NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767932166|ref|XP_011530353|]
View 

rho guanine nucleotide exchange factor 38 isoform X3 [Homo sapiens]

Protein Classification

RhoGEF and BAR domain-containing protein( domain architecture ID 11101204)

RhoGEF and BAR domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 98-283 1.78e-35

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: 128.96  E-value: 1.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932166   98 IIKELIQTEKDYLNDLELCVREVVQPLRNK-KTDRLDVDSLFSNIESVHQISAKLLslLEEaTTDVEPAMQVIGEVFLQI 176
Cdd:pfam00621   1 VIKELLQTERSYVRDLEILVEVFLPPNSKPlSESEEEIKTIFSNIEEIYELHRQLL--LEE-LLKEWISIQRIGDIFLKF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932166  177 KGPLEdIYKIYCYHHDEAHSILESYEKEEELKEHLSHCIQSLKKIymqegkpNLLDMGSLMIKPIQRVMKYPLLLCELRN 256
Cdd:pfam00621  78 APGFK-VYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPEC-------RGLDLNSFLIKPVQRIPRYPLLLKELLK 149

                         170       180
                  ....*....|....*....|....*..
gi 767932166  257 STPPSHPDYRALDDAFAAVKDINVNIN 283
Cdd:pfam00621 150 HTPPDHPDYEDLKKALEAIKEVAKQIN 176
BAR super family cl12013
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 336-419 4.62e-14

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


The actual alignment was detected with superfamily member cd07589:

Pssm-ID: 472257  Cd Length: 195  Bit Score: 70.42  E-value: 4.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932166 336 QVKDNTFNREEKLFRALEKTVRLCVKNISLCLQHIQDA---MPLALQSVMDLQEISYNKDDEMD---YSETLSNALNSCH 409
Cdd:cd07589    1 QTKDKEFDELEKKFGSLEKQVQLVVRNVELYLQHVQESvlvKVLALEVVLDLYPSNHPRLESKWerfRRVVRGISSKALP 80

                         90
                 ....*....|
gi 767932166 410 DFVLLFHSSI 419
Cdd:cd07589   81 EFKSRVRKLV 90
 
Name Accession Description Interval E-value
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 98-283 1.78e-35

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: 128.96  E-value: 1.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932166   98 IIKELIQTEKDYLNDLELCVREVVQPLRNK-KTDRLDVDSLFSNIESVHQISAKLLslLEEaTTDVEPAMQVIGEVFLQI 176
Cdd:pfam00621   1 VIKELLQTERSYVRDLEILVEVFLPPNSKPlSESEEEIKTIFSNIEEIYELHRQLL--LEE-LLKEWISIQRIGDIFLKF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932166  177 KGPLEdIYKIYCYHHDEAHSILESYEKEEELKEHLSHCIQSLKKIymqegkpNLLDMGSLMIKPIQRVMKYPLLLCELRN 256
Cdd:pfam00621  78 APGFK-VYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPEC-------RGLDLNSFLIKPVQRIPRYPLLLKELLK 149

                         170       180
                  ....*....|....*....|....*..
gi 767932166  257 STPPSHPDYRALDDAFAAVKDINVNIN 283
Cdd:pfam00621 150 HTPPDHPDYEDLKKALEAIKEVAKQIN 176
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 95-283 8.91e-32

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: 119.32  E-value: 8.91e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932166  95 REKIIKELIQTEKDYLNDLELCVREVVQPL--RNKKTDRLDVDSLFSNIESVHQISAKLLSLLEEATTDVEPAMQVIGEV 172
Cdd:cd00160    1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLdkELLPLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGPRIGDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932166 173 FLQIKGPLEdIYKIYCYHHDEAHSIlesyekeeelkehLSHCIQSLKK----IYMQEGKPNLLDMGSLMIKPIQRVMKYP 248
Cdd:cd00160   81 FLKLAPFFK-IYSEYCSNHPDALEL-------------LKKLKKFNKFfqefLEKAESECGRLKLESLLLKPVQRLTKYP 146

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767932166 249 LLLCELRNSTPPSHPDYRALDDAFAAVKDINVNIN 283
Cdd:cd00160  147 LLLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 98-284 9.63e-31

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: 116.25  E-value: 9.63e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932166    98 IIKELIQTEKDYLNDLELCVREVVQPLR--NKKTDRLDVDSLFSNIESVHQISAKLLSLLEEATTDVEPAMQVIGEVFLQ 175
Cdd:smart00325   1 VLKELLQTERNYVRDLKLLVEVFLKPLKkeLKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVERIGDVFLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932166   176 IKgPLEDIYKIYCYHHDEAHSILEsyekeeelkeHLSHCIQSLKKIYMQEGKPNL--LDMGSLMIKPIQRVMKYPLLLCE 253
Cdd:smart00325  81 LE-EFFKIYSEYCSNHPDALELLK----------KLKKNPRFQKFLKEIESSPQCrrLTLESLLLKPVQRLTKYPLLLKE 149

                          170       180       190
                   ....*....|....*....|....*....|.
gi 767932166   254 LRNSTPPSHPDYRALDDAFAAVKDINVNINE 284
Cdd:smart00325 150 LLKHTPEDHEDREDLKKALKAIKELANQVNE 180
BAR_DNMBP cd07589
The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin Binding Protein; BAR domains are dimerization, ...
 336-419 4.62e-14

The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin Binding Protein; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. DyNamin Binding Protein (DNMBP), also called Tuba, is a Cdc42-specific Guanine nucleotide Exchange Factor (GEF) that binds dynamin and various actin regulatory proteins. It serves as a link between dynamin function, Rho GTPase signaling, and actin dynamics. It plays an important role in regulating cell junction configuration. DNMBP contains BAR and SH3 domains as well as a Dbl Homology domain (DH domain), which harbors GEF activity. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of DNMBP may be involved in binding to membranes. The gene encoding DNMBP is a candidate gene for late onset Alzheimer's disease.


Pssm-ID: 153273  Cd Length: 195  Bit Score: 70.42  E-value: 4.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932166 336 QVKDNTFNREEKLFRALEKTVRLCVKNISLCLQHIQDA---MPLALQSVMDLQEISYNKDDEMD---YSETLSNALNSCH 409
Cdd:cd07589    1 QTKDKEFDELEKKFGSLEKQVQLVVRNVELYLQHVQESvlvKVLALEVVLDLYPSNHPRLESKWerfRRVVRGISSKALP 80

                         90
                 ....*....|
gi 767932166 410 DFVLLFHSSI 419
Cdd:cd07589   81 EFKSRVRKLV 90
BAR smart00721
BAR domain;
315-387 5.94e-05

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 44.30  E-value: 5.94e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767932166   315 SISKKSKRVTNHLKILTRGESQVK-DNTFNREEKLFRALEKTVRLCVKNISLCLQHiQDAMPLALQSVMDLQEI 387
Cdd:smart00721   1 GFKKQFNRAKQKVGEKVGKAEKTKlDEDFEELERRFDTTEAEIEKLQKDTKLYLQP-NPAVRAKLASQKKLSKS 73
 
Name Accession Description Interval E-value
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 98-283 1.78e-35

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: 128.96  E-value: 1.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932166   98 IIKELIQTEKDYLNDLELCVREVVQPLRNK-KTDRLDVDSLFSNIESVHQISAKLLslLEEaTTDVEPAMQVIGEVFLQI 176
Cdd:pfam00621   1 VIKELLQTERSYVRDLEILVEVFLPPNSKPlSESEEEIKTIFSNIEEIYELHRQLL--LEE-LLKEWISIQRIGDIFLKF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932166  177 KGPLEdIYKIYCYHHDEAHSILESYEKEEELKEHLSHCIQSLKKIymqegkpNLLDMGSLMIKPIQRVMKYPLLLCELRN 256
Cdd:pfam00621  78 APGFK-VYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPEC-------RGLDLNSFLIKPVQRIPRYPLLLKELLK 149

