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Conserved domains on  [gi|6325093|ref|NP_015161|]
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mismatch repair protein MLH3 [Saccharomyces cerevisiae S288C]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
12-213 4.36e-61

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: 203.05  E-value: 4.36e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   12 VSERLKSQACTVSLASAVREIVQNSVDAHATTIDVMIDLPNL-SFAVYDDGIGLTRSDLNILATQNYTSKIRKMNDLVTM 90
Cdd:cd16926   1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLkLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   91 KTYGYRGDALYSISNVSNLFVCSKKKDYNSAWMRKFPsksvmlsENTILPidpfwkICPWSRTKSGTVVIVEDMLYNLPV 170
Cdd:cd16926  81 TTLGFRGEALASIASVSRLTITTRTADDDVGTRLVVD-------GGGIIE------EVKPAAAPVGTTVTVRDLFYNTPA 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 6325093  171 RRRILKeePPFKTFNTIKADMLQILVMHPMISLNVQYTDKLRI 213
Cdd:cd16926 148 RRKFLK--SPKTELSKILDLVQRLALAHPDVSFSLTHDGKLVL 188
mutL super family cl35064
DNA mismatch repair endonuclease MutL;
24-713 2.39e-47

DNA mismatch repair endonuclease MutL;


The actual alignment was detected with superfamily member PRK00095:

Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 177.33  E-value: 2.39e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093    24 SLASAVREIVQNSVDAHATTIDVMIDLPNLSF-AVYDDGIGLTRSDLNILATQNYTSKIRKMNDLVTMKTYGYRGDALYS 102
Cdd:PRK00095  22 RPASVVKELVENALDAGATRIDIEIEEGGLKLiRVRDNGCGISKEDLALALARHATSKIASLDDLEAIRTLGFRGEALPS 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   103 ISNVSNLFVCSKKKDYNSAWmrkfpskSVMLSENTILPIDPfwkiCPWSRtksGTVVIVEDMLYNLPVRRRILKEEppfK 182
Cdd:PRK00095 102 IASVSRLTLTSRTADAAEGW-------QIVYEGGEIVEVKP----AAHPV---GTTIEVRDLFFNTPARRKFLKSE---K 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   183 T-FNTIkADMLQILVM-HPMISLNVQYTDKLRINTevlfrskniteglTKHQQMSQVLRNVFGAIIPPDMLkKVSLKFNE 260
Cdd:PRK00095 165 TeLGHI-DDVVNRLALaHPDVAFTLTHNGKLVLQT-------------RGAGQLLQRLAAILGREFAENAL-PIDAEHGD 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   261 YQIEGIISKmPV---GLKDLQFIYINGRryadsafqgYVDS--LFQA--QDFGekgmSLLktkSVGKpyrsHPVFILDVr 333
Cdd:PRK00095 230 LRLSGYVGL-PTlsrANRDYQYLFVNGR---------YVRDklLNHAirQAYH----DLL---PRGR----YPAFVLFL- 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   334 cpqTIDDLLQD----PAKKIVKPSHIRTIEPLIVKTIRSFLTFQGYLTPDKSDSSFeivncsqktaTLPDSRIQISKRNQ 409
Cdd:PRK00095 288 ---ELDPHQVDvnvhPAKHEVRFRDERLVHDLIVQAIQEALAQSGLIPAAAGANQV----------LEPAEPEPLPLQQT 354
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   410 VLNSkmkiARINSYIGKPAVNGCRINNSTINYEKIKNIRIDGQKSRLRNKLSSRPYDSGFTEDYDSIGKTITDFSISRSV 489
Cdd:PRK00095 355 PLYA----SGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSEAAAAASAEAAAAAPAAAPEPAEAAEEADSFPL 430
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   490 LAkyeVINQVDKKFILIRCLDQsihncplLVLVDQHACDERIRLEELFYS----------LLTEVVtgtfvardlkdccI 559
Cdd:PRK00095 431 GY---ALGQLHGTYILAENEDG-------LYLVDQHAAHERLLYEQLKDKlaevglasqpLLIPLV-------------L 487
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   560 EVDRTEADLFKHYQSEFKKWGIgyeTIEGTMETSLLeIKTLPEMLtskynGDKDYLKMV--LLQHAHDLKDFKklpmdls 637
Cdd:PRK00095 488 ELSEDEADRLEEHKELLARLGL---ELEPFGPNSFA-VREVPALL-----GQQELEELIrdLLDELAEEGDSD------- 551
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325093   638 hfenytsvdklywwkysscvPTVFHEILNSKACRSAVMFGDELTRQECIILISKLSRCHNPFECAHGRPSMVPIAE 713
Cdd:PRK00095 552 --------------------TLKERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIELSL 607
 
