RecName: Full=von Willebrand factor A domain-containing protein 2; AltName: Full=A domain-containing protein similar to matrilin and collagen; Short=AMACO; Flags: Precursor
Protein Classification
vWA domain-containing protein( domain architecture ID 10844836)
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, hemostasis, signaling, chromosomal stability, malignant transformation, and immune defenses
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| vWA_collagen | cd01472 | von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ... |
50-204 | 2.15e-45 | ||||
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif. : Pssm-ID: 238749 [Multi-domain] Cd Length: 164 Bit Score: 160.09 E-value: 2.15e-45
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| vWFA super family | cl00057 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
530-687 | 2.27e-39 | ||||
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 cd01482: Pssm-ID: 469594 [Multi-domain] Cd Length: 164 Bit Score: 143.20 E-value: 2.27e-39
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| VWA | pfam00092 | von Willebrand factor type A domain; |
342-515 | 1.42e-25 | ||||
von Willebrand factor type A domain; : Pssm-ID: 459670 [Multi-domain] Cd Length: 174 Bit Score: 103.89 E-value: 1.42e-25
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| EGF_CA | cd00054 | Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
712-747 | 1.04e-09 | ||||
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements. : Pssm-ID: 238011 Cd Length: 38 Bit Score: 54.18 E-value: 1.04e-09
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| EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
298-328 | 4.29e-06 | ||||
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains. : Pssm-ID: 394967 Cd Length: 31 Bit Score: 43.91 E-value: 4.29e-06
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| Name | Accession | Description | Interval | E-value | ||||
| vWA_collagen | cd01472 | von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ... |
50-204 | 2.15e-45 | ||||
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif. Pssm-ID: 238749 [Multi-domain] Cd Length: 164 Bit Score: 160.09 E-value: 2.15e-45
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| VWA | pfam00092 | von Willebrand factor type A domain; |
51-204 | 1.83e-39 | ||||
von Willebrand factor type A domain; Pssm-ID: 459670 [Multi-domain] Cd Length: 174 Bit Score: 143.57 E-value: 1.83e-39
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| vWA_collagen_alphaI-XII-like | cd01482 | Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ... |
530-687 | 2.27e-39 | ||||
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions. Pssm-ID: 238759 [Multi-domain] Cd Length: 164 Bit Score: 143.20 E-value: 2.27e-39
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| VWA | pfam00092 | von Willebrand factor type A domain; |
530-679 | 4.14e-35 | ||||
von Willebrand factor type A domain; Pssm-ID: 459670 [Multi-domain] Cd Length: 174 Bit Score: 131.24 E-value: 4.14e-35
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| VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
51-212 | 6.81e-35 | ||||
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: 130.65 E-value: 6.81e-35
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| VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
530-704 | 4.16e-33 | ||||
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: 125.64 E-value: 4.16e-33
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| VWA | pfam00092 | von Willebrand factor type A domain; |
342-515 | 1.42e-25 | ||||
von Willebrand factor type A domain; Pssm-ID: 459670 [Multi-domain] Cd Length: 174 Bit Score: 103.89 E-value: 1.42e-25
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| vWA_collagen | cd01472 | von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ... |
341-494 | 4.35e-24 | ||||
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif. Pssm-ID: 238749 [Multi-domain] Cd Length: 164 Bit Score: 99.22 E-value: 4.35e-24
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| VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
342-513 | 6.87e-24 | ||||
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: 99.07 E-value: 6.87e-24
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| EGF_CA | cd00054 | Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
712-747 | 1.04e-09 | ||||
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements. Pssm-ID: 238011 Cd Length: 38 Bit Score: 54.18 E-value: 1.04e-09
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| ChlD | COG1240 | vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
502-678 | 1.40e-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: 59.57 E-value: 1.40e-09
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| ViaA | COG2425 | Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ... |
48-184 | 7.45e-08 | ||||
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown]; Pssm-ID: 441973 [Multi-domain] Cd Length: 263 Bit Score: 54.30 E-value: 7.45e-08
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| EGF_CA | smart00179 | Calcium-binding EGF-like domain; |
712-747 | 1.98e-07 | ||||
Calcium-binding EGF-like domain; Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 47.63 E-value: 1.98e-07
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| EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
298-328 | 4.29e-06 | ||||
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains. Pssm-ID: 394967 Cd Length: 31 Bit Score: 43.91 E-value: 4.29e-06
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| EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
715-745 | 5.03e-05 | ||||
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains. Pssm-ID: 394967 Cd Length: 31 Bit Score: 40.83 E-value: 5.03e-05
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| EGF | cd00053 | Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ... |
297-331 | 5.89e-05 | ||||
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium. Pssm-ID: 238010 Cd Length: 36 Bit Score: 40.92 E-value: 5.89e-05
