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Conserved domains on  [gi|497557756|ref|WP_009871940|]
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DNA mismatch repair endonuclease MutL [Chlamydia trachomatis]

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;
6-514 1.40e-175

DNA mismatch repair endonuclease MutL;


:

Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 510.14  E-value: 1.40e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756   6 SRIRLLDSVTVNQISAGEVIENAASVVKELIENSLDAGADEIHIETLGGGRGQIVVRDNGVGMDPEEVPVALQRHATSKI 85
Cdd:PRK00095   1 MPIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756  86 AHFADIFSLASYGFRGEALPSIASISKMEIHTARAG-GLGSKTLIEKGEPVCCEPAPRQQGTTIAVHSLFYNVPMRQSFQ 164
Cdd:PRK00095  81 ASLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADaAEGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKFL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 165 KSPQMDRLAIRRLLENSVLSSEGIGWTWISECRQELYVAKKQGFIERVALVLGESFVQEAFFIDKQQGDLRVLGFLGSPN 244
Cdd:PRK00095 161 KSEKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 245 QHRSTRQGQRLFINNRAVESSFISKKVAEAYAWMIPAQRYPIFVLKLFLPPMWCDFNVHPQKTEVRLLQEGQISNLLVEA 324
Cdd:PRK00095 241 LSRANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDLIVQA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 325 ISEALLRRSPSLEETVLKVPTEKI--------------PIENEGISVPSIRPAIVSAPLSCPTFSQQPYLKTEMATIVSR 390
Cdd:PRK00095 321 IQEALAQSGLIPAAAGANQVLEPAepeplplqqtplyaSGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSEAA 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 391 DSASSSLSVVEKVRFLTS-----------LGKVL--------LVEDSEGVHVVFVQAARKHLFYVSLLSERLESRLACQT 451
Cdd:PRK00095 401 AAASAEAAAAAPAAAPEPaeaaeeadsfpLGYALgqlhgtyiLAENEDGLYLVDQHAAHERLLYEQLKDKLAEVGLASQP 480

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497557756 452 FLLPSSVQMTKLEADFLQMRLEALTALGIELSRISPDSFAIESAPPFIQEEELKEWIVALAQE 514
Cdd:PRK00095 481 LLIPLVLELSEDEADRLEEHKELLARLGLELEPFGPNSFAVREVPALLGQQELEELIRDLLDE 543
 
Name Accession Description Interval E-value
mutL PRK00095
DNA mismatch repair endonuclease MutL;
6-514 1.40e-175

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 510.14  E-value: 1.40e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756   6 SRIRLLDSVTVNQISAGEVIENAASVVKELIENSLDAGADEIHIETLGGGRGQIVVRDNGVGMDPEEVPVALQRHATSKI 85
Cdd:PRK00095   1 MPIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756  86 AHFADIFSLASYGFRGEALPSIASISKMEIHTARAG-GLGSKTLIEKGEPVCCEPAPRQQGTTIAVHSLFYNVPMRQSFQ 164
Cdd:PRK00095  81 ASLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADaAEGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKFL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 165 KSPQMDRLAIRRLLENSVLSSEGIGWTWISECRQELYVAKKQGFIERVALVLGESFVQEAFFIDKQQGDLRVLGFLGSPN 244
Cdd:PRK00095 161 KSEKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 245 QHRSTRQGQRLFINNRAVESSFISKKVAEAYAWMIPAQRYPIFVLKLFLPPMWCDFNVHPQKTEVRLLQEGQISNLLVEA 324
Cdd:PRK00095 241 LSRANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDLIVQA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 325 ISEALLRRSPSLEETVLKVPTEKI--------------PIENEGISVPSIRPAIVSAPLSCPTFSQQPYLKTEMATIVSR 390
Cdd:PRK00095 321 IQEALAQSGLIPAAAGANQVLEPAepeplplqqtplyaSGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSEAA 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 391 DSASSSLSVVEKVRFLTS-----------LGKVL--------LVEDSEGVHVVFVQAARKHLFYVSLLSERLESRLACQT 451
Cdd:PRK00095 401 AAASAEAAAAAPAAAPEPaeaaeeadsfpLGYALgqlhgtyiLAENEDGLYLVDQHAAHERLLYEQLKDKLAEVGLASQP 480

