polychaetoid, isoform A [Drosophila melanogaster]
SH3_ZO and GuKc domain-containing protein( domain architecture ID 10097950)
protein containing domains PDZ_signaling, SH3_ZO, GuKc, and ZU5
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
GuKc | smart00072 | Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ... |
604-780 | 1.21e-40 | ||||
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions. : Pssm-ID: 214504 [Multi-domain] Cd Length: 174 Bit Score: 148.60 E-value: 1.21e-40
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SH3_ZO | cd11859 | Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO ... |
502-563 | 5.11e-35 | ||||
Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO proteins are scaffolding proteins that associate with each other and with other proteins of the tight junction, zonula adherens, and gap junctions. They play roles in regulating cytoskeletal dynamics at these cell junctions. They are considered members of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. Vertebrates contain three ZO proteins (ZO-1, ZO-2, and ZO-3) with redundant and non-redundant roles. They contain three PDZ domains, followed by SH3 and GuK domains; in addition, ZO-1 and ZO-2 contains a proline-rich (PR) actin binding domain at the C-terminus while ZO-3 contains this PR domain between the second and third PDZ domains. The C-terminal regions of the three ZO proteins are unique. The SH3 domain of ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. : Pssm-ID: 212793 Cd Length: 62 Bit Score: 128.18 E-value: 5.11e-35
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ZU5 | pfam00791 | ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function. |
1959-2046 | 1.56e-28 | ||||
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function. : Pssm-ID: 425872 Cd Length: 96 Bit Score: 110.68 E-value: 1.56e-28
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PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
22-107 | 7.73e-21 | ||||
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: 88.39 E-value: 7.73e-21
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PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
406-483 | 4.50e-18 | ||||
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: 80.69 E-value: 4.50e-18
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PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
169-250 | 9.13e-06 | ||||
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: 45.64 E-value: 9.13e-06
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Name | Accession | Description | Interval | E-value | ||||
GuKc | smart00072 | Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ... |
604-780 | 1.21e-40 | ||||
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions. Pssm-ID: 214504 [Multi-domain] Cd Length: 174 Bit Score: 148.60 E-value: 1.21e-40
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SH3_ZO | cd11859 | Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO ... |
502-563 | 5.11e-35 | ||||
Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO proteins are scaffolding proteins that associate with each other and with other proteins of the tight junction, zonula adherens, and gap junctions. They play roles in regulating cytoskeletal dynamics at these cell junctions. They are considered members of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. Vertebrates contain three ZO proteins (ZO-1, ZO-2, and ZO-3) with redundant and non-redundant roles. They contain three PDZ domains, followed by SH3 and GuK domains; in addition, ZO-1 and ZO-2 contains a proline-rich (PR) actin binding domain at the C-terminus while ZO-3 contains this PR domain between the second and third PDZ domains. The C-terminal regions of the three ZO proteins are unique. The SH3 domain of ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212793 Cd Length: 62 Bit Score: 128.18 E-value: 5.11e-35
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ZU5 | pfam00791 | ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function. |
1959-2046 | 1.56e-28 | ||||
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function. Pssm-ID: 425872 Cd Length: 96 Bit Score: 110.68 E-value: 1.56e-28
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ZU5 | smart00218 | Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function. |
1957-2046 | 1.20e-22 | ||||
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function. Pssm-ID: 128514 Cd Length: 104 Bit Score: 94.34 E-value: 1.20e-22
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PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
22-107 | 7.73e-21 | ||||
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: 88.39 E-value: 7.73e-21
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PDZ | pfam00595 | PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins. |
23-107 | 3.12e-19 | ||||
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: 83.87 E-value: 3.12e-19
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PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
406-483 | 4.50e-18 | ||||
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: 80.69 E-value: 4.50e-18
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PDZ | smart00228 | Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ... |
