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Conserved domains on  [gi|1063727006|ref|NP_001328251|]
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MUTL protein homolog 3 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
mutl super family cl36694
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
2-388 1.10e-89

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]


The actual alignment was detected with superfamily member TIGR00585:

Pssm-ID: 273155 [Multi-domain]  Cd Length: 312  Bit Score: 291.47  E-value: 1.10e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006    2 KTIKPLPEGVRHSMRSGIIMFDMARVVEELVFNSLDAGATKVSIFVGVVSC-SVKVVDDGSGVSRDDLVLLGERYATSKF 80
Cdd:TIGR00585    1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLkLIEVSDNGSGIDKEDLPLACERHATSKI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006   81 HDFTnVETASETFGFRGEALASISDISLLEVRTKAIgRPNGYRKVMKGSKCLHLGIDDDRKDSGTTVTVRDLFYSQPVRR 160
Cdd:TIGR00585   81 QSFE-DLERIETLGFRGEALASISSVSRLTITTKTS-AADGLAYQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  161 KYMqSSPKKVLESIKKCVFRIALVHSNVSFSVLDiesdeelfqtNPSSSAFSLLMRDAGTEAVnslcKVNVTDGMLNVSG 240
Cdd:TIGR00585  159 KFL-KSPKKEFRKILDVLQRYALIHPDISFSLTH----------DGKKVLQLSTKPNQSTKEN----RIRSVFGTAVLRK 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  241 FECADDWKPTDGQQTGrrnrlqsnpgyilciacprrlyeFSFEPSKTHVEFKKWgpvlafieritlanwkkdriLELFDG 320
Cdd:TIGR00585  224 LIPLDEWEDLDLQLEG-----------------------FISQPNVTRSRRSGW--------------------QFLFIN 260
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063727006  321 GADILAKGDRQdliddkiRLQNDWPEAMEPakkklkrsnDHAPCSSLLFPSADFKQDGDYFSPRKDVW 388
Cdd:TIGR00585  261 GRPVELKLLLK-------AIREVYHEYLPK---------GQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
911-1083 1.35e-26

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: 106.28  E-value: 1.35e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006   911 VLQQVDKKYIPIVACGTVAIVDQHAADERIRLEELRTKVLAGKARtvtylsadqelfindaLLIFVLTLKvLPEMGYQLL 990
Cdd:smart00853    1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQAGGLESQ----------------PLLIPVRLE-LSPQEAALL 63
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006   991 QSYSEQIRDWGWIcnitvegstsfkknmsIIQRKPTPITLNAVPCILGvNLSDVDLLEFLQQLADTDGSSTIPPSVLRVL 1070
Cdd:smart00853   64 EEHLELLRQLGFE----------------LEIFGPQSLILRSVPALLR-QQNLQKLIPELLDLLSDEEENARPSRLEALL 126
                           170
                    ....*....|...
gi 1063727006  1071 NSKACRGAIMFGD 1083
Cdd:smart00853  127 ASLACRSAIRAGD 139
 
Name Accession Description Interval E-value
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
2-388 1.10e-89

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: 291.47  E-value: 1.10e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006    2 KTIKPLPEGVRHSMRSGIIMFDMARVVEELVFNSLDAGATKVSIFVGVVSC-SVKVVDDGSGVSRDDLVLLGERYATSKF 80
Cdd:TIGR00585    1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLkLIEVSDNGSGIDKEDLPLACERHATSKI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006   81 HDFTnVETASETFGFRGEALASISDISLLEVRTKAIgRPNGYRKVMKGSKCLHLGIDDDRKDSGTTVTVRDLFYSQPVRR 160
Cdd:TIGR00585   81 QSFE-DLERIETLGFRGEALASISSVSRLTITTKTS-AADGLAYQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  161 KYMqSSPKKVLESIKKCVFRIALVHSNVSFSVLDiesdeelfqtNPSSSAFSLLMRDAGTEAVnslcKVNVTDGMLNVSG 240
Cdd:TIGR00585  159 KFL-KSPKKEFRKILDVLQRYALIHPDISFSLTH----------DGKKVLQLSTKPNQSTKEN----RIRSVFGTAVLRK 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  241 FECADDWKPTDGQQTGrrnrlqsnpgyilciacprrlyeFSFEPSKTHVEFKKWgpvlafieritlanwkkdriLELFDG 320
Cdd:TIGR00585  224 LIPLDEWEDLDLQLEG-----------------------FISQPNVTRSRRSGW--------------------QFLFIN 260
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063727006  321 GADILAKGDRQdliddkiRLQNDWPEAMEPakkklkrsnDHAPCSSLLFPSADFKQDGDYFSPRKDVW 388
Cdd:TIGR00585  261 GRPVELKLLLK-------AIREVYHEYLPK---------GQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
11-192 1.69e-65