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| EGF_CA | smart00179 | Calcium-binding EGF-like domain; |
298-331 | 6.79e-04 | ||||
Calcium-binding EGF-like domain; Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 38.00 E-value: 6.79e-04
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| Name | Accession | Description | Interval | E-value | ||||
| vWA_collagen | cd01472 | von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ... |
50-204 | 2.15e-45 | ||||
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif. Pssm-ID: 238749 [Multi-domain] Cd Length: 164 Bit Score: 160.09 E-value: 2.15e-45
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| vWA_Matrilin | cd01475 | VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ... |
48-258 | 4.45e-42 | ||||
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands. Pssm-ID: 238752 [Multi-domain] Cd Length: 224 Bit Score: 152.92 E-value: 4.45e-42
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| vWA_collagen_alphaI-XII-like | cd01482 | Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ... |
51-204 | 1.68e-40 | ||||
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions. Pssm-ID: 238759 [Multi-domain] Cd Length: 164 Bit Score: 146.28 E-value: 1.68e-40
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| VWA | pfam00092 | von Willebrand factor type A domain; |
51-204 | 1.83e-39 | ||||
von Willebrand factor type A domain; Pssm-ID: 459670 [Multi-domain] Cd Length: 174 Bit Score: 143.57 E-value: 1.83e-39
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| vWA_collagen_alphaI-XII-like | cd01482 | Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ... |
530-687 | 2.27e-39 | ||||
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions. Pssm-ID: 238759 [Multi-domain] Cd Length: 164 Bit Score: 143.20 E-value: 2.27e-39
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| vWFA_subfamily_ECM | cd01450 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
529-683 | 2.31e-38 | ||||
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: 140.12 E-value: 2.31e-38
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| vWFA_subfamily_ECM | cd01450 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
50-205 | 8.39e-38 | ||||
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: 138.58 E-value: 8.39e-38
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| VWA | pfam00092 | von Willebrand factor type A domain; |
530-679 | 4.14e-35 | ||||
von Willebrand factor type A domain; Pssm-ID: 459670 [Multi-domain] Cd Length: 174 Bit Score: 131.24 E-value: 4.14e-35
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| VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
51-212 | 6.81e-35 | ||||
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: 130.65 E-value: 6.81e-35
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| vWA_collagen | cd01472 | von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ... |
530-693 | 3.18e-34 | ||||
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif. Pssm-ID: 238749 [Multi-domain] Cd Length: 164 Bit Score: 128.50 E-value: 3.18e-34
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| VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
530-704 | 4.16e-33 | ||||
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: 125.64 E-value: 4.16e-33
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| vWA_Matrilin | cd01475 | VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ... |
529-742 | 8.12e-32 | ||||
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands. Pssm-ID: 238752 [Multi-domain] Cd Length: 224 Bit Score: 123.65 E-value: 8.12e-32
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| vWFA | cd00198 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
50-204 | 1.32e-29 | ||||
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: 114.97 E-value: 1.32e-29
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| vWA_collagen_alpha3-VI-like | cd01481 | VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ... |
51-199 | 2.16e-28 | ||||
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions. Pssm-ID: 238758 Cd Length: 165 Bit Score: 111.65 E-value: 2.16e-28
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| vWA_integrins_alpha_subunit | cd01469 | Integrins are a class of adhesion receptors that link the extracellular matrix to the ... |
50-212 | 2.05e-26 | ||||
Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions. Pssm-ID: 238746 [Multi-domain] Cd Length: 177 Bit Score: 106.67 E-value: 2.05e-26
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| VWA | pfam00092 | von Willebrand factor type A domain; |
342-515 | 1.42e-25 | ||||
von Willebrand factor type A domain; Pssm-ID: 459670 [Multi-domain] Cd Length: 174 Bit Score: 103.89 E-value: 1.42e-25
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| vWA_collagen_alpha3-VI-like | cd01481 | VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ... |
530-668 | 4.10e-24 | ||||
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions. Pssm-ID: 238758 Cd Length: 165 Bit Score: 99.71 E-value: 4.10e-24
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| vWA_collagen | cd01472 | von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ... |
341-494 | 4.35e-24 | ||||
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif. Pssm-ID: 238749 [Multi-domain] Cd Length: 164 Bit Score: 99.22 E-value: 4.35e-24
|
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| VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
342-513 | 6.87e-24 | ||||
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: 99.07 E-value: 6.87e-24
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| vWFA_subfamily_ECM | cd01450 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
341-498 | 9.48e-23 | ||||
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: 95.44 E-value: 9.48e-23
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| vWA_collagen_alpha_1-VI-type | cd01480 | VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ... |
49-204 | 6.28e-22 | ||||