405-486 | 7.46e-18 | ||||
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: 80.12 E-value: 7.46e-18
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PDZ | smart00228 | Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ... |
20-109 | 2.33e-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: 78.57 E-value: 2.33e-17
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PDZ | pfam00595 | PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins. |
409-483 | 2.45e-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: 70.00 E-value: 2.45e-14
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SH3_2 | pfam07653 | Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ... |
502-564 | 5.40e-09 | ||||
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organisation. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel. Pssm-ID: 429575 [Multi-domain] Cd Length: 54 Bit Score: 53.75 E-value: 5.40e-09
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CtpA | COG0793 | C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ... |
415-471 | 1.69e-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: 55.80 E-value: 1.69e-07
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Guanylate_kin | pfam00625 | Guanylate kinase; |
678-777 | 1.85e-07 | ||||
Guanylate kinase; Pssm-ID: 395500 Cd Length: 182 Bit Score: 53.15 E-value: 1.85e-07
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PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
169-250 | 9.13e-06 | ||||
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: 45.64 E-value: 9.13e-06
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degP_htrA_DO | TIGR02037 | periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ... |
424-483 | 1.40e-04 | ||||
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: 46.45 E-value: 1.40e-04
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CtpA | COG0793 | C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ... |
56-108 | 1.47e-03 | ||||
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: 43.09 E-value: 1.47e-03
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Name | Accession | Description | Interval | E-value | ||||
GuKc | smart00072 | Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ... |
604-780 | 1.21e-40 | ||||
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions. Pssm-ID: 214504 [Multi-domain] Cd Length: 174 Bit Score: 148.60 E-value: 1.21e-40
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SH3_ZO | cd11859 | Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO ... |
502-563 | 5.11e-35 | ||||
Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO proteins are scaffolding proteins that associate with each other and with other proteins of the tight junction, zonula adherens, and gap junctions. They play roles in regulating cytoskeletal dynamics at these cell junctions. They are considered members of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. Vertebrates contain three ZO proteins (ZO-1, ZO-2, and ZO-3) with redundant and non-redundant roles. They contain three PDZ domains, followed by SH3 and GuK domains; in addition, ZO-1 and ZO-2 contains a proline-rich (PR) actin binding domain at the C-terminus while ZO-3 contains this PR domain between the second and third PDZ domains. The C-terminal regions of the three ZO proteins are unique. The SH3 domain of ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212793 Cd Length: 62 Bit Score: 128.18 E-value: 5.11e-35
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ZU5 | pfam00791 | ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function. |
1959-2046 | 1.56e-28 | ||||
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function. Pssm-ID: 425872 Cd Length: 96 Bit Score: 110.68 E-value: 1.56e-28
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ZU5 | smart00218 | Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function. |
1957-2046 | 1.20e-22 | ||||
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function. Pssm-ID: 128514 Cd Length: 104 Bit Score: 94.34 E-value: 1.20e-22
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PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
22-107 | 7.73e-21 | ||||
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: 88.39 E-value: 7.73e-21
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SH3_ZO-1 | cd12026 | Src homology 3 domain of the Tight junction protein, Zonula occludens protein 1; ZO-1 is a ... |
499-563 | 9.76e-21 | ||||
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 1; ZO-1 is a scaffolding protein that associates with other ZO proteins and other proteins of the tight junction, zonula adherens, and gap junctions. ZO proteins play roles in regulating cytoskeletal dynamics at these cell junctions. ZO-1 plays an essential role in embryonic development. It regulates the assembly and dynamics of the cortical cytoskeleton at cell-cell junctions. It is considered a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. The C-terminal region of ZO-1 is the largest of the three ZO proteins and contains an actin-binding region and domains of unknown function designated alpha and ZU5. The SH3 domain of ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212959 Cd Length: 65 Bit Score: 87.44 E-value: 9.76e-21
