MULTISPECIES: VWA domain-containing protein [Shewanella]
Protein Classification
vWA domain-containing protein( domain architecture ID 13939702)
vWA (von Willebrand factor type A) domain-containing protein may be involved in one of a wide variety of important cellular functions, including basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and immune defenses
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| YfbK | COG2304 | Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ... |
146-459 | 1.05e-92 | |||||
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only]; : Pssm-ID: 441879 [Multi-domain] Cd Length: 289 Bit Score: 288.54 E-value: 1.05e-92
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| DUF3520 | pfam12034 | Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. ... |
421-611 | 7.05e-84 | |||||
Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 180 amino acids in length. This domain is found associated with pfam00092. : Pssm-ID: 432277 Cd Length: 182 Bit Score: 261.32 E-value: 7.05e-84
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| Name | Accession | Description | Interval | E-value | |||||
| YfbK | COG2304 | Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ... |
146-459 | 1.05e-92 | |||||
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only]; Pssm-ID: 441879 [Multi-domain] Cd Length: 289 Bit Score: 288.54 E-value: 1.05e-92
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| DUF3520 | pfam12034 | Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. ... |
421-611 | 7.05e-84 | |||||
Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 180 amino acids in length. This domain is found associated with pfam00092. Pssm-ID: 432277 Cd Length: 182 Bit Score: 261.32 E-value: 7.05e-84
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| vWA_subgroup | cd01465 | VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
244-415 | 3.89e-67 | |||||
VWA subgroup: 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. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known. Pssm-ID: 238742 [Multi-domain] Cd Length: 170 Bit Score: 217.14 E-value: 3.89e-67
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| vWF_A | pfam12450 | von Willebrand factor; This domain family is found in bacteria, and is approximately 100 amino ... |
144-228 | 1.57e-44 | |||||
von Willebrand factor; This domain family is found in bacteria, and is approximately 100 amino acids in length. The family is found in association with pfam00092. There are two conserved sequence motifs: STF and DVD. There are two completely conserved residues (E and N) that may be functionally important. In hemostasis, platelet adhesion to the damaged vessel wall is mediated by several proteins, including von Willebrand factor. In solution vWF becomes immobilized via its A3 domain on the fibrillar collagen of the vessel wall and acts as an intermediary between collagen and the platelet receptor glycoprotein Ibalpha (GPIbalpha), which is the only platelet receptor that does not require prior activation for bond formation. Pssm-ID: 432562 [Multi-domain] Cd Length: 94 Bit Score: 153.85 E-value: 1.57e-44
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| VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
245-411 | 3.23e-20 | |||||
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods. Pssm-ID: 214621 [Multi-domain] Cd Length: 175 Bit Score: 88.28 E-value: 3.23e-20
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| hCaCC | TIGR00868 | calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ... |
240-410 | 1.22e-06 | |||||
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out AC found a row in 1A13.INFO that was not parsed out EC found a row in 1A13.INFO that was not parsed out GA found a row in 1A13.INFO that was not parsed out SO found a row in 1A13.INFO that was not parsed out RH found a row in 1A13.INFO that was not parsed out EN found a row in 1A13.INFO that was not parsed out GS found a row in 1A13.INFO that was not parsed out AL found a row in 1A13.INFO that was not parsed out The Epithelial Chloride Channel (E-ClC) Family (TC 1.A.13) found a row in 1A13.INFO that was not parsed out found a row in 1A13.INFO that was not parsed out Mammals have multiple isoforms of epithelial chloride channel proteins. The first member of this family to be characterized was a respiratory epithelium, Ca found a row in 1A13.INFO that was not parsed out 2+-regulated, chloride channel protein isolated from bovine tracheal apical membranes. It was biochemically characterized as a 140 kDa complex. The purified found a row in 1A13.INFO that was not parsed out complex when reconstituted in a planar lipid bilayer behaved as an anion-selective channel. It was regulated by Ca 2+ via a calmodulin kinase II-dependent found a row in 1A13.INFO that was not parsed out mechanism. When the cRNA was injected into Xenopus oocytes, an outward rectifying, DIDS-sensitive, anion conductance was measured. A related gene, found a row in 1A13.INFO that was not parsed out Lu-ECAM, was cloned from the bovine aortic endothelial cell line, BAEC. It is expressed in the lung and spleen but not in the trachea. Homologues are found in found a row in 1A13.INFO that was not parsed out several mammals, and at least three paralogues(hCaCC-1-3) are present in humans, each with different tissue distributions. found a row in 1A13.INFO that was not parsed out [Transport and binding proteins, Anions] Pssm-ID: 129946 [Multi-domain] Cd Length: 863 Bit Score: 51.81 E-value: 1.22e-06
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| PRK13685 | PRK13685 | hypothetical protein; Provisional |
244-414 | 1.29e-05 | |||||
hypothetical protein; Provisional Pssm-ID: 184242 [Multi-domain] Cd Length: 326 Bit Score: 47.77 E-value: 1.29e-05
