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Conserved domains on  [gi|1015172289|ref|NP_001308935|]
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mismatch repair endonuclease PMS2 isoform c [Homo sapiens]

Protein Classification

MutL and HATPase_MutL-MLH-PMS-like domain-containing protein( domain architecture ID 12851550)

MutL and HATPase_MutL-MLH-PMS-like domain-containing protein

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 ...
13-332 4.49e-134

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: 400.86  E-value: 4.49e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  13 KAIKPIDRKSVHQICSGQVVLSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSDNGCGVEEENFEGLTLKHHTSKI 92
Cdd:TIGR00585   1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  93 QEFADLTQVETFGFRGEALSSLCALSDVTISTCH-ASAKVGTRLMFDhNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRHK 171
Cdd:TIGR00585  81 QSFEDLERIETLGFRGEALASISSVSRLTITTKTsAADGLAYQALLE-GGMIESIKPAPRPVGTTVEVRDLFYNLPVRRK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 172 eFQRNIKKEYAKMVQVLHAYCIISAGIRVSCTNqlgQGKRQPVVCTGGSPSIKEN-IGSVFGQKQLQSLIPFVQLPPSDs 250
Cdd:TIGR00585 160 -FLKSPKKEFRKILDVLQRYALIHPDISFSLTH---DGKKVLQLSTKPNQSTKENrIRSVFGTAVLRKLIPLDEWEDLD- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 251 vceeyglscsdalhnlFYISGFISQCTHGVGRSSTDrQFFFINRRPCDPAKVCRLVNEVYHMYN-RHQYPFVVLNISVDS 329
Cdd:TIGR00585 235 ----------------LQLEGFISQPNVTRSRRSGW-QFLFINGRPVELKLLLKAIREVYHEYLpKGQYPVFVLNLEIDP 297

                  ...
gi 1015172289 330 GNL 332
Cdd:TIGR00585 298 ELV 300
mutL super family cl35064
DNA mismatch repair endonuclease MutL;
14-801 3.02e-70

DNA mismatch repair endonuclease MutL;


The actual alignment was detected with superfamily member PRK00095:

Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 242.81  E-value: 3.02e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  14 AIKPIDRKSVHQICSGQVVLSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSDNGCGVEEENfegLTL---KHHTS 90
Cdd:PRK00095    2 PIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKED---LALalaRHATS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  91 KIQEFADLTQVETFGFRGEALSSLCALSDVTISTCHASAKVGTRLMFdHNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRH 170
Cdd:PRK00095   79 KIASLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAEGWQIVY-EGGEIVEVKPAAHPVGTTIEVRDLFFNTPARR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 171 KeFQRNIKKEYAKMVQVLHAYCIISAGIRVSCTNqlgQGKrqPVVCTGGSPSIKENIGSVFGQKQLQSLIPFvqlppsds 250
Cdd:PRK00095  158 K-FLKSEKTELGHIDDVVNRLALAHPDVAFTLTH---NGK--LVLQTRGAGQLLQRLAAILGREFAENALPI-------- 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 251 vceeyglscsDALHNLFYISGFISQ--CThgvgRSSTDRQFFFINRRPcdpakV-CRLVN----EVYHMY-NRHQYPFVV 322
Cdd:PRK00095  224 ----------DAEHGDLRLSGYVGLptLS----RANRDYQYLFVNGRY-----VrDKLLNhairQAYHDLlPRGRYPAFV 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 323 LNISVDsgnlikmhaadlekpmvekqdqsPSLrtgeekKDVSisrlreafslRHTTenkphspKTpEPRRSPLGQKRGML 402
Cdd:PRK00095  285 LFLELD-----------------------PHQ------VDVN----------VHPA-------KH-EVRFRDERLVHDLI 317
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 403 ssstSGAISDkgVLRpQKEAVSSSHGPSDPTDRAEVEKDSGHGSTSVDSEGFSIPDTGSHCSSEYAASSPGDRGSQEHVD 482
Cdd:PRK00095  318 ----VQAIQE--ALA-QSGLIPAAAGANQVLEPAEPEPLPLQQTPLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPL 390
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 483 SQEKAPKTDDSFSDVDCHSNQEDTgckfrvlpqptnlatpntkrfkkeeilsssdicqklvntqdmsasqvdvavkinkk 562
Cdd:PRK00095  391 QPNASQSEAAAAASAEAAAAAPAA-------------------------------------------------------- 414
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 563 vvpldfsmsslakrikQLHHEAQQSEGEQnyrkfrakicpgenqaaedelrkeisktmFAEMEIIGQFNLGFIITKLNED 642
Cdd:PRK00095  415 ----------------APEPAEAAEEADS-----------------------------FPLGYALGQLHGTYILAENEDG 449
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 643 IFIVDQHATDEKYNFEMLQQH---TVLQGQRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDF-VIDENApVTERakliSL 718
Cdd:PRK00095  450 LYLVDQHAAHERLLYEQLKDKlaeVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLELePFGPNS-FAVR----EV 524
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 719 PTsknWtFGPQDVDELIF----MLSDSPGVmcRPSRVKQMFASRACRKSVMIGTALNTSEMKKLITHMGEMDHPWNCPHG 794
Cdd:PRK00095  525 PA---L-LGQQELEELIRdlldELAEEGDS--DTLKERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHG 598

