Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
31-453
1.88e-123
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: 378.20 E-value: 1.88e-123
Variant erythrocyte surface antigen-1; This family represents the N-terminal of the variant ...
520-616
6.97e-04
Variant erythrocyte surface antigen-1; This family represents the N-terminal of the variant erythrocyte surface antigen 1, versions a and b, of Babesia. Babesia bovis is a tick-borne, intra-erythrocytic, protozoal parasite of cattle that shares many lifestyle parallels with the most virulent of the human malarial parasites, Plasmodium falciparum. Babesia uses antigenic variation to establish consistent infections of long duration. The two variants of VESA1, a and b, are expressed from different but closely related genes, and variation is achieved through the involvement of a segmental gene conversion mechanism and low-frequency epigenetic in situ switching of transcriptional activity from the VESA1 gene-pair to a possible other gene pair.
The actual alignment was detected with superfamily member pfam12785:
Pssm-ID: 463704 Cd Length: 461 Bit Score: 43.03 E-value: 6.97e-04
Integrin beta tail domain; This is the beta tail domain of the Integrin protein. Integrins are ...
637-752
5.28e-03
Integrin beta tail domain; This is the beta tail domain of the Integrin protein. Integrins are receptors which are involved in cell-cell and cell-extracellular matrix interactions.
The actual alignment was detected with superfamily member pfam07965:
Pssm-ID: 462325 Cd Length: 84 Bit Score: 36.87 E-value: 5.28e-03
Integrin beta subunits (N-terminal portion of extracellular region); Portion of beta integrins ...
31-453
1.88e-123
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: 378.20 E-value: 1.88e-123
Integrin beta chain VWA domain; Integrins have been found in animals and their homologs have ...
119-369
1.48e-111
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: 340.63 E-value: 1.48e-111
Variant erythrocyte surface antigen-1; This family represents the N-terminal of the variant ...
520-616
6.97e-04
Variant erythrocyte surface antigen-1; This family represents the N-terminal of the variant erythrocyte surface antigen 1, versions a and b, of Babesia. Babesia bovis is a tick-borne, intra-erythrocytic, protozoal parasite of cattle that shares many lifestyle parallels with the most virulent of the human malarial parasites, Plasmodium falciparum. Babesia uses antigenic variation to establish consistent infections of long duration. The two variants of VESA1, a and b, are expressed from different but closely related genes, and variation is achieved through the involvement of a segmental gene conversion mechanism and low-frequency epigenetic in situ switching of transcriptional activity from the VESA1 gene-pair to a possible other gene pair.
Pssm-ID: 463704 Cd Length: 461 Bit Score: 43.03 E-value: 6.97e-04
Integrin beta tail domain; This is the beta tail domain of the Integrin protein. Integrins are ...
637-752
5.28e-03
Integrin beta tail domain; This is the beta tail domain of the Integrin protein. Integrins are receptors which are involved in cell-cell and cell-extracellular matrix interactions.
Pssm-ID: 462325 Cd Length: 84 Bit Score: 36.87 E-value: 5.28e-03
Integrin beta subunits (N-terminal portion of extracellular region); Portion of beta integrins ...
31-453
1.88e-123
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: 378.20 E-value: 1.88e-123
Integrin beta chain VWA domain; Integrins have been found in animals and their homologs have ...
119-369
1.48e-111
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: 340.63 E-value: 1.48e-111
Variant erythrocyte surface antigen-1; This family represents the N-terminal of the variant ...
520-616
6.97e-04
Variant erythrocyte surface antigen-1; This family represents the N-terminal of the variant erythrocyte surface antigen 1, versions a and b, of Babesia. Babesia bovis is a tick-borne, intra-erythrocytic, protozoal parasite of cattle that shares many lifestyle parallels with the most virulent of the human malarial parasites, Plasmodium falciparum. Babesia uses antigenic variation to establish consistent infections of long duration. The two variants of VESA1, a and b, are expressed from different but closely related genes, and variation is achieved through the involvement of a segmental gene conversion mechanism and low-frequency epigenetic in situ switching of transcriptional activity from the VESA1 gene-pair to a possible other gene pair.
Pssm-ID: 463704 Cd Length: 461 Bit Score: 43.03 E-value: 6.97e-04
Integrin beta tail domain; This is the beta tail domain of the Integrin protein. Integrins are ...
637-752
5.28e-03
Integrin beta tail domain; This is the beta tail domain of the Integrin protein. Integrins are receptors which are involved in cell-cell and cell-extracellular matrix interactions.
Pssm-ID: 462325 Cd Length: 84 Bit Score: 36.87 E-value: 5.28e-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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