GTPase-activating protein BUD2 [Saccharomyces cerevisiae S288C]
Protein Classification
C2 and RasGAP_CLA2_BUD2 domain-containing protein( domain architecture ID 10033683)
C2 and RasGAP_CLA2_BUD2 domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| RasGAP_CLA2_BUD2 | cd05137 | Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ... |
460-819 | 3.52e-154 | ||||||
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein (GAP) for BUD1/RSR1 and is necessary for proper bud-site selection in yeast. BUD2 has sequence similarity to the catalytic domain of RasGAPs, and stimulates the hydrolysis of BUD1-GTP to BUD1-GDP. Elimination of Bud2p activity by mutation causes a random budding pattern with no growth defect. Overproduction of Bud2p also alters the budding pattern. : Pssm-ID: 213339 [Multi-domain] Cd Length: 356 Bit Score: 462.80 E-value: 3.52e-154
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| C2 | cd00030 | C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
337-444 | 1.01e-05 | ||||||
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. : Pssm-ID: 175973 [Multi-domain] Cd Length: 102 Bit Score: 45.52 E-value: 1.01e-05
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| Name | Accession | Description | Interval | E-value | ||||||
| RasGAP_CLA2_BUD2 | cd05137 | Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ... |
460-819 | 3.52e-154 | ||||||
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein (GAP) for BUD1/RSR1 and is necessary for proper bud-site selection in yeast. BUD2 has sequence similarity to the catalytic domain of RasGAPs, and stimulates the hydrolysis of BUD1-GTP to BUD1-GDP. Elimination of Bud2p activity by mutation causes a random budding pattern with no growth defect. Overproduction of Bud2p also alters the budding pattern. Pssm-ID: 213339 [Multi-domain] Cd Length: 356 Bit Score: 462.80 E-value: 3.52e-154
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| RasGAP | smart00323 | GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ... |
449-823 | 3.17e-100 | ||||||
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position. Improved domain limits from structure. Pssm-ID: 214617 Cd Length: 344 Bit Score: 320.41 E-value: 3.17e-100
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| RasGAP | pfam00616 | GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ... |
542-721 | 7.94e-50 | ||||||
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position. Pssm-ID: 459871 Cd Length: 207 Bit Score: 175.17 E-value: 7.94e-50
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| C2 | cd00030 | C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
337-444 | 1.01e-05 | ||||||
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Pssm-ID: 175973 [Multi-domain] Cd Length: 102 Bit Score: 45.52 E-value: 1.01e-05
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| C2 | smart00239 | Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
336-426 | 4.93e-05 | ||||||
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles. Pssm-ID: 214577 [Multi-domain] Cd Length: 101 Bit Score: 43.24 E-value: 4.93e-05
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| C2 | pfam00168 | C2 domain; |
369-442 | 6.84e-03 | ||||||
C2 domain; Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 37.30 E-value: 6.84e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| RasGAP_CLA2_BUD2 | cd05137 | Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ... |
460-819 | 3.52e-154 | ||||||
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein (GAP) for BUD1/RSR1 and is necessary for proper bud-site selection in yeast. BUD2 has sequence similarity to the catalytic domain of RasGAPs, and stimulates the hydrolysis of BUD1-GTP to BUD1-GDP. Elimination of Bud2p activity by mutation causes a random budding pattern with no growth defect. Overproduction of Bud2p also alters the budding pattern. Pssm-ID: 213339 [Multi-domain] Cd Length: 356 Bit Score: 462.80 E-value: 3.52e-154
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| RasGAP | smart00323 | GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ... |
449-823 | 3.17e-100 | ||||||
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position. Improved domain limits from structure. Pssm-ID: 214617 Cd Length: 344 Bit Score: 320.41 E-value: 3.17e-100
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| RasGAP | cd04519 | Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ... |
472-755 | 2.87e-53 | ||||||
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: 186.93 E-value: 2.87e-53
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| RasGAP | pfam00616 | GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ... |
542-721 | 7.94e-50 | ||||||
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position. Pssm-ID: 459871 Cd Length: 207 Bit Score: 175.17 E-value: 7.94e-50