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PDZ | pfam00595 | PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins. |
23-107 | 3.12e-19 | ||||
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: 83.87 E-value: 3.12e-19
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SH3_ZO-2 | cd12027 | Src homology 3 domain of the Tight junction protein, Zonula occludens protein 2; ZO-2 is a ... |
498-563 | 8.68e-19 | ||||
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 2; ZO-2 is a scaffolding protein that associates with other ZO proteins and other proteins of the tight junction, zonula adherens, and gap junctions. ZO proteins play roles in regulating cytoskeletal dynamics at these cell junctions. ZO-2 plays an essential role in embryonic development. It is critical for the blood-testis barrier integrity and male fertility. It also regulates the expression of cyclin D1 and cell proliferation. It is considered a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. The C-terminal region of ZO-2 contains an actin-binding region and a domain of unknown function designated beta. The SH3 domain of the related protein ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212960 Cd Length: 63 Bit Score: 81.89 E-value: 8.68e-19
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PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
406-483 | 4.50e-18 | ||||
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: 80.69 E-value: 4.50e-18
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PDZ | smart00228 | Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ... |
405-486 | 7.46e-18 | ||||
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: 80.12 E-value: 7.46e-18
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SH3_ZO-3 | cd12028 | Src homology 3 domain of the Tight junction protein, Zonula occludens protein 3; ZO-3 is a ... |
499-563 | 8.67e-18 | ||||
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 3; ZO-3 is a scaffolding protein that associates with other ZO proteins and other proteins of the tight junction, zonula adherens, and gap junctions. ZO proteins play roles in regulating cytoskeletal dynamics at these cell junctions. ZO-3 is critical for epidermal barrier function. It regulates cyclin D1-dependent cell proliferation. It is considered a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. The C-terminal region of ZO-3 is the smallest of the three ZO proteins. The SH3 domain of the related protein ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212961 Cd Length: 65 Bit Score: 79.14 E-value: 8.67e-18
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PDZ | smart00228 | Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ... |
20-109 | 2.33e-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: 78.57 E-value: 2.33e-17
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PDZ | pfam00595 | PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins. |
409-483 | 2.45e-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: 70.00 E-value: 2.45e-14
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PDZ | cd00136 | PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ... |
415-468 | 2.03e-12 | ||||
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein. Pssm-ID: 238080 [Multi-domain] Cd Length: 70 Bit Score: 63.86 E-value: 2.03e-12
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PDZ_CTP_protease | cd00988 | PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ... |
415-471 | 5.37e-09 | ||||
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: 54.92 E-value: 5.37e-09
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SH3_2 | pfam07653 | Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ... |
502-564 | 5.40e-09 | ||||
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organisation. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel. Pssm-ID: 429575 [Multi-domain] Cd Length: 54 Bit Score: 53.75 E-value: 5.40e-09
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SH3_DLG5 | cd11860 | Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein ... |
514-564 | 1.31e-08 | ||||
Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein that is located at sites of cell-cell contact and is involved in the maintenance of cell shape and polarity. Mutations in the DLG5 gene are associated with Crohn's disease (CD) and inflammatory bowel disease (IBD). DLG5 is a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG5 contains 4 PDZ domains as well as an N-terminal domain of unknown function. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212794 Cd Length: 63 Bit Score: 53.11 E-value: 1.31e-08
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PDZ | cd00136 | PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ... |
33-107 | 1.41e-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: 53.08 E-value: 1.41e-08
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CtpA | COG0793 | C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ... |
415-471 | 1.69e-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: 55.80 E-value: 1.69e-07
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Guanylate_kin | pfam00625 | Guanylate kinase; |
678-777 | 1.85e-07 | ||||
Guanylate kinase; Pssm-ID: 395500 Cd Length: 182 Bit Score: 53.15 E-value: 1.85e-07
