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Conserved domains on  [gi|1958668105|ref|XP_038945107|]
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mismatch repair endonuclease PMS2 isoform X2 [Rattus norvegicus]

Protein Classification

DNA mismatch repair endonuclease MutL( domain architecture ID 11489264)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 13-344 2.08e-140

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: 408.57  E-value: 2.08e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105  13 KAIKPIDGKSVHQICSGQVVLSLSTAVKELIENSVDAGATSIDLRLKDYGVDLIEVSDNGCGVEEENFEGLALKHHTSKI 92
Cdd:TIGR00585   1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105  93 REFADLTQVETFGFRGEALSSLCALSDVTISTCHV-SASIGTRLVLDhNGKIIQKTPCPRPKGTTVSVQNLFYTLPVRHK 171
Cdd:TIGR00585  81 QSFEDLERIETLGFRGEALASISSVSRLTITTKTSaADGLAYQALLE-GGMIESIKPAPRPVGTTVEVRDLFYNLPVRRK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 172 eFQRNIKKEYAKMVQVLQAYCIISAGIRVSCTNqlgQGKRQPVVCTSGSSGMKEN-IGSVFGQKQLQSLVPFVQLPPSDs 250
Cdd:TIGR00585 160 -FLKSPKKEFRKILDVLQRYALIHPDISFSLTH---DGKKVLQLSTKPNQSTKENrIRSVFGTAVLRKLIPLDEWEDLD- 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 251 vceeyclsacgtpqspFRISGFISQCTHGAGRSSTDrQFFFINQRPCDPAKVSRLVNEVYHMYN-RHQYPFVVLNVSVDS 329
Cdd:TIGR00585 235 ----------------LQLEGFISQPNVTRSRRSGW-QFLFINGRPVELKLLLKAIREVYHEYLpKGQYPVFVLNLEIDP 297

                         330
                  ....*....|....*
gi 1958668105 330 ECVDINVTPDKRQIL 344
Cdd:TIGR00585 298 ELVDVNVHPDKKEVR 312
 
Name Accession Description Interval E-value
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 13-344 2.08e-140

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: 408.57  E-value: 2.08e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105  13 KAIKPIDGKSVHQICSGQVVLSLSTAVKELIENSVDAGATSIDLRLKDYGVDLIEVSDNGCGVEEENFEGLALKHHTSKI 92
Cdd:TIGR00585   1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105  93 REFADLTQVETFGFRGEALSSLCALSDVTISTCHV-SASIGTRLVLDhNGKIIQKTPCPRPKGTTVSVQNLFYTLPVRHK 171
Cdd:TIGR00585  81 QSFEDLERIETLGFRGEALASISSVSRLTITTKTSaADGLAYQALLE-GGMIESIKPAPRPVGTTVEVRDLFYNLPVRRK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 172 eFQRNIKKEYAKMVQVLQAYCIISAGIRVSCTNqlgQGKRQPVVCTSGSSGMKEN-IGSVFGQKQLQSLVPFVQLPPSDs 250
Cdd:TIGR00585 160 -FLKSPKKEFRKILDVLQRYALIHPDISFSLTH---DGKKVLQLSTKPNQSTKENrIRSVFGTAVLRKLIPLDEWEDLD- 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 251 vceeyclsacgtpqspFRISGFISQCTHGAGRSSTDrQFFFINQRPCDPAKVSRLVNEVYHMYN-RHQYPFVVLNVSVDS 329
Cdd:TIGR00585 235 ----------------LQLEGFISQPNVTRSRRSGW-QFLFINGRPVELKLLLKAIREVYHEYLpKGQYPVFVLNLEIDP 297

                         330
                  ....*....|....*
gi 1958668105 330 ECVDINVTPDKRQIL 344
Cdd:TIGR00585 298 ELVDVNVHPDKKEVR 312
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 22-205 5.85e-93

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: 282.40  E-value: 5.85e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105  22 SVHQICSGQVVLSLSTAVKELIENSVDAGATSIDLRLKDYGVDLIEVSDNGCGVEEENFEGLALKHHTSKIREFADLTQV 101
Cdd:cd16926     1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 102 ETFGFRGEALSSLCALSDVTISTCHVSASIGTRLVLDHNGKIIQKTPCPRPKGTTVSVQNLFYTLPVRHKeFQRNIKKEY 181
Cdd:cd16926    81 TTLGFRGEALASIASVSRLTITTRTADDDVGTRLVVDGGGIIEEVKPAAAPVGTTVTVRDLFYNTPARRK-FLKSPKTEL 159

