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Conserved domains on  [gi|149048567|gb|EDM01108|]
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ect2 oncogene (predicted), isoform CRA_c [Rattus norvegicus]

Protein Classification

ECT2 family protein( domain architecture ID 11101039)

ECT2 (epithelial cell-transforming sequence 2 oncogene) family protein similar to RhoGEF and PH (pleckstrin homology) domain regions of Homo sapiens protein ECT2, an exchange factor for Rho GTPases, and Drosophila melanogaster pebble, isoform F

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_Ect2 cd01229
Epithelial cell transforming 2 (Ect2) pleckstrin homology (PH) domain; Ect2, a mammalian ...
 119-292 5.27e-92

Epithelial cell transforming 2 (Ect2) pleckstrin homology (PH) domain; Ect2, a mammalian ortholog of Drosophila pebble, plays a role in neuronal differentiation and brain development. Pebble and Ect2 have been identified as Rho-family guanine nucleotide exchange factors (GEF) that mediate activation of Rho during cytokinesis, but are proposed to play slightly different roles. 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: 269936  Cd Length: 180  Bit Score: 274.54  E-value: 5.27e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048567 119 LKEVMTHINEDKRKTEAQKQIFDVVYEVDGCPANLLSSHRSLIQRVETVSLG-EHPCDRGEQVTLFLFNDCLEIARKRHK 197
Cdd:cd01229    1 LKEVMTHINEDKRKTESQAQMFDIVNEIENCPPTLLSSHRSFVSRCEVVELGdSLKSGRGDSLTLFLFSDLIEICKKRSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048567 198 VIGTFRSPHDRTR-----PPASLKHIHLMPLSQIKKVLDIRETEDCHNAFALLVRPPTEQANVLLSFQMTSEELPKESWL 272
Cdd:cd01229   81 VKGTSKSPRGSTGsglreSKKKYKHVKLMPLSTIKRVIDIRETEDCQRVFALLFRHPTELKEKLYSFQILDEETDKESFL 160

                        170       180
                 ....*....|....*....|
gi 149048567 273 KMLCRHVANTICKADAENLM 292
Cdd:cd01229  161 KTLCKQVANTVCRADAENFL 180
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 7-127 8.08e-33

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: 121.25  E-value: 8.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048567    7 LEDLIANWDESRSIGDIFLKYSKDLvKTYPPFVNFFEMSKEMIIKCEKQKPRFHAFLKINQAKPECGRQSLVELLIRPVQ 86
Cdd:pfam00621  57 LEELLKEWISIQRIGDIFLKFAPGF-KVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQ 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 149048567   87 RLPSVALLLNDLKKHTADENPDKSTLEKAIGSLKEVMTHIN 127
Cdd:pfam00621 136 RIPRYPLLLKELLKHTPPDHPDYEDLKKALEAIKEVAKQIN 176
 
Name Accession Description Interval E-value
PH_Ect2 cd01229
Epithelial cell transforming 2 (Ect2) pleckstrin homology (PH) domain; Ect2, a mammalian ...
 119-292 5.27e-92

Epithelial cell transforming 2 (Ect2) pleckstrin homology (PH) domain; Ect2, a mammalian ortholog of Drosophila pebble, plays a role in neuronal differentiation and brain development. Pebble and Ect2 have been identified as Rho-family guanine nucleotide exchange factors (GEF) that mediate activation of Rho during cytokinesis, but are proposed to play slightly different roles. 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: 269936  Cd Length: 180  Bit Score: 274.54  E-value: 5.27e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048567 119 LKEVMTHINEDKRKTEAQKQIFDVVYEVDGCPANLLSSHRSLIQRVETVSLG-EHPCDRGEQVTLFLFNDCLEIARKRHK 197
Cdd:cd01229    1 LKEVMTHINEDKRKTESQAQMFDIVNEIENCPPTLLSSHRSFVSRCEVVELGdSLKSGRGDSLTLFLFSDLIEICKKRSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048567 198 VIGTFRSPHDRTR-----PPASLKHIHLMPLSQIKKVLDIRETEDCHNAFALLVRPPTEQANVLLSFQMTSEELPKESWL 272
Cdd:cd01229   81 VKGTSKSPRGSTGsglreSKKKYKHVKLMPLSTIKRVIDIRETEDCQRVFALLFRHPTELKEKLYSFQILDEETDKESFL 160