Name Accession Description Interval E-value
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
12-213 4.36e-61

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: 203.05  E-value: 4.36e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   12 VSERLKSQACTVSLASAVREIVQNSVDAHATTIDVMIDLPNL-SFAVYDDGIGLTRSDLNILATQNYTSKIRKMNDLVTM 90
Cdd:cd16926   1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLkLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   91 KTYGYRGDALYSISNVSNLFVCSKKKDYNSAWMRKFPsksvmlsENTILPidpfwkICPWSRTKSGTVVIVEDMLYNLPV 170
Cdd:cd16926  81 TTLGFRGEALASIASVSRLTITTRTADDDVGTRLVVD-------GGGIIE------EVKPAAAPVGTTVTVRDLFYNTPA 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 6325093  171 RRRILKeePPFKTFNTIKADMLQILVMHPMISLNVQYTDKLRI 213
Cdd:cd16926 148 RRKFLK--SPKTELSKILDLVQRLALAHPDVSFSLTHDGKLVL 188
mutL PRK00095
DNA mismatch repair endonuclease MutL;
24-713 2.39e-47

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 177.33  E-value: 2.39e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093    24 SLASAVREIVQNSVDAHATTIDVMIDLPNLSF-AVYDDGIGLTRSDLNILATQNYTSKIRKMNDLVTMKTYGYRGDALYS 102
Cdd:PRK00095  22 RPASVVKELVENALDAGATRIDIEIEEGGLKLiRVRDNGCGISKEDLALALARHATSKIASLDDLEAIRTLGFRGEALPS 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   103 ISNVSNLFVCSKKKDYNSAWmrkfpskSVMLSENTILPIDPfwkiCPWSRtksGTVVIVEDMLYNLPVRRRILKEEppfK 182
Cdd:PRK00095 102 IASVSRLTLTSRTADAAEGW-------QIVYEGGEIVEVKP----AAHPV---GTTIEVRDLFFNTPARRKFLKSE---K 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   183 T-FNTIkADMLQILVM-HPMISLNVQYTDKLRINTevlfrskniteglTKHQQMSQVLRNVFGAIIPPDMLkKVSLKFNE 260
Cdd:PRK00095 165 TeLGHI-DDVVNRLALaHPDVAFTLTHNGKLVLQT-------------RGAGQLLQRLAAILGREFAENAL-PIDAEHGD 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   261 YQIEGIISKmPV---GLKDLQFIYINGRryadsafqgYVDS--LFQA--QDFGekgmSLLktkSVGKpyrsHPVFILDVr 333
Cdd:PRK00095 230 LRLSGYVGL-PTlsrANRDYQYLFVNGR---------YVRDklLNHAirQAYH----DLL---PRGR----YPAFVLFL- 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   334 cpqTIDDLLQD----PAKKIVKPSHIRTIEPLIVKTIRSFLTFQGYLTPDKSDSSFeivncsqktaTLPDSRIQISKRNQ 409
Cdd:PRK00095 288 ---ELDPHQVDvnvhPAKHEVRFRDERLVHDLIVQAIQEALAQSGLIPAAAGANQV----------LEPAEPEPLPLQQT 354
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   410 VLNSkmkiARINSYIGKPAVNGCRINNSTINYEKIKNIRIDGQKSRLRNKLSSRPYDSGFTEDYDSIGKTITDFSISRSV 489
Cdd:PRK00095 355 PLYA----SGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSEAAAAASAEAAAAAPAAAPEPAEAAEEADSFPL 430
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   490 LAkyeVINQVDKKFILIRCLDQsihncplLVLVDQHACDERIRLEELFYS----------LLTEVVtgtfvardlkdccI 559
Cdd:PRK00095 431 GY---ALGQLHGTYILAENEDG-------LYLVDQHAAHERLLYEQLKDKlaevglasqpLLIPLV-------------L 487
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   560 EVDRTEADLFKHYQSEFKKWGIgyeTIEGTMETSLLeIKTLPEMLtskynGDKDYLKMV--LLQHAHDLKDFKklpmdls 637
Cdd:PRK00095 488 ELSEDEADRLEEHKELLARLGL---ELEPFGPNSFA-VREVPALL-----GQQELEELIrdLLDELAEEGDSD------- 551
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325093   638 hfenytsvdklywwkysscvPTVFHEILNSKACRSAVMFGDELTRQECIILISKLSRCHNPFECAHGRPSMVPIAE 713
Cdd:PRK00095 552 --------------------TLKERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIELSL 607
MutL_Trans_MLH3 cd03486
MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
233-371 7.98e-47

