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Conserved domains on  [gi|1015130027|ref|NP_001308939|]
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mismatch repair endonuclease PMS2 isoform f [Homo sapiens]

Protein Classification

DNA mismatch repair MutL family protein( domain architecture ID 1001448)

DNA mismatch repair MutL family protein is required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage, or recombination events

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MutL super family cl33837
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
2-669 4.09e-59

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


The actual alignment was detected with superfamily member COG0323:

Pssm-ID: 223400 [Multi-domain]  Cd Length: 638  Bit Score: 210.27  E-value: 4.09e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027   2 FDHNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRHKeFQRNIKKEYAKMVQVLHAYCIISAGIRVSCTNQlgqGK-RQPVV 80
Cdd:COG0323   126 AEGGGMEVTVKPAAHPVGTTVEVRDLFYNTPARRK-FLKSEKTEFGHITELINRYALAHPDISFSLSHN---GKlRIELL 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027  81 CTGGSPSIKENIGSVFGQKQLQSLIPFvqlppsdsvceeyglscsDALHNLFYISGFISQCThgVGRSSTDRQFFFINRR 160
Cdd:COG0323   202 KLPGTGDLEERIAAVYGTEFLKNALPI------------------ENEHEDLRLSGYVSLPE--FTRASRDYQYLFVNGR 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 161 PCDPAKVCRLVNEVYHMYN-RHQYPFVVLNISVDsgnlikMHAADLekpmvekqDQSPSlrtgeeKKDVSISRLREAFSL 239
Cdd:COG0323   262 PVRDKLLNHALREAYADYLpRGRYPVFVLFLELD------PELVDV--------NVHPA------KKEVRFSDERLVHDL 321
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 240 rhttenkphspktpeprrsplgqkrgmLSSSTSGAISDKGVLRPQ-KEAVSSSHGPSDPTDRAEVEKDSGHGSTSVDSEG 318
Cdd:COG0323   322 ---------------------------IYEAIKEALAQQGLIPPAsVEAPKSASQPLPAFQEPSPLPESRIQKSKVAKSG 374
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 319 FSIPDTGShcsseyaasspgdrgsqehvdsqekapktddsfsdvdchsnqedtgckfrvLPQPTNLATPNtkrfkkeeil 398
Cdd:COG0323   375 SSKSDAPS---------------------------------------------------IAEPASGASPS---------- 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 399 sssdicqklvntqdmsasqvdvavKINKKVVPLDFSMSSLAKRikqlhheAQQSEGEQNYRKFRAKICPGENQAAEDElR 478
Cdd:COG0323   394 ------------------------PASPSIRPLSKNILPESSP-------GSLKNEDRSYDDLLEEPAESEDKQEEAE-Q 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 479 KEISKTMFAEMEIIGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQ--HTVLQGQRLIAPQTLNLTAVNEAVLIENL 556
Cdd:COG0323   442 KAISEDVFPLGEAIGQVHGTYILAEHEDGLVLVDQHAAHERILYEKLKNelGNVGELQPLLIPIRLELSPEEADVLEEHK 521
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 557 EIFRKNGFDFVIDENapvtERAKLISLPTSKNWTFGPQDVDELIFMLSdSPGVMCRPSRVKQMFASRACRKSVMIGTALN 636
Cdd:COG0323   522 EELEKLGFEIESFGE----NSVAVRSVPAMLGKAEVQELIRELLDDLL-EGKLKDLKELLEELAATMACRSAVKAGRELS 596
                         650       660       670
                  ....*....|....*....|....*....|...
gi 1015130027 637 TSEMKKLITHMGEMDHPWNCPHGRPTMRHIANL 669
Cdd:COG0323   597 AEEMNALLRDLEACPNPWTCPHGRPTYIVLSLA 629
 
Name Accession Description Interval E-value
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
2-669 4.09e-59

