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Conserved domains on  [gi|253723094|pdb|1RLF|A]
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Chain A, RLF

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
RA_RGL2 cd17211
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 2 ...
 3-89 7.72e-51

Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 2 (RalGDS-like 2) and similar proteins; RalGDS-like 2 (RGL2), also termed RalGDS-like factor (RLF), or Ras-associated protein RAB2L, is a novel Ras and Rap 1A-associating protein that belongs to RalGDS family, whose members are involved in Ras and Ral signaling pathways as downstream effector proteins. RGL2 exhibits guanine nucleotide exchange activity towards the small GTPase Ral. Members in this family have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal Ras-associating (RA) domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. The RA domain of RGL2 is phosphorylated by protein kinase A and the phosphorylation affects the ability of RGL2 to bind both Ras and Rap1.


:

Pssm-ID: 340731  Cd Length: 86  Bit Score: 154.21  E-value: 7.72e-51
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLF_A       3 SDCRIIRVQMELGeDGSVYKSILVTSQDKAPSVISRVLKKNNRDSAVASEFELVQLLPGDRELTIPHSANVFYAMDGASH 82
Cdd:cd17211  1 SDCRIIRVRMELH-DGSVYKSILVTSQDKTPAVISRALEKHNQSSQAASPYELVQLLPEGKELTIPPTANVFYAMSSASL 79


               ....*..
1RLF_A      83 DFLLRQR 89
Cdd:cd17211 80 DFILRPR 86
 
Name Accession Description Interval E-value
RA_RGL2 cd17211
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 2 ...
 3-89 7.72e-51

Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 2 (RalGDS-like 2) and similar proteins; RalGDS-like 2 (RGL2), also termed RalGDS-like factor (RLF), or Ras-associated protein RAB2L, is a novel Ras and Rap 1A-associating protein that belongs to RalGDS family, whose members are involved in Ras and Ral signaling pathways as downstream effector proteins. RGL2 exhibits guanine nucleotide exchange activity towards the small GTPase Ral. Members in this family have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal Ras-associating (RA) domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. The RA domain of RGL2 is phosphorylated by protein kinase A and the phosphorylation affects the ability of RGL2 to bind both Ras and Rap1.


Pssm-ID: 340731  Cd Length: 86  Bit Score: 154.21  E-value: 7.72e-51
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLF_A       3 SDCRIIRVQMELGeDGSVYKSILVTSQDKAPSVISRVLKKNNRDSAVASEFELVQLLPGDRELTIPHSANVFYAMDGASH 82
Cdd:cd17211  1 SDCRIIRVRMELH-DGSVYKSILVTSQDKTPAVISRALEKHNQSSQAASPYELVQLLPEGKELTIPPTANVFYAMSSASL 79


               ....*..
1RLF_A      83 DFLLRQR 89
Cdd:cd17211 80 DFILRPR 86
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 4-90 1.12e-19

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 75.80  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLF_A          4 DCRIIRVQMELGEDGSvYKSILVTSQDKAPSVISRVLKKNNRDsAVASEFELVQLLPGDRELTIPHSANVFYAM-----D 78
Cdd:smart00314  1 DTFVLRVYVDDLPGGT-YKTLRVSSRTTARDVIQQLLEKFHLT-DDPEEYVLVEVLPDGKERVLPDDENPLQLQklwprR 78

                          90
                  ....*....|..
1RLF_A         79 GASHDFLLRQRR 90
Cdd:smart00314 79 GPNLRFVLRKRD 90
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 4-90 2.17e-15

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 64.66  E-value: 2.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLF_A         4 DCRIIRVQMELGEDGSVYKSILVTSQDKAPSVISRVLKKNNRDSAvASEFELV-QLLPGDRELTIPHSANVFYAM----- 77
Cdd:pfam00788  1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGLEDD-PRDYVLVeVLERGGGERRLPDDECPLQIQlqwpr 79

                         90
                 ....*....|...
1RLF_A        78 DGASHDFLLRQRR 90
Cdd:pfam00788 80 DASDSRFLLRKRD 92
 
Name Accession Description Interval E-value
RA_RGL2 cd17211
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 2 ...
 3-89 7.72e-51

Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 2 (RalGDS-like 2) and similar proteins; RalGDS-like 2 (RGL2), also termed RalGDS-like factor (RLF), or Ras-associated protein RAB2L, is a novel Ras and Rap 1A-associating protein that belongs to RalGDS family, whose members are involved in Ras and Ral signaling pathways as downstream effector proteins. RGL2 exhibits guanine nucleotide exchange activity towards the small GTPase Ral. Members in this family have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal Ras-associating (RA) domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. The RA domain of RGL2 is phosphorylated by protein kinase A and the phosphorylation affects the ability of RGL2 to bind both Ras and Rap1.