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: 162.49  E-value: 7.98e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093  233 QMSQVLRNVFGAIIPpDMLKKVSLKFNEYQIEGIISKMPVGLKDLQFIYINGRRYADSAFQGYVDSLFQAQDFGEKGMSL 312
Cdd:cd03486   1 SILSVFKQIYGLVLA-QKLKEVSAKFQEYEVSGYISSEGHYSKSFQFIYVNGRLYLKTRFHKLINKLFRKTSAVAKNKSS 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325093  313 LKTKS---VGKPYRSHPVFILDVRCPQTIDDLLQDPAKKIVKPSHIRTIEPLIVKTIRSFLT 371
Cdd:cd03486  80 PQSKSsrrGKRSQESYPVFVLNITCPASEYDLSQEPSKTIIEFKDWKTLLPLILEVVKSFLK 141
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
26-709 1.96e-44

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 167.14  E-value: 1.96e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   26 ASAVREIVQNSVDAHATTIDV--------MIdlpnlsfAVYDDGIGLTRSDLnILATQNY-TSKIRKMNDLVTMKTYGYR 96
Cdd:COG0323  25 ASVVKELVENAIDAGATRIEVeieeggksLI-------RVTDNGCGMSPEDL-PLAFERHaTSKIRSAEDLFRIRTLGFR 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   97 GDALYSISNVSNLFVCSKKKDYNSAWmrkfpskSVMLSENTILPIDPfwkiCPWSRtksGTVVIVEDMLYNLPVRRRILK 176
Cdd:COG0323  97 GEALASIASVSRLTLTTRTAGAELGT-------RIEVEGGKVVEVEP----AAAPK---GTTVEVRDLFFNTPARRKFLK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093  177 EEppfKT-FNTIkADMLQILVM-HPMISLnvqytdKLRINTEVLFRsknitegLTKHQQMSQVLRNVFGAIIPPDMLkKV 254
Cdd:COG0323 163 SD---ATeLAHI-TDVVRRLALaHPDIAF------TLIHNGREVFQ-------LPGAGDLLQRIAAIYGREFAENLL-PV 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093  255 SLKFNEYQIEGIISKmPV---GLKDLQFIYINGR----RYADSA-FQGYVDSLfqaqdfgekgmsllktksvgkPYRSHP 326
Cdd:COG0323 225 EAEREGLRLSGYIGK-PEfsrSNRDYQYFFVNGRpvrdKLLSHAvREAYRDLL---------------------PKGRYP 282
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093  327 VFILDVRC-PQTIddllqD----PAKKIVKPSHIRTIEPLIVKTIRSFLTfqgyltpdksdssfeivncsqktatlpdsr 401
Cdd:COG0323 283 VAVLFLELdPELV-----DvnvhPTKTEVRFRDEREVYDLVRSAVREALA------------------------------ 327
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093  402 iqiskrnqvlnskmkiariNSYIGkpavngcrinnstinyekikniridgqksrlrnklssrpydsgftedydsigktit 481
Cdd:COG0323 328 -------------------QAALG-------------------------------------------------------- 332
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093  482 dfsisrsvlakyevinQVDKKFILIrcldQSIHNcplLVLVDQHACDERIRLEELFYS----------LLTEVVtgtfva 551
Cdd:COG0323 333 ----------------QLHGTYILA----ENEDG---LVLIDQHAAHERILYERLKKAlaeggvasqpLLIPET------ 383
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093  552 rdlkdccIEVDRTEADLFKHYQSEFKKWGIGYETIEGTMetslLEIKTLPEMLtskynGDKDYLKMVllqhaHDLKDfkk 631
Cdd:COG0323 384 -------LELSPAEAALLEEHLEELARLGFEIEPFGPNT----VAVRAVPALL-----GEGDAEELL-----RDLLD--- 439
                       650       660       670       680       690       700       710
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6325093  632 lpmDLSHFENYTSVDKLywwkysscvptvFHEILNSKACRSAVMFGDELTRQECIILISKLSRCHNPFECAHGRPSMV 709
Cdd:COG0323 440 ---ELAEEGSSESLEEL------------REELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTWI 502
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
4-350 3.93e-37

