MAC/Perforin domain-containing protein [Arabidopsis thaliana]
Protein Classification
MACPF domain-containing protein( domain architecture ID 10485658)
MACPF (MAC/Perforin) domain-containing protein similar to human macrophage-expressed gene 1 protein (MPEG1) that plays a key role in the innate immune response following bacterial infection by inserting into the bacterial surface to form pores
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| MACPF | pfam01823 | MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ... |
106-325 | 1.64e-37 | ||||
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms transmembrane channels. These channels disrupt the phospholipid bilayer of target cells, leading to cell lysis and death. A number of proteins participate in the assembly of the MAC. Freshly activated C5b binds to C6 to form a C5b-6 complex, then to C7 forming the C5b-7 complex. The C5b-7 complex binds to C8, which is composed of three chains (alpha, beta, and gamma), thus forming the C5b-8 complex. C5b-8 subsequently binds to C9 and acts as a catalyst in the polymerization of C9. Active MAC has a subunit composition of C5b-C6-C7-C8-C9{n}. Perforin is a protein found in cytolytic T-cell and killer cells. In the presence of calcium, perforin polymerizes into transmembrane tubules and is capable of lysing, non-specifically, a variety of target cells. There are a number of regions of similarity in the sequences of complement components C6, C7, C8-alpha, C8-beta, C9 and perforin. The X-ray crystal structure of a MACPF domain reveals that it shares a common fold with bacterial cholesterol dependent cytolysins (pfam01289) such as perfringolysin O. Three key pieces of evidence suggests that MACPF domains and CDCs are homologous: Functional similarity (pore formation), conservation of three glycine residues at a hinge in both families and conservation of a complex core fold. : Pssm-ID: 460349 Cd Length: 211 Bit Score: 138.69 E-value: 1.64e-37
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| Name | Accession | Description | Interval | E-value | ||||
| MACPF | pfam01823 | MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ... |
106-325 | 1.64e-37 | ||||
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms transmembrane channels. These channels disrupt the phospholipid bilayer of target cells, leading to cell lysis and death. A number of proteins participate in the assembly of the MAC. Freshly activated C5b binds to C6 to form a C5b-6 complex, then to C7 forming the C5b-7 complex. The C5b-7 complex binds to C8, which is composed of three chains (alpha, beta, and gamma), thus forming the C5b-8 complex. C5b-8 subsequently binds to C9 and acts as a catalyst in the polymerization of C9. Active MAC has a subunit composition of C5b-C6-C7-C8-C9{n}. Perforin is a protein found in cytolytic T-cell and killer cells. In the presence of calcium, perforin polymerizes into transmembrane tubules and is capable of lysing, non-specifically, a variety of target cells. There are a number of regions of similarity in the sequences of complement components C6, C7, C8-alpha, C8-beta, C9 and perforin. The X-ray crystal structure of a MACPF domain reveals that it shares a common fold with bacterial cholesterol dependent cytolysins (pfam01289) such as perfringolysin O. Three key pieces of evidence suggests that MACPF domains and CDCs are homologous: Functional similarity (pore formation), conservation of three glycine residues at a hinge in both families and conservation of a complex core fold. Pssm-ID: 460349 Cd Length: 211 Bit Score: 138.69 E-value: 1.64e-37
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| MACPF | smart00457 | membrane-attack complex / perforin; |
137-327 | 5.49e-14 | ||||
membrane-attack complex / perforin; Pssm-ID: 214671 Cd Length: 195 Bit Score: 70.92 E-value: 5.49e-14
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| Name | Accession | Description | Interval | E-value | ||||
| MACPF | pfam01823 | MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ... |
106-325 | 1.64e-37 | ||||
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms transmembrane channels. These channels disrupt the phospholipid bilayer of target cells, leading to cell lysis and death. A number of proteins participate in the assembly of the MAC. Freshly activated C5b binds to C6 to form a C5b-6 complex, then to C7 forming the C5b-7 complex. The C5b-7 complex binds to C8, which is composed of three chains (alpha, beta, and gamma), thus forming the C5b-8 complex. C5b-8 subsequently binds to C9 and acts as a catalyst in the polymerization of C9. Active MAC has a subunit composition of C5b-C6-C7-C8-C9{n}. Perforin is a protein found in cytolytic T-cell and killer cells. In the presence of calcium, perforin polymerizes into transmembrane tubules and is capable of lysing, non-specifically, a variety of target cells. There are a number of regions of similarity in the sequences of complement components C6, C7, C8-alpha, C8-beta, C9 and perforin. The X-ray crystal structure of a MACPF domain reveals that it shares a common fold with bacterial cholesterol dependent cytolysins (pfam01289) such as perfringolysin O. Three key pieces of evidence suggests that MACPF domains and CDCs are homologous: Functional similarity (pore formation), conservation of three glycine residues at a hinge in both families and conservation of a complex core fold. Pssm-ID: 460349 Cd Length: 211 Bit Score: 138.69 E-value: 1.64e-37
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| MACPF | smart00457 | membrane-attack complex / perforin; |
137-327 | 5.49e-14 | ||||
membrane-attack complex / perforin; Pssm-ID: 214671 Cd Length: 195 Bit Score: 70.92 E-value: 5.49e-14
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