLGG-KYPIAVLAIEADPLLVDVNVHPTKEEVRLSKEKELSRLI 316
Cdd:cd03485   79 RKSSLrRYPVFFLNILCPPGLVDVNIEPDKDDVLLQNKEAVLQAV 123
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 27-75 7.83e-08

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 50.73  E-value: 7.83e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 489706902    27 VVKELVENAIDA--QASRIRVEVQHSGLK-QISVQDNGSGIAPDQVDLAFMR 75
Cdd:smart00387   9 VLSNLLDNAIKYtpEGGRITVTLERDGDHvEITVEDNGPGIPPEDLEKIFEP 60
MutL_Trans_hPMS_2_like cd03484
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 203-312 3.62e-07

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: 49.96  E-value: 3.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902 203 NLKQDVANIYGRKVAEKMLTVENEDPD-----------------FTLYGLVS--EANLTRSS--RNFISIllNGR---YI 258
Cdd:cd03484    1 DIKDNIINVFGGKVIKGLIPINLELDVnptkeeldsdedladseVKITGYISkpSHGCGRSSsdRQFFYI--NGRpvdLK 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489706902 259 KNYQLSSALLDGYGNKlggKYPIAVLAIEADPLLVDVNVHPTKEEVRLSKEKEL 312
Cdd:cd03484   79 KVAKLINEVYKSFNSR---QYPFFILNISLPTSLYDVNVTPDKRTVLLHDEDRL 129
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
 24-122 1.94e-06

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: 433332 [Multi-domain]  Cd Length: 135  Bit Score: 47.71  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902   24 PASVVKELVENAIDAQASRIRVEVQH--SGLKQISVQDNGSGIAPDQVD----LAFMRHATSKIQDEHDLFNIatlgfrG 97
Cdd:pfam13589   1 LEGALAELIDNSIDADATNIKIEVNKnrGGGTEIVIEDDGHGMSPEELInalrLATSAKEAKRGSTDLGRYGI------G 74

                          90       100
                  ....*....|....*....|....*
gi 489706902   98 EALASIAAVAHVEILTSTDGQTATR 122
Cdd:pfam13589  75 LKLASLSLGAKLTVTSKKEGKSSTL 99
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 25-85 1.17e-04

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 44.84  E-value: 1.17e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489706902  25 ASVVKELVENAIDAQAS------RIRVEV-QHSGLKQISVQDNGSGIAPDQVDLAFMRHATSKIQDEH 85
Cdd:COG3290  283 VTILGNLLDNAIEAVEKlpeeerRVELSIrDDGDELVIEVEDSGPGIPEELLEKIFERGFSTKLGEGR 350
PRK04184 PRK04184
DNA topoisomerase VI subunit B; Validated
 27-73 1.33e-04

DNA topoisomerase VI subunit B; Validated


Pssm-ID: 235246 [Multi-domain]  Cd Length: 535  Bit Score: 44.88  E-value: 1.33e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489706902  27 VVKELVENAIDAQAS-----RIRVEVQHSGLKQ----ISVQDNGSGIAPDQVDLAF 73
Cdd:PRK04184  40 TVKELVDNSLDACEEagilpDIKIEIKRVDEGKdhyrVTVEDNGPGIPPEEIPKVF 95
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
27-80 1.54e-04

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 44.51  E-value: 1.54e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489706902  27 VVKELVENAIDA--QASRIRVEVQHSGLK-QISVQDNGSGIAPDQVDLAFMRHATSK 80
Cdd:COG0642  227 VLLNLLSNAIKYtpEGGTVTVSVRREGDRvRISVEDTGPGIPPEDLERIFEPFFRTD 283
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 25-85 1.83e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 41.12  E-value: 1.83e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489706902  25 ASVVKELVENAIDAQASRI----RVEV---QHSGLKQISVQDNGSGIAPDQVDLAFMRHATSKIQDEH 85
Cdd:cd16915    2 ITIVGNLIDNALDALAATGapnkQVEVflrDEGDDLVIEVRDTGPGIAPELRDKVFERGVSTKGQGER 69
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
6-85 2.87e-04

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 42.97  E-value: 2.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902   6 ELSENLTNQIAAGEVIERpasVVKELVENAIDA--QASRIRVEVQHSGLK-QISVQDNGSGIAPDQVDLAFMRHATSKIQ 82
Cdd:COG2205  118 DLPPELPLVYADPELLEQ---VLANLLDNAIKYspPGGTITISARREGDGvRISVSDNGPGIPEEELERIFERFYRGDNS 194


                 ...
gi 489706902  83 DEH 85
Cdd:COG2205  195 RGE 197
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 31-80 4.82e-04

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 43.03  E-value: 4.82e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489706902  31 LVENAIDAQASRIRVEV---QHSGLKQISVQDNGSGIAPDQVDLAFMRHATSK 80
Cdd:COG5000  325 LLKNAIEAIEEGGEIEVstrREDGRVRIEVSDNGPGIPEEVLERIFEPFFTTK 377
HATPase_TopVIB-like cd16933
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family ...
 27-118 8.99e-04

Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family includes the histidine kinase-like ATPase (HATPase) domain of the B subunit of topoisomerase VI (Topo VIB). Topo VI is a heterotetrameric complex composed of two TopVIA and two TopVIB subunits and is categorized as a type II B DNA topoisomerase. It is found in archaea and also in plants. Type II enzymes cleave both strands of a DNA duplex and pass a second duplex through the resulting break in an ATP-dependent mechanism. DNA cleavage by Topo VI generates two-nucleotide 5'-protruding ends.


