Plexin cytoplasmic RasGAP domain; This family features the C-terminal regions of various ...
1567-2102
0e+00
Plexin cytoplasmic RasGAP domain; This family features the C-terminal regions of various plexins. Plexins are receptors for semaphorins, and plexin signalling is important in path finding and patterning of both neurons and developing blood vessels. The cytoplasmic region, which has been called a SEX domain in some members of this family, is involved in downstream signalling pathways, by interaction with proteins such as Rac1, RhoD, Rnd1 and other plexins. This domain acts as a RasGAP domain.
:
Pssm-ID: 462434 [Multi-domain] Cd Length: 500 Bit Score: 877.68 E-value: 0e+00
The Sema domain, a protein interacting module, of Plexin B1; Plexin B1 serves as the ...
28-480
0e+00
The Sema domain, a protein interacting module, of Plexin B1; Plexin B1 serves as the Semaphorin 4D receptor and functions as a regulator of developing neurons and a tumor suppressor protein for melanoma. The Sema4D-plexin B signaling complex regulates dendritic and axonal complexity. The activation of Plexin B1 by Sema4D produces an acute collapse of axonal growth cones in hippocampal and retinal neurons over the early stages of neurite outgrowth and promotes branching and complexity. As a tumor suppressor, plexin B1 abrogates activation of the oncogenic receptor, c-Met, by its ligand, hepatocyte growth factor (HGF), in melanoma. Furthermore, plexin B1 suppresses integrin-dependent migration and activation of pp125FAK and inhibits Rho activity. Plexin B1 is highly expressed in endothelial cells and its activation by Sema4D elicits a potent proangiogenic response. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.
:
Pssm-ID: 200536 [Multi-domain] Cd Length: 461 Bit Score: 849.63 E-value: 0e+00
First repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are ...
1070-1161
3.68e-33
First repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.
:
Pssm-ID: 238585 Cd Length: 94 Bit Score: 123.96 E-value: 3.68e-33
Third repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are ...
1252-1381
5.40e-30
Third repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.
:
Pssm-ID: 238586 Cd Length: 99 Bit Score: 115.21 E-value: 5.40e-30
Second repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are ...
1162-1249
9.80e-26
Second repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.
:
Pssm-ID: 238584 Cd Length: 85 Bit Score: 102.69 E-value: 9.80e-26
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
481-533
9.89e-15
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).
:
Pssm-ID: 396154 [Multi-domain] Cd Length: 52 Bit Score: 70.04 E-value: 9.89e-15
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
1021-1061
3.06e-05
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).
:
Pssm-ID: 396154 [Multi-domain] Cd Length: 52 Bit Score: 43.47 E-value: 3.06e-05
Plexin cytoplasmic RasGAP domain; This family features the C-terminal regions of various ...
1567-2102
0e+00
Plexin cytoplasmic RasGAP domain; This family features the C-terminal regions of various plexins. Plexins are receptors for semaphorins, and plexin signalling is important in path finding and patterning of both neurons and developing blood vessels. The cytoplasmic region, which has been called a SEX domain in some members of this family, is involved in downstream signalling pathways, by interaction with proteins such as Rac1, RhoD, Rnd1 and other plexins. This domain acts as a RasGAP domain.
Pssm-ID: 462434 [Multi-domain] Cd Length: 500 Bit Score: 877.68 E-value: 0e+00
The Sema domain, a protein interacting module, of Plexin B1; Plexin B1 serves as the ...
28-480
0e+00
The Sema domain, a protein interacting module, of Plexin B1; Plexin B1 serves as the Semaphorin 4D receptor and functions as a regulator of developing neurons and a tumor suppressor protein for melanoma. The Sema4D-plexin B signaling complex regulates dendritic and axonal complexity. The activation of Plexin B1 by Sema4D produces an acute collapse of axonal growth cones in hippocampal and retinal neurons over the early stages of neurite outgrowth and promotes branching and complexity. As a tumor suppressor, plexin B1 abrogates activation of the oncogenic receptor, c-Met, by its ligand, hepatocyte growth factor (HGF), in melanoma. Furthermore, plexin B1 suppresses integrin-dependent migration and activation of pp125FAK and inhibits Rho activity. Plexin B1 is highly expressed in endothelial cells and its activation by Sema4D elicits a potent proangiogenic response. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.
Pssm-ID: 200536 [Multi-domain] Cd Length: 461 Bit Score: 849.63 E-value: 0e+00
Ras-GTPase Activating Domain of plexin-B1; Plexins form a conserved family of transmembrane ...
1567-2139
0e+00
Ras-GTPase Activating Domain of plexin-B1; Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestors of semaphorins. Plexins are divided into four types (A-D) according to sequence similarity. Plexin-B1 serves as the Semaphorin 4D receptor and functions as a regulator of developing neurons and a tumor suppressor protein for melanoma. The Sema4D and plexin-B1 signaling complex regulates dendritic and axonal complexity. The activation of Plexin-B1 by Sema4D produces an acute collapse of axonal growth cones in hippocampal and retinal neurons over the early stages of neurite outgrowth and promotes branching and complexity. As a tumor suppressor, plexin-B1 abrogates activation of the oncogenic receptor, c-Met, by its ligand, hepatocyte growth factor (HGF), in melanoma. Furthermore, plexin-B1 suppresses integrin-dependent migration and activation of pp125FAK and inhibits Rho activity. Plexin-B1 is highly expressed in endothelial cells and its activation by Sema4D elicits a potent proangiogenic response. Plexins contain a C-terminal RasGAP domain, which functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Plexins display GAP activity towards the Ras homolog Rap. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a large number of of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator.