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


Pssm-ID: 223400 [Multi-domain]  Cd Length: 638  Bit Score: 210.27  E-value: 4.09e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027   2 FDHNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRHKeFQRNIKKEYAKMVQVLHAYCIISAGIRVSCTNQlgqGK-RQPVV 80
Cdd:COG0323   126 AEGGGMEVTVKPAAHPVGTTVEVRDLFYNTPARRK-FLKSEKTEFGHITELINRYALAHPDISFSLSHN---GKlRIELL 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027  81 CTGGSPSIKENIGSVFGQKQLQSLIPFvqlppsdsvceeyglscsDALHNLFYISGFISQCThgVGRSSTDRQFFFINRR 160
Cdd:COG0323   202 KLPGTGDLEERIAAVYGTEFLKNALPI------------------ENEHEDLRLSGYVSLPE--FTRASRDYQYLFVNGR 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 161 PCDPAKVCRLVNEVYHMYN-RHQYPFVVLNISVDsgnlikMHAADLekpmvekqDQSPSlrtgeeKKDVSISRLREAFSL 239
Cdd:COG0323   262 PVRDKLLNHALREAYADYLpRGRYPVFVLFLELD------PELVDV--------NVHPA------KKEVRFSDERLVHDL 321
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 240 rhttenkphspktpeprrsplgqkrgmLSSSTSGAISDKGVLRPQ-KEAVSSSHGPSDPTDRAEVEKDSGHGSTSVDSEG 318
Cdd:COG0323   322 ---------------------------IYEAIKEALAQQGLIPPAsVEAPKSASQPLPAFQEPSPLPESRIQKSKVAKSG 374
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 319 FSIPDTGShcsseyaasspgdrgsqehvdsqekapktddsfsdvdchsnqedtgckfrvLPQPTNLATPNtkrfkkeeil 398
Cdd:COG0323   375 SSKSDAPS---------------------------------------------------IAEPASGASPS---------- 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 399 sssdicqklvntqdmsasqvdvavKINKKVVPLDFSMSSLAKRikqlhheAQQSEGEQNYRKFRAKICPGENQAAEDElR 478
Cdd:COG0323   394 ------------------------PASPSIRPLSKNILPESSP-------GSLKNEDRSYDDLLEEPAESEDKQEEAE-Q 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 479 KEISKTMFAEMEIIGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQ--HTVLQGQRLIAPQTLNLTAVNEAVLIENL 556
Cdd:COG0323   442 KAISEDVFPLGEAIGQVHGTYILAEHEDGLVLVDQHAAHERILYEKLKNelGNVGELQPLLIPIRLELSPEEADVLEEHK 521
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 557 EIFRKNGFDFVIDENapvtERAKLISLPTSKNWTFGPQDVDELIFMLSdSPGVMCRPSRVKQMFASRACRKSVMIGTALN 636
Cdd:COG0323   522 EELEKLGFEIESFGE----NSVAVRSVPAMLGKAEVQELIRELLDDLL-EGKLKDLKELLEELAATMACRSAVKAGRELS 596
                         650       660       670
                  ....*....|....*....|....*....|...
gi 1015130027 637 TSEMKKLITHMGEMDHPWNCPHGRPTMRHIANL 669
Cdd:COG0323   597 AEEMNALLRDLEACPNPWTCPHGRPTYIVLSLA 629
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
5-197 1.82e-58

