tectonin beta-propeller repeat-containing protein [Drosophila virilis]
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
Gal-bind_lectin | pfam00337 | Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ... |
821-953 | 7.13e-36 | ||||
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also includes enzymes such as human eosinophil lysophospholipase (EC:3.1.1.5). : Pssm-ID: 459768 Cd Length: 124 Bit Score: 132.38 E-value: 7.13e-36
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Tectonin super family | cl41172 | Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ... |
1164-1332 | 6.28e-18 | ||||
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a 6 bladed beta propeller structure. The actual alignment was detected with superfamily member pfam19193: Pssm-ID: 465992 [Multi-domain] Cd Length: 215 Bit Score: 83.84 E-value: 6.28e-18
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Tectonin super family | cl41172 | Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ... |
210-392 | 1.05e-17 | ||||
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a 6 bladed beta propeller structure. The actual alignment was detected with superfamily member pfam19193: Pssm-ID: 465992 [Multi-domain] Cd Length: 215 Bit Score: 83.46 E-value: 1.05e-17
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DysFC | smart00694 | Dysferlin domain, C-terminal region; Domain of unknown function present in yeast peroxisomal ... |
1092-1125 | 1.43e-11 | ||||
Dysferlin domain, C-terminal region; Domain of unknown function present in yeast peroxisomal proteins, dysferlin, myoferlin and hypothetical proteins. Due to an insertion of a dysferlin domain within a second dysferlin domain we have chosen to predict these domains in two parts: the N-terminal region and the C-terminal region. : Pssm-ID: 128935 Cd Length: 34 Bit Score: 59.92 E-value: 1.43e-11
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DysFN | smart00693 | Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal ... |
64-125 | 6.24e-10 | ||||
Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal proteins, dysferlin, myoferlin and hypothetical proteins. Due to an insertion of a dysferlin domain within a second dysferlin domain we have chosen to predict these domains in two parts: the N-terminal region and the C-terminal region. : Pssm-ID: 214777 Cd Length: 62 Bit Score: 56.38 E-value: 6.24e-10
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PH-like super family | cl17171 | Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ... |
643-764 | 4.82e-09 | ||||
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins. The actual alignment was detected with superfamily member cd13300: Pssm-ID: 473070 Cd Length: 122 Bit Score: 55.56 E-value: 4.82e-09
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DysFN | smart00693 | Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal ... |
1021-1081 | 1.90e-08 | ||||
Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal proteins, dysferlin, myoferlin and hypothetical proteins. Due to an insertion of a dysferlin domain within a second dysferlin domain we have chosen to predict these domains in two parts: the N-terminal region and the C-terminal region. : Pssm-ID: 214777 Cd Length: 62 Bit Score: 52.14 E-value: 1.90e-08
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TECPR | smart00706 | Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ... |
966-1000 | 2.31e-05 | ||||
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal hypothetical proteins; : Pssm-ID: 214782 [Multi-domain] Cd Length: 35 Bit Score: 42.48 E-value: 2.31e-05
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Name | Accession | Description | Interval | E-value | ||||
Gal-bind_lectin | pfam00337 | Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ... |
821-953 | 7.13e-36 | ||||
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also includes enzymes such as human eosinophil lysophospholipase (EC:3.1.1.5). Pssm-ID: 459768 Cd Length: 124 Bit Score: 132.38 E-value: 7.13e-36
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Gal-bind_lectin | smart00908 | Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ... |
822-953 | 2.91e-35 | ||||
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction. Pssm-ID: 214904 Cd Length: 122 Bit Score: 130.40 E-value: 2.91e-35
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GLECT | cd00070 | Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ... |
815-953 | 7.92e-31 | ||||
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as lactose, and does not require metal ions for activity. GLECT domains occur as homodimers or tandemly repeated domains. They are developmentally regulated and may be involved in differentiation, cell-cell interaction and cellular regulation. Pssm-ID: 238025 Cd Length: 127 Bit Score: 118.12 E-value: 7.92e-31
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Tectonin | pfam19193 | Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ... |
1164-1332 | 6.28e-18 | ||||
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a 6 bladed beta propeller structure. Pssm-ID: 465992 [Multi-domain] Cd Length: 215 Bit Score: 83.84 E-value: 6.28e-18
