collagen and calcium-binding EGF domain-containing protein 1 isoform X2 [Mus musculus]
calcium-binding EGF-like domain-containing protein( domain architecture ID 10630624)
calcium-binding epidermal growth factor (EGF)-like domain-containing protein may play a crucial role in numerous protein-protein interactions
List of domain hits
Name | Accession | Description | Interval | E-value | ||
FXa_inhibition | pfam14670 | Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
2-21 | 1.48e-04 | ||
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: 38.38 E-value: 1.48e-04
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Name | Accession | Description | Interval | E-value | ||
FXa_inhibition | pfam14670 | Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
2-21 | 1.48e-04 | ||
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: 38.38 E-value: 1.48e-04
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Name | Accession | Description | Interval | E-value | ||
FXa_inhibition | pfam14670 | Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
2-21 | 1.48e-04 | ||
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: 38.38 E-value: 1.48e-04
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cEGF | pfam12662 | Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ... |
5-22 | 7.56e-04 | ||
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteriztic pattern 'ababcc'. They are found in blood coagulation proteins such as fibrillin, Clr and Cls, thrombomodulin, and the LDL receptor. 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 cysteine residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In cEGFs the C-terminal thiol resides on the C-terminal beta-sheet, resulting in long loop-lengths between the cysteine residues of disulfide 'c', typically C[10+]XC. These longer loop-lengths may have arisen by selective cysteine loss from a four-disulfide EGF template such as laminin or integrin. Tandem cEGF domains have five linking residues between terminal cysteines of adjacent domains. cEGF domains may or may not bind calcium in the linker region. cEGF domains with the consensus motif CXN4X[F,Y]XCXC are hydroxylated exclusively on the asparagine residue. Pssm-ID: 463661 Cd Length: 22 Bit Score: 35.85 E-value: 7.56e-04
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Blast search parameters | ||||
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