dynamin-2 isoform X19 [Mus musculus]
dynamin( domain architecture ID 10470541)
dynamin such as human dynamin-1, which is involved in clathrin-mediated endocytosis and other vesicular trafficking processes; contains an N-terminal GTPase domain that binds and hydrolyzes GTP, a middle domain involved in self-assembly and oligomerization, and a pleckstrin homology (PH) domain responsible for interactions with the GTPase effector domain (GED)
List of domain hits
Name | Accession | Description | Interval | E-value | |||
PH_dynamin | cd01256 | Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ... |
124-233 | 5.67e-73 | |||
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle formation. It has an N-terminal GTPase domain, followed by a PH domain, a GTPase effector domain and a C-terminal proline arginine rich domain. Dynamin-like proteins, which are found in metazoa, plants and yeast have the same domain architecture as dynamin, but lack the PH domain. 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: 269958 Cd Length: 112 Bit Score: 225.66 E-value: 5.67e-73
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Dynamin_M | pfam01031 | Dynamin central region; This is the stalk region which lies between the GTPase domain, see ... |
1-92 | 1.95e-37 | |||
Dynamin central region; This is the stalk region which lies between the GTPase domain, see pfam00350, and the pleckstrin homology (PH) domain, see pfam00169. This region dimerizes in a cross-like fashion forming a dynamin dimer in which the two G-domains are oriented in opposite directions. : Pssm-ID: 460033 Cd Length: 287 Bit Score: 138.42 E-value: 1.95e-37
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GED | pfam02212 | Dynamin GTPase effector domain; |
253-343 | 5.41e-32 | |||
Dynamin GTPase effector domain; : Pssm-ID: 460495 Cd Length: 91 Bit Score: 117.61 E-value: 5.41e-32
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PHA03247 super family | cl33720 | large tegument protein UL36; Provisional |
341-472 | 1.83e-07 | |||
large tegument protein UL36; Provisional The actual alignment was detected with superfamily member PHA03247: Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.17 E-value: 1.83e-07
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Name | Accession | Description | Interval | E-value | |||
PH_dynamin | cd01256 | Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ... |
124-233 | 5.67e-73 | |||
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle formation. It has an N-terminal GTPase domain, followed by a PH domain, a GTPase effector domain and a C-terminal proline arginine rich domain. Dynamin-like proteins, which are found in metazoa, plants and yeast have the same domain architecture as dynamin, but lack the PH domain. 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: 269958 Cd Length: 112 Bit Score: 225.66 E-value: 5.67e-73
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Dynamin_M | pfam01031 | Dynamin central region; This is the stalk region which lies between the GTPase domain, see ... |
1-92 | 1.95e-37 | |||
Dynamin central region; This is the stalk region which lies between the GTPase domain, see pfam00350, and the pleckstrin homology (PH) domain, see pfam00169. This region dimerizes in a cross-like fashion forming a dynamin dimer in which the two G-domains are oriented in opposite directions. Pssm-ID: 460033 Cd Length: 287 Bit Score: 138.42 E-value: 1.95e-37
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GED | pfam02212 | Dynamin GTPase effector domain; |
253-343 | 5.41e-32 | |||
Dynamin GTPase effector domain; Pssm-ID: 460495 Cd Length: 91 Bit Score: 117.61 E-value: 5.41e-32
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GED | smart00302 | Dynamin GTPase effector domain; |
252-343 | 8.00e-27 | |||
Dynamin GTPase effector domain; Pssm-ID: 128597 Cd Length: 92 Bit Score: 103.47 E-value: 8.00e-27
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PH | smart00233 | Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
124-227 | 8.01e-11 | |||
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 [Multi-domain] Cd Length: 102 Bit Score: 58.71 E-value: 8.01e-11
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PH | pfam00169 | PH domain; PH stands for pleckstrin homology. |
124-227 | 1.02e-09 | |||
PH domain; PH stands for pleckstrin homology. Pssm-ID: 459697 [Multi-domain] Cd Length: 105 Bit Score: 55.65 E-value: 1.02e-09
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
341-472 | 1.83e-07 | |||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.17 E-value: 1.83e-07
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Mucin-like | pfam16058 | Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ... |
344-437 | 2.06e-04 | |||
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated lipase, where is O-glycosylated. This region is composed of biased amino acid composition that is likely to be disordered. The region contains many repeats of an approximately 11 residue degenerate repeat. Pssm-ID: 464997 [Multi-domain] Cd Length: 94 Bit Score: 40.10 E-value: 2.06e-04
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KLF9_13_N-like | cd21975 | Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ... |
366-473 | 7.69e-03 | |||
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins. Pssm-ID: 409240 [Multi-domain] Cd Length: 163 Bit Score: 37.36 E-value: 7.69e-03
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Name | Accession | Description | Interval | E-value | ||||
PH_dynamin | cd01256 | Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ... |
124-233 | 5.67e-73 | ||||
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle formation. It has an N-terminal GTPase domain, followed by a PH domain, a GTPase effector domain and a C-terminal proline arginine rich domain. Dynamin-like proteins, which are found in metazoa, plants and yeast have the same domain architecture as dynamin, but lack the PH domain. 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: 269958 Cd Length: 112 Bit Score: 225.66 E-value: 5.67e-73
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Dynamin_M | pfam01031 | Dynamin central region; This is the stalk region which lies between the GTPase domain, see ... |
1-92 | 1.95e-37 | ||||
Dynamin central region; This is the stalk region which lies between the GTPase domain, see pfam00350, and the pleckstrin homology (PH) domain, see pfam00169. This region dimerizes in a cross-like fashion forming a dynamin dimer in which the two G-domains are oriented in opposite directions. Pssm-ID: 460033 Cd Length: 287 Bit Score: 138.42 E-value: 1.95e-37
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GED | pfam02212 | Dynamin GTPase effector domain; |
253-343 | 5.41e-32 | ||||
Dynamin GTPase effector domain; Pssm-ID: 460495 Cd Length: 91 Bit Score: 117.61 E-value: 5.41e-32
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GED | smart00302 | Dynamin GTPase effector domain; |
252-343 | 8.00e-27 | ||||
Dynamin GTPase effector domain; Pssm-ID: 128597 Cd Length: 92 Bit Score: 103.47 E-value: 8.00e-27
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PH | smart00233 | Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
124-227 | 8.01e-11 | ||||
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 [Multi-domain] Cd Length: 102 Bit Score: 58.71 E-value: 8.01e-11
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PH | pfam00169 | PH domain; PH stands for pleckstrin homology. |
124-227 | 1.02e-09 | ||||
PH domain; PH stands for pleckstrin homology. Pssm-ID: 459697 [Multi-domain] Cd Length: 105 Bit Score: 55.65 E-value: 1.02e-09
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PH | cd00821 | Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ... |
126-220 | 1.08e-07 | ||||
Pleckstrin homology (PH) domain; 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: 275388 [Multi-domain] Cd Length: 92 Bit Score: 49.46 E-value: 1.08e-07
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
341-472 | 1.83e-07 | ||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.17 E-value: 1.83e-07
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
344-471 | 3.88e-06 | ||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.94 E-value: 3.88e-06
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PRK14951 | PRK14951 | DNA polymerase III subunits gamma and tau; Provisional |
349-470 | 6.66e-06 | ||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 48.56 E-value: 6.66e-06
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
344-471 | 8.84e-06 | ||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.78 E-value: 8.84e-06
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
370-470 | 2.62e-05 | ||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.24 E-value: 2.62e-05
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PH_GRP1-like | cd01252 | General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 ... |
124-220 | 5.67e-05 | ||||
General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 and the related proteins ARNO (ARF nucleotide-binding site opener)/cytohesin-2 and cytohesin-1 are ARF exchange factors that contain a pleckstrin homology (PH) domain thought to target these proteins to cell membranes through binding polyphosphoinositides. The PH domains of all three proteins exhibit relatively high affinity for PtdIns(3,4,5)P3. Within the Grp1 family, diglycine (2G) and triglycine (3G) splice variants, differing only in the number of glycine residues in the PH domain, strongly influence the affinity and specificity for phosphoinositides. The 2G variants selectively bind PtdIns(3,4,5)P3 with high affinity,the 3G variants bind PtdIns(3,4,5)P3 with about 30-fold lower affinity and require the polybasic region for plasma membrane targeting. These ARF-GEFs share a common, tripartite structure consisting of an N-terminal coiled-coil domain, a central domain with homology to the yeast protein Sec7, a PH domain, and a C-terminal polybasic region. The Sec7 domain is autoinhibited by conserved elements proximal to the PH domain. GRP1 binds to the DNA binding domain of certain nuclear receptors (TRalpha, TRbeta, AR, ER, but not RXR), and can repress thyroid hormone receptor (TR)-mediated transactivation by decreasing TR-complex formation on thyroid hormone response elements. ARNO promotes sequential activation of Arf6, Cdc42 and Rac1 and insulin secretion. Cytohesin acts as a PI 3-kinase effector mediating biological responses including cell spreading and adhesion, chemotaxis, protein trafficking, and cytoskeletal rearrangements, only some of which appear to depend on their ability to activate ARFs. 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: 269954 Cd Length: 119 Bit Score: 42.69 E-value: 5.67e-05
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
346-471 | 6.23e-05 | ||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.70 E-value: 6.23e-05
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PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
342-471 | 7.23e-05 | ||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.55 E-value: 7.23e-05
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PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
349-471 | 1.06e-04 | ||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.16 E-value: 1.06e-04
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
369-470 | 1.20e-04 | ||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 1.20e-04
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
351-471 | 1.37e-04 | ||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 1.37e-04
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PRK12323 | PRK12323 | DNA polymerase III subunit gamma/tau; |
351-471 | 1.61e-04 | ||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.10 E-value: 1.61e-04
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Mucin-like | pfam16058 | Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ... |
344-437 | 2.06e-04 | ||||
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated lipase, where is O-glycosylated. This region is composed of biased amino acid composition that is likely to be disordered. The region contains many repeats of an approximately 11 residue degenerate repeat. Pssm-ID: 464997 [Multi-domain] Cd Length: 94 Bit Score: 40.10 E-value: 2.06e-04
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
369-470 | 2.47e-04 | ||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.77 E-value: 2.47e-04
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PHA03321 | PHA03321 | tegument protein VP11/12; Provisional |
368-461 | 2.50e-04 | ||||
tegument protein VP11/12; Provisional Pssm-ID: 223041 [Multi-domain] Cd Length: 694 Bit Score: 43.79 E-value: 2.50e-04
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PRK12323 | PRK12323 | DNA polymerase III subunit gamma/tau; |
369-472 | 3.05e-04 | ||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 43.33 E-value: 3.05e-04
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
343-462 | 3.51e-04 | ||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.39 E-value: 3.51e-04
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PHA03418 | PHA03418 | hypothetical E4 protein; Provisional |
367-459 | 3.96e-04 | ||||
hypothetical E4 protein; Provisional Pssm-ID: 177646 [Multi-domain] Cd Length: 230 Bit Score: 42.03 E-value: 3.96e-04
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PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
351-470 | 4.27e-04 | ||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.05 E-value: 4.27e-04
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PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
339-470 | 4.69e-04 | ||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.67 E-value: 4.69e-04
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
343-470 | 7.02e-04 | ||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.62 E-value: 7.02e-04
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PHA01929 | PHA01929 | putative scaffolding protein |
345-440 | 7.63e-04 | ||||
putative scaffolding protein Pssm-ID: 177328 Cd Length: 306 Bit Score: 41.58 E-value: 7.63e-04
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PRK14963 | PRK14963 | DNA polymerase III subunits gamma and tau; Provisional |
313-419 | 8.23e-04 | ||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 184927 [Multi-domain] Cd Length: 504 Bit Score: 41.75 E-value: 8.23e-04
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PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
364-471 | 9.03e-04 | ||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.90 E-value: 9.03e-04
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
364-474 | 1.09e-03 | ||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.85 E-value: 1.09e-03
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PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
305-463 | 1.37e-03 | ||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.31 E-value: 1.37e-03
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
349-472 | 2.42e-03 | ||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.69 E-value: 2.42e-03
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PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
333-471 | 2.68e-03 | ||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 40.54 E-value: 2.68e-03
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PHA03379 | PHA03379 | EBNA-3A; Provisional |
344-471 | 3.37e-03 | ||||
EBNA-3A; Provisional Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 40.04 E-value: 3.37e-03
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PH_PEPP1_2_3 | cd13248 | Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ... |
124-220 | 3.74e-03 | ||||
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; PEPP1 (also called PLEKHA4/PH domain-containing family A member 4 and RHOXF1/Rhox homeobox family member 1), and related homologs PEPP2 (also called PLEKHA5/PH domain-containing family A member 5) and PEPP3 (also called PLEKHA6/PH domain-containing family A member 6), have PH domains that interact specifically with PtdIns(3,4)P3. Other proteins that bind PtdIns(3,4)P3 specifically are: TAPP1 (tandem PH-domain-containing protein-1) and TAPP2], PtdIns3P AtPH1, and Ptd- Ins(3,5)P2 (centaurin-beta2). All of these proteins contain at least 5 of the 6 conserved amino acids that make up the putative phosphatidylinositol 3,4,5- trisphosphate-binding motif (PPBM) located at their N-terminus. 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: 270068 Cd Length: 104 Bit Score: 36.87 E-value: 3.74e-03
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PHA03264 | PHA03264 | envelope glycoprotein D; Provisional |
353-463 | 5.15e-03 | ||||
envelope glycoprotein D; Provisional Pssm-ID: 223029 [Multi-domain] Cd Length: 416 Bit Score: 39.22 E-value: 5.15e-03
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PRK12323 | PRK12323 | DNA polymerase III subunit gamma/tau; |
364-470 | 6.41e-03 | ||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 39.09 E-value: 6.41e-03
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KLF9_13_N-like | cd21975 | Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ... |
366-473 | 7.69e-03 | ||||
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins. Pssm-ID: 409240 [Multi-domain] Cd Length: 163 Bit Score: 37.36 E-value: 7.69e-03
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KLF14_N | cd21576 | N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ... |
365-460 | 7.94e-03 | ||||
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as Krueppel-like factor 14 or basic transcription element-binding protein 5/BTEB5) is a protein that in humans is encoded by the KLF14 gene. KLF14 regulates the transcription of various genes, including TGFbetaRII (the type II receptor for TGFbeta). KLF14 is expressed in many tissues, lacks introns, and is subject to parent-specific expression. It also appears to be a master regulator of gene expression in adipose tissue. KLF14 is associated with coronary artery disease, hypercholesterolemia, and type 2 diabetes. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF14 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF14. Pssm-ID: 409238 [Multi-domain] Cd Length: 195 Bit Score: 37.49 E-value: 7.94e-03
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PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
369-471 | 9.31e-03 | ||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 38.43 E-value: 9.31e-03
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
326-468 | 9.43e-03 | ||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 38.77 E-value: 9.43e-03
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PRK14951 | PRK14951 | DNA polymerase III subunits gamma and tau; Provisional |
344-441 | 9.55e-03 | ||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 38.54 E-value: 9.55e-03
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PH3_MyoX-like | cd13297 | Myosin X-like Pleckstrin homology (PH) domain, repeat 3; MyoX, a MyTH-FERM myosin, is a ... |
124-157 | 9.70e-03 | ||||
Myosin X-like Pleckstrin homology (PH) domain, repeat 3; MyoX, a MyTH-FERM myosin, is a molecular motor that has crucial functions in the transport and/or tethering of integrins in the actin-based extensions known as filopodia, microtubule binding, and in netrin-mediated axon guidance. It functions as a dimer. MyoX walks on bundles of actin, rather than single filaments, unlike the other unconventional myosins. MyoX is present in organisms ranging from humans to choanoflagellates, but not in Drosophila and Caenorhabditis elegans.MyoX consists of a N-terminal motor/head region, a neck made of 3 IQ motifs, and a tail consisting of a coiled-coil domain, a PEST region, 3 PH domains, a myosin tail homology 4 (MyTH4), and a FERM domain at its very C-terminus. The first PH domain in the MyoX tail is a split-PH domain, interupted by the second PH domain such that PH 1a and PH 1b flanks PH 2. The third PH domain (PH 3) follows the PH 1b domain. This cd contains the third MyoX PH repeat. PLEKHH3/Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) member 3 is also part of this CD and like MyoX contains a FERM domain, a MyTH4 domain, and a single PH domain. Not much is known about the function of PLEKHH3. 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: 270109 Cd Length: 126 Bit Score: 36.26 E-value: 9.70e-03
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