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Tectonin | pfam19193 | Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ... |
210-392 | 1.05e-17 | ||||
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a 6 bladed beta propeller structure. Pssm-ID: 465992 [Multi-domain] Cd Length: 215 Bit Score: 83.46 E-value: 1.05e-17
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DysFC | smart00694 | Dysferlin domain, C-terminal region; Domain of unknown function present in yeast peroxisomal ... |
1092-1125 | 1.43e-11 | ||||
Dysferlin domain, C-terminal region; Domain of unknown function present in yeast peroxisomal proteins, dysferlin, myoferlin and hypothetical proteins. Due to an insertion of a dysferlin domain within a second dysferlin domain we have chosen to predict these domains in two parts: the N-terminal region and the C-terminal region. Pssm-ID: 128935 Cd Length: 34 Bit Score: 59.92 E-value: 1.43e-11
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DysFN | smart00693 | Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal ... |
64-125 | 6.24e-10 | ||||
Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal proteins, dysferlin, myoferlin and hypothetical proteins. Due to an insertion of a dysferlin domain within a second dysferlin domain we have chosen to predict these domains in two parts: the N-terminal region and the C-terminal region. Pssm-ID: 214777 Cd Length: 62 Bit Score: 56.38 E-value: 6.24e-10
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PH1_TECPR1 | cd13300 | Tectonin beta-propeller repeat-containing protein 1 Pleckstrin homology (PH) domain, repeat 1; ... |
643-764 | 4.82e-09 | ||||
Tectonin beta-propeller repeat-containing protein 1 Pleckstrin homology (PH) domain, repeat 1; TECPR1 is a tethering factor involved in autophagy. It promotes the autophagosome fusion with lysosomes by associating with both the ATG5-ATG12 conjugate and phosphatidylinositol-3-phosphate (PtdIns3P) present at the surface of autophagosomes. TECPR1 is also involved in selective autophagy against bacterial pathogens, by being required for phagophore/preautophagosomal structure biogenesis and maturation. It contains 2 DysFN (Dysferlin domains of unknown function, N-terminal), 2 Hyd_WA domains that is a probably beta-propeller, a PH-like domain, a TECPR domain, and a DysFC (C-terminal). The PH domain mediates the binding to phosphatidylinositol-3-phosphate (PtdIns3P). Binding to the ATG5-ATG12 conjugate exposes the PH domain, allowing the association with PtdIns3P. 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: 270112 Cd Length: 122 Bit Score: 55.56 E-value: 4.82e-09
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DysFN | smart00693 | Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal ... |
1021-1081 | 1.90e-08 | ||||
Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal proteins, dysferlin, myoferlin and hypothetical proteins. Due to an insertion of a dysferlin domain within a second dysferlin domain we have chosen to predict these domains in two parts: the N-terminal region and the C-terminal region. Pssm-ID: 214777 Cd Length: 62 Bit Score: 52.14 E-value: 1.90e-08
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TECPR | smart00706 | Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ... |
966-1000 | 2.31e-05 | ||||
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal hypothetical proteins; Pssm-ID: 214782 [Multi-domain] Cd Length: 35 Bit Score: 42.48 E-value: 2.31e-05
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TECPR | smart00706 | Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ... |
1188-1222 | 4.33e-05 | ||||
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal hypothetical proteins; Pssm-ID: 214782 [Multi-domain] Cd Length: 35 Bit Score: 41.71 E-value: 4.33e-05
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TECPR | smart00706 | Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ... |
345-378 | 1.99e-04 | ||||
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal hypothetical proteins; Pssm-ID: 214782 [Multi-domain] Cd Length: 35 Bit Score: 39.79 E-value: 1.99e-04
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Pex24p | pfam06398 | Integral peroxisomal membrane peroxin; Peroxisomes play diverse roles in the cell, ... |
1024-1118 | 1.17e-03 | ||||
Integral peroxisomal membrane peroxin; Peroxisomes play diverse roles in the cell, compartmentalising many activities related to lipid metabolism and functioning in the decomposition of toxic hydrogen peroxide. Sequence similarity was identified between two hypothetical proteins and the peroxin integral membrane protein Pex24p. Pssm-ID: 399414 [Multi-domain] Cd Length: 369 Bit Score: 42.80 E-value: 1.17e-03
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Pex24p | pfam06398 | Integral peroxisomal membrane peroxin; Peroxisomes play diverse roles in the cell, ... |
64-160 | 1.78e-03 | ||||