Pssm-ID: 213353 [Multi-domain] Cd Length: 394 Bit Score: 786.92 E-value: 0e+00
First repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are ...
1070-1161
3.68e-33
First repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.
Pssm-ID: 238585 Cd Length: 94 Bit Score: 123.96 E-value: 3.68e-33
Third repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are ...
1252-1381
5.40e-30
Third repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.
Pssm-ID: 238586 Cd Length: 99 Bit Score: 115.21 E-value: 5.40e-30
Second repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are ...
1162-1249
9.80e-26
Second repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.
Pssm-ID: 238584 Cd Length: 85 Bit Score: 102.69 E-value: 9.80e-26
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
276-460
1.13e-17
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and transmembrane proteins, some of which function as repellent signals during axon guidance. Sema domains also occur in the hepatocyte growth factor receptor and Swiss:P51805
Pssm-ID: 460197 [Multi-domain] Cd Length: 180 Bit Score: 82.70 E-value: 1.13e-17
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
481-533
9.89e-15
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).
Pssm-ID: 396154 [Multi-domain] Cd Length: 52 Bit Score: 70.04 E-value: 9.89e-15
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
1070-1133
2.82e-10
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members.
Pssm-ID: 460355 [Multi-domain] Cd Length: 84 Bit Score: 58.61 E-value: 2.82e-10
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
1162-1248
3.41e-09
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members.
Pssm-ID: 460355 [Multi-domain] Cd Length: 84 Bit Score: 55.53 E-value: 3.41e-09
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
1021-1061
3.06e-05
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).
Pssm-ID: 396154 [Multi-domain] Cd Length: 52 Bit Score: 43.47 E-value: 3.06e-05
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
668-888
3.09e-05
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 49.38 E-value: 3.09e-05
N-terminal domain of Kruppel-like factor 17; Kruppel-like factor 17 (KLF17), or Krueppel-like ...
694-821
1.12e-03
N-terminal domain of Kruppel-like factor 17; Kruppel-like factor 17 (KLF17), or Krueppel-like factor 17, is a protein that, in humans, is encoded by the KLF17 gene and acts as a tumor suppressor. It negatively regulates epithelial-mesenchymal transition and metastasis in breast cancer. KLF17 is thought to be the human ortholog of the mouse gene, zinc finger protein 393 (Zfp393), although it has diverged significantly. KLF17 can regulate gene transcription from CACCC-box elements. It belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF17.
Pssm-ID: 410567 Cd Length: 286 Bit Score: 43.14 E-value: 1.12e-03
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
641-666
3.87e-03
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).
Pssm-ID: 396154 [Multi-domain] Cd Length: 52 Bit Score: 37.30 E-value: 3.87e-03
Plexin cytoplasmic RasGAP domain; This family features the C-terminal regions of various ...
1567-2102
0e+00
Plexin cytoplasmic RasGAP domain; This family features the C-terminal regions of various plexins. Plexins are receptors for semaphorins, and plexin signalling is important in path finding and patterning of both neurons and developing blood vessels. The cytoplasmic region, which has been called a SEX domain in some members of this family, is involved in downstream signalling pathways, by interaction with proteins such as Rac1, RhoD, Rnd1 and other plexins. This domain acts as a RasGAP domain.
Pssm-ID: 462434 [Multi-domain] Cd Length: 500 Bit Score: 877.68 E-value: 0e+00
The Sema domain, a protein interacting module, of Plexin B1; Plexin B1 serves as the ...
28-480
0e+00
The Sema domain, a protein interacting module, of Plexin B1; Plexin B1 serves as the Semaphorin 4D receptor and functions as a regulator of developing neurons and a tumor suppressor protein for melanoma. The Sema4D-plexin B signaling complex regulates dendritic and axonal complexity. The activation of Plexin B1 by Sema4D produces an acute collapse of axonal growth cones in hippocampal and retinal neurons over the early stages of neurite outgrowth and promotes branching and complexity. As a tumor suppressor, plexin B1 abrogates activation of the oncogenic receptor, c-Met, by its ligand, hepatocyte growth factor (HGF), in melanoma. Furthermore, plexin B1 suppresses integrin-dependent migration and activation of pp125FAK and inhibits Rho activity. Plexin B1 is highly expressed in endothelial cells and its activation by Sema4D elicits a potent proangiogenic response. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.
Pssm-ID: 200536 [Multi-domain] Cd Length: 461 Bit Score: 849.63 E-value: 0e+00
Ras-GTPase Activating Domain of plexin-B1; Plexins form a conserved family of transmembrane ...