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: 199.40  E-value: 1.82e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027   5 NGKIIQKTPYPRPRGTTVSVQQLFSTLPVRHKeFQRNIKKEYAKMVQVLHAYCIISAGIRVSCTNqlgQGKRQPVVCTGG 84
Cdd:TIGR00585 128 GGMIESIKPAPRPVGTTVEVRDLFYNLPVRRK-FLKSPKKEFRKILDVLQRYALIHPDISFSLTH---DGKKVLQLSTKP 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027  85 SPSIKEN-IGSVFGQKQLQSLIPFVQLPPSDsvceeyglscsdalhnlFYISGFISQCTHGVGRSSTDrQFFFINRRPCD 163
Cdd:TIGR00585 204 NQSTKENrIRSVFGTAVLRKLIPLDEWEDLD-----------------LQLEGFISQPNVTRSRRSGW-QFLFINGRPVE 265
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1015130027 164 PAKVCRLVNEVYHMYN-RHQYPFVVLNISVDSGNL 197
Cdd:TIGR00585 266 LKLLLKAIREVYHEYLpKGQYPVFVLNLEIDPELV 300
MutL_Trans_hPMS_2_like cd03484
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
87-197 1.92e-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: 160.90  E-value: 1.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027  87 SIKENIGSVFGQKQLQSLIPFVQLPPSDSVCEEYgLSCSDALHNLFYISGFISQCTHGVGRSSTDRQFFFINRRPCDPAK 166
Cdd:cd03484     1 DIKDNIINVFGGKVIKGLIPINLELDVNPTKEEL-DSDEDLADSEVKITGYISKPSHGCGRSSSDRQFFYINGRPVDLKK 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1015130027 167 VCRLVNEVYHMYNRHQYPFVVLNISVDSGNL 197
Cdd:cd03484    80 VAKLINEVYKSFNSRQYPFFILNISLPTSLY 110
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
491-634 6.83e-38

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: 6.83e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027  491 IIGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQHTV-LQGQRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDFVID 569
Cdd:smart00853   1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQAGgLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELEIF 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1015130027  570 ENAPVTerakLISLPTSKNWTFGPQDVDELIFMLSDSPGVMCrPSRVKQMFASRACRKSVMIGTA 634
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 ...
492-635 1.62e-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: 1.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 492 IGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQHTVLQG---QRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDFvi 568
Cdd:pfam08676   4 LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGlaaQPLLIPLVLELSPEEAALLEEHKEELAQLGFEL-- 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1015130027 569 deNAPVTERAKLISLPTSKNWTFGPQDVDELIFMLSDSPGVMCrPSRVKQMFASRACRKSVMIGTAL 635
Cdd:pfam08676  82 --EEFGPNSVIVRSVPALLRQQNLQELIRELLDELAEKGGSSL-EESLEELLATMACHSAVRAGRRL 145
mutL PRK00095
DNA mismatch repair endonuclease MutL;
4-666 3.34e-24

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 107.61  E-value: 3.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027   4 HNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRHKeFQRNIKKEYAKMVQVLHAYCIISAGIRVSCTNQlgqGKrqPVVCTG 83
Cdd:PRK00095  126 EGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRK-FLKSEKTELGHIDDVVNRLALAHPDVAFTLTHN---GK--LVLQTR 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027  84 GSPSIKENIGSVFGQKQLQSLIPFvqlppsdsvceeyglscsDALHNLFYISGFISQ--CThgvgRSSTDRQFFFINRRP 161
Cdd:PRK00095  200 GAGQLLQRLAAILGREFAENALPI------------------DAEHGDLRLSGYVGLptLS----RANRDYQYLFVNGRY 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 162 cdpakV-CRLVN----EVYHMY-NRHQYPFVVLNISVDsgnlikmhaadlekpmvekqdqsPSLrtgeekKDVSisrlre 235
Cdd:PRK00095  258 -----VrDKLLNhairQAYHDLlPRGRYPAFVLFLELD-----------------------PHQ------VDVN------ 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 236 afslRHTTenkphspKTpEPRRSPLGQKRGMLSsstsGAISDkgVLRpQKEAVSSSHGPSDPTDRAEVEKDSGHGSTSVD 315
Cdd:PRK00095  298 ----VHPA-------KH-EVRFRDERLVHDLIV----QAIQE--ALA-QSGLIPAAAGANQVLEPAEPEPLPLQQTPLYA 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 316 SEGFSIPDTGSHCSSEYAASSPGDRGSQEHVDSQEKAPKTDDSFSDVDCHSNQEDTgckfrvlpqptnlatpntkrfkke 395
Cdd:PRK00095  359 SGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSEAAAAASAEAAAAAPAA------------------------ 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 396 eilsssdicqklvntqdmsasqvdvavkinkkvvpldfsmsslakrikQLHHEAQQSEGEQnyrkfrakicpgenqaaed 475
Cdd:PRK00095  415 ------------------------------------------------APEPAEAAEEADS------------------- 427
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 476 elrkeisktmFAEMEIIGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQH---TVLQGQRLIAPQTLNLTAVNEAVL 552
Cdd:PRK00095  428 ----------FPLGYALGQLHGTYILAENEDGLYLVDQHAAHERLLYEQLKDKlaeVGLASQPLLIPLVLELSEDEADRL 497
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 553 IENLEIFRKNGFDF-VIDENApVTERakliSLPTsknWtFGPQDVDELIF----MLSDSPGVmcRPSRVKQMFASRACRK 627
Cdd:PRK00095  498 EEHKELLARLGLELePFGPNS-FAVR----EVPA---L-LGQQELEELIRdlldELAEEGDS--DTLKERELLATMACHG 566
                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 1015130027 628 SVMIGTALNTSEMKKLITHMGEMDHPWNCPHGRPTMRHI 666
Cdd:PRK00095  567 AIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIEL 605
 
