NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|193202277|ref|NP_001122421|]
View 

Rho-GAP domain-containing protein [Caenorhabditis elegans]

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
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 55-264 5.57e-58

RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in OCRL1-like proteins. OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins contain two conserved domains: a central inositol polyphosphate 5-phosphatase domain and a C-terminal Rho GAP domain, this GAP domain lacks the catalytic residue and therefore maybe inactive. OCRL-like proteins are type II inositol polyphosphate 5-phosphatases that can hydrolyze lipid PI(4,5)P2 and PI(3,4,5)P3 and soluble Ins(1,4,5)P3 and Ins(1,3,4,5)P4, but their individual specificities vary. The functionality of the RhoGAP domain is still unclear. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


:

Pssm-ID: 239845  Cd Length: 220  Bit Score: 184.47  E-value: 5.57e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202277  55 FIPITAVYNNSCFGSTLEKLLSMRPKKEVNLIDFGDFSENSLSDNCPPNVPRVIYRLVMALRTRGAVQLNIEEEQDNEV- 133
Cdd:cd04380    1 FITVTGVYLPSCFGSSLETLIRLPDPGIRNLIDQLELGDNPDYSEVPLSIPKEIWRLVDYLYTRGLAQEGLFEEPGLPSe 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202277 134 ----FNRIRSALESGQPDDLSqlASSYMLYSALIRLLDSLDEPIILEGMFKIIHKEMikyRTDARQLWTVVRSSLPKQNQ 209
Cdd:cd04380   81 pgelLAEIRDALDTGSPFNSP--GSAESVAEALLLFLESLPDPIIPYSLYERLLEAV---ANNEEDKRQVIRISLPPVHR 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193202277 210 AVLELICLMLREFFSQKYELKDQLSLWATVLFRHDIQDE----------KMHGMFSTILQTICDY 264
Cdd:cd04380  156 NVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPpraggkerraERDRKRAFIEQFLLND 220
 
Name Accession Description Interval E-value
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 55-264 5.57e-58

RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in OCRL1-like proteins. OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins contain two conserved domains: a central inositol polyphosphate 5-phosphatase domain and a C-terminal Rho GAP domain, this GAP domain lacks the catalytic residue and therefore maybe inactive. OCRL-like proteins are type II inositol polyphosphate 5-phosphatases that can hydrolyze lipid PI(4,5)P2 and PI(3,4,5)P3 and soluble Ins(1,4,5)P3 and Ins(1,3,4,5)P4, but their individual specificities vary. The functionality of the RhoGAP domain is still unclear. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239845  Cd Length: 220  Bit Score: 184.47  E-value: 5.57e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202277  55 FIPITAVYNNSCFGSTLEKLLSMRPKKEVNLIDFGDFSENSLSDNCPPNVPRVIYRLVMALRTRGAVQLNIEEEQDNEV- 133
Cdd:cd04380    1 FITVTGVYLPSCFGSSLETLIRLPDPGIRNLIDQLELGDNPDYSEVPLSIPKEIWRLVDYLYTRGLAQEGLFEEPGLPSe 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202277 134 ----FNRIRSALESGQPDDLSqlASSYMLYSALIRLLDSLDEPIILEGMFKIIHKEMikyRTDARQLWTVVRSSLPKQNQ 209
Cdd:cd04380   81 pgelLAEIRDALDTGSPFNSP--GSAESVAEALLLFLESLPDPIIPYSLYERLLEAV---ANNEEDKRQVIRISLPPVHR 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193202277 210 AVLELICLMLREFFSQKYELKDQLSLWATVLFRHDIQDE----------KMHGMFSTILQTICDY 264
Cdd:cd04380  156 NVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPpraggkerraERDRKRAFIEQFLLND 220
 
Name Accession Description Interval E-value
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 55-264 5.57e-58

RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in OCRL1-like proteins. OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins contain two conserved domains: a central inositol polyphosphate 5-phosphatase domain and a C-terminal Rho GAP domain, this GAP domain lacks the catalytic residue and therefore maybe inactive. OCRL-like proteins are type II inositol polyphosphate 5-phosphatases that can hydrolyze lipid PI(4,5)P2 and PI(3,4,5)P3 and soluble Ins(1,4,5)P3 and Ins(1,3,4,5)P4, but their individual specificities vary. The functionality of the RhoGAP domain is still unclear. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239845  Cd Length: 220  Bit Score: 184.47  E-value: 5.57e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202277  55 FIPITAVYNNSCFGSTLEKLLSMRPKKEVNLIDFGDFSENSLSDNCPPNVPRVIYRLVMALRTRGAVQLNIEEEQDNEV- 133
Cdd:cd04380    1 FITVTGVYLPSCFGSSLETLIRLPDPGIRNLIDQLELGDNPDYSEVPLSIPKEIWRLVDYLYTRGLAQEGLFEEPGLPSe 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202277 134 ----FNRIRSALESGQPDDLSqlASSYMLYSALIRLLDSLDEPIILEGMFKIIHKEMikyRTDARQLWTVVRSSLPKQNQ 209
Cdd:cd04380   81 pgelLAEIRDALDTGSPFNSP--GSAESVAEALLLFLESLPDPIIPYSLYERLLEAV---ANNEEDKRQVIRISLPPVHR 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193202277 210 AVLELICLMLREFFSQKYELKDQLSLWATVLFRHDIQDE----------KMHGMFSTILQTICDY 264
Cdd:cd04380  156 NVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPpraggkerraERDRKRAFIEQFLLND 220
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 104-263 1.58e-03

RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of FAM13A1, isoform a-like proteins. The function of FAM13A1a is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by up several orders of magnitude.


Pssm-ID: 239858 [Multi-domain]  Cd Length: 189  Bit Score: 38.60  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202277 104 VPRVIYRLVMALRTRGAVQLNIEEEQDN-EVFNRIRSALESGQPDDLSQLASSYMLYSALIRLLDSLDEPIILEGMFKII 182
Cdd:cd04393   20 VPAVVRHIVEYLEQHGLEQEGLFRVNGNaETVEWLRQRLDSGEEVDLSKEADVCSAASLLRLFLQELPEGLIPASLQIRL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202277 183 HKEMIKYRTD---ARQLWTVVRsSLPKQNQAVLELICLMLREFFSQKYELKDQLSLWATVL------FRHDIQDEKMHGM 253
Cdd:cd04393  100 MQLYQDYNGEdefGRKLRDLLQ-QLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAAVFgpdvfhVYTDVEDMKEQEI 178

                        170
                 ....*....|
gi 193202277 254 FSTILQTICD 263
Cdd:cd04393  179 CSRIMAKLLE 188
 
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