Pssm-ID: 340731  Cd Length: 86  Bit Score: 154.21  E-value: 7.72e-51
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLF_A       3 SDCRIIRVQMELGeDGSVYKSILVTSQDKAPSVISRVLKKNNRDSAVASEFELVQLLPGDRELTIPHSANVFYAMDGASH 82
Cdd:cd17211  1 SDCRIIRVRMELH-DGSVYKSILVTSQDKTPAVISRALEKHNQSSQAASPYELVQLLPEGKELTIPPTANVFYAMSSASL 79


               ....*..
1RLF_A      83 DFLLRQR 89
Cdd:cd17211 80 DFILRPR 86
RA_RalGDS_like cd00153
Ras-associating (RA) domain of RalGDS family; The RalGDS family RA domains can interact with ...
 4-89 3.05e-38

Ras-associating (RA) domain of RalGDS family; The RalGDS family RA domains can interact with activated Ras and may function as effectors for other Ras family. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes and is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. The RalGDS family includes RalGDS, RGL, RGL2/Rlf and RGL3. All family members have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal RA domain. The RA domain mediates the GTP-dependent interaction with Ras and Ras-related proteins.


Pssm-ID: 340449  Cd Length: 88  Bit Score: 122.68  E-value: 3.05e-38
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLF_A       4 DCRIIRVQMELG-EDGSVYKSILVTSQDKAPSVISRVLKKNNRDSAVASEFELVQLLPGDRELTIPHSANVFYAMDGAS- 81
Cdd:cd00153  1 DSRIIRVSLEDGsEDGNLYKSILLTNQDRTPSVIRRALEKHNLEDEDPDDFSLVQILPDDKELVIPDNANVFYAMNSSAn 80


               ....*...
1RLF_A      82 HDFLLRQR 89
Cdd:cd00153 81 LNFILRKK 88
RA_RGL3 cd17212
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 3 ...
 3-89 2.36e-33

Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 3 (RalGDS-like 3) and similar proteins; RalGDS-like 3 (RGL3), also termed Ras pathway modulator (RPM), interacts in a GTP- and effector loop-dependent manner with Rit and Ras. As a novel potential effector of both p21 Ras and M-Ras, RGL3 negatively regulates Elk-1-dependent gene induction downstream of p21 Ras or mitogen activated protein/extracellular signal regulated kinase Kinase 1 (MEKK1). It also functions as a potential binding partner for Rap-family small G-proteins and profilin II. RGL3 belongs to RalGDS family, whose members are involved in Ras and Ral signaling pathways as downstream effector proteins. Members in this family have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal Ras-associating (RA) domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier (Ubiquitination) in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair.


Pssm-ID: 340732  Cd Length: 87  Bit Score: 110.41  E-value: 2.36e-33
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLF_A       3 SDCRIIRVQMElGEDGSVYKSILVTSQDKAPSVISRVLKKNNRDSAVASEFELVQLLPGDRELTIPHSANVFYAMD-GAS 81
Cdd:cd17212  1 SEARVIRVSID-NDHGNLYRSILLTSQDKAPSVVQRALQKHNVPQPWARDYQLFQVLPGDRELLIPDNANVFYAMSpAAP 79


               ....*...
1RLF_A      82 HDFLLRQR 89
Cdd:cd17212 80 GDFMLRRK 87
RA_RalGDS cd17209
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator (RalGDS) ...
 4-89 7.24e-30

Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator (RalGDS) and similar proteins; RalGDS, also termed Ral guanine nucleotide exchange factor (RalGEF), is a guanine exchange factor (GEF) for the Ral family of small GTPases. It is the prototype of RalGDS family proteins that are involved in Ras and Ral signaling pathways as downstream effector proteins. RalGDS stimulates the dissociation of GDP from the Ras-related RalA and RalB GTPases which allows GTP binding and activation of the GTPases. It interacts and acts as an effector molecule for R-Ras, H-Ras, K-Ras, and Rap. Moreover, RalGDS functions as a novel interacting partner for Rab7-interacting lysosomal protein (RILP), a key regulator for late endosomal/lysosomal trafficking. RILP suppresses invasion of breast cancer cells by inhibiting the GEF activity for RalA of RalGDS. RalGDS also plays a vital role in the regulation of Ral-dependent Weibel-Palade bodies (WPB) exocytosis from endothelial cells. In addition, RalGDS couples growth factor signaling to Akt activation by promoting PDK1-induced Akt phosphorylation. Members in this family have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal Ras-associating (RA) domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair.


Pssm-ID: 340729  Cd Length: 86  Bit Score: 101.57  E-value: 7.24e-30
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLF_A       4 DCRIIRVQMELgEDGSVYKSILVTSQDKAPSVISRVLKKNNRDSAVASEFELVQLLPGDRELTIPHSANVFYAMDG-ASH 82
Cdd:cd17209  1 DCCIIRVSLDV-DNGNMYKSILVTSQDKTPVVIRKAMAKHNLDEEEPEDYELLQILSEDRELKIPDNANVFYAMNStANY 79


               ....*..
1RLF_A      83 DFLLRQR 89
Cdd:cd17209 80 DFVLKKR 86
RA_RGL cd17210
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 1 ...
 4-89 2.20e-29

Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 1 (RalGDS-like 1) and similar proteins; RalGDS-like 1 (RGL) is a Ral-specific guanine nucleotide exchange factor that belongs to RalGDS family, whose members are involved in Ras and Ral signaling pathways as downstream effector proteins. RGL has been identified as a possible effector protein of Ras. It also regulates c-fos promoter and the GDP/GTP exchange of Ral. Members in this family have similar structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal Ras-associating (RA) domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair.


Pssm-ID: 340730  Cd Length: 87  Bit Score: 100.06  E-value: 2.20e-29
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLF_A       4 DCRIIRVQMELGeDGSVYKSILVTSQDKAPSVISRVLKKNNRDSAVASEFELVQLLPGDRELTIPHSANVFYAMD-GASH 82
Cdd:cd17210  2 DTCIIRVSVEDN-NGNMYKSIMLTSQDKTPAVIQRAMSKHNLESDPAEDYELVQVISEDRELVIPDNANVFYAMNsSVNF 80


               ....*..
1RLF_A      83 DFLLRQR 89
Cdd:cd17210 81 DFILRKK 87
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 4-90 1.12e-19

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 75.80  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLF_A          4 DCRIIRVQMELGEDGSvYKSILVTSQDKAPSVISRVLKKNNRDsAVASEFELVQLLPGDRELTIPHSANVFYAM-----D 78
Cdd:smart00314  1 DTFVLRVYVDDLPGGT-YKTLRVSSRTTARDVIQQLLEKFHLT-DDPEEYVLVEVLPDGKERVLPDDENPLQLQklwprR 78

                          90
                  ....*....|..
1RLF_A         79 GASHDFLLRQRR 90
Cdd:smart00314 79 GPNLRFVLRKRD 90
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 4-90 2.17e-15

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 64.66  E-value: 2.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLF_A         4 DCRIIRVQMELGEDGSVYKSILVTSQDKAPSVISRVLKKNNRDSAvASEFELV-QLLPGDRELTIPHSANVFYAM----- 77
Cdd:pfam00788  1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGLEDD-PRDYVLVeVLERGGGERRLPDDECPLQIQlqwpr 79

                         90
                 ....*....|...
1RLF_A        78 DGASHDFLLRQRR 90
Cdd:pfam00788 80 DASDSRFLLRKRD 92
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 7-87 5.51e-06

Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in various functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon.


Pssm-ID: 340563  Cd Length: 87  Bit Score: 40.76  E-value: 5.51e-06
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLF_A       7 IIRVQMELGEDGSVYKSILVTSQDKAPSVISRVLKKNNRDsAVASEFELVQLLP-GDRELTIPHSANVFYAMDGASHD-- 83
Cdd:cd17043  1 VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLLEKYGLE-EDPEDYSLYEVSEkQETERVLHDDECPLLIQLEWGPQgt 79


               ....*..
1RLF_A      84 ---FLLR 87
Cdd:cd17043 80 efrFVLK 86
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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