                         170       180
                  ....*....|....*....|....
gi 1958668105 182 AKMVQVLQAYCIISAGIRVSCTNQ 205
Cdd:cd16926   160 SKILDLVQRLALAHPDVSFSLTHD 183
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
23-359 5.46e-84

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 270.76  E-value: 5.46e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105  23 VHQICSGQVV---LSlstAVKELIENSVDAGATSIDLRLKDYGVDLIEVSDNGCGVEEENFEgLALKHH-TSKIREFADL 98
Cdd:COG0323    12 ANQIAAGEVVerpAS---VVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLP-LAFERHaTSKIRSAEDL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105  99 TQVETFGFRGEALSSLCALSDVTISTCHVSASIGTRLVLDhNGKIIQKTPCPRPKGTTVSVQNLFYTLPVRHKeFQRNIK 178
Cdd:COG0323    88 FRIRTLGFRGEALASIASVSRLTLTTRTAGAELGTRIEVE-GGKVVEVEPAAAPKGTTVEVRDLFFNTPARRK-FLKSDA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 179 KEYAKMVQVLQAYCIISAGIRVSCTNqlgQGKrqPVVCTSGSSGMKENIGSVFGQKQLQSLVPfvqlppsdsVCEEycls 258
Cdd:COG0323   166 TELAHITDVVRRLALAHPDIAFTLIH---NGR--EVFQLPGAGDLLQRIAAIYGREFAENLLP---------VEAE---- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 259 acgtpQSPFRISGFISQCTHgaGRSSTDRQFFFINQRPCDPAKVSRLVNEVYH---MYNRHqyPFVVLNVSVDSECVDIN 335
Cdd:COG0323   228 -----REGLRLSGYIGKPEF--SRSNRDYQYFFVNGRPVRDKLLSHAVREAYRdllPKGRY--PVAVLFLELDPELVDVN 298

                         330       340
                  ....*....|....*....|....
gi 1958668105 336 VTPDKRQILLQEEKLLLAVLKTSL 359
Cdd:COG0323   299 VHPTKTEVRFRDEREVYDLVRSAV 322
mutL PRK00095
DNA mismatch repair endonuclease MutL;
14-351 7.07e-74

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 246.67  E-value: 7.07e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105  14 AIKPIDGKSVHQICSGQVVLSLSTAVKELIENSVDAGATSIDLRLKDYGVDLIEVSDNGCGVEEENFEgLALK-HHTSKI 92
Cdd:PRK00095    2 PIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLA-LALArHATSKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105  93 REFADLTQVETFGFRGEALSSLCALSDVTISTCHVSASIGTRLVlDHNGKIIQKTPCPRPKGTTVSVQNLFYTLPVRHKe 172
Cdd:PRK00095   81 ASLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAEGWQIV-YEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRK- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 173 FQRNIKKEYAKMVQVLQAYCIISAGIRVSCTNqlgQGKrqPVVCTSGSSGMKENIGSVFGQKQLQSLVPFvqlppsDSVc 252
Cdd:PRK00095  159 FLKSEKTELGHIDDVVNRLALAHPDVAFTLTH---NGK--LVLQTRGAGQLLQRLAAILGREFAENALPI------DAE- 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 253 eeyclsacgtpQSPFRISGFISQ--CThgagRSSTDRQFFFINQRPcdpakV-SRLVN----EVYHMY-NRHQYPFVVLN 324
Cdd:PRK00095  227 -----------HGDLRLSGYVGLptLS----RANRDYQYLFVNGRY-----VrDKLLNhairQAYHDLlPRGRYPAFVLF 286

                         330       340
                  ....*....|....*....|....*..
gi 1958668105 325 VSVDSECVDINVTPDKRQILLQEEKLL 351
Cdd:PRK00095  287 LELDPHQVDVNVHPAKHEVRFRDERLV 313
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 267-359 2.43e-25

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: 100.65  E-value: 2.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 267 FRISGFISQctHGAGRSSTDRQFFFINQRPCDPAKVSRLVNEVYHMY-NRHQYPFVVLNVSVDSECVDINVTPDKRQILL 345
Cdd:pfam01119  22 LRLSGYISK--PTLSRSNRDYQYLFVNGRPVRDKLLSHAIREAYRDLlPKGRYPVAVLFLEIDPELVDVNVHPTKREVRF 99

                          90
                  ....*....|....
gi 1958668105 346 QEEKLLLAVLKTSL 359
Cdd:pfam01119 100 RDEREVYDFIKEAL 113
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 35-169 1.19e-04

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 41.48  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105   35 LSTAVKELIENSVDAGATS--IDLRLKDYGVDL-IEVSDNGCGVEEEnfeglalkhhtskirefaDLTQVETFGFRGEAL 111
Cdd:smart00387   6 LRQVLSNLLDNAIKYTPEGgrITVTLERDGDHVeITVEDNGPGIPPE------------------DLEKIFEPFFRTDKR 67

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958668105  112 SSlcalsdvTISTCHVSASIGTRLVLDHNGKI-IQKTPcprPKGTTVSVqnlfyTLPVR 169
Cdd:smart00387  68 SR-------KIGGTGLGLSIVKKLVELHGGEIsVESEP---GGGTTFTI-----TLPLE 111
 
Name Accession Description Interval E-value
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 13-344 2.08e-140

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: 408.57  E-value: 2.08e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105  13 KAIKPIDGKSVHQICSGQVVLSLSTAVKELIENSVDAGATSIDLRLKDYGVDLIEVSDNGCGVEEENFEGLALKHHTSKI 92
Cdd:TIGR00585   1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105  93 REFADLTQVETFGFRGEALSSLCALSDVTISTCHV-SASIGTRLVLDhNGKIIQKTPCPRPKGTTVSVQNLFYTLPVRHK 171
Cdd:TIGR00585  81 QSFEDLERIETLGFRGEALASISSVSRLTITTKTSaADGLAYQALLE-GGMIESIKPAPRPVGTTVEVRDLFYNLPVRRK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 172 eFQRNIKKEYAKMVQVLQAYCIISAGIRVSCTNqlgQGKRQPVVCTSGSSGMKEN-IGSVFGQKQLQSLVPFVQLPPSDs 250
Cdd:TIGR00585 160 -FLKSPKKEFRKILDVLQRYALIHPDISFSLTH---DGKKVLQLSTKPNQSTKENrIRSVFGTAVLRKLIPLDEWEDLD- 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 251 vceeyclsacgtpqspFRISGFISQCTHGAGRSSTDrQFFFINQRPCDPAKVSRLVNEVYHMYN-RHQYPFVVLNVSVDS 329
Cdd:TIGR00585 235 ----------------LQLEGFISQPNVTRSRRSGW-QFLFINGRPVELKLLLKAIREVYHEYLpKGQYPVFVLNLEIDP 297

                         330
                  ....*....|....*
gi 1958668105 330 ECVDINVTPDKRQIL 344
Cdd:TIGR00585 298 ELVDVNVHPDKKEVR 312
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 22-205 5.85e-93

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: 282.40  E-value: 5.85e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105  22 SVHQICSGQVVLSLSTAVKELIENSVDAGATSIDLRLKDYGVDLIEVSDNGCGVEEENFEGLALKHHTSKIREFADLTQV 101
Cdd:cd16926     1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 102 ETFGFRGEALSSLCALSDVTISTCHVSASIGTRLVLDHNGKIIQKTPCPRPKGTTVSVQNLFYTLPVRHKeFQRNIKKEY 181
Cdd:cd16926    81 TTLGFRGEALASIASVSRLTITTRTADDDVGTRLVVDGGGIIEEVKPAAAPVGTTVTVRDLFYNTPARRK-FLKSPKTEL 159

                         170       180
                  ....*....|....*....|....
gi 1958668105 182 AKMVQVLQAYCIISAGIRVSCTNQ 205
Cdd:cd16926   160 SKILDLVQRLALAHPDVSFSLTHD 183
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
23-359 5.46e-84

