SET domain found in SET domain-containing protein 3 (SETD3) and similar proteins; SETD3 (EC 2. ...
80-329
6.83e-162
SET domain found in SET domain-containing protein 3 (SETD3) and similar proteins; SETD3 (EC 2.1.1.43) is a histone-lysine N-methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3 (H3K4me and H3K36me). It functions as a transcriptional activator that plays an important role in the transcriptional regulation of muscle cell differentiation via interaction with MYOD1.
:
Pssm-ID: 380953 Cd Length: 251 Bit Score: 462.11 E-value: 6.83e-162
Rubisco LSMT substrate-binding; Members of this family adopt a multihelical structure, with an ...
344-475
9.59e-35
Rubisco LSMT substrate-binding; Members of this family adopt a multihelical structure, with an irregular array of long and short alpha-helices. They allow binding of the protein to substrate, such as the N-terminal tails of histones H3 and H4 and the large subunit of the Rubisco holoenzyme complex.
:
Pssm-ID: 462737 Cd Length: 130 Bit Score: 127.92 E-value: 9.59e-35
SET domain found in SET domain-containing protein 3 (SETD3) and similar proteins; SETD3 (EC 2. ...
80-329
6.83e-162
SET domain found in SET domain-containing protein 3 (SETD3) and similar proteins; SETD3 (EC 2.1.1.43) is a histone-lysine N-methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3 (H3K4me and H3K36me). It functions as a transcriptional activator that plays an important role in the transcriptional regulation of muscle cell differentiation via interaction with MYOD1.
Pssm-ID: 380953 Cd Length: 251 Bit Score: 462.11 E-value: 6.83e-162
Rubisco LSMT substrate-binding; Members of this family adopt a multihelical structure, with an ...
344-475
9.59e-35
Rubisco LSMT substrate-binding; Members of this family adopt a multihelical structure, with an irregular array of long and short alpha-helices. They allow binding of the protein to substrate, such as the N-terminal tails of histones H3 and H4 and the large subunit of the Rubisco holoenzyme complex.
Pssm-ID: 462737 Cd Length: 130 Bit Score: 127.92 E-value: 9.59e-35
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
105-137
8.78e-03
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure.
Pssm-ID: 459965 [Multi-domain] Cd Length: 115 Bit Score: 36.35 E-value: 8.78e-03
SET domain found in SET domain-containing protein 3 (SETD3) and similar proteins; SETD3 (EC 2. ...
80-329
6.83e-162
SET domain found in SET domain-containing protein 3 (SETD3) and similar proteins; SETD3 (EC 2.1.1.43) is a histone-lysine N-methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3 (H3K4me and H3K36me). It functions as a transcriptional activator that plays an important role in the transcriptional regulation of muscle cell differentiation via interaction with MYOD1.
Pssm-ID: 380953 Cd Length: 251 Bit Score: 462.11 E-value: 6.83e-162
SET domain found in Rubisco large subunit methyltransferase (LSMT) and similar proteins; ...
95-327
3.21e-62
SET domain found in Rubisco large subunit methyltransferase (LSMT) and similar proteins; Rubisco LSMT is a non-histone protein methyl transferase responsible for the trimethylation of lysine14 in the large subunit of Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase). The family also includes SET domain-containing proteins, SETD3, SETD4 and SETD6, which belong to methyltransferase class VII that represents classical non-histone SET domain methyltransferases. Members in this family contain a SET domain and a C-terminal RubisCO LSMT substrate-binding (Rubis-subs-bind) domain.
Pssm-ID: 380925 [Multi-domain] Cd Length: 236 Bit Score: 205.38 E-value: 3.21e-62
SET domain found in SET domain-containing protein 4 (SETD4) and similar proteins; SETD4 is a ...
99-327
5.45e-41
SET domain found in SET domain-containing protein 4 (SETD4) and similar proteins; SETD4 is a cytosolic and nuclear functional lysine methyltransferase that plays a crucial role in breast carcinogenesis. However, its specific substrates and modification sites remain to be disclosed.
Pssm-ID: 380954 [Multi-domain] Cd Length: 245 Bit Score: 148.99 E-value: 5.45e-41
SET domain found in Schizosaccharomyces pombe SET domain-containing protein 10 (SETD10) and ...
84-328
5.94e-40
SET domain found in Schizosaccharomyces pombe SET domain-containing protein 10 (SETD10) and similar proteins; Schizosaccharomyces pombe SETD10 is a ribosomal S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates ribosomal protein L23 (rpl23a and rpl23b).
Pssm-ID: 380957 Cd Length: 252 Bit Score: 146.33 E-value: 5.94e-40
SET domain found in chloroplastic ribulose-1,5 bisphosphate carboxylase/oxygenase large ...
96-327
2.97e-39
SET domain found in chloroplastic ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase (RBCMT) and similar proteins; RBCMT (EC 2.1.1.127; also termed [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase, RuBisCO LSMT, RuBisCO methyltransferase, or rbcMT) methylates 'Lys-14' of the large subunit of RuBisCO.
Pssm-ID: 380956 Cd Length: 237 Bit Score: 143.99 E-value: 2.97e-39
Rubisco LSMT substrate-binding; Members of this family adopt a multihelical structure, with an ...
344-475
9.59e-35
Rubisco LSMT substrate-binding; Members of this family adopt a multihelical structure, with an irregular array of long and short alpha-helices. They allow binding of the protein to substrate, such as the N-terminal tails of histones H3 and H4 and the large subunit of the Rubisco holoenzyme complex.
Pssm-ID: 462737 Cd Length: 130 Bit Score: 127.92 E-value: 9.59e-35
SET domain found in SET domain-containing protein 6 (SETD6) and similar proteins; SETD6 is a ...
105-327
8.76e-28
SET domain found in SET domain-containing protein 6 (SETD6) and similar proteins; SETD6 is a lysine N-methyltransferase that monomethylates 'Lys-310' of the RELA subunit of NF-kappa-B complex, leading to down-regulate NF-kappa-B transcription factor activity. It also monomethylates 'Lys-8' of H2AZ (H2AZK8me1).
Pssm-ID: 380955 [Multi-domain] Cd Length: 250 Bit Score: 112.01 E-value: 8.76e-28
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
105-137
8.78e-03
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure.
Pssm-ID: 459965 [Multi-domain] Cd Length: 115 Bit Score: 36.35 E-value: 8.78e-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.
Click on the triangle to view details about the feature, including a multiple sequence alignment
of your query sequence and the protein sequences used to curate the domain model,
where hash marks (#) above the aligned sequences show the location of the conserved feature residues.
The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
Functional characterization of the conserved domain architecture found on the query.
Click here to see more details.
This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
(labeled illustration) or all hits
(labeled illustration).
Domains are color coded according to superfamilies
to which they have been assigned. Hits with scores that pass a domain-specific threshold
(specific hits) are drawn in bright colors.
Others (non-specific hits) and
superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features),
they are mapped to the query sequence and indicated through sets of triangles
with the same color and shade of the domain or superfamily that provides the annotation. Mouse over the colored bars or triangles to see descriptions of the domains and features.
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.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
mapped to the query sequence.
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.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
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
non-specific hits
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
(CDART).
Modify your query to search against a different database and/or use advanced search options
