NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15826359]
View 

Chain F, KIAA0380

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RGS_PDZRhoGEF cd08753
Regulator of G protein signaling (RGS) domain found in the PDZ-Rho guanine nucleotide exchange ...
 10-154 5.71e-102

Regulator of G protein signaling (RGS) domain found in the PDZ-Rho guanine nucleotide exchange factor (RhoGEF) protein; The RGS domain is an essential part of the PDZ-RhoGEF (PDZ:Postsynaptic density 95, Disk large, Zona occludens-1; RhoGEF: Rho guanine nucleotide exchange factor; alias PRG) protein, a member of RhoGEFs subfamily of the RGS protein family. The RhoGEFs are peripheral membrane proteins that regulate essential cellular processes, including cell shape, cell migration, and cell cycle progression, as well as gene transcription by linking signals from heterotrimeric G-alpha12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. RhoGEFs subfamily includes leukemia-associated RhoGEF protein (LARG), p115RhoGEF, PDZ-RhoGEF and its rat specific splice variant GTRAP48. The RGS domain of RhoGEFs has very little sequence similarity with the canonical RGS domain of the RGS proteins and is often refered to as RH (RGS Homology) domain. In contrast to p115RhoGEF and LARG, PDZ-RhoGEF cannot serve as a GTPase-activating protein (GAP), due to the mutation of sites in the RGS domain region that are crucial for GAP activity. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


:

Pssm-ID: 188707  Cd Length: 145  Bit Score: 291.00  E-value: 5.71e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826359  10 LIIGPEEDYDPGYFNNESDIIFQDLEKLKSRPAHLGVFLRYIFSQADPSPLLFYLCAEVYQQASPKDSRSLGKDIWNIFL 89
Cdd:cd08753   1 LIIGPEEDYDPGYFNNESDIIFQDLEKLKSRPAHLVVFLRYIFSQADPGPLLFYLCSEVYQQTSPKDSRSLGKDIWNIFL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15826359  90 EKNAPLRVKIPE*LQAEIDSRLRNSEDARGVLCEAQEAA*PEIQEQIHDYRTKRTLGLGSLYGEN 154
Cdd:cd08753  81 EKNAPLRVKIPEMLQAEIDLRLRNNEDPRGVLCEAQEAVMPEIQEQIQDYRSKRTLGLGSLYGEN 145
 
Name Accession Description Interval E-value
RGS_PDZRhoGEF cd08753
Regulator of G protein signaling (RGS) domain found in the PDZ-Rho guanine nucleotide exchange ...
 10-154 5.71e-102

Regulator of G protein signaling (RGS) domain found in the PDZ-Rho guanine nucleotide exchange factor (RhoGEF) protein; The RGS domain is an essential part of the PDZ-RhoGEF (PDZ:Postsynaptic density 95, Disk large, Zona occludens-1; RhoGEF: Rho guanine nucleotide exchange factor; alias PRG) protein, a member of RhoGEFs subfamily of the RGS protein family. The RhoGEFs are peripheral membrane proteins that regulate essential cellular processes, including cell shape, cell migration, and cell cycle progression, as well as gene transcription by linking signals from heterotrimeric G-alpha12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. RhoGEFs subfamily includes leukemia-associated RhoGEF protein (LARG), p115RhoGEF, PDZ-RhoGEF and its rat specific splice variant GTRAP48. The RGS domain of RhoGEFs has very little sequence similarity with the canonical RGS domain of the RGS proteins and is often refered to as RH (RGS Homology) domain. In contrast to p115RhoGEF and LARG, PDZ-RhoGEF cannot serve as a GTPase-activating protein (GAP), due to the mutation of sites in the RGS domain region that are crucial for GAP activity. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