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497557756 452 FLLPSSVQMTKLEADFLQMRLEALTALGIELSRISPDSFAIESAPPFIQEEELKEWIVALAQE 514
Cdd:PRK00095 481 LLIPLVLELSEDEADRLEEHKELLARLGLELEPFGPNSFAVREVPALLGQQELEELIRDLLDE 543
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
6-514 4.35e-140

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 415.98  E-value: 4.35e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756   6 SRIRLLDSVTVNQISAGEVIENAASVVKELIENSLDAGADEIHIETLGGGRGQIVVRDNGVGMDPEEVPVALQRHATSKI 85
Cdd:COG0323    2 PKIRLLPDELANQIAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLPLAFERHATSKI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756  86 AHFADIFSLASYGFRGEALPSIASISKMEIHTARAGG-LGSKTLIEKGEPVCCEPAPRQQGTTIAVHSLFYNVPMRQSFQ 164
Cdd:COG0323   82 RSAEDLFRIRTLGFRGEALASIASVSRLTLTTRTAGAeLGTRIEVEGGKVVEVEPAAAPKGTTVEVRDLFFNTPARRKFL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 165 KSPQMDRLAIRRLLENSVLSSEGIGWTWISECRQELYVAKKQGFIERVALVLGESFVQEAFFIDKQQGDLRVLGFLGSPN 244
Cdd:COG0323  162 KSDATELAHITDVVRRLALAHPDIAFTLIHNGREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKPE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 245 QHRSTRQGQRLFINNRAVESSFISKKVAEAYAWMIPAQRYPIFVLKLFLPPMWCDFNVHPQKTEVRLLQEGQISNLLVEA 324
Cdd:COG0323  242 FSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRSA 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 325 ISEALlrrspsleetvlkvptekipienegisvpsirpaivsaplscptfsQQPYLktemATIvsrdsassslsvvekvr 404
Cdd:COG0323  322 VREAL----------------------------------------------AQAAL----GQL----------------- 334

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 405 fltsLGKVLLVEDSEGVHVVFVQAARKHLFYVSLLSERLESRLACQTFLLPSSVQMTKLEADFLQMRLEALTALGIELSR 484
Cdd:COG0323  335 ----HGTYILAENEDGLVLIDQHAAHERILYERLKKALAEGGVASQPLLIPETLELSPAEAALLEEHLEELARLGFEIEP 410

                        490       500       510
                 ....*....|....*....|....*....|
gi 497557756 485 ISPDSFAIESAPPFIQEEELKEWIVALAQE 514
Cdd:COG0323  411 FGPNTVAVRAVPALLGEGDAEELLRDLLDE 440
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 6-310 5.54e-132

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: 387.77  E-value: 5.54e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756    6 SRIRLLDSVTVNQISAGEVIENAASVVKELIENSLDAGADEIHIETLGGGRGQIVVRDNGVGMDPEEVPVALQRHATSKI 85
Cdd:TIGR00585   1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756   86 AHFADIFSLASYGFRGEALPSIASISKMEIHTAR--AGGLGSKTLIEKGEPVCCEPAPRQQGTTIAVHSLFYNVPMRQSF 163
Cdd:TIGR00585  81 QSFEDLERIETLGFRGEALASISSVSRLTITTKTsaADGLAYQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRKF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756  164 QKSPQMDRLAIRRLLENSVLSSEGIGWTWISECRQELYVAKK--QGFIE-RVALVLGESFVQEAF-FIDKQQGDLRVLGF 239
Cdd:TIGR00585 161 LKSPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLQLSTKpnQSTKEnRIRSVFGTAVLRKLIpLDEWEDLDLQLEGF 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497557756  240 LGSPNQHRSTRQG-QRLFINNRAVESSFISKKVAEAYAWMIPAQRYPIFVLKLFLPPMWCDFNVHPQKTEVR 310
Cdd:TIGR00585 241 ISQPNVTRSRRSGwQFLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 15-195 3.23e-77

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: 242.34  E-value: 3.23e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756  15 TVNQISAGEVIENAASVVKELIENSLDAGADEIHIETLGGGRGQIVVRDNGVGMDPEEVPVALQRHATSKIAHFADIFSL 94
Cdd:cd16926    1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756  95 ASYGFRGEALPSIASISKMEIHTARAGG-LGSKTLIEKG-EPVCCEPAPRQQGTTIAVHSLFYNVPMRQSFQKSPQMDRL 172
Cdd:cd16926   81 TTLGFRGEALASIASVSRLTITTRTADDdVGTRLVVDGGgIIEEVKPAAAPVGTTVTVRDLFYNTPARRKFLKSPKTELS 160

                        170       180
                 ....*....|....*....|...
gi 497557756 173 AIRRLLENSVLSSEGIGWTWISE 195
Cdd:cd16926  161 KILDLVQRLALAHPDVSFSLTHD 183
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 215-329 2.70e-34

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: 125.69  E-value: 2.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756  215 VLGESFVQEAFFIDKQQGDLRVLGFLGSPNQHRSTRQGQRLFINNRAVESSFISKKVAEAYAWMIPAQRYPIFVLKLFLP 294
Cdd:pfam01119   3 IYGKEFAENLLPIEKEDDGLRLSGYISKPTLSRSNRDYQYLFVNGRPVRDKLLSHAIREAYRDLLPKGRYPVAVLFLEID 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 497557756  295 PMWCDFNVHPQKTEVRLLQEGQISNLLVEAISEAL 329
Cdd:pfam01119  83 PELVDVNVHPTKREVRFRDEREVYDFIKEALREAL 117
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
 410-545 9.01e-15

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: 71.62  E-value: 9.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756   410 GKVLLVEDSEGVHVVFVQAARKHLFYVSLLSErlESRLACQTFLLPSSVQMTKLEADFLQMRLEALTALGIELSRISPDS 489
Cdd:smart00853   7 GTYILAEREDGLYLLDQHAAHERILYEQLLKQ--AGGLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELEIFGPQS 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 497557756   490 FAIESAPPFIQEEELKEWIVALAQEGALHVGESFEQLVENTVQKLVFSRNARAFDY 545
Cdd:smart00853  85 LILRSVPALLRQQNLQKLIPELLDLLSDEEENARPSRLEALLASLACRSAIRAGDA 140
 
Name Accession Description Interval E-value
mutL PRK00095
DNA mismatch repair endonuclease MutL;
6-514 1.40e-175

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 510.14  E-value: 1.40e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756   6 SRIRLLDSVTVNQISAGEVIENAASVVKELIENSLDAGADEIHIETLGGGRGQIVVRDNGVGMDPEEVPVALQRHATSKI 85
Cdd:PRK00095   1 MPIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756  86 AHFADIFSLASYGFRGEALPSIASISKMEIHTARAG-GLGSKTLIEKGEPVCCEPAPRQQGTTIAVHSLFYNVPMRQSFQ 164
Cdd:PRK00095  81 ASLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADaAEGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKFL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 165 KSPQMDRLAIRRLLENSVLSSEGIGWTWISECRQELYVAKKQGFIERVALVLGESFVQEAFFIDKQQGDLRVLGFLGSPN 244
Cdd:PRK00095 161 KSEKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 245 QHRSTRQGQRLFINNRAVESSFISKKVAEAYAWMIPAQRYPIFVLKLFLPPMWCDFNVHPQKTEVRLLQEGQISNLLVEA 324
Cdd:PRK00095 241 LSRANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDLIVQA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 325 ISEALLRRSPSLEETVLKVPTEKI--------------PIENEGISVPSIRPAIVSAPLSCPTFSQQPYLKTEMATIVSR 390
Cdd:PRK00095 321 IQEALAQSGLIPAAAGANQVLEPAepeplplqqtplyaSGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSEAA 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 391 DSASSSLSVVEKVRFLTS-----------LGKVL--------LVEDSEGVHVVFVQAARKHLFYVSLLSERLESRLACQT 451
Cdd:PRK00095 401 AAASAEAAAAAPAAAPEPaeaaeeadsfpLGYALgqlhgtyiLAENEDGLYLVDQHAAHERLLYEQLKDKLAEVGLASQP 480

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497557756 452 FLLPSSVQMTKLEADFLQMRLEALTALGIELSRISPDSFAIESAPPFIQEEELKEWIVALAQE 514
Cdd:PRK00095 481 LLIPLVLELSEDEADRLEEHKELLARLGLELEPFGPNSFAVREVPALLGQQELEELIRDLLDE 543
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
6-514 4.35e-140

