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Conserved domains on  [gi|568998006|ref|XP_006523294|]
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rho guanine nucleotide exchange factor TIAM2 isoform X5 [Mus musculus]

Protein Classification

TIAM family RhoGEF and PH domain-containing protein( domain architecture ID 11264311)

TIAM (T-lymphoma invasion and metastasis-inducing protein) family RhoGEF (rho guanine nucleotide exchange factor) and PH (pleckstrin homology) domain-containing protein similar to RhoGEF and PH domain regions of Homo sapiens Rho guanine nucleotide exchange factor TIAM1/TIAM2 that modulates the activity of RHO-like proteins and connects extracellular signals to cytoskeletal activities

CATH:  2.30.29.30
Gene Ontology:  GO:0005085|GO:0051056|GO:0005515
SCOP:  3000134

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PH2_Tiam1_2 cd01255
T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, C-terminal domain; ...
242-414 4.25e-99

T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, C-terminal domain; Tiam1 activates Rac GTPases to induce membrane ruffling and cell motility while Tiam2 (also called STEF (SIF (still life) and Tiam1 like-exchange factor) contributes to neurite growth. Tiam1/2 are Dbl-family of GEFs that possess a Dbl(DH) domain with a PH domain in tandem. DH-PH domain catalyzes the GDP/GTP exchange reaction in the GTPase cycle and facillitating the switch between inactive GDP-bound and active GTP-bound states. The DH domain of Tiam1 interacts with Switch regions 1 and 2 of Rac1 which blocks magnesium binding and GDP is released. Tiam1/2 possess two PH domains, which are often referred to as PHn and PHc domains. The DH-PH tandem domain is made up of the PHc domain while the PHn is part of a novel N-terminal PHCCEx domain which is made up of the PHn domain, a coiled coil region(CC), and an extra region (Ex). PHCCEx mediates binding to plasma membranes and signalling proteins in the activation of Rac GTPases. The PH domain resembles the beta-spectrin PH domain, suggesting non-canonical phosphatidylinositol binding. CC and Ex form a positively charged surface for protein binding. There are 2 motifs in Tiam1/2-interacting proteins that bind to the PHCCEx domain: Motif-I in CD44, ephrinBs, and the NMDA receptor and Motif-II in Par3 and JIP2. 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: 269957  Cd Length: 172  Bit Score: 300.07  E-value: 4.25e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006 242 QKIYEDYGMVFDQLVAEQSGTEKEVTELSMGELLMHSTVSWLNPFLSLGKARKDIELTVFVFKRAVILVYKENCKLKKKL 321
Cdd:cd01255    1 QKIHEEYGAVFDQLIREQSGTKKEVADLSMGDLLLYGTVEWLNPPSSLGKVKKEPELAVFVFKTAVVLVCKERSKQKKKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006 322 PSNSRPAHnSADLDPFKFRWLIPISALQVRLGNTAGTENNSTWELIHTKSEIEGRPETIFQLCCSDSENKTSIVKVIRSI 401
Cdd:cd01255   81 MGSHRKSS-YEERDPFRFRHLIPVSALQVRNSNTADTESRCLWELIHTKSELEGRPEKVFQLCCSTPEFKNAFLKVIRSI 159
                        170
                 ....*....|...
gi 568998006 402 LRENFRRHIKCEL 414
Cdd:cd01255  160 LREKVRRQSSKTE 172
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
51-240 3.34e-49

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: 169.40  E-value: 3.34e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006    51 VIQELVDTEKSYVKDLSCLFELYLEPLQNE-TFLTQDEMESLFGSLPEMLEFQKVFLETLEDAISASSDFSvletpsqfr 129
Cdd:smart00325   1 VLKELLQTERNYVRDLKLLVEVFLKPLKKElKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSV--------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006   130 kllFSLGGSFLYYADHFKLYSGFCANHIKVQRVLERAKTDKAFKAFLDARNPTKQHSS-TLESYLIKPVQRVLKYPLLLK 208
Cdd:smart00325  72 ---ERIGDVFLKLEEFFKIYSEYCSNHPDALELLKKLKKNPRFQKFLKEIESSPQCRRlTLESLLLKPVQRLTKYPLLLK 148
                          170       180       190
                   ....*....|....*....|....*....|..
gi 568998006   209 ELVSLTDHESEEHYHLTEALKAMEKVASHINE 240
Cdd:smart00325 149 ELLKHTPEDHEDREDLKKALKAIKELANQVNE 180
 
Name Accession Description Interval E-value
PH2_Tiam1_2 cd01255
T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, C-terminal domain; ...
242-414 4.25e-99

