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Conserved domains on  [gi|81900344|sp|Q8CGF1|]
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RecName: Full=Rho GTPase-activating protein 29; AltName: Full=Rho-type GTPase-activating protein 29

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RhoGAP super family cl02570
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 671-883 1.40e-123

RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like small GTPases. Small GTPases (G proteins) cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when bound to GDP. The Rho family of small G proteins, which includes Cdc42Hs, activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. G proteins 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. The RhoGAPs are one of the major classes of regulators of Rho G proteins.


The actual alignment was detected with superfamily member cd04409:

Pssm-ID: 470621  Cd Length: 211  Bit Score: 380.31  E-value: 1.40e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  671 FGAEFIQVAKKEPDGIPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLVDISEFSSHDICDVLKLYLR 750
Cdd:cd04409    1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLKLYLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  751 QLPEPFILFRLYKEFIDLAKEIQHVNEEQEAKKDSpeDKKHPHVSIEVNRILLKSKDLLRQLPASHFNSLHYLIAHLRRV 830
Cdd:cd04409   81 QLPEPLILFRLYNEFIGLAKESQHVNETQEAKKNS--DKKWPNMCTELNRILLKSKDLLRQLPAPNYNTLQFLIVHLHRV 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 81900344  831 VDHAEENKMNSKNLGVIFGPTLIRPRPTTAPVTISSLAEYSNQARLVEFLITY 883
Cdd:cd04409  159 SEQAEENKMSASNLGIIFGPTLIRPRPTDATVSLSSLVDYPHQARLVELLITY 211
C1_GMIP-like cd20816
protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP) ...
 613-663 1.58e-23

protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP)-like family; The GMIP-like family includes GMIP, Rho GTPase-activating protein 29 (ARHGAP29) and Rho GTPase-activating protein 45 (ARHGAP45). GMIP is a RhoA-specific GTPase-activating protein that acts as a key factor in saltatory neuronal migration. It associates with the Rab27a effector JFC1 and modulates vesicular transport and exocytosis. ARHGAP29, also called PTPL1-associated RhoGAP protein 1 (PARG1) or Rho-type GTPase-activating protein 29, is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. It has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. ARHGAP29 may act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, ARHGAP29 suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis. ARHGAP45, also called minor histocompatibility antigen HA-1 (mHag HA-1), is a Rac-GAP (GTPase-Activating Protein) in endothelial cells. It acts as a novel regulator of endothelial integrity. ARHGAP45 contains a GTPase activator for the Rho-type GTPases (RhoGAP) domain that would be able to negatively regulate the actin cytoskeleton as well as cell spreading. However, it also contains N-terminally a BAR-domin which can play an autoinhibitory effect on this RhoGAP activity. Members of this family contain a zinc-binding C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410366  Cd Length: 51  Bit Score: 94.25  E-value: 1.58e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 81900344  613 LTHKFRKLRSPTKCRDCDGIVMFPGVECEECLLVCHRKCLENLVIICGHQK 663
Cdd:cd20816    1 QTHRFRRLRTPSKCRECDSYVYFNGAECEECGLACHKKCLETLAIQCGHKR 51
BAR super family cl12013
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 220-436 6.44e-11

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 cd07652:

Pssm-ID: 472257 [Multi-domain]  Cd Length: 234  Bit Score: 63.91  E-value: 6.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  220 KNIVSWVEKKLNLELESTRNIVKLAEATRSSIGIQEFmpLQSLFTNALlsdiHSSHLLQQTIA------ALQANKFVQPL 293
Cdd:cd07652   22 KEFATFLKKRAAIEEEHARGLKKLARTTLDTYKRPDH--KQGSFSNAY----HSSLEFHEKLAdnglrfAKALNEMSDEL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  294 LGRKNEMEKQRKEIKDLWKQQQNKLLETETALKKAKLLCMQRQDEYEKAKSSmfraeEEQLSSSVGLAKnlNKQLEKrrr 373
Cdd:cd07652   96 SSLAKTVEKSRKSIKETGKRAEKKVQDAEAAAEKAKARYDSLADDLERVKTG-----DPGKKLKFGLKG--NKSAAQ--- 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81900344  374 LEEEALQKVEEANEHYKVCVTNVEERRNDLENTKR-EILTQLRTLVFQCDltlKAVTVNLFHMQ 436
Cdd:cd07652  166 HEDELLRKVQAADQDYASKVNAAQALRQELLSRHRpEAVKDLFDLILEID---AALRLQYQKYA 226
 
Name Accession Description Interval E-value
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 671-883 1.40e-123

RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of PARG1 (PTPL1-associated RhoGAP1). PARG1 was originally cloned as an interaction partner of PTPL1, an intracellular protein-tyrosine phosphatase. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. 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: 239874  Cd Length: 211  Bit Score: 380.31  E-value: 1.40e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  671 FGAEFIQVAKKEPDGIPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLVDISEFSSHDICDVLKLYLR 750
Cdd:cd04409    1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLKLYLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  751 QLPEPFILFRLYKEFIDLAKEIQHVNEEQEAKKDSpeDKKHPHVSIEVNRILLKSKDLLRQLPASHFNSLHYLIAHLRRV 830
Cdd:cd04409   81 QLPEPLILFRLYNEFIGLAKESQHVNETQEAKKNS--DKKWPNMCTELNRILLKSKDLLRQLPAPNYNTLQFLIVHLHRV 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 81900344  831 VDHAEENKMNSKNLGVIFGPTLIRPRPTTAPVTISSLAEYSNQARLVEFLITY 883
Cdd:cd04409  159 SEQAEENKMSASNLGIIFGPTLIRPRPTDATVSLSSLVDYPHQARLVELLITY 211
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 686-884 3.51e-54

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 186.70  E-value: 3.51e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344     686 IPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLV-DISEFSSHDICDVLKLYLRQLPEPFILFRLYKE 764
Cdd:smart00324    3 IPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDlDLSEYDVHDVAGLLKLFLRELPEPLITYELYEE 82

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344     765 FIDLAKeiqhVNEEQEAKKdspedkkhphvsievnrillKSKDLLRQLPASHFNSLHYLIAHLRRVVDHAEENKMNSKNL 844
Cdd:smart00324   83 FIEAAK----LEDETERLR--------------------ALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNL 138

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 81900344     845 GVIFGPTLIRPRPTTAPvtisSLAEYSNQARLVEFLITYS 884
Cdd:smart00324  139 AIVFGPTLLRPPDGEVA----SLKDIRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 687-857 2.43e-42

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 459875  Cd Length: 148  Bit Score: 151.54  E-value: 2.43e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344    687 PFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLV-DISEFSSHDICDVLKLYLRQLPEPFILFRLYKEF 765
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDlDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344    766 IDLAKeiqhvneeqeakKDSPEDKKHphvsievnrillKSKDLLRQLPASHFNSLHYLIAHLRRVVDHAEENKMNSKNLG 845
Cdd:pfam00620   81 IEAAK------------LPDEEERLE------------ALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLA 136

                          170
                   ....*....|..
gi 81900344    846 VIFGPTLIRPRP 857
Cdd:pfam00620  137 IVFGPTLLRPPD 148
C1_GMIP-like cd20816
protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP) ...
 613-663 1.58e-23

protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP)-like family; The GMIP-like family includes GMIP, Rho GTPase-activating protein 29 (ARHGAP29) and Rho GTPase-activating protein 45 (ARHGAP45). GMIP is a RhoA-specific GTPase-activating protein that acts as a key factor in saltatory neuronal migration. It associates with the Rab27a effector JFC1 and modulates vesicular transport and exocytosis. ARHGAP29, also called PTPL1-associated RhoGAP protein 1 (PARG1) or Rho-type GTPase-activating protein 29, is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. It has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. ARHGAP29 may act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, ARHGAP29 suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis. ARHGAP45, also called minor histocompatibility antigen HA-1 (mHag HA-1), is a Rac-GAP (GTPase-Activating Protein) in endothelial cells. It acts as a novel regulator of endothelial integrity. ARHGAP45 contains a GTPase activator for the Rho-type GTPases (RhoGAP) domain that would be able to negatively regulate the actin cytoskeleton as well as cell spreading. However, it also contains N-terminally a BAR-domin which can play an autoinhibitory effect on this RhoGAP activity. Members of this family contain a zinc-binding C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410366  Cd Length: 51  Bit Score: 94.25  E-value: 1.58e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 81900344  613 LTHKFRKLRSPTKCRDCDGIVMFPGVECEECLLVCHRKCLENLVIICGHQK 663
Cdd:cd20816    1 QTHRFRRLRTPSKCRECDSYVYFNGAECEECGLACHKKCLETLAIQCGHKR 51
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
 220-436 6.44e-11

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho GTPase activating protein Rgd1 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Saccharomyces cerevisiae Rgd1 is a GTPase activating protein (GAP) with activity towards Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively. At low pH, S. cerevisiae Rgd1 is required for cell survival and the activation of the protein kinase C pathway, which is important in cell integrity and the maintenance of cell shape. It contains an N-terminal F-BAR domain and a C-terminal Rho GAP domain. The F-BAR domain of S. cerevisiae Rgd1 binds to phosphoinositides and plays an important role in the localization of the protein to the bud tip/neck during the cell cycle. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153336 [Multi-domain]  Cd Length: 234  Bit Score: 63.91  E-value: 6.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  220 KNIVSWVEKKLNLELESTRNIVKLAEATRSSIGIQEFmpLQSLFTNALlsdiHSSHLLQQTIA------ALQANKFVQPL 293
Cdd:cd07652   22 KEFATFLKKRAAIEEEHARGLKKLARTTLDTYKRPDH--KQGSFSNAY----HSSLEFHEKLAdnglrfAKALNEMSDEL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  294 LGRKNEMEKQRKEIKDLWKQQQNKLLETETALKKAKLLCMQRQDEYEKAKSSmfraeEEQLSSSVGLAKnlNKQLEKrrr 373
Cdd:cd07652   96 SSLAKTVEKSRKSIKETGKRAEKKVQDAEAAAEKAKARYDSLADDLERVKTG-----DPGKKLKFGLKG--NKSAAQ--- 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81900344  374 LEEEALQKVEEANEHYKVCVTNVEERRNDLENTKR-EILTQLRTLVFQCDltlKAVTVNLFHMQ 436
Cdd:cd07652  166 HEDELLRKVQAADQDYASKVNAAQALRQELLSRHRpEAVKDLFDLILEID---AALRLQYQKYA 226
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 614-659 4.36e-08