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 415.98  E-value: 4.35e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756   6 SRIRLLDSVTVNQISAGEVIENAASVVKELIENSLDAGADEIHIETLGGGRGQIVVRDNGVGMDPEEVPVALQRHATSKI 85
Cdd:COG0323    2 PKIRLLPDELANQIAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLPLAFERHATSKI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756  86 AHFADIFSLASYGFRGEALPSIASISKMEIHTARAGG-LGSKTLIEKGEPVCCEPAPRQQGTTIAVHSLFYNVPMRQSFQ 164
Cdd:COG0323   82 RSAEDLFRIRTLGFRGEALASIASVSRLTLTTRTAGAeLGTRIEVEGGKVVEVEPAAAPKGTTVEVRDLFFNTPARRKFL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 165 KSPQMDRLAIRRLLENSVLSSEGIGWTWISECRQELYVAKKQGFIERVALVLGESFVQEAFFIDKQQGDLRVLGFLGSPN 244
Cdd:COG0323  162 KSDATELAHITDVVRRLALAHPDIAFTLIHNGREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKPE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 245 QHRSTRQGQRLFINNRAVESSFISKKVAEAYAWMIPAQRYPIFVLKLFLPPMWCDFNVHPQKTEVRLLQEGQISNLLVEA 324
Cdd:COG0323  242 FSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRSA 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 325 ISEALlrrspsleetvlkvptekipienegisvpsirpaivsaplscptfsQQPYLktemATIvsrdsassslsvvekvr 404
Cdd:COG0323  322 VREAL----------------------------------------------AQAAL----GQL----------------- 334

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 405 fltsLGKVLLVEDSEGVHVVFVQAARKHLFYVSLLSERLESRLACQTFLLPSSVQMTKLEADFLQMRLEALTALGIELSR 484
Cdd:COG0323  335 ----HGTYILAENEDGLVLIDQHAAHERILYERLKKALAEGGVASQPLLIPETLELSPAEAALLEEHLEELARLGFEIEP 410

                        490       500       510
                 ....*....|....*....|....*....|
gi 497557756 485 ISPDSFAIESAPPFIQEEELKEWIVALAQE 514
Cdd:COG0323  411 FGPNTVAVRAVPALLGEGDAEELLRDLLDE 440
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 6-310 5.54e-132

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: 387.77  E-value: 5.54e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756    6 SRIRLLDSVTVNQISAGEVIENAASVVKELIENSLDAGADEIHIETLGGGRGQIVVRDNGVGMDPEEVPVALQRHATSKI 85
Cdd:TIGR00585   1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756   86 AHFADIFSLASYGFRGEALPSIASISKMEIHTAR--AGGLGSKTLIEKGEPVCCEPAPRQQGTTIAVHSLFYNVPMRQSF 163
Cdd:TIGR00585  81 QSFEDLERIETLGFRGEALASISSVSRLTITTKTsaADGLAYQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRKF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756  164 QKSPQMDRLAIRRLLENSVLSSEGIGWTWISECRQELYVAKK--QGFIE-RVALVLGESFVQEAF-FIDKQQGDLRVLGF 239
Cdd:TIGR00585 161 LKSPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLQLSTKpnQSTKEnRIRSVFGTAVLRKLIpLDEWEDLDLQLEGF 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497557756  240 LGSPNQHRSTRQG-QRLFINNRAVESSFISKKVAEAYAWMIPAQRYPIFVLKLFLPPMWCDFNVHPQKTEVR 310
Cdd:TIGR00585 241 ISQPNVTRSRRSGwQFLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 15-195 3.23e-77

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: 242.34  E-value: 3.23e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756  15 TVNQISAGEVIENAASVVKELIENSLDAGADEIHIETLGGGRGQIVVRDNGVGMDPEEVPVALQRHATSKIAHFADIFSL 94
Cdd:cd16926    1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756  95 ASYGFRGEALPSIASISKMEIHTARAGG-LGSKTLIEKG-EPVCCEPAPRQQGTTIAVHSLFYNVPMRQSFQKSPQMDRL 172
Cdd:cd16926   81 TTLGFRGEALASIASVSRLTITTRTADDdVGTRLVVDGGgIIEEVKPAAAPVGTTVTVRDLFYNTPARRKFLKSPKTELS 160