Pssm-ID: 188707  Cd Length: 145  Bit Score: 291.00  E-value: 5.71e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826359  10 LIIGPEEDYDPGYFNNESDIIFQDLEKLKSRPAHLGVFLRYIFSQADPSPLLFYLCAEVYQQASPKDSRSLGKDIWNIFL 89
Cdd:cd08753   1 LIIGPEEDYDPGYFNNESDIIFQDLEKLKSRPAHLVVFLRYIFSQADPGPLLFYLCSEVYQQTSPKDSRSLGKDIWNIFL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15826359  90 EKNAPLRVKIPE*LQAEIDSRLRNSEDARGVLCEAQEAA*PEIQEQIHDYRTKRTLGLGSLYGEN 154
Cdd:cd08753  81 EKNAPLRVKIPEMLQAEIDLRLRNNEDPRGVLCEAQEAVMPEIQEQIQDYRSKRTLGLGSLYGEN 145
RGS-like pfam09128
Regulator of G protein signalling-like domain; Members of this family adopt a structure ...
 27-206 1.82e-84

Regulator of G protein signalling-like domain; Members of this family adopt a structure consisting of twelve helices that fold into a compact domain that contains the overall structural scaffold observed in other RGS proteins and three additional helical elements that pack closely to it. Helices 1-9 comprise the RGS (pfam00615) fold, in which helices 4-7 form a classic antiparallel bundle adjacent to the other helices. Like other RGS structures, helices 7 and 8 span the length of the folded domain and form essentially one continuous helix with a kink in the middle. Helices 10-12 form an apparently stable C-terminal extension of the structural domain, and although other RGS proteins lack this structure, these elements are intimately associated with the rest of the structural framework by hydrophobic interactions. Members of the family bind to active G-alpha proteins, promoting GTP hydrolysis by the alpha subunit of heterotrimeric G proteins, thereby inactivating the G protein and rapidly switching off G protein-coupled receptor signalling pathways.


Pssm-ID: 462687  Cd Length: 191  Bit Score: 248.18  E-value: 1.82e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826359    27 SDIIFQDLEKLKSRPAHLGVFLRYIFSQADPSPLLFYLCAEVYQQASPKDSRSLGKDIWNIFLEKNAPLRVKIPE*LQAE 106
Cdd:pfam09128   1 QCSCFQSLEQLKSRPAHLAVFLHHVVSQFDPSPLLCYLYADLYQQTNSKETRRVFLDIHNFFLEKNAPLRVPVPESVAAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826359   107 ID---SRLRNSEDARGVLCEAQEAA*PEIQEQIHDYRTKRTLGLGSLYGENDLLDLDGD-----PLRERQVAEKQLAALG 178
Cdd:pfam09128  81 LDrrrPELIPEDLHRRYIQTMQERAVPDIQRQLEDFRQKRSMGLTLAEGELSLLDAERDgdrgtLERERRVAEQILSKIE 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 15826359   179 DIL---SAYAADRSAP*DFALNTY*SHAGIR 206
Cdd:pfam09128 161 EILstsQTFDEERSATIQYVILTYMKHLGVR 191
RGS smart00315
Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins ...
 33-127 2.77e-16

Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.


Pssm-ID: 214613  Cd Length: 118  Bit Score: 71.53  E-value: 2.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826359     33 DLEKLKSRPAHLGVFLRYIFSQADPSPLLFYLCAEVYQQA-SPKDSRSLGKDIWNIFLEKNAPLRVKIPE*LQAEIDSRL 111
Cdd:smart00315   1 SLESLLSDPIGRLLFREFLESEFSEENLEFWLAVEEFKKAeDDEERIAKAREIYDKFLSPNAPKEVNLDSDLREKIEENL 80

                           90
                   ....*....|....*.
gi 15826359    112 RNSEDARGVLCEAQEA 127
Cdd:smart00315  81 ESEEPPPDLFDEAQRE 96
 
Name Accession Description Interval E-value
RGS_PDZRhoGEF cd08753
Regulator of G protein signaling (RGS) domain found in the PDZ-Rho guanine nucleotide exchange ...
 10-154 5.71e-102