                  ....*..
gi 1015172289 795 RPTMRHI 801
Cdd:PRK00095  599 RPTYIEL 605
 
Name Accession Description Interval E-value
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
13-332 4.49e-134

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: 400.86  E-value: 4.49e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  13 KAIKPIDRKSVHQICSGQVVLSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSDNGCGVEEENFEGLTLKHHTSKI 92
Cdd:TIGR00585   1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  93 QEFADLTQVETFGFRGEALSSLCALSDVTISTCH-ASAKVGTRLMFDhNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRHK 171
Cdd:TIGR00585  81 QSFEDLERIETLGFRGEALASISSVSRLTITTKTsAADGLAYQALLE-GGMIESIKPAPRPVGTTVEVRDLFYNLPVRRK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 172 eFQRNIKKEYAKMVQVLHAYCIISAGIRVSCTNqlgQGKRQPVVCTGGSPSIKEN-IGSVFGQKQLQSLIPFVQLPPSDs 250
Cdd:TIGR00585 160 -FLKSPKKEFRKILDVLQRYALIHPDISFSLTH---DGKKVLQLSTKPNQSTKENrIRSVFGTAVLRKLIPLDEWEDLD- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 251 vceeyglscsdalhnlFYISGFISQCTHGVGRSSTDrQFFFINRRPCDPAKVCRLVNEVYHMYN-RHQYPFVVLNISVDS 329
Cdd:TIGR00585 235 ----------------LQLEGFISQPNVTRSRRSGW-QFLFINGRPVELKLLLKAIREVYHEYLpKGQYPVFVLNLEIDP 297

                  ...
gi 1015172289 330 GNL 332
Cdd:TIGR00585 298 ELV 300
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
22-205 5.50e-89

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: 278.55  E-value: 5.50e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  22 SVHQICSGQVVLSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSDNGCGVEEENFEGLTLKHHTSKIQEFADLTQV 101
Cdd:cd16926     1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 102 ETFGFRGEALSSLCALSDVTISTCHASAKVGTRLMFDHNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRHKeFQRNIKKEY 181
Cdd:cd16926    81 TTLGFRGEALASIASVSRLTITTRTADDDVGTRLVVDGGGIIEEVKPAAAPVGTTVTVRDLFYNTPARRK-FLKSPKTEL 159
                         170       180
                  ....*....|....*....|....
gi 1015172289 182 AKMVQVLHAYCIISAGIRVSCTNQ 205
Cdd:cd16926   160 SKILDLVQRLALAHPDVSFSLTHD 183
mutL PRK00095
DNA mismatch repair endonuclease MutL;
14-801 3.02e-70