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 270.76  E-value: 5.46e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105  23 VHQICSGQVV---LSlstAVKELIENSVDAGATSIDLRLKDYGVDLIEVSDNGCGVEEENFEgLALKHH-TSKIREFADL 98
Cdd:COG0323    12 ANQIAAGEVVerpAS---VVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLP-LAFERHaTSKIRSAEDL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105  99 TQVETFGFRGEALSSLCALSDVTISTCHVSASIGTRLVLDhNGKIIQKTPCPRPKGTTVSVQNLFYTLPVRHKeFQRNIK 178
Cdd:COG0323    88 FRIRTLGFRGEALASIASVSRLTLTTRTAGAELGTRIEVE-GGKVVEVEPAAAPKGTTVEVRDLFFNTPARRK-FLKSDA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 179 KEYAKMVQVLQAYCIISAGIRVSCTNqlgQGKrqPVVCTSGSSGMKENIGSVFGQKQLQSLVPfvqlppsdsVCEEycls 258
Cdd:COG0323   166 TELAHITDVVRRLALAHPDIAFTLIH---NGR--EVFQLPGAGDLLQRIAAIYGREFAENLLP---------VEAE---- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 259 acgtpQSPFRISGFISQCTHgaGRSSTDRQFFFINQRPCDPAKVSRLVNEVYH---MYNRHqyPFVVLNVSVDSECVDIN 335
Cdd:COG0323   228 -----REGLRLSGYIGKPEF--SRSNRDYQYFFVNGRPVRDKLLSHAVREAYRdllPKGRY--PVAVLFLELDPELVDVN 298

                         330       340
                  ....*....|....*....|....
gi 1958668105 336 VTPDKRQILLQEEKLLLAVLKTSL 359
Cdd:COG0323   299 VHPTKTEVRFRDEREVYDLVRSAV 322
mutL PRK00095
DNA mismatch repair endonuclease MutL;
14-351 7.07e-74

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 246.67  E-value: 7.07e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105  14 AIKPIDGKSVHQICSGQVVLSLSTAVKELIENSVDAGATSIDLRLKDYGVDLIEVSDNGCGVEEENFEgLALK-HHTSKI 92
Cdd:PRK00095    2 PIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLA-LALArHATSKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105  93 REFADLTQVETFGFRGEALSSLCALSDVTISTCHVSASIGTRLVlDHNGKIIQKTPCPRPKGTTVSVQNLFYTLPVRHKe 172
Cdd:PRK00095   81 ASLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAEGWQIV-YEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRK- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 173 FQRNIKKEYAKMVQVLQAYCIISAGIRVSCTNqlgQGKrqPVVCTSGSSGMKENIGSVFGQKQLQSLVPFvqlppsDSVc 252
Cdd:PRK00095  159 FLKSEKTELGHIDDVVNRLALAHPDVAFTLTH---NGK--LVLQTRGAGQLLQRLAAILGREFAENALPI------DAE- 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 253 eeyclsacgtpQSPFRISGFISQ--CThgagRSSTDRQFFFINQRPcdpakV-SRLVN----EVYHMY-NRHQYPFVVLN 324
Cdd:PRK00095  227 -----------HGDLRLSGYVGLptLS----RANRDYQYLFVNGRY-----VrDKLLNhairQAYHDLlPRGRYPAFVLF 286

                         330       340
                  ....*....|....*....|....*..
gi 1958668105 325 VSVDSECVDINVTPDKRQILLQEEKLL 351
Cdd:PRK00095  287 LELDPHQVDVNVHPAKHEVRFRDERLV 313
MutL_Trans_hPMS_2_like cd03484
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 223-364 5.40e-67

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: 213.67  E-value: 5.40e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 223 MKENIGSVFGQKQLQSLVPFVQLPPSDSVCEEYcLSACGTPQSPFRISGFISQCTHGAGRSSTDRQFFFINQRPCDPAKV 302
Cdd:cd03484     2 IKDNIINVFGGKVIKGLIPINLELDVNPTKEEL-DSDEDLADSEVKITGYISKPSHGCGRSSSDRQFFYINGRPVDLKKV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958668105 303 SRLVNEVYHMYNRHQYPFVVLNVSVDSECVDINVTPDKRQILLQEEKLLLAVLKTSLMGMFD 364
Cdd:cd03484    81 AKLINEVYKSFNSRQYPFFILNISLPTSLYDVNVTPDKRTVLLHDEDRLIDTLKTSLSELFE 142
MutL_Trans cd00782
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 223-359 6.14e-37

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: 133.05  E-value: 6.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 223 MKENIGSVFGQKQLQSLVPFVQLPPSdsvceeyclsacgtpqspFRISGFISQCTHGagRSSTDRQFFFINQRPCDPAKV 302
Cdd:cd00782     1 LKDRIAQVYGKEVAKNLIEVELESGD------------------FRISGYISKPDFG--RSSKDRQFLFVNGRPVRDKLL 60