Regulator of G protein signaling (RGS) domain found in the PDZ-Rho guanine nucleotide exchange factor (RhoGEF) protein; The RGS domain is an essential part of the PDZ-RhoGEF (PDZ:Postsynaptic density 95, Disk large, Zona occludens-1; RhoGEF: Rho guanine nucleotide exchange factor; alias PRG) protein, a member of RhoGEFs subfamily of the RGS protein family. The RhoGEFs are peripheral membrane proteins that regulate essential cellular processes, including cell shape, cell migration, and cell cycle progression, as well as gene transcription by linking signals from heterotrimeric G-alpha12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. RhoGEFs subfamily includes leukemia-associated RhoGEF protein (LARG), p115RhoGEF, PDZ-RhoGEF and its rat specific splice variant GTRAP48. The RGS domain of RhoGEFs has very little sequence similarity with the canonical RGS domain of the RGS proteins and is often refered to as RH (RGS Homology) domain. In contrast to p115RhoGEF and LARG, PDZ-RhoGEF cannot serve as a GTPase-activating protein (GAP), due to the mutation of sites in the RGS domain region that are crucial for GAP activity. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


Pssm-ID: 188707  Cd Length: 145  Bit Score: 291.00  E-value: 5.71e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826359  10 LIIGPEEDYDPGYFNNESDIIFQDLEKLKSRPAHLGVFLRYIFSQADPSPLLFYLCAEVYQQASPKDSRSLGKDIWNIFL 89
Cdd:cd08753   1 LIIGPEEDYDPGYFNNESDIIFQDLEKLKSRPAHLVVFLRYIFSQADPGPLLFYLCSEVYQQTSPKDSRSLGKDIWNIFL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15826359  90 EKNAPLRVKIPE*LQAEIDSRLRNSEDARGVLCEAQEAA*PEIQEQIHDYRTKRTLGLGSLYGEN 154
Cdd:cd08753  81 EKNAPLRVKIPEMLQAEIDLRLRNNEDPRGVLCEAQEAVMPEIQEQIQDYRSKRTLGLGSLYGEN 145
RGS-like pfam09128
Regulator of G protein signalling-like domain; Members of this family adopt a structure ...
 27-206 1.82e-84

Regulator of G protein signalling-like domain; Members of this family adopt a structure consisting of twelve helices that fold into a compact domain that contains the overall structural scaffold observed in other RGS proteins and three additional helical elements that pack closely to it. Helices 1-9 comprise the RGS (pfam00615) fold, in which helices 4-7 form a classic antiparallel bundle adjacent to the other helices. Like other RGS structures, helices 7 and 8 span the length of the folded domain and form essentially one continuous helix with a kink in the middle. Helices 10-12 form an apparently stable C-terminal extension of the structural domain, and although other RGS proteins lack this structure, these elements are intimately associated with the rest of the structural framework by hydrophobic interactions. Members of the family bind to active G-alpha proteins, promoting GTP hydrolysis by the alpha subunit of heterotrimeric G proteins, thereby inactivating the G protein and rapidly switching off G protein-coupled receptor signalling pathways.


Pssm-ID: 462687  Cd Length: 191  Bit Score: 248.18  E-value: 1.82e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826359    27 SDIIFQDLEKLKSRPAHLGVFLRYIFSQADPSPLLFYLCAEVYQQASPKDSRSLGKDIWNIFLEKNAPLRVKIPE*LQAE 106
Cdd:pfam09128   1 QCSCFQSLEQLKSRPAHLAVFLHHVVSQFDPSPLLCYLYADLYQQTNSKETRRVFLDIHNFFLEKNAPLRVPVPESVAAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826359   107 ID---SRLRNSEDARGVLCEAQEAA*PEIQEQIHDYRTKRTLGLGSLYGENDLLDLDGD-----PLRERQVAEKQLAALG 178
Cdd:pfam09128  81 LDrrrPELIPEDLHRRYIQTMQERAVPDIQRQLEDFRQKRSMGLTLAEGELSLLDAERDgdrgtLERERRVAEQILSKIE 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 15826359   179 DIL---SAYAADRSAP*DFALNTY*SHAGIR 206
Cdd:pfam09128 161 EILstsQTFDEERSATIQYVILTYMKHLGVR 191
RGS_RhoGEF-like cd08736
Regulator of G protein signaling (RGS) domain found in the Rho guanine nucleotide exchange ...
 38-154 2.16e-61

Regulator of G protein signaling (RGS) domain found in the Rho guanine nucleotide exchange factor (RhoGEF) protein; The RGS domain found in the Rho guanine nucleotide exchange factor (RhoGEF) protein subfamily of the RGS domain containing protein family, which is a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RhoGEFs link signals from heterotrimeric G-alpha12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. The RGS domain of the RhoGEFs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. The RGS-GEFs subfamily includes the leukemia-associated RhoGEF (LARG), p115RhoGEF, and PDZ-RhoGEF. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


Pssm-ID: 188690  Cd Length: 120  Bit Score: 187.07  E-value: 2.16e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826359  38 KSRPAHLGVFLRYIFSQADPSPLLFYLCAEVYQQASPKDSRSLGKDIWNIFLEKNAPLRVKIPE*LQAEIDSRLRNS--- 114
Cdd:cd08736   1 KSRPAHLAVFLHYVLSQFDPSPLLFYLITDLYKQGNPKDMRKWAYEIYSTFLEKNAPLKVKVPESLAAEIDKRLPNLide 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15826359 115 EDARGVLCEAQEAA*PEIQEQIHDYRTKRTLGLGSLYGEN 154
Cdd:cd08736  81 EDLRRVFQEAQERAMPEIQEQLEDFRQKRTMGLGSLEGEL 120
RGS_LARG cd08754
Regulator of G protein signaling (RGS) domain found in the leukemia-associated Rho guanine ...
 11-210 2.45e-34

Regulator of G protein signaling (RGS) domain found in the leukemia-associated Rho guanine nucleotide exchange factor (RhoGEF) protein (LARG); The RGS domain is an essential part of the leukemia-associated RhoGEF protein (LARG), a member of the RhoGEF (Rho guanine nucleotide exchange factor) subfamily of the RGS protein family. The RhoGEFs are peripheral membrane proteins that regulate essential cellular processes, including cell shape, cell migration, cell cycle progression of cells, and gene transcription by linking signals from heterotrimeric G-alpha12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. The RhoGEF subfamily includes p115RhoGEF, LARG, PDZ-RhoGEF, and its rat specific splice variant GTRAP48. The RGS domain of RhoGEFs has very little sequence similarity with the canonical RGS domain of the RGS proteins and is often refered to as RH (RGS Homology) domain. In addition to being a G-alpha13 effector, the LARG protein also functions as a GTPase-activating protein (GAP) for G-alpha13. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


Pssm-ID: 188708  Cd Length: 222  Bit Score: 121.64  E-value: 2.45e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826359  11 IIGPEEDYdpgyFNNESDII------FQDLEKLKSRPAHLGVFLRYIFSQADPSPLLFYLCAEVYQQASPKDSRSLGKDI 84
Cdd:cd08754   2 IIGAEDDD----FPTESEQIngqcscFQNIELLKSRPAHLAVFLHHVVSQFDPAALLCYLYADLYKQTNSKETRRVFLEF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826359  85 WNIFLEKNAPLRVKIPE*LQAEIDSR---LRNSEDARGVLCEAQEAA*PEIQEQIHDYRTKRTLGLGSLYGENDLLDLDG 161
Cdd:cd08754  78 NQFFLDRAANLKVPVPDEVSLDLEKRrpeLIPEELHRHYIQTMQERVSPEVQRNLEDFRQKRSMGLTLAEGELTKLDAER 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15826359 162 DPLR-----ERQVAEKQLAALGDIL---SAYAADRSAP*DFALNTY*SHAGIRLREA 210
Cdd:cd08754 158 FRDRntiekERACAEQIVAKIEEVLmtsQTPEEDKSSTIQYVILTYMKHLGVKVKEP 214
RGS_GEF_like cd08756
Regulator of G protein signaling (RGS) domain found in the Rho guanine nucleotide exchange ...
 38-154 6.18e-31