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| Name | Accession | Description | Interval | E-value | |||||
| YfbK | COG2304 | Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ... |
146-459 | 1.05e-92 | |||||
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only]; Pssm-ID: 441879 [Multi-domain] Cd Length: 289 Bit Score: 288.54 E-value: 1.05e-92
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| DUF3520 | pfam12034 | Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. ... |
421-611 | 7.05e-84 | |||||
Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 180 amino acids in length. This domain is found associated with pfam00092. Pssm-ID: 432277 Cd Length: 182 Bit Score: 261.32 E-value: 7.05e-84
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| vWA_subgroup | cd01465 | VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
244-415 | 3.89e-67 | |||||
VWA subgroup: 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. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known. Pssm-ID: 238742 [Multi-domain] Cd Length: 170 Bit Score: 217.14 E-value: 3.89e-67
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| vWF_A | pfam12450 | von Willebrand factor; This domain family is found in bacteria, and is approximately 100 amino ... |
144-228 | 1.57e-44 | |||||
von Willebrand factor; This domain family is found in bacteria, and is approximately 100 amino acids in length. The family is found in association with pfam00092. There are two conserved sequence motifs: STF and DVD. There are two completely conserved residues (E and N) that may be functionally important. In hemostasis, platelet adhesion to the damaged vessel wall is mediated by several proteins, including von Willebrand factor. In solution vWF becomes immobilized via its A3 domain on the fibrillar collagen of the vessel wall and acts as an intermediary between collagen and the platelet receptor glycoprotein Ibalpha (GPIbalpha), which is the only platelet receptor that does not require prior activation for bond formation. Pssm-ID: 432562 [Multi-domain] Cd Length: 94 Bit Score: 153.85 E-value: 1.57e-44
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| ChlD | COG1240 | vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
178-414 | 2.16e-31 | |||||
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism]; Pssm-ID: 440853 [Multi-domain] Cd Length: 262 Bit Score: 123.12 E-value: 2.16e-31
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| vWFA | cd00198 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
244-404 | 8.31e-23 | |||||
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. Pssm-ID: 238119 [Multi-domain] Cd Length: 161 Bit Score: 95.33 E-value: 8.31e-23
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| VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
245-411 | 3.23e-20 | |||||
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods. Pssm-ID: 214621 [Multi-domain] Cd Length: 175 Bit Score: 88.28 E-value: 3.23e-20
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| VWA | pfam00092 | von Willebrand factor type A domain; |
245-418 | 1.66e-17 | |||||
von Willebrand factor type A domain; Pssm-ID: 459670 [Multi-domain] Cd Length: 174 Bit Score: 80.40 E-value: 1.66e-17
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| vWA_interalpha_trypsin_inhibitor | cd01461 | vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ... |
245-405 | 2.07e-16 | |||||
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix. Pssm-ID: 238738 [Multi-domain] Cd Length: 171 Bit Score: 77.26 E-value: 2.07e-16
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| vWA_C3HC4_type | cd01466 | VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
246-405 | 1.39e-14 | |||||
VWA C3HC4-type: 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. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known. Pssm-ID: 238743 [Multi-domain] Cd Length: 155 Bit Score: 71.65 E-value: 1.39e-14
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| ViaA | COG2425 | Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ... |
196-396 | 9.34e-14 | |||||
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown]; Pssm-ID: 441973 [Multi-domain] Cd Length: 263 Bit Score: 71.63 E-value: 9.34e-14
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| vWFA_subfamily_ECM | cd01450 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
244-404 | 3.07e-12 | |||||
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 Pssm-ID: 238727 [Multi-domain] Cd Length: 161 Bit Score: 65.01 E-value: 3.07e-12
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| VWA_3 | pfam13768 | von Willebrand factor type A domain; |
244-402 | 7.30e-11 | |||||
von Willebrand factor type A domain; Pssm-ID: 372716 [Multi-domain] Cd Length: 155 Bit Score: 60.87 E-value: 7.30e-11
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| VWA_2 | pfam13519 | von Willebrand factor type A domain; |
246-334 | 1.39e-10 | |||||
von Willebrand factor type A domain; Pssm-ID: 463909 [Multi-domain] Cd Length: 103 Bit Score: 58.46 E-value: 1.39e-10
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| vWA_ywmD_type | cd01456 | VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
243-404 | 1.91e-10 | |||||
VWA ywmD type: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. Not much is known about the function of the members of this subgroup. All members of this subgroup however have a conserved MIDAS motif. Pssm-ID: 238733 [Multi-domain] Cd Length: 206 Bit Score: 60.91 E-value: 1.91e-10
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| vWA_Magnesium_chelatase | cd01451 | Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ... |
246-409 | 1.67e-08 | |||||
