1B63


Conserved Protein Domain Family
MutL_Trans_MutL

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cd03482: MutL_Trans_MutL 
Click on image for an interactive view with Cn3D
MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to Escherichia coli MutL. EcMutL belongs to the DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from the ATP-binding site to the DNA breakage/reunion regions of the enzymes. It has been suggested that during initiation of DNA mismatch repair in E. coli, the mismatch recognition protein MutS recruits MutL in the presence of ATP. The MutS(ATP)-MutL ternary complex formed, then recruits the latent endonuclease MutH. Prokaryotic MutS and MutL are homodimers.
Statistics
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PSSM-Id: 239564
Aligned: 25 rows
Threshold Bit Score: 152.737
Created: 17-Feb-2006
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
ATP binding
Conserved site include 1 residue -Click on image for an interactive view with Cn3D
Feature 1:ATP binding site [chemical binding site]
Evidence:
  • Structure:1B63_A, Escherichia coli MutL bound with Adpnp ((non-hydrolyzable ATP analog), contacts at 3.5A
  • Comment:conserved Lys residue from the transducer domain interacts with the gamma-phosphate of bound nucleotide.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                                       
1B63_A      210 KERRLGAICGTAFLEQALAIEwqhgdLTLRGWVADPnhttpaLAEIQYCYVNGRMMRDRLINHAIRQACEDKLGADqqPA 289 Escherichia coli
ZP_00865895 210 AERRLGELLGEGFLGECIHLEcaaagLKLSGWLALPtfs-rsQGDLQYFYVNGRMIRDRMAGHALRRAYADVLYRDrfPA 288 Alkalilimnicola ...
ABA56862    209 QLKRITELCGRNFAEHSMYFKreiegLCLWGWLGHPefa-rsQTDLQYCYVNHRMVRDKLLSHAARQAYGNRLSQGrhPA 287 Nitrosococcus oc...
AAV81174    208 QLQRLAKICGGGFAEQASAIDavdgdFHLSGWLVPPehc-rhQGDIQHFFVNGRMMRDKLLSHAVRQAYEKYLPNErvPT 286 Idiomarina loihi...
ZP_01041819 210 WRRRLAKVCGSGFAQDALYFQqhahdIHIEGWLAAPeqc-rhQGDVQYSFVNGRMMKDKLINHAIRQAYDSFLTAErvPT 288 Idiomarina balti...
CAG45119    212 KYNRVLDLYSREFIENAIYVDkqvgdAHLWGWVASPrfn-raRADMQSFYINGRIIKDKIVSHAIKNAYKDVMYGNryPA 290 Francisella tula...
ABB41679    220 LKQRLKQLMGTPFVDQSLELNfeaqdIQLSGWVGQAtfn-rsQTDMQYLFVNGRIVRDRLLSYAVKQAYADVLYHGrhPA 298 Thiomicrospira c...
CAI85368    208 AIARVAQVAGKAFAEQGLHIQsgeggLQLHGWVLPVg----sANTVQYTYVNNRMMRDKLILHAIRQAFEEVSGAQelPG 283 Pseudoalteromona...
AAU28755    208 KAIRMGRILGNTFMREAIFLDvehsgMRLYGWISNHrlq-rsQNDRQWIYVNQRMVKDKLLQHAVKQAYDGLLHAGrfPI 286 Legionella pneum...
EAN70357    208 MQQRLSQICGRAFAEQAITLAcehdgLSLEGYIQSPhd--nsVTDTNYFYVNGRLVRDKLVNHAVRQAFAEHQWHQq-PS 284 Shewanella denit...
Feature 1                          #                        
1B63_A      290 FVLYLEIDPHQVDVNVHPAKHEVRFHQSRLVHDFIYQGVLSVLQ 333 Escherichia coli
ZP_00865895 289 YLLYLDLDPDRVDVNVHPTKHEVRFRDSRLVYDFLFRQVREALA 332 Alkalilimnicola ehrlichei MLHE-1
ABA56862    288 YLLYLELPTHQVDVNAHPAKHEVRFRESRQVHGFIVRTLAEILE 331 Nitrosococcus oceani ATCC 19707
AAV81174    287 FVLYFELPAEEVDVNVHPAKHEVRFHRQRQVHDFILTRIEQALN 330 Idiomarina loihiensis L2TR
ZP_01041819 289 FAIYLTVPADQVDVNVHPAKHEVRFHQQRQVHDFVLNTVKQLLL 332 Idiomarina baltica OS145
CAG45119    291 FLLYLDIDYCEVDVNVHPAKSEVRFRNQKFIYDFLFGNINKAIT 334 Francisella tularensis subsp. tularensis SCHU S4
ABB41679    299 YLLFLNIPHDLVDVNVHPAKYEVRFANGRWVYDFLRRSVREAVT 342 Thiomicrospira crunogena XCL-2
CAI85368    284 FVIYIDIDPRQVDVNVHPAKHEVRFHQGRLVHDFILQAIKQVVV 327 Pseudoalteromonas haloplanktis TAC125
AAU28755    287 CLLYFTLPASEVDVNVHPTKHEVRFQQPRLVHDFFTSQLTKALQ 330 Legionella pneumophila subsp. pneumophila str. Phila...
EAN70357    285 YVLKLTLDPHQVDVNVHPAKHEVRFHQSRYVHDFILQALQSALA 328 Shewanella denitrificans OS217

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