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 242.81  E-value: 3.02e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  14 AIKPIDRKSVHQICSGQVVLSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSDNGCGVEEENfegLTL---KHHTS 90
Cdd:PRK00095    2 PIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKED---LALalaRHATS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  91 KIQEFADLTQVETFGFRGEALSSLCALSDVTISTCHASAKVGTRLMFdHNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRH 170
Cdd:PRK00095   79 KIASLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAEGWQIVY-EGGEIVEVKPAAHPVGTTIEVRDLFFNTPARR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 171 KeFQRNIKKEYAKMVQVLHAYCIISAGIRVSCTNqlgQGKrqPVVCTGGSPSIKENIGSVFGQKQLQSLIPFvqlppsds 250
Cdd:PRK00095  158 K-FLKSEKTELGHIDDVVNRLALAHPDVAFTLTH---NGK--LVLQTRGAGQLLQRLAAILGREFAENALPI-------- 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 251 vceeyglscsDALHNLFYISGFISQ--CThgvgRSSTDRQFFFINRRPcdpakV-CRLVN----EVYHMY-NRHQYPFVV 322
Cdd:PRK00095  224 ----------DAEHGDLRLSGYVGLptLS----RANRDYQYLFVNGRY-----VrDKLLNhairQAYHDLlPRGRYPAFV 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 323 LNISVDsgnlikmhaadlekpmvekqdqsPSLrtgeekKDVSisrlreafslRHTTenkphspKTpEPRRSPLGQKRGML 402
Cdd:PRK00095  285 LFLELD-----------------------PHQ------VDVN----------VHPA-------KH-EVRFRDERLVHDLI 317
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 403 ssstSGAISDkgVLRpQKEAVSSSHGPSDPTDRAEVEKDSGHGSTSVDSEGFSIPDTGSHCSSEYAASSPGDRGSQEHVD 482
Cdd:PRK00095  318 ----VQAIQE--ALA-QSGLIPAAAGANQVLEPAEPEPLPLQQTPLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPL 390
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 483 SQEKAPKTDDSFSDVDCHSNQEDTgckfrvlpqptnlatpntkrfkkeeilsssdicqklvntqdmsasqvdvavkinkk 562
Cdd:PRK00095  391 QPNASQSEAAAAASAEAAAAAPAA-------------------------------------------------------- 414
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 563 vvpldfsmsslakrikQLHHEAQQSEGEQnyrkfrakicpgenqaaedelrkeisktmFAEMEIIGQFNLGFIITKLNED 642
Cdd:PRK00095  415 ----------------APEPAEAAEEADS-----------------------------FPLGYALGQLHGTYILAENEDG 449
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 643 IFIVDQHATDEKYNFEMLQQH---TVLQGQRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDF-VIDENApVTERakliSL 718
Cdd:PRK00095  450 LYLVDQHAAHERLLYEQLKDKlaeVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLELePFGPNS-FAVR----EV 524
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 719 PTsknWtFGPQDVDELIF----MLSDSPGVmcRPSRVKQMFASRACRKSVMIGTALNTSEMKKLITHMGEMDHPWNCPHG 794
Cdd:PRK00095  525 PA---L-LGQQELEELIRdlldELAEEGDS--DTLKERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHG 598

                  ....*..
gi 1015172289 795 RPTMRHI 801
Cdd:PRK00095  599 RPTYIEL 605
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
23-328 1.59e-66

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 229.93  E-value: 1.59e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  23 VHQICSGQVV---LSlstAVKELVENSLDAGATNIDLKLKDYGVDLIEVSDNGCGVEEENFEgLTLKHH-TSKIQEFADL 98
Cdd:COG0323    12 ANQIAAGEVVerpAS---VVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLP-LAFERHaTSKIRSAEDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  99 TQVETFGFRGEALSSLCALSDVTISTCHASAKVGTRLMFDhNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRHKeFQRNIK 178
Cdd:COG0323    88 FRIRTLGFRGEALASIASVSRLTLTTRTAGAELGTRIEVE-GGKVVEVEPAAAPKGTTVEVRDLFFNTPARRK-FLKSDA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 179 KEYAKMVQVLHAYCIISAGIRVSCTNqlgQGKrqPVVCTGGSPSIKENIGSVFGQKQLQSLIPFvqlppsdsvceeygls 258
Cdd:COG0323   166 TELAHITDVVRRLALAHPDIAFTLIH---NGR--EVFQLPGAGDLLQRIAAIYGREFAENLLPV---------------- 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1015172289 259 csDALHNLFYISGFISQCThgVGRSSTDRQFFFINRRPCDPAKVCRLVNEVYH---MYNRHqyPFVVLNISVD 328
Cdd:COG0323   225 --EAEREGLRLSGYIGKPE--FSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRdllPKGRY--PVAVLFLELD 291
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
626-769 1.17e-37

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: 137.49  E-value: 1.17e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  626 IIGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQHTV-LQGQRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDFVID 704
Cdd:smart00853   1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQAGgLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELEIF 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1015172289  705 ENAPVTerakLISLPTSKNWTFGPQDVDELIFMLSDSPGVMCrPSRVKQMFASRACRKSVMIGTA 769
Cdd:smart00853  81 GPQSLI----LRSVPALLRQQNLQKLIPELLDLLSDEEENAR-PSRLEALLASLACRSAIRAGDA 140
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
627-770 2.18e-29

