coagulation factor is a vitamin K-dependent protein S1 family serine peptidase, similar to human coagulation factor X that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting| trypsin-like serine protease catalyzes the cleavage of specific peptide bonds in protein substrates using an active site serine as the nucleophile; contains C-terminal DNA polymerase III subunits gamma and tau
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
369-621
2.45e-89
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: 276.85 E-value: 2.45e-89
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
113-194
1.99e-35
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: 1.99e-35
Thrombin light chain; Thrombin is an enzyme that cleaves bonds after Arg and Lys, converts ...
321-368
2.55e-28
Thrombin light chain; Thrombin is an enzyme that cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII. Prothrombin is activated on the surface of a phospholipid membrane where factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. This domain corresponds to the light chain of thrombin.
:
Pssm-ID: 430582 Cd Length: 48 Bit Score: 106.99 E-value: 2.55e-28
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
216-298
2.90e-28
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: 108.25 E-value: 2.90e-28
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
32-96
1.24e-23
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in proteins associated with the extracellular matrix, cell adhesion and cell migration.
:
Pssm-ID: 214503 Cd Length: 65 Bit Score: 94.30 E-value: 1.24e-23
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
369-621
2.45e-89
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: 276.85 E-value: 2.45e-89
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
368-618
4.99e-88
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: 273.40 E-value: 4.99e-88
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
113-194
1.99e-35
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: 1.99e-35
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
114-196
4.08e-35
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: 127.12 E-value: 4.08e-35
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
111-194
3.33e-30
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: 113.56 E-value: 3.33e-30
Thrombin light chain; Thrombin is an enzyme that cleaves bonds after Arg and Lys, converts ...
321-368
2.55e-28
Thrombin light chain; Thrombin is an enzyme that cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII. Prothrombin is activated on the surface of a phospholipid membrane where factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. This domain corresponds to the light chain of thrombin.
Pssm-ID: 430582 Cd Length: 48 Bit Score: 106.99 E-value: 2.55e-28
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
216-298
2.90e-28
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: 108.25 E-value: 2.90e-28
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
218-296
3.62e-26
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: 102.00 E-value: 3.62e-26
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
215-297
1.81e-25
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: 100.15 E-value: 1.81e-25
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
32-96
1.24e-23
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in proteins associated with the extracellular matrix, cell adhesion and cell migration.
Pssm-ID: 214503 Cd Length: 65 Bit Score: 94.30 E-value: 1.24e-23
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
56-96
5.57e-20
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is responsible for the high-affinity binding of calcium ions. This domain contains post-translational modifications of many glutamate residues by Vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla).
Pssm-ID: 459861 Cd Length: 41 Bit Score: 83.35 E-value: 5.57e-20
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
369-621
2.45e-89
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: 276.85 E-value: 2.45e-89
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
368-618
4.99e-88
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: 273.40 E-value: 4.99e-88
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
113-194
1.99e-35
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: 1.99e-35
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
114-196
4.08e-35
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: 127.12 E-value: 4.08e-35
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
111-194
3.33e-30
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: 113.56 E-value: 3.33e-30
Thrombin light chain; Thrombin is an enzyme that cleaves bonds after Arg and Lys, converts ...
321-368
2.55e-28
Thrombin light chain; Thrombin is an enzyme that cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII. Prothrombin is activated on the surface of a phospholipid membrane where factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. This domain corresponds to the light chain of thrombin.
Pssm-ID: 430582 Cd Length: 48 Bit Score: 106.99 E-value: 2.55e-28
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
216-298
2.90e-28
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: 108.25 E-value: 2.90e-28
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
218-296
3.62e-26
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: 102.00 E-value: 3.62e-26
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
215-297
1.81e-25
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: 100.15 E-value: 1.81e-25
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
32-96
1.24e-23
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in proteins associated with the extracellular matrix, cell adhesion and cell migration.
Pssm-ID: 214503 Cd Length: 65 Bit Score: 94.30 E-value: 1.24e-23
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
56-96
5.57e-20
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is responsible for the high-affinity binding of calcium ions. This domain contains post-translational modifications of many glutamate residues by Vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla).
Pssm-ID: 459861 Cd Length: 41 Bit Score: 83.35 E-value: 5.57e-20
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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Others (non-specific hits) and
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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)
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
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