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 50.54  E-value: 4.36e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 81900344     614 THKFRKLRSPTKC---RDCDGIVMFPGVECEECLLVCHRKCLENLVIIC 659
Cdd:smart00109    2 KHVFRTFTKPTFCcvcRKSIWGSFKQGLRCSECKVKCHKKCADKVPKAC 50
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 615-660 3.54e-07

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 48.21  E-value: 3.54e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 81900344    615 HKF--RKLRSPTKCRDCDGIVMF---PGVECEECLLVCHRKCLENLVIICG 660
Cdd:pfam00130    1 HHFvhRNFKQPTFCDHCGEFLWGlgkQGLKCSWCKLNVHKRCHEKVPPECG 51
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 286-417 6.38e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 6.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344    286 ANKFVQPLLGRKNEMEKQRKEIkdlwKQQQNKLLETETALKKAKllcmQRQDEYEKAKSSMfRAEEEQLSSSVGLAKNLN 365
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKI----EELEEKIAELEKALAELR----KELEELEEELEQL-RKELEELSRQISALRKDL 735

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 81900344    366 KQLEKRRRLEEEALQKVEEANEHYKVCVTNVEERRNDLENTKREILTQLRTL 417
Cdd:TIGR02168  736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
PTZ00121 PTZ00121
MAEBL; Provisional
 296-409 3.63e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344   296 RKNEMEKQRKEIKDLWKQQQNKLLETETALKKAKLlcmQRQDEYEKAKSSMFR-AEEEQLSSSVGLAKNLN--KQLEKRR 372
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE---AKKAEEDKKKAEEAKkAEEDEKKAAEALKKEAEeaKKAEELK 1708

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 81900344   373 RLEEEALQKVEEANEHYKVCVTNVEERRNDLENTKRE 409
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK 1745
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 200-275 1.62e-03

Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also known as the RAEYL motif or the S. pombe Cdc15 N-terminal domain.


Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 38.86  E-value: 1.62e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344     200 KNTDSIELALSYAKTWSKYTKNIVSWVEKKLNLELESTRNIVKLAEATRSSIGIQ-EFMPLQSLFTNAL-----LSDIHS 273
Cdd:smart00055    6 ELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKLRAVRDTEpEYGSLSKAWEVLLsetdaLAKQHL 85


                    ..
gi 81900344     274 SH 275
Cdd:smart00055   86 EL 87
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
277-462 2.11e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  277 LQQTIAALQANkfVQPLLGRKNEMEKQRKEIKDLWKQQQNKLLETETALKKAKLLCMQRQDEYEKAKssmfrAEEEQLSS 356
Cdd:COG4372   43 LQEELEQLREE--LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ-----EEAEELQE 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  357 SVglaknlnKQLEKRRRLEEEALQKVEEANEHYKVCVTNVEERRNDLENTKREILTQLRTLVFQCDLTLKAVTVNLFHMQ 436
Cdd:COG4372  116 EL-------EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188

                        170       180
                 ....*....|....*....|....*.
gi 81900344  437 QLQAASLANSLQSLCDSAKLYDPGQE 462
Cdd:COG4372  189 LKEANRNAEKEEELAEAEKLIESLPR 214
 
Name Accession Description Interval E-value
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 671-883 1.40e-123

RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of PARG1 (PTPL1-associated RhoGAP1). PARG1 was originally cloned as an interaction partner of PTPL1, an intracellular protein-tyrosine phosphatase. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. 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: 239874  Cd Length: 211  Bit Score: 380.31  E-value: 1.40e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  671 FGAEFIQVAKKEPDGIPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLVDISEFSSHDICDVLKLYLR 750
Cdd:cd04409    1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLKLYLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  751 QLPEPFILFRLYKEFIDLAKEIQHVNEEQEAKKDSpeDKKHPHVSIEVNRILLKSKDLLRQLPASHFNSLHYLIAHLRRV 830
Cdd:cd04409   81 QLPEPLILFRLYNEFIGLAKESQHVNETQEAKKNS--DKKWPNMCTELNRILLKSKDLLRQLPAPNYNTLQFLIVHLHRV 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 81900344  831 VDHAEENKMNSKNLGVIFGPTLIRPRPTTAPVTISSLAEYSNQARLVEFLITY 883
Cdd:cd04409  159 SEQAEENKMSASNLGIIFGPTLIRPRPTDATVSLSSLVDYPHQARLVELLITY 211
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 671-883 2.41e-120

RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein) and PARG1 (PTPL1-associated RhoGAP1). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. 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: 239843  Cd Length: 203  Bit Score: 371.37  E-value: 2.41e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  671 FGAEFIQVAKKEPDGIPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLVDISEFSSHDICDVLKLYLR 750
Cdd:cd04378    1 FGVDFSQVPRDFPDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  751 QLPEPFILFRLYKEFIDLAKEIQHVNEEQEAkkdspedkkhPHVSIEVNRILLKSKDLLRQLPASHFNSLHYLIAHLRRV 830
Cdd:cd04378   81 QLPEPLILFRLYNDFIALAKEIQRDTEEDKA----------PNTPIEVNRIIRKLKDLLRQLPASNYNTLQHLIAHLYRV 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 81900344  831 VDHAEENKMNSKNLGVIFGPTLIRPRPTTAPVTISSLAEYSNQARLVEFLITY 883
Cdd:cd04378  151 AEQFEENKMSPNNLGIVFGPTLIRPRPGDADVSLSSLVDYGYQARLVEFLITN 203
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 671-881 6.31e-66

RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. 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: 239873  Cd Length: 200  Bit Score: 221.23  E-value: 6.31e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  671 FGAEFIQVAKKEPDGIPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLVDISEFSSHDICDVLKLYLR 750
Cdd:cd04408    1 FGVDFSQLPRDFPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  751 QLPEPFILFRLYKEFIDLAKEIQhvneeqeakKDSPEDKKHPHVSIEVNRILlksKDLLRQLPASHFNSLHYLIAHLRRV 830
Cdd:cd04408   81 ELPEPVLPFQLYDDFIALAKELQ---------RDSEKAAESPSIVENIIRSL---KELLGRLPVSNYNTLRHLMAHLYRV 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 81900344  831 VDHAEENKMNSKNLGVIFGPTLIRPRPTTApVTISSLAEYSNQARLVEFLI 881
Cdd:cd04408  149 AERFEDNKMSPNNLGIVFGPTLLRPLVGGD-VSMICLLDTGYQAQLVEFLI 198
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 686-884 3.51e-54

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 186.70  E-value: 3.51e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344     686 IPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLV-DISEFSSHDICDVLKLYLRQLPEPFILFRLYKE 764
Cdd:smart00324    3 IPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDlDLSEYDVHDVAGLLKLFLRELPEPLITYELYEE 82

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344     765 FIDLAKeiqhVNEEQEAKKdspedkkhphvsievnrillKSKDLLRQLPASHFNSLHYLIAHLRRVVDHAEENKMNSKNL 844
Cdd:smart00324   83 FIEAAK----LEDETERLR--------------------ALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNL 138

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 81900344     845 GVIFGPTLIRPRPTTAPvtisSLAEYSNQARLVEFLITYS 884
Cdd:smart00324  139 AIVFGPTLLRPPDGEVA----SLKDIRHQNTVIEFLIENA 174
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 687-883 7.14e-48

RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like small GTPases. Small GTPases (G proteins) cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when bound to GDP. The Rho family of small G proteins, which includes Cdc42Hs, activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. G proteins 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. The RhoGAPs are one of the major classes of regulators of Rho G proteins.


Pssm-ID: 238090 [Multi-domain]  Cd Length: 169  Bit Score: 168.25  E-value: 7.14e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  687 PFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLVDISEFSSHDICDVLKLYLRQLPEPFILFRLYKEFI 766
Cdd:cd00159    1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  767 DLAKEIQHVNEEQEAKKdspedkkhphvsievnrillkskdLLRQLPASHFNSLHYLIAHLRRVVDHAEENKMNSKNLGV 846
Cdd:cd00159   81 ELAKIEDEEERIEALKE------------------------LLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAI 136

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 81900344  847 IFGPTLIRPRPTtapvTISSLAEYSNQARLVEFLITY 883
Cdd:cd00159  137 VFAPTLLRPPDS----DDELLEDIKKLNEIVEFLIEN 169
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 687-857 2.43e-42

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 459875  Cd Length: 148  Bit Score: 151.54  E-value: 2.43e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344    687 PFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLV-DISEFSSHDICDVLKLYLRQLPEPFILFRLYKEF 765
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDlDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344    766 IDLAKeiqhvneeqeakKDSPEDKKHphvsievnrillKSKDLLRQLPASHFNSLHYLIAHLRRVVDHAEENKMNSKNLG 845
Cdd:pfam00620   81 IEAAK------------LPDEEERLE------------ALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLA 136

                          170
                   ....*....|..
gi 81900344    846 VIFGPTLIRPRP 857
Cdd:pfam00620  137 IVFGPTLLRPPD 148
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 671-888 1.15e-36

RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of chimaerins. Chimaerins are a family of phorbolester- and diacylglycerol-responsive GAPs specific for the Rho-like GTPase Rac. Chimaerins exist in two alternative splice forms that each contain a C-terminal GAP domain, and a central C1 domain which binds phorbol esters, inducing a conformational change that activates the protein; one splice form is lacking the N-terminal Src homology-2 (SH2) domain. 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: 239837 [Multi-domain]  Cd Length: 194  Bit Score: 137.26  E-value: 1.15e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  671 FGAEFIQVAKKEPDGIPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLVDISEFSSHD---ICDVLKL 747
Cdd:cd04372    1 YGCDLTTLVKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKADISATVYPDinvITGALKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  748 YLRQLPEPFILFRLYKEFIDLAKeIQHVNEEQEAKKDSpedkkhphvsievnrillkskdlLRQLPASHFNSLHYLIAHL 827
Cdd:cd04372   81 YFRDLPIPVITYDTYPKFIDAAK-ISNPDERLEAVHEA-----------------------LMLLPPAHYETLRYLMEHL 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81900344  828 RRVVDHAEENKMNSKNLGVIFGPTLIRPRPTTAPVTISSLAEysnQARLVEFLITYSQKIF 888
Cdd:cd04372  137 KRVTLHEKDNKMNAENLGIVFGPTLMRPPEDSALTTLNDMRY---QILIVQLLITNEDVLF 194
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 671-888 3.38e-33

RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD1-like proteins. Yeast Rgd1 is a GAP protein for Rho3 and Rho4 and plays a role in low-pH response. 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: 239863  Cd Length: 192  Bit Score: 127.13  E-value: 3.38e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  671 FGAEFIQVAKKEPDGIPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLVDI--SEFSSHDI---CDVL 745
Cdd:cd04398    1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLLisPEDYESDIhsvASLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  746 KLYLRQLPEPFILFRLYKEFIDLAKeiqhvNEEQEAKKDspedKKHphvsievnrillkskDLLRQLPASHFNSLHYLIA 825
Cdd:cd04398   81 KLFFRELPEPLLTKALSREFIEAAK-----IEDESRRRD----ALH---------------GLINDLPDANYATLRALMF 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81900344  826 HLRRVVDHAEENKMNSKNLGVIFGPTLIRPRPTtapvtisSLAEYSNQARLVEFLITYSQKIF 888
Cdd:cd04398  137 HLARIKEHESVNRMSVNNLAIIWGPTLMNAAPD-------NAADMSFQSRVIETLLDNAYQIF 192
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 671-882 1.44e-32

RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP27 (also called CAMGAP1), ARHGAP15, 12 and 9-like proteins; This subgroup of ARHGAPs are multidomain proteins that contain RhoGAP, PH, SH3 and WW domains. Most members that are studied show GAP activity towards Rac1, some additionally show activity towards Cdc42. 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: 239868 [Multi-domain]  Cd Length: 187  Bit Score: 125.20  E-value: 1.44e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  671 FGAEFIQVAKKEPDGIPFVLKICASEIENRALCLQGIYRVCGNKIKTEKL-CQA-LENGMHLVDISEFSSHDICDVLKLY 748
Cdd:cd04403    1 FGCHLEALCQRENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLrFAVdHDEKLDLDDSKWEDIHVITGALKLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  749 LRQLPEPFILFRLYKEFIdlakeiqhvneeqEAKKDSPEDKKHPHVsievnrillksKDLLRQLPASHFNSLHYLIAHLR 828
Cdd:cd04403   81 FRELPEPLFPYSLFNDFV-------------AAIKLSDYEQRVSAV-----------KDLIKSLPKPNHDTLKMLFRHLC 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 81900344  829 RVVDHAEENKMNSKNLGVIFGPTLIRPRPTTAPVTISSLaeYSNQarLVEFLIT 882
Cdd:cd04403  137 RVIEHGEKNRMTTQNLAIVFGPTLLRPEQETGNIAVHMV--YQNQ--IVELILL 186
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 686-888 4.54e-32

RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP21-like proteins. ArhGAP21 is a multi-domain protein, containing RhoGAP, PH and PDZ domains, and is believed to play a role in the organization of the cell-cell junction complex. It has been shown to function as a GAP of Cdc42 and RhoA, and to interact with alpha-catenin and Arf6. 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: 239860  Cd Length: 196  Bit Score: 124.05  E-value: 4.54e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  686 IPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLVDISEFSSHD---ICDVLKLYLRQLPEPFILFRLY 762
Cdd:cd04395   18 VPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGFDIDLQDPRWRDvnvVSSLLKSFFRKLPEPLFTNELY 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  763 KEFIDlakeiqhvneeqeakkdspEDKKHPHVsievNRiLLKSKDLLRQLPASHFNSLHYLIAHLRRVVDHAEENKMNSK 842
Cdd:cd04395   98 PDFIE-------------------ANRIEDPV----ER-LKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPR 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 81900344  843 NLGVIFGPTLIRPRPTTAPVTISSLaeySNQARLVEFLITYSQKIF 888
Cdd:cd04395  154 NLAIVFGPTLVRTSDDNMETMVTHM---PDQCKIVETLIQHYDWFF 196
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
 685-881 1.70e-30

RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase regulator associated with focal adhesion kinase); Graf is a multi-domain protein, containing SH3 and PH domains, that binds focal adhesion kinase and influences cytoskeletal changes mediated by Rho proteins. Graf exhibits GAP activity toward RhoA and Cdc42, but only weakly activates Rac1. 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: 239839  Cd Length: 203  Bit Score: 119.81  E-value: 1.70e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  685 GIPFVLKiCASEIENRALCLQGIYRVCGNKIKTEKLCQAL-------ENGMHLvDISEFSSHDICDVLKLYLRQLPEPFI 757
Cdd:cd04374   28 GFKFVRK-CIEAVETRGINEQGLYRVVGVNSKVQKLLSLGldpktstPGDVDL-DNSEWEIKTITSALKTYLRNLPEPLM 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  758 LFRLYKEFIDLAKeiqhvNEEQEAKkdspedkkhphvsieVNRIllksKDLLRQLPASHFNSLHYLIAHLRRVVDHAEEN 837
Cdd:cd04374  106 TYELHNDFINAAK-----SENLESR---------------VNAI----HSLVHKLPEKNREMLELLIKHLTNVSDHSKKN 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 81900344  838 KMNSKNLGVIFGPTLIRPRPTtapvTISSLAEYSNQARLVEFLI 881
Cdd:cd04374  162 LMTVSNLGVVFGPTLLRPQEE----TVAAIMDIKFQNIVVEILI 201
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 684-883 8.17e-30

RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in ARAPs. ARAPs (also known as centaurin deltas) contain, besides the RhoGAP domain, an Arf GAP, ankyrin repeat ras-associating, and PH domains. Since their ArfGAP activity is PIP3-dependent, ARAPs are considered integration points for phosphoinositide, Arf and Rho signaling. 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: 239850  Cd Length: 184  Bit Score: 117.02  E-value: 8.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  684 DGIPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALEN---GMHLvDISEFSSHDICDVLKLYLRQLPEPFILFR 760
Cdd:cd04385   13 NDIPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKdarSVQL-REGEYTVHDVADVLKRFLRDLPDPLLTSE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  761 LYKEFIDLAkEIQHVNEEqeakkdspedkkhphvsievnriLLKSKDLLRQLPASHFNSLHYLIAHLRRVVDHAEENKMN 840
Cdd:cd04385   92 LHAEWIEAA-ELENKDER-----------------------IARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMS 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 81900344  841 SKNLGVIFGPTLIRPRPttapvtiSSLAEYSNQARLVEFLITY 883
Cdd:cd04385  148 VHNLALVFGPTLFQTDE-------HSVGQTSHEVKVIEDLIDN 183
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 671-881 1.37e-26

RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in class IX myosins. Class IX myosins contain a characteristic head domain, a neck domain, a tail domain which contains a C6H2-zinc binding motif and a RhoGAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. 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: 239842  Cd Length: 186  Bit Score: 107.91  E-value: 1.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  671 FGAEFIQVAKkEPDGIPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLVDISEFSSHDICDVLKLYLR 750
Cdd:cd04377    1 FGVSLSSLTS-EDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLKQWLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  751 QLPEPFILFRLYKEFIDlAKEIQhvnEEQEAkkdspedkkhphvsievnriLLKSKDLLRQLPASHFNSLHYLIAHLRRV 830
Cdd:cd04377   80 ELPEPLMTFELYENFLR-AMELE---EKQER--------------------VRALYSVLEQLPRANLNTLERLIFHLVRV 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 81900344  831 VDHAEENKMNSKNLGVIFGPTLIRPRPTTAPVTisSLAEYSNQARLVEFLI 881
Cdd:cd04377  136 ALQEEVNRMSANALAIVFAPCILRCPDTADPLQ--SLQDVSKTTTCVETLI 184
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 686-880 3.20e-26

RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in MgcRacGAP proteins. MgcRacGAP plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling. ii) after phosphorylation by aurora B MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain a N-terminal C1-like domain, and a C-terminal RhoGAP domain. 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: 239847  Cd Length: 193  Bit Score: 106.99  E-value: 3.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  686 IPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLVDISEFSSHDICDVLKLYLRQLPEPFILFRLYKEF 765
Cdd:cd04382   17 IPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVDIHVICGCLKDFLRSLKEPLITFALWKEF 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  766 IDLAKEIQHVNEEQEAKKdspedkkhphvsievnrillkskdLLRQLPASHFNSLHYLIAHLRRVVdHAEENKMNSKNLG 845
Cdd:cd04382   97 MEAAEILDEDNSRAALYQ------------------------AISELPQPNRDTLAFLILHLQRVA-QSPECKMDINNLA 151