Name Accession Description Interval E-value
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
2-669 4.09e-59

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


Pssm-ID: 223400 [Multi-domain]  Cd Length: 638  Bit Score: 210.27  E-value: 4.09e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027   2 FDHNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRHKeFQRNIKKEYAKMVQVLHAYCIISAGIRVSCTNQlgqGK-RQPVV 80
Cdd:COG0323   126 AEGGGMEVTVKPAAHPVGTTVEVRDLFYNTPARRK-FLKSEKTEFGHITELINRYALAHPDISFSLSHN---GKlRIELL 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027  81 CTGGSPSIKENIGSVFGQKQLQSLIPFvqlppsdsvceeyglscsDALHNLFYISGFISQCThgVGRSSTDRQFFFINRR 160
Cdd:COG0323   202 KLPGTGDLEERIAAVYGTEFLKNALPI------------------ENEHEDLRLSGYVSLPE--FTRASRDYQYLFVNGR 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 161 PCDPAKVCRLVNEVYHMYN-RHQYPFVVLNISVDsgnlikMHAADLekpmvekqDQSPSlrtgeeKKDVSISRLREAFSL 239
Cdd:COG0323   262 PVRDKLLNHALREAYADYLpRGRYPVFVLFLELD------PELVDV--------NVHPA------KKEVRFSDERLVHDL 321
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 240 rhttenkphspktpeprrsplgqkrgmLSSSTSGAISDKGVLRPQ-KEAVSSSHGPSDPTDRAEVEKDSGHGSTSVDSEG 318
Cdd:COG0323   322 ---------------------------IYEAIKEALAQQGLIPPAsVEAPKSASQPLPAFQEPSPLPESRIQKSKVAKSG 374
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 319 FSIPDTGShcsseyaasspgdrgsqehvdsqekapktddsfsdvdchsnqedtgckfrvLPQPTNLATPNtkrfkkeeil 398
Cdd:COG0323   375 SSKSDAPS---------------------------------------------------IAEPASGASPS---------- 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 399 sssdicqklvntqdmsasqvdvavKINKKVVPLDFSMSSLAKRikqlhheAQQSEGEQNYRKFRAKICPGENQAAEDElR 478
Cdd:COG0323   394 ------------------------PASPSIRPLSKNILPESSP-------GSLKNEDRSYDDLLEEPAESEDKQEEAE-Q 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 479 KEISKTMFAEMEIIGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQ--HTVLQGQRLIAPQTLNLTAVNEAVLIENL 556
Cdd:COG0323   442 KAISEDVFPLGEAIGQVHGTYILAEHEDGLVLVDQHAAHERILYEKLKNelGNVGELQPLLIPIRLELSPEEADVLEEHK 521
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 557 EIFRKNGFDFVIDENapvtERAKLISLPTSKNWTFGPQDVDELIFMLSdSPGVMCRPSRVKQMFASRACRKSVMIGTALN 636
Cdd:COG0323   522 EELEKLGFEIESFGE----NSVAVRSVPAMLGKAEVQELIRELLDDLL-EGKLKDLKELLEELAATMACRSAVKAGRELS 596
                         650       660       670
                  ....*....|....*....|....*....|...
gi 1015130027 637 TSEMKKLITHMGEMDHPWNCPHGRPTMRHIANL 669
Cdd:COG0323   597 AEEMNALLRDLEACPNPWTCPHGRPTYIVLSLA 629
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
5-197 1.82e-58