1567-2139
0e+00
Ras-GTPase Activating Domain of plexin-B1; Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestors of semaphorins. Plexins are divided into four types (A-D) according to sequence similarity. Plexin-B1 serves as the Semaphorin 4D receptor and functions as a regulator of developing neurons and a tumor suppressor protein for melanoma. The Sema4D and plexin-B1 signaling complex regulates dendritic and axonal complexity. The activation of Plexin-B1 by Sema4D produces an acute collapse of axonal growth cones in hippocampal and retinal neurons over the early stages of neurite outgrowth and promotes branching and complexity. As a tumor suppressor, plexin-B1 abrogates activation of the oncogenic receptor, c-Met, by its ligand, hepatocyte growth factor (HGF), in melanoma. Furthermore, plexin-B1 suppresses integrin-dependent migration and activation of pp125FAK and inhibits Rho activity. Plexin-B1 is highly expressed in endothelial cells and its activation by Sema4D elicits a potent proangiogenic response. Plexins contain a C-terminal RasGAP domain, which functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Plexins display GAP activity towards the Ras homolog Rap. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a large number of of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator.
Pssm-ID: 213353 [Multi-domain] Cd Length: 394 Bit Score: 786.92 E-value: 0e+00
Ras-GTPase Activating Domain of type B plexins; Plexins form a conserved family of ...
1567-2135
0e+00
Ras-GTPase Activating Domain of type B plexins; Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestors of semaphorins. Plexins are divided into four types (A-D) according to sequence similarity.There are three members of the Plexin-B subfamily, namely B1, B2 and B3. Plexins-B1, B2 and B3 are receptors for Sema4D, Sema4C and Sema4G, and Sema5A, respectively. The activation of plexin-B1 by Sema4D produces an acute collapse of axonal growth cones in hippocampal and retinal neurons over the early stages of neurite outgrowth and promotes branching and complexity. By signaling the effect of Sema4C and Sema4G, the plexin-B2 receptor is critically involved in neural tube closure and cerebellar granule cell development. Plexin-B3, the receptor of Sema5A, is a highly potent stimulator of neurite outgrowth of primary murine cerebellar neurons. Plexin-B3 has been linked to verbal performance and white matter volume in human brain. Small GTPases play important roles in plexin-B signaling. Plexin-B1 activates Rho through Rho-specific guanine nucleotide exchange factors, leading to neurite retraction. Plexin-B1 possesses an intrinsic GTPase-activating protein activity for R-Ras and induces growth cone collapse through R-Ras inactivation. Plexins contain a C-terminal RasGAP domain, which functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Plexins display GAP activity towards the Ras homolog Rap. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a large number of of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator.
Pssm-ID: 213347 [Multi-domain] Cd Length: 391 Bit Score: 754.46 E-value: 0e+00
The Sema domain, a protein interacting module, of Plexin B; Plexins, which contain semaphorin ...
34-480
0e+00
The Sema domain, a protein interacting module, of Plexin B; Plexins, which contain semaphorin domains, function as receptors of semaphorins and may be the ancestors of semaphorins. There are three members of the Plexin B subfamily, namely B1, B2 and B3. Plexins B1, B2 and B3 are receptors for Sema4D, Sema4C and Sema4G, and Sema5A, respectively. The activation of plexin B1 by Sema4D produces an acute collapse of axonal growth cones in hippocampal and retinal neurons over the early stages of neurite outgrowth and promotes branching and complexity. By signaling the effect of Sema4C and Sema4G, the plexin B2 receptor is critically involved in neural tube closure and cerebellar granule cell development. Plexin B3, the receptor of Sema5A, is a highly potent stimulator of neurite outgrowth of primary murine cerebellar neurons. Plexin B3 has been linked to verbal performance and white matter volume in human brain. Small GTPases play important roles in plexin B signaling. Plexin B1 activates Rho through Rho-specific guanine nucleotide exchange factors, leading to neurite retraction. Plexin B1 possesses an intrinsic GTPase-activating protein activity for R-Ras and induces growth cone collapse through R-Ras inactivation. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.
Pssm-ID: 200506 [Multi-domain] Cd Length: 440 Bit Score: 746.76 E-value: 0e+00
Ras-GTPase Activating Domain of plexin-B3; Plexins form a conserved family of transmembrane ...
1567-2139
0e+00
Ras-GTPase Activating Domain of plexin-B3; Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestors of semaphorins. Plexins are divided into four types (A-D) according to sequence similarity. Plexin-B3 is the receptor of semaphorin 5A. It is a highly potent stimulator of neurite outgrowth of primary murine cerebellar neurons. Plexin-B3 has been linked to verbal performance and white matter volume in human brain. Furthermore, Sema5A and plexin-B3 have been implicated in the progression of various types of cancer. They play an important role in the invasion and metastasis of gastric carcinoma. The protein and mRNA expression of Sema5A and its receptor plexin-B3 increased gradually in non-neoplastic mucosa, primary gastric carcinoma, and lymph node metastasis, and their expression is correlated. The stimulation of plexin-B3 by Sema5A binding in human glioma cells results in the inhibition of cell migration and invasion. Plexins contain a C-terminal RasGAP domain, which functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Plexins display GAP activity towards the Ras homolog Rap. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a large number of of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator.
Pssm-ID: 213351 [Multi-domain] Cd Length: 397 Bit Score: 684.65 E-value: 0e+00
Ras-GTPase Activating Domain of plexins; Plexins form a conserved family of transmembrane ...