Integral peroxisomal membrane peroxin; Peroxisomes play diverse roles in the cell, compartmentalising many activities related to lipid metabolism and functioning in the decomposition of toxic hydrogen peroxide. Sequence similarity was identified between two hypothetical proteins and the peroxin integral membrane protein Pex24p. Pssm-ID: 399414 [Multi-domain] Cd Length: 369 Bit Score: 42.41 E-value: 1.78e-03
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Name | Accession | Description | Interval | E-value | ||||
Gal-bind_lectin | pfam00337 | Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ... |
821-953 | 7.13e-36 | ||||
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also includes enzymes such as human eosinophil lysophospholipase (EC:3.1.1.5). Pssm-ID: 459768 Cd Length: 124 Bit Score: 132.38 E-value: 7.13e-36
|
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Gal-bind_lectin | smart00908 | Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ... |
822-953 | 2.91e-35 | ||||
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction. Pssm-ID: 214904 Cd Length: 122 Bit Score: 130.40 E-value: 2.91e-35
|
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GLECT | cd00070 | Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ... |
815-953 | 7.92e-31 | ||||
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as lactose, and does not require metal ions for activity. GLECT domains occur as homodimers or tandemly repeated domains. They are developmentally regulated and may be involved in differentiation, cell-cell interaction and cellular regulation. Pssm-ID: 238025 Cd Length: 127 Bit Score: 118.12 E-value: 7.92e-31
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GLECT | smart00276 | Galectin; Galectin - galactose-binding lectin |
816-954 | 3.49e-28 | ||||
Galectin; Galectin - galactose-binding lectin Pssm-ID: 214596 Cd Length: 128 Bit Score: 110.40 E-value: 3.49e-28
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Tectonin | pfam19193 | Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ... |
1164-1332 | 6.28e-18 | ||||
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a 6 bladed beta propeller structure. Pssm-ID: 465992 [Multi-domain] Cd Length: 215 Bit Score: 83.84 E-value: 6.28e-18
|
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Tectonin | pfam19193 | Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ... |
210-392 | 1.05e-17 | ||||
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a 6 bladed beta propeller structure. Pssm-ID: 465992 [Multi-domain] Cd Length: 215 Bit Score: 83.46 E-value: 1.05e-17
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Tectonin | pfam19193 | Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ... |
1164-1311 | 9.93e-14 | ||||
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a 6 bladed beta propeller structure. Pssm-ID: 465992 [Multi-domain] Cd Length: 215 Bit Score: 71.90 E-value: 9.93e-14
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DysFC | smart00694 | Dysferlin domain, C-terminal region; Domain of unknown function present in yeast peroxisomal ... |
1092-1125 | 1.43e-11 | ||||
Dysferlin domain, C-terminal region; Domain of unknown function present in yeast peroxisomal proteins, dysferlin, myoferlin and hypothetical proteins. Due to an insertion of a dysferlin domain within a second dysferlin domain we have chosen to predict these domains in two parts: the N-terminal region and the C-terminal region. Pssm-ID: 128935 Cd Length: 34 Bit Score: 59.92 E-value: 1.43e-11
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Tectonin | pfam19193 | Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ... |
205-317 | 7.45e-11 | ||||
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a 6 bladed beta propeller structure. Pssm-ID: 465992 [Multi-domain] Cd Length: 215 Bit Score: 63.43 E-value: 7.45e-11
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DysFN | smart00693 | Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal ... |
64-125 | 6.24e-10 | ||||
Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal proteins, dysferlin, myoferlin and hypothetical proteins. Due to an insertion of a dysferlin domain within a second dysferlin domain we have chosen to predict these domains in two parts: the N-terminal region and the C-terminal region. Pssm-ID: 214777 Cd Length: 62 Bit Score: 56.38 E-value: 6.24e-10
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PH1_TECPR1 | cd13300 | Tectonin beta-propeller repeat-containing protein 1 Pleckstrin homology (PH) domain, repeat 1; ... |
643-764 | 4.82e-09 | ||||
Tectonin beta-propeller repeat-containing protein 1 Pleckstrin homology (PH) domain, repeat 1; TECPR1 is a tethering factor involved in autophagy. It promotes the autophagosome fusion with lysosomes by associating with both the ATG5-ATG12 conjugate and phosphatidylinositol-3-phosphate (PtdIns3P) present at the surface of autophagosomes. TECPR1 is also involved in selective autophagy against bacterial pathogens, by being required for phagophore/preautophagosomal structure biogenesis and maturation. It contains 2 DysFN (Dysferlin domains of unknown function, N-terminal), 2 Hyd_WA domains that is a probably beta-propeller, a PH-like domain, a TECPR domain, and a DysFC (C-terminal). The PH domain mediates the binding to phosphatidylinositol-3-phosphate (PtdIns3P). Binding to the ATG5-ATG12 conjugate exposes the PH domain, allowing the association with PtdIns3P. 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: 270112 Cd Length: 122 Bit Score: 55.56 E-value: 4.82e-09
