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von Willebrand factor A domain-containing protein 3B isoform X6 [Homo sapiens]
VWA domain-containing protein; VWA domain-containing protein; vWA domain-containing protein( domain architecture ID 10077493)
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 (von Willebrand factor type A) domain-containing protein; 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 (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 (von Willebrand factor type A) domain-containing protein, similar to Dictyostelium discoideum integrin beta-like protein A and mammalian calcium-activated chloride channel regulator; VWA (von Willebrand factor type A) domain-containing protein with an extracellular solute-binding protein (SBP) domain; VWA (von Willebrand factor type A) domain-containing protein, similar to Dictyostelium discoideum integrin beta-like protein A and mammalian calcium-activated chloride channel regulator; VWA (von Willebrand factor type A) domain-containing protein; VWA (von Willebrand factor type A) domain-containing protein similar to Bos taurus von Willebrand factor A domain-containing protein 7; 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 (von Willebrand factor type A) domain-containing protein with C-terminal prealbumin-like fold domain that is similar to Corynebacterium diphtheriae domain 1 and domain 3 of surface-anchored protein fimbrial subunit SpaA; VWA (von Willebrand factor type A) domain-containing protein; VWA (von Willebrand factor type A) domain-containing protein similar to Bos taurus von Willebrand factor A domain-containing protein 7; VWA (von Willebrand factor type A) domain-containing protein; VWA (von Willebrand factor type A) domain-containing protein similar to Bos taurus von Willebrand factor A domain-containing protein 7; VWA (von Willebrand factor type A) domain-containing protein, similar to Dictyostelium discoideum integrin beta-like protein A and mammalian calcium-activated chloride channel regulator; VWA (von Willebrand factor type A) domain-containing protein; 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 (von Willebrand factor type A) domain-containing protein; VWA (von Willebrand factor type A) domain-containing protein with C-terminal prealbumin-like fold domain that is similar to bacterial pilin adhesin subunit SpaC; von Willebrand factor type A (vWA) domain containing protein, often found at C-terminus of CalY family proteins
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
DUF4537 | pfam15057 | Domain of unknown function (DUF4537); The function of this domain family is unknown. It is ... |
694-820 | 1.65e-43 | |||
Domain of unknown function (DUF4537); The function of this domain family is unknown. It is found in eukaryotes, and is typically between 119 and 141 amino acids in length. In humans, it is found in the chromosomal position C11orf16. : Pssm-ID: 464475 [Multi-domain] Cd Length: 124 Bit Score: 153.62 E-value: 1.65e-43
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ChlD | COG1240 | vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
166-315 | 1.13e-19 | |||
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: 90.00 E-value: 1.13e-19
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Name | Accession | Description | Interval | E-value | ||||
DUF4537 | pfam15057 | Domain of unknown function (DUF4537); The function of this domain family is unknown. It is ... |
694-820 | 1.65e-43 | ||||
Domain of unknown function (DUF4537); The function of this domain family is unknown. It is found in eukaryotes, and is typically between 119 and 141 amino acids in length. In humans, it is found in the chromosomal position C11orf16. Pssm-ID: 464475 [Multi-domain] Cd Length: 124 Bit Score: 153.62 E-value: 1.65e-43
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ChlD | COG1240 | vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
166-315 | 1.13e-19 | ||||
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: 90.00 E-value: 1.13e-19
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vWFA | cd00198 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
165-316 | 2.99e-19 | ||||
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: 85.70 E-value: 2.99e-19
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VWA_3 | pfam13768 | von Willebrand factor type A domain; |
166-315 | 2.05e-14 | ||||
von Willebrand factor type A domain; Pssm-ID: 372716 [Multi-domain] Cd Length: 155 Bit Score: 71.66 E-value: 2.05e-14
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VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
166-318 | 5.04e-11 | ||||
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: 62.47 E-value: 5.04e-11
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acidobact_VWFA | TIGR03436 | VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ... |
168-317 | 6.73e-05 | ||||
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196. Pssm-ID: 274577 [Multi-domain] Cd Length: 296 Bit Score: 45.76 E-value: 6.73e-05
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Tudor_53BP1 | cd20383 | Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; ... |
694-734 | 2.57e-03 | ||||
Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; 53BP1, also called p53-binding protein 1 (p53BP1), is a double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics, and class-switch recombination (CSR) during antibody genesis. It plays a key role in the repair of DSBs in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1. It is recruited to DSB sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSB sites. 53BP1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Pssm-ID: 410454 Cd Length: 52 Bit Score: 36.86 E-value: 2.57e-03
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Name | Accession | Description | Interval | E-value | ||||
DUF4537 | pfam15057 | Domain of unknown function (DUF4537); The function of this domain family is unknown. It is ... |
694-820 | 1.65e-43 | ||||
Domain of unknown function (DUF4537); The function of this domain family is unknown. It is found in eukaryotes, and is typically between 119 and 141 amino acids in length. In humans, it is found in the chromosomal position C11orf16. Pssm-ID: 464475 [Multi-domain] Cd Length: 124 Bit Score: 153.62 E-value: 1.65e-43
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ChlD | COG1240 | vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
166-315 | 1.13e-19 | ||||
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: 90.00 E-value: 1.13e-19
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vWFA | cd00198 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
165-316 | 2.99e-19 | ||||
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: 85.70 E-value: 2.99e-19
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YfbK | COG2304 | Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ... |
168-315 | 7.09e-17 | ||||
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only]; Pssm-ID: 441879 [Multi-domain] Cd Length: 289 Bit Score: 82.07 E-value: 7.09e-17
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VWA_3 | pfam13768 | von Willebrand factor type A domain; |
166-315 | 2.05e-14 | ||||
von Willebrand factor type A domain; Pssm-ID: 372716 [Multi-domain] Cd Length: 155 Bit Score: 71.66 E-value: 2.05e-14
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vWA_interalpha_trypsin_inhibitor | cd01461 | vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ... |
169-314 | 4.50e-12 | ||||
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: 65.31 E-value: 4.50e-12
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ViaA | COG2425 | Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ... |
166-306 | 6.56e-12 | ||||
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown]; Pssm-ID: 441973 [Multi-domain] Cd Length: 263 Bit Score: 67.01 E-value: 6.56e-12
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VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
166-318 | 5.04e-11 | ||||
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: 62.47 E-value: 5.04e-11
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VWA | pfam00092 | von Willebrand factor type A domain; |
166-318 | 1.86e-10 | ||||
von Willebrand factor type A domain; Pssm-ID: 459670 [Multi-domain] Cd Length: 174 Bit Score: 60.75 E-value: 1.86e-10
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TerY | COG4245 | Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown]; |
160-289 | 2.44e-06 | ||||
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown]; Pssm-ID: 443387 [Multi-domain] Cd Length: 196 Bit Score: 49.15 E-value: 2.44e-06
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vWA_subgroup | cd01465 | VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
169-316 | 2.55e-06 | ||||
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: 48.42 E-value: 2.55e-06
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vWA_complement_factors | cd01470 | Complement factors B and C2 are two critical proteases for complement activation. They both ... |
166-316 | 2.56e-05 | ||||
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: 46.13 E-value: 2.56e-05
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vWA_C3HC4_type | cd01466 | VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
169-315 | 3.81e-05 | ||||
VWA C3HC4-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. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known. Pssm-ID: 238743 [Multi-domain] Cd Length: 155 Bit Score: 44.69 E-value: 3.81e-05
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acidobact_VWFA | TIGR03436 | VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ... |
168-317 | 6.73e-05 | ||||
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196. Pssm-ID: 274577 [Multi-domain] Cd Length: 296 Bit Score: 45.76 E-value: 6.73e-05
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vWFA_subfamily_ECM | cd01450 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
166-316 | 3.62e-04 | ||||
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: 42.28 E-value: 3.62e-04
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Tudor_53BP1 | cd20383 | Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; ... |
694-734 | 2.57e-03 | ||||
Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; 53BP1, also called p53-binding protein 1 (p53BP1), is a double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics, and class-switch recombination (CSR) during antibody genesis. It plays a key role in the repair of DSBs in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1. It is recruited to DSB sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSB sites. 53BP1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Pssm-ID: 410454 Cd Length: 52 Bit Score: 36.86 E-value: 2.57e-03
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VWA_2 | pfam13519 | von Willebrand factor type A domain; |
166-252 | 8.77e-03 | ||||
von Willebrand factor type A domain; Pssm-ID: 463909 [Multi-domain] Cd Length: 103 Bit Score: 36.89 E-value: 8.77e-03
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Blast search parameters | ||||
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