1567-2131
0e+00
Ras-GTPase Activating Domain of plexins; Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestors of semaphorins. Ligand binding activates signal transduction pathways controlling axon guidance in the nervous system and other developmental processes, including cell migration and morphogenesis, immune function, and tumor progression. Plexins are divided into four types (A-D) according to sequence similarity. In vertebrates, type A Plexins serve as the co-receptors for neuropilins to mediate the signaling of class 3 semaphorins except Sema3E, which signals through Plexin D1. Plexins serve as direct receptors for several other members of the semaphorin family: class 6 semaphorins signal through type A plexins and class 4 semaphorins through type B. Plexin C1 serves as the receptor of Sema7A and plays regulation roles in both immune and nervous systems. Plexins contain a C-terminal RasGAP domain, which functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Plexins display GAP activity towards the Ras homolog Rap. Other proteins having a RasGAP domain include p120GAP, IQGAP, Rab5-activating protein 6, and Neurofibromin. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a large number of of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator.
Pssm-ID: 213344 [Multi-domain] Cd Length: 382 Bit Score: 578.02 E-value: 0e+00
Ras-GTPase Activating Domain of plexin-B2; Plexins form a conserved family of transmembrane ...
1567-2139
0e+00
Ras-GTPase Activating Domain of plexin-B2; Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestors of semaphorins. Plexins are divided into four types (A-D) according to sequence similarity. Plexin-B2 serves as the receptor of Sema4C and Sema4G. By signaling the effect of Sema4C and Sema4G, the plexin-B2 receptor is critically involved in neural tube closure and cerebellar granule cell development. Mice lacking Plexin-B2 demonstrated defects in closure of the neural tube and disorganization of the embryonic brain. In developing kidney, Sema4C and Plexin-B2 signaling modulates ureteric branching. Plexin-B2 is expressed both in the pretubular aggregates and the ureteric epithelium in the developing kidney. Deletion of Plexin-B2 results in renal hypoplasia and occasional double ureters. Plexins contain a C-terminal RasGAP domain, which functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Plexins display GAP activity towards the Ras homolog Rap. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a large number of of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator.
Pssm-ID: 213352 [Multi-domain] Cd Length: 400 Bit Score: 558.47 E-value: 0e+00
The Sema domain, a protein interacting module, of Plexin B3; Plexin B3 is the receptor of ...
28-480
3.08e-169
The Sema domain, a protein interacting module, of Plexin B3; Plexin B3 is the receptor of semaphorin 5A. It is a highly potent stimulator of neurite outgrowth of primary murine cerebellar neurons. Plexin B3 has been linked to verbal performance and white matter volume in human brain. Furthermore, Sema5A and plexin B3 have been implicated in the progression of various types of cancer. They play an important role in the invasion and metastasis of gastric carcinoma. The stimulation of plexin B3 by Sema5A binding in human glioma cells results in the inhibition of cell migration and invasion. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.
Pssm-ID: 200538 [Multi-domain] Cd Length: 434 Bit Score: 525.14 E-value: 3.08e-169
Ras-GTPase Activating Domain of type A plexins; Plexins form a conserved family of ...
1567-2129
2.37e-159
Ras-GTPase Activating Domain of type A plexins; Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestors of semaphorins. They are divided into four types (A-D) according to sequence similarity. In vertebrates, there are four type A plexins (A1-A4) that serve as the co-receptors for neuropilins to mediate the signaling of class 3 semaphorins except Sema3E, which signals through Plexin-D1. Plexins serve as direct receptors for several other members of the semaphorin family: class 1 and class 6 semaphorins signal through type A plexins, which mediate diverse biological functions including axon guidance, cardiovascular development, and immune function. Guanylyl cyclase Gyc76C and Off-track kinase (OTK), a putative receptor tyrosine kinase, modulate Sema1a and Plexin-A mediated axon repulsion. In their complex with Sema6s, type A plexins serve as signal-transducing subunits. An increasing number of molecules that interact with the intracellular region of Plexin-A have been identified; among them are IgCAMs (in axon guidance events) and Trem2-DAP12 (in immune responses). Plexins contain a C-terminal RasGAP domain, which functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Plexins display GAP activity towards the Ras homolog Rap. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a large number of of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator.
Pssm-ID: 213350 [Multi-domain] Cd Length: 385 Bit Score: 495.79 E-value: 2.37e-159
Ras-GTPase Activating Domain of plexin-D1; Plexins form a conserved family of transmembrane ...
1567-2137
8.60e-143
Ras-GTPase Activating Domain of plexin-D1; Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestors of semaphorins. Plexins are divided into four types (A-D) according to sequence similarity. Plexin-D1 has been identified as the receptor of Sema3E. It binds to Sema3E directly with high affinity. Sema3E is implicated in axonal path finding and inhibition of developmental and postischemic angiogenesis. Plexin-D1 is broadly expressed on tumor vessels and tumor cells in a number of different types of human tumors. The Plexin-D1 and Sema3E interaction inhibits tumor growth but promotes invasiveness and metastasis. Plexins contain a C-terminal RasGAP domain, which functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Plexins display GAP activity towards the Ras homolog Rap. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a large number of of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator.
Pssm-ID: 213348 [Multi-domain] Cd Length: 419 Bit Score: 450.98 E-value: 8.60e-143
The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine ...
34-480
4.35e-122
The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine kinases; Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestor of semaphorins. Ligand binding activates signal transduction pathways controlling axon guidance in the nervous system and other developmental processes including cell migration and morphogenesis, immune function, and tumor progression. Plexins are divided into four types (A-D) according to sequence similarity. In vertebrates, type A Plexins serve as the co-receptors for neuropilins to mediate the signalling of class 3 semaphorins except Sema3E, which signals through Plexin D1. Plexins serve as direct receptors for several other members of the semaphorin family: class 6 semaphorins signal through type A plexins and class 4 semaphorins through type B. Plexin C1 serves as the receptor of Sema7A and plays regulation roles in both immune and nervous systems. This family also includes the Met and RON receptor tyrosine kinases. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.