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958668105 303 SRLVNEVYHMYN-RHQYPFVVLNVSVDSECVDINVTPDKRQILLQEEKLLLAVLKTSL 359
Cdd:cd00782    61 SKAINEAYRSYLpKGRYPVFVLNLELPPELVDVNVHPTKREVRFSDEEEVLELIREAL 118
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 267-359 2.43e-25

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: 100.65  E-value: 2.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 267 FRISGFISQctHGAGRSSTDRQFFFINQRPCDPAKVSRLVNEVYHMY-NRHQYPFVVLNVSVDSECVDINVTPDKRQILL 345
Cdd:pfam01119  22 LRLSGYISK--PTLSRSNRDYQYLFVNGRPVRDKLLSHAIREAYRDLlPKGRYPVAVLFLEIDPELVDVNVHPTKREVRF 99

                          90
                  ....*....|....
gi 1958668105 346 QEEKLLLAVLKTSL 359
Cdd:pfam01119 100 RDEREVYDFIKEAL 113
TopoII_MutL_Trans cd00329
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 223-344 1.99e-19

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: 83.46  E-value: 1.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 223 MKENIGSVFGQKQLQSLVPFVQLPpsdsvceeyclsacgtpqSPFRISGFISQCTHGagRSSTDRQFFFINQRPCDPAK- 301
Cdd:cd00329     1 LKDRLAEILGDKVADKLIYVEGES------------------DGFRVEGAISYPDSG--RSSKDRQFSFVNGRPVREGGt 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958668105 302 VSRLVNEVYHMY----NRHQYPFVVLNVSVDSECVDINVTPDKRQIL 344
Cdd:cd00329    61 HVKAVREAYTRAlngdDVRRYPVAVLSLKIPPSLVDVNVHPTKEEVR 107
MutL_Trans_hPMS_1_like cd03485
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 262-354 8.43e-12

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: 62.67  E-value: 8.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 262 TPQSPFRISGFISQCTHGAGRSSTDRQFFFINQRPCDPAK-VSRLVNEVYHMYNRH----QYPFVVLNVSVDSECVDINV 336
Cdd:cd03485    25 DEDPQISLEGFLPKPGSDVSKTKSDGKFISVNSRPVSLGKdIGKLLRQYYSSAYRKsslrRYPVFFLNILCPPGLVDVNI 104

                          90
                  ....*....|....*....
gi 1958668105 337 TPDKRQILLQ-EEKLLLAV 354
Cdd:cd03485   105 EPDKDDVLLQnKEAVLQAV 123
MutL_Trans_MLH1 cd03483
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 224-348 5.08e-10

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: 57.24  E-value: 5.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 224 KENIGSVFGQKQLQSLVPFvqlppSDSVCEEYCLsacgtpqspFRISGFISQcthgAGRSSTDRQF-FFINQR--PCDPA 300
Cdd:cd03483     3 KDNIRSVYGAAVANELIEV-----EISDDDDDLG---------FKVKGLISN----ANYSKKKIIFiLFINNRlvECSAL 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958668105 301 KvsRLVNEVYHMY-NRHQYPFVVLNVSVDSECVDINVTPDKRQI--LLQEE 348
Cdd:cd03483    65 R--RAIENVYANYlPKGAHPFVYLSLEIPPENVDVNVHPTKREVhfLNEEE 113
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
 35-161 9.61e-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: 56.96  E-value: 9.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105  35 LSTAVKELIENSVDAGATSIDLRLKDY--GVDLIEVSDNGCGVEEENFEGlALKHHTSKIREFADLTQVETFGFrGEALS 112
Cdd:pfam13589   1 LEGALAELIDNSIDADATNIKIEVNKNrgGGTEIVIEDDGHGMSPEELIN-ALRLATSAKEAKRGSTDLGRYGI-GLKLA 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958668105 113 SLCALSDVTISTCHVSASIGTRLVLD----HNGKIIQKTPcPRPKGTTVSVQN 161
Cdd:pfam13589  79 SLSLGAKLTVTSKKEGKSSTLTLDRDkisnENDWLLPLLT-PAPIENFDELDK 130
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 31-170 6.86e-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: 50.83  E-value: 6.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105  31 VVLSLSTAVKELIENSVD--AGATSIDLRLKDYGVDLIEVSDNGCGVEEENFEGLalkhhtskireFADLTQVETFGFRG 108
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKhaAKAGEITVTLSEGGELTLTVEDNGIGIPPEDLPRI-----------FEPFSTADKRGGGG 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958668105 109 EALSslcalsdvtISTCHvsasigtRLVLDHNGKIiqKTPCPRPKGTTVSVqnlfyTLPVRH 170
Cdd:pfam02518  71 TGLG---------LSIVR-------KLVELLGGTI--TVESEPGGGTTVTL-----TLPLAQ 109
MutL_Trans_MutL cd03482
MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 267-343 1.92e-07