Regulator of G protein signaling (RGS) domain found in the Rho guanine nucleotide exchange factor (RhoGEF) protein; The RGS domain found in the Rho guanine nucleotide exchange factor (RhoGEF) protein subfamily of the RGS domain containing protein family, which is a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). The RhoGEFs are peripheral membrane proteins that regulate essential cellular processes, including cell shape, cell migration and cell cycle progression as well as gene transcription by linking signals from heterotrimeric G-alpha12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. The RhoGEF subfamily includes the leukemia-associated RhoGEF protein (LARG), p115RhoGEF, PDZ-RhoGEF, and its rat specific splice variant GTRAP48. The RGS domain of RhoGEFs has very little sequence similarity with the canonical RGS domain of the RGS proteins and is often refered to as RH (RGS Homology) domain. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


Pssm-ID: 188710  Cd Length: 122  Bit Score: 109.79  E-value: 6.18e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826359  38 KSRPAHLGVFLRYIFSQADPSPLLFYLCAEVYQQASPKDSRSLGKDIWNIFLEKNAPL-RVKIPE*LQAEIDSRLRNS-- 114
Cdd:cd08756   1 KTHPAHLAVFLNYLLSNSDPSSLFFYLITDLYKSGNIKDMRKWAYEIFSTFLVPNAPLlWPNIDESLIQEIDKILQNEqd 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15826359 115 --EDARGVLCEAQEAA*PEIQEQIHDYRTKRTLGLGSLYGEN 154
Cdd:cd08756  81 deEILRRVFLKAREKARDEINDQLADFRQKRTLGLGSIFGPN 122
RGS_p115RhoGEF cd08755
Regulator of G protein signaling (RGS) domain found in the Rho guanine nucleotide exchange ...
 37-210 1.17e-26

Regulator of G protein signaling (RGS) domain found in the Rho guanine nucleotide exchange factor (GEF), p115 RhoGEF; The RGS (Regulator of G-protein Signaling) domain is an essential part of the p115RhoGEF protein, a member of the RhoGEF (Rho guanine nucleotide exchange factor) subfamily of the RGS protein family. The RhoGEFs are peripheral membrane proteins that regulate essential cellular processes, including cell shape, cell migration, cell cycle progression of cells, and gene transcription by linking signals from heterotrimeric G-alpha12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. The RhoGEF subfamily includes p115RhoGEF, LARG, PDZ-RhoGEF and its rat specific splice variant GTRAP48. The RGS domain of RhoGEFs has very little sequence similarity with the canonical RGS domain of the RGS proteins and is often refered to as RH (RGS Homology) domain. In addition to being a G-alpha13/12 effector, the p115RhoGEF protein also functions as a GTPase-activating protein (GAP) for G-alpha13. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


Pssm-ID: 188709  Cd Length: 193  Bit Score: 100.74  E-value: 1.17e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826359  37 LKSRPAHLGVFLRYIFSQADPSPLLFYLCAEVYQQASPKDSRSLGKDIWNIFLEKNAPLRVKIPE*LQAEIDsRLR---- 112
Cdd:cd08755   1 VKSRPAHLMVFLQHVMLQFDPAPLLCYLHADMLKNLNTKETKKHFGDFYNTFLEKGAVLKVSVPSNVAFELD-RTRpeli 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826359 113 NSEDARGVLCEAQEAA*PEIQEQIHDYRTKRTLGLGSLYGE------NDLLDLDGDPLRERQVAEKQLAALGDILSAYAA 186
Cdd:cd08755  80 NEEQQRRYVNEIQFAQSPAILRQLEDFRQKRMMGMTPNERElndlesHRPTDRIPMEAKEKAVAESLLEKLVEMNPTIVP 159

                       170       180
                ....*....|....*....|....*.
gi 15826359 187 D--RSAP*DFALNTY*SHAGIRLREA 210
Cdd:cd08755 160 DeeKSNAIFGAIAYYMKHLGVKTKAF 185
RGS smart00315
Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins ...
 33-127 2.77e-16

Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.