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: 113.85  E-value: 2.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 627 IGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQHTVLQG---QRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDFvi 703
Cdd:pfam08676   4 LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGlaaQPLLIPLVLELSPEEAALLEEHKEELAQLGFEL-- 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1015172289 704 deNAPVTERAKLISLPTSKNWTFGPQDVDELIFMLSDSPGVMCrPSRVKQMFASRACRKSVMIGTAL 770
Cdd:pfam08676  82 --EEFGPNSVIVRSVPALLRQQNLQELIRELLDELAEKGGSSL-EESLEELLATMACHSAVRAGRRL 145
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
625-801 1.26e-26

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 114.76  E-value: 1.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 625 EIIGQFNLGFIITKLNEDIFIVDQHATDEKYNFE-MLQQHTV--LQGQRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDF 701
Cdd:COG0323   329 AALGQLHGTYILAENEDGLVLIDQHAAHERILYErLKKALAEggVASQPLLIPETLELSPAEAALLEEHLEELARLGFEI 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 702 videnAPVTERAKLI-SLPTSknwtFGPQDVDELIF----MLSDSPGVMCRPSRVKQMFASRACRKSVMIGTALNTSEMK 776
Cdd:COG0323   409 -----EPFGPNTVAVrAVPAL----LGEGDAEELLRdlldELAEEGSSESLEELREELLATMACHGAIKAGRRLSLEEMN 479
                         170       180
                  ....*....|....*....|....*
gi 1015172289 777 KLITHMGEMDHPWNCPHGRPTMRHI 801
Cdd:COG0323   480 ALLRDLEATENPYTCPHGRPTWIEL 504
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
229-332 3.06e-12

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: 64.06  E-value: 3.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 229 SVFGQKQLQSLIPFvqlppsdsvceeyglscsDALHNLFYISGFISQctHGVGRSSTDRQFFFINRRPCDPAKVCRLVNE 308
Cdd:pfam01119   2 AIYGKEFAENLLPI------------------EKEDDGLRLSGYISK--PTLSRSNRDYQYLFVNGRPVRDKLLSHAIRE 61
                          90       100
                  ....*....|....*....|....*
gi 1015172289 309 VYHMY-NRHQYPFVVLNISVDSGNL 332
Cdd:pfam01119  62 AYRDLlPKGRYPVAVLFLEIDPELV 86
PRK04184 PRK04184
DNA topoisomerase VI subunit B; Validated
34-79 2.47e-04

DNA topoisomerase VI subunit B; Validated


Pssm-ID: 235246 [Multi-domain]  Cd Length: 535  Bit Score: 44.50  E-value: 2.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1015172289  34 SLSTAVKELVENSLDAGATN-------IDLKLKDYGVDL--IEVSDNGCGVEEEN 79
Cdd:PRK04184   36 ALYTTVKELVDNSLDACEEAgilpdikIEIKRVDEGKDHyrVTVEDNGPGIPPEE 90
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
35-95 1.36e-03

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 39.17  E-value: 1.36e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1015172289   35 LSTAVKELVENSLDAGATN--IDLKLKDYGVDL-IEVSDNGCGVEEEN----FE-GLTLKHHTSKIQEF 95
Cdd:smart00387   6 LRQVLSNLLDNAIKYTPEGgrITVTLERDGDHVeITVEDNGPGIPPEDlekiFEpFFRTDKRSRKIGGT 74
 
Name Accession Description Interval E-value
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
13-332 4.49e-134

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: 400.86  E-value: 4.49e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  13 KAIKPIDRKSVHQICSGQVVLSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSDNGCGVEEENFEGLTLKHHTSKI 92
Cdd:TIGR00585   1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  93 QEFADLTQVETFGFRGEALSSLCALSDVTISTCH-ASAKVGTRLMFDhNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRHK 171
Cdd:TIGR00585  81 QSFEDLERIETLGFRGEALASISSVSRLTITTKTsAADGLAYQALLE-GGMIESIKPAPRPVGTTVEVRDLFYNLPVRRK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 172 eFQRNIKKEYAKMVQVLHAYCIISAGIRVSCTNqlgQGKRQPVVCTGGSPSIKEN-IGSVFGQKQLQSLIPFVQLPPSDs 250
Cdd:TIGR00585 160 -FLKSPKKEFRKILDVLQRYALIHPDISFSLTH---DGKKVLQLSTKPNQSTKENrIRSVFGTAVLRKLIPLDEWEDLD- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 251 vceeyglscsdalhnlFYISGFISQCTHGVGRSSTDrQFFFINRRPCDPAKVCRLVNEVYHMYN-RHQYPFVVLNISVDS 329
Cdd:TIGR00585 235 ----------------LQLEGFISQPNVTRSRRSGW-QFLFINGRPVELKLLLKAIREVYHEYLpKGQYPVFVLNLEIDP 297