                        170       180
                 ....*....|....*....|
gi 149048567 273 KMLCRHVANTICKADAENLM 292
Cdd:cd01229  161 KTLCKQVANTVCRADAENFL 180
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 7-127 8.08e-33

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: 121.25  E-value: 8.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048567    7 LEDLIANWDESRSIGDIFLKYSKDLvKTYPPFVNFFEMSKEMIIKCEKQKPRFHAFLKINQAKPECGRQSLVELLIRPVQ 86
Cdd:pfam00621  57 LEELLKEWISIQRIGDIFLKFAPGF-KVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQ 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 149048567   87 RLPSVALLLNDLKKHTADENPDKSTLEKAIGSLKEVMTHIN 127
Cdd:pfam00621 136 RIPRYPLLLKELLKHTPPDHPDYEDLKKALEAIKEVAKQIN 176
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 5-128 3.10e-30

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: 114.71  E-value: 3.10e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048567     5 DDLEDLIANWDES-RSIGDIFLKYSKDLvKTYPPFVNFFEMSKEMIIKCeKQKPRFHAFLKINQAKPECGRQSLVELLIR 83
Cdd:smart00325  58 DELEERIEEWDDSvERIGDVFLKLEEFF-KIYSEYCSNHPDALELLKKL-KKNPRFQKFLKEIESSPQCRRLTLESLLLK 135

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 149048567    84 PVQRLPSVALLLNDLKKHTADENPDKSTLEKAIGSLKEVMTHINE 128
Cdd:smart00325 136 PVQRLTKYPLLLKELLKHTPEDHEDREDLKKALKAIKELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 5-127 4.89e-27

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: 105.84  E-value: 4.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048567   5 DDLEDLIANWDES-RSIGDIFLKYsKDLVKTYPPFVNFFEMSKEMIIKCEKQKPRFHAFLKinQAKPECGRQSLVELLIR 83
Cdd:cd00160   61 KSLEERVEEWDKSgPRIGDVFLKL-APFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLE--KAESECGRLKLESLLLK 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 149048567  84 PVQRLPSVALLLNDLKKHTADENPDKSTLEKAIGSLKEVMTHIN 127
Cdd:cd00160  138 PVQRLTKYPLLLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 18-163 5.36e-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: 48.73  E-value: 5.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048567   18 RSIGDIFLKYskdlVKTYPPFVNFFEMSKEMIIKCEKQK---PRFHAFLKINQAKPECGRQSLVELLIRPVQRLPSVALL 94
Cdd:COG5422   561 NGIADIFLDY----VPKFEPFIKYGASQPYAKYEFEREKsvnPNFARFDHEVERLDESRKLELDGYLTKPTTRLARYPLL 636

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149048567   95 LNDLKKHTADENPDKSTLEKAIGSLKEVMTHINEDKRKTEAQKQIF----DVVYEVDGCPANLLSSHRSLIQR 163
Cdd:COG5422   637 LEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFESGKAENRGDLFhlnqQLLFKPEYVNLGLNDEYRKIIFK 709
 
Name Accession Description Interval E-value
PH_Ect2 cd01229
Epithelial cell transforming 2 (Ect2) pleckstrin homology (PH) domain; Ect2, a mammalian ...
 119-292 5.27e-92