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: 141.24  E-value: 3.93e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093      4 HIRKLDSDVSERLKSQACTVSLASAVREIVQNSVDAHATTIDvmIDLPNLSFA---VYDDGIGLTRSDLNILATQNYTSK 80
Cdd:TIGR00585   2 TIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRID--VEIEEGGLKlieVSDNGSGIDKEDLPLACERHATSK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093     81 IRKMNDLVTMKTYGYRGDALYSISNVSNLFVCSK-KKDYNSAWMRKFPSKsvmlsenTILPIDPfwkicpwSRTKSGTVV 159
Cdd:TIGR00585  80 IQSFEDLERIETLGFRGEALASISSVSRLTITTKtSAADGLAYQALLEGG-------MIESIKP-------APRPVGTTV 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093    160 IVEDMLYNLPVRRRILKEEPpfKTFNTIKADMLQILVMHPMISLNVqytdkLRINTEVLFRSKNITEGLTKhqqmsQVLR 239
Cdd:TIGR00585 146 EVRDLFYNLPVRRKFLKSPK--KEFRKILDVLQRYALIHPDISFSL-----THDGKKVLQLSTKPNQSTKE-----NRIR 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093    240 NVFGAIIPPDMLKKVSLKFNEYQIEGIISKMPVG---LKDLQFIYINGRRYADsafqgyvDSLFQAQDFGEKGMSllktk 316
Cdd:TIGR00585 214 SVFGTAVLRKLIPLDEWEDLDLQLEGFISQPNVTrsrRSGWQFLFINGRPVEL-------KLLLKAIREVYHEYL----- 281
                         330       340       350
                  ....*....|....*....|....*....|....
gi 6325093    317 svgkPYRSHPVFILDVRCPQTIDDLLQDPAKKIV 350
Cdd:TIGR00585 282 ----PKGQYPVFVLNLEIDPELVDVNVHPDKKEV 311
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
495-678 1.60e-22

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: 93.96  E-value: 1.60e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093     495 VINQVDKKFILIRCLDQsihncplLVLVDQHACDERIRLEELFYS--------LLTEVVtgtfvardlkdccIEVDRTEA 566
Cdd:smart00853   1 ALGQVAGTYILAEREDG-------LYLLDQHAAHERILYEQLLKQagglesqpLLIPVR-------------LELSPQEA 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093     567 DLFKHYQSEFKKWGIGYETIEGTmetsLLEIKTLPEMLtskyngdKDYLKMVLLQHAHDLKDFKKLPMDLShfenytsvd 646
Cdd:smart00853  61 ALLEEHLELLRQLGFELEIFGPQ----SLILRSVPALL-------RQQNLQKLIPELLDLLSDEEENARPS--------- 120
                          170       180       190
                   ....*....|....*....|....*....|..
gi 6325093     647 klywwkysscvptVFHEILNSKACRSAVMFGD 678
Cdd:smart00853 121 -------------RLEALLASLACRSAIRAGD 139
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
25-157 8.90e-07

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: 48.87  E-value: 8.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093     25 LASAVREIVQNSVDAHATTIDVMID---LPNLSFAVYDDGIGLTRSDLN---ILATQNYTSKiRKMNDLvtmKTYGyRGD 98
Cdd:pfam13589   1 LEGALAELIDNSIDADATNIKIEVNknrGGGTEIVIEDDGHGMSPEELInalRLATSAKEAK-RGSTDL---GRYG-IGL 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6325093     99 ALYSISNVSNLFVCSKKKDYNSA--WMRKFPSKSvmlSENTILPIDPFWKICPWSRTK--SGT 157
Cdd:pfam13589  76 KLASLSLGAKLTVTSKKEGKSSTltLDRDKISNE---NDWLLPLLTPAPIENFDELDKdaHGT 135
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
498-680 5.96e-05