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 81900344  846 VIFGPTLI-RPRPTTAPVTIssLAEYSNQARLVEFL 880
Cdd:cd04382  152 RVFGPTIVgYSVPNPDPMTI--LQDTVRQPRVVERL 185
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 669-888 9.10e-26

RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p50RhoGAP-like proteins; p50RhoGAP, also known as RhoGAP-1, contains a C-terminal RhoGAP domain and an N-terminal Sec14 domain which binds phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). It is ubiquitously expressed and preferentially active on Cdc42. This subgroup also contains closely related ARHGAP8. 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: 239869 [Multi-domain]  Cd Length: 195  Bit Score: 105.88  E-value: 9.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  669 HIFGA--EFIQVAKKEPDGIPFVLKICASEIENRALCLQGIYRVCGNkIKTEKLCQALENGMHLVDISEF-SSHDICDVL 745
Cdd:cd04404    4 QQFGVslQFLKEKNPEQEPIPPVVRETVEYLQAHALTTEGIFRRSAN-TQVVKEVQQKYNMGEPVDFDQYeDVHLPAVIL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  746 KLYLRQLPEPFILFRLYKEFIDlakeIQHVNEEQEAKKdspedkkhphvsievnrillkSKDLLRQLPASHFNSLHYLIA 825
Cdd:cd04404   83 KTFLRELPEPLLTFDLYDDIVG----FLNVDKEERVER---------------------VKQLLQTLPEENYQVLKYLIK 137

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81900344  826 HLRRVVDHAEENKMNSKNLGVIFGPTLIRPRPTTApvTISSLAEYSNqarLVEFLITYSQKIF 888
Cdd:cd04404  138 FLVQVSAHSDQNKMTNSNLAVVFGPNLLWAKDASM--SLSAINPINT---FTKFLLDHQDEIF 195
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 670-881 1.94e-24

RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of CdGAP-like proteins; CdGAP contains an N-terminal RhoGAP domain and a C-terminal proline-rich region, and it is active on both Cdc42 and Rac1 but not RhoA. CdGAP is recruited to focal adhesions via the interaction with the scaffold protein actopaxin (alpha-parvin). 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: 239849 [Multi-domain]  Cd Length: 195  Bit Score: 102.20  E-value: 1.94e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  670 IFGAEFIQVAKKEPDGIPFVLKICASEIENRALcLQGIYRVCGNKIKTEKLCQALENGmHLVDISEFS-SHDICDV---L 745
Cdd:cd04384    2 VFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGI-VDGIYRLSGIASNIQRLRHEFDSE-QIPDLTKDVyIQDIHSVsslC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  746 KLYLRQLPEPFILFRLYKEFIDlakeiqhvneeqEAKKDSPEDKkhphvsievnriLLKSKDLLRQLPASHFNSLHYLIA 825
Cdd:cd04384   80 KLYFRELPNPLLTYQLYEKFSE------------AVSAASDEER------------LEKIHDVIQQLPPPHYRTLEFLMR 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 81900344  826 HLRRVVDHAEENKMNSKNLGVIFGPTLIRPRPT--TAPVTISSLAEYSNQARLVEFLI 881
Cdd:cd04384  136 HLSRLAKYCSITNMHAKNLAIVWAPNLLRSKQIesACFSGTAAFMEVRIQSVVVEFIL 193
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 671-865 5.76e-24

RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in SYD-1_like proteins. Syd-1, first identified and best studied in C.elegans, has been shown to play an important role in neuronal development by specifying axonal properties. 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: 239844  Cd Length: 207  Bit Score: 101.00  E-value: 5.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  671 FGAEFIQVAKKEPDG--IPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLVDISEFSSHD---ICDVL 745
Cdd:cd04379    1 FGVPLSRLVEREGESrdVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELSEELYPDinvITGVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  746 KLYLRQLPEPFILFRLYKEFIDLakeiqhvneeqeAKKDSPEDKkhphvsiEVNRILLKSkdLLRQLPASHFNSLHYLIA 825
Cdd:cd04379   81 KDYLRELPEPLITPQLYEMVLEA------------LAVALPNDV-------QTNTHLTLS--IIDCLPLSAKATLLLLLD 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 81900344  826 HLRRVVDHAEENKMNSKNLGVIFGPTLIRPRPTTAPVTIS 865
Cdd:cd04379  140 HLSLVLSNSERNKMTPQNLAVCFGPVLMFCSQEFSRYGIS 179
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 671-885 1.30e-23

RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr (breakpoint cluster region protein)-like proteins. Bcr is a multidomain protein with a variety of enzymatic functions. It contains a RhoGAP and a Rho GEF domain, a Ser/Thr kinase domain, an N-terminal oligomerization domain, and a C-terminal PDZ binding domain, in addition to PH and C2 domains. Bcr is a negative regulator of: i) RacGTPase, via the Rho GAP domain, ii) the Ras-Raf-MEK-ERK pathway, via phosphorylation of the Ras binding protein AF-6, and iii) the Wnt signaling pathway through binding beta-catenin. Bcr can form a complex with beta-catenin and Tcf1. The Wnt signaling pathway is involved in cell proliferation, differentiation, and cell renewal. Bcr was discovered as a fusion partner of Abl. The Bcr-Abl fusion is characteristic for a large majority of chronic myelogenous leukemias (CML). 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: 239852 [Multi-domain]  Cd Length: 196  Bit Score: 100.00  E-value: 1.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  671 FGAEFIQVAKKEPDGIPFVLKICASEIENRALCLQGIYRVCG--NKIKTEKLCQALENGMHLVDISEFSSHDICDVLKLY 748
Cdd:cd04387    1 FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGvaTDIQALKAAFDTNNKDVSVMLSEMDVNAIAGTLKLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  749 LRQLPEPFILFRLYKEF---IDLAKEIqhvneeqeAKKDSpedkkhphvsievnriLLkskDLLRQLPASHFNSLHYLIA 825
Cdd:cd04387   81 FRELPEPLFTDELYPNFaegIALSDPV--------AKESC----------------ML---NLLLSLPDPNLVTFLFLLH 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81900344  826 HLRRVVDHAEENKMNSKNLGVIFGPTLIRP-----RPTTAPVTISSLAEYSNQarlVEFLITYSQ 885
Cdd:cd04387  134 HLKRVAEREEVNKMSLHNLATVFGPTLLRPsekesKIPTNTMTDSWSLEVMSQ---VQVLLYFLQ 195
C1_GMIP-like cd20816
protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP) ...
 613-663 1.58e-23

protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP)-like family; The GMIP-like family includes GMIP, Rho GTPase-activating protein 29 (ARHGAP29) and Rho GTPase-activating protein 45 (ARHGAP45). GMIP is a RhoA-specific GTPase-activating protein that acts as a key factor in saltatory neuronal migration. It associates with the Rab27a effector JFC1 and modulates vesicular transport and exocytosis. ARHGAP29, also called PTPL1-associated RhoGAP protein 1 (PARG1) or Rho-type GTPase-activating protein 29, is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. It has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. ARHGAP29 may act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, ARHGAP29 suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis. ARHGAP45, also called minor histocompatibility antigen HA-1 (mHag HA-1), is a Rac-GAP (GTPase-Activating Protein) in endothelial cells. It acts as a novel regulator of endothelial integrity. ARHGAP45 contains a GTPase activator for the Rho-type GTPases (RhoGAP) domain that would be able to negatively regulate the actin cytoskeleton as well as cell spreading. However, it also contains N-terminally a BAR-domin which can play an autoinhibitory effect on this RhoGAP activity. Members of this family contain a zinc-binding C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410366  Cd Length: 51  Bit Score: 94.25  E-value: 1.58e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 81900344  613 LTHKFRKLRSPTKCRDCDGIVMFPGVECEECLLVCHRKCLENLVIICGHQK 663
Cdd:cd20816    1 QTHRFRRLRTPSKCRECDSYVYFNGAECEECGLACHKKCLETLAIQCGHKR 51
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 670-890 6.67e-23

RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Nadrin-like proteins. Nadrin, also named Rich-1, has been shown to be involved in the regulation of Ca2+-dependent exocytosis in neurons and recently has been implicated in tight junction maintenance in mammalian epithelium. 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: 239851  Cd Length: 203  Bit Score: 97.91  E-value: 6.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  670 IFGA---EFIQVAKKEpdgIPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLVDISEFSS--HDICDV 744
Cdd:cd04386    4 VFGTpleEHLKRTGRE---IALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSLPLDEFYSdpHAVASA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  745 LKLYLRQLPEPFILFRLYKEFIdlakeiQHVNEEQEAKKdspedkkhphvsievnriLLKSKDLLRQLPASHFNSLHYLI 824
Cdd:cd04386   81 LKSYLRELPDPLLTYNLYEDWV------QAANKPDEDER------------------LQAIWRILNKLPRENRDNLRYLI 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81900344  825 AHLRRVVDHAEENKMNSKNLGVIFGPTLIRPRpTTAPVTISSLAEYSNQARLVEFLITYSQKIFDG 890
Cdd:cd04386  137 KFLSKLAQKSDENKMSPSNIAIVLAPNLLWAK-NEGSLAEMAAGTSVHVVAIVELIISHADWFFPG 201
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 686-881 1.29e-22

RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXB. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons 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: 239872 [Multi-domain]  Cd Length: 186  Bit Score: 96.60  E-value: 1.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  686 IPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLVDISEFSSHDICDVLKLYLRQLPEPFILFRLYKEF 765
Cdd:cd04407   15 VPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRELPEPLMTFAQYNDF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  766 IdLAKEIQhvnEEQEAkkdspedkkhphvsievnriLLKSKDLLRQLPASHFNSLHYLIAHLRRVVDHAEENKMNSKNLG 845
Cdd:cd04407   95 L-RAVELP---EKQEQ--------------------LQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALA 150

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 81900344  846 VIFGPTLIRPRPTTAPVTisSLAEYSNQARLVEFLI 881
Cdd:cd04407  151 IVFAPCLLRCPDSSDPLT--SMKDVAKTTTCVEMLI 184
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 686-855 7.24e-21

RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p190-like proteins. p190, also named RhoGAP5, plays a role in neuritogenesis and axon branch stability. p190 shows a preference for Rho, over Rac and Cdc42, and consists of an N-terminal GTPase domain and a C-terminal GAP domain. The central portion of p190 contains important regulatory phosphorylation sites. 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: 239838  Cd Length: 185  Bit Score: 91.36  E-value: 7.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  686 IPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGmHLVDISE--FSSHDICDVLKLYLRQLPEPFILFRLYK 763
Cdd:cd04373   15 IPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQD-HNLDLVSkdFTVNAVAGALKSFFSELPDPLIPYSMHL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  764 EFidlaKEIQHVNEEQEAkkdspedkkhphvsievnriLLKSKDLLRQLPASHFNSLHYLIAHLRRVVDHAEENKMNSKN 843
Cdd:cd04373   94 EL----VEAAKINDREQR--------------------LHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSEN 149

                        170
                 ....*....|..
gi 81900344  844 LGVIFGPTLIRP 855
Cdd:cd04373  150 LSICFWPTLMRP 161
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 681-888 1.03e-20

RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP18-like proteins. The function of ArhGAP18 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 several orders of magnitude.