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DysFN | smart00693 | Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal ... |
1021-1081 | 1.90e-08 | ||||
Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal proteins, dysferlin, myoferlin and hypothetical proteins. Due to an insertion of a dysferlin domain within a second dysferlin domain we have chosen to predict these domains in two parts: the N-terminal region and the C-terminal region. Pssm-ID: 214777 Cd Length: 62 Bit Score: 52.14 E-value: 1.90e-08
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Hyd_WA | pfam06462 | Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from ... |
1207-1236 | 3.34e-08 | ||||
Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from plasmodia of Physarum polycephalum (Slime mold) and both proteins contain six tandem repeats that are each 33-37 amino acids in length. Homologous repeats are found in L-6, a bacterial lipopolysaccharide-binding lectin from horseshoe crab hemocytes. The repetitive sequences of the tectonins and L-6 are reminiscent of the WD repeats of the beta-subunit of G proteins, suggesting that they form beta-propeller domains. The tectonins may be lectins that function as part of a transmembrane signalling complex during phagocytosis. Tectonin beta-propeller repeat-containing protein 1 (TECPR1) has a critical function during autophagosome maturation and autophagosome-lysosome fusion. Pssm-ID: 461921 [Multi-domain] Cd Length: 30 Bit Score: 50.49 E-value: 3.34e-08
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Hyd_WA | pfam06462 | Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from ... |
1164-1191 | 6.95e-07 | ||||
Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from plasmodia of Physarum polycephalum (Slime mold) and both proteins contain six tandem repeats that are each 33-37 amino acids in length. Homologous repeats are found in L-6, a bacterial lipopolysaccharide-binding lectin from horseshoe crab hemocytes. The repetitive sequences of the tectonins and L-6 are reminiscent of the WD repeats of the beta-subunit of G proteins, suggesting that they form beta-propeller domains. The tectonins may be lectins that function as part of a transmembrane signalling complex during phagocytosis. Tectonin beta-propeller repeat-containing protein 1 (TECPR1) has a critical function during autophagosome maturation and autophagosome-lysosome fusion. Pssm-ID: 461921 [Multi-domain] Cd Length: 30 Bit Score: 46.64 E-value: 6.95e-07
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Tectonin | pfam19193 | Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ... |
1196-1333 | 6.96e-07 | ||||
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a 6 bladed beta propeller structure. Pssm-ID: 465992 [Multi-domain] Cd Length: 215 Bit Score: 51.49 E-value: 6.96e-07
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Hyd_WA | pfam06462 | Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from ... |
256-282 | 5.88e-06 | ||||
Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from plasmodia of Physarum polycephalum (Slime mold) and both proteins contain six tandem repeats that are each 33-37 amino acids in length. Homologous repeats are found in L-6, a bacterial lipopolysaccharide-binding lectin from horseshoe crab hemocytes. The repetitive sequences of the tectonins and L-6 are reminiscent of the WD repeats of the beta-subunit of G proteins, suggesting that they form beta-propeller domains. The tectonins may be lectins that function as part of a transmembrane signalling complex during phagocytosis. Tectonin beta-propeller repeat-containing protein 1 (TECPR1) has a critical function during autophagosome maturation and autophagosome-lysosome fusion. Pssm-ID: 461921 [Multi-domain] Cd Length: 30 Bit Score: 43.94 E-value: 5.88e-06
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Hyd_WA | pfam06462 | Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from ... |
1307-1332 | 1.28e-05 | ||||
Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from plasmodia of Physarum polycephalum (Slime mold) and both proteins contain six tandem repeats that are each 33-37 amino acids in length. Homologous repeats are found in L-6, a bacterial lipopolysaccharide-binding lectin from horseshoe crab hemocytes. The repetitive sequences of the tectonins and L-6 are reminiscent of the WD repeats of the beta-subunit of G proteins, suggesting that they form beta-propeller domains. The tectonins may be lectins that function as part of a transmembrane signalling complex during phagocytosis. Tectonin beta-propeller repeat-containing protein 1 (TECPR1) has a critical function during autophagosome maturation and autophagosome-lysosome fusion. Pssm-ID: 461921 [Multi-domain] Cd Length: 30 Bit Score: 43.17 E-value: 1.28e-05
