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Conserved domains on  [gi|2243215895|dbj|BDI55117|]
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MAG: hypothetical protein (plasmid) [uncultured archaeon]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WH_MUS81 super family cl41230
winged helix domain found in crossover junction endonuclease MUS81 and similar proteins; MUS81 ...
45-70 1.73e-03

winged helix domain found in crossover junction endonuclease MUS81 and similar proteins; MUS81 is a crossover junction endonuclease that interacts with EME1 (essential meiotic structure-specific endonuclease 1) and EME2, to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. The MUS80-EME1 endonuclease maintains genomic integrity in metazoans by cleaving branched DNA structures that can form during mitosis and fission yeast meiosis, and during processing of damaged replication folks. This model corresponds to the winged helix (WH) domain of MUS81, which is responsible for DNA binding. It comprises four helices and two beta strands.


The actual alignment was detected with superfamily member cd21036:

Pssm-ID: 411029  Cd Length: 94  Bit Score: 34.05  E-value: 1.73e-03
                         10        20
                 ....*....|....*....|....*...
gi 2243215895 45 SLKTLEKKDLIKKYGNA--YSLTSSGYQ 70
Cdd:cd21036   59 SMKTLIKKGLVYKEGRParYSLTEEGRE 86
 
Name Accession Description Interval E-value
WH_MUS81 cd21036
winged helix domain found in crossover junction endonuclease MUS81 and similar proteins; MUS81 ...
45-70 1.73e-03

winged helix domain found in crossover junction endonuclease MUS81 and similar proteins; MUS81 is a crossover junction endonuclease that interacts with EME1 (essential meiotic structure-specific endonuclease 1) and EME2, to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. The MUS80-EME1 endonuclease maintains genomic integrity in metazoans by cleaving branched DNA structures that can form during mitosis and fission yeast meiosis, and during processing of damaged replication folks. This model corresponds to the winged helix (WH) domain of MUS81, which is responsible for DNA binding. It comprises four helices and two beta strands.


Pssm-ID: 411029  Cd Length: 94  Bit Score: 34.05  E-value: 1.73e-03
                         10        20
                 ....*....|....*....|....*...
gi 2243215895 45 SLKTLEKKDLIKKYGNA--YSLTSSGYQ 70
Cdd:cd21036   59 SMKTLIKKGLVYKEGRParYSLTEEGRE 86
 
Name Accession Description Interval E-value
WH_MUS81 cd21036
winged helix domain found in crossover junction endonuclease MUS81 and similar proteins; MUS81 ...
45-70 1.73e-03

winged helix domain found in crossover junction endonuclease MUS81 and similar proteins; MUS81 is a crossover junction endonuclease that interacts with EME1 (essential meiotic structure-specific endonuclease 1) and EME2, to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. The MUS80-EME1 endonuclease maintains genomic integrity in metazoans by cleaving branched DNA structures that can form during mitosis and fission yeast meiosis, and during processing of damaged replication folks. This model corresponds to the winged helix (WH) domain of MUS81, which is responsible for DNA binding. It comprises four helices and two beta strands.


Pssm-ID: 411029  Cd Length: 94  Bit Score: 34.05  E-value: 1.73e-03
                         10        20
                 ....*....|....*....|....*...
gi 2243215895 45 SLKTLEKKDLIKKYGNA--YSLTSSGYQ 70
Cdd:cd21036   59 SMKTLIKKGLVYKEGRParYSLTEEGRE 86
 
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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