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). In chlorophyll biosynthesis, insertion of Mg2+ into protoporphyrin IX is catalysed by magnesium chelatase in an ATP-dependent reaction. Magnesium chelatase is a three sub-unit (BchI, BchD and BchH) enzyme with a novel arrangement of domains: the C-terminal helical domain is located behind the nucleotide binding site. The BchD domain contains a AAA domain at its N-terminus and a VWA domain at its C-terminus. The VWA domain has been speculated to be involved in mediating protein-protein interactions. Pssm-ID: 238728 [Multi-domain] Cd Length: 178 Bit Score: 54.59 E-value: 1.67e-08
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| vWA_BatA_type | cd01467 | VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
243-403 | 7.52e-08 | |||||
VWA BatA type: 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. Members of this subgroup are bacterial in origin. They are typified by the presence of a MIDAS motif. Pssm-ID: 238744 [Multi-domain] Cd Length: 180 Bit Score: 52.72 E-value: 7.52e-08
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| TerY | COG4245 | Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown]; |
247-396 | 1.07e-06 | |||||
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown]; Pssm-ID: 443387 [Multi-domain] Cd Length: 196 Bit Score: 49.54 E-value: 1.07e-06
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| hCaCC | TIGR00868 | calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ... |
240-410 | 1.22e-06 | |||||
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out AC found a row in 1A13.INFO that was not parsed out EC found a row in 1A13.INFO that was not parsed out GA found a row in 1A13.INFO that was not parsed out SO found a row in 1A13.INFO that was not parsed out RH found a row in 1A13.INFO that was not parsed out EN found a row in 1A13.INFO that was not parsed out GS found a row in 1A13.INFO that was not parsed out AL found a row in 1A13.INFO that was not parsed out The Epithelial Chloride Channel (E-ClC) Family (TC 1.A.13) found a row in 1A13.INFO that was not parsed out found a row in 1A13.INFO that was not parsed out Mammals have multiple isoforms of epithelial chloride channel proteins. The first member of this family to be characterized was a respiratory epithelium, Ca found a row in 1A13.INFO that was not parsed out 2+-regulated, chloride channel protein isolated from bovine tracheal apical membranes. It was biochemically characterized as a 140 kDa complex. The purified found a row in 1A13.INFO that was not parsed out complex when reconstituted in a planar lipid bilayer behaved as an anion-selective channel. It was regulated by Ca 2+ via a calmodulin kinase II-dependent found a row in 1A13.INFO that was not parsed out mechanism. When the cRNA was injected into Xenopus oocytes, an outward rectifying, DIDS-sensitive, anion conductance was measured. A related gene, found a row in 1A13.INFO that was not parsed out Lu-ECAM, was cloned from the bovine aortic endothelial cell line, BAEC. It is expressed in the lung and spleen but not in the trachea. Homologues are found in found a row in 1A13.INFO that was not parsed out several mammals, and at least three paralogues(hCaCC-1-3) are present in humans, each with different tissue distributions. found a row in 1A13.INFO that was not parsed out [Transport and binding proteins, Anions] Pssm-ID: 129946 [Multi-domain] Cd Length: 863 Bit Score: 51.81 E-value: 1.22e-06
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| vWA_VGCC_like | cd01463 | VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ... |
245-408 | 1.20e-05 | |||||
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The alpha 2 and delta subunits result from proteolytic processing of a single gene product and carries at its N-terminus the VWA and cache domains, The alpha 2 delta gene family has orthologues in D. melanogaster and C. elegans but none have been detected in aither A. thaliana or yeast. The exact biochemical function of the VWA domain is not known but the alpha 2 delta complex has been shown to regulate various functional properties of the channel complex. Pssm-ID: 238740 [Multi-domain] Cd Length: 190 Bit Score: 46.62 E-value: 1.20e-05
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| vWA_micronemal_protein | cd01471 | Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ... |
245-384 | 1.27e-05 | |||||
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners. Pssm-ID: 238748 [Multi-domain] Cd Length: 186 Bit Score: 46.22 E-value: 1.27e-05
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| PRK13685 | PRK13685 | hypothetical protein; Provisional |
244-414 | 1.29e-05 | |||||
hypothetical protein; Provisional Pssm-ID: 184242 [Multi-domain] Cd Length: 326 Bit Score: 47.77 E-value: 1.29e-05
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| vWA_collagen_alpha_1-VI-type | cd01480 | VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ... |
242-350 | 7.44e-04 | |||||
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions. Pssm-ID: 238757 [Multi-domain] Cd Length: 186 Bit Score: 41.22 E-value: 7.44e-04
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| vWA_subfamily | cd01464 | VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
247-328 | 4.02e-03 | |||||
VWA subfamily: 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. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif. Pssm-ID: 238741 [Multi-domain] Cd Length: 176 Bit Score: 38.86 E-value: 4.02e-03
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| vWA_ATR | cd01474 | ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ... |
242-396 | 8.18e-03 | |||||
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells. Pssm-ID: 238751 [Multi-domain] Cd Length: 185 Bit Score: 37.88 E-value: 8.18e-03
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