Pssm-ID: 239856  Cd Length: 216  Bit Score: 92.02  E-value: 1.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  681 KEPDG--IPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALEN--GMHLVDISEFSSHDICDVLKLYLRQLPEPF 756
Cdd:cd04391   15 KKVPGskVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAkfYEGTFLWDQVKQHDAASLLKLFIRELPQPL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  757 ilfrLYKEFIDLAKEIQHVneeqeakkdspedkkhPHVSIEVNRILLkskdLLRQLPASHFNSLHYLIAHLRRVVDHAEE 836
Cdd:cd04391   95 ----LTVEYLPAFYSVQGL----------------PSKKDQLQALNL----LVLLLPEANRDTLKALLEFLQKVVDHEEK 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 81900344  837 NKMNSKNLGVIFGPTLIRPRpTTAPVTISSLAEYSNQA----RLVEFLITYSQKIF 888
Cdd:cd04391  151 NKMNLWNVAMIMAPNLFPPR-GKHSKDNESLQEEVNMAagcaNIMRLLIRYQDLLW 205
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 670-857 6.18e-20

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: 89.06  E-value: 6.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  670 IFGA--EFIQVAKKEPDGIPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHlVDISEFSshDICDV--- 744
Cdd:cd04393    2 VFGVplQELQQAGQPENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEE-VDLSKEA--DVCSAasl 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  745 LKLYLRQLPEPFILFRLYKEFIDLAKEIQhVNEEQEAkkdspedkkhphvsievnrillKSKDLLRQLPASHFNSLHYLI 824
Cdd:cd04393   79 LRLFLQELPEGLIPASLQIRLMQLYQDYN-GEDEFGR----------------------KLRDLLQQLPPVNYSLLKFLC 135

                        170       180       190
                 ....*....|....*....|....*....|...
gi 81900344  825 AHLRRVVDHAEENKMNSKNLGVIFGPTLIRPRP 857
Cdd:cd04393  136 HFLSNVASQHHENRMTAENLAAVFGPDVFHVYT 168
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 705-888 2.48e-19

RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP19-like proteins. The function of ArhGAP19 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 several orders of magnitude.


Pssm-ID: 239857  Cd Length: 208  Bit Score: 87.90  E-value: 2.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  705 QGIYRVCGNKIKTEKLCQALENGMHL-VDISEFSSHDICDVLKLYLRQLPEPFILFRLYKEFIDLAkEIQHVNEEQEakK 783
Cdd:cd04392   27 EGLFRKPGNSARQQELRDLLNSGTDLdLESGGFHAHDCATVLKGFLGELPEPLLTHAHYPAHLQIA-DLCQFDEKGN--K 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  784 DSPEDKKHphvSIEVNRILLkskdLLrqLPASHFNSLHYLIAHLRRVVDHAEENKMNSKNLGVIFGPTLIRPRPTTAPVT 863
Cdd:cd04392  104 TSAPDKER---LLEALQLLL----LL--LPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLICPRNLTPEDL 174

                        170       180
                 ....*....|....*....|....*
gi 81900344  864 ISSLAEYSNqarLVEFLITYSQKIF 888
Cdd:cd04392  175 HENAQKLNS---IVTFMIKHSQKLF 196
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
 670-862 4.26e-19

RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of fungal BEM3-like proteins. Bem3 is a GAP protein of Cdc42, and is specifically involved in the control of the initial assembly of the septin ring in yeast bud formation. 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: 239865 [Multi-domain]  Cd Length: 190  Bit Score: 86.64  E-value: 4.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  670 IFGAEFIQV----AKKEPD-GIPFVLKICASEIE-NRALCLQGIYRVCGNK--IKTEKLCQALENGMHLVDISE-FSSHD 740
Cdd:cd04400    1 IFGSPLEEAvelsSHKYNGrDLPSVVYRCIEYLDkNRAIYEEGIFRLSGSAsvIKQLKERFNTEYDVDLFSSSLyPDVHT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  741 ICDVLKLYLRQLPEPFILFRLYKEFidlakeiQHVNEEQEAKKDspedkkhphvsievnrILLKSKDLLRQLPASHFNSL 820
Cdd:cd04400   81 VAGLLKLYLRELPTLILGGELHNDF-------KRLVEENHDRSQ----------------RALELKDLVSQLPQANYDLL 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 81900344  821 HYLIAHLRRVVDHAEENKMNSKNLGVIFGPTLIRPRPTTAPV 862
Cdd:cd04400  138 YVLFSFLRKIIEHSDVNKMNLRNVCIVFSPTLNIPAGIFVLF 179
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 686-888 2.23e-18

RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP6-like proteins. ArhGAP6 shows GAP activity towards RhoA, but not towards Cdc42 and Rac1. ArhGAP6 is often deleted in microphthalmia with linear skin defects syndrome (MLS); MLS is a severe X-linked developmental disorder. 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: 239841  Cd Length: 206  Bit Score: 84.80  E-value: 2.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  686 IPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLVDISEFSSHDICDVLKLYLRQLPEPFILFRLYKEF 765
Cdd:cd04376    9 VPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENHSVHDVAALLKEFFRDMPDPLLPRELYTAF 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  766 IDLAKEiqhvneeqeakkdSPEDKkhphvsIEVNRILLKskdllrQLPASHFNSLHYLIAHLRRVVDHAEE--------- 836
Cdd:cd04376   89 IGTALL-------------EPDEQ------LEALQLLIY------LLPPCNCDTLHRLLKFLHTVAEHAADsidedgqev 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 81900344  837 --NKMNSKNLGVIFGPTLIR-PRPTTAPVTISSL--AEYSNQARLVEFLITYSQKIF 888
Cdd:cd04376  144 sgNKMTSLNLATIFGPNLLHkQKSGEREFVQASLriEESTAIINVVQTMIDNYEELF 200
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 670-887 3.48e-18

RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal SAC7 and BAG7-like proteins. Both proteins are GTPase activating proteins of Rho1, but differ functionally in vivo: SAC7, but not BAG7, is involved in the control of Rho1-mediated activation of the PKC-MPK1 pathway. 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: 239861  Cd Length: 225  Bit Score: 84.77  E-value: 3.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  670 IFG---AEFIQVAKKE-----PDG-------IPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHL---V 731
Cdd:cd04396    1 VFGvslEESLKYASVAisivdEDGeqyvygyIPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPDYgksF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  732 DISEFSSHDICDVLKLYLRQLPEPFILFRLYKEFIDLAKEIQHVNEEQEAKKDSPEDKkhphvsiEVNRILLKSKDLLRQ 811
Cdd:cd04396   81 DWDGYTVHDAASVLRRYLNNLPEPLVPLDLYEEFRNPLRKRPRILQYMKGRINEPLNT-------DIDQAIKEYRDLITR 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81900344  812 LPASHFNSLHYLIAHLRRVVDHAEENKMNSKNLGVIFGPTLI-RPRPTTAPvtisslAEYSNQARLVEFLITYSQKI 887
Cdd:cd04396  154 LPNLNRQLLLYLLDLLAVFARNSDKNLMTASNLAAIFQPGILsHPDHEMDP------KEYKLSRLVVEFLIEHQDKF 224
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 671-881 5.31e-18

RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXA. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. 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: 239871  Cd Length: 186  Bit Score: 83.51  E-value: 5.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  671 FGAEFIQVAKKEpDGIPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLVDISEFSSHDICDVLKLYLR 750
Cdd:cd04406    1 FGVELSRLTSED-RSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  751 QLPEPFILFRLYKEFIDlAKEIQHVNEeqeakkdspedkkhphvsievnrILLKSKDLLRQLPASHFNSLHYLIAHLRRV 830
Cdd:cd04406   80 DLPNPLMTFELYEEFLR-AMGLQERRE-----------------------TVRGVYSVIDQLSRTHLNTLERLIFHLVRI 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 81900344  831 VDHAEENKMNSKNLGVIFGPTLIRPRPTTAPvtISSLAEYSNQARLVEFLI 881
Cdd:cd04406  136 ALQEETNRMSANALAIVFAPCILRCPDTTDP--LQSVQDISKTTTCVELIV 184
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 700-888 1.28e-17

RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP20-like proteins. ArhGAP20, also known as KIAA1391 and RA-RhoGAP, contains a RhoGAP, a RA, and a PH domain, and ANXL repeats. ArhGAP20 is activated by Rap1 and induces inactivation of Rho, which in turn leads to neurite outgrowth. 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: 239867  Cd Length: 192  Bit Score: 82.35  E-value: 1.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  700 RALCLQGIYRVCGNKIKTEKLCQALENGMHlVDISEFSSHDICDVLKLYLRQLPEPFILFRLYKEFIDlakeiqhvneeq 779
Cdd:cd04402   29 KGPSTEGIFRRSANAKACKELKEKLNSGVE-VDLKAEPVLLLASVLKDFLRNIPGSLLSSDLYEEWMS------------ 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  780 eAKKDSPEDKKHPHVsievnrillksKDLLRQLPASHFNSLHYLIAHLRRVVDHAEENKMNSKNLGVIFGPTLIRPrPTT 859
Cdd:cd04402   96 -ALDQENEEEKIAEL-----------QRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLWP-PAS 162

                        170       180
                 ....*....|....*....|....*....
gi 81900344  860 APVTISSLaeySNQARLVEFLITYSQKIF 888
Cdd:cd04402  163 SELQNEDL---KKVTSLVQFLIENCQEIF 188
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 686-864 5.67e-17

RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP22, 24 and 25-like proteins; longer isoforms of these proteins contain an additional N-terminal pleckstrin homology (PH) domain. ARHGAP25 (KIA0053) has been identified as a GAP for Rac1 and Cdc42. Short isoforms (without the PH domain) of ARHGAP24, called RC-GAP72 and p73RhoGAP, and of ARHGAP22, called p68RacGAP, has been shown to be involved in angiogenesis and endothelial cell capillary formation. 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: 239855 [Multi-domain]  Cd Length: 199  Bit Score: 80.56  E-value: 5.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  686 IPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLVDISEFSSHDICDVLKLYLRQLPEPFILFRLYKEF 765
Cdd:cd04390   22 VPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASLLKLYLRELPEPVIPWAQYEDF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  766 IDLAKEIqhvneeqeakkDSPEDKKHPHvsievnriLLKskdLLRQLPASHFNSLHYLIAHLRRVVDHAEENKMNSKNLG 845
Cdd:cd04390  102 LSCAQLL-----------SKDEEKGLGE--------LMK---QVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLA 159

                        170
                 ....*....|....*....
gi 81900344  846 VIFGPTLIRPRpTTAPVTI 864
Cdd:cd04390  160 TVFGPNILRPK-VEDPATI 177
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 684-852 2.79e-16

RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in RalBP1 proteins, also known as RLIP, RLIP76 or cytocentrin. RalBP1 plays an important role in endocytosis during interphase. During mitosis, RalBP1 transiently associates with the centromere and has been shown to play an essential role in the proper assembly of the mitotic apparatus. RalBP1 is an effector of the Ral GTPase which itself is an effector of Ras. RalBP1 contains a RhoGAP domain, which shows weak activity towards Rac1 and Cdc42, but not towards Ral, and a Ral effector domain binding motif. 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: 239846 [Multi-domain]  Cd Length: 182  Bit Score: 78.25  E-value: 2.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  684 DGI--PFVLKICASEIENRALCLQGIYRVCGNKIKTEKLcQALENGMHLVDISEFSSHDICDVLKLYLRQLPEPFilfrl 761
Cdd:cd04381   16 DGIdlPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDEL-KAAYNRRESPNLEEYEPPTVASLLKQYLRELPEPL----- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  762 ykefidLAKEIQHVNEEQEAKKDSPEDKKHphvsievnrillkSKDLLRQLPASHFNSLHYLIAHLRRVVDHAEENKMNS 841
Cdd:cd04381   90 ------LTKELMPRFEEACGRPTEAEREQE-------------LQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNI 150

                        170
                 ....*....|.
gi 81900344  842 KNLGVIFGPTL 852
Cdd:cd04381  151 QNISIVLSPTV 161
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 674-854 5.37e-15

RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in srGAPs. srGAPs are components of the intracellular part of Slit-Robo signalling pathway that is important for axon guidance and cell migration. srGAPs contain an N-terminal FCH domain, a central RhoGAP domain and a C-terminal SH3 domain; this SH3 domain interacts with the intracellular proline-rich-tail of the Roundabout receptor (Robo). This interaction with Robo then activates the rhoGAP domain which in turn inhibits Cdc42 activity. 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: 239848  Cd Length: 188  Bit Score: 74.76  E-value: 5.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  674 EFIQVAKKEpdgIPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMH-LVDisEFSSHDI---CDVLKLYL 749
Cdd:cd04383    9 EYIQDSGQA---IPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDpLAD--DQNDHDInsvAGVLKLYF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  750 RQLPEPFILFRLYKEFIDLAKeiqhvneeqeakKDSPEDKKHphvsievnrillKSKDLLRQLPASHFNSLHYLIAHLRR 829
Cdd:cd04383   84 RGLENPLFPKERFEDLMSCVK------------LENPTERVH------------QIREILSTLPRSVIIVMRYLFAFLNH 139

                        170       180
                 ....*....|....*....|....*
gi 81900344  830 VVDHAEENKMNSKNLGVIFGPTLIR 854
Cdd:cd04383  140 LSQFSDENMMDPYNLAICFGPTLMP 164
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 686-887 6.13e-14

RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP11A-like proteins. The mouse homolog of human ArhGAP11A has been detected as a gene exclusively expressed in immature ganglion cells, potentially playing a role in retinal development. The exact function of ArhGAP11A 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 several orders of magnitude.


Pssm-ID: 239859 [Multi-domain]  Cd Length: 202  Bit Score: 72.12  E-value: 6.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  686 IP-FVLKICASeIENRaLCLQGIYRVCGNKIKTEKLCQALENGMHLVdisefSSHDICDV---LKLYLRQLPEPFILFRL 761
Cdd:cd04394   20 VPkFLVDACTF-LLDH-LSTEGLFRKSGSVVRQKELKAKLEGGEACL-----SSALPCDVaglLKQFFRELPEPLLPYDL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  762 YKEFIDlAKEIQHVNEEQEAkkdspedkkhphvsievnrILLKSkdLLrqLPASHFNSLHYLIAHLRRVVDHAEENKMNS 841
Cdd:cd04394   93 HEALLK-AQELPTDEERKSA-------------------TLLLT--CL--LPDEHVNTLRYFFSFLYDVAQRCSENKMDS 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 81900344  842 KNLGVIFGPTLIRPRPTTAPVTISSLAEYSNQARLVEFLITYSQKI 887
Cdd:cd04394  149 SNLAVIFAPNLFQSEEGGEKMSSSTEKRLRLQAAVVQTLIDNASNI 194
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 683-882 2.11e-13

RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in the p85 isoforms of the regulatory subunit of the class IA PI3K (phosphatidylinositol 3'-kinase). This domain is also called Bcr (breakpoint cluster region protein) homology (BH) domain. Class IA PI3Ks are heterodimers, containing a regulatory subunit (p85) and a catalytic subunit (p110) and are activated by growth factor receptor tyrosine kinases (RTKs); this activation is mediated by the p85 subunit. p85 isoforms, alpha and beta, contain a C-terminal p110-binding domain flanked by two SH2 domains, an N-terminal SH3 domain, and a RhoGAP domain flanked by two proline-rich regions. 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: 239853  Cd Length: 200  Bit Score: 70.29  E-value: 2.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  683 PDGIPFVLKICASEIENRALCLQGIYRVCGNKIKTEkLCQALENGMHLVDISEFSSHDICDVLKLYLRQLPEPFILFRLY 762
Cdd:cd04388   12 PDVAPPLLIKLVEAIEKKGLESSTLYRTQSSSSLTE-LRQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPAPVY 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  763 KEFIDLAKEIQHVNEeqeakkdspedkkhphvSIEVNRILLKSKDllrqLPASHFNSLHYLIAHLRRVVDHAEENKMNSK 842
Cdd:cd04388   91 SEMISRAQEVQSSDE-----------------YAQLLRKLIRSPN----LPHQYWLTLQYLLKHFFRLCQSSSKNLLSAR 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 81900344  843 NLGVIFGPTLIRPRPTTAPVTisslaeySNQARLVEFLIT 882
Cdd:cd04388  150 ALAEIFSPLLFRFQPASSDSP-------EFHIRIIEVLIT 182
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 670-852 5.04e-13

RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of DLC1-like proteins. DLC1 shows in vitro GAP activity towards RhoA and CDC42. Beside its C-terminal GAP domain, DLC1 also contains a SAM (sterile alpha motif) and a START (StAR-related lipid transfer action) domain. DLC1 has tumor suppressor activity in cell culture. 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: 239840  Cd Length: 220  Bit Score: 69.75  E-value: 5.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  670 IFGAEFIQVAKKEPDGIPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLVDISEFSSHDICDVLKLYL 749
Cdd:cd04375    4 VFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQAYDVADMLKQYF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  750 RQLPEPFILFRLYKEFIDLakeIQHVNEEQEAKKdspedkkhphvsievnrilLKSKDLLrqLPASHFNSLHYLIAHLRR 829
Cdd:cd04375   84 RDLPEPLLTNKLSETFIAI---FQYVPKEQRLEA-------------------VQCAILL--LPDENREVLQTLLYFLSD 139

                        170       180
                 ....*....|....*....|...
gi 81900344  830 VVDHAEENKMNSKNLGVIFGPTL 852
Cdd:cd04375  140 VAANSQENQMTATNLAVCLAPSL 162
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 686-883 1.15e-11