                        170       180
                 ....*....|....*....|...
gi 497557756 173 AIRRLLENSVLSSEGIGWTWISE 195
Cdd:cd16926  161 KILDLVQRLALAHPDVSFSLTHD 183
MutL_Trans cd00782
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 209-329 6.59e-41

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: 144.22  E-value: 6.59e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 209 IERVALVLGESFVQEAFFIDKQQGDLRVLGFLGSPNQHRSTRQGQRLFINNRAVESSFISKKVAEAYAWMIPAQRYPIFV 288
Cdd:cd00782    2 KDRIAQVYGKEVAKNLIEVELESGDFRISGYISKPDFGRSSKDRQFLFVNGRPVRDKLLSKAINEAYRSYLPKGRYPVFV 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 497557756 289 LKLFLPPMWCDFNVHPQKTEVRLLQEGQISNLLVEAISEAL 329
Cdd:cd00782   82 LNLELPPELVDVNVHPTKREVRFSDEEEVLELIREALRSAL 122
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 215-329 2.70e-34

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: 125.69  E-value: 2.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756  215 VLGESFVQEAFFIDKQQGDLRVLGFLGSPNQHRSTRQGQRLFINNRAVESSFISKKVAEAYAWMIPAQRYPIFVLKLFLP 294
Cdd:pfam01119   3 IYGKEFAENLLPIEKEDDGLRLSGYISKPTLSRSNRDYQYLFVNGRPVRDKLLSHAIREAYRDLLPKGRYPVAVLFLEID 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 497557756  295 PMWCDFNVHPQKTEVRLLQEGQISNLLVEAISEAL 329
Cdd:pfam01119  83 PELVDVNVHPTKREVRFRDEREVYDFIKEALREAL 117
MutL_Trans_MutL cd03482
MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 209-329 3.00e-28

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: 109.21  E-value: 3.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 209 IERVALVLGESFVQEAFFIDKQQGDLRVLGFLGSPNQHRSTRQGQRLFINNRAVESSFISKKVAEAYAWMIPAQRYPIFV 288
Cdd:cd03482    2 LQRLADILGEDFAEQALAIDEEAGGLRLSGWIALPTFARSQADIQYFYVNGRMVRDKLISHAVRQAYSDVLHGGRHPAYV 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 497557756 289 LKLFLPPMWCDFNVHPQKTEVRLLQEGQISNLLVEAISEAL 329
Cdd:cd03482   82 LYLELDPAQVDVNVHPAKHEVRFRDSRLVHDFIYHAVKKAL 122
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
 410-545 7.02e-26

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: 103.45  E-value: 7.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756  410 GKVLLVEDSEGVHVVFVQAARKHLFYVSLLSERLESRLACQTFLLPSSVQMTKLEADFLQMRLEALTALGIELSRISPDS 489
Cdd:pfam08676   9 GTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFELEEFGPNS 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 497557756  490 FAIESAPPFIQEEELKEWIVALAQEGALHVGESFEQLVENTVQKLVFSRNARAFDY 545
Cdd:pfam08676  89 VIVRSVPALLRQQNLQELIRELLDELAEKGGSSLEESLEELLATMACHSAVRAGRR 144
TopoII_MutL_Trans cd00329
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 208-310 2.98e-24

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: 97.33  E-value: 2.98e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 208 FIERVALVLGESFVQEAFFIDKQQGDLRVLGFLGSPNQHRSTRQGQRLFINNRAVESSF-ISKKVAEAYAWMI---PAQR 283
Cdd:cd00329    1 LKDRLAEILGDKVADKLIYVEGESDGFRVEGAISYPDSGRSSKDRQFSFVNGRPVREGGtHVKAVREAYTRALngdDVRR 80

                         90       100
                 ....*....|....*....|....*..
gi 497557756 284 YPIFVLKLFLPPMWCDFNVHPQKTEVR 310
Cdd:cd00329   81 YPVAVLSLKIPPSLVDVNVHPTKEEVR 107
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
 410-545 9.01e-15

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: 71.62  E-value: 9.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756   410 GKVLLVEDSEGVHVVFVQAARKHLFYVSLLSErlESRLACQTFLLPSSVQMTKLEADFLQMRLEALTALGIELSRISPDS 489
Cdd:smart00853   7 GTYILAEREDGLYLLDQHAAHERILYEQLLKQ--AGGLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELEIFGPQS 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 497557756   490 FAIESAPPFIQEEELKEWIVALAQEGALHVGESFEQLVENTVQKLVFSRNARAFDY 545
Cdd:smart00853  85 LILRSVPALLRQQNLQKLIPELLDLLSDEEENARPSRLEALLASLACRSAIRAGDA 140
MutL_Trans_MLH1 cd03483
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 255-330 8.55e-13