T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, C-terminal domain; Tiam1 activates Rac GTPases to induce membrane ruffling and cell motility while Tiam2 (also called STEF (SIF (still life) and Tiam1 like-exchange factor) contributes to neurite growth. Tiam1/2 are Dbl-family of GEFs that possess a Dbl(DH) domain with a PH domain in tandem. DH-PH domain catalyzes the GDP/GTP exchange reaction in the GTPase cycle and facillitating the switch between inactive GDP-bound and active GTP-bound states. The DH domain of Tiam1 interacts with Switch regions 1 and 2 of Rac1 which blocks magnesium binding and GDP is released. Tiam1/2 possess two PH domains, which are often referred to as PHn and PHc domains. The DH-PH tandem domain is made up of the PHc domain while the PHn is part of a novel N-terminal PHCCEx domain which is made up of the PHn domain, a coiled coil region(CC), and an extra region (Ex). PHCCEx mediates binding to plasma membranes and signalling proteins in the activation of Rac GTPases. The PH domain resembles the beta-spectrin PH domain, suggesting non-canonical phosphatidylinositol binding. CC and Ex form a positively charged surface for protein binding. There are 2 motifs in Tiam1/2-interacting proteins that bind to the PHCCEx domain: Motif-I in CD44, ephrinBs, and the NMDA receptor and Motif-II in Par3 and JIP2. 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: 269957  Cd Length: 172  Bit Score: 300.07  E-value: 4.25e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006 242 QKIYEDYGMVFDQLVAEQSGTEKEVTELSMGELLMHSTVSWLNPFLSLGKARKDIELTVFVFKRAVILVYKENCKLKKKL 321
Cdd:cd01255    1 QKIHEEYGAVFDQLIREQSGTKKEVADLSMGDLLLYGTVEWLNPPSSLGKVKKEPELAVFVFKTAVVLVCKERSKQKKKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006 322 PSNSRPAHnSADLDPFKFRWLIPISALQVRLGNTAGTENNSTWELIHTKSEIEGRPETIFQLCCSDSENKTSIVKVIRSI 401
Cdd:cd01255   81 MGSHRKSS-YEERDPFRFRHLIPVSALQVRNSNTADTESRCLWELIHTKSELEGRPEKVFQLCCSTPEFKNAFLKVIRSI 159
                        170
                 ....*....|...
gi 568998006 402 LRENFRRHIKCEL 414
Cdd:cd01255  160 LREKVRRQSSKTE 172
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
51-240 3.34e-49

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: 169.40  E-value: 3.34e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006    51 VIQELVDTEKSYVKDLSCLFELYLEPLQNE-TFLTQDEMESLFGSLPEMLEFQKVFLETLEDAISASSDFSvletpsqfr 129
Cdd:smart00325   1 VLKELLQTERNYVRDLKLLVEVFLKPLKKElKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSV--------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006   130 kllFSLGGSFLYYADHFKLYSGFCANHIKVQRVLERAKTDKAFKAFLDARNPTKQHSS-TLESYLIKPVQRVLKYPLLLK 208
Cdd:smart00325  72 ---ERIGDVFLKLEEFFKIYSEYCSNHPDALELLKKLKKNPRFQKFLKEIESSPQCRRlTLESLLLKPVQRLTKYPLLLK 148
                          170       180       190
                   ....*....|....*....|....*....|..
gi 568998006   209 ELVSLTDHESEEHYHLTEALKAMEKVASHINE 240
Cdd:smart00325 149 ELLKHTPEDHEDREDLKKALKAIKELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
48-239 6.96e-48

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: 165.93  E-value: 6.96e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006  48 LRKVIQELVDTEKSYVKDLSCLFELYLEPLQNE-TFLTQDEMESLFGSLPEMLEFQKVFLETLEDAISASsdfsvletps 126
Cdd:cd00160    1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKElLPLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEW---------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006 127 qfRKLLFSLGGSFLYYADHFKLYSGFCANHIKVQRVLE-RAKTDKAFKAFLDARNpTKQHSSTLESYLIKPVQRVLKYPL 205
Cdd:cd00160   71 --DKSGPRIGDVFLKLAPFFKIYSEYCSNHPDALELLKkLKKFNKFFQEFLEKAE-SECGRLKLESLLLKPVQRLTKYPL 147
                        170       180       190
                 ....*....|....*....|....*....|....
gi 568998006 206 LLKELVSLTDHESEEHYHLTEALKAMEKVASHIN 239
Cdd:cd00160  148 LLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
51-239 6.89e-45

