partitioning defective 3 homolog isoform X15 [Mus musculus]
partitioning defective 3 homolog( domain architecture ID 10572431)
partitioning defective 3 homolog is a PDZ (PSD-95, Dlg, and ZO-1/2) domain-containing protein that functions as an adapter protein involved in asymmetrical cell division and cell polarization processes
List of domain hits
Name | Accession | Description | Interval | E-value | |||
DUF3534 | pfam12053 | N-terminal of Par3 and HAL proteins; This presumed domain is functionally uncharacterized. ... |
2-83 | 1.07e-50 | |||
N-terminal of Par3 and HAL proteins; This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 150 amino acids in length. This eukaryotic domain is found associated with pfam00595. It has a conserved GILD sequence motif. Family members have been found to be essential for cell polarity establishment and maintenance such as Par3 (partitioning defective) and involved in conversion of histidine into ammonia (a crucial step for forming histamine in humans) such as Histidine ammonia lyase (HAL). This N-terminal domain is found to mediate oligomerization critical for the membrane localization of Par-3. It is also found to possess a self-association capacity via a front-to-back mode in Par-3 and HAL proteins. However, unlike the Par-3 N-terminal domain which self-assembles into a left-handed helical filament, the HAL N-terminal domain does not tend to form a helical filament but rather self-assembles into circular oligomeric particles. This has been suggested to be likely due to the absence of equivalent charged residues that are essential for the longitudinal packing of the Par-3 N-terminal domain filament. : Pssm-ID: 432291 Cd Length: 82 Bit Score: 171.37 E-value: 1.07e-50
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PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
465-544 | 1.70e-17 | |||
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: 77.61 E-value: 1.70e-17
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PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
588-681 | 1.51e-14 | |||
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: 69.13 E-value: 1.51e-14
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PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
272-347 | 3.27e-09 | |||
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: 54.11 E-value: 3.27e-09
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Name | Accession | Description | Interval | E-value | ||||
DUF3534 | pfam12053 | N-terminal of Par3 and HAL proteins; This presumed domain is functionally uncharacterized. ... |
2-83 | 1.07e-50 | ||||
N-terminal of Par3 and HAL proteins; This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 150 amino acids in length. This eukaryotic domain is found associated with pfam00595. It has a conserved GILD sequence motif. Family members have been found to be essential for cell polarity establishment and maintenance such as Par3 (partitioning defective) and involved in conversion of histidine into ammonia (a crucial step for forming histamine in humans) such as Histidine ammonia lyase (HAL). This N-terminal domain is found to mediate oligomerization critical for the membrane localization of Par-3. It is also found to possess a self-association capacity via a front-to-back mode in Par-3 and HAL proteins. However, unlike the Par-3 N-terminal domain which self-assembles into a left-handed helical filament, the HAL N-terminal domain does not tend to form a helical filament but rather self-assembles into circular oligomeric particles. This has been suggested to be likely due to the absence of equivalent charged residues that are essential for the longitudinal packing of the Par-3 N-terminal domain filament. Pssm-ID: 432291 Cd Length: 82 Bit Score: 171.37 E-value: 1.07e-50
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PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
465-544 | 1.70e-17 | ||||
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: 77.61 E-value: 1.70e-17
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PDZ | smart00228 | Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ... |
458-547 | 4.84e-17 | ||||
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: 76.26 E-value: 4.84e-17
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PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
588-681 | 1.51e-14 | ||||
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: 69.13 E-value: 1.51e-14
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PDZ | pfam00595 | PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins. |
462-544 | 6.47e-14 | ||||
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: 67.31 E-value: 6.47e-14
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PDZ | smart00228 | Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ... |
597-683 | 6.11e-13 | ||||
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: 64.71 E-value: 6.11e-13
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PDZ | pfam00595 | PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins. |
590-681 | 2.19e-10 | ||||
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: 57.29 E-value: 2.19e-10
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PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
272-347 | 3.27e-09 | ||||
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: 54.11 E-value: 3.27e-09
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PDZ | smart00228 | Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ... |
271-347 | 4.46e-07 | ||||
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: 48.14 E-value: 4.46e-07
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CtpA | COG0793 | C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ... |
449-547 | 8.54e-07 | ||||
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: 51.95 E-value: 8.54e-07
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PDZ | pfam00595 | PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins. |
281-347 | 3.48e-04 | ||||
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: 39.96 E-value: 3.48e-04
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degP_htrA_DO | TIGR02037 | periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ... |
489-649 | 8.71e-03 | ||||
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides] Pssm-ID: 273938 [Multi-domain] Cd Length: 428 Bit Score: 39.13 E-value: 8.71e-03
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Name | Accession | Description | Interval | E-value | ||||