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: 65.83  E-value: 1.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  686 IPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQ----ALENGMHlvDISEFSSHDICDVLKLYLRQLPEPFILFRL 761
Cdd:cd04380   50 IPKEIWRLVDYLYTRGLAQEGLFEEPGLPSEPGELLAeirdALDTGSP--FNSPGSAESVAEALLLFLESLPDPIIPYSL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  762 YKEFIdlakeiqhvneeqEAKKDSPEDKKHphvsievnrillkskdLLR-QLPASHFNSLHYLIAHLRRVVDHAEENKMN 840
Cdd:cd04380  128 YERLL-------------EAVANNEEDKRQ----------------VIRiSLPPVHRNVFVYLCSFLRELLSESADRGLD 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 81900344  841 SKNLGVIFGPTLIRPrPTTAPVTISSLAEYSNQARLVEFLITY 883
Cdd:cd04380  179 ENTLATIFGRVLLRD-PPRAGGKERRAERDRKRAFIEQFLLND 220
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
 220-436 6.44e-11

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho GTPase activating protein Rgd1 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Saccharomyces cerevisiae Rgd1 is a GTPase activating protein (GAP) with activity towards Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively. At low pH, S. cerevisiae Rgd1 is required for cell survival and the activation of the protein kinase C pathway, which is important in cell integrity and the maintenance of cell shape. It contains an N-terminal F-BAR domain and a C-terminal Rho GAP domain. The F-BAR domain of S. cerevisiae Rgd1 binds to phosphoinositides and plays an important role in the localization of the protein to the bud tip/neck during the cell cycle. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153336 [Multi-domain]  Cd Length: 234  Bit Score: 63.91  E-value: 6.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  220 KNIVSWVEKKLNLELESTRNIVKLAEATRSSIGIQEFmpLQSLFTNALlsdiHSSHLLQQTIA------ALQANKFVQPL 293
Cdd:cd07652   22 KEFATFLKKRAAIEEEHARGLKKLARTTLDTYKRPDH--KQGSFSNAY----HSSLEFHEKLAdnglrfAKALNEMSDEL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  294 LGRKNEMEKQRKEIKDLWKQQQNKLLETETALKKAKLLCMQRQDEYEKAKSSmfraeEEQLSSSVGLAKnlNKQLEKrrr 373
Cdd:cd07652   96 SSLAKTVEKSRKSIKETGKRAEKKVQDAEAAAEKAKARYDSLADDLERVKTG-----DPGKKLKFGLKG--NKSAAQ--- 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81900344  374 LEEEALQKVEEANEHYKVCVTNVEERRNDLENTKR-EILTQLRTLVFQCDltlKAVTVNLFHMQ 436
Cdd:cd07652  166 HEDELLRKVQAADQDYASKVNAAQALRQELLSRHRpEAVKDLFDLILEID---AALRLQYQKYA 226
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 686-887 2.41e-10

RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal LRG1-like proteins. Yeast Lrg1p is required for efficient cell fusion, and mother-daughter cell separation, possibly through acting as a RhoGAP specifically regulating 1,3-beta-glucan synthesis. 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: 239862  Cd Length: 213  Bit Score: 61.61  E-value: 2.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  686 IPFVLKICASEIENRALCLQGIYRVCGNKIKTEKLCQALE-NGMHLVDISEFSSHDICDVLKLYLRQLPEPFILFRLYKE 764
Cdd:cd04397   27 IPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDkNPTEVPDLSKENPVQLAALLKKFLRELPDPLLTFKLYRL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  765 FIdlakeiqhvneeQEAKKDSPEDKKhphvsievnRILLKSKDLlrqLPASHFNSLHYLIAHLRRV-----VDHAEENKM 839
Cdd:cd04397  107 WI------------SSQKIEDEEERK---------RVLHLVYCL---LPKYHRDTMEVLFSFLKWVssfshIDEETGSKM 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 81900344  840 NSKNLGVIFGPTLIRPRPTTAPVTisslAEYSNQARLVEFLITYSQKI 887
Cdd:cd04397  163 DIHNLATVITPNILYSKTDNPNTG----DEYFLAIEAVNYLIENNEEF 206
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 614-659 4.36e-08

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 50.54  E-value: 4.36e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 81900344     614 THKFRKLRSPTKC---RDCDGIVMFPGVECEECLLVCHRKCLENLVIIC 659
Cdd:smart00109    2 KHVFRTFTKPTFCcvcRKSIWGSFKQGLRCSECKVKCHKKCADKVPKAC 50
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 615-660 3.54e-07

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 48.21  E-value: 3.54e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 81900344    615 HKF--RKLRSPTKCRDCDGIVMF---PGVECEECLLVCHRKCLENLVIICG 660
Cdd:pfam00130    1 HHFvhRNFKQPTFCDHCGEFLWGlgkQGLKCSWCKLNVHKRCHEKVPPECG 51
C1_ScPKC1-like_rpt1 cd20822
first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...
 615-659 3.76e-07

first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae protein kinase C-like 1 (ScPKC1) and similar proteins; ScPKC1 is required for cell growth and for the G2 to M transition of the cell division cycle. It mediates a protein kinase cascade, activating BCK1 which itself activates MKK1/MKK2. The family also includes Schizosaccharomyces pombe PKC1 and PKC2, which are involved in the control of cell shape and act as targets of the inhibitor staurosporine. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410372  Cd Length: 52  Bit Score: 48.05  E-value: 3.76e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 81900344  615 HKFRKLR--SPTKCRDCDGIVMFPGVECEECLLVCHRKCLENLVIIC 659
Cdd:cd20822    3 HKFVQKQfyQIMRCAVCGEFLVNAGYQCEDCKYTCHKKCYEKVVTKC 49
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 615-659 5.66e-07

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 47.51  E-value: 5.66e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 81900344  615 HKFRK--LRSPTKCRDCDGIVMF---PGVECEECLLVCHRKCLENLVIIC 659
Cdd:cd00029    1 HRFVPttFSSPTFCDVCGKLIWGlfkQGLKCSDCGLVCHKKCLDKAPSPC 50
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 286-417 6.38e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 6.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344    286 ANKFVQPLLGRKNEMEKQRKEIkdlwKQQQNKLLETETALKKAKllcmQRQDEYEKAKSSMfRAEEEQLSSSVGLAKNLN 365
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKI----EELEEKIAELEKALAELR----KELEELEEELEQL-RKELEELSRQISALRKDL 735

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 81900344    366 KQLEKRRRLEEEALQKVEEANEHYKVCVTNVEERRNDLENTKREILTQLRTL 417
Cdd:TIGR02168  736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
C1_KSR cd20812
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ...
 615-660 1.54e-05

protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) family; KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410362  Cd Length: 48  Bit Score: 43.47  E-value: 1.54e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 81900344  615 HKF-RKLRSPTKCRDCDGIVMFpGVECEECLLVCHRKCLENLVIICG 660
Cdd:cd20812    3 HRFsKKLFMRQTCDYCHKQMFF-GLKCKDCKYKCHKKCAKKAPPSCG 48
C1_TNS2-like cd20826
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ...
 615-662 1.60e-05

protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; The TNS2-like group includes TNS2, and variants of TNS1 and TNS3. Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity and interferes with AKT1 signaling. Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. Typical TNS1 and TNS3 do not contain C1 domains, but some isoforms/variants do. Members of this family contain an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410376  Cd Length: 52  Bit Score: 43.53  E-value: 1.60e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 81900344  615 HKFR--KLRSPTKCRDCDGIVMFPGVECEECLLVCHRKCLENLVIICGHQ 662
Cdd:cd20826    3 HSFKekSFRKPRTCDVCKQIIWNEGSSCRVCKYACHRKCEPKVTAACSPS 52
C1_cPKC_nPKC_rpt1 cd20792
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
 615-659 3.36e-05

first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410342  Cd Length: 53  Bit Score: 42.62  E-value: 3.36e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 81900344  615 HKF--RKLRSPTKCRDCDGI---VMFPGVECEECLLVCHRKCLENLVIIC 659
Cdd:cd20792    2 HKFvaTFFKQPTFCSHCKDFiwgLGKQGYQCQVCRFVVHKRCHEYVVFKC 51
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 717-888 3.50e-05

RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD2-like proteins. Yeast Rgd2 is a GAP protein for Cdc42 and Rho5. 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: 239864  Cd Length: 212  Bit Score: 46.56  E-value: 3.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  717 TEKLCQALENGMHLVDI----SEFSSHDICDVLKLYLRQLPEPFILFRLYkefiDLAKEIqhVNEEQEAKKDSPEDkkhp 792
Cdd:cd04399   53 THQLRNLLNKPKKPDKEviilKKFEPSTVASVLKLYLLELPDSLIPHDIY----DLIRSL--YSAYPPSQEDSDTA---- 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  793 hvsievnRI-LLKSkdLLRQLPASHFNSLHYLIAHLRRVVD---HAEENKMNSKNLGVIFGPTLIRPRpTTAPVTISSLA 868
Cdd:cd04399  123 -------RIqGLQS--TLSQLPKSHIATLDAIITHFYRLIEitkMGESEEEYADKLATSLSREILRPI-IESLLTIGDKH 192

                        170       180
                 ....*....|....*....|
gi 81900344  869 EYsnqaRLVEFLITYSQKIF 888
Cdd:cd04399  193 GY----KFFRDLLTHKDQIF 208
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 705-882 5.54e-05

RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in KIAA1688-like proteins; KIAA1688 is a protein of unknown function that contains a RhoGAP domain and a myosin tail homology 4 (MyTH4) domain. 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: 239854  Cd Length: 187  Bit Score: 45.46  E-value: 5.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  705 QGIYRVCGN--KIKTEKLC--QALENGMHLVDIsefssHDICDVLKLYLRQLPEPFILFRLYKEFIDlakeiqhvneeqe 780
Cdd:cd04389   41 EGIFRVPGDidEVNELKLRvdQWDYPLSGLEDP-----HVPASLLKLWLRELEEPLIPDALYQQCIS------------- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  781 aKKDSPEdkkhphvsievnrillKSKDLLRQLPASHFNSLHYLIAHLR-----RVVDHaeeNKMNSKNLGVIFGPTLIRP 855
Cdd:cd04389  103 -ASEDPD----------------KAVEIVQKLPIINRLVLCYLINFLQvfaqpENVAH---TKMDVSNLAMVFAPNILRC 162

