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Conserved domains on  [gi|2103691414|ref|XP_039502127|]
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uncharacterized protein LOC120458521 [Drosophila santomea]

Protein Classification

RA domain-containing protein( domain architecture ID 13645598)

RA domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 157-243 9.92e-28

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: 105.09  E-value: 9.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103691414 157 LIRVHTSALQPSSQYKSLVISEETTCDELLHLLLGCYSSPEPVENFSLYEVCPGQECQRKLHPDDLPLRTQMERMKRGEG 236
Cdd:cd17043     1 VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLLEKYGLEEDPEDYSLYEVSEKQETERVLHDDECPLLIQLEWGPQGTE 80


                  ....*..
gi 2103691414 237 CHFLVRR 243
Cdd:cd17043    81 FRFVLKR 87
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 60-154 3.27e-17

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: 76.22  E-value: 3.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103691414  60 PQTTIKVYTNCLKIDIEYKTLGIQWDTTSKEVIGQLLRRLKMrHRDPRLFYLSmEVAVRRAGVKTilvLDDDTRPAIMQA 139
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGL-EDDPRDYVLV-EVLERGGGERR---LPDDECPLQIQL 75

                          90
                  ....*....|....*..
gi 2103691414 140 CHPKGE--SRFCLQLKP 154
Cdd:pfam00788  76 QWPRDAsdSRFLLRKRD 92
 
Name Accession Description Interval E-value
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 157-243 9.92e-28

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: 105.09  E-value: 9.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103691414 157 LIRVHTSALQPSSQYKSLVISEETTCDELLHLLLGCYSSPEPVENFSLYEVCPGQECQRKLHPDDLPLRTQMERMKRGEG 236
Cdd:cd17043     1 VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLLEKYGLEEDPEDYSLYEVSEKQETERVLHDDECPLLIQLEWGPQGTE 80


                  ....*..
gi 2103691414 237 CHFLVRR 243
Cdd:cd17043    81 FRFVLKR 87
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 60-154 3.27e-17

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: 76.22  E-value: 3.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103691414  60 PQTTIKVYTNCLKIDIEYKTLGIQWDTTSKEVIGQLLRRLKMrHRDPRLFYLSmEVAVRRAGVKTilvLDDDTRPAIMQA 139
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGL-EDDPRDYVLV-EVLERGGGERR---LPDDECPLQIQL 75

                          90
                  ....*....|....*..
gi 2103691414 140 CHPKGE--SRFCLQLKP 154
Cdd:pfam00788  76 QWPRDAsdSRFLLRKRD 92
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 154-245 7.59e-13

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: 63.89  E-value: 7.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103691414 154 PGGLIRVHTSALQPSSQYKSLVISEETTCDELLHLLL---GCYSSPEpveNFSLYEVCPGQECQRKLHPDDLPLRTQMER 230
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLekfGLEDDPR---DYVLVEVLERGGGERRLPDDECPLQIQLQW 77

                          90
                  ....*....|....*
gi 2103691414 231 MKRGEGCHFLVRRTP 245
Cdd:pfam00788  78 PRDASDSRFLLRKRD 92
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 156-243 3.49e-06

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: 44.98  E-value: 3.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103691414  156 GLIRVHTSaLQPSSQYKSLVISEETTCDELLHLLL---GCYSSPEpveNFSLYEVCPGQEcQRKLHPDDLPLRTQMERMK 232
Cdd:smart00314   3 FVLRVYVD-DLPGGTYKTLRVSSRTTARDVIQQLLekfHLTDDPE---EYVLVEVLPDGK-ERVLPDDENPLQLQKLWPR 77

                           90
                   ....*....|.
gi 2103691414  233 RGEGCHFLVRR 243
Cdd:smart00314  78 RGPNLRFVLRK 88
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 61-153 2.37e-05

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: 42.67  E-value: 2.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103691414   61 QTTIKVYTNcLKIDIEYKTLGIQWDTTSKEVIGQLLRRLKmRHRDPRLFYLsmevaVRRAGVKTILVLDDDTRPAIMQAC 140
Cdd:smart00314   2 TFVLRVYVD-DLPGGTYKTLRVSSRTTARDVIQQLLEKFH-LTDDPEEYVL-----VEVLPDGKERVLPDDENPLQLQKL 74

                           90
                   ....*....|...
gi 2103691414  141 HPKGESRFCLQLK 153
Cdd:smart00314  75 WPRRGPNLRFVLR 87
RA2_Afadin cd01781
Ras-associating (RA) domain 2 found in Afadin; Afadin, also termed ALL1-fused gene from ...
 63-154 8.38e-04

Ras-associating (RA) domain 2 found in Afadin; Afadin, also termed ALL1-fused gene from chromosome 6 protein (AF-6), or canoe, is involved in many fundamental signaling cascades in cells. In addition, it is involved in oncogenesis and metastasis. Afadin has multiple domains: from the N-terminus to the C-terminus it has two Ras-associated (RA) domains, a forkhead-associated domain, a dilute domain, a PDZ domain, three proline-rich domains, and an F-actin binding domain. 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 a 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 in eukaryotes. Afadin is abundant at cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. This family corresponds to the second RA domain of afadin.