Pssm-ID: 340410 [Multi-domain]  Cd Length: 203  Bit Score: 41.18  E-value: 8.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489706902  27 VVKELVENAIDAQASR-----IRVEVQHSGLK--QISVQDNGSGIAPDQVDLAFMR-HATSKIQdehdlfNIAT-----L 93
Cdd:cd16933   23 TVRELVENSLDATEEAgilpdIKVEIEEIGKDhyKVIVEDNGPGIPEEQIPKVFGKvLYGSKYH------NKQSrgqqgL 96

                         90       100
                 ....*....|....*....|....*.
gi 489706902  94 GFRGEALAS-IAAVAHVEILTSTDGQ 118
Cdd:cd16933   97 GISAAVLYSqMTTGKPVEIISSTKDS 122
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 31-73 2.14e-03

Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 40.94  E-value: 2.14e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 489706902  31 LVENAIDA----QASRIRVEVQHSGLK-QISVQDNGSGIAPDQVDLAF 73
Cdd:COG4191  264 LLINAIDAmeegEGGRITISTRREGDYvVISVRDNGPGIPPEVLERIF 311
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
22-82 2.24e-03

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 40.93  E-value: 2.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489706902  22 ERPASVVKELVENAIDA--QASRIRVEVQHSGLK-QISVQDNGSGIAPDQVDLAFMRHATSKIQ 82
Cdd:PRK10364 347 DRLTQVLLNLYLNAIQAigQHGVISVTASESGAGvKISVTDSGKGIAADQLEAIFTPYFTTKAE 410
HATPase_MORC-like cd16931
Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger ...
 24-86 4.05e-03

Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger proteins MORC1-4, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of human microrchidia (MORC) family CW-type zinc finger proteins MORC1-4, and related domains. In addition to the HATPase domain, MORC family proteins have a CW-type zinc finger domain containing four conserved cysteines and two conserved tryptophans, and coiled-coil domains at the carboxy-terminus. MORC1 has cross-species differential methylation in association with early life stress, and genome-wide association with major depressive disorder (MDD). MORC2 is involved in several nuclear processes, including transcription modulation and DNA damage repair, and exhibits a cytosolic function in lipogenesis, adipogenic differentiation, and lipid homeostasis by increasing the activity of ACLY. MORC3 regulates p53, and is an antiviral factor which plays an important role during HSV-1 and HCMV infection, and is a positive regulator of influenza virus transcription. MORC4 is highly expressed in a subset of diffuse large B-cell lymphomas and has potential as a lymphoma biomarker.


Pssm-ID: 340408 [Multi-domain]  Cd Length: 118  Bit Score: 37.77  E-value: 4.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489706902  24 PASVVKELVENAIDAQASRIRVEVQHSGLKQ----ISVQDNGSGIAPDQvdlafMRHA-----TSKIQDEHD 86
Cdd:cd16931   12 PFGAVAELVDNARDADATRLDIFIDDINLLRggfmLSFLDDGNGMTPEE-----AHHMisfgfSDKRSDDHD 78
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 28-75 8.56e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain.


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 36.62  E-value: 8.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489706902  28 VKELVENAI--DAQASRIRVEVQHSGLKQISVQDNGSGIAPDQVDLAFMR 75
Cdd:cd16940   18 LRNLVDNAVrySPQGSRVEIKLSADDGAVIRVEDNGPGIDEEELEALFER 67
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 27-73 9.02e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli EnvZ and Pseudomonas aeruginosa BfmS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli EnvZ of the EnvZ-OmpR two-component regulatory system (TCS), which functions in osmoregulation. It also contains the HATPase domain of Pseudomonas aeruginosa BfmS, the HK of the BfmSR TCS, which functions in the regulation of the rhl quorum-sensing system and bacterial virulence in P. aeruginosa. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a periplasmic domain.


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 36.27  E-value: 9.02e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 489706902  27 VVKELVENAIDAQASRIRVEVQHSGLK-QISVQDNGSGIAPDQVDLAF 73
Cdd:cd16950    4 VLSNLVDNALRYGGGWVEVSSDGEGNRtRIQVLDNGPGIAPEEVDELF 51
 
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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