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Conserved domains on  [gi|2783091225|ref|WP_369010154|]
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HNH endonuclease [Caldibacillus thermoamylovorans]

Protein Classification

HNH endonuclease family protein( domain architecture ID 1640)

HNH endonuclease family protein, similar to Physarum polycephalum intron-encoded endonuclease I-Ppoi which mediates the mobility of intron 3 in the ribosomal DNA

EC:  3.1.-.-
Gene Ontology:  GO:0004519

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HNHc super family cl00083
HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic ...
1-35 2.78e-09

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.


The actual alignment was detected with superfamily member pfam14414:

Pssm-ID: 469607  Cd Length: 43  Bit Score: 45.84  E-value: 2.78e-09
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 2783091225  1 MAWHHTEVPGKMELVPFGIHNITIHNGGRSTGMWA 35
Cdd:pfam14414  9 YTWHHLDDTGTMQLVPEELHNATPHTGGVSLWKKG 43
 
Name Accession Description Interval E-value
WHH pfam14414
A nuclease of the HNH/ENDO VII superfamily with conserved WHH; WHH is a predicted nuclease of ...
1-35 2.78e-09

A nuclease of the HNH/ENDO VII superfamily with conserved WHH; WHH is a predicted nuclease of the HNH/ENDO VII superfamily of the treble clef fold. The name is derived from the conserved motif WHH. It is found in bacterial polymorphic toxin systems and functions as a toxin module. WHH is the shortest version of HNH nuclease families. Like AHH and LHH, the WHH nuclease contains 4 conserved histidines of which the first one is predicted to bind a metal-ion and other three ones are involved in activation of water molecule for hydrolysis.


Pssm-ID: 433943  Cd Length: 43  Bit Score: 45.84  E-value: 2.78e-09
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 2783091225  1 MAWHHTEVPGKMELVPFGIHNITIHNGGRSTGMWA 35
Cdd:pfam14414  9 YTWHHLDDTGTMQLVPEELHNATPHTGGVSLWKKG 43
 
Name Accession Description Interval E-value
WHH pfam14414
A nuclease of the HNH/ENDO VII superfamily with conserved WHH; WHH is a predicted nuclease of ...
1-35 2.78e-09

A nuclease of the HNH/ENDO VII superfamily with conserved WHH; WHH is a predicted nuclease of the HNH/ENDO VII superfamily of the treble clef fold. The name is derived from the conserved motif WHH. It is found in bacterial polymorphic toxin systems and functions as a toxin module. WHH is the shortest version of HNH nuclease families. Like AHH and LHH, the WHH nuclease contains 4 conserved histidines of which the first one is predicted to bind a metal-ion and other three ones are involved in activation of water molecule for hydrolysis.


Pssm-ID: 433943  Cd Length: 43  Bit Score: 45.84  E-value: 2.78e-09
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 2783091225  1 MAWHHTEVPGKMELVPFGIHNITIHNGGRSTGMWA 35
Cdd:pfam14414  9 YTWHHLDDTGTMQLVPEELHNATPHTGGVSLWKKG 43
Colicin-DNase pfam12639
DNase/tRNase domain of colicin-like bacteriocin; Colicin-like bacteriocins are complex ...
3-27 6.93e-05

DNase/tRNase domain of colicin-like bacteriocin; Colicin-like bacteriocins are complex structures with an N-terminal beta-barrel translocation domain (pfam09000), a long double-alpha-helical receptor-binding domain (pfam11570) and this C-terminal RNAse/DNase domain with endonuclease activity. Their competitor bacteriocidal action is by a process that involves binding to a surface receptor, entering the cell, and, finally, killing it. The lethal action of colicin E3 is a specific cleavage in the ribosomal decoding A site. The crystal structure of colicin E3 reveals a Y-shaped molecule with the receptor binding domain forming a 100 Angstrom long stalk and the two globular heads of the translocation domain and this catalytic domain comprising the two arms.


Pssm-ID: 432688  Cd Length: 96  Bit Score: 35.91  E-value: 6.93e-05
                         10        20
                 ....*....|....*....|....*
gi 2783091225  3 WHHTEVPGKMELVPFGIHNITIHNG 27
Cdd:pfam12639 72 WHHHQDTGTMQLVPTEIHDKTGHTG 96
 
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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