                  ...
gi 1015172289 330 GNL 332
Cdd:TIGR00585 298 ELV 300
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
22-205 5.50e-89

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: 278.55  E-value: 5.50e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  22 SVHQICSGQVVLSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSDNGCGVEEENFEGLTLKHHTSKIQEFADLTQV 101
Cdd:cd16926     1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 102 ETFGFRGEALSSLCALSDVTISTCHASAKVGTRLMFDHNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRHKeFQRNIKKEY 181
Cdd:cd16926    81 TTLGFRGEALASIASVSRLTITTRTADDDVGTRLVVDGGGIIEEVKPAAAPVGTTVTVRDLFYNTPARRK-FLKSPKTEL 159
                         170       180
                  ....*....|....*....|....
gi 1015172289 182 AKMVQVLHAYCIISAGIRVSCTNQ 205
Cdd:cd16926   160 SKILDLVQRLALAHPDVSFSLTHD 183
mutL PRK00095
DNA mismatch repair endonuclease MutL;
14-801 3.02e-70

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 242.81  E-value: 3.02e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  14 AIKPIDRKSVHQICSGQVVLSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSDNGCGVEEENfegLTL---KHHTS 90
Cdd:PRK00095    2 PIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKED---LALalaRHATS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  91 KIQEFADLTQVETFGFRGEALSSLCALSDVTISTCHASAKVGTRLMFdHNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRH 170
Cdd:PRK00095   79 KIASLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAEGWQIVY-EGGEIVEVKPAAHPVGTTIEVRDLFFNTPARR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 171 KeFQRNIKKEYAKMVQVLHAYCIISAGIRVSCTNqlgQGKrqPVVCTGGSPSIKENIGSVFGQKQLQSLIPFvqlppsds 250
Cdd:PRK00095  158 K-FLKSEKTELGHIDDVVNRLALAHPDVAFTLTH---NGK--LVLQTRGAGQLLQRLAAILGREFAENALPI-------- 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 251 vceeyglscsDALHNLFYISGFISQ--CThgvgRSSTDRQFFFINRRPcdpakV-CRLVN----EVYHMY-NRHQYPFVV 322
Cdd:PRK00095  224 ----------DAEHGDLRLSGYVGLptLS----RANRDYQYLFVNGRY-----VrDKLLNhairQAYHDLlPRGRYPAFV 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 323 LNISVDsgnlikmhaadlekpmvekqdqsPSLrtgeekKDVSisrlreafslRHTTenkphspKTpEPRRSPLGQKRGML 402
Cdd:PRK00095  285 LFLELD-----------------------PHQ------VDVN----------VHPA-------KH-EVRFRDERLVHDLI 317
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 403 ssstSGAISDkgVLRpQKEAVSSSHGPSDPTDRAEVEKDSGHGSTSVDSEGFSIPDTGSHCSSEYAASSPGDRGSQEHVD 482
Cdd:PRK00095  318 ----VQAIQE--ALA-QSGLIPAAAGANQVLEPAEPEPLPLQQTPLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPL 390
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 483 SQEKAPKTDDSFSDVDCHSNQEDTgckfrvlpqptnlatpntkrfkkeeilsssdicqklvntqdmsasqvdvavkinkk 562
Cdd:PRK00095  391 QPNASQSEAAAAASAEAAAAAPAA-------------------------------------------------------- 414
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 563 vvpldfsmsslakrikQLHHEAQQSEGEQnyrkfrakicpgenqaaedelrkeisktmFAEMEIIGQFNLGFIITKLNED 642
Cdd:PRK00095  415 ----------------APEPAEAAEEADS-----------------------------FPLGYALGQLHGTYILAENEDG 449
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 643 IFIVDQHATDEKYNFEMLQQH---TVLQGQRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDF-VIDENApVTERakliSL 718
Cdd:PRK00095  450 LYLVDQHAAHERLLYEQLKDKlaeVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLELePFGPNS-FAVR----EV 524
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 719 PTsknWtFGPQDVDELIF----MLSDSPGVmcRPSRVKQMFASRACRKSVMIGTALNTSEMKKLITHMGEMDHPWNCPHG 794
Cdd:PRK00095  525 PA---L-LGQQELEELIRdlldELAEEGDS--DTLKERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHG 598

