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Conserved domains on  [gi|1573864389|gb|RZD53828|]
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MAG: hypothetical protein CXT64_01315, partial [Methanobacteriota archaeon]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MutL_C super family cl07336
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
 1-94 3.35e-08

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.


The actual alignment was detected with superfamily member pfam08676:

Pssm-ID: 447329  Cd Length: 145  Bit Score: 48.37  E-value: 3.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864389   1 RYERLREQM--ISWDGQELMAPIVISLGAREKEAANSGESRLAELGISF-AVTEEGIAITSVPeVLVGSDGLEDFLHDLL 77
Cdd:pfam08676  33 LYEKLKRALaeGGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFELeEFGPNSVIVRSVP-ALLRQQNLQELIRELL 111

                          90       100
                  ....*....|....*....|..
gi 1573864389  78 IELASAPDGA-----EESCATM 94
Cdd:pfam08676 112 DELAEKGGSSleeslEELLATM 133
 
Name Accession Description Interval E-value
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
 1-94 3.35e-08

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: 48.37  E-value: 3.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864389   1 RYERLREQM--ISWDGQELMAPIVISLGAREKEAANSGESRLAELGISF-AVTEEGIAITSVPeVLVGSDGLEDFLHDLL 77
Cdd:pfam08676  33 LYEKLKRALaeGGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFELeEFGPNSVIVRSVP-ALLRQQNLQELIRELL 111

                          90       100
                  ....*....|....*....|..
gi 1573864389  78 IELASAPDGA-----EESCATM 94
Cdd:pfam08676 112 DELAEKGGSSleeslEELLATM 133
 
Name Accession Description Interval E-value
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
 1-94 3.35e-08

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: 48.37  E-value: 3.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573864389   1 RYERLREQM--ISWDGQELMAPIVISLGAREKEAANSGESRLAELGISF-AVTEEGIAITSVPeVLVGSDGLEDFLHDLL 77
Cdd:pfam08676  33 LYEKLKRALaeGGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFELeEFGPNSVIVRSVP-ALLRQQNLQELIRELL 111

                          90       100
                  ....*....|....*....|..
gi 1573864389  78 IELASAPDGA-----EESCATM 94
Cdd:pfam08676 112 DELAEKGGSSleeslEELLATM 133
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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