Neurobeachin/BDCP, DUF4704 alpha solenoid region; This domain of unknown function is found in ...
1303-1826
1.81e-155
Neurobeachin/BDCP, DUF4704 alpha solenoid region; This domain of unknown function is found in eukaryotes on neurobeachin and BEACH domain-containing proteins (BDCPs). Mutations in this proteins are associated with Lipopolysaccharide-responsive and beige-like anchor (LRBA) deficiency. According to structure prediction is adopts an alpha-helical solenoid structure.
:
Pssm-ID: 464870 Cd Length: 486 Bit Score: 491.42 E-value: 1.81e-155
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
2376-2522
3.98e-21
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in several eukaroyotic proteins CHS, neurobeachin (Nbea), LRBA (also called BGL, beige-like, or CDC4L), FAN, KIAA1607, and LvsA-LvsF. CHS is a rare, autosomal recessive disorder that can cause severe immunodeficiency and albinism in mammals and beige is the name for the CHS disease in mice. The CHS disease is associated with the presence of giant, perinuclear vesicles (lysosomes, melanosomes, and others) and CHS protein is thought to play an important role in the fusion, fission, or trafficking of these vesicles. All BEACH proteins contain the following domains: PH, BEACH, and WD40. The WD40 domain is involved in mediating protein-protein interactions involved in targeting proteins to subcellular compartments. The combined PH-BEACH motifs may present a single continuous structural unit involved in protein binding. Some members have an additional N-terminal Laminin G-like (LamG) domains Ca++ mediated receptors or an additional C-terminal FYVE zinc-binding domain which targets proteins to membrane lipids via interaction with phosphatidylinositol-3-phosphate, PI3P. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
:
Pssm-ID: 275391 Cd Length: 112 Bit Score: 90.76 E-value: 3.98e-21
Domain of unknown function (DUF4800); This presumed domain is functionally uncharacterized. ...
2219-2275
3.26e-05
Domain of unknown function (DUF4800); This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 310 amino acids in length. The family is found in association with pfam02138, pfam00400. There is a conserved RDN sequence motif.
The actual alignment was detected with superfamily member pfam16057:
Pssm-ID: 464996 Cd Length: 254 Bit Score: 48.09 E-value: 3.26e-05
Neurobeachin/BDCP, DUF4704 alpha solenoid region; This domain of unknown function is found in ...
1303-1826
1.81e-155
Neurobeachin/BDCP, DUF4704 alpha solenoid region; This domain of unknown function is found in eukaryotes on neurobeachin and BEACH domain-containing proteins (BDCPs). Mutations in this proteins are associated with Lipopolysaccharide-responsive and beige-like anchor (LRBA) deficiency. According to structure prediction is adopts an alpha-helical solenoid structure.
Pssm-ID: 464870 Cd Length: 486 Bit Score: 491.42 E-value: 1.81e-155
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the ...
2556-2700
7.13e-84
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the highly homologous CHS protein. The BEACH domain is usually followed by a series of WD repeats. The function of the BEACH domain is unknown.
Pssm-ID: 214982 Cd Length: 280 Bit Score: 277.18 E-value: 7.13e-84
BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in ...
2556-2698
1.92e-73
BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in a family of proteins conserved throughout eukaryotes. This group contains human lysosomal trafficking regulator (LYST), LPS-responsive and beige-like anchor (LRBA) and neurobeachin. Disruption of LYST leads to Chediak-Higashi syndrome, characterized by severe immunodeficiency, albinism, poor blood coagulation and neurologic problems. Neurobeachin is a candidate gene linked to autism. LBRA seems to be upregulated in several cancer types. It has been shown that the BEACH domain itself is important for the function of these proteins.
Pssm-ID: 100117 [Multi-domain] Cd Length: 275 Bit Score: 247.16 E-value: 1.92e-73
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
2376-2522
3.98e-21
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in several eukaroyotic proteins CHS, neurobeachin (Nbea), LRBA (also called BGL, beige-like, or CDC4L), FAN, KIAA1607, and LvsA-LvsF. CHS is a rare, autosomal recessive disorder that can cause severe immunodeficiency and albinism in mammals and beige is the name for the CHS disease in mice. The CHS disease is associated with the presence of giant, perinuclear vesicles (lysosomes, melanosomes, and others) and CHS protein is thought to play an important role in the fusion, fission, or trafficking of these vesicles. All BEACH proteins contain the following domains: PH, BEACH, and WD40. The WD40 domain is involved in mediating protein-protein interactions involved in targeting proteins to subcellular compartments. The combined PH-BEACH motifs may present a single continuous structural unit involved in protein binding. Some members have an additional N-terminal Laminin G-like (LamG) domains Ca++ mediated receptors or an additional C-terminal FYVE zinc-binding domain which targets proteins to membrane lipids via interaction with phosphatidylinositol-3-phosphate, PI3P. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 275391 Cd Length: 112 Bit Score: 90.76 E-value: 3.98e-21
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the ...
2383-2519
1.37e-13
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the Beige/BEACH domain (pfam02138), it immediately precedes the Beige/BEACH domain.
Pssm-ID: 434260 Cd Length: 99 Bit Score: 68.83 E-value: 1.37e-13
Domain of unknown function (DUF4800); This presumed domain is functionally uncharacterized. ...
2219-2275
3.26e-05
Domain of unknown function (DUF4800); This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 310 amino acids in length. The family is found in association with pfam02138, pfam00400. There is a conserved RDN sequence motif.
Pssm-ID: 464996 Cd Length: 254 Bit Score: 48.09 E-value: 3.26e-05
Neurobeachin/BDCP, DUF4704 alpha solenoid region; This domain of unknown function is found in ...
1303-1826
1.81e-155
Neurobeachin/BDCP, DUF4704 alpha solenoid region; This domain of unknown function is found in eukaryotes on neurobeachin and BEACH domain-containing proteins (BDCPs). Mutations in this proteins are associated with Lipopolysaccharide-responsive and beige-like anchor (LRBA) deficiency. According to structure prediction is adopts an alpha-helical solenoid structure.
Pssm-ID: 464870 Cd Length: 486 Bit Score: 491.42 E-value: 1.81e-155
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the ...
2556-2700
7.13e-84
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the highly homologous CHS protein. The BEACH domain is usually followed by a series of WD repeats. The function of the BEACH domain is unknown.
Pssm-ID: 214982 Cd Length: 280 Bit Score: 277.18 E-value: 7.13e-84
BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in ...
2556-2698
1.92e-73
BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in a family of proteins conserved throughout eukaryotes. This group contains human lysosomal trafficking regulator (LYST), LPS-responsive and beige-like anchor (LRBA) and neurobeachin. Disruption of LYST leads to Chediak-Higashi syndrome, characterized by severe immunodeficiency, albinism, poor blood coagulation and neurologic problems. Neurobeachin is a candidate gene linked to autism. LBRA seems to be upregulated in several cancer types. It has been shown that the BEACH domain itself is important for the function of these proteins.
Pssm-ID: 100117 [Multi-domain] Cd Length: 275 Bit Score: 247.16 E-value: 1.92e-73
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
2376-2522
3.98e-21
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in several eukaroyotic proteins CHS, neurobeachin (Nbea), LRBA (also called BGL, beige-like, or CDC4L), FAN, KIAA1607, and LvsA-LvsF. CHS is a rare, autosomal recessive disorder that can cause severe immunodeficiency and albinism in mammals and beige is the name for the CHS disease in mice. The CHS disease is associated with the presence of giant, perinuclear vesicles (lysosomes, melanosomes, and others) and CHS protein is thought to play an important role in the fusion, fission, or trafficking of these vesicles. All BEACH proteins contain the following domains: PH, BEACH, and WD40. The WD40 domain is involved in mediating protein-protein interactions involved in targeting proteins to subcellular compartments. The combined PH-BEACH motifs may present a single continuous structural unit involved in protein binding. Some members have an additional N-terminal Laminin G-like (LamG) domains Ca++ mediated receptors or an additional C-terminal FYVE zinc-binding domain which targets proteins to membrane lipids via interaction with phosphatidylinositol-3-phosphate, PI3P. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 275391 Cd Length: 112 Bit Score: 90.76 E-value: 3.98e-21
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the ...
2383-2519
1.37e-13
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the Beige/BEACH domain (pfam02138), it immediately precedes the Beige/BEACH domain.
Pssm-ID: 434260 Cd Length: 99 Bit Score: 68.83 E-value: 1.37e-13
Domain of unknown function (DUF4800); This presumed domain is functionally uncharacterized. ...
2219-2275
3.26e-05
Domain of unknown function (DUF4800); This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 310 amino acids in length. The family is found in association with pfam02138, pfam00400. There is a conserved RDN sequence motif.
Pssm-ID: 464996 Cd Length: 254 Bit Score: 48.09 E-value: 3.26e-05
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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