vitamin K-dependent protein C isoform X1 [Mus musculus]
Protein Classification
coagulation factor( domain architecture ID 10637862)
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
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| Tryp_SPc | cd00190 | Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
236-470 | 2.26e-88 | ||||
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: 269.92 E-value: 2.26e-88
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| GLA | smart00069 | Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ... |
50-110 | 3.15e-25 | ||||
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: 98.15 E-value: 3.15e-25
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| FXa_inhibition | pfam14670 | Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
163-198 | 4.76e-12 | ||||
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: 60.33 E-value: 4.76e-12
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| EGF_CA | cd00054 | Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
111-155 | 3.50e-08 | ||||
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements. : Pssm-ID: 238011 Cd Length: 38 Bit Score: 49.17 E-value: 3.50e-08
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| Name | Accession | Description | Interval | E-value | |||||
| Tryp_SPc | cd00190 | Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
236-470 | 2.26e-88 | |||||
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: 269.92 E-value: 2.26e-88
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| Tryp_SPc | smart00020 | Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
235-468 | 2.19e-85 | |||||
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: 262.23 E-value: 2.19e-85
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| Trypsin | pfam00089 | Trypsin; |
236-468 | 7.36e-75 | |||||
Trypsin; Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 234.64 E-value: 7.36e-75
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| COG5640 | COG5640 | Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
231-474 | 5.61e-68 | |||||
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 218.37 E-value: 5.61e-68
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| GLA | smart00069 | Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ... |
50-110 | 3.15e-25 | |||||
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: 98.15 E-value: 3.15e-25
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| Gla | pfam00594 | Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ... |
70-109 | 4.66e-23 | |||||
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: 91.44 E-value: 4.66e-23
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| FXa_inhibition | pfam14670 | Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
163-198 | 4.76e-12 | |||||
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: 60.33 E-value: 4.76e-12
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| EGF_CA | cd00054 | Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
111-155 | 3.50e-08 | |||||
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements. Pssm-ID: 238011 Cd Length: 38 Bit Score: 49.17 E-value: 3.50e-08
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| EGF_CA | smart00179 | Calcium-binding EGF-like domain; |
111-155 | 4.45e-06 | |||||
Calcium-binding EGF-like domain; Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 43.39 E-value: 4.45e-06
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| EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
124-153 | 1.63e-04 | |||||
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains. Pssm-ID: 394967 Cd Length: 31 Bit Score: 38.90 E-value: 1.63e-04
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| Name | Accession | Description | Interval | E-value | |||||
| Tryp_SPc | cd00190 | Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
236-470 | 2.26e-88 | |||||
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: 269.92 E-value: 2.26e-88
|
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| Tryp_SPc | smart00020 | Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
235-468 | 2.19e-85 | |||||
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: 262.23 E-value: 2.19e-85
|
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| Trypsin | pfam00089 | Trypsin; |
236-468 | 7.36e-75 | |||||
Trypsin; Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 234.64 E-value: 7.36e-75
|
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| COG5640 | COG5640 | Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
231-474 | 5.61e-68 | |||||
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 218.37 E-value: 5.61e-68
|
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| GLA | smart00069 | Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ... |
50-110 | 3.15e-25 | |||||
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: 98.15 E-value: 3.15e-25
|
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| Gla | pfam00594 | Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ... |
70-109 | 4.66e-23 | |||||
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: 91.44 E-value: 4.66e-23
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| eMpr | COG3591 | V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
262-458 | 4.24e-14 | |||||
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 70.86 E-value: 4.24e-14
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| FXa_inhibition | pfam14670 | Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
163-198 | 4.76e-12 | |||||
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: 60.33 E-value: 4.76e-12
|
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| EGF_CA | cd00054 | Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
111-155 | 3.50e-08 | |||||
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements. Pssm-ID: 238011 Cd Length: 38 Bit Score: 49.17 E-value: 3.50e-08
|
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| EGF_CA | smart00179 | Calcium-binding EGF-like domain; |
111-155 | 4.45e-06 | |||||
Calcium-binding EGF-like domain; Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 43.39 E-value: 4.45e-06
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| EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
124-153 | 1.63e-04 | |||||
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains. Pssm-ID: 394967 Cd Length: 31 Bit Score: 38.90 E-value: 1.63e-04
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| EGF | cd00053 | Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ... |
126-155 | 2.36e-04 | |||||
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium. Pssm-ID: 238010 Cd Length: 36 Bit Score: 38.61 E-value: 2.36e-04
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| EGF | smart00181 | Epidermal growth factor-like domain; |
129-155 | 4.66e-04 | |||||
Epidermal growth factor-like domain; Pssm-ID: 214544 Cd Length: 35 Bit Score: 37.50 E-value: 4.66e-04
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| hEGF | pfam12661 | Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ... |
128-149 | 8.57e-03 | |||||
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue. Pssm-ID: 463660 Cd Length: 22 Bit Score: 33.85 E-value: 8.57e-03
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| Blast search parameters | ||||
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