Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
32-419
5.37e-141
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 smart00187:
Pssm-ID: 469594 [Multi-domain] Cd Length: 423 Bit Score: 422.50 E-value: 5.37e-141
Integrin beta epidermal growth factor like domain 1; This is the I-EGF 1 domain found in ...
417-448
1.04e-04
Integrin beta epidermal growth factor like domain 1; This is the I-EGF 1 domain found in several integrin betas such as integrin beta 1-7. Structural analysis reveal an epidermal growth factor-like (I-EGF) domains 1 and 2. EGF1 lacks one disulfide (C2-C4) relative to the integrin EGF 2, 3, and 4 domains, this allows the C-terminal end of EGF1 to flex remarkably relative to its N-terminal end.
:
Pssm-ID: 465729 Cd Length: 29 Bit Score: 39.78 E-value: 1.04e-04
Integrin beta subunits (N-terminal portion of extracellular region); Portion of beta integrins ...
32-419
5.37e-141
Integrin beta subunits (N-terminal portion of extracellular region); Portion of beta integrins that lies N-terminal to their EGF-like repeats. Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Beta integrins are proposed to have a von Willebrand factor type-A "insert" or "I" -like domain (although this remains to be confirmed).
Pssm-ID: 197563 [Multi-domain] Cd Length: 423 Bit Score: 422.50 E-value: 5.37e-141
Integrin beta chain VWA domain; Integrins have been found in animals and their homologs have ...
123-339
2.18e-76
Integrin beta chain VWA domain; Integrins have been found in animals and their homologs have also been found in cyanobacteria, probably due to horizontal gene transfer. This domain corresponds to the integrin beta VWA domain.
Pssm-ID: 459781 Cd Length: 248 Bit Score: 247.41 E-value: 2.18e-76
Integrin beta epidermal growth factor like domain 1; This is the I-EGF 1 domain found in ...
417-448
1.04e-04
Integrin beta epidermal growth factor like domain 1; This is the I-EGF 1 domain found in several integrin betas such as integrin beta 1-7. Structural analysis reveal an epidermal growth factor-like (I-EGF) domains 1 and 2. EGF1 lacks one disulfide (C2-C4) relative to the integrin EGF 2, 3, and 4 domains, this allows the C-terminal end of EGF1 to flex remarkably relative to its N-terminal end.
Pssm-ID: 465729 Cd Length: 29 Bit Score: 39.78 E-value: 1.04e-04
Integrin beta subunits (N-terminal portion of extracellular region); Portion of beta integrins ...
32-419
5.37e-141
Integrin beta subunits (N-terminal portion of extracellular region); Portion of beta integrins that lies N-terminal to their EGF-like repeats. Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Beta integrins are proposed to have a von Willebrand factor type-A "insert" or "I" -like domain (although this remains to be confirmed).
Pssm-ID: 197563 [Multi-domain] Cd Length: 423 Bit Score: 422.50 E-value: 5.37e-141
Integrin beta chain VWA domain; Integrins have been found in animals and their homologs have ...
123-339
2.18e-76
Integrin beta chain VWA domain; Integrins have been found in animals and their homologs have also been found in cyanobacteria, probably due to horizontal gene transfer. This domain corresponds to the integrin beta VWA domain.
Pssm-ID: 459781 Cd Length: 248 Bit Score: 247.41 E-value: 2.18e-76
Integrin beta epidermal growth factor like domain 1; This is the I-EGF 1 domain found in ...
417-448
1.04e-04
Integrin beta epidermal growth factor like domain 1; This is the I-EGF 1 domain found in several integrin betas such as integrin beta 1-7. Structural analysis reveal an epidermal growth factor-like (I-EGF) domains 1 and 2. EGF1 lacks one disulfide (C2-C4) relative to the integrin EGF 2, 3, and 4 domains, this allows the C-terminal end of EGF1 to flex remarkably relative to its N-terminal end.
Pssm-ID: 465729 Cd Length: 29 Bit Score: 39.78 E-value: 1.04e-04
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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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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