                  ....*..
gi 1015172289 795 RPTMRHI 801
Cdd:PRK00095  599 RPTYIEL 605
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
23-328 1.59e-66

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 229.93  E-value: 1.59e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  23 VHQICSGQVV---LSlstAVKELVENSLDAGATNIDLKLKDYGVDLIEVSDNGCGVEEENFEgLTLKHH-TSKIQEFADL 98
Cdd:COG0323    12 ANQIAAGEVVerpAS---VVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLP-LAFERHaTSKIRSAEDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  99 TQVETFGFRGEALSSLCALSDVTISTCHASAKVGTRLMFDhNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRHKeFQRNIK 178
Cdd:COG0323    88 FRIRTLGFRGEALASIASVSRLTLTTRTAGAELGTRIEVE-GGKVVEVEPAAAPKGTTVEVRDLFFNTPARRK-FLKSDA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 179 KEYAKMVQVLHAYCIISAGIRVSCTNqlgQGKrqPVVCTGGSPSIKENIGSVFGQKQLQSLIPFvqlppsdsvceeygls 258
Cdd:COG0323   166 TELAHITDVVRRLALAHPDIAFTLIH---NGR--EVFQLPGAGDLLQRIAAIYGREFAENLLPV---------------- 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1015172289 259 csDALHNLFYISGFISQCThgVGRSSTDRQFFFINRRPCDPAKVCRLVNEVYH---MYNRHqyPFVVLNISVD 328
Cdd:COG0323   225 --EAEREGLRLSGYIGKPE--FSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRdllPKGRY--PVAVLFLELD 291
MutL_Trans_hPMS_2_like cd03484
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
222-332 2.18e-46

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: 162.05  E-value: 2.18e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 222 SIKENIGSVFGQKQLQSLIPFVQLPPSDSVCEEYgLSCSDALHNLFYISGFISQCTHGVGRSSTDRQFFFINRRPCDPAK 301
Cdd:cd03484     1 DIKDNIINVFGGKVIKGLIPINLELDVNPTKEEL-DSDEDLADSEVKITGYISKPSHGCGRSSSDRQFFYINGRPVDLKK 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1015172289 302 VCRLVNEVYHMYNRHQYPFVVLNISVDSGNL 332
Cdd:cd03484    80 VAKLINEVYKSFNSRQYPFFILNISLPTSLY 110
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
626-769 1.17e-37

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: 137.49  E-value: 1.17e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  626 IIGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQHTV-LQGQRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDFVID 704
Cdd:smart00853   1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQAGgLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELEIF 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1015172289  705 ENAPVTerakLISLPTSKNWTFGPQDVDELIFMLSDSPGVMCrPSRVKQMFASRACRKSVMIGTA 769
Cdd:smart00853  81 GPQSLI----LRSVPALLRQQNLQKLIPELLDLLSDEEENAR-PSRLEALLASLACRSAIRAGDA 140
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
627-770 2.18e-29

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: 113.85  E-value: 2.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 627 IGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQHTVLQG---QRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDFvi 703
Cdd:pfam08676   4 LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGlaaQPLLIPLVLELSPEEAALLEEHKEELAQLGFEL-- 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1015172289 704 deNAPVTERAKLISLPTSKNWTFGPQDVDELIFMLSDSPGVMCrPSRVKQMFASRACRKSVMIGTAL 770
Cdd:pfam08676  82 --EEFGPNSVIVRSVPALLRQQNLQELIRELLDELAEKGGSSL-EESLEELLATMACHSAVRAGRRL 145
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
625-801 1.26e-26

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 114.76  E-value: 1.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 625 EIIGQFNLGFIITKLNEDIFIVDQHATDEKYNFE-MLQQHTV--LQGQRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDF 701
Cdd:COG0323   329 AALGQLHGTYILAENEDGLVLIDQHAAHERILYErLKKALAEggVASQPLLIPETLELSPAEAALLEEHLEELARLGFEI 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 702 videnAPVTERAKLI-SLPTSknwtFGPQDVDELIF----MLSDSPGVMCRPSRVKQMFASRACRKSVMIGTALNTSEMK 776
Cdd:COG0323   409 -----EPFGPNTVAVrAVPAL----LGEGDAEELLRdlldELAEEGSSESLEELREELLATMACHGAIKAGRRLSLEEMN 479
                         170       180
                  ....*....|....*....|....*
gi 1015172289 777 KLITHMGEMDHPWNCPHGRPTMRHI 801
Cdd:COG0323   480 ALLRDLEATENPYTCPHGRPTWIEL 504
MutL_Trans cd00782
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
223-332 9.78e-24

