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 ...
178-409
6.54e-95
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: 284.55 E-value: 6.54e-95
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
67-107
5.03e-22
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: 87.97 E-value: 5.03e-22
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
114-151
1.33e-09
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.
:
Pssm-ID: 464251 [Multi-domain] Cd Length: 36 Bit Score: 53.02 E-value: 1.33e-09
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
178-409
6.54e-95
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: 284.55 E-value: 6.54e-95
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
176-406
1.36e-90
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: 1.36e-90
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
67-107
5.03e-22
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: 87.97 E-value: 5.03e-22
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
44-107
6.77e-22
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: 88.52 E-value: 6.77e-22
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
114-151
1.33e-09
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.
Pssm-ID: 464251 [Multi-domain] Cd Length: 36 Bit Score: 53.02 E-value: 1.33e-09
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
178-409
6.54e-95
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: 284.55 E-value: 6.54e-95
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
176-406
1.36e-90
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: 1.36e-90
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
67-107
5.03e-22
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: 87.97 E-value: 5.03e-22
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
44-107
6.77e-22
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: 88.52 E-value: 6.77e-22
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
114-151
1.33e-09
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.
Pssm-ID: 464251 [Multi-domain] Cd Length: 36 Bit Score: 53.02 E-value: 1.33e-09
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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if a domain or superfamily has been annotated with functional sites (conserved features),
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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.
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(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.
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