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Conserved domains on  [gi|929346278|ref|XP_014088258|]
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uncharacterized protein LOC106616211 isoform X3 [Bactrocera oleae]

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 cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 152-236 4.32e-23

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: 93.15  E-value: 4.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929346278 152 LIRVHTSALQPSSQYKSLVISEETTSDELLQLLLSCYNSMEPVEQFSIYEVCPGQEYQRKLHPDDIPLRAQSERMRRGET 231
Cdd:cd17043    1 VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLLEKYGLEEDPEDYSLYEVSEKQETERVLHDDECPLLIQLEWGPQGTE 80


                 ....*
gi 929346278 232 CHFLV 236
Cdd:cd17043   81 FRFVL 85
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 55-149 2.67e-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: 76.99  E-value: 2.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929346278   55 PQTTIKVFTNCLKIDIEYKTLGIQWDTTSKEVITQLLRRLKMrHRDPRLFYLSmEVSVRRAGVKTilvLDDDTRPAILQA 134
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGL-EDDPRDYVLV-EVLERGGGERR---LPDDECPLQIQL 75

                          90
                  ....*....|....*..
gi 929346278  135 CHPKGE--SRFCLQLKP 149
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 ...
 152-236 4.32e-23

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: 93.15  E-value: 4.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929346278 152 LIRVHTSALQPSSQYKSLVISEETTSDELLQLLLSCYNSMEPVEQFSIYEVCPGQEYQRKLHPDDIPLRAQSERMRRGET 231
Cdd:cd17043    1 VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLLEKYGLEEDPEDYSLYEVSEKQETERVLHDDECPLLIQLEWGPQGTE 80


                 ....*
gi 929346278 232 CHFLV 236
Cdd:cd17043   81 FRFVL 85
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 55-149 2.67e-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: 76.99  E-value: 2.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929346278   55 PQTTIKVFTNCLKIDIEYKTLGIQWDTTSKEVITQLLRRLKMrHRDPRLFYLSmEVSVRRAGVKTilvLDDDTRPAILQA 134
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGL-EDDPRDYVLV-EVLERGGGERR---LPDDECPLQIQL 75

                          90
                  ....*....|....*..
gi 929346278  135 CHPKGE--SRFCLQLKP 149
Cdd:pfam00788  76 QWPRDAsdSRFLLRKRD 92
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 149-236 1.24e-10

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: 58.11  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929346278  149 PGGLIRVHTSALQPSSQYKSLVISEETTSDELLQLLLSCYNSMEPVEQFSIYEVCPGQEYQRKLHPDDIPLRAQSERMRR 228
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGLEDDPRDYVLVEVLERGGGERRLPDDECPLQIQLQWPRD 80


                  ....*...
gi 929346278  229 GETCHFLV 236
Cdd:pfam00788  81 ASDSRFLL 88
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 151-236 1.82e-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: 46.14  E-value: 1.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929346278   151 GLIRVHTSaLQPSSQYKSLVISEETTSDELLQLLLSCYNSMEPVEQFSIYEVCPGQEYqRKLHPDDIPLRAQSERMRRGE 230
Cdd:smart00314   3 FVLRVYVD-DLPGGTYKTLRVSSRTTARDVIQQLLEKFHLTDDPEEYVLVEVLPDGKE-RVLPDDENPLQLQKLWPRRGP 80


                   ....*.
gi 929346278   231 TCHFLV 236
Cdd:smart00314  81 NLRFVL 86
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 56-148 7.30e-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: 44.21  E-value: 7.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929346278    56 QTTIKVFTNcLKIDIEYKTLGIQWDTTSKEVITQLLRRLKmRHRDPRLFYLSMEVSVRragvkTILVLDDDTRPAILQAC 135
Cdd:smart00314   2 TFVLRVYVD-DLPGGTYKTLRVSSRTTARDVIQQLLEKFH-LTDDPEEYVLVEVLPDG-----KERVLPDDENPLQLQKL 74

                           90
                   ....*....|...
gi 929346278   136 HPKGESRFCLQLK 148
Cdd:smart00314  75 WPRRGPNLRFVLR 87
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 58-148 5.15e-04

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: 39.22  E-value: 5.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929346278  58 TIKVFTNCLKIDIEYKTLGIQWDTTSKEVITQLLRRLKmRHRDPRLFYLsMEVSVRRAgvkTILVLDDDTRPAILQACHP 137
Cdd:cd17043    1 VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLLEKYG-LEEDPEDYSL-YEVSEKQE---TERVLHDDECPLLIQLEWG 75

                         90
                 ....*....|.
gi 929346278 138 KGESRFCLQLK 148
Cdd:cd17043   76 PQGTEFRFVLK 86
 
Name Accession Description Interval E-value
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 152-236 4.32e-23

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: 93.15  E-value: 4.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929346278 152 LIRVHTSALQPSSQYKSLVISEETTSDELLQLLLSCYNSMEPVEQFSIYEVCPGQEYQRKLHPDDIPLRAQSERMRRGET 231
Cdd:cd17043    1 VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLLEKYGLEEDPEDYSLYEVSEKQETERVLHDDECPLLIQLEWGPQGTE 80


                 ....*
gi 929346278 232 CHFLV 236
Cdd:cd17043   81 FRFVL 85
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 55-149 2.67e-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: 76.99  E-value: 2.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929346278   55 PQTTIKVFTNCLKIDIEYKTLGIQWDTTSKEVITQLLRRLKMrHRDPRLFYLSmEVSVRRAGVKTilvLDDDTRPAILQA 134
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGL-EDDPRDYVLV-EVLERGGGERR---LPDDECPLQIQL 75

