VWA (von Willebrand factor type A) domain-containing protein similar to mammalian von Willebrand factor that plays an essential role in the formation of a platelet plug, to stop bleeding, by anchoring blood platelets to the damaged vessel wall under conditions of high shear stress
VWA-like domain (DUF2201); This domain, found in various hypothetical bacterial proteins, has ...
292-432
1.46e-10
VWA-like domain (DUF2201); This domain, found in various hypothetical bacterial proteins, has no known function. However, it is clearly related to the VWA domain.
Pssm-ID: 401806 Cd Length: 123 Bit Score: 58.55 E-value: 1.46e-10
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
291-402
1.46e-08
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: 54.00 E-value: 1.46e-08
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
292-405
3.80e-08
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: 52.57 E-value: 3.80e-08
VWA-like domain (DUF2201); This domain, found in various hypothetical bacterial proteins, has ...
292-432
1.46e-10
VWA-like domain (DUF2201); This domain, found in various hypothetical bacterial proteins, has no known function. However, it is clearly related to the VWA domain.
Pssm-ID: 401806 Cd Length: 123 Bit Score: 58.55 E-value: 1.46e-10
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
291-402
1.46e-08
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: 54.00 E-value: 1.46e-08
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
292-405
3.80e-08
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: 52.57 E-value: 3.80e-08
Putative metallopeptidase domain; This domain, found in various hypothetical bacterial ...
34-245
1.39e-06
Putative metallopeptidase domain; This domain, found in various hypothetical bacterial proteins, has no known function. However, it is related to pfam01435.
Pssm-ID: 404152 Cd Length: 271 Bit Score: 49.43 E-value: 1.39e-06
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
290-396
4.69e-04
VWA YIEM 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 have a conserved MIDAS motif, however, their biochemical function is not well characterised.
Pssm-ID: 238739 [Multi-domain] Cd Length: 152 Bit Score: 40.41 E-value: 4.69e-04
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
292-396
2.19e-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: 38.81 E-value: 2.19e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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