Pssm-ID: 214613  Cd Length: 118  Bit Score: 71.53  E-value: 2.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826359     33 DLEKLKSRPAHLGVFLRYIFSQADPSPLLFYLCAEVYQQA-SPKDSRSLGKDIWNIFLEKNAPLRVKIPE*LQAEIDSRL 111
Cdd:smart00315   1 SLESLLSDPIGRLLFREFLESEFSEENLEFWLAVEEFKKAeDDEERIAKAREIYDKFLSPNAPKEVNLDSDLREKIEENL 80

                           90
                   ....*....|....*.
gi 15826359    112 RNSEDARGVLCEAQEA 127
Cdd:smart00315  81 ESEEPPPDLFDEAQRE 96
RGS cd07440
Regulator of G protein signaling (RGS) domain superfamily; The RGS domain is an essential part ...
 38-134 2.45e-14

Regulator of G protein signaling (RGS) domain superfamily; The RGS domain is an essential part of the Regulator of G-protein Signaling (RGS) protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. While inactive, G-alpha-subunits bind GDP, which is released and replaced by GTP upon agonist activation. GTP binding leads to dissociation of the alpha-subunit and the beta-gamma-dimer, allowing them to interact with effectors molecules and propagate signaling cascades associated with cellular growth, survival, migration, and invasion. Deactivation of the G-protein signaling controlled by the RGS domain accelerates GTPase activity of the alpha subunit by hydrolysis of GTP to GDP, which results in the reassociation of the alpha-subunit with the beta-gamma-dimer and thereby inhibition of downstream activity. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS proteins are also involved in apoptosis and cell proliferation, as well as modulation of cardiac development. Several RGS proteins can fine-tune immune responses, while others play important roles in neuronal signals modulation. Some RGS proteins are principal elements needed for proper vision.


Pssm-ID: 188659 [Multi-domain]  Cd Length: 113  Bit Score: 66.26  E-value: 2.45e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826359  38 KSRPAHLGVFLRYIFSQADPSPLLFYLCAEVYQQASPKDS--RSLGKDIWNIFLEKNAPLRVKIPE*LQAEIDSRLRNSE 115
Cdd:cd07440   1 LRDPYGLEYFRQFLKSEHCEENLEFWLAVEKFKKTTSSDEelKSKAKEIYDKYISKDAPKEINIPESIREEIEENLEEPY 80

                        90
                ....*....|....*....
gi 15826359 116 DARGVLCEAQEAA*PEIQE 134
Cdd:cd07440  81 PDPDCFDEAQEHILNLLEK 99
RGS pfam00615
Regulator of G protein signaling domain; RGS family members are GTPase-activating proteins for ...
 33-127 1.88e-05

Regulator of G protein signaling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.


Pssm-ID: 459870  Cd Length: 117  Bit Score: 42.60  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826359    33 DLEKLKSRPAHLGVFLRYIFSQADPSPLLFYLCAEVYQQASPKDSR-SLGKDIWNIFLEKNAPLRVKIPE*LQAEIDSRL 111
Cdd:pfam00615   1 SFDSLLEDQPGRRLFRQFLESEFSEENLEFWLACEEFKKADPDEERlKKAKEIYNEFLAPGSPKEINLDSDLREEIRENL 80

                          90
                  ....*....|....*.
gi 15826359   112 RNSEDaRGVLCEAQEA 127
Cdd:pfam00615  81 EKEPT-RDLFDEAQAE 95
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH