RAS guanyl-releasing protein 2 isoform X4 [Mus musculus]
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
RasGEF | smart00147 | Guanine nucleotide exchange factor for Ras-like small GTPases; |
150-387 | 6.23e-86 | |||||
Guanine nucleotide exchange factor for Ras-like small GTPases; : Pssm-ID: 214539 Cd Length: 242 Bit Score: 264.11 E-value: 6.23e-86
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RasGEFN | smart00229 | Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ... |
7-121 | 4.71e-23 | |||||
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this domain N-terminal to the RasGef (Cdc25-like) domain. The recent crystal structureof Sos shows that this domain is alpha-helical and plays a "purely structural role" (Nature 394, 337-343). : Pssm-ID: 214571 Cd Length: 127 Bit Score: 94.32 E-value: 4.71e-23
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FRQ1 super family | cl34916 | Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
407-452 | 4.80e-05 | |||||
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; The actual alignment was detected with superfamily member COG5126: Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 43.24 E-value: 4.80e-05
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Name | Accession | Description | Interval | E-value | |||||
RasGEF | smart00147 | Guanine nucleotide exchange factor for Ras-like small GTPases; |
150-387 | 6.23e-86 | |||||
Guanine nucleotide exchange factor for Ras-like small GTPases; Pssm-ID: 214539 Cd Length: 242 Bit Score: 264.11 E-value: 6.23e-86
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RasGEF | cd00155 | Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ... |
150-383 | 5.31e-84 | |||||
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of the Ras superfamily function as molecular switches in fundamental events such as signal transduction, cytoskeleton dynamics and intracellular trafficking. Guanine-nucleotide-exchange factors (GEFs) positively regulate these GTP-binding proteins in response to a variety of signals. GEFs catalyze the dissociation of GDP from the inactive GTP-binding proteins. GTP can then bind and induce structural changes that allow interaction with effectors. Pssm-ID: 238087 [Multi-domain] Cd Length: 237 Bit Score: 259.11 E-value: 5.31e-84
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RasGEF | pfam00617 | RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases. |
157-335 | 2.06e-61 | |||||
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases. Pssm-ID: 459872 Cd Length: 179 Bit Score: 198.59 E-value: 2.06e-61
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RasGEFN | smart00229 | Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ... |
7-121 | 4.71e-23 | |||||
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this domain N-terminal to the RasGef (Cdc25-like) domain. The recent crystal structureof Sos shows that this domain is alpha-helical and plays a "purely structural role" (Nature 394, 337-343). Pssm-ID: 214571 Cd Length: 127 Bit Score: 94.32 E-value: 4.71e-23
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REM | cd06224 | Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ... |
12-123 | 2.01e-17 | |||||
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also called REM domain (Ras exchanger motif). This domain is common in nucleotide exchange factors for Ras-like small GTPases and is typically found immediately N-terminal to the RasGef (Cdc25-like) domain. REM contacts the GTPase and is assumed to participate in the catalytic activity of the exchange factor. Proteins with the REM domain include Sos1 and Sos2, which relay signals from tyrosine-kinase mediated signalling to Ras, RasGRP1-4, RasGRF1,2, CNrasGEF, and RAP-specific nucleotide exchange factors, to name a few. Pssm-ID: 100121 Cd Length: 122 Bit Score: 78.22 E-value: 2.01e-17
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FRQ1 | COG5126 | Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
407-452 | 4.80e-05 | |||||
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 43.24 E-value: 4.80e-05
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EF-hand_1 | pfam00036 | EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ... |
431-452 | 4.47e-04 | |||||
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes. Pssm-ID: 425435 [Multi-domain] Cd Length: 29 Bit Score: 37.38 E-value: 4.47e-04
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EFh | cd00051 | EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
430-454 | 9.22e-04 | |||||
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers. Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 37.53 E-value: 9.22e-04
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EFh | smart00054 | EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ... |
431-454 | 2.27e-03 | |||||
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions. Pssm-ID: 197492 [Multi-domain] Cd Length: 29 Bit Score: 35.43 E-value: 2.27e-03
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Name | Accession | Description | Interval | E-value | |||||
RasGEF | smart00147 | Guanine nucleotide exchange factor for Ras-like small GTPases; |
150-387 | 6.23e-86 | |||||
Guanine nucleotide exchange factor for Ras-like small GTPases; Pssm-ID: 214539 Cd Length: 242 Bit Score: 264.11 E-value: 6.23e-86
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RasGEF | cd00155 | Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ... |
150-383 | 5.31e-84 | |||||
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of the Ras superfamily function as molecular switches in fundamental events such as signal transduction, cytoskeleton dynamics and intracellular trafficking. Guanine-nucleotide-exchange factors (GEFs) positively regulate these GTP-binding proteins in response to a variety of signals. GEFs catalyze the dissociation of GDP from the inactive GTP-binding proteins. GTP can then bind and induce structural changes that allow interaction with effectors. Pssm-ID: 238087 [Multi-domain] Cd Length: 237 Bit Score: 259.11 E-value: 5.31e-84
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RasGEF | pfam00617 | RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases. |
157-335 | 2.06e-61 | |||||
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases. Pssm-ID: 459872 Cd Length: 179 Bit Score: 198.59 E-value: 2.06e-61
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RasGEFN | smart00229 | Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ... |
7-121 | 4.71e-23 | |||||
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this domain N-terminal to the RasGef (Cdc25-like) domain. The recent crystal structureof Sos shows that this domain is alpha-helical and plays a "purely structural role" (Nature 394, 337-343). Pssm-ID: 214571 Cd Length: 127 Bit Score: 94.32 E-value: 4.71e-23
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REM | cd06224 | Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ... |
12-123 | 2.01e-17 | |||||
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also called REM domain (Ras exchanger motif). This domain is common in nucleotide exchange factors for Ras-like small GTPases and is typically found immediately N-terminal to the RasGef (Cdc25-like) domain. REM contacts the GTPase and is assumed to participate in the catalytic activity of the exchange factor. Proteins with the REM domain include Sos1 and Sos2, which relay signals from tyrosine-kinase mediated signalling to Ras, RasGRP1-4, RasGRF1,2, CNrasGEF, and RAP-specific nucleotide exchange factors, to name a few. Pssm-ID: 100121 Cd Length: 122 Bit Score: 78.22 E-value: 2.01e-17
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FRQ1 | COG5126 | Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
407-452 | 4.80e-05 | |||||
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 43.24 E-value: 4.80e-05
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EF-hand_1 | pfam00036 | EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ... |
431-452 | 4.47e-04 | |||||
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes. Pssm-ID: 425435 [Multi-domain] Cd Length: 29 Bit Score: 37.38 E-value: 4.47e-04
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EF-hand_5 | pfam13202 | EF hand; |
431-452 | 5.09e-04 | |||||
EF hand; Pssm-ID: 433035 [Multi-domain] Cd Length: 25 Bit Score: 37.30 E-value: 5.09e-04
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EF-hand_7 | pfam13499 | EF-hand domain pair; |
428-454 | 6.77e-04 | |||||
EF-hand domain pair; Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 38.00 E-value: 6.77e-04
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EFh | cd00051 | EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
430-454 | 9.22e-04 | |||||
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers. Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 37.53 E-value: 9.22e-04
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FRQ1 | COG5126 | Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
424-477 | 2.03e-03 | |||||
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 38.62 E-value: 2.03e-03
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EFh | smart00054 | EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ... |
431-454 | 2.27e-03 | |||||
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions. Pssm-ID: 197492 [Multi-domain] Cd Length: 29 Bit Score: 35.43 E-value: 2.27e-03
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EFh | cd00051 | EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
428-452 | 2.30e-03 | |||||
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers. Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 36.37 E-value: 2.30e-03
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EFh_CREC_cab45 | cd16225 | EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ... |
401-451 | 3.38e-03 | |||||
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN. Pssm-ID: 320023 [Multi-domain] Cd Length: 278 Bit Score: 39.20 E-value: 3.38e-03
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EF-hand_6 | pfam13405 | EF-hand domain; |
431-454 | 4.25e-03 | |||||
EF-hand domain; Pssm-ID: 463869 [Multi-domain] Cd Length: 30 Bit Score: 34.84 E-value: 4.25e-03
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Blast search parameters | ||||
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