                         170       180
                  ....*....|....*....|....*..
gi 767932166  257 STPPSHPDYRALDDAFAAVKDINVNIN 283
Cdd:pfam00621 150 HTPPDHPDYEDLKKALEAIKEVAKQIN 176
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 95-283 8.91e-32

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: 119.32  E-value: 8.91e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932166  95 REKIIKELIQTEKDYLNDLELCVREVVQPL--RNKKTDRLDVDSLFSNIESVHQISAKLLSLLEEATTDVEPAMQVIGEV 172
Cdd:cd00160    1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLdkELLPLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGPRIGDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932166 173 FLQIKGPLEdIYKIYCYHHDEAHSIlesyekeeelkehLSHCIQSLKK----IYMQEGKPNLLDMGSLMIKPIQRVMKYP 248
Cdd:cd00160   81 FLKLAPFFK-IYSEYCSNHPDALEL-------------LKKLKKFNKFfqefLEKAESECGRLKLESLLLKPVQRLTKYP 146

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767932166 249 LLLCELRNSTPPSHPDYRALDDAFAAVKDINVNIN 283
Cdd:cd00160  147 LLLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 98-284 9.63e-31

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: 116.25  E-value: 9.63e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932166    98 IIKELIQTEKDYLNDLELCVREVVQPLR--NKKTDRLDVDSLFSNIESVHQISAKLLSLLEEATTDVEPAMQVIGEVFLQ 175
Cdd:smart00325   1 VLKELLQTERNYVRDLKLLVEVFLKPLKkeLKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVERIGDVFLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932166   176 IKgPLEDIYKIYCYHHDEAHSILEsyekeeelkeHLSHCIQSLKKIYMQEGKPNL--LDMGSLMIKPIQRVMKYPLLLCE 253
Cdd:smart00325  81 LE-EFFKIYSEYCSNHPDALELLK----------KLKKNPRFQKFLKEIESSPQCrrLTLESLLLKPVQRLTKYPLLLKE 149

                          170       180       190
                   ....*....|....*....|....*....|.
gi 767932166   254 LRNSTPPSHPDYRALDDAFAAVKDINVNINE 284
Cdd:smart00325 150 LLKHTPEDHEDREDLKKALKAIKELANQVNE 180
BAR_DNMBP cd07589
The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin Binding Protein; BAR domains are dimerization, ...
 336-419 4.62e-14

The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin Binding Protein; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. DyNamin Binding Protein (DNMBP), also called Tuba, is a Cdc42-specific Guanine nucleotide Exchange Factor (GEF) that binds dynamin and various actin regulatory proteins. It serves as a link between dynamin function, Rho GTPase signaling, and actin dynamics. It plays an important role in regulating cell junction configuration. DNMBP contains BAR and SH3 domains as well as a Dbl Homology domain (DH domain), which harbors GEF activity. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of DNMBP may be involved in binding to membranes. The gene encoding DNMBP is a candidate gene for late onset Alzheimer's disease.


Pssm-ID: 153273  Cd Length: 195  Bit Score: 70.42  E-value: 4.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932166 336 QVKDNTFNREEKLFRALEKTVRLCVKNISLCLQHIQDA---MPLALQSVMDLQEISYNKDDEMD---YSETLSNALNSCH 409
Cdd:cd07589    1 QTKDKEFDELEKKFGSLEKQVQLVVRNVELYLQHVQESvlvKVLALEVVLDLYPSNHPRLESKWerfRRVVRGISSKALP 80

                         90
                 ....*....|
gi 767932166 410 DFVLLFHSSI 419
Cdd:cd07589   81 EFKSRVRKLV 90
BAR smart00721
BAR domain;
315-387 5.94e-05

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 44.30  E-value: 5.94e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767932166   315 SISKKSKRVTNHLKILTRGESQVK-DNTFNREEKLFRALEKTVRLCVKNISLCLQHiQDAMPLALQSVMDLQEI 387
Cdd:smart00721   1 GFKKQFNRAKQKVGEKVGKAEKTKlDEDFEELERRFDTTEAEIEKLQKDTKLYLQP-NPAVRAKLASQKKLSKS 73
 
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