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions. Pssm-ID: 238757 [Multi-domain] Cd Length: 186 Bit Score: 93.99 E-value: 6.28e-22
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| VWA_integrin_invertebrates | cd01476 | VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ... |
529-679 | 3.86e-21 | ||||
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands. Pssm-ID: 238753 [Multi-domain] Cd Length: 163 Bit Score: 90.92 E-value: 3.86e-21
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| VWA_integrin_invertebrates | cd01476 | VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ... |
51-187 | 2.49e-20 | ||||
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands. Pssm-ID: 238753 [Multi-domain] Cd Length: 163 Bit Score: 88.61 E-value: 2.49e-20
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| vWA_integrins_alpha_subunit | cd01469 | Integrins are a class of adhesion receptors that link the extracellular matrix to the ... |
529-676 | 2.83e-20 | ||||
Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions. Pssm-ID: 238746 [Multi-domain] Cd Length: 177 Bit Score: 88.95 E-value: 2.83e-20
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| vWFA | cd00198 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
529-683 | 1.90e-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: 86.08 E-value: 1.90e-19
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| vWFA | cd00198 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
341-491 | 8.74e-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: 84.15 E-value: 8.74e-19
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| vWA_Matrilin | cd01475 | VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ... |
340-565 | 2.83e-18 | ||||
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands. Pssm-ID: 238752 [Multi-domain] Cd Length: 224 Bit Score: 84.36 E-value: 2.83e-18
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| vWA_collagen_alphaI-XII-like | cd01482 | Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ... |
342-493 | 1.77e-16 | ||||
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions. Pssm-ID: 238759 [Multi-domain] Cd Length: 164 Bit Score: 77.71 E-value: 1.77e-16
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| VWA_integrin_invertebrates | cd01476 | VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ... |
342-499 | 2.91e-16 | ||||
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands. Pssm-ID: 238753 [Multi-domain] Cd Length: 163 Bit Score: 77.05 E-value: 2.91e-16
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| vWA_micronemal_protein | cd01471 | Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ... |
50-183 | 1.28e-15 | ||||
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners. Pssm-ID: 238748 [Multi-domain] Cd Length: 186 Bit Score: 75.88 E-value: 1.28e-15
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| VWA_2 | pfam13519 | von Willebrand factor type A domain; |
52-155 | 7.99e-15 | ||||
von Willebrand factor type A domain; Pssm-ID: 463909 [Multi-domain] Cd Length: 103 Bit Score: 70.78 E-value: 7.99e-15
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| vWA_collagen_alpha3-VI-like | cd01481 | VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ... |
342-501 | 1.78e-14 | ||||
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions. Pssm-ID: 238758 Cd Length: 165 Bit Score: 71.97 E-value: 1.78e-14
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| vWA_micronemal_protein | cd01471 | Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ... |
529-683 | 3.80e-13 | ||||
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners. Pssm-ID: 238748 [Multi-domain] Cd Length: 186 Bit Score: 68.57 E-value: 3.80e-13
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| EGF_CA | cd00054 | Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
712-747 | 1.04e-09 | ||||
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements. Pssm-ID: 238011 Cd Length: 38 Bit Score: 54.18 E-value: 1.04e-09
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| vWA_collagen_alpha_1-VI-type | cd01480 | VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ... |
339-457 | 1.20e-09 | ||||
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions. Pssm-ID: 238757 [Multi-domain] Cd Length: 186 Bit Score: 58.55 E-value: 1.20e-09
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| ChlD | COG1240 | vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
502-678 | 1.40e-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: 59.57 E-value: 1.40e-09
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| vWA_integrins_alpha_subunit | cd01469 | Integrins are a class of adhesion receptors that link the extracellular matrix to the ... |
341-458 | 1.71e-09 | ||||
Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions. Pssm-ID: 238746 [Multi-domain] Cd Length: 177 Bit Score: 57.75 E-value: 1.71e-09
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| ViaA | COG2425 | Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ... |
48-184 | 7.45e-08 | ||||
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown]; Pssm-ID: 441973 [Multi-domain] Cd Length: 263 Bit Score: 54.30 E-value: 7.45e-08
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| EGF_CA | smart00179 | Calcium-binding EGF-like domain; |
712-747 | 1.98e-07 | ||||
Calcium-binding EGF-like domain; Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 47.63 E-value: 1.98e-07
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| EGF | cd00053 | Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ... |
717-747 | 8.01e-07 | ||||
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium. Pssm-ID: 238010 Cd Length: 36 Bit Score: 45.93 E-value: 8.01e-07
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| vWA_collagen_alpha_1-VI-type | cd01480 | VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ... |
529-678 | 8.80e-07 | ||||
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions. Pssm-ID: 238757 [Multi-domain] Cd Length: 186 Bit Score: 50.08 E-value: 8.80e-07
