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Conserved domains on  [gi|568964662|ref|XP_006512502|]
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pleckstrin homology domain-containing family G member 1 isoform X1 [Mus musculus]

Protein Classification

pleckstrin homology domain-containing family G protein( domain architecture ID 10457355)

pleckstrin homology (PH) domain-containing family G protein contains PH and RhoGEF domains and may function as a guanine nucleotide exchange factor; similar to Homo sapiens pleckstrin homology domain-containing family G members 1/2/3 (PLEKHG1/2/3) that are involved in the regulation of Rho protein signal transduction

Gene Ontology:  GO:0005085|GO:0051056
PubMed:  11738596

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PH_PLEKHG1_G2_G3 cd13243
Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) ...
369-514 3.78e-72

Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) domain; PLEKHG1 (also called ARHGEF41), PLEKHG2 (also called ARHGEF42 or CLG/common-site lymphoma/leukemia guanine nucleotide exchange factor2), and PLEKHG3 (also called ARHGEF43) have RhoGEF DH/double-homology domains in tandem with a PH domain which is involved in phospholipid binding. They function as a guanine nucleotide exchange factor (GEF) and are involved in the regulation of Rho protein signal transduction. Mutations in PLEKHG1 have been associated panic disorder (PD), an anxiety disorder characterized by panic attacks and anticipatory anxiety. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 270063 [Multi-domain]  Cd Length: 147  Bit Score: 237.25  E-value: 3.78e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662  369 YDVVLDAIDTMQRVAWHINDMKRKHEHAVRLQEIQSLLTNWEGPDLTSYGELVLEGTFRIQKAKKERTLFLLDQLLLITK 448
Cdd:cd13243     1 RSVVEEALDTMTQVAWHINDMKRKHEHAVRVQEIQSLLDGWEGPELTTYGDLVLEGTFRMAGAKNERLLFLFDKMLLITK 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568964662  449 KRDD-TFTYKAHILCGNLMLVEVIPKEPLSFSVFHYKNPKLQHTVQAKSQQDKRLWVLHLKRLILEN 514
Cdd:cd13243    81 KREDgILQYKTHIMCSNLMLSESIPKEPLSFQVLPFDNPKLQYTLQAKNQEQKRLWTQEIKRLILEN 147
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
213-387 3.33e-52

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


:

Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 181.34  E-value: 3.33e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662   213 VVQEILETERTYVQDLKSIVEGYLECIRDqtKLPLVTEDRAALFGNIQDIYHFN-SELLQDLENCENDPVAIAECFVSKS 291
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSK--PLSESEEEIKTIFSNIEEIYELHrQLLLEELLKEWISIQRIGDIFLKFA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662   292 EEFHIYTQYCTNYPRSVAVLTECMR-NKILTKFFRERQETLR-HSLPLGSYLLKPVQRILKYHLLLHEIENHLDKATEGY 369
Cdd:pfam00621   79 PGFKVYSTYCSNYPKALKLLKKLLKkNPKFRAFLEELEANPEcRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDHPDY 158
                          170
                   ....*....|....*...
gi 568964662   370 DVVLDAIDTMQRVAWHIN 387
Cdd:pfam00621  159 EDLKKALEAIKEVAKQIN 176
 
Name Accession Description Interval E-value
PH_PLEKHG1_G2_G3 cd13243
Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) ...
369-514 3.78e-72

Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) domain; PLEKHG1 (also called ARHGEF41), PLEKHG2 (also called ARHGEF42 or CLG/common-site lymphoma/leukemia guanine nucleotide exchange factor2), and PLEKHG3 (also called ARHGEF43) have RhoGEF DH/double-homology domains in tandem with a PH domain which is involved in phospholipid binding. They function as a guanine nucleotide exchange factor (GEF) and are involved in the regulation of Rho protein signal transduction. Mutations in PLEKHG1 have been associated panic disorder (PD), an anxiety disorder characterized by panic attacks and anticipatory anxiety. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270063 [Multi-domain]  Cd Length: 147  Bit Score: 237.25  E-value: 3.78e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662  369 YDVVLDAIDTMQRVAWHINDMKRKHEHAVRLQEIQSLLTNWEGPDLTSYGELVLEGTFRIQKAKKERTLFLLDQLLLITK 448
Cdd:cd13243     1 RSVVEEALDTMTQVAWHINDMKRKHEHAVRVQEIQSLLDGWEGPELTTYGDLVLEGTFRMAGAKNERLLFLFDKMLLITK 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568964662  449 KRDD-TFTYKAHILCGNLMLVEVIPKEPLSFSVFHYKNPKLQHTVQAKSQQDKRLWVLHLKRLILEN 514
Cdd:cd13243    81 KREDgILQYKTHIMCSNLMLSESIPKEPLSFQVLPFDNPKLQYTLQAKNQEQKRLWTQEIKRLILEN 147
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
213-387 3.33e-52

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 181.34  E-value: 3.33e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662   213 VVQEILETERTYVQDLKSIVEGYLECIRDqtKLPLVTEDRAALFGNIQDIYHFN-SELLQDLENCENDPVAIAECFVSKS 291
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSK--PLSESEEEIKTIFSNIEEIYELHrQLLLEELLKEWISIQRIGDIFLKFA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662   292 EEFHIYTQYCTNYPRSVAVLTECMR-NKILTKFFRERQETLR-HSLPLGSYLLKPVQRILKYHLLLHEIENHLDKATEGY 369
Cdd:pfam00621   79 PGFKVYSTYCSNYPKALKLLKKLLKkNPKFRAFLEELEANPEcRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDHPDY 158
                          170
                   ....*....|....*...
gi 568964662   370 DVVLDAIDTMQRVAWHIN 387
Cdd:pfam00621  159 EDLKKALEAIKEVAKQIN 176
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
211-387 3.91e-50

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 175.56  E-value: 3.91e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662  211 DRVVQEILETERTYVQDLKSIVEGYLECIrDQTKLPLVTEDRAALFGNIQDIYHFNSELLQDLENC----ENDPVAIAEC 286
Cdd:cd00160     2 QEVIKELLQTERNYVRDLKLLVEVFLKPL-DKELLPLSPEEVELLFGNIEEIYEFHRIFLKSLEERveewDKSGPRIGDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662  287 FVSKSEEFHIYTQYCTNYPRSVAVLTECMRNKilTKF--FRERQETLRHSLPLGSYLLKPVQRILKYHLLLHEIENHLDK 364
Cdd:cd00160    81 FLKLAPFFKIYSEYCSNHPDALELLKKLKKFN--KFFqeFLEKAESECGRLKLESLLLKPVQRLTKYPLLLKELLKHTPD 158
                         170       180
                  ....*....|....*....|...
gi 568964662  365 ATEGYDVVLDAIDTMQRVAWHIN 387
Cdd:cd00160   159 GHEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
213-388 2.47e-48

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 170.56  E-value: 2.47e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662    213 VVQEILETERTYVQDLKSIVEGYLECIRDQTKLpLVTEDRAALFGNIQDIYHFNSELLQDLENC----ENDPVAIAECFV 288
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKL-LSPNELETLFGNIEEIYEFHRDFLDELEERieewDDSVERIGDVFL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662    289 SKSEEFHIYTQYCTNYPRSVAVLTECMRNKILTKFFRERQETLRH-SLPLGSYLLKPVQRILKYHLLLHEIENHLDKATE 367
Cdd:smart00325   80 KLEEFFKIYSEYCSNHPDALELLKKLKKNPRFQKFLKEIESSPQCrRLTLESLLLKPVQRLTKYPLLLKELLKHTPEDHE 159
                           170       180
                    ....*....|....*....|.
gi 568964662    368 GYDVVLDAIDTMQRVAWHIND 388
Cdd:smart00325  160 DREDLKKALKAIKELANQVNE 180
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
172-377 2.64e-03

