alpha-1-syntrophin isoform 1 [Homo sapiens]
PDZ_signaling and PHsplit_syntrophin domain-containing protein( domain architecture ID 11538998)
protein containing domains PDZ_signaling, PHsplit_syntrophin, and PH
List of domain hits
Name | Accession | Description | Interval | E-value | |||
PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
86-167 | 2.86e-25 | |||
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases. : Pssm-ID: 238492 [Multi-domain] Cd Length: 82 Bit Score: 98.79 E-value: 2.86e-25
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PHsplit_syntrophin | cd01258 | Syntrophin Split Pleckstrin homology (PH) domain; Syntrophins are scaffold proteins that ... |
209-270 | 6.62e-23 | |||
Syntrophin Split Pleckstrin homology (PH) domain; Syntrophins are scaffold proteins that associate with associate with the Duchenne muscular dystrophy protein dystrophin and the dystrophin-related proteins, utrophin and dystrobrevin to form the dystrophin glycoprotein complex (DGC). There are 5 members: alpha, beta1, beta2, gamma1, and gamma2) all of which contains a split (also called joined) PH domain and a PDZ domain (PHN-PDZ-PHC). The split PH domain of alpha-syntrophin adopts a canonical PH domain fold and together with PDZ forms a supramodule functioning synergistically in binding to inositol phospholipids. The alpha-syntrophin PH-PDZ supramodule showed strong binding to phosphoinositides PI(3,5)P2 and PI(5)P, modest binding to PI(3,4)P2 and PI(4,5)P2, and weak binding to PI(3)P, PI(4)P, and PI(3,4,5)P. There are a large number of signaling proteins that bind to the PDZ domain of syntrophins: nitric oxide synthase (nNOS), aquaporin-4, voltage-gated sodium channels, potassium channels, serine/threonine protein kinases, and the ATP-binding cassette transporter A1. 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: 269960 Cd Length: 89 Bit Score: 92.74 E-value: 6.62e-23
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PH | pfam00169 | PH domain; PH stands for pleckstrin homology. |
298-401 | 2.99e-08 | |||
PH domain; PH stands for pleckstrin homology. : Pssm-ID: 395117 [Multi-domain] Cd Length: 105 Bit Score: 51.41 E-value: 2.99e-08
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Name | Accession | Description | Interval | E-value | |||
PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
86-167 | 2.86e-25 | |||
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases. Pssm-ID: 238492 [Multi-domain] Cd Length: 82 Bit Score: 98.79 E-value: 2.86e-25
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PHsplit_syntrophin | cd01258 | Syntrophin Split Pleckstrin homology (PH) domain; Syntrophins are scaffold proteins that ... |
209-270 | 6.62e-23 | |||
Syntrophin Split Pleckstrin homology (PH) domain; Syntrophins are scaffold proteins that associate with associate with the Duchenne muscular dystrophy protein dystrophin and the dystrophin-related proteins, utrophin and dystrobrevin to form the dystrophin glycoprotein complex (DGC). There are 5 members: alpha, beta1, beta2, gamma1, and gamma2) all of which contains a split (also called joined) PH domain and a PDZ domain (PHN-PDZ-PHC). The split PH domain of alpha-syntrophin adopts a canonical PH domain fold and together with PDZ forms a supramodule functioning synergistically in binding to inositol phospholipids. The alpha-syntrophin PH-PDZ supramodule showed strong binding to phosphoinositides PI(3,5)P2 and PI(5)P, modest binding to PI(3,4)P2 and PI(4,5)P2, and weak binding to PI(3)P, PI(4)P, and PI(3,4,5)P. There are a large number of signaling proteins that bind to the PDZ domain of syntrophins: nitric oxide synthase (nNOS), aquaporin-4, voltage-gated sodium channels, potassium channels, serine/threonine protein kinases, and the ATP-binding cassette transporter A1. 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: 269960 Cd Length: 89 Bit Score: 92.74 E-value: 6.62e-23
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PDZ | smart00228 | Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ... |
84-168 | 6.74e-21 | |||
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities. Pssm-ID: 214570 [Multi-domain] Cd Length: 85 Bit Score: 86.66 E-value: 6.74e-21
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PH_17 | pfam18012 | PH domain; This entry represents the C-terminal part of the split PH domain from syntrophin ... |
208-266 | 5.53e-18 | |||
PH domain; This entry represents the C-terminal part of the split PH domain from syntrophin proteins. Pssm-ID: 436210 Cd Length: 60 Bit Score: 77.83 E-value: 5.53e-18
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PDZ | pfam00595 | PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins. |
87-167 | 7.86e-17 | |||
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins. Pssm-ID: 395476 [Multi-domain] Cd Length: 81 Bit Score: 75.01 E-value: 7.86e-17
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PH | pfam00169 | PH domain; PH stands for pleckstrin homology. |
298-401 | 2.99e-08 | |||
PH domain; PH stands for pleckstrin homology. Pssm-ID: 395117 [Multi-domain] Cd Length: 105 Bit Score: 51.41 E-value: 2.99e-08
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CtpA | COG0793 | C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ... |
96-166 | 1.40e-04 | |||
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 223864 [Multi-domain] Cd Length: 406 Bit Score: 44.24 E-value: 1.40e-04
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PH | smart00233 | Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
298-401 | 2.55e-04 | |||
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids. Pssm-ID: 214574 Cd Length: 102 Bit Score: 40.22 E-value: 2.55e-04
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Name | Accession | Description | Interval | E-value | |||
PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
86-167 | 2.86e-25 | |||
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases. Pssm-ID: 238492 [Multi-domain] Cd Length: 82 Bit Score: 98.79 E-value: 2.86e-25
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PHsplit_syntrophin | cd01258 | Syntrophin Split Pleckstrin homology (PH) domain; Syntrophins are scaffold proteins that ... |
209-270 | 6.62e-23 | |||
Syntrophin Split Pleckstrin homology (PH) domain; Syntrophins are scaffold proteins that associate with associate with the Duchenne muscular dystrophy protein dystrophin and the dystrophin-related proteins, utrophin and dystrobrevin to form the dystrophin glycoprotein complex (DGC). There are 5 members: alpha, beta1, beta2, gamma1, and gamma2) all of which contains a split (also called joined) PH domain and a PDZ domain (PHN-PDZ-PHC). The split PH domain of alpha-syntrophin adopts a canonical PH domain fold and together with PDZ forms a supramodule functioning synergistically in binding to inositol phospholipids. The alpha-syntrophin PH-PDZ supramodule showed strong binding to phosphoinositides PI(3,5)P2 and PI(5)P, modest binding to PI(3,4)P2 and PI(4,5)P2, and weak binding to PI(3)P, PI(4)P, and PI(3,4,5)P. There are a large number of signaling proteins that bind to the PDZ domain of syntrophins: nitric oxide synthase (nNOS), aquaporin-4, voltage-gated sodium channels, potassium channels, serine/threonine protein kinases, and the ATP-binding cassette transporter A1. 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: 269960 Cd Length: 89 Bit Score: 92.74 E-value: 6.62e-23
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PDZ | smart00228 | Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ... |
84-168 | 6.74e-21 | |||
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities. Pssm-ID: 214570 [Multi-domain] Cd Length: 85 Bit Score: 86.66 E-value: 6.74e-21
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PH_17 | pfam18012 | PH domain; This entry represents the C-terminal part of the split PH domain from syntrophin ... |
208-266 | 5.53e-18 | |||
PH domain; This entry represents the C-terminal part of the split PH domain from syntrophin proteins. Pssm-ID: 436210 Cd Length: 60 Bit Score: 77.83 E-value: 5.53e-18
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PDZ | pfam00595 | PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins. |
87-167 | 7.86e-17 | |||
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins. Pssm-ID: 395476 [Multi-domain] Cd Length: 81 Bit Score: 75.01 E-value: 7.86e-17
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PDZ | cd00136 | PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ... |
96-167 | 6.26e-12 | |||
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein. Pssm-ID: 238080 [Multi-domain] Cd Length: 70 Bit Score: 60.78 E-value: 6.26e-12
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PH | pfam00169 | PH domain; PH stands for pleckstrin homology. |
298-401 | 2.99e-08 | |||
PH domain; PH stands for pleckstrin homology. Pssm-ID: 395117 [Multi-domain] Cd Length: 105 Bit Score: 51.41 E-value: 2.99e-08
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PDZ_CTP_protease | cd00988 | PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ... |
96-167 | 6.68e-08 | |||
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in posttranslational protein processing, maturation, and disassembly or degradation, in Bacteria, Archaea, and plant chloroplasts. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins. Pssm-ID: 238488 [Multi-domain] Cd Length: 85 Bit Score: 49.92 E-value: 6.68e-08
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CtpA | COG0793 | C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ... |
96-166 | 1.40e-04 | |||
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 223864 [Multi-domain] Cd Length: 406 Bit Score: 44.24 E-value: 1.40e-04
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PH | smart00233 | Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
298-401 | 2.55e-04 | |||
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids. Pssm-ID: 214574 Cd Length: 102 Bit Score: 40.22 E-value: 2.55e-04
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Blast search parameters | ||||
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