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: 43.75  E-value: 5.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093    498 QVDKKFILIRCLDQsihncplLVLVDQHACDERIRLEELFYS----------LLTEVVtgtfvardlkdccIEVDRTEAD 567
Cdd:pfam08676   6 QVHGTYILAENEDG-------LYLIDQHAAHERILYEKLKRAlaegglaaqpLLIPLV-------------LELSPEEAA 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093    568 LFKHYQSEFKKWGIGYETIEGTMetslLEIKTLPEMLtSKYNGDKDYLKMVllqhaHDLKDFKKLPMDLSHfenytsvdk 647
Cdd:pfam08676  66 LLEEHKEELAQLGFELEEFGPNS----VIVRSVPALL-RQQNLQELIRELL-----DELAEKGGSSLEESL--------- 126
                         170       180       190
                  ....*....|....*....|....*....|...
gi 6325093    648 lywwkysscvptvfHEILNSKACRSAVMFGDEL 680
Cdd:pfam08676 127 --------------EELLATMACHSAVRAGRRL 145
 
Name Accession Description Interval E-value
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
12-213 4.36e-61

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: 203.05  E-value: 4.36e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   12 VSERLKSQACTVSLASAVREIVQNSVDAHATTIDVMIDLPNL-SFAVYDDGIGLTRSDLNILATQNYTSKIRKMNDLVTM 90
Cdd:cd16926   1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLkLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   91 KTYGYRGDALYSISNVSNLFVCSKKKDYNSAWMRKFPsksvmlsENTILPidpfwkICPWSRTKSGTVVIVEDMLYNLPV 170
Cdd:cd16926  81 TTLGFRGEALASIASVSRLTITTRTADDDVGTRLVVD-------GGGIIE------EVKPAAAPVGTTVTVRDLFYNTPA 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 6325093  171 RRRILKeePPFKTFNTIKADMLQILVMHPMISLNVQYTDKLRI 213
Cdd:cd16926 148 RRKFLK--SPKTELSKILDLVQRLALAHPDVSFSLTHDGKLVL 188
mutL PRK00095
DNA mismatch repair endonuclease MutL;
24-713 2.39e-47

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 177.33  E-value: 2.39e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093    24 SLASAVREIVQNSVDAHATTIDVMIDLPNLSF-AVYDDGIGLTRSDLNILATQNYTSKIRKMNDLVTMKTYGYRGDALYS 102
Cdd:PRK00095  22 RPASVVKELVENALDAGATRIDIEIEEGGLKLiRVRDNGCGISKEDLALALARHATSKIASLDDLEAIRTLGFRGEALPS 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   103 ISNVSNLFVCSKKKDYNSAWmrkfpskSVMLSENTILPIDPfwkiCPWSRtksGTVVIVEDMLYNLPVRRRILKEEppfK 182
Cdd:PRK00095 102 IASVSRLTLTSRTADAAEGW-------QIVYEGGEIVEVKP----AAHPV---GTTIEVRDLFFNTPARRKFLKSE---K 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   183 T-FNTIkADMLQILVM-HPMISLNVQYTDKLRINTevlfrskniteglTKHQQMSQVLRNVFGAIIPPDMLkKVSLKFNE 260
Cdd:PRK00095 165 TeLGHI-DDVVNRLALaHPDVAFTLTHNGKLVLQT-------------RGAGQLLQRLAAILGREFAENAL-PIDAEHGD 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   261 YQIEGIISKmPV---GLKDLQFIYINGRryadsafqgYVDS--LFQA--QDFGekgmSLLktkSVGKpyrsHPVFILDVr 333
Cdd:PRK00095 230 LRLSGYVGL-PTlsrANRDYQYLFVNGR---------YVRDklLNHAirQAYH----DLL---PRGR----YPAFVLFL- 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   334 cpqTIDDLLQD----PAKKIVKPSHIRTIEPLIVKTIRSFLTFQGYLTPDKSDSSFeivncsqktaTLPDSRIQISKRNQ 409
Cdd:PRK00095 288 ---ELDPHQVDvnvhPAKHEVRFRDERLVHDLIVQAIQEALAQSGLIPAAAGANQV----------LEPAEPEPLPLQQT 354
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   410 VLNSkmkiARINSYIGKPAVNGCRINNSTINYEKIKNIRIDGQKSRLRNKLSSRPYDSGFTEDYDSIGKTITDFSISRSV 489
Cdd:PRK00095 355 PLYA----SGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSEAAAAASAEAAAAAPAAAPEPAEAAEEADSFPL 430
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   490 LAkyeVINQVDKKFILIRCLDQsihncplLVLVDQHACDERIRLEELFYS----------LLTEVVtgtfvardlkdccI 559
Cdd:PRK00095 431 GY---ALGQLHGTYILAENEDG-------LYLVDQHAAHERLLYEQLKDKlaevglasqpLLIPLV-------------L 487
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   560 EVDRTEADLFKHYQSEFKKWGIgyeTIEGTMETSLLeIKTLPEMLtskynGDKDYLKMV--LLQHAHDLKDFKklpmdls 637
Cdd:PRK00095 488 ELSEDEADRLEEHKELLARLGL---ELEPFGPNSFA-VREVPALL-----GQQELEELIrdLLDELAEEGDSD------- 551
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325093   638 hfenytsvdklywwkysscvPTVFHEILNSKACRSAVMFGDELTRQECIILISKLSRCHNPFECAHGRPSMVPIAE 713
Cdd:PRK00095 552 --------------------TLKERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIELSL 607
MutL_Trans_MLH3 cd03486
MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
233-371 7.98e-47