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 42.57  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662  172 PQNMNGVSEKQ--PRTPWrmdTSGTPQTTADSATSPKLLYVDrVVQEILETERTYVQDLksivegylECIRDQTKLPLVT 249
Cdd:COG5422   449 KRNSSLALDKFdeEKNLW---TLSVPKEVWESLPKQEIKRQE-AIYEVIYTERDFVKDL--------EYLRDTWIKPLEE 516
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662  250 EDRAA----------LFGNIQDIYHFNSELLQDLENCEN-DPVA--IAECFVSKSEEFHIYTQYCTNYPRSVAVLTEcmR 316
Cdd:COG5422   517 SNIIPenarrnfikhVFANINEIYAVNSKLLKALTNRQClSPIVngIADIFLDYVPKFEPFIKYGASQPYAKYEFER--E 594
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568964662  317 NKILTKFFRERQETLRHSLP----LGSYLLKPVQRILKYHLLLHEIENHLDKATEGYDVVLDAID 377
Cdd:COG5422   595 KSVNPNFARFDHEVERLDESrkleLDGYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVID 659
 
Name Accession Description Interval E-value
PH_PLEKHG1_G2_G3 cd13243
Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) ...
369-514 3.78e-72

Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) domain; PLEKHG1 (also called ARHGEF41), PLEKHG2 (also called ARHGEF42 or CLG/common-site lymphoma/leukemia guanine nucleotide exchange factor2), and PLEKHG3 (also called ARHGEF43) have RhoGEF DH/double-homology domains in tandem with a PH domain which is involved in phospholipid binding. They function as a guanine nucleotide exchange factor (GEF) and are involved in the regulation of Rho protein signal transduction. Mutations in PLEKHG1 have been associated panic disorder (PD), an anxiety disorder characterized by panic attacks and anticipatory anxiety. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270063 [Multi-domain]  Cd Length: 147  Bit Score: 237.25  E-value: 3.78e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662  369 YDVVLDAIDTMQRVAWHINDMKRKHEHAVRLQEIQSLLTNWEGPDLTSYGELVLEGTFRIQKAKKERTLFLLDQLLLITK 448
Cdd:cd13243     1 RSVVEEALDTMTQVAWHINDMKRKHEHAVRVQEIQSLLDGWEGPELTTYGDLVLEGTFRMAGAKNERLLFLFDKMLLITK 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568964662  449 KRDD-TFTYKAHILCGNLMLVEVIPKEPLSFSVFHYKNPKLQHTVQAKSQQDKRLWVLHLKRLILEN 514
Cdd:cd13243    81 KREDgILQYKTHIMCSNLMLSESIPKEPLSFQVLPFDNPKLQYTLQAKNQEQKRLWTQEIKRLILEN 147
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
213-387 3.33e-52

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 181.34  E-value: 3.33e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662   213 VVQEILETERTYVQDLKSIVEGYLECIRDqtKLPLVTEDRAALFGNIQDIYHFN-SELLQDLENCENDPVAIAECFVSKS 291
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSK--PLSESEEEIKTIFSNIEEIYELHrQLLLEELLKEWISIQRIGDIFLKFA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662   292 EEFHIYTQYCTNYPRSVAVLTECMR-NKILTKFFRERQETLR-HSLPLGSYLLKPVQRILKYHLLLHEIENHLDKATEGY 369
Cdd:pfam00621   79 PGFKVYSTYCSNYPKALKLLKKLLKkNPKFRAFLEELEANPEcRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDHPDY 158
                          170
                   ....*....|....*...
gi 568964662   370 DVVLDAIDTMQRVAWHIN 387
Cdd:pfam00621  159 EDLKKALEAIKEVAKQIN 176
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
211-387 3.91e-50

