NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1866606268]
View 

Chain A, Deoxynucleotidyltransferase terminal-interacting protein 1

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DNTTIP1_dimer pfam18192
DNTTIP1 dimerization domain; This is the N-terminal domain of DNTTIP1, a protein that forms ...
 65-130 5.56e-30

DNTTIP1 dimerization domain; This is the N-terminal domain of DNTTIP1, a protein that forms part of a novel histone deacetylase complex present in Homo sapiens. Histone deacetylase complexes comprise DNTTIP1, histone deacetylase (HDAC) and the repressor protein MIDEAS. The acetylation of histone tails plays a critical role in determining the accessibility of chromatin to transcriptional regulators and RNA polymerase complexes. This N-terminal domain is responsible for dimerization of histone deacetylase 1(HDAC1). The N-terminal domain also interacts and mediates the assembly of the HDAC1- MIDEAS complex.


:

Pssm-ID: 408020  Cd Length: 69  Bit Score: 102.85  E-value: 5.56e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1866606268  65 ISMDLLRAVLQPSINEEIQTVFNKYM-KFFQKAALNVRDNVGEEVDAEQLIQEACRSCLEQAKLLFS 130
Cdd:pfam18192   1 KSLDLLRQVVQPAINKEIQEVIKKYMeKFFKPAAENIRENLGEEVVNEDLIQAACRSILENAKLLFS 67
 
Name Accession Description Interval E-value
DNTTIP1_dimer pfam18192
DNTTIP1 dimerization domain; This is the N-terminal domain of DNTTIP1, a protein that forms ...
 65-130 5.56e-30

DNTTIP1 dimerization domain; This is the N-terminal domain of DNTTIP1, a protein that forms part of a novel histone deacetylase complex present in Homo sapiens. Histone deacetylase complexes comprise DNTTIP1, histone deacetylase (HDAC) and the repressor protein MIDEAS. The acetylation of histone tails plays a critical role in determining the accessibility of chromatin to transcriptional regulators and RNA polymerase complexes. This N-terminal domain is responsible for dimerization of histone deacetylase 1(HDAC1). The N-terminal domain also interacts and mediates the assembly of the HDAC1- MIDEAS complex.


Pssm-ID: 408020  Cd Length: 69  Bit Score: 102.85  E-value: 5.56e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1866606268  65 ISMDLLRAVLQPSINEEIQTVFNKYM-KFFQKAALNVRDNVGEEVDAEQLIQEACRSCLEQAKLLFS 130
Cdd:pfam18192   1 KSLDLLRQVVQPAINKEIQEVIKKYMeKFFKPAAENIRENLGEEVVNEDLIQAACRSILENAKLLFS 67
 
Name Accession Description Interval E-value
DNTTIP1_dimer pfam18192
DNTTIP1 dimerization domain; This is the N-terminal domain of DNTTIP1, a protein that forms ...
 65-130 5.56e-30

DNTTIP1 dimerization domain; This is the N-terminal domain of DNTTIP1, a protein that forms part of a novel histone deacetylase complex present in Homo sapiens. Histone deacetylase complexes comprise DNTTIP1, histone deacetylase (HDAC) and the repressor protein MIDEAS. The acetylation of histone tails plays a critical role in determining the accessibility of chromatin to transcriptional regulators and RNA polymerase complexes. This N-terminal domain is responsible for dimerization of histone deacetylase 1(HDAC1). The N-terminal domain also interacts and mediates the assembly of the HDAC1- MIDEAS complex.


Pssm-ID: 408020  Cd Length: 69  Bit Score: 102.85  E-value: 5.56e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1866606268  65 ISMDLLRAVLQPSINEEIQTVFNKYM-KFFQKAALNVRDNVGEEVDAEQLIQEACRSCLEQAKLLFS 130
Cdd:pfam18192   1 KSLDLLRQVVQPAINKEIQEVIKKYMeKFFKPAAENIRENLGEEVVNEDLIQAACRSILENAKLLFS 67
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH