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Conserved domains on  [gi|3880530|emb|CAA98966|]
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Ras-associating domain-containing protein [Caenorhabditis elegans]

Protein Classification

ubiquitin family protein( domain architecture ID 13645598)

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 pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 70-167 1.49e-16

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: 72.75  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3880530     70 DVGVLKVDTRSVKQCTDYKTIRVTNSTTARQVVEKFLTTLKLTcRDINMFELWMELTTRASGapvvtlLKLDPESRPYEL 149
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGLE-DDPRDYVLVEVLERGGGE------RRLPDDECPLQI 73

                          90       100
                  ....*....|....*....|
gi 3880530    150 QRCHPI--GMSRFILLQSPT 167
Cdd:pfam00788  74 QLQWPRdaSDSRFLLRKRDD 93
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 170-250 9.82e-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: 43.08  E-value: 9.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3880530  170 LVRVHDHNISPQSNYKSLLLSSQTTVLEAIHIVLglnRKY---DDISKYGLFLATPGGDAQIP-EDVSLVSIARLCQPNQ 245
Cdd:cd17043   1 VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLL---EKYgleEDPEDYSLYEVSEKQETERVlHDDECPLLIQLEWGPQ 77


                ....*
gi 3880530  246 KIIIR 250
Cdd:cd17043  78 GTEFR 82
 
Name Accession Description Interval E-value
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 70-167 1.49e-16

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: 72.75  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3880530     70 DVGVLKVDTRSVKQCTDYKTIRVTNSTTARQVVEKFLTTLKLTcRDINMFELWMELTTRASGapvvtlLKLDPESRPYEL 149
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGLE-DDPRDYVLVEVLERGGGE------RRLPDDECPLQI 73

                          90       100
                  ....*....|....*....|
gi 3880530    150 QRCHPI--GMSRFILLQSPT 167
Cdd:pfam00788  74 QLQWPRdaSDSRFLLRKRDD 93
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 70-175 5.64e-12

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: 60.39  E-value: 5.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3880530      70 DVGVLKVDTRSVKQCTdYKTIRVTNSTTARQVVEKFLTTLKLTCrDINMFELWMELttrasgaPVVTLLKLDPESRPYEL 149
Cdd:smart00314   1 DTFVLRVYVDDLPGGT-YKTLRVSSRTTARDVIQQLLEKFHLTD-DPEEYVLVEVL-------PDGKERVLPDDENPLQL 71

                           90       100
                   ....*....|....*....|....*.
gi 3880530     150 QRCHPIGmsrfillQSPTGYLVRVHD 175
Cdd:smart00314  72 QKLWPRR-------GPNLRFVLRKRD 90
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 170-250 9.82e-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: 43.08  E-value: 9.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3880530  170 LVRVHDHNISPQSNYKSLLLSSQTTVLEAIHIVLglnRKY---DDISKYGLFLATPGGDAQIP-EDVSLVSIARLCQPNQ 245
Cdd:cd17043   1 VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLL---EKYgleEDPEDYSLYEVSEKQETERVlHDDECPLLIQLEWGPQ 77


                ....*
gi 3880530  246 KIIIR 250
Cdd:cd17043  78 GTEFR 82
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 169-247 1.35e-03

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: 36.89  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3880530     169 YLVRVHDHNISPQSnYKSLLLSSQTTVLEAIHIVLGLNRKYDDISKYGLFLATPGG-DAQIPEDVSLVSIARLCQPNQKI 247
Cdd:smart00314   3 FVLRVYVDDLPGGT-YKTLRVSSRTTARDVIQQLLEKFHLTDDPEEYVLVEVLPDGkERVLPDDENPLQLQKLWPRRGPN 81
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 171-243 2.60e-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: 36.16  E-value: 2.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3880530    171 VRVHDHNISPQSNYKSLLLSSQTTVLEAIHIVLglnRKY---DDISKYGLFLATPGGDAQ--IPEDVSLVSIARLCQP 243
Cdd:pfam00788   5 LKVYTEDGKPGTTYKTILVSSSTTAEEVIEALL---EKFgleDDPRDYVLVEVLERGGGErrLPDDECPLQIQLQWPR 79
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 73-122 3.69e-03

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: 35.76  E-value: 3.69e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 3880530   73 VLKVDTRSVKQCTDYKTIRVTNSTTARQVVEKFLTTLKLTcRDINMFELW 122
Cdd:cd17043   1 VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLLEKYGLE-EDPEDYSLY 49
 
Name Accession Description Interval E-value
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 70-167 1.49e-16

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: 72.75  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3880530     70 DVGVLKVDTRSVKQCTDYKTIRVTNSTTARQVVEKFLTTLKLTcRDINMFELWMELTTRASGapvvtlLKLDPESRPYEL 149
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGLE-DDPRDYVLVEVLERGGGE------RRLPDDECPLQI 73

                          90       100
                  ....*....|....*....|
gi 3880530    150 QRCHPI--GMSRFILLQSPT 167
Cdd:pfam00788  74 QLQWPRdaSDSRFLLRKRDD 93
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 70-175 5.64e-12

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: 60.39  E-value: 5.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3880530      70 DVGVLKVDTRSVKQCTdYKTIRVTNSTTARQVVEKFLTTLKLTCrDINMFELWMELttrasgaPVVTLLKLDPESRPYEL 149
Cdd:smart00314   1 DTFVLRVYVDDLPGGT-YKTLRVSSRTTARDVIQQLLEKFHLTD-DPEEYVLVEVL-------PDGKERVLPDDENPLQL 71

                           90       100
                   ....*....|....*....|....*.
gi 3880530     150 QRCHPIGmsrfillQSPTGYLVRVHD 175
Cdd:smart00314  72 QKLWPRR-------GPNLRFVLRKRD 90
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 170-250 9.82e-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: 43.08  E-value: 9.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3880530  170 LVRVHDHNISPQSNYKSLLLSSQTTVLEAIHIVLglnRKY---DDISKYGLFLATPGGDAQIP-EDVSLVSIARLCQPNQ 245
Cdd:cd17043   1 VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLL---EKYgleEDPEDYSLYEVSEKQETERVlHDDECPLLIQLEWGPQ 77


                ....*
gi 3880530  246 KIIIR 250
Cdd:cd17043  78 GTEFR 82
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 169-247 1.35e-03

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: 36.89  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3880530     169 YLVRVHDHNISPQSnYKSLLLSSQTTVLEAIHIVLGLNRKYDDISKYGLFLATPGG-DAQIPEDVSLVSIARLCQPNQKI 247
Cdd:smart00314   3 FVLRVYVDDLPGGT-YKTLRVSSRTTARDVIQQLLEKFHLTDDPEEYVLVEVLPDGkERVLPDDENPLQLQKLWPRRGPN 81
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 171-243 2.60e-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: 36.16  E-value: 2.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3880530    171 VRVHDHNISPQSNYKSLLLSSQTTVLEAIHIVLglnRKY---DDISKYGLFLATPGGDAQ--IPEDVSLVSIARLCQP 243
Cdd:pfam00788   5 LKVYTEDGKPGTTYKTILVSSSTTAEEVIEALL---EKFgleDDPRDYVLVEVLERGGGErrLPDDECPLQIQLQWPR 79
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 73-122 3.69e-03

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: 35.76  E-value: 3.69e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 3880530   73 VLKVDTRSVKQCTDYKTIRVTNSTTARQVVEKFLTTLKLTcRDINMFELW 122
Cdd:cd17043   1 VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLLEKYGLE-EDPEDYSLY 49
 
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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