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: 199.40  E-value: 1.82e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027   5 NGKIIQKTPYPRPRGTTVSVQQLFSTLPVRHKeFQRNIKKEYAKMVQVLHAYCIISAGIRVSCTNqlgQGKRQPVVCTGG 84
Cdd:TIGR00585 128 GGMIESIKPAPRPVGTTVEVRDLFYNLPVRRK-FLKSPKKEFRKILDVLQRYALIHPDISFSLTH---DGKKVLQLSTKP 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027  85 SPSIKEN-IGSVFGQKQLQSLIPFVQLPPSDsvceeyglscsdalhnlFYISGFISQCTHGVGRSSTDrQFFFINRRPCD 163
Cdd:TIGR00585 204 NQSTKENrIRSVFGTAVLRKLIPLDEWEDLD-----------------LQLEGFISQPNVTRSRRSGW-QFLFINGRPVE 265
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1015130027 164 PAKVCRLVNEVYHMYN-RHQYPFVVLNISVDSGNL 197
Cdd:TIGR00585 266 LKLLLKAIREVYHEYLpKGQYPVFVLNLEIDPELV 300
MutL_Trans_hPMS_2_like cd03484
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
87-197 1.92e-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: 160.90  E-value: 1.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027  87 SIKENIGSVFGQKQLQSLIPFVQLPPSDSVCEEYgLSCSDALHNLFYISGFISQCTHGVGRSSTDRQFFFINRRPCDPAK 166
Cdd:cd03484     1 DIKDNIINVFGGKVIKGLIPINLELDVNPTKEEL-DSDEDLADSEVKITGYISKPSHGCGRSSSDRQFFYINGRPVDLKK 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1015130027 167 VCRLVNEVYHMYNRHQYPFVVLNISVDSGNL 197
Cdd:cd03484    80 VAKLINEVYKSFNSRQYPFFILNISLPTSLY 110
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
491-634 6.83e-38

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: 6.83e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027  491 IIGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQHTV-LQGQRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDFVID 569
Cdd:smart00853   1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQAGgLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELEIF 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1015130027  570 ENAPVTerakLISLPTSKNWTFGPQDVDELIFMLSDSPGVMCrPSRVKQMFASRACRKSVMIGTA 634
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 ...
492-635 1.62e-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: 1.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 492 IGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQHTVLQG---QRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDFvi 568
Cdd:pfam08676   4 LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGlaaQPLLIPLVLELSPEEAALLEEHKEELAQLGFEL-- 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1015130027 569 deNAPVTERAKLISLPTSKNWTFGPQDVDELIFMLSDSPGVMCrPSRVKQMFASRACRKSVMIGTAL 635
Cdd:pfam08676  82 --EEFGPNSVIVRSVPALLRQQNLQELIRELLDELAEKGGSSL-EESLEELLATMACHSAVRAGRRL 145
mutL PRK00095
DNA mismatch repair endonuclease MutL;
4-666 3.34e-24