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: 96.84  E-value: 9.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 223 IKENIGSVFGQKQLQSLIPFvqlppsdsvceeyglscsDALHNLFYISGFISQCTHGvgRSSTDRQFFFINRRPCDPAKV 302
Cdd:cd00782     1 LKDRIAQVYGKEVAKNLIEV------------------ELESGDFRISGYISKPDFG--RSSKDRQFLFVNGRPVRDKLL 60
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1015172289 303 CRLVNEVYHMYN-RHQYPFVVLNISVDSGNL 332
Cdd:cd00782    61 SKAINEAYRSYLpKGRYPVFVLNLELPPELV 91
TopoII_MutL_Trans cd00329
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
223-328 8.93e-13

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: 64.97  E-value: 8.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 223 IKENIGSVFGQKQLQSLIPFvqlppsdsvceeyglscsDALHNLFYISGFISQCTHGvgRSSTDRQFFFINRRPCDPAK- 301
Cdd:cd00329     1 LKDRLAEILGDKVADKLIYV------------------EGESDGFRVEGAISYPDSG--RSSKDRQFSFVNGRPVREGGt 60
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1015172289 302 VCRLVNEVYHMY----NRHQYPFVVLNISVD 328
Cdd:cd00329    61 HVKAVREAYTRAlngdDVRRYPVAVLSLKIP 91
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
229-332 3.06e-12

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: 64.06  E-value: 3.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 229 SVFGQKQLQSLIPFvqlppsdsvceeyglscsDALHNLFYISGFISQctHGVGRSSTDRQFFFINRRPCDPAKVCRLVNE 308
Cdd:pfam01119   2 AIYGKEFAENLLPI------------------EKEDDGLRLSGYISK--PTLSRSNRDYQYLFVNGRPVRDKLLSHAIRE 61
                          90       100
                  ....*....|....*....|....*
gi 1015172289 309 VYHMY-NRHQYPFVVLNISVDSGNL 332
Cdd:pfam01119  62 AYRDLlPKGRYPVAVLFLEIDPELV 86
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
35-151 3.70e-09

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: 55.80  E-value: 3.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  35 LSTAVKELVENSLDAGATNIDLKLKDY--GVDLIEVSDNGCGVEEENF-EGLTLkHHTSKIQEFaDLTQVETFGFrGEAL 111
Cdd:pfam13589   1 LEGALAELIDNSIDADATNIKIEVNKNrgGGTEIVIEDDGHGMSPEELiNALRL-ATSAKEAKR-GSTDLGRYGI-GLKL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1015172289 112 SSLCALSDVTISTcHASAKVGTR-LMFD----HNGKIIQKTPYPR 151
Cdd:pfam13589  78 ASLSLGAKLTVTS-KKEGKSSTLtLDRDkisnENDWLLPLLTPAP 121
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
31-170 9.35e-07

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: 48.13  E-value: 9.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289  31 VVLSLSTAVKELVENSLD--AGATNIDLKLKDYGVDLIEVSDNGCGVEEENFEGLtlkhhtskiqeFADLTQVETFGFRG 108
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKhaAKAGEITVTLSEGGELTLTVEDNGIGIPPEDLPRI-----------FEPFSTADKRGGGG 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1015172289 109 EALSslcalsdvtISTCHASAKVgtrlmfdHNGKI-IQKTPyprPRGTTVSVqqlfsTLPVRH 170
Cdd:pfam02518  71 TGLG---------LSIVRKLVEL-------LGGTItVESEP---GGGTTVTL-----TLPLAQ 109
PRK04184 PRK04184
DNA topoisomerase VI subunit B; Validated
34-79 2.47e-04