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 175.56  E-value: 3.91e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662  211 DRVVQEILETERTYVQDLKSIVEGYLECIrDQTKLPLVTEDRAALFGNIQDIYHFNSELLQDLENC----ENDPVAIAEC 286
Cdd:cd00160     2 QEVIKELLQTERNYVRDLKLLVEVFLKPL-DKELLPLSPEEVELLFGNIEEIYEFHRIFLKSLEERveewDKSGPRIGDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662  287 FVSKSEEFHIYTQYCTNYPRSVAVLTECMRNKilTKF--FRERQETLRHSLPLGSYLLKPVQRILKYHLLLHEIENHLDK 364
Cdd:cd00160    81 FLKLAPFFKIYSEYCSNHPDALELLKKLKKFN--KFFqeFLEKAESECGRLKLESLLLKPVQRLTKYPLLLKELLKHTPD 158
                         170       180
                  ....*....|....*....|...
gi 568964662  365 ATEGYDVVLDAIDTMQRVAWHIN 387
Cdd:cd00160   159 GHEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
213-388 2.47e-48

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 170.56  E-value: 2.47e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662    213 VVQEILETERTYVQDLKSIVEGYLECIRDQTKLpLVTEDRAALFGNIQDIYHFNSELLQDLENC----ENDPVAIAECFV 288
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKL-LSPNELETLFGNIEEIYEFHRDFLDELEERieewDDSVERIGDVFL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662    289 SKSEEFHIYTQYCTNYPRSVAVLTECMRNKILTKFFRERQETLRH-SLPLGSYLLKPVQRILKYHLLLHEIENHLDKATE 367
Cdd:smart00325   80 KLEEFFKIYSEYCSNHPDALELLKKLKKNPRFQKFLKEIESSPQCrRLTLESLLLKPVQRLTKYPLLLKELLKHTPEDHE 159
                           170       180
                    ....*....|....*....|.
gi 568964662    368 GYDVVLDAIDTMQRVAWHIND 388
Cdd:smart00325  160 DREDLKKALKAIKELANQVNE 180
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
453-514 3.29e-04

p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor p63RhoGEF is an effector of the heterotrimeric G protein, Galphaq and linking Galphaq-coupled receptors (GPCRs) to the activation of RhoA. The Dbl(DH) and PH domains of p63RhoGEF interact with the effector-binding site and the C-terminal region of Galphaq and appear to relieve autoinhibition of the catalytic DH domain by the PH domain. Trio, Duet, and p63RhoGEF are shown to constitute a family of Galphaq effectors that appear to activate RhoA both in vitro and in intact cells. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270061  Cd Length: 140  Bit Score: 42.25  E-value: 3.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568964662  453 TFTYKAHILCGNLMLVEVIPKEPLSFsVFHYKNPKLQH---TVQAKSQQDKRLWVLHLKRlILEN 514
Cdd:cd13241    64 GYIYKNHIKVNKMSLEENVDGDPLRF-ALKSRDPNNPSetfILQAASPEVRQEWVDTINQ-ILDT 126
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
172-377 2.64e-03

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 42.57  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662  172 PQNMNGVSEKQ--PRTPWrmdTSGTPQTTADSATSPKLLYVDrVVQEILETERTYVQDLksivegylECIRDQTKLPLVT 249
Cdd:COG5422   449 KRNSSLALDKFdeEKNLW---TLSVPKEVWESLPKQEIKRQE-AIYEVIYTERDFVKDL--------EYLRDTWIKPLEE 516
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964662  250 EDRAA----------LFGNIQDIYHFNSELLQDLENCEN-DPVA--IAECFVSKSEEFHIYTQYCTNYPRSVAVLTEcmR 316
Cdd:COG5422   517 SNIIPenarrnfikhVFANINEIYAVNSKLLKALTNRQClSPIVngIADIFLDYVPKFEPFIKYGASQPYAKYEFER--E 594
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568964662  317 NKILTKFFRERQETLRHSLP----LGSYLLKPVQRILKYHLLLHEIENHLDKATEGYDVVLDAID 377
Cdd:COG5422   595 KSVNPNFARFDHEVERLDESrkleLDGYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVID 659
 
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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