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integrator complex subunit 6 isoform c [Homo sapiens]
VWA domain-containing protein( domain architecture ID 10608872)
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 | |||
VWA_2 | pfam13519 | von Willebrand factor type A domain; |
4-103 | 8.32e-18 | |||
von Willebrand factor type A domain; : Pssm-ID: 463909 [Multi-domain] Cd Length: 103 Bit Score: 72.32 E-value: 8.32e-18
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Name | Accession | Description | Interval | E-value | |||
VWA_2 | pfam13519 | von Willebrand factor type A domain; |
4-103 | 8.32e-18 | |||
von Willebrand factor type A domain; Pssm-ID: 463909 [Multi-domain] Cd Length: 103 Bit Score: 72.32 E-value: 8.32e-18
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vWFA | cd00198 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
4-100 | 2.05e-11 | |||
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: 57.19 E-value: 2.05e-11
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ChlD | COG1240 | vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
4-114 | 2.06e-09 | |||
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: 53.02 E-value: 2.06e-09
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VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
4-100 | 1.88e-07 | |||
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: 47.06 E-value: 1.88e-07
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Name | Accession | Description | Interval | E-value | |||
VWA_2 | pfam13519 | von Willebrand factor type A domain; |
4-103 | 8.32e-18 | |||
von Willebrand factor type A domain; Pssm-ID: 463909 [Multi-domain] Cd Length: 103 Bit Score: 72.32 E-value: 8.32e-18
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vWFA | cd00198 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
4-100 | 2.05e-11 | |||
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: 57.19 E-value: 2.05e-11
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ChlD | COG1240 | vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
4-114 | 2.06e-09 | |||
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: 53.02 E-value: 2.06e-09
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VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
4-100 | 1.88e-07 | |||
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: 47.06 E-value: 1.88e-07
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YfbK | COG2304 | Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ... |
4-105 | 1.60e-05 | |||
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only]; Pssm-ID: 441879 [Multi-domain] Cd Length: 289 Bit Score: 42.01 E-value: 1.60e-05
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YeaD2 | COG1721 | Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown]; |
4-99 | 4.30e-04 | |||
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown]; Pssm-ID: 441327 [Multi-domain] Cd Length: 287 Bit Score: 37.88 E-value: 4.30e-04
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vWA_interalpha_trypsin_inhibitor | cd01461 | vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ... |
4-100 | 4.54e-03 | |||
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: 34.88 E-value: 4.54e-03
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vWA_subgroup | cd01465 | VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
4-99 | 4.60e-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: 34.56 E-value: 4.60e-03
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vWA_BABAM1 | cd21502 | Von-Willebrand factor A (vWA) domain found in BRISC and BRCA1-A complex member 1; BRISC and ... |
4-98 | 7.15e-03 | |||
Von-Willebrand factor A (vWA) domain found in BRISC and BRCA1-A complex member 1; BRISC and BRCA1 A complex member 1 (BABAM1) is also known as Mediator of RAP80 interactions and targeting subunit of 40 kDa (MERIT40), New component of the BRCA1-A complex (NBA1), HSPC142, or C19orf620. It is a core component of the BRCA1-A and BRISC complexes that function in DNA double-strand break repair and immune signaling, and contain the lysine-63 linkage-specific BRCC36 subunit that is functionalized by scaffold subunits Abraxas and ABRO1, respectively. BABAM1 interacts with Rap80, BRCC36, BRCC45, and Abraxas to form the BRCA1-A complex, a lysine-63-Ub specific deubiquitinating enzyme (DUB) which specifically recognizes lysine-63-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). BRISC is a DUB complex containing three other subunits, BRCC36, ABRO1 and BRCC45. It specifically hydrolyzes lysine-63 polyubiquitin chains, and is involved in multiple biological processes, including IFN-mediated antiviral immune regulation and inflammatory reaction. BABAM1 likely serves as a scaffold protein by integrating other components to form a functional complex. Furthermore, BABAM1 has been shown to play a critical role in BRISC-mediated regulation of Tankyrase1 (TNKS1) function during spindle assembly; it directly binds to the ankyrin repeat cluster V (ARC-V) domain of TNKS1 via its RXXPEG motif. BABAM1 contains a Von-Willebrand factor A (vWA) domain that is distantly related to classical vWA domains. Pssm-ID: 411071 Cd Length: 216 Bit Score: 34.53 E-value: 7.15e-03
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ViaA | COG2425 | Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ... |
4-99 | 8.89e-03 | |||
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown]; Pssm-ID: 441973 [Multi-domain] Cd Length: 263 Bit Score: 34.27 E-value: 8.89e-03
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Blast search parameters | ||||
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