Epithelial cell transforming 2 (Ect2) pleckstrin homology (PH) domain; Ect2, a mammalian ortholog of Drosophila pebble, plays a role in neuronal differentiation and brain development. Pebble and Ect2 have been identified as Rho-family guanine nucleotide exchange factors (GEF) that mediate activation of Rho during cytokinesis, but are proposed to play slightly different roles. 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: 269936  Cd Length: 180  Bit Score: 274.54  E-value: 5.27e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048567 119 LKEVMTHINEDKRKTEAQKQIFDVVYEVDGCPANLLSSHRSLIQRVETVSLG-EHPCDRGEQVTLFLFNDCLEIARKRHK 197
Cdd:cd01229    1 LKEVMTHINEDKRKTESQAQMFDIVNEIENCPPTLLSSHRSFVSRCEVVELGdSLKSGRGDSLTLFLFSDLIEICKKRSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048567 198 VIGTFRSPHDRTR-----PPASLKHIHLMPLSQIKKVLDIRETEDCHNAFALLVRPPTEQANVLLSFQMTSEELPKESWL 272
Cdd:cd01229   81 VKGTSKSPRGSTGsglreSKKKYKHVKLMPLSTIKRVIDIRETEDCQRVFALLFRHPTELKEKLYSFQILDEETDKESFL 160

                        170       180
                 ....*....|....*....|
gi 149048567 273 KMLCRHVANTICKADAENLM 292
Cdd:cd01229  161 KTLCKQVANTVCRADAENFL 180
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 7-127 8.08e-33

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: 121.25  E-value: 8.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048567    7 LEDLIANWDESRSIGDIFLKYSKDLvKTYPPFVNFFEMSKEMIIKCEKQKPRFHAFLKINQAKPECGRQSLVELLIRPVQ 86
Cdd:pfam00621  57 LEELLKEWISIQRIGDIFLKFAPGF-KVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQ 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 149048567   87 RLPSVALLLNDLKKHTADENPDKSTLEKAIGSLKEVMTHIN 127
Cdd:pfam00621 136 RIPRYPLLLKELLKHTPPDHPDYEDLKKALEAIKEVAKQIN 176
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 5-128 3.10e-30

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: 114.71  E-value: 3.10e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048567     5 DDLEDLIANWDES-RSIGDIFLKYSKDLvKTYPPFVNFFEMSKEMIIKCeKQKPRFHAFLKINQAKPECGRQSLVELLIR 83
Cdd:smart00325  58 DELEERIEEWDDSvERIGDVFLKLEEFF-KIYSEYCSNHPDALELLKKL-KKNPRFQKFLKEIESSPQCRRLTLESLLLK 135

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 149048567    84 PVQRLPSVALLLNDLKKHTADENPDKSTLEKAIGSLKEVMTHINE 128
Cdd:smart00325 136 PVQRLTKYPLLLKELLKHTPEDHEDREDLKKALKAIKELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 5-127 4.89e-27

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: 105.84  E-value: 4.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048567   5 DDLEDLIANWDES-RSIGDIFLKYsKDLVKTYPPFVNFFEMSKEMIIKCEKQKPRFHAFLKinQAKPECGRQSLVELLIR 83
Cdd:cd00160   61 KSLEERVEEWDKSgPRIGDVFLKL-APFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLE--KAESECGRLKLESLLLK 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 149048567  84 PVQRLPSVALLLNDLKKHTADENPDKSTLEKAIGSLKEVMTHIN 127
Cdd:cd00160  138 PVQRLTKYPLLLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 18-163 5.36e-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: 48.73  E-value: 5.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048567   18 RSIGDIFLKYskdlVKTYPPFVNFFEMSKEMIIKCEKQK---PRFHAFLKINQAKPECGRQSLVELLIRPVQRLPSVALL 94
Cdd:COG5422   561 NGIADIFLDY----VPKFEPFIKYGASQPYAKYEFEREKsvnPNFARFDHEVERLDESRKLELDGYLTKPTTRLARYPLL 636

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149048567   95 LNDLKKHTADENPDKSTLEKAIGSLKEVMTHINEDKRKTEAQKQIF----DVVYEVDGCPANLLSSHRSLIQR 163
Cdd:COG5422   637 LEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFESGKAENRGDLFhlnqQLLFKPEYVNLGLNDEYRKIIFK 709
 
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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