Restriction endonuclease MutH and similar endonucleases; MutH is a 28kD endonuclease involved ...
13-220
8.45e-129
Restriction endonuclease MutH and similar endonucleases; MutH is a 28kD endonuclease involved in methyl-directed DNA mismatch repair in gram negative bacteria. MutH is both sequence-specific and methylation-specific, introducing a nick in the unmethylated strand of a hemi-methylated d(GATC) DNA duplex. MutH is homologous to the type II restriction endonuclease Sau3AI which also recognizes the d(GATC) sequence however, Sau3AI cleaves both strands regardless of their methylation state. The active form of MutH is monomeric while that of Sau3AI is homodimeric. In addition to MutH, MutS, involved in mismatch recognition, and MutL, involved in mediating the interactions between MutH and MutS, are essential in initiating mismatch repair in Escherichia coli.
Pssm-ID: 411704 Cd Length: 208 Bit Score: 361.79 E-value: 8.45e-129
DNA mismatch repair endonuclease MutH; This family consists exclusively of MutH, an ...
6-221
5.56e-95
DNA mismatch repair endonuclease MutH; This family consists exclusively of MutH, an endonuclease in some Proteobacteria that is activated by MutS1 and MutL for methylation-directed mismatch repair. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 131302 Cd Length: 217 Bit Score: 276.33 E-value: 5.56e-95
DNA mismatch repair enzyme MutH; MutS, MutL and MutH are the three essential proteins for ...
54-152
2.69e-44
DNA mismatch repair enzyme MutH; MutS, MutL and MutH are the three essential proteins for initiation of methyl-directed DNA mismatch repair to correct mistakes made during DNA replication in Escherichia coli. MutH cleaves a newly synthesized and unmethylated daughter strand 5' to the sequence d(GATC) in a hemi-methylated duplex. Activation of MutH requires the recognition of a DNA mismatch by MutS and MutL.
Pssm-ID: 214917 Cd Length: 100 Bit Score: 143.51 E-value: 2.69e-44
Sau3AI family type II restriction endonuclease; Members of this family include type II ...
8-217
2.88e-15
Sau3AI family type II restriction endonuclease; Members of this family include type II restriction enzymes such as Sau3AI, while excluding proteins more closely related to the DNA repair protein MutH. Both Sau3AI and MutH endonucleases act on GATC sequences.
Pssm-ID: 468903 [Multi-domain] Cd Length: 464 Bit Score: 73.83 E-value: 2.88e-15
Restriction endonuclease MutH and similar endonucleases; MutH is a 28kD endonuclease involved ...
13-220
8.45e-129
Restriction endonuclease MutH and similar endonucleases; MutH is a 28kD endonuclease involved in methyl-directed DNA mismatch repair in gram negative bacteria. MutH is both sequence-specific and methylation-specific, introducing a nick in the unmethylated strand of a hemi-methylated d(GATC) DNA duplex. MutH is homologous to the type II restriction endonuclease Sau3AI which also recognizes the d(GATC) sequence however, Sau3AI cleaves both strands regardless of their methylation state. The active form of MutH is monomeric while that of Sau3AI is homodimeric. In addition to MutH, MutS, involved in mismatch recognition, and MutL, involved in mediating the interactions between MutH and MutS, are essential in initiating mismatch repair in Escherichia coli.
Pssm-ID: 411704 Cd Length: 208 Bit Score: 361.79 E-value: 8.45e-129
DNA mismatch repair endonuclease MutH; This family consists exclusively of MutH, an ...
6-221
5.56e-95
DNA mismatch repair endonuclease MutH; This family consists exclusively of MutH, an endonuclease in some Proteobacteria that is activated by MutS1 and MutL for methylation-directed mismatch repair. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 131302 Cd Length: 217 Bit Score: 276.33 E-value: 5.56e-95
DNA mismatch repair enzyme MutH; MutS, MutL and MutH are the three essential proteins for ...
54-152
2.69e-44
DNA mismatch repair enzyme MutH; MutS, MutL and MutH are the three essential proteins for initiation of methyl-directed DNA mismatch repair to correct mistakes made during DNA replication in Escherichia coli. MutH cleaves a newly synthesized and unmethylated daughter strand 5' to the sequence d(GATC) in a hemi-methylated duplex. Activation of MutH requires the recognition of a DNA mismatch by MutS and MutL.
Pssm-ID: 214917 Cd Length: 100 Bit Score: 143.51 E-value: 2.69e-44
N-terminal catalytic domain of type II restriction enzyme Sau3AI and similar endonucleases; ...
24-209
1.81e-26
N-terminal catalytic domain of type II restriction enzyme Sau3AI and similar endonucleases; Sau3AI is a type II restriction enzyme that recognizes the 5'-|GATC-3' sequence in double-strand DNA (| denotes the cleavage site). The N-terminal domain modeled here conveys the catalytic activity, it belongs to a superfamily of nucleases including very short patch repair (Vsr) endonucleases, archaeal Holliday junction resolvases, MutH methyl-directed DNA mismatch-repair endonucleases, and catalytic domains of many restriction endonucleases, such as EcoRI, BamHI, and FokI.
Pssm-ID: 411760 Cd Length: 188 Bit Score: 100.71 E-value: 1.81e-26
Sau3AI family type II restriction endonuclease; Members of this family include type II ...
8-217
2.88e-15
Sau3AI family type II restriction endonuclease; Members of this family include type II restriction enzymes such as Sau3AI, while excluding proteins more closely related to the DNA repair protein MutH. Both Sau3AI and MutH endonucleases act on GATC sequences.
Pssm-ID: 468903 [Multi-domain] Cd Length: 464 Bit Score: 73.83 E-value: 2.88e-15
C-terminal allosteric effector domain of the restriction endonuclease Sau3AI; Sau3AI is a type ...
21-218
3.64e-05
C-terminal allosteric effector domain of the restriction endonuclease Sau3AI; Sau3AI is a type II restriction enzyme that recognizes the 5'-|GATC-3' sequence in double-strand DNA (| denotes the cleavage site). The C-terminal domain modeled here does not have catalytic activity, it functions as an allosteric effector domain that assists in DNA binding and cleavage. It belongs to a superfamily of nucleases including very short patch repair (Vsr) endonucleases, archaeal Holliday junction resolvases, MutH methy-directed DNA mismatch-repair endonucleases, and catalytic domains of many restriction endonucleases, such as EcoRI, BamHI, and FokI.
Pssm-ID: 411759 Cd Length: 214 Bit Score: 43.35 E-value: 3.64e-05
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