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| RasGAP_DAB2IP | cd05136 | Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ... |
542-741 | 1.04e-35 | ||||||
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras GTPase-activating proteins includes DAB2IP, nGAP, and Syn GAP. Disabled 2 interactive protein, (DAB2IP; also known as ASK-interacting protein 1 (AIP1)), is a member of the GTPase-activating proteins, down-regulates Ras-mediated signal pathways, and mediates TNF-induced activation of ASK1-JNK signaling pathways. The mechanism by which TNF signaling is coupled to DAB2IP is not known. Pssm-ID: 213338 Cd Length: 324 Bit Score: 138.49 E-value: 1.04e-35
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| RasGAP_GAP1_like | cd05128 | Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ... |
516-753 | 2.78e-34 | ||||||
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras GTPase-activating proteins includes GAP1(m) (or RASA2), GAP1_IP4BP (or RASA3), Ca2+ -promoted Ras inactivator (CAPRI, or RASAL4), and Ras GTPase activating-like proteins (RASAL) or RASAL1. The members are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin homology domain that is associated with a Bruton's tyrosine kinase motif. While this domain structure is conserved, a small change in the function of each individual domain and the interaction between domains has a marked effect on the regulation of each protein. Pssm-ID: 213330 Cd Length: 269 Bit Score: 132.76 E-value: 2.78e-34
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| RasGAP_Neurofibromin_like | cd05392 | Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ... |
508-813 | 1.21e-28 | ||||||
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins include the Saccharomyces cerevisiae RasGAP proteins Ira1 and Ira2, the closest homolog of neurofibromin, which is responsible for the human autosomal dominant disease neurofibromatosis type I (NF1). The RasGAP Ira1/2 proteins are negative regulators of the Ras-cAMP signaling pathway and conserved from yeast to human. In yeast Ras proteins are activated by GEFs, and inhibited by two GAPs, Ira1 and Ira2. Ras proteins activate the cAMP/protein kinase A (PKA) pathway, which controls metabolism, stress resistance, growth, and meiosis. Recent studies showed that the kelch proteins Gpb1 and Gpb2 inhibit Ras activity via association with Ira1 and Ira2. Gpb1/2 bind to a conserved C-terminal domain of Ira1/2, and loss of Gpb1/2 results in a destabilization of Ira1 and Ira2, leading to elevated levels of Ras2-GTP and uninhibited cAMP-PKA signaling. Since the Gpb1/2 binding domain on Ira1/2 is conserved in the human neurofibromin protein, the studies suggest that an analogous signaling mechanism may contribute to the neoplastic development of NF1. Pssm-ID: 213341 Cd Length: 317 Bit Score: 117.77 E-value: 1.21e-28
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| RasGAP_p120GAP | cd05391 | Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ... |
468-753 | 1.01e-27 | ||||||
Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates hydrolysis of bound GTP to GDP. Once the Ras regulator p120GAP, a member of the GAP protein family, is recruited to the membrane, it is transiently immobilized to interact with Ras-GTP. The down-regulation of Ras by p120GAP is a critical step in the regulation of many cellular processes, which is disrupted in approximately 30% of human cancers. p120GAP contains SH2, SH3, PH, calcium- and lipid-binding domains, suggesting its involvement in a complex network of cellular interactions in vivo. Pssm-ID: 213340 Cd Length: 328 Bit Score: 115.28 E-value: 1.01e-27
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| RasGAP_RASA3 | cd05134 | Ras-GTPase Activating Domain of RASA3; RASA3 (or GAP1_IP4BP) is a member of the GAP1 family ... |
557-770 | 4.16e-22 | ||||||
Ras-GTPase Activating Domain of RASA3; RASA3 (or GAP1_IP4BP) is a member of the GAP1 family and has been shown to specifically bind 1,3,4,5-tetrakisphosphate (IP4). Thus, RASA3 may function as an IP4 receptor. The members of GAP1 family are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. Purified RASA3 stimulates GAP activity on Ras with about a five-fold lower potency than p120RasGAP, but shows no GAP-stimulating activity at all against Rac or Rab3A. Pssm-ID: 213336 Cd Length: 269 Bit Score: 97.40 E-value: 4.16e-22
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| RasGAP_RASAL | cd05135 | Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ... |
557-753 | 3.02e-21 | ||||||