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: 219.23  E-value: 1.69e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006   11 VRHSMRSGIIMFDMARVVEELVFNSLDAGATKVSIFV-GVVSCSVKVVDDGSGVSRDDLVLLGERYATSKFHDFTNVETA 89
Cdd:cd16926      1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIeEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006   90 sETFGFRGEALASISDISLLEVRTKAIGRPNGYRKVMKGSKCLHlGIDDDRKDSGTTVTVRDLFYSQPVRRKYMqSSPKK 169
Cdd:cd16926     81 -TTLGFRGEALASIASVSRLTITTRTADDDVGTRLVVDGGGIIE-EVKPAAAPVGTTVTVRDLFYNTPARRKFL-KSPKT 157
                          170       180
                   ....*....|....*....|...
gi 1063727006  170 VLESIKKCVFRIALVHSNVSFSV 192
Cdd:cd16926    158 ELSKILDLVQRLALAHPDVSFSL 180
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
25-241 2.88e-44

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 168.68  E-value: 2.88e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006   25 ARVVEELVFNSLDAGATKVSIFV--GVVScSVKVVDDGSGVSRDDLVLLGERYATSK---FHDFTNVETasetFGFRGEA 99
Cdd:COG0323     25 ASVVKELVENAIDAGATRIEVEIeeGGKS-LIRVTDNGCGMSPEDLPLAFERHATSKirsAEDLFRIRT----LGFRGEA 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  100 LASISDISLLEVRTKAIGRPNGYRKVMKGSKclhlgIDDDRKDS---GTTVTVRDLFYSQPVRRKYMQSSP---KKVLES 173
Cdd:COG0323    100 LASIASVSRLTLTTRTAGAELGTRIEVEGGK-----VVEVEPAAapkGTTVEVRDLFFNTPARRKFLKSDAtelAHITDV 174
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063727006  174 IKkcvfRIALVHSNVSFSVldIESDEELFQTNPSSSafsllMRDA-----GTEAVNSLCKVNVTDGMLNVSGF 241
Cdd:COG0323    175 VR----RLALAHPDIAFTL--IHNGREVFQLPGAGD-----LLQRiaaiyGREFAENLLPVEAEREGLRLSGY 236
mutL PRK00095
DNA mismatch repair endonuclease MutL;
25-261 4.91e-39

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 154.99  E-value: 4.91e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006   25 ARVVEELVFNSLDAGATKVSIFV--GVVScSVKVVDDGSGVSRDDLVLLGERYATSKFHDFTNVETASeTFGFRGEALAS 102
Cdd:PRK00095    24 ASVVKELVENALDAGATRIDIEIeeGGLK-LIRVRDNGCGISKEDLALALARHATSKIASLDDLEAIR-TLGFRGEALPS 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  103 ISDISLLEVRTKAIGRPNGYRKVMKGskclhlGIDDDRKDS----GTTVTVRDLFYSQPVRRKYMQsSPKKVLESIKKCV 178
Cdd:PRK00095   102 IASVSRLTLTSRTADAAEGWQIVYEG------GEIVEVKPAahpvGTTIEVRDLFFNTPARRKFLK-SEKTELGHIDDVV 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  179 FRIALVHSNVSFSVldIESDEELFQTNPSSsafSLLMRDA---GTEAVNSLCKVNVTDGMLNVSGFECaddwKPT----- 250
Cdd:PRK00095   175 NRLALAHPDVAFTL--THNGKLVLQTRGAG---QLLQRLAailGREFAENALPIDAEHGDLRLSGYVG----LPTlsran 245
                          250
                   ....*....|....*..
gi 1063727006  251 -DGQQT---GR--RNRL 261
Cdd:PRK00095   246 rDYQYLfvnGRyvRDKL 262
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
911-1083 1.35e-26

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: 106.28  E-value: 1.35e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006   911 VLQQVDKKYIPIVACGTVAIVDQHAADERIRLEELRTKVLAGKARtvtylsadqelfindaLLIFVLTLKvLPEMGYQLL 990
Cdd:smart00853    1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQAGGLESQ----------------PLLIPVRLE-LSPQEAALL 63
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006   991 QSYSEQIRDWGWIcnitvegstsfkknmsIIQRKPTPITLNAVPCILGvNLSDVDLLEFLQQLADTDGSSTIPPSVLRVL 1070
Cdd:smart00853   64 EEHLELLRQLGFE----------------LEIFGPQSLILRSVPALLR-QQNLQKLIPELLDLLSDEEENARPSRLEALL 126
                           170
                    ....*....|...
gi 1063727006  1071 NSKACRGAIMFGD 1083
Cdd:smart00853  127 ASLACRSAIRAGD 139
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
892-1132 1.78e-20

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 96.65  E-value: 1.78e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  892 SDESLVPESInRHSLEDA---KVLQQVDKKYIpivacgtVA-------IVDQHAADERIRLEELRTKVLAGKARTvtyls 961
Cdd:COG0323    309 RDEREVYDLV-RSAVREAlaqAALGQLHGTYI-------LAenedglvLIDQHAAHERILYERLKKALAEGGVAS----- 375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  962 adQELfindallIFVLTLKvLPEMGYQLLQSYSEQIRDWGwicnITVE--GSTSFKknmsiiqrkptpitLNAVPCILGv 1039
Cdd:COG0323    376 --QPL-------LIPETLE-LSPAEAALLEEHLEELARLG----FEIEpfGPNTVA--------------VRAVPALLG- 426
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006 1040 NLSDVDLL-EFLQQLADTDGSSTIPPSVLRVLNSKACRGAIMFGDSLLPSECSLIIDGLKQTSLCFQCAHGRPTtvpLVD 1118
Cdd:COG0323    427 EGDAEELLrDLLDELAEEGSSESLEELREELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPT---WIE 503
                          250
                   ....*....|....
gi 1063727006 1119 LKalHKQIAKLSGR 1132
Cdd:COG0323    504 LS--LEELEKLFKR 515
mutL PRK00095
DNA mismatch repair endonuclease MutL;
891-1124 3.02e-18

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 90.28  E-value: 3.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  891 RSDESLVPESINRHSLedAKVLQQVDKKYIPIVACGTVAIVDQHAADERIRLEELRTKVLAGKARTvtylsadQELFINd 970
Cdd:PRK00095   415 APEPAEAAEEADSFPL--GYALGQLHGTYILAENEDGLYLVDQHAAHERLLYEQLKDKLAEVGLAS-------QPLLIP- 484
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  971 allifvLTLKvLPEMGYQLLQSYSEQIRDWGwicnITVE--GSTSFkknmsiiqrkptpiTLNAVPCILG-VNLSDVdLL 1047
Cdd:PRK00095   485 ------LVLE-LSEDEADRLEEHKELLARLG----LELEpfGPNSF--------------AVREVPALLGqQELEEL-IR 538
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063727006 1048 EFLQQLADTDGSSTIppSVLRVLNSKACRGAIMFGDSLLPSECSLIIDGLKQTSLCFQCAHGRPTTVPLvDLKALHK 1124
Cdd:PRK00095   539 DLLDELAEEGDSDTL--KERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIEL-SLSDLEK 612
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
912-1085 1.07e-11

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: 63.78  E-value: 1.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  912 LQQVDKKYIPIVACGTVAIVDQHAADERIRLEELRTKVLAGKARTvtylsadQElfindalLIFVLTLKvLPEMGYQLLQ 991
Cdd:pfam08676    4 LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGLAA-------QP-------LLIPLVLE-LSPEEAALLE 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  992 SYSEQIRDWGWicNITVEGSTSFkknmsiiqrkptpiTLNAVPCILG-VNLSDvDLLEFLQQLADtDGSSTIPPSVLRVL 1070
Cdd:pfam08676   69 EHKEELAQLGF--ELEEFGPNSV--------------IVRSVPALLRqQNLQE-LIRELLDELAE-KGGSSLEESLEELL 130
                          170
                   ....*....|....*
gi 1063727006 1071 NSKACRGAIMFGDSL 1085
Cdd:pfam08676  131 ATMACHSAVRAGRRL 145
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
24-123 3.75e-06

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


Pssm-ID: 433332 [Multi-domain]  Cd Length: 135  Bit Score: 47.71  E-value: 3.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006   24 MARVVEELVFNSLDAGATKVSIFV-----GVVSCSVKvvDDGSGVSRDDLVlLGERYATS-KFHDFTnvETASETFGFrG 97
Cdd:pfam13589    1 LEGALAELIDNSIDADATNIKIEVnknrgGGTEIVIE--DDGHGMSPEELI-NALRLATSaKEAKRG--STDLGRYGI-G 74
                           90       100
                   ....*....|....*....|....*.
gi 1063727006   98 EALASISDISLLEVRTKAIGRPNGYR 123
Cdd:pfam13589   75 LKLASLSLGAKLTVTSKKEGKSSTLT 100
 
Name Accession Description Interval E-value
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
2-388 1.10e-89

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: 291.47  E-value: 1.10e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006    2 KTIKPLPEGVRHSMRSGIIMFDMARVVEELVFNSLDAGATKVSIFVGVVSC-SVKVVDDGSGVSRDDLVLLGERYATSKF 80
Cdd:TIGR00585    1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLkLIEVSDNGSGIDKEDLPLACERHATSKI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006   81 HDFTnVETASETFGFRGEALASISDISLLEVRTKAIgRPNGYRKVMKGSKCLHLGIDDDRKDSGTTVTVRDLFYSQPVRR 160
Cdd:TIGR00585   81 QSFE-DLERIETLGFRGEALASISSVSRLTITTKTS-AADGLAYQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  161 KYMqSSPKKVLESIKKCVFRIALVHSNVSFSVLDiesdeelfqtNPSSSAFSLLMRDAGTEAVnslcKVNVTDGMLNVSG 240
Cdd:TIGR00585  159 KFL-KSPKKEFRKILDVLQRYALIHPDISFSLTH----------DGKKVLQLSTKPNQSTKEN----RIRSVFGTAVLRK 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  241 FECADDWKPTDGQQTGrrnrlqsnpgyilciacprrlyeFSFEPSKTHVEFKKWgpvlafieritlanwkkdriLELFDG 320
Cdd:TIGR00585  224 LIPLDEWEDLDLQLEG-----------------------FISQPNVTRSRRSGW--------------------QFLFIN 260
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063727006  321 GADILAKGDRQdliddkiRLQNDWPEAMEPakkklkrsnDHAPCSSLLFPSADFKQDGDYFSPRKDVW 388
Cdd:TIGR00585  261 GRPVELKLLLK-------AIREVYHEYLPK---------GQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
11-192 1.69e-65

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: 219.23  E-value: 1.69e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006   11 VRHSMRSGIIMFDMARVVEELVFNSLDAGATKVSIFV-GVVSCSVKVVDDGSGVSRDDLVLLGERYATSKFHDFTNVETA 89
Cdd:cd16926      1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIeEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006   90 sETFGFRGEALASISDISLLEVRTKAIGRPNGYRKVMKGSKCLHlGIDDDRKDSGTTVTVRDLFYSQPVRRKYMqSSPKK 169
Cdd:cd16926     81 -TTLGFRGEALASIASVSRLTITTRTADDDVGTRLVVDGGGIIE-EVKPAAAPVGTTVTVRDLFYNTPARRKFL-KSPKT 157
                          170       180
                   ....*....|....*....|...
gi 1063727006  170 VLESIKKCVFRIALVHSNVSFSV 192
Cdd:cd16926    158 ELSKILDLVQRLALAHPDVSFSL 180
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
25-241 2.88e-44

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 168.68  E-value: 2.88e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006   25 ARVVEELVFNSLDAGATKVSIFV--GVVScSVKVVDDGSGVSRDDLVLLGERYATSK---FHDFTNVETasetFGFRGEA 99
Cdd:COG0323     25 ASVVKELVENAIDAGATRIEVEIeeGGKS-LIRVTDNGCGMSPEDLPLAFERHATSKirsAEDLFRIRT----LGFRGEA 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  100 LASISDISLLEVRTKAIGRPNGYRKVMKGSKclhlgIDDDRKDS---GTTVTVRDLFYSQPVRRKYMQSSP---KKVLES 173
Cdd:COG0323    100 LASIASVSRLTLTTRTAGAELGTRIEVEGGK-----VVEVEPAAapkGTTVEVRDLFFNTPARRKFLKSDAtelAHITDV 174
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063727006  174 IKkcvfRIALVHSNVSFSVldIESDEELFQTNPSSSafsllMRDA-----GTEAVNSLCKVNVTDGMLNVSGF 241
Cdd:COG0323    175 VR----RLALAHPDIAFTL--IHNGREVFQLPGAGD-----LLQRiaaiyGREFAENLLPVEAEREGLRLSGY 236
mutL PRK00095
DNA mismatch repair endonuclease MutL;
25-261 4.91e-39

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 154.99  E-value: 4.91e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006   25 ARVVEELVFNSLDAGATKVSIFV--GVVScSVKVVDDGSGVSRDDLVLLGERYATSKFHDFTNVETASeTFGFRGEALAS 102
Cdd:PRK00095    24 ASVVKELVENALDAGATRIDIEIeeGGLK-LIRVRDNGCGISKEDLALALARHATSKIASLDDLEAIR-TLGFRGEALPS 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  103 ISDISLLEVRTKAIGRPNGYRKVMKGskclhlGIDDDRKDS----GTTVTVRDLFYSQPVRRKYMQsSPKKVLESIKKCV 178
Cdd:PRK00095   102 IASVSRLTLTSRTADAAEGWQIVYEG------GEIVEVKPAahpvGTTIEVRDLFFNTPARRKFLK-SEKTELGHIDDVV 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  179 FRIALVHSNVSFSVldIESDEELFQTNPSSsafSLLMRDA---GTEAVNSLCKVNVTDGMLNVSGFECaddwKPT----- 250
Cdd:PRK00095   175 NRLALAHPDVAFTL--THNGKLVLQTRGAG---QLLQRLAailGREFAENALPIDAEHGDLRLSGYVG----LPTlsran 245
                          250
                   ....*....|....*..
gi 1063727006  251 -DGQQT---GR--RNRL 261
Cdd:PRK00095   246 rDYQYLfvnGRyvRDKL 262
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
911-1083 1.35e-26

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: 106.28  E-value: 1.35e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006   911 VLQQVDKKYIPIVACGTVAIVDQHAADERIRLEELRTKVLAGKARtvtylsadqelfindaLLIFVLTLKvLPEMGYQLL 990
Cdd:smart00853    1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQAGGLESQ----------------PLLIPVRLE-LSPQEAALL 63
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006   991 QSYSEQIRDWGWIcnitvegstsfkknmsIIQRKPTPITLNAVPCILGvNLSDVDLLEFLQQLADTDGSSTIPPSVLRVL 1070
Cdd:smart00853   64 EEHLELLRQLGFE----------------LEIFGPQSLILRSVPALLR-QQNLQKLIPELLDLLSDEEENARPSRLEALL 126
                           170
                    ....*....|...
gi 1063727006  1071 NSKACRGAIMFGD 1083
Cdd:smart00853  127 ASLACRSAIRAGD 139
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
892-1132 1.78e-20

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 96.65  E-value: 1.78e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  892 SDESLVPESInRHSLEDA---KVLQQVDKKYIpivacgtVA-------IVDQHAADERIRLEELRTKVLAGKARTvtyls 961
Cdd:COG0323    309 RDEREVYDLV-RSAVREAlaqAALGQLHGTYI-------LAenedglvLIDQHAAHERILYERLKKALAEGGVAS----- 375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  962 adQELfindallIFVLTLKvLPEMGYQLLQSYSEQIRDWGwicnITVE--GSTSFKknmsiiqrkptpitLNAVPCILGv 1039
Cdd:COG0323    376 --QPL-------LIPETLE-LSPAEAALLEEHLEELARLG----FEIEpfGPNTVA--------------VRAVPALLG- 426
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006 1040 NLSDVDLL-EFLQQLADTDGSSTIPPSVLRVLNSKACRGAIMFGDSLLPSECSLIIDGLKQTSLCFQCAHGRPTtvpLVD 1118
Cdd:COG0323    427 EGDAEELLrDLLDELAEEGSSESLEELREELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPT---WIE 503
                          250
                   ....*....|....
gi 1063727006 1119 LKalHKQIAKLSGR 1132
Cdd:COG0323    504 LS--LEELEKLFKR 515
mutL PRK00095
DNA mismatch repair endonuclease MutL;
891-1124 3.02e-18

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 90.28  E-value: 3.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  891 RSDESLVPESINRHSLedAKVLQQVDKKYIPIVACGTVAIVDQHAADERIRLEELRTKVLAGKARTvtylsadQELFINd 970
Cdd:PRK00095   415 APEPAEAAEEADSFPL--GYALGQLHGTYILAENEDGLYLVDQHAAHERLLYEQLKDKLAEVGLAS-------QPLLIP- 484
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  971 allifvLTLKvLPEMGYQLLQSYSEQIRDWGwicnITVE--GSTSFkknmsiiqrkptpiTLNAVPCILG-VNLSDVdLL 1047
Cdd:PRK00095   485 ------LVLE-LSEDEADRLEEHKELLARLG----LELEpfGPNSF--------------AVREVPALLGqQELEEL-IR 538
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063727006 1048 EFLQQLADTDGSSTIppSVLRVLNSKACRGAIMFGDSLLPSECSLIIDGLKQTSLCFQCAHGRPTTVPLvDLKALHK 1124
Cdd:PRK00095   539 DLLDELAEEGDSDTL--KERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIEL-SLSDLEK 612
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
912-1085 1.07e-11

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: 63.78  E-value: 1.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  912 LQQVDKKYIPIVACGTVAIVDQHAADERIRLEELRTKVLAGKARTvtylsadQElfindalLIFVLTLKvLPEMGYQLLQ 991
Cdd:pfam08676    4 LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGLAA-------QP-------LLIPLVLE-LSPEEAALLE 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006  992 SYSEQIRDWGWicNITVEGSTSFkknmsiiqrkptpiTLNAVPCILG-VNLSDvDLLEFLQQLADtDGSSTIPPSVLRVL 1070
Cdd:pfam08676   69 EHKEELAQLGF--ELEEFGPNSV--------------IVRSVPALLRqQNLQE-LIRELLDELAE-KGGSSLEESLEELL 130
                          170
                   ....*....|....*
gi 1063727006 1071 NSKACRGAIMFGDSL 1085
Cdd:pfam08676  131 ATMACHSAVRAGRRL 145
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
24-123 3.75e-06

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


Pssm-ID: 433332 [Multi-domain]  Cd Length: 135  Bit Score: 47.71  E-value: 3.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727006   24 MARVVEELVFNSLDAGATKVSIFV-----GVVSCSVKvvDDGSGVSRDDLVlLGERYATS-KFHDFTnvETASETFGFrG 97
Cdd:pfam13589    1 LEGALAELIDNSIDADATNIKIEVnknrgGGTEIVIE--DDGHGMSPEELI-NALRLATSaKEAKRG--STDLGRYGI-G 74
                           90       100
                   ....*....|....*....|....*.
gi 1063727006   98 EALASISDISLLEVRTKAIGRPNGYR 123
Cdd:pfam13589   75 LKLASLSLGAKLTVTSKKEGKSSTLT 100
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
26-94 3.71e-05

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: 43.90  E-value: 3.71e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063727006   26 RVVEELVFNSLDAGATKVSIFVGVVS---CSVKVVDDGSGVSRDDLVLLGERYATSKFHD-------FTNVETASETFG 94
Cdd:pfam02518    8 QVLSNLLDNALKHAAKAGEITVTLSEggeLTLTVEDNGIGIPPEDLPRIFEPFSTADKRGgggtglgLSIVRKLVELLG 86
MutL_Trans_MLH3 cd03486
MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
248-302 1.40e-04

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: 43.07  E-value: 1.40e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1063727006  248 KPTDGQQTGRRNRLQSNPGYILCIACPRRLYEFSFEPSKTHVEFKKWGPVLAFIE 302
Cdd:cd03486     79 SPQSKSSRRGKRSQESYPVFVLNITCPASEYDLSQEPSKTIIEFKDWKTLLPLIL 133
 
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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