multiple epidermal growth factor-like domains protein 6 isoform X1 [Rattus norvegicus]
matrilin; VIT and vWA domain-containing protein( domain architecture ID 10540644)
matrilin acts as the component of the extracellular matrix of cartilage| VIT (vault protein inter-alpha-trypsin) and vWA (von Willebrand factor type A) domain-containing protein
List of domain hits
Name | Accession | Description | Interval | E-value | ||
EMI | pfam07546 | EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ... |
41-113 | 1.15e-07 | ||
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains. : Pssm-ID: 462204 Cd Length: 69 Bit Score: 50.11 E-value: 1.15e-07
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vWFA super family | cl00057 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
243-284 | 5.15e-06 | ||
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. The actual alignment was detected with superfamily member cd01475: Pssm-ID: 469594 [Multi-domain] Cd Length: 224 Bit Score: 49.31 E-value: 5.15e-06
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FXa_inhibition | pfam14670 | Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
127-162 | 1.28e-05 | ||
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: 43.39 E-value: 1.28e-05
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FXa_inhibition | pfam14670 | Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
297-332 | 8.27e-05 | ||
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: 41.07 E-value: 8.27e-05
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vWFA super family | cl00057 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
372-411 | 1.02e-04 | ||
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. The actual alignment was detected with superfamily member cd01475: Pssm-ID: 469594 [Multi-domain] Cd Length: 224 Bit Score: 45.45 E-value: 1.02e-04
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vWFA super family | cl00057 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
196-244 | 1.39e-04 | ||
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. The actual alignment was detected with superfamily member cd01475: Pssm-ID: 469594 [Multi-domain] Cd Length: 224 Bit Score: 45.07 E-value: 1.39e-04
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FXa_inhibition | pfam14670 | Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
168-204 | 6.21e-03 | ||
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: 35.68 E-value: 6.21e-03
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vWFA super family | cl00057 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
330-369 | 7.42e-03 | ||
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. The actual alignment was detected with superfamily member cd01475: Pssm-ID: 469594 [Multi-domain] Cd Length: 224 Bit Score: 39.68 E-value: 7.42e-03
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Name | Accession | Description | Interval | E-value | ||
EMI | pfam07546 | EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ... |
41-113 | 1.15e-07 | ||
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains. Pssm-ID: 462204 Cd Length: 69 Bit Score: 50.11 E-value: 1.15e-07
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vWA_Matrilin | cd01475 | VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ... |
243-284 | 5.15e-06 | ||
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands. Pssm-ID: 238752 [Multi-domain] Cd Length: 224 Bit Score: 49.31 E-value: 5.15e-06
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FXa_inhibition | pfam14670 | Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
127-162 | 1.28e-05 | ||
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: 43.39 E-value: 1.28e-05
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vWA_Matrilin | cd01475 | VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ... |
117-161 | 1.41e-05 | ||
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands. Pssm-ID: 238752 [Multi-domain] Cd Length: 224 Bit Score: 48.15 E-value: 1.41e-05
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FXa_inhibition | pfam14670 | Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
297-332 | 8.27e-05 | ||
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: 41.07 E-value: 8.27e-05
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vWA_Matrilin | cd01475 | VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ... |
372-411 | 1.02e-04 | ||
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands. Pssm-ID: 238752 [Multi-domain] Cd Length: 224 Bit Score: 45.45 E-value: 1.02e-04
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vWA_Matrilin | cd01475 | VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ... |
196-244 | 1.39e-04 | ||
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands. Pssm-ID: 238752 [Multi-domain] Cd Length: 224 Bit Score: 45.07 E-value: 1.39e-04
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FXa_inhibition | pfam14670 | Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
210-245 | 4.10e-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: 39.15 E-value: 4.10e-04
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FXa_inhibition | pfam14670 | Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
378-413 | 1.45e-03 | ||
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: 37.61 E-value: 1.45e-03
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EGF_CA | smart00179 | Calcium-binding EGF-like domain; |
123-162 | 1.47e-03 | ||
Calcium-binding EGF-like domain; Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 37.61 E-value: 1.47e-03
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FXa_inhibition | pfam14670 | Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
168-204 | 6.21e-03 | ||
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: 35.68 E-value: 6.21e-03
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vWA_Matrilin | cd01475 | VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ... |
330-369 | 7.42e-03 | ||
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands. Pssm-ID: 238752 [Multi-domain] Cd Length: 224 Bit Score: 39.68 E-value: 7.42e-03
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Name | Accession | Description | Interval | E-value | ||
EMI | pfam07546 | EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ... |
41-113 | 1.15e-07 | ||
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains. Pssm-ID: 462204 Cd Length: 69 Bit Score: 50.11 E-value: 1.15e-07
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vWA_Matrilin | cd01475 | VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ... |
243-284 | 5.15e-06 | ||
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands. Pssm-ID: 238752 [Multi-domain] Cd Length: 224 Bit Score: 49.31 E-value: 5.15e-06
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FXa_inhibition | pfam14670 | Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
127-162 | 1.28e-05 | ||
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: 43.39 E-value: 1.28e-05
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vWA_Matrilin | cd01475 | VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ... |
117-161 | 1.41e-05 | ||
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands. Pssm-ID: 238752 [Multi-domain] Cd Length: 224 Bit Score: 48.15 E-value: 1.41e-05
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FXa_inhibition | pfam14670 | Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
297-332 | 8.27e-05 | ||
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: 41.07 E-value: 8.27e-05
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vWA_Matrilin | cd01475 | VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ... |
372-411 | 1.02e-04 | ||
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands. Pssm-ID: 238752 [Multi-domain] Cd Length: 224 Bit Score: 45.45 E-value: 1.02e-04
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vWA_Matrilin | cd01475 | VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ... |
196-244 | 1.39e-04 | ||
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands. Pssm-ID: 238752 [Multi-domain] Cd Length: 224 Bit Score: 45.07 E-value: 1.39e-04
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FXa_inhibition | pfam14670 | Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
210-245 | 4.10e-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: 39.15 E-value: 4.10e-04
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FXa_inhibition | pfam14670 | Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
378-413 | 1.45e-03 | ||
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: 37.61 E-value: 1.45e-03
|
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EGF_CA | smart00179 | Calcium-binding EGF-like domain; |
123-162 | 1.47e-03 | ||
Calcium-binding EGF-like domain; Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 37.61 E-value: 1.47e-03
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FXa_inhibition | pfam14670 | Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
168-204 | 6.21e-03 | ||
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: 35.68 E-value: 6.21e-03
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vWA_Matrilin | cd01475 | VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ... |
330-369 | 7.42e-03 | ||
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands. Pssm-ID: 238752 [Multi-domain] Cd Length: 224 Bit Score: 39.68 E-value: 7.42e-03
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cEGF | pfam12662 | Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ... |
229-250 | 8.85e-03 | ||
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: 35.08 E-value: 8.85e-03
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Blast search parameters | ||||
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