Pssm-ID: 200497 [Multi-domain] Cd Length: 401 Bit Score: 391.69 E-value: 4.35e-122
Ras-GTPase Activating Domain of plexin-C1; Plexins form a conserved family of transmembrane ...
1568-2136
3.97e-116
Ras-GTPase Activating Domain of plexin-C1; Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestors of semaphorins. Plexins are divided into four types (A-D) according to sequence similarity. Plexin-C1 has been identified as the receptor of semaphorin 7A, which plays regulatory roles in both the immune and nervous systems. Unlike other semaphorins which act as repulsive guidance cues, Sema7A enhances central and peripheral axon growth and is required for proper axon tract formation during embryonic development. Plexin-C1 is a potential tumor suppressor for melanoma progression. The expression of Plexin-C1 is diminished or absent in human melanoma cell lines. Cofilin, an actin-binding protein involved in cell migration, is a downstream target of Sema7A and Plexin-C1 signaling. Melanoma invasion and metastasis may be promoted through the loss of Plexin-C1 inhibitory signaling on cofilin activation. Plexins contain a C-terminal RasGAP domain, which functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Plexins display GAP activity towards the Ras homolog Rap. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a large number of of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator.
Pssm-ID: 213349 [Multi-domain] Cd Length: 393 Bit Score: 374.20 E-value: 3.97e-116
The Sema domain, a protein interacting module, of Plexin B2; Plexin B2 serves as the receptor ...
33-479
7.58e-106
The Sema domain, a protein interacting module, of Plexin B2; Plexin B2 serves as the receptor of Sema4C and Sema4G. By signaling the effect of Sema4C and Sema4G, the plexin B2 receptor plays important roles in neural tube closure and cerebellar granule cell development. Mice lacking Plexin B2 demonstrated defects in closure of the neural tube and disorganization of the embryonic brain. In developing kidney, Sema4C-Plexin B2 signaling modulates ureteric branching. Plexin B2 is expressed both in the pretubular aggregates and the ureteric epithelium in the developing kidney. Deletion of Plexin B2 results in renal hypoplasia and occasional double ureters. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.
Pssm-ID: 200537 [Multi-domain] Cd Length: 449 Bit Score: 347.15 E-value: 7.58e-106
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
35-520
2.03e-64
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor for class 6 semaphorins. Interactions between Plexin A2, A4 and semaphorins 6A and 6B control the lamina-restricted projection of hippocampal mossy fibers. Sema6B also repels the growth of mossy fibers in a Plexin A4 dependent manner. Plexin A2 does not suppress Sema6B function. In addition, studies have shown that Plexin A2 may be related to anxiety and other psychiatric disorders. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.
Pssm-ID: 200533 [Multi-domain] Cd Length: 515 Bit Score: 229.43 E-value: 2.03e-64
The Sema domain, a protein interacting module, of Plexin A; Plexins serve as receptors of ...
25-479
9.52e-54
The Sema domain, a protein interacting module, of Plexin A; Plexins serve as receptors of semaphorins and may be the ancestor of semaphorins. Members of the Plexin A subfamily are receptors for Sema1s, Sema3s, and Sema6s, and they mediate diverse biological functions including axon guidance, cardiovascular development, and immune function. Guanylyl cyclase Gyc76C and Off-track kinase (OTK), a putative receptor tyrosine kinase, modulate Sema1a-Plexin A mediated axon repulsion. Sema3s do not interact directly with plexin A receptors, but instead bind Neuropilin-1 or Neuropilin-2 toactivate neuropilin-plexin A holoreceptor complexes. In contrast to Sema3s, Sema6s do not require neuropilins for plexin A binding. In the complex, plexin As serve as signal-transducing subunits. An increasing number of molecules that interact with the intracellular region of Plexin A have been identified; among them are IgCAMs (in axon guidance events) and Trem2-DAP12 (in immune responses). The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.
Pssm-ID: 200505 [Multi-domain] Cd Length: 470 Bit Score: 196.58 E-value: 9.52e-54
The Sema domain, a protein interacting module, of Plexin A1; Plexin A1 is found in both the ...
22-479
6.30e-50
The Sema domain, a protein interacting module, of Plexin A1; Plexin A1 is found in both the nervous and immune systems. Its external Sema domain is also shared by semaphorin proteins. In the nervous system, Plexin A1 mediates Sema3A axon guidance function by interacting with the Sema3A coreceptor neuropilin, resulting in actin depolarization and cell repulsion. In the immune system, Plexin A1 mediates Sema6D signaling by binding to the Sema6D-Trem2-DAP12 complex on immune cells and osteoclasts to promote Rac activation and DAP12 phosphorylation. In gene profiling experiments, Plexin A1 was identified as a CIITA (class II transactivator) regulated gene in primary dendritic cells (DCs). The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.
Pssm-ID: 200532 [Multi-domain] Cd Length: 474 Bit Score: 185.56 E-value: 6.30e-50
The Sema domain, a protein interacting module, of Plexin A3; Plexin-A3 forms a receptor ...
24-479
3.21e-49
The Sema domain, a protein interacting module, of Plexin A3; Plexin-A3 forms a receptor complex with neuropilin-2 and transduces signals for class 3 semaphorins in the nervous system. Both plexins A3 and A4 are essential for normal sympathetic neuron development. They function cooperatively to regulate the migration of sympathetic neurons, and differentially to guide sympathetic axons. Both plexins A3 and A4 are not required for guiding neural crest precursors prior to reaching the sympathetic anlagen. Plexin A3 is a major driving force for intraspinal motor growth cone guidance. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.
Pssm-ID: 200534 [Multi-domain] Cd Length: 469 Bit Score: 183.21 E-value: 3.21e-49
The Sema domain, a protein interacting module, of Plexin A4; Plexin A4 forms a receptor ...
30-482
2.32e-45
The Sema domain, a protein interacting module, of Plexin A4; Plexin A4 forms a receptor complex with neuropilins (NRPs) and transduces signals for class 3 semaphorins in the nervous system. It regulates facial nerve development by functioning as a receptor for Sema3A/NRP1. Both plexins A3 and A4 are essential for normal sympathetic development. They function both cooperatively, to regulate the migration of sympathetic neurons, and differentially, to guide sympathetic axons. Plexin A4 is also expressed in lymphoid tissues and functions in the immune system. It negatively regulates T lymphocyte responses. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.
Pssm-ID: 200535 [Multi-domain] Cd Length: 473 Bit Score: 172.06 E-value: 2.32e-45
The Sema domain, a protein interacting module, of Plexin D1; Plexins are known as semaphorin ...
39-480
3.46e-44
The Sema domain, a protein interacting module, of Plexin D1; Plexins are known as semaphorin receptors and Plexin D1 has been identified as the receptor of Sema3E. It binds to Sema3E directly with high affinity. Sema3E is implicated in axonal path finding and inhibition of developmental and post-ischemic angiogenesis. Plexin D1 is broadly expressed on tumor vessels and tumor cells in a number of different types of human tumors. Plexin D1-Sema3E interaction inhibits tumor growth but promotes invasiveness and metastasis. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.
Pssm-ID: 200508 [Multi-domain] Cd Length: 483 Bit Score: 168.87 E-value: 3.46e-44
First repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are ...
1070-1161
3.68e-33
First repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.
Pssm-ID: 238585 Cd Length: 94 Bit Score: 123.96 E-value: 3.68e-33
Third repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are ...
1252-1381
5.40e-30
Third repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.
Pssm-ID: 238586 Cd Length: 99 Bit Score: 115.21 E-value: 5.40e-30
Second repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are ...
1162-1249
9.80e-26
Second repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.
Pssm-ID: 238584 Cd Length: 85 Bit Score: 102.69 E-value: 9.80e-26
The Sema domain, a protein interacting module, of MET and RON receptor tyrosine kinases; This ...
32-479
1.16e-23
The Sema domain, a protein interacting module, of MET and RON receptor tyrosine kinases; This family includes MET and RON receptor tyrosine kinases. MET is encoded by the c-met protooncogene. MET is the receptor for hepatocyte growth factor/scatter factor (HGF/SF). HGF/SF and MET regulates multiple cellular events and are essential for the development of several tissues and organs, including the placenta, liver, and several groups of skeletal muscles. RON receptor tyrosine kinase is a Macrophage-stimulating protein (MSP) receptor. Upon binding of MSP, RON is activated via autophosphorylation within its kinase catalytic domain, resulting in a variety of effects including proliferation, tubular morphogenesis, angiogenesis, cellular motility and invasiveness. By interacting with downstream signaling molecules, it regulates macrophage migration, phagocytosis, and nitric oxide production. MET and RON receptors have been implicated in cancer development and migration. They are composed of alpha-beta heterodimers. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a Sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic tyrosine kinase domain. The Sema domain is necessary for receptor dimerization and activation.
Pssm-ID: 200509 [Multi-domain] Cd Length: 467 Bit Score: 107.12 E-value: 1.16e-23
IPT domain of Plexins and Cell Surface Receptors (PCSR) and related proteins . This subgroup ...
1162-1249
1.31e-18
IPT domain of Plexins and Cell Surface Receptors (PCSR) and related proteins . This subgroup contains IPT domains of plexins, receptors, like the plasminogen-related growth factor receptors, the hepatocyte growth factor-scatter factors, and the macrophage-stimulating receptors and of fibrocystin. Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT_PCSR domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.
Pssm-ID: 238337 [Multi-domain] Cd Length: 90 Bit Score: 82.50 E-value: 1.31e-18
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
276-460
1.13e-17
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and transmembrane proteins, some of which function as repellent signals during axon guidance. Sema domains also occur in the hepatocyte growth factor receptor and Swiss:P51805
Pssm-ID: 460197 [Multi-domain] Cd Length: 180 Bit Score: 82.70 E-value: 1.13e-17
IPT domain of Plexins and Cell Surface Receptors (PCSR) and related proteins . This subgroup ...
1070-1161
1.91e-17
IPT domain of Plexins and Cell Surface Receptors (PCSR) and related proteins . This subgroup contains IPT domains of plexins, receptors, like the plasminogen-related growth factor receptors, the hepatocyte growth factor-scatter factors, and the macrophage-stimulating receptors and of fibrocystin. Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT_PCSR domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.
Pssm-ID: 238337 [Multi-domain] Cd Length: 90 Bit Score: 79.04 E-value: 1.91e-17
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
481-533
9.89e-15
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).
Pssm-ID: 396154 [Multi-domain] Cd Length: 52 Bit Score: 70.04 E-value: 9.89e-15
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
1162-1249
2.56e-14
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as Transcription factor ImmunoGlobin (TIG) domains. They are present in intracellular transcription factors, cell surface receptors (such as plexins and scatter factor receptors), as well as, cyclodextrin glycosyltransferase and similar enzymes. Although they are involved in DNA binding in transcription factors, their function in other proteins is unknown. In these transcription factors, IPTs form homo- or heterodimers with the exception of the nuclear factor of activated Tcells (NFAT) transcription factors which are mainly monomers.
Pssm-ID: 238050 [Multi-domain] Cd Length: 89 Bit Score: 70.18 E-value: 2.56e-14
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
1921-2063
1.09e-13
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Proteins having a RasGAP domain include p120GAP, IQGAP, Rab5-activating protein 6, and Neurofibromin, among others. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP exhibit no similarity at their amino acid sequence level. RasGTPases function as molecular switches in a large number of signaling pathways. They are in the on state when bound to GTP, and in the off state when bound to GDP. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator.
Pssm-ID: 213328 Cd Length: 256 Bit Score: 73.29 E-value: 1.09e-13
The Sema domain, a protein interacting module, of RON Receptor Tyrosine Kinase; RON receptor ...
32-479
9.87e-13
The Sema domain, a protein interacting module, of RON Receptor Tyrosine Kinase; RON receptor tyrosine kinase is a Macrophage-stimulating protein (MSP) receptor. Upon binding of MSP, RON is activated via autophosphorylation within its kinase catalytic domain, resulting in a wide range of effects, including proliferation, tubular morphogenesis, angiogenesis, cellular motility and invasiveness. By interacting with downstream signaling molecules, it regulates macrophage migration, phagocytosis, and nitric oxide production. RON has been implicated in cancers of the breast, colon, pancreas and ovaries because both splice variants and receptor overexpression have been identified in these tumors. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as ligand recognition and binding model. RON is composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a Sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic tyrosine kinase domain. The Sema domain of RON may be necessary for receptor dimerization and activation.
Pssm-ID: 200540 [Multi-domain] Cd Length: 493 Bit Score: 72.89 E-value: 9.87e-13
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
1070-1161
9.99e-13
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as Transcription factor ImmunoGlobin (TIG) domains. They are present in intracellular transcription factors, cell surface receptors (such as plexins and scatter factor receptors), as well as, cyclodextrin glycosyltransferase and similar enzymes. Although they are involved in DNA binding in transcription factors, their function in other proteins is unknown. In these transcription factors, IPTs form homo- or heterodimers with the exception of the nuclear factor of activated Tcells (NFAT) transcription factors which are mainly monomers.
Pssm-ID: 238050 [Multi-domain] Cd Length: 89 Bit Score: 65.56 E-value: 9.99e-13
The Sema domain, a protein interacting module, of MET (also called hepatocyte growth factor ...
45-338
2.39e-12
The Sema domain, a protein interacting module, of MET (also called hepatocyte growth factor receptor, HGFR); MET is encoded by the c-met protooncogene. MET is a receptor tyrosine kinase that binds its ligand, hepatocyte growth factor/scatter factor (HGF/SF). HGF/SF and MET are essential for the development of several tissues and organs, including the placenta, liver, and several groups of skeletal muscles. It also plays a major role in the abnormal migration of cancer cells as a result of overexpression or MET mutations. MET is composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a Sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic tyrosine kinase domain. The cytoplasmic C-terminal region acts as a docking site for multiple protein substrates, including Grb2, Gab1, STAT3, Shc, SHIP-1 and Src. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. The Sema domain of Met is necessary for receptor dimerization and activation.
Pssm-ID: 200539 [Multi-domain] Cd Length: 492 Bit Score: 71.82 E-value: 2.39e-12
IPT domain of Plexins and Cell Surface Receptors (PCSR) and related proteins . This subgroup ...
1252-1380
4.95e-11
IPT domain of Plexins and Cell Surface Receptors (PCSR) and related proteins . This subgroup contains IPT domains of plexins, receptors, like the plasminogen-related growth factor receptors, the hepatocyte growth factor-scatter factors, and the macrophage-stimulating receptors and of fibrocystin. Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT_PCSR domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.
Pssm-ID: 238337 [Multi-domain] Cd Length: 90 Bit Score: 60.93 E-value: 4.95e-11
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
1070-1133
2.82e-10
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members.
Pssm-ID: 460355 [Multi-domain] Cd Length: 84 Bit Score: 58.61 E-value: 2.82e-10
First repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are ...
1162-1232
5.14e-10
First repeat of the IPT domain of Plexins and Cell Surface Receptors (PCSR) . Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains.
Pssm-ID: 238585 Cd Length: 94 Bit Score: 58.10 E-value: 5.14e-10
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
1162-1248
3.41e-09
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members.