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: 157.85  E-value: 6.89e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006   51 VIQELVDTEKSYVKDLSCLFELYLEPLQNETFLTQDEMESLFGSLPEMLEFQKVFLetledaisassdfsvLETPSQFRK 130
Cdd:pfam00621   1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHRQLL---------------LEELLKEWI 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006  131 LLFSLGGSFLYYADHFKLYSGFCANHIKVQRVLERAK-TDKAFKAFLDARNPTKQHSS-TLESYLIKPVQRVLKYPLLLK 208
Cdd:pfam00621  66 SIQRIGDIFLKFAPGFKVYSTYCSNYPKALKLLKKLLkKNPKFRAFLEELEANPECRGlDLNSFLIKPVQRIPRYPLLLK 145
                         170       180       190
                  ....*....|....*....|....*....|.
gi 568998006  209 ELVSLTDHESEEHYHLTEALKAMEKVASHIN 239
Cdd:pfam00621 146 ELLKHTPPDHPDYEDLKKALEAIKEVAKQIN 176
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
35-252 7.75e-06

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


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 49.12  E-value: 7.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006   35 PRPLARHLSDADRLRK-VIQELVDTEKSYVKDLSCLFELYLEPLQNETFLTQDEMEslfgslpemlEFQKVFLETLEDAI 113
Cdd:COG5422   471 PKEVWESLPKQEIKRQeAIYEVIYTERDFVKDLEYLRDTWIKPLEESNIIPENARR----------NFIKHVFANINEIY 540
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006  114 SASSDFSVLETPSQ-FRKLLFSLGGSFLYYADHFKLYSGFCANHIKVQRVLERAK-TDKAFKAFLD----ARNPTKQHss 187
Cdd:COG5422   541 AVNSKLLKALTNRQcLSPIVNGIADIFLDYVPKFEPFIKYGASQPYAKYEFEREKsVNPNFARFDHeverLDESRKLE-- 618
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568998006  188 tLESYLIKPVQRVLKYPLLLKELVSLTDHESEEHYHLTEALKAMEKVASHINEMQKIYEDYGMVF 252
Cdd:COG5422   619 -LDGYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFESGKAENRGDLF 682
 
Name Accession Description Interval E-value
PH2_Tiam1_2 cd01255
T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, C-terminal domain; ...
242-414 4.25e-99

T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, C-terminal domain; Tiam1 activates Rac GTPases to induce membrane ruffling and cell motility while Tiam2 (also called STEF (SIF (still life) and Tiam1 like-exchange factor) contributes to neurite growth. Tiam1/2 are Dbl-family of GEFs that possess a Dbl(DH) domain with a PH domain in tandem. DH-PH domain catalyzes the GDP/GTP exchange reaction in the GTPase cycle and facillitating the switch between inactive GDP-bound and active GTP-bound states. The DH domain of Tiam1 interacts with Switch regions 1 and 2 of Rac1 which blocks magnesium binding and GDP is released. Tiam1/2 possess two PH domains, which are often referred to as PHn and PHc domains. The DH-PH tandem domain is made up of the PHc domain while the PHn is part of a novel N-terminal PHCCEx domain which is made up of the PHn domain, a coiled coil region(CC), and an extra region (Ex). PHCCEx mediates binding to plasma membranes and signalling proteins in the activation of Rac GTPases. The PH domain resembles the beta-spectrin PH domain, suggesting non-canonical phosphatidylinositol binding. CC and Ex form a positively charged surface for protein binding. There are 2 motifs in Tiam1/2-interacting proteins that bind to the PHCCEx domain: Motif-I in CD44, ephrinBs, and the NMDA receptor and Motif-II in Par3 and JIP2. 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: 269957  Cd Length: 172  Bit Score: 300.07  E-value: 4.25e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006 242 QKIYEDYGMVFDQLVAEQSGTEKEVTELSMGELLMHSTVSWLNPFLSLGKARKDIELTVFVFKRAVILVYKENCKLKKKL 321
Cdd:cd01255    1 QKIHEEYGAVFDQLIREQSGTKKEVADLSMGDLLLYGTVEWLNPPSSLGKVKKEPELAVFVFKTAVVLVCKERSKQKKKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006 322 PSNSRPAHnSADLDPFKFRWLIPISALQVRLGNTAGTENNSTWELIHTKSEIEGRPETIFQLCCSDSENKTSIVKVIRSI 401
Cdd:cd01255   81 MGSHRKSS-YEERDPFRFRHLIPVSALQVRNSNTADTESRCLWELIHTKSELEGRPEKVFQLCCSTPEFKNAFLKVIRSI 159
                        170
                 ....*....|...
gi 568998006 402 LRENFRRHIKCEL 414
Cdd:cd01255  160 LREKVRRQSSKTE 172
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
51-240 3.34e-49