Pssm-ID: 340479  Cd Length: 102  Bit Score: 38.41  E-value: 8.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103691414  63 TIKVYTNCLKIDIEYKTLGIQWDTTSKEVIGQLLRRLKMRHRDPRLFYLSMEVAVRRA------GVKTILVLDDDTRP-A 135
Cdd:cd01781     3 TLKIYGDSLKPEVPYKTLLLSTNDTADFVVREALEKYGLEKENPKDYCLVQVVLPPGGsprldgGGGKERILDDDECPlA 82

                          90       100
                  ....*....|....*....|
gi 2103691414 136 IMQACHP-KGESRFCLQLKP 154
Cdd:cd01781    83 ILMRWPPsKGTLVFQLRRRP 102
 
Name Accession Description Interval E-value
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 157-243 9.92e-28

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: 105.09  E-value: 9.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103691414 157 LIRVHTSALQPSSQYKSLVISEETTCDELLHLLLGCYSSPEPVENFSLYEVCPGQECQRKLHPDDLPLRTQMERMKRGEG 236
Cdd:cd17043     1 VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLLEKYGLEEDPEDYSLYEVSEKQETERVLHDDECPLLIQLEWGPQGTE 80


                  ....*..
gi 2103691414 237 CHFLVRR 243
Cdd:cd17043    81 FRFVLKR 87
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 60-154 3.27e-17

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: 76.22  E-value: 3.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103691414  60 PQTTIKVYTNCLKIDIEYKTLGIQWDTTSKEVIGQLLRRLKMrHRDPRLFYLSmEVAVRRAGVKTilvLDDDTRPAIMQA 139
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGL-EDDPRDYVLV-EVLERGGGERR---LPDDECPLQIQL 75

                          90
                  ....*....|....*..
gi 2103691414 140 CHPKGE--SRFCLQLKP 154
Cdd:pfam00788  76 QWPRDAsdSRFLLRKRD 92
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 154-245 7.59e-13

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: 63.89  E-value: 7.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103691414 154 PGGLIRVHTSALQPSSQYKSLVISEETTCDELLHLLL---GCYSSPEpveNFSLYEVCPGQECQRKLHPDDLPLRTQMER 230
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLekfGLEDDPR---DYVLVEVLERGGGERRLPDDECPLQIQLQW 77

                          90
                  ....*....|....*
gi 2103691414 231 MKRGEGCHFLVRRTP 245
Cdd:pfam00788  78 PRDASDSRFLLRKRD 92
RA_ARAPs cd17113
Ras-associating (RA) domain found in Arf-GAP with Rho-GAP domain, ANK repeat and PH ...
 157-245 1.96e-07

Ras-associating (RA) domain found in Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing proteins ARAP1, ARAP2, ARAP3, and similar proteins; ARAPs are phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P(3))-dependent Arf Rap-activated guanosine triphosphatase (GTPase)-activating proteins (GAPs). They contain multiple functional domains, including ArfGAP and RhoGAP domains, as well as a sterile alpha motif (Sam) domain, five PH domains, and a RA domain. The RA domain has the beta-grasp ubiquitin-like 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 in eukaryotes.


Pssm-ID: 340633  Cd Length: 95  Bit Score: 48.78  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103691414 157 LIRVHtsALQPSSQYKSLVISEETTCDELLHLLLGCYSSPEPVENFSLYEVCPGQECQRKLHPDDLPLRTQMER-MKRGE 235
Cdd:cd17113     5 LIPVY--IEEKEGTSVNIKVTPTMTAEEVVEQALNKKNLGGPEGNWALFEVIEDGGLERPLHESEKVLDVVLRWsQWPRK 82

                          90
                  ....*....|
gi 2103691414 236 GCHFLVRRTP 245
Cdd:cd17113    83 SNYLCVKKNP 92
RA_Myosin-IX cd01779
Ras-associating (RA) domain found in Myosin-IX; Myosins IX (Myo9) is a class of unique motor ...
 158-244 1.40e-06

Ras-associating (RA) domain found in Myosin-IX; Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains and a C-terminal tail containing a Rho-GTPase activating protein (RhoGAP) domain. The RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis and IXb is expressed abundantly in tissues of the immune system.


Pssm-ID: 340477  Cd Length: 97  Bit Score: 46.55  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103691414 158 IRVHTSALQPSSQYKSLVISEETTCDELLHLLLGCYSSPEPvENFSLYEVC--PGQEC-QRKLHPDDLPLRTQM------ 228
Cdd:cd01779     2 VRVYPGALSPETEFLSVEATKQTTASEVIECLVAKLRLDKA-ECYELAEVCgsGGQGCkERRLGPSENPVQVQLlwpkma 80

                          90
                  ....*....|....*..
gi 2103691414 229 -ERMKRGEGCHFLVRRT 244
Cdd:cd01779    81 gDSDNQVTSYRFFLREK 97
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 156-243 3.49e-06

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: 44.98  E-value: 3.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103691414  156 GLIRVHTSaLQPSSQYKSLVISEETTCDELLHLLL---GCYSSPEpveNFSLYEVCPGQEcQRKLHPDDLPLRTQMERMK 232
Cdd:smart00314   3 FVLRVYVD-DLPGGTYKTLRVSSRTTARDVIQQLLekfHLTDDPE---EYVLVEVLPDGK-ERVLPDDENPLQLQKLWPR 77

                           90
                   ....*....|.
gi 2103691414  233 RGEGCHFLVRR 243
Cdd:smart00314  78 RGPNLRFVLRK 88
RA_RASSF7_like cd16123
Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, ...
 176-226 1.37e-05

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: 43.00  E-value: 1.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2103691414 176 ISEETTCDELLHLLLGCYSSPEPVENFSLYEVCPGqeCQRKLHPDDLPLRT 226
Cdd:cd16123    16 VTERTTCQDVIYALAQATGQTNDTGRYVLVERWRG--IERPLPPRTRILKV 64
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 61-153 2.37e-05

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: 42.67  E-value: 2.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103691414   61 QTTIKVYTNcLKIDIEYKTLGIQWDTTSKEVIGQLLRRLKmRHRDPRLFYLsmevaVRRAGVKTILVLDDDTRPAIMQAC 140
Cdd:smart00314   2 TFVLRVYVD-DLPGGTYKTLRVSSRTTARDVIQQLLEKFH-LTDDPEEYVL-----VEVLPDGKERVLPDDENPLQLQKL 74

                           90
                   ....*....|...
gi 2103691414  141 HPKGESRFCLQLK 153
Cdd:smart00314  75 WPRRGPNLRFVLR 87
RA2_Afadin cd01781
Ras-associating (RA) domain 2 found in Afadin; Afadin, also termed ALL1-fused gene from ...
 63-154 8.38e-04

Ras-associating (RA) domain 2 found in Afadin; Afadin, also termed ALL1-fused gene from chromosome 6 protein (AF-6), or canoe, is involved in many fundamental signaling cascades in cells. In addition, it is involved in oncogenesis and metastasis. Afadin has multiple domains: from the N-terminus to the C-terminus it has two Ras-associated (RA) domains, a forkhead-associated domain, a dilute domain, a PDZ domain, three proline-rich domains, and an F-actin binding domain. 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 a 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 in eukaryotes. Afadin is abundant at cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. This family corresponds to the second RA domain of afadin.


Pssm-ID: 340479  Cd Length: 102  Bit Score: 38.41  E-value: 8.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103691414  63 TIKVYTNCLKIDIEYKTLGIQWDTTSKEVIGQLLRRLKMRHRDPRLFYLSMEVAVRRA------GVKTILVLDDDTRP-A 135
Cdd:cd01781     3 TLKIYGDSLKPEVPYKTLLLSTNDTADFVVREALEKYGLEKENPKDYCLVQVVLPPGGsprldgGGGKERILDDDECPlA 82

                          90       100
                  ....*....|....*....|
gi 2103691414 136 IMQACHP-KGESRFCLQLKP 154
Cdd:cd01781    83 ILMRWPPsKGTLVFQLRRRP 102
RA2_DAGK-theta cd01783
Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar ...
 64-134 8.83e-04

Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar proteins; DAGK phosphorylates the second messenger diacylglycerol to phosphatidic acid as part of a protein kinase C pathway. DAGK-theta is characterized as a type V DAGK that has three cysteine-rich domains (all other isoforms have two), a proline/glycine-rich domain at its N-terminal, and a proposed Ras-associating (RA) domain. 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 a 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 in eukaryotes. There are ten mammalian isoforms of DAGK have been identified to date, these are organized into five categories based on the domain architecture. DAGK-theta also contains a pleckstrin homology (PH) domain. The subcellular localization and the activity of DAGK-theta are regulated in a complex (stimulation- and cell type-dependent) manner. This family corresponds to the second RA domain of DAGK-theta.


Pssm-ID: 340481  Cd Length: 95  Bit Score: 38.36  E-value: 8.83e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2103691414  64 IKVYTNCLKIDIEYKTLGIQWDTTSKEVIGQLLRRLKMRHRDPRLFYLsMEVAVRRAGVKTilVLDDDTRP 134
Cdd:cd01783     3 IRVYPGWLKVGVAYKSIPVTKETTVEEVIKEALPKFGLQDEDPEDFRL-VEVLMDKGVVER--VMLRDECP 70
 
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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