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like protein (RASAL) or RASAL1 is a member of the GAP1 family, and a Ca2+ sensor responding in-phase to repetitive Ca2+ signals by associating with the plasma membrane and deactivating Ras. It contains a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. RASAL, like Ca2+ -promoted Ras inactivator (CAPRI, or RASAL4), is a cytosolic protein that undergoes a rapid translocation to the plasma membrane in response to receptor-mediated elevation in the concentration of intracellular free Ca2+, a translocation that activates its ability to function as a RasGAP. However, unlike RASAL4, RASAL undergoes an oscillatory translocation to the plasma membrane that occurs in synchrony with repetitive Ca2+ spikes. Pssm-ID: 213337 Cd Length: 287 Bit Score: 95.26 E-value: 3.02e-21
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| RasGAP_RASA2 | cd05394 | Ras-GTPase Activating Domain of RASA2; RASA2 (or GAP1(m)) is a member of the GAP1 family of ... |
542-730 | 7.24e-21 | ||||||
Ras-GTPase Activating Domain of RASA2; RASA2 (or GAP1(m)) is a member of the GAP1 family of Ras GTPase-activating proteins that includes GAP1_IP4BP (or RASA3), CAPRI, and RASAL. In vitro, RASA2 has been shown to bind inositol 1,3,4,5-tetrakisphosphate (IP4), the water soluble inositol head group of the lipid second messenger phosphatidylinositol 3,4,5-trisphosphate (PIP3). In vivo studies also demonstrated that RASA2 binds PIP3, and it is recruited to the plasma membrane following agonist stimulation of PI 3-kinase. Furthermore, the membrane translocation is a consequence of the ability of its pleckstrin homology (PH) domain to bind PIP3. Pssm-ID: 213342 Cd Length: 272 Bit Score: 93.80 E-value: 7.24e-21
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| RasGAP_GAPA | cd05132 | Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ... |
556-799 | 2.71e-16 | ||||||
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to bind to small GTPases, which are yet to be identified. IQGAP proteins are integral components of cytoskeletal regulation. Results from truncated GAPAs indicated that almost the entire region of GAPA homologous to IQGAP is required for cytokinesis in Dictyostelium. More members of the IQGAP family are emerging, and evidence suggests that there are both similarities and differences in their function. Pssm-ID: 213334 Cd Length: 352 Bit Score: 81.63 E-value: 2.71e-16
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| RasGAP_RASA4 | cd05395 | Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also ... |
557-753 | 4.69e-16 | ||||||
Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also known as Ca2+ -promoted Ras inactivator (CAPRI), is a member of the GAP1 family. Members of the GAP1 family are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. RASAL4, like RASAL, is a cytosolic protein that undergoes a rapid translocation to the plasma membrane in response to a receptor-mediated elevation in the concentration of intracellular free Ca2+ ([Ca2+]i). However, unlike RASAL, RASAL4 does not sense oscillations in [Ca2+]i. Pssm-ID: 213343 [Multi-domain] Cd Length: 287 Bit Score: 79.92 E-value: 4.69e-16
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| RasGAP_Neurofibromin | cd05130 | Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ... |
557-753 | 5.64e-15 | ||||||
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the neurofibromatosis type 1 gene (NF1) and shares a region of similarity with catalytic domain of the mammalian p120RasGAP protein and an extended similarity with the Saccharomyces cerevisiae RasGAP proteins Ira1 and Ira2. Neurofibromin has been shown to function as a GAP (GTPase-activating protein) which inhibits low molecular weight G proteins such as Ras by stimulating their intrinsic GTPase activity. NF1 is a common genetic disorder characterized by various symptoms ranging from predisposition for the development of tumors to learning disability or mental retardation. Loss of neurofibromin activity can be correlated to the increase in Ras-GTP concentration in neurofibromas of NF1 of patients, supporting the notion that unregulated Ras signaling may contribute to their development. Pssm-ID: 213332 [Multi-domain] Cd Length: 332 Bit Score: 77.36 E-value: 5.64e-15
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| RasGAP_IQGAP_like | cd05127 | Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ... |
561-755 | 1.52e-07 | ||||||
