multicopper oxidase (MCO) that couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water, and which may contain three cupredoxin domains that include one mononuclear and one trinuclear copper center
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence ...
317-698
0e+00
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence of calcium ions, PAD enzymes EC:3.5.3.15 catalyze the post-translational modification reaction responsible for the formation of citrulline residues: Protein L-arginine + H2O <=> Protein L-citrulline + NH3. Several types are recognized (and included in the family) on the basis of molecular mass, substrate specificity, and tissue localization. The expression of type I PAD is known to be under the control of oestrogen.
:
Pssm-ID: 460794 Cd Length: 393 Bit Score: 631.18 E-value: 0e+00
Protein-arginine deiminase (PAD) middle domain; This family represents the central ...
136-307
3.54e-83
Protein-arginine deiminase (PAD) middle domain; This family represents the central non-catalytic domain of protein-arginine deiminase. This domain has an immunoglobulin-like fold.
:
Pssm-ID: 462510 Cd Length: 159 Bit Score: 259.74 E-value: 3.54e-83
Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal ...
30-134
9.56e-35
Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal non-catalytic domain of protein-arginine deiminase. This domain has a cupredoxin-like fold.
The actual alignment was detected with superfamily member pfam08526:
Pssm-ID: 462509 Cd Length: 113 Bit Score: 127.68 E-value: 9.56e-35
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence ...
317-698
0e+00
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence of calcium ions, PAD enzymes EC:3.5.3.15 catalyze the post-translational modification reaction responsible for the formation of citrulline residues: Protein L-arginine + H2O <=> Protein L-citrulline + NH3. Several types are recognized (and included in the family) on the basis of molecular mass, substrate specificity, and tissue localization. The expression of type I PAD is known to be under the control of oestrogen.
Pssm-ID: 460794 Cd Length: 393 Bit Score: 631.18 E-value: 0e+00
Protein-arginine deiminase (PAD) middle domain; This family represents the central ...
136-307
3.54e-83
Protein-arginine deiminase (PAD) middle domain; This family represents the central non-catalytic domain of protein-arginine deiminase. This domain has an immunoglobulin-like fold.
Pssm-ID: 462510 Cd Length: 159 Bit Score: 259.74 E-value: 3.54e-83
Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal ...
30-134
9.56e-35
Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal non-catalytic domain of protein-arginine deiminase. This domain has a cupredoxin-like fold.
Pssm-ID: 462509 Cd Length: 113 Bit Score: 127.68 E-value: 9.56e-35
N-terminal non-catalytic domain of protein-arginine deiminase; The N-terminal non-catalytic ...
33-135
8.66e-28
N-terminal non-catalytic domain of protein-arginine deiminase; The N-terminal non-catalytic domain of protein-arginine deiminase has a cupredoxin-like fold, but lacks the Cu binding site. PAD (protein-arginine deiminase) and protein L-arginine iminohydrolase catalyze the conversion of protein arginine residues to citrulline residues post-translationally in a process called citrullination. The modification plays crucial regulatory roles in development and cell differentiation.
Pssm-ID: 259876 Cd Length: 108 Bit Score: 107.85 E-value: 8.66e-28
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence ...
317-698
0e+00
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence of calcium ions, PAD enzymes EC:3.5.3.15 catalyze the post-translational modification reaction responsible for the formation of citrulline residues: Protein L-arginine + H2O <=> Protein L-citrulline + NH3. Several types are recognized (and included in the family) on the basis of molecular mass, substrate specificity, and tissue localization. The expression of type I PAD is known to be under the control of oestrogen.
Pssm-ID: 460794 Cd Length: 393 Bit Score: 631.18 E-value: 0e+00
Protein-arginine deiminase (PAD) middle domain; This family represents the central ...
136-307
3.54e-83
Protein-arginine deiminase (PAD) middle domain; This family represents the central non-catalytic domain of protein-arginine deiminase. This domain has an immunoglobulin-like fold.
Pssm-ID: 462510 Cd Length: 159 Bit Score: 259.74 E-value: 3.54e-83
Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal ...
30-134
9.56e-35
Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal non-catalytic domain of protein-arginine deiminase. This domain has a cupredoxin-like fold.
Pssm-ID: 462509 Cd Length: 113 Bit Score: 127.68 E-value: 9.56e-35
N-terminal non-catalytic domain of protein-arginine deiminase; The N-terminal non-catalytic ...
33-135
8.66e-28
N-terminal non-catalytic domain of protein-arginine deiminase; The N-terminal non-catalytic domain of protein-arginine deiminase has a cupredoxin-like fold, but lacks the Cu binding site. PAD (protein-arginine deiminase) and protein L-arginine iminohydrolase catalyze the conversion of protein arginine residues to citrulline residues post-translationally in a process called citrullination. The modification plays crucial regulatory roles in development and cell differentiation.
Pssm-ID: 259876 Cd Length: 108 Bit Score: 107.85 E-value: 8.66e-28
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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of your query sequence and the protein sequences used to curate the domain model,
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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
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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.
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
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Domains are color coded according to superfamilies
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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.
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)
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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.
(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
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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
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