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Conserved domains on  [gi|2104952192|ref|WP_224912955|]
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MULTISPECIES: HNH endonuclease signature motif containing protein [Bacillus]

Protein Classification

HNH endonuclease( domain architecture ID 10003646)

HNH endonuclease contains an HNH endonuclease signature motif and may catalyze the hydrolysis of DNA

Gene Ontology:  GO:0004519|GO:0003676|GO:0008270
PubMed:  28211904

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
McrA COG1403
5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];
286-314 2.41e-04

5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];


:

Pssm-ID: 441013 [Multi-domain]  Cd Length: 64  Bit Score: 38.81  E-value: 2.41e-04
                          10        20
                  ....*....|....*....|....*....
gi 2104952192 286 KWDWSAIDIHHVIPRERGGNNSFNNLYPL 314
Cdd:COG1403    28 PFSGDALEVDHIIPRSRGGTDTWENLVLL 56
 
Name Accession Description Interval E-value
McrA COG1403
5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];
286-314 2.41e-04

5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];


Pssm-ID: 441013 [Multi-domain]  Cd Length: 64  Bit Score: 38.81  E-value: 2.41e-04
                          10        20
                  ....*....|....*....|....*....
gi 2104952192 286 KWDWSAIDIHHVIPRERGGNNSFNNLYPL 314
Cdd:COG1403    28 PFSGDALEVDHIIPRSRGGTDTWENLVLL 56
HNHc cd00085
HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic ...
 290-321 6.03e-04

HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic proteins. The alignment includes members of the large group of homing endonucleases, yeast intron 1 protein, MutS, as well as bacterial colicins, pyocins, and anaredoxins.


Pssm-ID: 238038 [Multi-domain]  Cd Length: 57  Bit Score: 37.45  E-value: 6.03e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2104952192 290 SAIDIHHVIPRERGGNNSFNNLYPLPRTMHQQ 321
Cdd:cd00085    24 EGLEVDHIIPLSDGGNNDLDNLVLLCRKCHRK 55
HNHc smart00507
HNH nucleases;
290-320 3.29e-03

HNH nucleases;


Pssm-ID: 214702 [Multi-domain]  Cd Length: 52  Bit Score: 35.13  E-value: 3.29e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2104952192  290 SAIDIHHVIPRERGGNNSFNNLYPLPRTMHQ 320
Cdd:smart00507  22 EGLEVDHIIPLSDGGNDDLDNLVLLCPKCHI 52
 
Name Accession Description Interval E-value
McrA COG1403
5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];
286-314 2.41e-04

5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];


Pssm-ID: 441013 [Multi-domain]  Cd Length: 64  Bit Score: 38.81  E-value: 2.41e-04
                          10        20
                  ....*....|....*....|....*....
gi 2104952192 286 KWDWSAIDIHHVIPRERGGNNSFNNLYPL 314
Cdd:COG1403    28 PFSGDALEVDHIIPRSRGGTDTWENLVLL 56
HNHc cd00085
HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic ...
 290-321 6.03e-04

HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic proteins. The alignment includes members of the large group of homing endonucleases, yeast intron 1 protein, MutS, as well as bacterial colicins, pyocins, and anaredoxins.


Pssm-ID: 238038 [Multi-domain]  Cd Length: 57  Bit Score: 37.45  E-value: 6.03e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2104952192 290 SAIDIHHVIPRERGGNNSFNNLYPLPRTMHQQ 321
Cdd:cd00085    24 EGLEVDHIIPLSDGGNNDLDNLVLLCRKCHRK 55
HNHc smart00507
HNH nucleases;
290-320 3.29e-03

HNH nucleases;


Pssm-ID: 214702 [Multi-domain]  Cd Length: 52  Bit Score: 35.13  E-value: 3.29e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2104952192  290 SAIDIHHVIPRERGGNNSFNNLYPLPRTMHQ 320
Cdd:smart00507  22 EGLEVDHIIPLSDGGNDDLDNLVLLCPKCHI 52
 
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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