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von Willebrand factor A domain-containing protein 3B isoform X11 [Homo sapiens]
vWA domain-containing protein( domain architecture ID 10076759)
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
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Name | Accession | Description | Interval | E-value | |||
vWFA | cd00198 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
508-612 | 3.67e-13 | |||
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: 67.59 E-value: 3.67e-13
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Name | Accession | Description | Interval | E-value | |||
vWFA | cd00198 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
508-612 | 3.67e-13 | |||
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: 67.59 E-value: 3.67e-13
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YfbK | COG2304 | Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ... |
511-610 | 1.39e-10 | |||
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only]; Pssm-ID: 441879 [Multi-domain] Cd Length: 289 Bit Score: 62.81 E-value: 1.39e-10
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VWA_3 | pfam13768 | von Willebrand factor type A domain; |
509-612 | 4.16e-08 | |||
von Willebrand factor type A domain; Pssm-ID: 372716 [Multi-domain] Cd Length: 155 Bit Score: 52.78 E-value: 4.16e-08
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VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
509-611 | 1.31e-05 | |||
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: 45.91 E-value: 1.31e-05
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Name | Accession | Description | Interval | E-value | |||
vWFA | cd00198 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
508-612 | 3.67e-13 | |||
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: 67.59 E-value: 3.67e-13
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vWA_interalpha_trypsin_inhibitor | cd01461 | vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ... |
512-608 | 2.17e-11 | |||
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: 62.62 E-value: 2.17e-11
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YfbK | COG2304 | Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ... |
511-610 | 1.39e-10 | |||
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only]; Pssm-ID: 441879 [Multi-domain] Cd Length: 289 Bit Score: 62.81 E-value: 1.39e-10
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ChlD | COG1240 | vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
509-610 | 3.37e-10 | |||
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: 61.11 E-value: 3.37e-10
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ViaA | COG2425 | Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ... |
509-608 | 1.01e-08 | |||
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown]; Pssm-ID: 441973 [Multi-domain] Cd Length: 263 Bit Score: 56.61 E-value: 1.01e-08
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VWA_3 | pfam13768 | von Willebrand factor type A domain; |
509-612 | 4.16e-08 | |||
von Willebrand factor type A domain; Pssm-ID: 372716 [Multi-domain] Cd Length: 155 Bit Score: 52.78 E-value: 4.16e-08
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VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
509-611 | 1.31e-05 | |||
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: 45.91 E-value: 1.31e-05
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VWA | pfam00092 | von Willebrand factor type A domain; |
509-611 | 2.60e-05 | |||
von Willebrand factor type A domain; Pssm-ID: 459670 [Multi-domain] Cd Length: 174 Bit Score: 45.34 E-value: 2.60e-05
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TerY | COG4245 | Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown]; |
503-610 | 4.90e-05 | |||
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown]; Pssm-ID: 443387 [Multi-domain] Cd Length: 196 Bit Score: 44.53 E-value: 4.90e-05
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vWA_subgroup | cd01465 | VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
512-610 | 1.01e-03 | |||
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: 40.33 E-value: 1.01e-03
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vWA_complement_factors | cd01470 | Complement factors B and C2 are two critical proteases for complement activation. They both ... |
509-641 | 1.35e-03 | |||
Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains. Pssm-ID: 238747 [Multi-domain] Cd Length: 198 Bit Score: 40.35 E-value: 1.35e-03
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vWFA_subfamily_ECM | cd01450 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
509-611 | 2.09e-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 Pssm-ID: 238727 [Multi-domain] Cd Length: 161 Bit Score: 39.20 E-value: 2.09e-03
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VWA_2 | pfam13519 | von Willebrand factor type A domain; |
509-595 | 5.79e-03 | |||
von Willebrand factor type A domain; Pssm-ID: 463909 [Multi-domain] Cd Length: 103 Bit Score: 36.89 E-value: 5.79e-03
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Blast search parameters | ||||
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