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: 162.49  E-value: 7.98e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093  233 QMSQVLRNVFGAIIPpDMLKKVSLKFNEYQIEGIISKMPVGLKDLQFIYINGRRYADSAFQGYVDSLFQAQDFGEKGMSL 312
Cdd:cd03486   1 SILSVFKQIYGLVLA-QKLKEVSAKFQEYEVSGYISSEGHYSKSFQFIYVNGRLYLKTRFHKLINKLFRKTSAVAKNKSS 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325093  313 LKTKS---VGKPYRSHPVFILDVRCPQTIDDLLQDPAKKIVKPSHIRTIEPLIVKTIRSFLT 371
Cdd:cd03486  80 PQSKSsrrGKRSQESYPVFVLNITCPASEYDLSQEPSKTIIEFKDWKTLLPLILEVVKSFLK 141
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
26-709 1.96e-44

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 167.14  E-value: 1.96e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   26 ASAVREIVQNSVDAHATTIDV--------MIdlpnlsfAVYDDGIGLTRSDLnILATQNY-TSKIRKMNDLVTMKTYGYR 96
Cdd:COG0323  25 ASVVKELVENAIDAGATRIEVeieeggksLI-------RVTDNGCGMSPEDL-PLAFERHaTSKIRSAEDLFRIRTLGFR 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   97 GDALYSISNVSNLFVCSKKKDYNSAWmrkfpskSVMLSENTILPIDPfwkiCPWSRtksGTVVIVEDMLYNLPVRRRILK 176
Cdd:COG0323  97 GEALASIASVSRLTLTTRTAGAELGT-------RIEVEGGKVVEVEP----AAAPK---GTTVEVRDLFFNTPARRKFLK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093  177 EEppfKT-FNTIkADMLQILVM-HPMISLnvqytdKLRINTEVLFRsknitegLTKHQQMSQVLRNVFGAIIPPDMLkKV 254
Cdd:COG0323 163 SD---ATeLAHI-TDVVRRLALaHPDIAF------TLIHNGREVFQ-------LPGAGDLLQRIAAIYGREFAENLL-PV 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093  255 SLKFNEYQIEGIISKmPV---GLKDLQFIYINGR----RYADSA-FQGYVDSLfqaqdfgekgmsllktksvgkPYRSHP 326
Cdd:COG0323 225 EAEREGLRLSGYIGK-PEfsrSNRDYQYFFVNGRpvrdKLLSHAvREAYRDLL---------------------PKGRYP 282
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093  327 VFILDVRC-PQTIddllqD----PAKKIVKPSHIRTIEPLIVKTIRSFLTfqgyltpdksdssfeivncsqktatlpdsr 401
Cdd:COG0323 283 VAVLFLELdPELV-----DvnvhPTKTEVRFRDEREVYDLVRSAVREALA------------------------------ 327
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093  402 iqiskrnqvlnskmkiariNSYIGkpavngcrinnstinyekikniridgqksrlrnklssrpydsgftedydsigktit 481
Cdd:COG0323 328 -------------------QAALG-------------------------------------------------------- 332
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093  482 dfsisrsvlakyevinQVDKKFILIrcldQSIHNcplLVLVDQHACDERIRLEELFYS----------LLTEVVtgtfva 551
Cdd:COG0323 333 ----------------QLHGTYILA----ENEDG---LVLIDQHAAHERILYERLKKAlaeggvasqpLLIPET------ 383
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093  552 rdlkdccIEVDRTEADLFKHYQSEFKKWGIGYETIEGTMetslLEIKTLPEMLtskynGDKDYLKMVllqhaHDLKDfkk 631
Cdd:COG0323 384 -------LELSPAEAALLEEHLEELARLGFEIEPFGPNT----VAVRAVPALL-----GEGDAEELL-----RDLLD--- 439
                       650       660       670       680       690       700       710
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6325093  632 lpmDLSHFENYTSVDKLywwkysscvptvFHEILNSKACRSAVMFGDELTRQECIILISKLSRCHNPFECAHGRPSMV 709
Cdd:COG0323 440 ---ELAEEGSSESLEEL------------REELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTWI 502
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
4-350 3.93e-37