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 107.61  E-value: 3.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027   4 HNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRHKeFQRNIKKEYAKMVQVLHAYCIISAGIRVSCTNQlgqGKrqPVVCTG 83
Cdd:PRK00095  126 EGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRK-FLKSEKTELGHIDDVVNRLALAHPDVAFTLTHN---GK--LVLQTR 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027  84 GSPSIKENIGSVFGQKQLQSLIPFvqlppsdsvceeyglscsDALHNLFYISGFISQ--CThgvgRSSTDRQFFFINRRP 161
Cdd:PRK00095  200 GAGQLLQRLAAILGREFAENALPI------------------DAEHGDLRLSGYVGLptLS----RANRDYQYLFVNGRY 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 162 cdpakV-CRLVN----EVYHMY-NRHQYPFVVLNISVDsgnlikmhaadlekpmvekqdqsPSLrtgeekKDVSisrlre 235
Cdd:PRK00095  258 -----VrDKLLNhairQAYHDLlPRGRYPAFVLFLELD-----------------------PHQ------VDVN------ 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 236 afslRHTTenkphspKTpEPRRSPLGQKRGMLSsstsGAISDkgVLRpQKEAVSSSHGPSDPTDRAEVEKDSGHGSTSVD 315
Cdd:PRK00095  298 ----VHPA-------KH-EVRFRDERLVHDLIV----QAIQE--ALA-QSGLIPAAAGANQVLEPAEPEPLPLQQTPLYA 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 316 SEGFSIPDTGSHCSSEYAASSPGDRGSQEHVDSQEKAPKTDDSFSDVDCHSNQEDTgckfrvlpqptnlatpntkrfkke 395
Cdd:PRK00095  359 SGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSEAAAAASAEAAAAAPAA------------------------ 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 396 eilsssdicqklvntqdmsasqvdvavkinkkvvpldfsmsslakrikQLHHEAQQSEGEQnyrkfrakicpgenqaaed 475
Cdd:PRK00095  415 ------------------------------------------------APEPAEAAEEADS------------------- 427
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 476 elrkeisktmFAEMEIIGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQH---TVLQGQRLIAPQTLNLTAVNEAVL 552
Cdd:PRK00095  428 ----------FPLGYALGQLHGTYILAENEDGLYLVDQHAAHERLLYEQLKDKlaeVGLASQPLLIPLVLELSEDEADRL 497
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027 553 IENLEIFRKNGFDF-VIDENApVTERakliSLPTsknWtFGPQDVDELIF----MLSDSPGVmcRPSRVKQMFASRACRK 627
Cdd:PRK00095  498 EEHKELLARLGLELePFGPNS-FAVR----EVPA---L-LGQQELEELIRdlldELAEEGDS--DTLKERELLATMACHG 566
                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 1015130027 628 SVMIGTALNTSEMKKLITHMGEMDHPWNCPHGRPTMRHI 666
Cdd:PRK00095  567 AIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIEL 605
MutL_Trans cd00782
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
88-197 1.11e-23

MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the C-terminal domain of DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. Included in this group are proteins similar to human MLH1, hPMS2, hPMS1, hMLH3 and E. coli MutL, MLH1 forms heterodimers with PMS2, PMS1 and MLH3. These three complexes have distinct functions in meiosis. hMLH1-hPMS2 also participates in the repair of all DNA mismatch repair (MMR) substrates. Roles for hMLH1-hPMS1 or hMLH1-hMLH3 in MMR have not been established. Cells lacking either hMLH1 or hPMS2 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hMLH1 causes predisposition to HNPCC, Muir-Torre syndrome and Turcot syndrome (HNPCC variant). Mutation in hPMS2 causes predisposition to HPNCC and Turcot syndrome. Mutation in hMLH1 accounts for a large fraction of HNPCC families. There is no convincing evidence to support hPMS1 having a role in HNPCC predisposition. It has been suggested that hMLH3 may be a low risk gene for colorectal cancer; however there is little evidence to support it having a role in classical HNPCC. It has been suggested that during initiation of DNA mismatch repair in E. coli, the mismatch recognition protein MutS recruits MutL in the presence of ATP. The MutS(ATP)-MutL ternary complex formed, then recruits the latent endonuclease MutH.