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| VWA_2 | pfam13519 | von Willebrand factor type A domain; |
531-638 | 8.91e-07 | ||||
von Willebrand factor type A domain; Pssm-ID: 463909 [Multi-domain] Cd Length: 103 Bit Score: 48.06 E-value: 8.91e-07
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| VWA_2 | pfam13519 | von Willebrand factor type A domain; |
343-451 | 2.08e-06 | ||||
von Willebrand factor type A domain; Pssm-ID: 463909 [Multi-domain] Cd Length: 103 Bit Score: 46.90 E-value: 2.08e-06
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| vWA_micronemal_protein | cd01471 | Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ... |
341-485 | 3.38e-06 | ||||
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners. Pssm-ID: 238748 [Multi-domain] Cd Length: 186 Bit Score: 48.15 E-value: 3.38e-06
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| EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
298-328 | 4.29e-06 | ||||
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains. Pssm-ID: 394967 Cd Length: 31 Bit Score: 43.91 E-value: 4.29e-06
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| vWA_complement_factors | cd01470 | Complement factors B and C2 are two critical proteases for complement activation. They both ... |
51-212 | 3.29e-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: 45.36 E-value: 3.29e-05
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| EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
715-745 | 5.03e-05 | ||||
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains. Pssm-ID: 394967 Cd Length: 31 Bit Score: 40.83 E-value: 5.03e-05
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| EGF | cd00053 | Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ... |
297-331 | 5.89e-05 | ||||
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium. Pssm-ID: 238010 Cd Length: 36 Bit Score: 40.92 E-value: 5.89e-05
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| vWA_ATR | cd01474 | ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ... |
46-199 | 9.36e-05 | ||||
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells. Pssm-ID: 238751 [Multi-domain] Cd Length: 185 Bit Score: 44.04 E-value: 9.36e-05
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| EGF_CA | cd00054 | Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
298-331 | 2.06e-04 | ||||
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements. Pssm-ID: 238011 Cd Length: 38 Bit Score: 39.16 E-value: 2.06e-04
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| EGF_2 | pfam07974 | EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins. |
720-746 | 3.75e-04 | ||||
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins. Pssm-ID: 400365 Cd Length: 26 Bit Score: 38.10 E-value: 3.75e-04
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| vWA_BatA_type | cd01467 | VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
48-184 | 6.23e-04 | ||||
VWA BatA 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 are bacterial in origin. They are typified by the presence of a MIDAS motif. Pssm-ID: 238744 [Multi-domain] Cd Length: 180 Bit Score: 41.55 E-value: 6.23e-04
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| EGF_CA | smart00179 | Calcium-binding EGF-like domain; |
298-331 | 6.79e-04 | ||||
Calcium-binding EGF-like domain; Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 38.00 E-value: 6.79e-04
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| EGF | smart00181 | Epidermal growth factor-like domain; |
717-747 | 7.02e-04 | ||||
Epidermal growth factor-like domain; Pssm-ID: 214544 Cd Length: 35 Bit Score: 37.88 E-value: 7.02e-04
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| SLR1-BP | pfam07333 | S locus-related glycoprotein 1 binding pollen coat protein (SLR1-BP); This family consists of ... |
283-321 | 1.11e-03 | ||||
S locus-related glycoprotein 1 binding pollen coat protein (SLR1-BP); This family consists of a number of cysteine rich SLR1 binding pollen coat like proteins. Adhesion of pollen grains to the stigmatic surface is a critical step during sexual reproduction in plants. In Brassica, S locus-related glycoprotein 1 (SLR1), a stigma-specific protein belonging to the S gene family of proteins, has been shown to be involved in this step. SLR1-BP specifically binds SLR1 with high affinity. The SLR1-BP gene is specifically expressed in pollen at late stages of development and is a member of the class A pollen coat protein (PCP) family, which includes PCP-A1, an SLG (S locus glycoprotein)-binding protein. Pssm-ID: 284695 Cd Length: 56 Bit Score: 37.85 E-value: 1.11e-03
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| vWA_ATR | cd01474 | ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ... |
530-682 | 1.30e-03 | ||||
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells. Pssm-ID: 238751 [Multi-domain] Cd Length: 185 Bit Score: 40.57 E-value: 1.30e-03
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| YfbK | COG2304 | Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ... |
529-678 | 1.71e-03 | ||||
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only]; Pssm-ID: 441879 [Multi-domain] Cd Length: 289 Bit Score: 41.24 E-value: 1.71e-03
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| hEGF | pfam12661 | Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ... |
720-741 | 4.66e-03 | ||||
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue. Pssm-ID: 463660 Cd Length: 22 Bit Score: 35.00 E-value: 4.66e-03
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| vWA_subgroup | cd01465 | VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
529-692 | 5.30e-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: 38.41 E-value: 5.30e-03
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| hEGF | pfam12661 | Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ... |
303-322 | 6.63e-03 | ||||
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue. Pssm-ID: 463660 Cd Length: 22 Bit Score: 34.62 E-value: 6.63e-03
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