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PDZ_CTP_protease | cd00988 | PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ... |
56-111 | 2.57e-07 | ||||
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in posttranslational protein processing, maturation, and disassembly or degradation, in Bacteria, Archaea, and plant chloroplasts. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins. Pssm-ID: 238488 [Multi-domain] Cd Length: 85 Bit Score: 49.92 E-value: 2.57e-07
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PDZ_serine_protease | cd00987 | PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ... |
420-483 | 2.79e-07 | ||||
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: 49.95 E-value: 2.79e-07
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PDZ_6 | pfam17820 | PDZ domain; This entry represents the PDZ domain from a wide variety of proteins. |
56-108 | 2.56e-06 | ||||
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins. Pssm-ID: 436067 [Multi-domain] Cd Length: 54 Bit Score: 46.37 E-value: 2.56e-06
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PDZ_signaling | cd00992 | PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ... |
169-250 | 9.13e-06 | ||||
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: 45.64 E-value: 9.13e-06
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PDZ_6 | pfam17820 | PDZ domain; This entry represents the PDZ domain from a wide variety of proteins. |
430-472 | 1.86e-05 | ||||
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins. Pssm-ID: 436067 [Multi-domain] Cd Length: 54 Bit Score: 43.67 E-value: 1.86e-05
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PDZ_metalloprotease | cd00989 | PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ... |
415-456 | 2.46e-05 | ||||
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: 44.15 E-value: 2.46e-05
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DegQ | COG0265 | Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ... |
426-480 | 5.97e-05 | ||||
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 223343 [Multi-domain] Cd Length: 347 Bit Score: 47.58 E-value: 5.97e-05
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degP_htrA_DO | TIGR02037 | periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ... |
424-483 | 1.40e-04 | ||||
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: 46.45 E-value: 1.40e-04
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PDZ_serine_protease | cd00987 | PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ... |
56-108 | 1.85e-04 | ||||
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: 42.24 E-value: 1.85e-04
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PDZ_LON_protease | cd00986 | PDZ domain of ATP-dependent LON serine proteases. Most PDZ domains bind C-terminal ... |
54-108 | 3.21e-04 | ||||
PDZ domain of ATP-dependent LON serine proteases. Most PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this bacterial subfamily of protease-associated PDZ domains a C-terminal beta-strand is thought to form the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins. Pssm-ID: 238486 [Multi-domain] Cd Length: 79 Bit Score: 41.29 E-value: 3.21e-04
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PDZ_metalloprotease | cd00989 | PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ... |
56-108 | 4.30e-04 | ||||
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: 40.68 E-value: 4.30e-04
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CtpA | COG0793 | C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ... |
56-108 | 1.47e-03 | ||||
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: 43.09 E-value: 1.47e-03
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prc | TIGR00225 | C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different ... |
408-468 | 2.47e-03 | ||||
C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different species including processing of D1 protein of the photosystem II reaction center in higher plants and cleavage of a peptide of 11 residues from the precursor form of penicillin-binding protein in E.coli E.coli and H influenza have the most distal branch of the tree and their proteins have an N-terminal 200 amino acids that show no homology to other proteins in the database. [Protein fate, Degradation of proteins, peptides, and glycopeptides, Protein fate, Protein modification and repair] Pssm-ID: 272970 [Multi-domain] Cd Length: 334 Bit Score: 42.35 E-value: 2.47e-03
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degP_htrA_DO | TIGR02037 | periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ... |
428-460 | 2.76e-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: 42.59 E-value: 2.76e-03
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PDZ_2 | pfam13180 | PDZ domain; |
47-109 | 4.21e-03 | ||||
PDZ domain; Pssm-ID: 433015 [Multi-domain] Cd Length: 74 Bit Score: 37.64 E-value: 4.21e-03
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PDZ_2 | pfam13180 | PDZ domain; |
425-456 | 4.97e-03 | ||||
PDZ domain; Pssm-ID: 433015 [Multi-domain] Cd Length: 74 Bit Score: 37.64 E-value: 4.97e-03
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Blast search parameters | ||||
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