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Conserved domains on  [gi|86565011|ref|NP_001033555|]
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Ras-associating domain-containing protein [Caenorhabditis elegans]

Protein Classification

ubiquitin family protein( domain architecture ID 13006353)

ubiquitin family protein belongs to an diverse class of protein modifier and gene expression regulatory proteins that participate in a number of cellular processes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RA_RASSF7_like cd16123
Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, ...
 2-79 9.19e-35

Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, RASSF9, and RASSF10; The RASSF family of proteins shares a conserved RalGDS/AF6 Ras association (RA) domain either in the C-terminus (RASSF1-6) or N-terminus (RASSF7-10). RASSF7-10 lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The structural differences between the C-terminus and N-terminus RASSF subgroups have led to the suggestion that they are two distinct families. RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ras proteins are small GTPases that are involved in cellular signal transduction. The N-terminus RASSF proteins are potential Ras effectors that have been linked to key biological processes, including cell death, proliferation, microtubule stability, promoter methylation, vesicle trafficking and response to hypoxia.


:

Pssm-ID: 340540  Cd Length: 81  Bit Score: 121.58  E-value: 9.19e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565011   2 ELKINIDGLERSVSGVTDTTTCSQIIYALAHATSQR---GRFVMVEKYRNVERRLAPTDRPLETLRKWREHAANVTFQML 78
Cdd:cd16123   1 ELKVWVDGEERVVSGVTERTTCQDVIYALAQATGQTndtGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQSNVQFVLR 80


                .
gi 86565011  79 R 79
Cdd:cd16123  81 R 81
 
Name Accession Description Interval E-value
RA_RASSF7_like cd16123
Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, ...
 2-79 9.19e-35

Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, RASSF9, and RASSF10; The RASSF family of proteins shares a conserved RalGDS/AF6 Ras association (RA) domain either in the C-terminus (RASSF1-6) or N-terminus (RASSF7-10). RASSF7-10 lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The structural differences between the C-terminus and N-terminus RASSF subgroups have led to the suggestion that they are two distinct families. RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ras proteins are small GTPases that are involved in cellular signal transduction. The N-terminus RASSF proteins are potential Ras effectors that have been linked to key biological processes, including cell death, proliferation, microtubule stability, promoter methylation, vesicle trafficking and response to hypoxia.


Pssm-ID: 340540  Cd Length: 81  Bit Score: 121.58  E-value: 9.19e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565011   2 ELKINIDGLERSVSGVTDTTTCSQIIYALAHATSQR---GRFVMVEKYRNVERRLAPTDRPLETLRKWREHAANVTFQML 78
Cdd:cd16123   1 ELKVWVDGEERVVSGVTERTTCQDVIYALAQATGQTndtGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQSNVQFVLR 80


                .
gi 86565011  79 R 79
Cdd:cd16123  81 R 81
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 17-82 1.43e-03

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: 37.31  E-value: 1.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86565011    17 VTDTTTCSQIIYALA---HATSQRGRFVMVE--KYRNVERRLAPTDRPLETLRKWREHAANVTFQMLRVDQ 82
Cdd:pfam00788  23 VSSSTTAEEVIEALLekfGLEDDPRDYVLVEvlERGGGERRLPDDECPLQIQLQWPRDASDSRFLLRKRDD 93
 
Name Accession Description Interval E-value
RA_RASSF7_like cd16123
Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, ...
 2-79 9.19e-35

Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, RASSF9, and RASSF10; The RASSF family of proteins shares a conserved RalGDS/AF6 Ras association (RA) domain either in the C-terminus (RASSF1-6) or N-terminus (RASSF7-10). RASSF7-10 lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The structural differences between the C-terminus and N-terminus RASSF subgroups have led to the suggestion that they are two distinct families. RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ras proteins are small GTPases that are involved in cellular signal transduction. The N-terminus RASSF proteins are potential Ras effectors that have been linked to key biological processes, including cell death, proliferation, microtubule stability, promoter methylation, vesicle trafficking and response to hypoxia.


Pssm-ID: 340540  Cd Length: 81  Bit Score: 121.58  E-value: 9.19e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565011   2 ELKINIDGLERSVSGVTDTTTCSQIIYALAHATSQR---GRFVMVEKYRNVERRLAPTDRPLETLRKWREHAANVTFQML 78
Cdd:cd16123   1 ELKVWVDGEERVVSGVTERTTCQDVIYALAQATGQTndtGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQSNVQFVLR 80


                .
gi 86565011  79 R 79
Cdd:cd16123  81 R 81
RA_RASSF8 cd16134
Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); ...
 2-79 1.12e-27

Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); RASSF8, also termed carcinoma-associated protein HOJ-1, is a member of the N-terminus RASSF7-10 protein family. RASSF7-10 has an RA-domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of N-terminal RASSF proteins family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF8 has been described as a potential tumor suppressor. RASSF8 might have a role in the regulation of cell-cell adhesion and cell growth.


Pssm-ID: 340551  Cd Length: 82  Bit Score: 102.90  E-value: 1.12e-27
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86565011   2 ELKINIDGLERSVSGVTDTTTCSQIIYALAHATSQRGRFVMVEKYRNVERRLAPTDRPLETLRKWREHAANVTFQMLR 79
Cdd:cd16134   1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRR 78
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 1-79 3.21e-21

Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); RASSF7, also termed HRAS1-related cluster protein 1, is a member of the N-terminus RASSF7-10 protein family. RASSF7-10 has an RA-domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of N-terminal RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF7 is a potential Ras effector as its function has been linked to some key biological processes including the regulation of cell death and proliferation; for example, RASSF7 is up-regulated in pancreatic cancer.


Pssm-ID: 340552  Cd Length: 83  Bit Score: 85.77  E-value: 3.21e-21
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86565011   1 MELKINIDGLERSVSGVTDTTTCSQIIYALAHATSQRGRFVMVEKYRNVERRLAPTDRPLETLRKWREHAANVTFQMLR 79
Cdd:cd16135   1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRR 79
RA_RASSF9 cd16133
Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, ...
 11-81 1.17e-06

Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, also termed PAM COOH-terminal interactor protein 1 (P-CIP1), or peptidylglycine alpha-amidating monooxygenase COOH-terminal interactor, is a member of N-terminus RASSF7-10 protein family. RASSF7-10 has an RA domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of the N-terminal RASSF proteins family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF9 was formerly known as PAM COOH-terminal interactor-1 (P-CIP1) because of its interaction with peptidylglycine alpha-amidating mono-oxygenase (PAM) and possibility of its role in regulating the trafficking of integral membrane PAM. RASSF9 is widely expressed in multiple organs such as testis, kidney, skeletal muscle, liver, lung, brain, and heart. Cloned RASSF9 showed preferential binding to N-Ras and K-Ras.


Pssm-ID: 340550  Cd Length: 93  Bit Score: 45.99  E-value: 1.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565011  11 ERSVSGVTDTTTCSQIIYAL-----------AHATSQRGRFVMVEKYRNVERRLAPTDRPLETLRKWREHAANVTFQMLR 79
Cdd:cd16133  10 EKVVCGLTKHTTCADVIQALleeheatfgekRFLLGQPSDYCIVEKWRGFERVLPPLTKILRLWKAWGDEQPNLQFVLVK 89


                ..
gi 86565011  80 VD 81
Cdd:cd16133  90 AD 91
RA_RASSF10 cd16132
Ras-associating (RA) domain found in N-terminal Ras-association domain family 10 (RASSF10); ...
 11-79 3.70e-04

Ras-associating (RA) domain found in N-terminal Ras-association domain family 10 (RASSF10); RASSF10 is a member of a family of N-terminus RASSF7-10 proteins. RASSF7-10 has an RA domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. RA domain of N-terminal RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF10 is expressed in a wide variety of tissues and its expression in human thyroid, pancreas, placenta, heart, lung and kidney has been observed. RASSF10 is the most frequently methylated of the N-terminal RASSFs in some cancers such as in childhood acute lymphoblastic leukemia and both, thyroid cancer cell lines and primary thyroid carcinomas.


