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Conserved domains on  [gi|197099936|ref|NP_001124534|]
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histone deacetylase complex subunit SAP30L isoform 2 [Homo sapiens]

Protein Classification

histone deacetylase complex subunit SAP30 Sin3-binding domain-containing protein( domain architecture ID 10341280)

histone deacetylase complex subunit SAP30 Sin3-binding domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAP30_Sin3_bdg pfam13867
Sin3 binding region of histone deacetylase complex subunit SAP30; This C-terminal domain of ...
 73-125 2.54e-27

Sin3 binding region of histone deacetylase complex subunit SAP30; This C-terminal domain of the SAP30 proteins appears to be the binding region for Sin3.


:

Pssm-ID: 464006  Cd Length: 53  Bit Score: 96.08  E-value: 2.54e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 197099936   73 LQVNTLRRYKRHYKLQTRPGFNKAQLAETVSRHFRNIPVNEKETLAYFIYMVK 125
Cdd:pfam13867   1 LQTNTLRRYKRHYKLQVRPGSSKEQLVEAVQRHFAAQPVDEKEVITSFIYAVK 53
zf-SAP30 super family cl16442
SAP30 zinc-finger; SAP30 is a subunit of the histone deacetylase complex, and this domain is a ...
 24-68 5.12e-21

SAP30 zinc-finger; SAP30 is a subunit of the histone deacetylase complex, and this domain is a zinc-finger. Solution of the structure shows a novel fold comprising two beta-strands and two alpha-helices with the zinc organizing centre showing remote resemblance to the treble clef motif. In silico analysis of the structure revealed a highly conserved surface dominated by basic residues. NMR-based analysis of potential ligands for the SAP30 zn-finger motif indicated a strong preference for nucleic acid substrates. The zinc-finger of SAP3 probably functions as a double-stranded DNA-binding motif, thereby expanding the known functions of both SAP30 and the mammalian Sin3 co-repressor complex.


The actual alignment was detected with superfamily member pfam13866:

Pssm-ID: 404707  Cd Length: 72  Bit Score: 80.55  E-value: 5.12e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 197099936   24 GYGQSCCLIEDGERCVRPAGNASFSKRVQKSISQKKLKLDIDKSV 68
Cdd:pfam13866   1 ESDQICCLVDDGERCTRPAGNASYSKRIQKTVAQKKLKLSIDSTA 45
 
Name Accession Description Interval E-value
SAP30_Sin3_bdg pfam13867
Sin3 binding region of histone deacetylase complex subunit SAP30; This C-terminal domain of ...
 73-125 2.54e-27

Sin3 binding region of histone deacetylase complex subunit SAP30; This C-terminal domain of the SAP30 proteins appears to be the binding region for Sin3.


Pssm-ID: 464006  Cd Length: 53  Bit Score: 96.08  E-value: 2.54e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 197099936   73 LQVNTLRRYKRHYKLQTRPGFNKAQLAETVSRHFRNIPVNEKETLAYFIYMVK 125
Cdd:pfam13867   1 LQTNTLRRYKRHYKLQVRPGSSKEQLVEAVQRHFAAQPVDEKEVITSFIYAVK 53
zf-SAP30 pfam13866
SAP30 zinc-finger; SAP30 is a subunit of the histone deacetylase complex, and this domain is a ...
 24-68 5.12e-21

SAP30 zinc-finger; SAP30 is a subunit of the histone deacetylase complex, and this domain is a zinc-finger. Solution of the structure shows a novel fold comprising two beta-strands and two alpha-helices with the zinc organizing centre showing remote resemblance to the treble clef motif. In silico analysis of the structure revealed a highly conserved surface dominated by basic residues. NMR-based analysis of potential ligands for the SAP30 zn-finger motif indicated a strong preference for nucleic acid substrates. The zinc-finger of SAP3 probably functions as a double-stranded DNA-binding motif, thereby expanding the known functions of both SAP30 and the mammalian Sin3 co-repressor complex.


Pssm-ID: 404707  Cd Length: 72  Bit Score: 80.55  E-value: 5.12e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 197099936   24 GYGQSCCLIEDGERCVRPAGNASFSKRVQKSISQKKLKLDIDKSV 68
Cdd:pfam13866   1 ESDQICCLVDDGERCTRPAGNASYSKRIQKTVAQKKLKLSIDSTA 45
 
Name Accession Description Interval E-value
SAP30_Sin3_bdg pfam13867
Sin3 binding region of histone deacetylase complex subunit SAP30; This C-terminal domain of ...
 73-125 2.54e-27

Sin3 binding region of histone deacetylase complex subunit SAP30; This C-terminal domain of the SAP30 proteins appears to be the binding region for Sin3.


Pssm-ID: 464006  Cd Length: 53  Bit Score: 96.08  E-value: 2.54e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 197099936   73 LQVNTLRRYKRHYKLQTRPGFNKAQLAETVSRHFRNIPVNEKETLAYFIYMVK 125
Cdd:pfam13867   1 LQTNTLRRYKRHYKLQVRPGSSKEQLVEAVQRHFAAQPVDEKEVITSFIYAVK 53
zf-SAP30 pfam13866
SAP30 zinc-finger; SAP30 is a subunit of the histone deacetylase complex, and this domain is a ...
 24-68 5.12e-21

SAP30 zinc-finger; SAP30 is a subunit of the histone deacetylase complex, and this domain is a zinc-finger. Solution of the structure shows a novel fold comprising two beta-strands and two alpha-helices with the zinc organizing centre showing remote resemblance to the treble clef motif. In silico analysis of the structure revealed a highly conserved surface dominated by basic residues. NMR-based analysis of potential ligands for the SAP30 zn-finger motif indicated a strong preference for nucleic acid substrates. The zinc-finger of SAP3 probably functions as a double-stranded DNA-binding motif, thereby expanding the known functions of both SAP30 and the mammalian Sin3 co-repressor complex.


Pssm-ID: 404707  Cd Length: 72  Bit Score: 80.55  E-value: 5.12e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 197099936   24 GYGQSCCLIEDGERCVRPAGNASFSKRVQKSISQKKLKLDIDKSV 68
Cdd:pfam13866   1 ESDQICCLVDDGERCTRPAGNASYSKRIQKTVAQKKLKLSIDSTA 45
 
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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