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TECPR | smart00706 | Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ... |
966-1000 | 2.31e-05 | ||||
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal hypothetical proteins; Pssm-ID: 214782 [Multi-domain] Cd Length: 35 Bit Score: 42.48 E-value: 2.31e-05
|
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TECPR | smart00706 | Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ... |
1188-1222 | 4.33e-05 | ||||
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal hypothetical proteins; Pssm-ID: 214782 [Multi-domain] Cd Length: 35 Bit Score: 41.71 E-value: 4.33e-05
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Hyd_WA | pfam06462 | Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from ... |
210-238 | 9.07e-05 | ||||
Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from plasmodia of Physarum polycephalum (Slime mold) and both proteins contain six tandem repeats that are each 33-37 amino acids in length. Homologous repeats are found in L-6, a bacterial lipopolysaccharide-binding lectin from horseshoe crab hemocytes. The repetitive sequences of the tectonins and L-6 are reminiscent of the WD repeats of the beta-subunit of G proteins, suggesting that they form beta-propeller domains. The tectonins may be lectins that function as part of a transmembrane signalling complex during phagocytosis. Tectonin beta-propeller repeat-containing protein 1 (TECPR1) has a critical function during autophagosome maturation and autophagosome-lysosome fusion. Pssm-ID: 461921 [Multi-domain] Cd Length: 30 Bit Score: 40.86 E-value: 9.07e-05
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Tectonin | pfam19193 | Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ... |
303-392 | 1.75e-04 | ||||
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a 6 bladed beta propeller structure. Pssm-ID: 465992 [Multi-domain] Cd Length: 215 Bit Score: 44.55 E-value: 1.75e-04
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TECPR | smart00706 | Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ... |
345-378 | 1.99e-04 | ||||
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal hypothetical proteins; Pssm-ID: 214782 [Multi-domain] Cd Length: 35 Bit Score: 39.79 E-value: 1.99e-04
|
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TECPR | smart00706 | Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ... |
234-271 | 8.85e-04 | ||||
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal hypothetical proteins; Pssm-ID: 214782 [Multi-domain] Cd Length: 35 Bit Score: 37.86 E-value: 8.85e-04
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Pex24p | pfam06398 | Integral peroxisomal membrane peroxin; Peroxisomes play diverse roles in the cell, ... |
1024-1118 | 1.17e-03 | ||||
Integral peroxisomal membrane peroxin; Peroxisomes play diverse roles in the cell, compartmentalising many activities related to lipid metabolism and functioning in the decomposition of toxic hydrogen peroxide. Sequence similarity was identified between two hypothetical proteins and the peroxin integral membrane protein Pex24p. Pssm-ID: 399414 [Multi-domain] Cd Length: 369 Bit Score: 42.80 E-value: 1.17e-03
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Pex24p | pfam06398 | Integral peroxisomal membrane peroxin; Peroxisomes play diverse roles in the cell, ... |
64-160 | 1.78e-03 | ||||
Integral peroxisomal membrane peroxin; Peroxisomes play diverse roles in the cell, compartmentalising many activities related to lipid metabolism and functioning in the decomposition of toxic hydrogen peroxide. Sequence similarity was identified between two hypothetical proteins and the peroxin integral membrane protein Pex24p. Pssm-ID: 399414 [Multi-domain] Cd Length: 369 Bit Score: 42.41 E-value: 1.78e-03
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TECPR | smart00706 | Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ... |
300-327 | 3.06e-03 | ||||
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal hypothetical proteins; Pssm-ID: 214782 [Multi-domain] Cd Length: 35 Bit Score: 36.32 E-value: 3.06e-03
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Hyd_WA | pfam06462 | Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from ... |
1254-1280 | 3.94e-03 | ||||
Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from plasmodia of Physarum polycephalum (Slime mold) and both proteins contain six tandem repeats that are each 33-37 amino acids in length. Homologous repeats are found in L-6, a bacterial lipopolysaccharide-binding lectin from horseshoe crab hemocytes. The repetitive sequences of the tectonins and L-6 are reminiscent of the WD repeats of the beta-subunit of G proteins, suggesting that they form beta-propeller domains. The tectonins may be lectins that function as part of a transmembrane signalling complex during phagocytosis. Tectonin beta-propeller repeat-containing protein 1 (TECPR1) has a critical function during autophagosome maturation and autophagosome-lysosome fusion. Pssm-ID: 461921 [Multi-domain] Cd Length: 30 Bit Score: 36.24 E-value: 3.94e-03
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