DEUBAD domain found in nuclear factor related to kappa-B-binding protein (NFRKB) and similar ...
55-166
3.00e-53
DEUBAD domain found in nuclear factor related to kappa-B-binding protein (NFRKB) and similar proteins; NFRKB, also called DNA-binding protein R kappa-B, or INO80 complex subunit G (INO80G), is a regulatory component of the metazoan INO80 complex involved in chromatin remodeling, transcription regulation, DNA replication and DNA repair. It modulates the deubiquitinase activity of UCHL5 in the INO80 complex. It binds to the DNA consensus sequence 5'-GGGGAATCTCC-3'. The model corresponds to the DEUBAD domain (conserved domain within the UCH regulatory proteins RPN13, NFRKB/INO80G, and ASX) of NFRKB, which binds primarily to the C-terminal ULD domain of UCH-L5.
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Pssm-ID: 439381 Cd Length: 112 Bit Score: 181.64 E-value: 3.00e-53
DEUBAD domain found in nuclear factor related to kappa-B-binding protein (NFRKB) and similar ...
55-166
3.00e-53
DEUBAD domain found in nuclear factor related to kappa-B-binding protein (NFRKB) and similar proteins; NFRKB, also called DNA-binding protein R kappa-B, or INO80 complex subunit G (INO80G), is a regulatory component of the metazoan INO80 complex involved in chromatin remodeling, transcription regulation, DNA replication and DNA repair. It modulates the deubiquitinase activity of UCHL5 in the INO80 complex. It binds to the DNA consensus sequence 5'-GGGGAATCTCC-3'. The model corresponds to the DEUBAD domain (conserved domain within the UCH regulatory proteins RPN13, NFRKB/INO80G, and ASX) of NFRKB, which binds primarily to the C-terminal ULD domain of UCH-L5.
Pssm-ID: 439381 Cd Length: 112 Bit Score: 181.64 E-value: 3.00e-53
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
802-986
4.53e-03
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.
Pssm-ID: 411776 [Multi-domain] Cd Length: 511 Bit Score: 41.07 E-value: 4.53e-03
DEUBAD domain found in nuclear factor related to kappa-B-binding protein (NFRKB) and similar ...
55-166
3.00e-53
DEUBAD domain found in nuclear factor related to kappa-B-binding protein (NFRKB) and similar proteins; NFRKB, also called DNA-binding protein R kappa-B, or INO80 complex subunit G (INO80G), is a regulatory component of the metazoan INO80 complex involved in chromatin remodeling, transcription regulation, DNA replication and DNA repair. It modulates the deubiquitinase activity of UCHL5 in the INO80 complex. It binds to the DNA consensus sequence 5'-GGGGAATCTCC-3'. The model corresponds to the DEUBAD domain (conserved domain within the UCH regulatory proteins RPN13, NFRKB/INO80G, and ASX) of NFRKB, which binds primarily to the C-terminal ULD domain of UCH-L5.
Pssm-ID: 439381 Cd Length: 112 Bit Score: 181.64 E-value: 3.00e-53
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
802-986
4.53e-03
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.
Pssm-ID: 411776 [Multi-domain] Cd Length: 511 Bit Score: 41.07 E-value: 4.53e-03
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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