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Conserved domains on  [gi|26331036|dbj|BAC29248|]
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unnamed protein product, partial [Mus musculus]

Protein Classification

E3 ubiquitin-protein ligase MSL2( domain architecture ID 11245019)

E3 ubiquitin-protein ligase MSL2 is a component of the histone acetyltransferase complex responsible for the majority of histone H4 acetylation at lysine 16 which is implicated in the formation of higher-order chromatin structure

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MSL2-CXC pfam16682
CXC domain of E3 ubiquitin-protein ligase MSL2; MSL2-CXC is an autonomously folded domain ...
 34-88 6.92e-23

CXC domain of E3 ubiquitin-protein ligase MSL2; MSL2-CXC is an autonomously folded domain containing that binds three zinc ions. It lies on the E3 ubiquitin-protein ligase MSL2 in eukaryotes. The CXC domain critically contributes to the DNA-binding activity of MSL2. It carries 9 invariant cysteines within about a 50 residue region.


:

Pssm-ID: 435512  Cd Length: 55  Bit Score: 85.18  E-value: 6.92e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 26331036    34 KPQEKKGCKCGRATQNPSVLTCRGQRCPCYSNRKACLDCICRGCQNSYMANGEKK 88
Cdd:pfam16682   1 KPPEKKGCRCGTSTPTPPKLTCRNQRCPCYSNGKSCTDCKCRGCKNPHKADSIDS 55
 
Name Accession Description Interval E-value
MSL2-CXC pfam16682
CXC domain of E3 ubiquitin-protein ligase MSL2; MSL2-CXC is an autonomously folded domain ...
 34-88 6.92e-23

CXC domain of E3 ubiquitin-protein ligase MSL2; MSL2-CXC is an autonomously folded domain containing that binds three zinc ions. It lies on the E3 ubiquitin-protein ligase MSL2 in eukaryotes. The CXC domain critically contributes to the DNA-binding activity of MSL2. It carries 9 invariant cysteines within about a 50 residue region.


Pssm-ID: 435512  Cd Length: 55  Bit Score: 85.18  E-value: 6.92e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 26331036    34 KPQEKKGCKCGRATQNPSVLTCRGQRCPCYSNRKACLDCICRGCQNSYMANGEKK 88
Cdd:pfam16682   1 KPPEKKGCRCGTSTPTPPKLTCRNQRCPCYSNGKSCTDCKCRGCKNPHKADSIDS 55
MSL2_CXC cd13122
DNA-binding cysteine-rich domain of male-specific lethal 2 and related proteins; The CXC ...
 35-84 1.63e-21

DNA-binding cysteine-rich domain of male-specific lethal 2 and related proteins; The CXC domain of Drosophila melanogaster MSL2 forms a Zn(3)Cys(9) cluster and is involved in recruiting members of the dosage compensation complex (DCC) to sites on the X chromosome.


Pssm-ID: 240555  Cd Length: 50  Bit Score: 81.67  E-value: 1.63e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 26331036  35 PQEKKGCKCGRATQNPSVLTCRGQRCPCYSNRKACLDCICRGCQNSYMAN 84
Cdd:cd13122   1 PPEKKGCRCGTATQSPGVLTCRGQRCPCYSNGKSCLDCKCRGCKNPHKAD 50
 
Name Accession Description Interval E-value
MSL2-CXC pfam16682
CXC domain of E3 ubiquitin-protein ligase MSL2; MSL2-CXC is an autonomously folded domain ...
 34-88 6.92e-23

CXC domain of E3 ubiquitin-protein ligase MSL2; MSL2-CXC is an autonomously folded domain containing that binds three zinc ions. It lies on the E3 ubiquitin-protein ligase MSL2 in eukaryotes. The CXC domain critically contributes to the DNA-binding activity of MSL2. It carries 9 invariant cysteines within about a 50 residue region.


Pssm-ID: 435512  Cd Length: 55  Bit Score: 85.18  E-value: 6.92e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 26331036    34 KPQEKKGCKCGRATQNPSVLTCRGQRCPCYSNRKACLDCICRGCQNSYMANGEKK 88
Cdd:pfam16682   1 KPPEKKGCRCGTSTPTPPKLTCRNQRCPCYSNGKSCTDCKCRGCKNPHKADSIDS 55
MSL2_CXC cd13122
DNA-binding cysteine-rich domain of male-specific lethal 2 and related proteins; The CXC ...
 35-84 1.63e-21

DNA-binding cysteine-rich domain of male-specific lethal 2 and related proteins; The CXC domain of Drosophila melanogaster MSL2 forms a Zn(3)Cys(9) cluster and is involved in recruiting members of the dosage compensation complex (DCC) to sites on the X chromosome.


Pssm-ID: 240555  Cd Length: 50  Bit Score: 81.67  E-value: 1.63e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 26331036  35 PQEKKGCKCGRATQNPSVLTCRGQRCPCYSNRKACLDCICRGCQNSYMAN 84
Cdd:cd13122   1 PPEKKGCRCGTATQSPGVLTCRGQRCPCYSNGKSCLDCKCRGCKNPHKAD 50
 
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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