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: 49.89  E-value: 1.92e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958668105 267 FRISGFISQctHGAGRSSTDRQFFFINQRPCDPAKVSRLVNEVYHMYNRHQ-YPFVVLNVSVDSECVDINVTPDKRQI 343
Cdd:cd03482    27 LRLSGWIAL--PTFARSQADIQYFYVNGRMVRDKLISHAVRQAYSDVLHGGrHPAYVLYLELDPAQVDVNVHPAKHEV 102
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 35-169 1.19e-04

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 41.48  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105   35 LSTAVKELIENSVDAGATS--IDLRLKDYGVDL-IEVSDNGCGVEEEnfeglalkhhtskirefaDLTQVETFGFRGEAL 111
Cdd:smart00387   6 LRQVLSNLLDNAIKYTPEGgrITVTLERDGDHVeITVEDNGPGIPPE------------------DLEKIFEPFFRTDKR 67

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958668105  112 SSlcalsdvTISTCHVSASIGTRLVLDHNGKI-IQKTPcprPKGTTVSVqnlfyTLPVR 169
Cdd:smart00387  68 SR-------KIGGTGLGLSIVKKLVELHGGEIsVESEP---GGGTTFTI-----TLPLE 111
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 35-78 5.86e-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: 39.58  E-value: 5.86e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958668105  35 LSTAVKELIENSVDAGATS------IDLRLKDYGVDL-IEVSDNGCGVEEE 78
Cdd:cd16915     1 LITIVGNLIDNALDALAATgapnkqVEVFLRDEGDDLvIEVRDTGPGIAPE 51
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 35-91 1.17e-03

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 41.37  E-value: 1.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958668105  35 LSTAVKELIENSVDAGATS------IDLRLKDYGVDL-IEVSDNGCGVEEENFEGLALKHHTSK 91
Cdd:COG3290   282 LVTILGNLLDNAIEAVEKLpeeerrVELSIRDDGDELvIEVEDSGPGIPEELLEKIFERGFSTK 345
MutL_Trans_MLH3 cd03486
MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 267-355 1.32e-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: 39.22  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668105 267 FRISGFISQCTHGagrsSTDRQFFFINQRPCDPAKVSRLVNEVY---------------HMYNRHQ-----YPFVVLNVS 326
Cdd:cd03486    28 YEVSGYISSEGHY----SKSFQFIYVNGRLYLKTRFHKLINKLFrktsavaknksspqsKSSRRGKrsqesYPVFVLNIT 103

                          90       100
                  ....*....|....*....|....*....
gi 1958668105 327 VDSECVDINVTPDKRQILLQEEKLLLAVL 355
Cdd:cd03486   104 CPASEYDLSQEPSKTIIEFKDWKTLLPLI 132
HATPase_MORC-like cd16931
Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger ...
 38-78 1.55e-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: 38.54  E-value: 1.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958668105  38 AVKELIENSVDAGATS----IDLRLKDYGVDLIEVSDNGCGVEEE 78
Cdd:cd16931    15 AVAELVDNARDADATRldifIDDINLLRGGFMLSFLDDGNGMTPE 59
PRK04184 PRK04184
DNA topoisomerase VI subunit B; Validated
 34-79 3.41e-03

DNA topoisomerase VI subunit B; Validated


Pssm-ID: 235246 [Multi-domain]  Cd Length: 535  Bit Score: 40.26  E-value: 3.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958668105  34 SLSTAVKELIENSVDAGATS-------IDLRLKDYGVDL--IEVSDNGCGVEEEN 79
Cdd:PRK04184   36 ALYTTVKELVDNSLDACEEAgilpdikIEIKRVDEGKDHyrVTVEDNGPGIPPEE 90
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
 18-77 5.06e-03

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 39.82  E-value: 5.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958668105  18 IDGKSVHQICSGQVVLSLSTAVKELIENSVDA------GATSIDLRLKDYGVD-LIEVSDNGCGVEE 77
Cdd:PRK15053  416 VPGSQLSQLPPGLDSTEFAAIVGNLLDNAFEAslrsdeGNKIVELFLSDEGDDvVIEVADQGCGVPE 482
 
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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