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: 169.40  E-value: 3.34e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006    51 VIQELVDTEKSYVKDLSCLFELYLEPLQNE-TFLTQDEMESLFGSLPEMLEFQKVFLETLEDAISASSDFSvletpsqfr 129
Cdd:smart00325   1 VLKELLQTERNYVRDLKLLVEVFLKPLKKElKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSV--------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006   130 kllFSLGGSFLYYADHFKLYSGFCANHIKVQRVLERAKTDKAFKAFLDARNPTKQHSS-TLESYLIKPVQRVLKYPLLLK 208
Cdd:smart00325  72 ---ERIGDVFLKLEEFFKIYSEYCSNHPDALELLKKLKKNPRFQKFLKEIESSPQCRRlTLESLLLKPVQRLTKYPLLLK 148
                          170       180       190
                   ....*....|....*....|....*....|..
gi 568998006   209 ELVSLTDHESEEHYHLTEALKAMEKVASHINE 240
Cdd:smart00325 149 ELLKHTPEDHEDREDLKKALKAIKELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
48-239 6.96e-48

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: 165.93  E-value: 6.96e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006  48 LRKVIQELVDTEKSYVKDLSCLFELYLEPLQNE-TFLTQDEMESLFGSLPEMLEFQKVFLETLEDAISASsdfsvletps 126
Cdd:cd00160    1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKElLPLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEW---------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006 127 qfRKLLFSLGGSFLYYADHFKLYSGFCANHIKVQRVLE-RAKTDKAFKAFLDARNpTKQHSSTLESYLIKPVQRVLKYPL 205
Cdd:cd00160   71 --DKSGPRIGDVFLKLAPFFKIYSEYCSNHPDALELLKkLKKFNKFFQEFLEKAE-SECGRLKLESLLLKPVQRLTKYPL 147
                        170       180       190
                 ....*....|....*....|....*....|....
gi 568998006 206 LLKELVSLTDHESEEHYHLTEALKAMEKVASHIN 239
Cdd:cd00160  148 LLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
51-239 6.89e-45

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: 157.85  E-value: 6.89e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006   51 VIQELVDTEKSYVKDLSCLFELYLEPLQNETFLTQDEMESLFGSLPEMLEFQKVFLetledaisassdfsvLETPSQFRK 130
Cdd:pfam00621   1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHRQLL---------------LEELLKEWI 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006  131 LLFSLGGSFLYYADHFKLYSGFCANHIKVQRVLERAK-TDKAFKAFLDARNPTKQHSS-TLESYLIKPVQRVLKYPLLLK 208
Cdd:pfam00621  66 SIQRIGDIFLKFAPGFKVYSTYCSNYPKALKLLKKLLkKNPKFRAFLEELEANPECRGlDLNSFLIKPVQRIPRYPLLLK 145
                         170       180       190
                  ....*....|....*....|....*....|.
gi 568998006  209 ELVSLTDHESEEHYHLTEALKAMEKVASHIN 239
Cdd:pfam00621 146 ELLKHTPPDHPDYEDLKKALEAIKEVAKQIN 176
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
35-252 7.75e-06

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


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 49.12  E-value: 7.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006   35 PRPLARHLSDADRLRK-VIQELVDTEKSYVKDLSCLFELYLEPLQNETFLTQDEMEslfgslpemlEFQKVFLETLEDAI 113
Cdd:COG5422   471 PKEVWESLPKQEIKRQeAIYEVIYTERDFVKDLEYLRDTWIKPLEESNIIPENARR----------NFIKHVFANINEIY 540
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006  114 SASSDFSVLETPSQ-FRKLLFSLGGSFLYYADHFKLYSGFCANHIKVQRVLERAK-TDKAFKAFLD----ARNPTKQHss 187
Cdd:COG5422   541 AVNSKLLKALTNRQcLSPIVNGIADIFLDYVPKFEPFIKYGASQPYAKYEFEREKsVNPNFARFDHeverLDESRKLE-- 618
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568998006  188 tLESYLIKPVQRVLKYPLLLKELVSLTDHESEEHYHLTEALKAMEKVASHINEMQKIYEDYGMVF 252
Cdd:COG5422   619 -LDGYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFESGKAENRGDLF 682
PH_PLEKHG1_G2_G3 cd13243
Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) ...
226-321 6.22e-03

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: 37.72  E-value: 6.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998006 226 EALKAMEKVASHINEMQKIYEDygMVFDQLVAEQSGTEKEVTELSMGELLMHSTvswlnpflsLGKARKDIELTVFVFKR 305
Cdd:cd13243    6 EALDTMTQVAWHINDMKRKHEH--AVRVQEIQSLLDGWEGPELTTYGDLVLEGT---------FRMAGAKNERLLFLFDK 74
                         90
                 ....*....|....*..
gi 568998006 306 AVILV-YKENCKLKKKL 321
Cdd:cd13243   75 MLLITkKREDGILQYKT 91
 
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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