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: 141.24  E-value: 3.93e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093      4 HIRKLDSDVSERLKSQACTVSLASAVREIVQNSVDAHATTIDvmIDLPNLSFA---VYDDGIGLTRSDLNILATQNYTSK 80
Cdd:TIGR00585   2 TIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRID--VEIEEGGLKlieVSDNGSGIDKEDLPLACERHATSK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093     81 IRKMNDLVTMKTYGYRGDALYSISNVSNLFVCSK-KKDYNSAWMRKFPSKsvmlsenTILPIDPfwkicpwSRTKSGTVV 159
Cdd:TIGR00585  80 IQSFEDLERIETLGFRGEALASISSVSRLTITTKtSAADGLAYQALLEGG-------MIESIKP-------APRPVGTTV 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093    160 IVEDMLYNLPVRRRILKEEPpfKTFNTIKADMLQILVMHPMISLNVqytdkLRINTEVLFRSKNITEGLTKhqqmsQVLR 239
Cdd:TIGR00585 146 EVRDLFYNLPVRRKFLKSPK--KEFRKILDVLQRYALIHPDISFSL-----THDGKKVLQLSTKPNQSTKE-----NRIR 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093    240 NVFGAIIPPDMLKKVSLKFNEYQIEGIISKMPVG---LKDLQFIYINGRRYADsafqgyvDSLFQAQDFGEKGMSllktk 316
Cdd:TIGR00585 214 SVFGTAVLRKLIPLDEWEDLDLQLEGFISQPNVTrsrRSGWQFLFINGRPVEL-------KLLLKAIREVYHEYL----- 281
                         330       340       350
                  ....*....|....*....|....*....|....
gi 6325093    317 svgkPYRSHPVFILDVRCPQTIDDLLQDPAKKIV 350
Cdd:TIGR00585 282 ----PKGQYPVFVLNLEIDPELVDVNVHPDKKEV 311
MutL_Trans cd00782
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
234-370 5.13e-23

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: 94.53  E-value: 5.13e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093  234 MSQVLRNVFGAIIPPDMLKkVSLKFNEYQIEGIISKMPVGL--KDLQFIYINGRRYADSAFQGYVDSLFQaqdfgekgmS 311
Cdd:cd00782   1 LKDRIAQVYGKEVAKNLIE-VELESGDFRISGYISKPDFGRssKDRQFLFVNGRPVRDKLLSKAINEAYR---------S 70
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6325093  312 LLktksvgkPYRSHPVFILDVRCPQTIDDLLQDPAKKIVKPSHIRTIEPLIVKTIRSFL 370
Cdd:cd00782  71 YL-------PKGRYPVFVLNLELPPELVDVNVHPTKREVRFSDEEEVLELIREALRSAL 122
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
495-678 1.60e-22

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: 93.96  E-value: 1.60e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093     495 VINQVDKKFILIRCLDQsihncplLVLVDQHACDERIRLEELFYS--------LLTEVVtgtfvardlkdccIEVDRTEA 566
Cdd:smart00853   1 ALGQVAGTYILAEREDG-------LYLLDQHAAHERILYEQLLKQagglesqpLLIPVR-------------LELSPQEA 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093     567 DLFKHYQSEFKKWGIGYETIEGTmetsLLEIKTLPEMLtskyngdKDYLKMVLLQHAHDLKDFKKLPMDLShfenytsvd 646
Cdd:smart00853  61 ALLEEHLELLRQLGFELEIFGPQ----SLILRSVPALL-------RQQNLQKLIPELLDLLSDEEENARPS--------- 120
                          170       180       190
                   ....*....|....*....|....*....|..
gi 6325093     647 klywwkysscvptVFHEILNSKACRSAVMFGD 678
Cdd:smart00853 121 -------------RLEALLASLACRSAIRAGD 139
TopoII_MutL_Trans cd00329
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
234-351 6.23e-10