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family represents IQ motif containing GTPase activating protein (IQGAP) which associated with the Ras GTP-binding protein. A primary function of IQGAP proteins is to modulate cytoskeletal architecture. There are three known IQGAP family members: IQGAP1, IQGAP2 and IQGAP3. Human IQGAP1 and IQGAP2 share 62% identity. IQGAPs are multi-domain molecules having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP is an essential regulator of cytoskeletal function. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity, the protein actually lacks GAP activity. Both IQGAP1 and IQGAP2 specifically bind to Cdc42 and Rac1, but not to RhoA. Despite of their similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP3, only present in mammals, regulates the organization of the cytoskeleton under the regulation of Rac1 and Cdc42 in neuronal cells. The depletion of IQGAP3 is shown to impair neurite or axon outgrowth in neuronal cells with disorganized cytoskeleton. Pssm-ID: 213329 [Multi-domain] Cd Length: 331 Bit Score: 54.51 E-value: 1.52e-07
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| RasGAP_RAP6 | cd05129 | Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is ... |
581-742 | 2.44e-06 | ||||||
Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is an endosomal protein with a role in the regulation of receptor-mediated endocytosis. RAP6 contains a Vps9 domain, which is involved in the activation of Rab5, and a Ras GAP domain (RGD). Rab5 is a small GTPase required for the control of the endocytic route, and its activity is regulated by guanine nucleotide exchange factor, such as Rabex5, and GAPs, such as RN-tre. Human Rap6 protein is localized on the plasma membrane and on the endosome. RAP6 binds to Rab5 and Ras through the Vps9 and RGD domains, respectively. Pssm-ID: 213331 Cd Length: 365 Bit Score: 51.19 E-value: 2.44e-06
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| C2 | cd00030 | C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
337-444 | 1.01e-05 | ||||||
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Pssm-ID: 175973 [Multi-domain] Cd Length: 102 Bit Score: 45.52 E-value: 1.01e-05
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| C2 | smart00239 | Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
336-426 | 4.93e-05 | ||||||
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles. Pssm-ID: 214577 [Multi-domain] Cd Length: 101 Bit Score: 43.24 E-value: 4.93e-05
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| RasGAP_IQGAP2 | cd05131 | Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ... |
612-778 | 6.12e-05 | ||||||
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a member of the IQGAP family that contains a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeat, a single WW domain, four IQ motifs which mediate interactions with calmodulin, and a Ras-GTPase-activating protein (GAP)-related domain that binds Rho family GTPases. IQGAP2 and IQGAP3 play important roles in the regulation of the cytoskeleton for axon outgrowth in hippocampal neurons and are thought to stay in a common regulatory pathway. The results of RNA interference studies indicated that IQGAP3 partially compensates functions of IQGAP2, but has lesser ability than IQGAP2 to promote axon outgrowth in hippocampal neuron. Moreover, IQGAP2 is required for the cadherin-mediated cell-to-cell adhesion in Xenopus laevis embryos. Pssm-ID: 213333 [Multi-domain] Cd Length: 359 Bit Score: 46.53 E-value: 6.12e-05
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| C2A_RasA2_RasA3 | cd08401 | C2 domain first repeat present in RasA2 and RasA3; RasA2 and RasA3 are GAP1s (GTPase ... |
374-448 | 8.58e-04 | ||||||
C2 domain first repeat present in RasA2 and RasA3; RasA2 and RasA3 are GAP1s (GTPase activating protein 1s ), Ras-specific GAP members, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. RasA2 and RasA3 are both inositol 1,3,4,5-tetrakisphosphate-binding proteins and contain an N-terminal C2 domain, a Ras-GAP domain, a pleckstrin-homology (PH) domain which localizes it to the plasma membrane, and Bruton's Tyrosine Kinase (BTK) a zinc binding domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology. Pssm-ID: 176046 [Multi-domain] Cd Length: 121 Bit Score: 40.50 E-value: 8.58e-04
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| C2_SynGAP_like | cd04013 | C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ... |
326-463 | 4.31e-03 | ||||||
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and neurofibromin are all members of the Ras-specific GAP (GTPase-activating protein) family. SynGAP regulates the MAP kinase signaling pathway and is critical for cognition and synapse function. Mutations in this gene causes mental retardation in humans. SynGAP contains a PH-like domain, a C2 domain, and a Ras-GAP domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Pssm-ID: 175980 [Multi-domain] Cd Length: 146 Bit Score: 38.83 E-value: 4.31e-03
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| C2 | pfam00168 | C2 domain; |
369-442 | 6.84e-03 | ||||||
C2 domain; Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 37.30 E-value: 6.84e-03
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