Pssm-ID: 460355 [Multi-domain] Cd Length: 84 Bit Score: 55.53 E-value: 3.41e-09
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
1252-1379
3.00e-08
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as Transcription factor ImmunoGlobin (TIG) domains. They are present in intracellular transcription factors, cell surface receptors (such as plexins and scatter factor receptors), as well as, cyclodextrin glycosyltransferase and similar enzymes. Although they are involved in DNA binding in transcription factors, their function in other proteins is unknown. In these transcription factors, IPTs form homo- or heterodimers with the exception of the nuclear factor of activated Tcells (NFAT) transcription factors which are mainly monomers.
Pssm-ID: 238050 [Multi-domain] Cd Length: 89 Bit Score: 52.85 E-value: 3.00e-08
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed ...
37-255
4.76e-06
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed in regions of the basal telencephalon in rat. Sema5B is an inhibitory cue for corticofugal axons and acts as a source of repulsion for the appropriate guidance of cortical axons away from structures such as the ventricular zone as they navigate toward and within subcortical regions. In addition to its role as a guidance cue, Sema5B regulates the development and maintenance of synapse size and number in hippocampal neurons. In addition, the sema domain of Sema5B can be cleaved of the whole protein and exerts its function in regulation of synapse morphology. Sema5B belongs to the class 5 semaphorin family of proteins, which are transmembrane glycoproteins characterized by unique thrombospondin specific repeats in the extracellular region of the protein. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.
Pssm-ID: 200525 [Multi-domain] Cd Length: 437 Bit Score: 51.52 E-value: 4.76e-06
The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins ...
32-255
2.23e-05
The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins are transmembrane glycoproteins characterized by unique thrombospondin specific repeats in the extracellular region of the protein. There are three subfamilies in class 5 semaphorins, namely 5A, 5B and 5C. Sema5A and Sema5B function as guidance cues for optic and corticofugal nerve development, respectively. Sema5A-induced cell migration requires Met signaling. Sema5C is an early development gene and may play a role in odor-guided behavior. Sema5A is also implicated in cancer. In a screening model for metastasis, the Drosophila Sema5A ortholog, Dsema-5C, has been found to be required in tumorigenicity and metastasis. Sema5A is highly expressed in human pancreatic cancer cells and is associated with tumor growth, invasion and metastasis. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.
Pssm-ID: 200502 [Multi-domain] Cd Length: 438 Bit Score: 49.47 E-value: 2.23e-05
The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 ...
217-480
2.84e-05
The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 semaphorins (Sema6s) are membrane associated semaphorins. There are 6 subfamilies named 6A to 6D. Sema6s bind to plexin As in a neuropilin independent fashion. Sema6-plexin A signaling plays important roles in lamina-specific axon projections. Interactions between plexin A2, plexin A4, and Sema6A control lamina-restricted projection of hippocampal mossy fibers. Interactions between Sema6C, Sema6D and plexin A1 shape the stereotypic trajectories of sensory axons in the spinal cord. In addition to axon targeting, Sema6D-plexin A1 interactions influence a wide range of other biological processes. During cardiac development, Sema6D attracts or repels endothelial cells in the cardiac tube depending on the expression patterns of specific coreceptors in addition to plexin A1. Furthermore, Sema6D binds a receptor complex comprising of plexin A1, Trem2 (triggering receptor expressed on myeloid cells 2), and DAP12 on dendritic cells and osteoclasts to mediate T-cell-DC interactions and to control bone development, respectively. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.
Pssm-ID: 200503 [Multi-domain] Cd Length: 465 Bit Score: 49.05 E-value: 2.84e-05
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
1021-1061
3.06e-05
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).
Pssm-ID: 396154 [Multi-domain] Cd Length: 52 Bit Score: 43.47 E-value: 3.06e-05
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
668-888
3.09e-05
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 49.38 E-value: 3.09e-05
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
661-882
1.01e-04
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 47.60 E-value: 1.01e-04
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
1619-1729
1.16e-04
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Proteins having a RasGAP domain include p120GAP, IQGAP, Rab5-activating protein 6, and Neurofibromin, among others. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP exhibit no similarity at their amino acid sequence level. RasGTPases function as molecular switches in a large number of signaling pathways. They are in the on state when bound to GTP, and in the off state when bound to GDP. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator.
Pssm-ID: 213328 Cd Length: 256 Bit Score: 45.95 E-value: 1.16e-04
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
666-838
3.93e-04
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 45.91 E-value: 3.93e-04
N-terminal domain of Kruppel-like factor 17; Kruppel-like factor 17 (KLF17), or Krueppel-like ...
694-821
1.12e-03
N-terminal domain of Kruppel-like factor 17; Kruppel-like factor 17 (KLF17), or Krueppel-like factor 17, is a protein that, in humans, is encoded by the KLF17 gene and acts as a tumor suppressor. It negatively regulates epithelial-mesenchymal transition and metastasis in breast cancer. KLF17 is thought to be the human ortholog of the mouse gene, zinc finger protein 393 (Zfp393), although it has diverged significantly. KLF17 can regulate gene transcription from CACCC-box elements. It belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF17.
Pssm-ID: 410567 Cd Length: 286 Bit Score: 43.14 E-value: 1.12e-03
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
689-826
3.54e-03
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins.
Pssm-ID: 409240 [Multi-domain] Cd Length: 163 Bit Score: 40.44 E-value: 3.54e-03
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
641-666
3.87e-03
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).
Pssm-ID: 396154 [Multi-domain] Cd Length: 52 Bit Score: 37.30 E-value: 3.87e-03
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
671-814
6.06e-03
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 41.68 E-value: 6.06e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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