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: 56.89  E-value: 6.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093  234 MSQVLRNVFGAIIPPDMLKkVSLKFNEYQIEGIISKMPVGL--KDLQFIYINGRR-YADSAFQGYVDSLFQaqdfgekgm 310
Cdd:cd00329   1 LKDRLAEILGDKVADKLIY-VEGESDGFRVEGAISYPDSGRssKDRQFSFVNGRPvREGGTHVKAVREAYT--------- 70
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 6325093  311 sllkTKSVGKPYRSHPVFILDVRCPQTIDDLLQDPAKKIVK 351
Cdd:cd00329  71 ----RALNGDDVRRYPVAVLSLKIPPSLVDVNVHPTKEEVR 107
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
25-157 8.90e-07

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: 48.87  E-value: 8.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093     25 LASAVREIVQNSVDAHATTIDVMID---LPNLSFAVYDDGIGLTRSDLN---ILATQNYTSKiRKMNDLvtmKTYGyRGD 98
Cdd:pfam13589   1 LEGALAELIDNSIDADATNIKIEVNknrGGGTEIVIEDDGHGMSPEELInalRLATSAKEAK-RGSTDL---GRYG-IGL 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6325093     99 ALYSISNVSNLFVCSKKKDYNSA--WMRKFPSKSvmlSENTILPIDPFWKICPWSRTK--SGT 157
Cdd:pfam13589  76 KLASLSLGAKLTVTSKKEGKSSTltLDRDKISNE---NDWLLPLLTPAPIENFDELDKdaHGT 135
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
498-680 5.96e-05

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: 43.75  E-value: 5.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093    498 QVDKKFILIRCLDQsihncplLVLVDQHACDERIRLEELFYS----------LLTEVVtgtfvardlkdccIEVDRTEAD 567
Cdd:pfam08676   6 QVHGTYILAENEDG-------LYLIDQHAAHERILYEKLKRAlaegglaaqpLLIPLV-------------LELSPEEAA 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093    568 LFKHYQSEFKKWGIGYETIEGTMetslLEIKTLPEMLtSKYNGDKDYLKMVllqhaHDLKDFKKLPMDLSHfenytsvdk 647
Cdd:pfam08676  66 LLEEHKEELAQLGFELEEFGPNS----VIVRSVPALL-RQQNLQELIRELL-----DELAEKGGSSLEESL--------- 126
                         170       180       190
                  ....*....|....*....|....*....|...
gi 6325093    648 lywwkysscvptvfHEILNSKACRSAVMFGDEL 680
Cdd:pfam08676 127 --------------EELLATMACHSAVRAGRRL 145
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
25-84 1.10e-04

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: 41.97  E-value: 1.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6325093     25 LASAVREIVQNSVD--AHATTIDVMIDLPN-LSFAVYDDGIGLTRSDLNILATQNYTSKIRKM 84
Cdd:pfam02518   6 LRQVLSNLLDNALKhaAKAGEITVTLSEGGeLTLTVEDNGIGIPPEDLPRIFEPFSTADKRGG 68
HATPase_MORC-like cd16931
Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger ...
16-69 3.67e-03

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


Pssm-ID: 340408 [Multi-domain]  Cd Length: 118  Bit Score: 37.77  E-value: 3.67e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325093   16 LKSQACTVSLA-SAVREIVQNSVDAHATTIDVMIDLPNLS-----FAVYDDGIGLTRSDL 69
Cdd:cd16931   2 LHSNSTTHSWPfGAVAELVDNARDADATRLDIFIDDINLLrggfmLSFLDDGNGMTPEEA 61
MutL_Trans_hPMS_2_like cd03484
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
249-285 8.92e-03

MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to human PSM2 (hPSM2). hPSM2 belongs to the DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. Included in this group are proteins similar to yeast PMS1. The yeast MLH1-PMS1 and the human MLH1-PMS2 heterodimers play a role in meiosis. hMLH1-hPMS2 also participates in the repair of all DNA mismatch repair (MMR) substrates. Cells lacking hPMS2 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hPMS2 causes predisposition to HPNCC and Turcot syndrome.


Pssm-ID: 239566 [Multi-domain]  Cd Length: 142  Bit Score: 37.25  E-value: 8.92e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 6325093  249 DMLKKVSLKFNEYQIEGIISKMPVGL----KDLQFIYINGR 285
Cdd:cd03484  33 ELDSDEDLADSEVKITGYISKPSHGCgrssSDRQFFYINGR 73
 
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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