Pssm-ID: 340549  Cd Length: 102  Bit Score: 39.11  E-value: 3.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565011  11 ERSVSGVTDTTTCSQIIYALAHATSQRGR--------------------FVMVEKYRNVERRLAPTDRPLETLRKWREHA 70
Cdd:cd16132  10 EKLVSGLSRRTTCADVVRVLLEDQNRSQQeeeeeegerdggmlsgppqsYCIVEKWRGFERILPNKTKILRLWAAWGEEQ 89


                ....*....
gi 86565011  71 ANVTFQMLR 79
Cdd:cd16132  90 ENVRFVLVR 98
RA_ASPP1_2 cd16125
Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 (ASPP) 1 and 2; The ...
 1-75 1.21e-03

Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 (ASPP) 1 and 2; The ASPP protein (apoptosis-stimulating protein of p53; also called ankyrin repeat-, Src homology 3 domain- and Pro-rich region-containing protein) plays a critical role in regulating apoptosis. The ASPP family consists of three members, ASPP1, ASPP2 and iASPP, all of which bind to p53 and regulate p53-mediated apoptosis. ASPP1 and ASPP2, have a RA domain at their N-terminus and have pro-apoptotic functions, while iASPP is involved in anti-apoptotic responses. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different 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 fold with low sequence similarity to ubiquitin.


Pssm-ID: 340542  Cd Length: 80  Bit Score: 37.28  E-value: 1.21e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86565011   1 MELKINIDGLERSVSGV--TDTTTCSQIIYALAHATsqRGRFVMVEKYRNVERRLAPTDRPLETLRKWREHAANVTF 75
Cdd:cd16125   1 VILKVYLSDNNQTVTEVpiTPETTCQDVVDCCKEPG--EENCHLVEVWRGCERPLPEEENPYEILQQWGSHRDEVKF 75
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 17-82 1.43e-03

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: 37.31  E-value: 1.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86565011    17 VTDTTTCSQIIYALA---HATSQRGRFVMVE--KYRNVERRLAPTDRPLETLRKWREHAANVTFQMLRVDQ 82
Cdd:pfam00788  23 VSSSTTAEEVIEALLekfGLEDDPRDYVLVEvlERGGGERRLPDDECPLQIQLQWPRDASDSRFLLRKRDD 93
RA_CYR1_like cd17214
Ras-associating (RA) domain found in Saccharomyces cerevisiae adenylate cyclase and similar ...
 20-66 2.17e-03

Ras-associating (RA) domain found in Saccharomyces cerevisiae adenylate cyclase and similar proteins; CYR1, also termed ATP pyrophosphate-lyase, or adenylyl cyclase, is a fungal adenylate cyclase that regulates developmental processes such as hyphal growth, biofilm formation, and phenotypic switching. CYR1 plays essential roles in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP. It acts as a scaffold protein keeping Ras2 available for its regulatory factors, the Ira proteins. CYR1 has at least four domains, including an N-terminal adenylate cyclase G-alpha binding domain, a Ras-associating (RA) domain, a middle leucine-rich repeat region, and a catalytic 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 CYR1 post-translationally modifies a small GTPase called Ras, which is involved in cellular signal transduction. CYR1 activity is stimulated directly by regulatory proteins (Ras1 and Gpa2), peptidoglycan fragments and carbon dioxide.


Pssm-ID: 340734  Cd Length: 99  Bit Score: 36.81  E-value: 2.17e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 86565011  20 TTTCSQIIYALAH----ATSQRGRFVMVEkyRNVERRLAPTDRPLETLRKW 66
Cdd:cd17214  20 NTTTSELLSMLAKkfflPDSANYRLYLRE--RGLERILRSNEKPLLIQKRL 68
 
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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