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: 65.33  E-value: 8.55e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497557756 255 LFINNRAVESSFISKKVAEAYAWMIPAQRYPIFVLKLFLPPMWCDFNVHPQKTEVRLLQEGQISNLLVEAISEALL 330
Cdd:cd03483   52 LFINNRLVECSALRRAIENVYANYLPKGAHPFVYLSLEIPPENVDVNVHPTKREVHFLNEEEIIERIQKLVEDKLS 127
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
 30-129 1.46e-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: 433332 [Multi-domain]  Cd Length: 135  Bit Score: 59.27  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756   30 SVVKELIENSLDAGADEIHIE--TLGGGRGQIVVRDNGVGMDPEEVPVALQRHATSKIAHFaDIFSLASYGFrGEALPSI 107
Cdd:pfam13589   3 GALAELIDNSIDADATNIKIEvnKNRGGGTEIVIEDDGHGMSPEELINALRLATSAKEAKR-GSTDLGRYGI-GLKLASL 80

                          90       100
                  ....*....|....*....|..
gi 497557756  108 ASISKMEIHTARAGGLGSKTLI 129
Cdd:pfam13589  81 SLGAKLTVTSKKEGKSSTLTLD 102
MutL_Trans_hPMS_2_like cd03484
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 235-327 4.13e-08

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: 52.27  E-value: 4.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 235 RVLGFLGSP--NQHRSTRQGQRLFINNRAVESSFISKKVAEAYAwMIPAQRYPIFVLKLFLPPMWCDFNVHPQKTEVRLL 312
Cdd:cd03484   46 KITGYISKPshGCGRSSSDRQFFYINGRPVDLKKVAKLINEVYK-SFNSRQYPFFILNISLPTSLYDVNVTPDKRTVLLH 124

                         90
                 ....*....|....*
gi 497557756 313 QEGQISNLLVEAISE 327
Cdd:cd03484  125 DEDRLIDTLKTSLSE 139
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 31-84 4.77e-08

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: 51.21  E-value: 4.77e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 497557756   31 VVKELIENSLD--AGADEIHIETLGGGRGQIVVRDNGVGMDPEEVPVALQRHATSK 84
Cdd:pfam02518   9 VLSNLLDNALKhaAKAGEITVTLSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTAD 64
PRK04184 PRK04184
DNA topoisomerase VI subunit B; Validated
 31-74 2.37e-06

DNA topoisomerase VI subunit B; Validated


Pssm-ID: 235246 [Multi-domain]  Cd Length: 535  Bit Score: 50.28  E-value: 2.37e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 497557756  31 VVKELIENSLDAgADE--------IHIETLGGGRG--QIVVRDNGVGMDPEEVP 74
Cdd:PRK04184  40 TVKELVDNSLDA-CEEagilpdikIEIKRVDEGKDhyRVTVEDNGPGIPPEEIP 92
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 31-79 2.54e-06

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 46.49  E-value: 2.54e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 497557756    31 VVKELIENSLDAGADEIHIE---TLGGGRGQIVVRDNGVGMDPEEVPVALQR 79
Cdd:smart00387   9 VLSNLLDNAIKYTPEGGRITvtlERDGDHVEITVEDNGPGIPPEDLEKIFEP 60
HATPase_TopVIB-like cd16933
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family ...
 31-74 5.71e-06

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: 47.34  E-value: 5.71e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 497557756  31 VVKELIENSLDAgADE--------IHIETLGGGRGQIVVRDNGVGMDPEEVP 74
Cdd:cd16933   23 TVRELVENSLDA-TEEagilpdikVEIEEIGKDHYKVIVEDNGPGIPEEQIP 73
MutL_Trans_hPMS_1_like cd03485
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 231-331 9.51e-06

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: 45.34  E-value: 9.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 231 QGDLRVLGFLGSPNQHRS--TRQGQRLFINNRAVESSF-ISKKVAEAY---AWMIPAQRYPIFVLKLFLPPMWCDFNVHP 304
Cdd:cd03485   27 DPQISLEGFLPKPGSDVSktKSDGKFISVNSRPVSLGKdIGKLLRQYYssaYRKSSLRRYPVFFLNILCPPGLVDVNIEP 106

