lymphocyte antigen 86 isoform X1 [Mus musculus]
ML domain-containing protein( domain architecture ID 5313)
ML (MD-2-related lipid-recognition) domain-containing protein; the ML domain is present in MD-1, MD-2, GM2 activator protein, Niemann-Pick type C2 (Npc2) protein, phosphatidylinositol/phosphatidylglycerol transfer protein (PG/PI-TP), mite allergen Der p 2 and several proteins of unknown function in plants, animals and fungi; it is predicted to mediate diverse biological functions through interaction with specific lipids
List of domain hits
Name | Accession | Description | Interval | E-value | |||
ML super family | cl00274 | The ML (MD-2-related lipid-recognition) domain is present in MD-1, MD-2, GM2 activator protein, ... |
30-118 | 1.31e-40 | |||
The ML (MD-2-related lipid-recognition) domain is present in MD-1, MD-2, GM2 activator protein, Niemann-Pick type C2 (Npc2) protein, phosphatidylinositol/phosphatidylglycerol transfer protein (PG/PI-TP), mite allergen Der p 2 and several proteins of unknown function in plants, animals and fungi. These single-domain proteins form two anti-parallel beta-pleated sheets stabilized by three disulfide bonds and with an accessible central hydrophobic cavity, and are predicted to mediate diverse biological functions through interaction with specific lipids. The actual alignment was detected with superfamily member cd00915: Pssm-ID: 469700 Cd Length: 130 Bit Score: 131.53 E-value: 1.31e-40
|
|||||||
Name | Accession | Description | Interval | E-value | |||
MD-1_MD-2 | cd00915 | MD-1 and MD-2 are cofactors required for LPS signaling through cell surface receptors. MD-2 ... |
30-118 | 1.31e-40 | |||
MD-1 and MD-2 are cofactors required for LPS signaling through cell surface receptors. MD-2 and its binding partner, Toll-like receptor 4 (TLR4), are essential for the innate immune responses of mammalian cells to bacterial lipopolysaccharide (LPS); MD-2 directly binds the lipid A moiety of LPS. The TLR4-like receptor, RP105, which mediates LPS-induced lymphocyte proliferation, interacts with MD-1; MD-1 enhances RP105-mediated LPS-induced growth of B cells. These proteins belong to the ML domain family. Pssm-ID: 238457 Cd Length: 130 Bit Score: 131.53 E-value: 1.31e-40
|
|||||||
ML | smart00737 | Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ... |
42-118 | 1.05e-13 | |||
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) is a novel domain identified in MD-1, MD-2, GM2A, Npc2 and multiple proteins of unknown function in plants, animals and fungi. These single-domain proteins were predicted to form a beta-rich fold containing multiple strands, and to mediate diverse biological functions through interacting with specific lipids. Pssm-ID: 214796 Cd Length: 119 Bit Score: 62.38 E-value: 1.05e-13
|
|||||||
Name | Accession | Description | Interval | E-value | |||
MD-1_MD-2 | cd00915 | MD-1 and MD-2 are cofactors required for LPS signaling through cell surface receptors. MD-2 ... |
30-118 | 1.31e-40 | |||
MD-1 and MD-2 are cofactors required for LPS signaling through cell surface receptors. MD-2 and its binding partner, Toll-like receptor 4 (TLR4), are essential for the innate immune responses of mammalian cells to bacterial lipopolysaccharide (LPS); MD-2 directly binds the lipid A moiety of LPS. The TLR4-like receptor, RP105, which mediates LPS-induced lymphocyte proliferation, interacts with MD-1; MD-1 enhances RP105-mediated LPS-induced growth of B cells. These proteins belong to the ML domain family. Pssm-ID: 238457 Cd Length: 130 Bit Score: 131.53 E-value: 1.31e-40
|
|||||||
ML | smart00737 | Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ... |
42-118 | 1.05e-13 | |||
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) is a novel domain identified in MD-1, MD-2, GM2A, Npc2 and multiple proteins of unknown function in plants, animals and fungi. These single-domain proteins were predicted to form a beta-rich fold containing multiple strands, and to mediate diverse biological functions through interacting with specific lipids. Pssm-ID: 214796 Cd Length: 119 Bit Score: 62.38 E-value: 1.05e-13
|
|||||||
ML | cd00912 | The ML (MD-2-related lipid-recognition) domain is present in MD-1, MD-2, GM2 activator protein, ... |
30-117 | 3.96e-12 | |||
The ML (MD-2-related lipid-recognition) domain is present in MD-1, MD-2, GM2 activator protein, Niemann-Pick type C2 (Npc2) protein, phosphatidylinositol/phosphatidylglycerol transfer protein (PG/PI-TP), mite allergen Der p 2 and several proteins of unknown function in plants, animals and fungi. These single-domain proteins form two anti-parallel beta-pleated sheets stabilized by three disulfide bonds and with an accessible central hydrophobic cavity, and are predicted to mediate diverse biological functions through interaction with specific lipids. Pssm-ID: 238454 Cd Length: 127 Bit Score: 58.68 E-value: 3.96e-12
|
|||||||
Blast search parameters | ||||
|