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Conserved domains on  [gi|38454278|ref|NP_942065|]
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zinc finger MYND domain-containing protein 19 [Rattus norvegicus]

Protein Classification

SET and MYND domain-containing protein( domain architecture ID 11621033)

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) and zinc finger MYND domain-containing protein similar to human N-lysine methyltransferase SMYD2 and histone-lysine N-methyltransferase SMYD3

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
zf-MYND pfam01753
MYND finger;
174-212 1.36e-09

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 52.04  E-value: 1.36e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 38454278   174 CTVIEKQLREFNICGRCQVARYCGSQCQQKDWPAHKKHC 212
Cdd:pfam01753   1 CAVCGKEALKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
HNHc super family cl00083
HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic ...
66-105 3.63e-06

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 pfam13392:

Pssm-ID: 469607  Cd Length: 46  Bit Score: 42.58  E-value: 3.63e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 38454278    66 RLLHELLWERHRGGVAPGFQVVHLNAVTVDNRLDNLQLVP 105
Cdd:pfam13392   1 KYAHRVAWELHNGPIPDGMVVDHIDGDRRNNRPENLRLVT 40
 
Name Accession Description Interval E-value
zf-MYND pfam01753
MYND finger;
174-212 1.36e-09

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 52.04  E-value: 1.36e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 38454278   174 CTVIEKQLREFNICGRCQVARYCGSQCQQKDWPAHKKHC 212
Cdd:pfam01753   1 CAVCGKEALKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
HNH_3 pfam13392
HNH endonuclease; This is a zinc-binding loop of Fold group 7 as found in ...
66-105 3.63e-06

HNH endonuclease; This is a zinc-binding loop of Fold group 7 as found in endo-deoxy-ribonucleases and HNH nucleases.


Pssm-ID: 433169  Cd Length: 46  Bit Score: 42.58  E-value: 3.63e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 38454278    66 RLLHELLWERHRGGVAPGFQVVHLNAVTVDNRLDNLQLVP 105
Cdd:pfam13392   1 KYAHRVAWELHNGPIPDGMVVDHIDGDRRNNRPENLRLVT 40
 
Name Accession Description Interval E-value
zf-MYND pfam01753
MYND finger;
174-212 1.36e-09

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 52.04  E-value: 1.36e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 38454278   174 CTVIEKQLREFNICGRCQVARYCGSQCQQKDWPAHKKHC 212
Cdd:pfam01753   1 CAVCGKEALKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
HNH_3 pfam13392
HNH endonuclease; This is a zinc-binding loop of Fold group 7 as found in ...
66-105 3.63e-06

HNH endonuclease; This is a zinc-binding loop of Fold group 7 as found in endo-deoxy-ribonucleases and HNH nucleases.


Pssm-ID: 433169  Cd Length: 46  Bit Score: 42.58  E-value: 3.63e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 38454278    66 RLLHELLWERHRGGVAPGFQVVHLNAVTVDNRLDNLQLVP 105
Cdd:pfam13392   1 KYAHRVAWELHNGPIPDGMVVDHIDGDRRNNRPENLRLVT 40
 
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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