                         90       100
                 ....*....|....*....|....*..
gi 497557756 305 QKTEVrLLQEGQISNLLVEAISEALLR 331
Cdd:cd03485  107 DKDDV-LLQNKEAVLQAVENLLESLYG 132
PRK14083 PRK14083
HSP90 family protein; Provisional
 32-73 2.70e-04

HSP90 family protein; Provisional


Pssm-ID: 237603 [Multi-domain]  Cd Length: 601  Bit Score: 43.78  E-value: 2.70e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 497557756  32 VKELIENSLDA----------GADEIHIETLGGGRGQIVVRDNGVGMDPEEV 73
Cdd:PRK14083  28 VRELLQNAVDAitarraldptAPGRIRIELTDAGGGTLIVEDNGIGLTEEEV 79
HATPase_MORC-like cd16931
Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger ...
 30-73 3.49e-04

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: 40.47  E-value: 3.49e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 497557756  30 SVVKELIENSLDAGADEIHI----ETLGGGRGQIVVRDNGVGMDPEEV 73
Cdd:cd16931   14 GAVAELVDNARDADATRLDIfiddINLLRGGFMLSFLDDGNGMTPEEA 61
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 35-71 1.42e-03

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 41.32  E-value: 1.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 497557756  35 LIENSLDAGAD----EIHIET-LGGGRGQIVVRDNGVGMDPE 71
Cdd:COG4191  264 LLINAIDAMEEgeggRITISTrREGDYVVISVRDNGPGIPPE 305
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 31-78 1.87e-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: 37.81  E-value: 1.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 497557756  31 VVKELIENSLDAGADEIHIETLGGGRG-QIVVRDNGVGMDPEEVPVALQ 78
Cdd:cd16950    4 VLSNLVDNALRYGGGWVEVSSDGEGNRtRIQVLDNGPGIAPEEVDELFQ 52
MutL_Trans_MLH3 cd03486
MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 215-329 1.95e-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 [Multi-domain]  Cd Length: 141  Bit Score: 38.84  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497557756 215 VLGESFVQEAFFIDKQQGDLRVLGFLGSPnQHRSTRQgQRLFINNRAVESSFISKKVAEAYA--------WMIPA----- 281
Cdd:cd03486    9 IYGLVLAQKLKEVSAKFQEYEVSGYISSE-GHYSKSF-QFIYVNGRLYLKTRFHKLINKLFRktsavaknKSSPQskssr 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 497557756 282 ------QRYPIFVLKLFLPPMWCDFNVHPQKTEVRLLQEGQISNLLVEAISEAL 329
Cdd:cd03486   87 rgkrsqESYPVFVLNITCPASEYDLSQEPSKTIIEFKDWKTLLPLILEVVKSFL 140
PRK14867 PRK14867
DNA topoisomerase VI subunit B; Provisional
 25-74 4.43e-03

DNA topoisomerase VI subunit B; Provisional


Pssm-ID: 237841 [Multi-domain]  Cd Length: 659  Bit Score: 39.80  E-value: 4.43e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 497557756  25 IENAASVVKELIENSLDAGAD-------EIHIETLGGGRGQIVVRDNGVGMDPEEVP 74
Cdd:PRK14867  34 LRSMTTIIHELVTNSLDACEEaeilpdiKVEIEKLGSDHYKVAVEDNGPGIPPEFVP 90
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 35-84 5.44e-03

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: 39.56  E-value: 5.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 497557756  35 LIENSLDAGAD--EIHIET-LGGGRGQIVVRDNGVGMDPEEVPVALQRHATSK 84
Cdd:COG5000  325 LLKNAIEAIEEggEIEVSTrREDGRVRIEVSDNGPGIPEEVLERIFEPFFTTK 377
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
31-84 7.33e-03

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 38.74  E-value: 7.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 497557756  31 VVKELIENSLDAGAD--EIHIET-LGGGRGQIVVRDNGVGMDPEEVPVALQRHATSK 84
Cdd:COG0642  227 VLLNLLSNAIKYTPEggTVTVSVrREGDRVRISVEDTGPGIPPEDLERIFEPFFRTD 283
 
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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