Ras guanine nucleotide exchange factor (Ras-GEF) domain-containing protein activates Ras-like small GTPases by mediating the replacement of GDP with GTP
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
287-360
4.09e-06
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.
The actual alignment was detected with superfamily member cd06224:
Pssm-ID: 470601 Cd Length: 122 Bit Score: 46.25 E-value: 4.09e-06
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
430-680
2.13e-38
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: 142.39 E-value: 2.13e-38
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
287-360
4.09e-06
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: 46.25 E-value: 4.09e-06
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
283-360
4.98e-06
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this motif/domain N-terminal to the RasGef (Cdc25-like) domain.
Pssm-ID: 459873 Cd Length: 104 Bit Score: 45.76 E-value: 4.98e-06
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
283-373
1.19e-04
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: 42.32 E-value: 1.19e-04
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
430-680
2.13e-38
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: 142.39 E-value: 2.13e-38
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
287-360
4.09e-06
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: 46.25 E-value: 4.09e-06
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
283-360
4.98e-06
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this motif/domain N-terminal to the RasGef (Cdc25-like) domain.
Pssm-ID: 459873 Cd Length: 104 Bit Score: 45.76 E-value: 4.98e-06
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
283-373
1.19e-04
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: 42.32 E-value: 1.19e-04
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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