                          90
                  ....*....|....*..
gi 929346278  135 CHPKGE--SRFCLQLKP 149
Cdd:pfam00788  76 QWPRDAsdSRFLLRKRD 92
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 149-236 1.24e-10

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: 58.11  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929346278  149 PGGLIRVHTSALQPSSQYKSLVISEETTSDELLQLLLSCYNSMEPVEQFSIYEVCPGQEYQRKLHPDDIPLRAQSERMRR 228
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGLEDDPRDYVLVEVLERGGGERRLPDDECPLQIQLQWPRD 80


                  ....*...
gi 929346278  229 GETCHFLV 236
Cdd:pfam00788  81 ASDSRFLL 88
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 151-236 1.82e-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: 46.14  E-value: 1.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929346278   151 GLIRVHTSaLQPSSQYKSLVISEETTSDELLQLLLSCYNSMEPVEQFSIYEVCPGQEYqRKLHPDDIPLRAQSERMRRGE 230
Cdd:smart00314   3 FVLRVYVD-DLPGGTYKTLRVSSRTTARDVIQQLLEKFHLTDDPEEYVLVEVLPDGKE-RVLPDDENPLQLQKLWPRRGP 80


                   ....*.
gi 929346278   231 TCHFLV 236
Cdd:smart00314  81 NLRFVL 86
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 56-148 7.30e-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: 44.21  E-value: 7.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929346278    56 QTTIKVFTNcLKIDIEYKTLGIQWDTTSKEVITQLLRRLKmRHRDPRLFYLSMEVSVRragvkTILVLDDDTRPAILQAC 135
Cdd:smart00314   2 TFVLRVYVD-DLPGGTYKTLRVSSRTTARDVIQQLLEKFH-LTDDPEEYVLVEVLPDG-----KERVLPDDENPLQLQKL 74

                           90
                   ....*....|...
gi 929346278   136 HPKGESRFCLQLK 148
Cdd:smart00314  75 WPRRGPNLRFVLR 87
RA_Myosin-IX cd01779
Ras-associating (RA) domain found in Myosin-IX; Myosins IX (Myo9) is a class of unique motor ...
 153-222 2.84e-05

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: 43.08  E-value: 2.84e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 929346278 153 IRVHTSALQPSSQYKSLVISEETTSDELLQLLLSCYNSMEPvEQFSIYEVC--PGQE-YQRKLHPDDIPLRAQ 222
Cdd:cd01779    2 VRVYPGALSPETEFLSVEATKQTTASEVIECLVAKLRLDKA-ECYELAEVCgsGGQGcKERRLGPSENPVQVQ 73
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 58-148 5.15e-04

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: 39.22  E-value: 5.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929346278  58 TIKVFTNCLKIDIEYKTLGIQWDTTSKEVITQLLRRLKmRHRDPRLFYLsMEVSVRRAgvkTILVLDDDTRPAILQACHP 137
Cdd:cd17043    1 VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLLEKYG-LEEDPEDYSL-YEVSEKQE---TERVLHDDECPLLIQLEWG 75

                         90
                 ....*....|.
gi 929346278 138 KGESRFCLQLK 148
Cdd:cd17043   76 PQGTEFRFVLK 86
RA2_Afadin cd01781
Ras-associating (RA) domain 2 found in Afadin; Afadin, also termed ALL1-fused gene from ...
 58-149 1.23e-03

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: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929346278  58 TIKVFTNCLKIDIEYKTLGIQWDTTSKEVITQLLRRLKMRHRDPRLFYLSMEVSVRRA------GVKTILVLDDDTRP-A 130
Cdd:cd01781    3 TLKIYGDSLKPEVPYKTLLLSTNDTADFVVREALEKYGLEKENPKDYCLVQVVLPPGGsprldgGGGKERILDDDECPlA 82

                         90       100
                 ....*....|....*....|
gi 929346278 131 ILQACHP-KGESRFCLQLKP 149
Cdd:cd01781   83 ILMRWPPsKGTLVFQLRRRP 102
RA_ARAPs cd17113
Ras-associating (RA) domain found in Arf-GAP with Rho-GAP domain, ANK repeat and PH ...
 152-219 1.44e-03

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: 38.00  E-value: 1.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 929346278 152 LIRVHtsALQPSSQYKSLVISEETTSDELLQLLLSCYNSMEPVEQFSIYEVCPGQEYQRKLHPDDIPL 219
Cdd:cd17113    5 LIPVY--IEEKEGTSVNIKVTPTMTAEEVVEQALNKKNLGGPEGNWALFEVIEDGGLERPLHESEKVL 70
RA_RASSF7_like cd16123
Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, ...
 171-221 2.69e-03

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: 36.84  E-value: 2.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 929346278 171 ISEETTSDELLQLLLSCYNSMEPVEQFSIYEVCPGQEyqRKLHPDDIPLRA 221
Cdd:cd16123   16 VTERTTCQDVIYALAQATGQTNDTGRYVLVERWRGIE--RPLPPRTRILKV 64
RA2_DAGK-theta cd01783
Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar ...
 59-129 5.85e-03

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: 36.44  E-value: 5.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 929346278  59 IKVFTNCLKIDIEYKTLGIQWDTTSKEVITQLLRRLKMRHRDPRLFYLsMEVSVRRAGVKTilVLDDDTRP 129
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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