Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
158-381
2.36e-77
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.
:
Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 238.33 E-value: 2.36e-77
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
46-128
3.23e-41
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.
:
Pssm-ID: 214527 Cd Length: 83 Bit Score: 139.83 E-value: 3.23e-41
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
4-39
2.53e-12
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.
The actual alignment was detected with superfamily member pfam00051:
Pssm-ID: 412161 Cd Length: 79 Bit Score: 61.94 E-value: 2.53e-12
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
158-381
2.36e-77
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.
Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 238.33 E-value: 2.36e-77
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
157-378
8.54e-71
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.
Pssm-ID: 214473 Cd Length: 229 Bit Score: 221.40 E-value: 8.54e-71
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
46-128
3.23e-41
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.
Pssm-ID: 214527 Cd Length: 83 Bit Score: 139.83 E-value: 3.23e-41
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
46-127
8.70e-37
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.
Pssm-ID: 238056 Cd Length: 83 Bit Score: 128.26 E-value: 8.70e-37
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
48-126
4.39e-33
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.
Pssm-ID: 395005 Cd Length: 79 Bit Score: 118.56 E-value: 4.39e-33
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
4-39
2.53e-12
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.
Pssm-ID: 395005 Cd Length: 79 Bit Score: 61.94 E-value: 2.53e-12
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
4-41
2.52e-11
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.
Pssm-ID: 214527 Cd Length: 83 Bit Score: 59.33 E-value: 2.52e-11
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
4-39
4.48e-10
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.
Pssm-ID: 238056 Cd Length: 83 Bit Score: 55.85 E-value: 4.48e-10
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
158-381
2.36e-77
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.
Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 238.33 E-value: 2.36e-77
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
157-378
8.54e-71
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.
Pssm-ID: 214473 Cd Length: 229 Bit Score: 221.40 E-value: 8.54e-71
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
46-128
3.23e-41
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.
Pssm-ID: 214527 Cd Length: 83 Bit Score: 139.83 E-value: 3.23e-41
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
46-127
8.70e-37
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.
Pssm-ID: 238056 Cd Length: 83 Bit Score: 128.26 E-value: 8.70e-37
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
48-126
4.39e-33
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.
Pssm-ID: 395005 Cd Length: 79 Bit Score: 118.56 E-value: 4.39e-33
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
4-39
2.53e-12
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.
Pssm-ID: 395005 Cd Length: 79 Bit Score: 61.94 E-value: 2.53e-12
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
4-41
2.52e-11
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.
Pssm-ID: 214527 Cd Length: 83 Bit Score: 59.33 E-value: 2.52e-11
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
4-39
4.48e-10
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.
Pssm-ID: 238056 Cd Length: 83 Bit Score: 55.85 E-value: 4.48e-10
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.
Click on the triangle for interactive 3D structure viewing options.
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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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
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