DUF3534 | pfam12053 | N-terminal of Par3 and HAL proteins; This presumed domain is functionally uncharacterized. ... |
2-83 | 1.07e-50 | ||||
N-terminal of Par3 and HAL proteins; This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 150 amino acids in length. This eukaryotic domain is found associated with pfam00595. It has a conserved GILD sequence motif. Family members have been found to be essential for cell polarity establishment and maintenance such as Par3 (partitioning defective) and involved in conversion of histidine into ammonia (a crucial step for forming histamine in humans) such as Histidine ammonia lyase (HAL). This N-terminal domain is found to mediate oligomerization critical for the membrane localization of Par-3. It is also found to possess a self-association capacity via a front-to-back mode in Par-3 and HAL proteins. However, unlike the Par-3 N-terminal domain which self-assembles into a left-handed helical filament, the HAL N-terminal domain does not tend to form a helical filament but rather self-assembles into circular oligomeric particles. This has been suggested to be likely due to the absence of equivalent charged residues that are essential for the longitudinal packing of the Par-3 N-terminal domain filament. Pssm-ID: 432291 Cd Length: 82 Bit Score: 171.37 E-value: 1.07e-50
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PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
465-544 | 1.70e-17 | ||||
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: 77.61 E-value: 1.70e-17
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PDZ | smart00228 | Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ... |
458-547 | 4.84e-17 | ||||
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: 76.26 E-value: 4.84e-17
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PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
588-681 | 1.51e-14 | ||||
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: 69.13 E-value: 1.51e-14
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PDZ | pfam00595 | PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins. |
462-544 | 6.47e-14 | ||||
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: 67.31 E-value: 6.47e-14
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PDZ | smart00228 | Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ... |
597-683 | 6.11e-13 | ||||
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: 64.71 E-value: 6.11e-13
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PDZ | cd00136 | PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ... |
470-544 | 2.09e-10 | ||||
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: 56.93 E-value: 2.09e-10
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PDZ | pfam00595 | PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins. |
590-681 | 2.19e-10 | ||||
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: 57.29 E-value: 2.19e-10
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PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
272-347 | 3.27e-09 | ||||
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: 54.11 E-value: 3.27e-09
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PDZ | cd00136 | PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ... |
600-669 | 3.73e-08 | ||||
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: 50.77 E-value: 3.73e-08
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PDZ | smart00228 | Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ... |
271-347 | 4.46e-07 | ||||
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: 48.14 E-value: 4.46e-07
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CtpA | COG0793 | C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ... |
449-547 | 8.54e-07 | ||||
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: 51.95 E-value: 8.54e-07
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PDZ_CTP_protease | cd00988 | PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ... |
469-549 | 3.85e-05 | ||||
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: 42.60 E-value: 3.85e-05
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PDZ | cd00136 | PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ... |
282-352 | 1.83e-04 | ||||
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: 40.37 E-value: 1.83e-04
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PDZ | pfam00595 | PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins. |
281-347 | 3.48e-04 | ||||
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: 39.96 E-value: 3.48e-04
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PDZ_CTP_protease | cd00988 | PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ... |
599-663 | 4.76e-04 | ||||
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: 39.52 E-value: 4.76e-04
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PDZ_serine_protease | cd00987 | PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ... |
488-546 | 3.36e-03 | ||||
PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins involved in heat-shock response, chaperone function, and apoptosis. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, though 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: 238487 [Multi-domain] Cd Length: 90 Bit Score: 37.23 E-value: 3.36e-03
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PDZ_metalloprotease | cd00989 | PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ... |
470-552 | 5.14e-03 | ||||
PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or integral membrane proteases, which may be involved in signalling and regulatory mechanisms. 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: 238489 [Multi-domain] Cd Length: 79 Bit Score: 36.44 E-value: 5.14e-03
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degP_htrA_DO | TIGR02037 | periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ... |
489-649 | 8.71e-03 | ||||
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides] Pssm-ID: 273938 [Multi-domain] Cd Length: 428 Bit Score: 39.13 E-value: 8.71e-03
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PDZ_6 | pfam17820 | PDZ domain; This entry represents the PDZ domain from a wide variety of proteins. |
489-546 | 9.54e-03 | ||||
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins. Pssm-ID: 436067 [Multi-domain] Cd Length: 54 Bit Score: 34.81 E-value: 9.54e-03
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Blast search parameters | ||||
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