Pssm-ID: 238405 [Multi-domain]  Cd Length: 122  Bit Score: 96.46  E-value: 1.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027  88 IKENIGSVFGQKQLQSLIPFvqlppsdsvceeyglscsDALHNLFYISGFISQCTHGvgRSSTDRQFFFINRRPCDPAKV 167
Cdd:cd00782     1 LKDRIAQVYGKEVAKNLIEV------------------ELESGDFRISGYISKPDFG--RSSKDRQFLFVNGRPVRDKLL 60
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1015130027 168 CRLVNEVYHMYN-RHQYPFVVLNISVDSGNL 197
Cdd:cd00782    61 SKAINEAYRSYLpKGRYPVFVLNLELPPELV 91
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
1-70 1.28e-19

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: 87.11  E-value: 1.28e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027   1 MFDHNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRHKeFQRNIKKEYAKMVQVLHAYCIISAGIRVSCTNQ 70
Cdd:cd16926   115 VVDGGGIIEEVKPAAAPVGTTVTVRDLFYNTPARRK-FLKSPKTELSKILDLVQRLALAHPDVSFSLTHD 183
TopoII_MutL_Trans cd00329
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
88-193 9.15e-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: 9.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027  88 IKENIGSVFGQKQLQSLIPFvqlppsdsvceeyglscsDALHNLFYISGFISQCTHGvgRSSTDRQFFFINRRPCDPAK- 166
Cdd:cd00329     1 LKDRLAEILGDKVADKLIYV------------------EGESDGFRVEGAISYPDSG--RSSKDRQFSFVNGRPVREGGt 60
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1015130027 167 VCRLVNEVYHMY----NRHQYPFVVLNISVD 193
Cdd:cd00329    61 HVKAVREAYTRAlngdDVRRYPVAVLSLKIP 91
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
94-197 3.19e-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: 63.67  E-value: 3.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027  94 SVFGQKQLQSLIPFvqlppsdsvceeyglscsDALHNLFYISGFISQctHGVGRSSTDRQFFFINRRPCDPAKVCRLVNE 173
Cdd:pfam01119   2 AIYGKEFAENLLPI------------------EKEDDGLRLSGYISK--PTLSRSNRDYQYLFVNGRPVRDKLLSHAIRE 61
                          90       100
                  ....*....|....*....|....*
gi 1015130027 174 VYHMY-NRHQYPFVVLNISVDSGNL 197
Cdd:pfam01119  62 AYRDLlPKGRYPVAVLFLEIDPELV 86
MutL_Trans_MLH3 cd03486
MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
120-175 5.50e-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: 5.50e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1015130027 120 YGLSCSDAL------HNLFYISGFISQCTHGvgrsSTDRQFFFINRRPCDPAKVCRLVNEVY 175
Cdd:cd03486    10 YGLVLAQKLkevsakFQEYEVSGYISSEGHY----SKSFQFIYVNGRLYLKTRFHKLINKLF 67
MutL_Trans_MLH1 cd03483
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
87-197 1.28e-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: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027  87 SIKENIGSVFGQKQLQSLIPFvqlppSDSVCEEYGlscsdalhnLFYISGFISQCTHgvgrSSTDRQF-FFINRR--PCD 163
Cdd:cd03483     1 STKDNIRSVYGAAVANELIEV-----EISDDDDDL---------GFKVKGLISNANY----SKKKIIFiLFINNRlvECS 62
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1015130027 164 PAKvcRLVNEVYHMY-NRHQYPFVVLNISVDSGNL 197
Cdd:cd03483    63 ALR--RAIENVYANYlPKGAHPFVYLSLEIPPENV 95
MutL_Trans_hPMS_1_like cd03485
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
87-197 7.90e-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: 7.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015130027  87 SIKENIGSVFGQKQLQSLIPFvqlppsDSVCEEYGlscsdalhnlFYISGFISQCTHGVGRSSTDRQFFFINRRPCDPAK 166
Cdd:cd03485     1 DHKEALARVLGTAVAANMVPV------QSTDEDPQ----------ISLEGFLPKPGSDVSKTKSDGKFISVNSRPVSLGK 64
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1015130027 167 -VCRLVNEVYHMYNRH----QYPFVVLNISVDSGNL 197
Cdd:cd03485    65 dIGKLLRQYYSSAYRKsslrRYPVFFLNILCPPGLV 100
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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