DNA topoisomerase VI subunit B; Validated


Pssm-ID: 235246 [Multi-domain]  Cd Length: 535  Bit Score: 44.50  E-value: 2.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1015172289  34 SLSTAVKELVENSLDAGATN-------IDLKLKDYGVDL--IEVSDNGCGVEEEN 79
Cdd:PRK04184   36 ALYTTVKELVDNSLDACEEAgilpdikIEIKRVDEGKDHyrVTVEDNGPGIPPEE 90
MutL_Trans_MLH3 cd03486
MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
255-310 5.97e-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: 40.76  E-value: 5.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1015172289 255 YGLSCSDAL------HNLFYISGFISQCTHGvgrsSTDRQFFFINRRPCDPAKVCRLVNEVY 310
Cdd:cd03486    10 YGLVLAQKLkevsakFQEYEVSGYISSEGHY----SKSFQFIYVNGRLYLKTRFHKLINKLF 67
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
35-95 1.36e-03

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 39.17  E-value: 1.36e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1015172289   35 LSTAVKELVENSLDAGATN--IDLKLKDYGVDL-IEVSDNGCGVEEEN----FE-GLTLKHHTSKIQEF 95
Cdd:smart00387   6 LRQVLSNLLDNAIKYTPEGgrITVTLERDGDHVeITVEDNGPGIPPEDlekiFEpFFRTDKRSRKIGGT 74
MutL_Trans_MLH1 cd03483
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
222-332 1.53e-03

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: 39.14  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 222 SIKENIGSVFGQKQLQSLIPFvqlppSDSVCEEYGlscsdalhnLFYISGFISQCTHgvgrSSTDRQF-FFINRR--PCD 298
Cdd:cd03483     1 STKDNIRSVYGAAVANELIEV-----EISDDDDDL---------GFKVKGLISNANY----SKKKIIFiLFINNRlvECS 62
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1015172289 299 PAKvcRLVNEVYHMY-NRHQYPFVVLNISVDSGNL 332
Cdd:cd03483    63 ALR--RAIENVYANYlPKGAHPFVYLSLEIPPENV 95
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
35-91 1.90e-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: 1.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1015172289  35 LSTAVKELVENSLDAGATN------IDLKLKDYGVDL-IEVSDNGCGVEEENFEGLTLKHHTSK 91
Cdd:COG3290   282 LVTILGNLLDNAIEAVEKLpeeerrVELSIRDDGDELvIEVEDSGPGIPEELLEKIFERGFSTK 345
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
35-78 2.65e-03

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: 38.04  E-value: 2.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1015172289  35 LSTAVKELVENSLDAGA------TNIDLKLKDYGVDL-IEVSDNGCGVEEE 78
Cdd:cd16915     1 LITIVGNLIDNALDALAatgapnKQVEVFLRDEGDDLvIEVRDTGPGIAPE 51
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
29-83 3.27e-03

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


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 38.16  E-value: 3.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1015172289  29 GQVVLsLSTAVKELVENSLD---AGaTNIDLKLKDYGVDLIEVSDNGCGVEEENFEGL 83
Cdd:cd16940     9 GDALL-LFLLLRNLVDNAVRyspQG-SRVEIKLSADDGAVIRVEDNGPGIDEEELEAL 64
HATPase_TopVIB-like cd16933
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family ...
34-78 6.06e-03

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


Pssm-ID: 340410 [Multi-domain]  Cd Length: 203  Bit Score: 38.87  E-value: 6.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1015172289  34 SLSTAVKELVENSLDAGAT-----NIDLKLKDYGVD--LIEVSDNGCGVEEE 78
Cdd:cd16933    19 SLYTTVRELVENSLDATEEagilpDIKVEIEEIGKDhyKVIVEDNGPGIPEE 70
HATPase_MORC-like cd16931
Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger ...
38-78 7.28e-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: 37.00  E-value: 7.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1015172289  38 AVKELVENSLDAGATN----IDLKLKDYGVDLIEVSDNGCGVEEE 78
Cdd:cd16931    15 AVAELVDNARDADATRldifIDDINLLRGGFMLSFLDDGNGMTPE 59
MutL_Trans_hPMS_1_like cd03485
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
222-332 8.64e-03

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: 37.25  E-value: 8.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015172289 222 SIKENIGSVFGQKQLQSLIPFvqlppsDSVCEEYGlscsdalhnlFYISGFISQCTHGVGRSSTDRQFFFINRRPCDPAK 301
Cdd:cd03485     1 DHKEALARVLGTAVAANMVPV------QSTDEDPQ----------ISLEGFLPKPGSDVSKTKSDGKFISVNSRPVSLGK 64
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1015172289 302 -VCRLVNEVYHMYNRH----QYPFVVLNISVDSGNL 332
Cdd:cd03485    65 dIGKLLRQYYSSAYRKsslrRYPVFFLNILCPPGLV 100
 
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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