                        170       180
                 ....*....|....*....|....*..
gi 81900344  856 RpTTAPVTIssLAEYSNQARLVEFLIT 882
Cdd:cd04389  163 T-SDDPRVI--FENTRKEMSFLRTLIE 186
C1_nPKC_epsilon-like_rpt1 cd20835
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 615-663 9.92e-05

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410385  Cd Length: 64  Bit Score: 41.68  E-value: 9.92e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 81900344  615 HKFRK--LRSPTKCRDCD----GIVMFPGVECEECLLVCHRKCLENLVIICGHQK 663
Cdd:cd20835   10 HKFMAtyLRQPTYCSHCKdfiwGVIGKQGYQCQVCTCVVHKRCHQLVVTKCPGNK 64
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
 615-660 1.90e-04

protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) family; MRCK is thought to be a coincidence detector of signaling by the small GTPase Cdc42 and phosphoinositides. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCK has been shown to promote cytoskeletal reorganization, which affects many biological processes. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410359  Cd Length: 53  Bit Score: 40.33  E-value: 1.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 81900344  615 HKF--RKLRSPTKCRDCdGIVMF----PGVECEECLLVCHRKCLENLVIICG 660
Cdd:cd20809    1 HKFivRTFSTPTKCNHC-TSLMVglvrQGLVCEVCGYACHVSCADKAPQVCP 51
F-BAR_FCHO cd07648
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; ...
 218-466 2.07e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proteins in this group have been named FCH domain Only (FCHO) proteins. Vertebrates have two members, FCHO1 and FCHO2. These proteins contain an F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153332 [Multi-domain]  Cd Length: 261  Bit Score: 44.64  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  218 YTKNIVSWVEKKLNLELESTRNIVKLAEATRSSIGIQEFMPLQSLF--TNALLSDIHsshllQQTIAALQanKFVQPLLG 295
Cdd:cd07648   20 AVKELADFLRERATIEETYSKALNKLAKQASNSSQLGTFAPLWLVLrvSTEKLSELH-----LQLVQKLQ--ELIKDVQK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  296 RKNEMEKQRKEIKDLWKQQQNKLLETET---ALKKAKLLCMQRQDEYEKAKSsmfraeeeqlsssvglAKNLNKQLEKrr 372
Cdd:cd07648   93 YGEEQHKKHKKVKEEESGTAEAVQAIQTttaALQKAKEAYHARCLELERLRR----------------ENASPKEIEK-- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  373 rleeeALQKVEEANEHYKVCVTNVEERRNDLEnTKREILTQlrtlVFQcdltlkavTVNLFHMQQLQA--ASLANSLQSL 450
Cdd:cd07648  155 -----AEAKLKKAQDEYKALVEKYNNIRADFE-TKMTDSCK----RFQ--------EIEESHLRQMKEflASYAEVLSEN 216

                        250
                 ....*....|....*.
gi 81900344  451 CDSAklydpGQEYSEF 466
Cdd:cd07648  217 HSAV-----GQVHEEF 227
C1_DGKtheta_typeV_rpt1 cd20803
first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
 615-659 2.56e-04

first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410353  Cd Length: 56  Bit Score: 39.98  E-value: 2.56e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 81900344  615 HKFRK--LRSPTKCRDC-DGI--VMFPGVECEECLLVCHRKCLENLVIIC 659
Cdd:cd20803    2 HSFRKktFHKPTYCHHCtDLLwgLLNQGYQCEVCNFVSHERCLKTVVTPC 51
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
 615-660 2.75e-04

protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and similar proteins; MgcRacGAP, also called Rac GTPase-activating protein 1 (RACGAP1) or protein CYK4, plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling; and ii) after phosphorylation by aurora B, MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain an N-terminal C1 domain, and a C-terminal RhoGAP domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410371  Cd Length: 55  Bit Score: 40.08  E-value: 2.75e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 81900344  615 HKF--RKLRSPTKCRDCDGIVMF--PGVECEECLLVCHRKCLENLVIICG 660
Cdd:cd20821    3 HRFvsKTVIKPETCVVCGKRIKFgkKALKCKDCRVVCHPDCKDKLPLPCV 52
PTZ00121 PTZ00121
MAEBL; Provisional
 296-409 3.63e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344   296 RKNEMEKQRKEIKDLWKQQQNKLLETETALKKAKLlcmQRQDEYEKAKSSMFR-AEEEQLSSSVGLAKNLN--KQLEKRR 372
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE---AKKAEEDKKKAEEAKkAEEDEKKAAEALKKEAEeaKKAEELK 1708

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 81900344   373 RLEEEALQKVEEANEHYKVCVTNVEERRNDLENTKRE 409
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK 1745
C1_DEF8 cd20819
protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 ...
 610-663 5.65e-04

protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 (DEF-8) and similar proteins; DEF-8 positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts. It is involved in bone resorption. DEF-8 contains a protein kinase C conserved region 1 (C1) domain followed by a putative zinc-RING and/or ribbon. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410369  Cd Length: 62  Bit Score: 39.18  E-value: 5.65e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81900344  610 KAALTHKF--RKLRSPTK--CRDCDGIVMfpGV-----ECEECLLVCHRKCLENLVIICGHQK 663
Cdd:cd20819    1 KVVLGHHFvlQKSKSSSKqyCDKCCGIIW--GLlqtwyRCTDCGYRCHSKCLNSITRTCASVK 61
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 200-275 1.62e-03

Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also known as the RAEYL motif or the S. pombe Cdc15 N-terminal domain.


Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 38.86  E-value: 1.62e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344     200 KNTDSIELALSYAKTWSKYTKNIVSWVEKKLNLELESTRNIVKLAEATRSSIGIQ-EFMPLQSLFTNAL-----LSDIHS 273
Cdd:smart00055    6 ELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKLRAVRDTEpEYGSLSKAWEVLLsetdaLAKQHL 85


                    ..
gi 81900344     274 SH 275
Cdd:smart00055   86 EL 87
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
277-462 2.11e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  277 LQQTIAALQANkfVQPLLGRKNEMEKQRKEIKDLWKQQQNKLLETETALKKAKLLCMQRQDEYEKAKssmfrAEEEQLSS 356
Cdd:COG4372   43 LQEELEQLREE--LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ-----EEAEELQE 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  357 SVglaknlnKQLEKRRRLEEEALQKVEEANEHYKVCVTNVEERRNDLENTKREILTQLRTLVFQCDLTLKAVTVNLFHMQ 436
Cdd:COG4372  116 EL-------EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188

                        170       180
                 ....*....|....*....|....*.
gi 81900344  437 QLQAASLANSLQSLCDSAKLYDPGQE 462
Cdd:COG4372  189 LKEANRNAEKEEELAEAEKLIESLPR 214
C1_nPKC_theta-like_rpt2 cd20837
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 615-659 2.11e-03

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410387  Cd Length: 50  Bit Score: 37.42  E-value: 2.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 81900344  615 HKFR--KLRSPTKCRDCdGIVMF----PGVECEECLLVCHRKCLENLVIIC 659
Cdd:cd20837    1 HRFKvyNYMSPTFCDHC-GSLLWglfrQGLKCEECGMNVHHKCQKKVANLC 50
C1_PKD2_rpt2 cd20843
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
 605-652 2.98e-03

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410393  Cd Length: 79  Bit Score: 38.03  E-value: 2.98e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 81900344  605 KTLMSKAALTHKF--RKLRSPTKCRDCDGIV--MF-PGVECEECLLVCHRKCL 652
Cdd:cd20843    2 KMLLSKVKVPHTFviHSYTRPTVCQFCKKLLkgLFrQGLQCKDCKFNCHKRCA 54
C1_PDZD8 cd20825
protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 ...
 615-654 4.16e-03

protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 (PDZD8) and similar proteins; PDZD8, also called Sarcoma antigen NY-SAR-84/NY-SAR-104, is a molecular tethering protein that connects endoplasmic reticulum (ER) and mitochondrial membranes. PDZD8-dependent ER-mitochondria membrane tethering is essential for ER-mitochondria Ca2+ transfer. In neurons, it is involved in the regulation of dendritic Ca2+ dynamics by regulating mitochondrial Ca2+ uptake. PDZD8 also plays an indirect role in the regulation of cell morphology and cytoskeletal organization. It contains a PDZ domain and a C1 domain. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410375  Cd Length: 55  Bit Score: 36.49  E-value: 4.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 81900344  615 HKF--RKLRSPTKCRDCDG-IVMFPGVECEECLLVCHRKCLEN 654
Cdd:cd20825    4 HDFvlTQFQNATYCDFCKKkIWLKEAFQCRLCGMICHKKCLDK 46
C1_Munc13 cd20807
protein kinase C conserved region 1 (C1 domain) found in the Munc13 family; The Munc13 gene ...
 622-659 4.96e-03

protein kinase C conserved region 1 (C1 domain) found in the Munc13 family; The Munc13 gene family encodes a family of neuron-specific, synaptic molecules that bind to syntaxin, an essential mediator of neurotransmitter release. Munc13-1 is a component of presynaptic active zones in which it acts as an essential synaptic vesicle priming protein. Munc13-2 is essential for normal release probability at hippocampal mossy fiber synapses. Munc13-3 is almost exclusively expressed in the cerebellum. It acts as a tumor suppressor and plays a critical role in the formation of release sites with calcium channel nanodomains. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410357  Cd Length: 53  Bit Score: 36.30  E-value: 4.96e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 81900344  622 SPTKCRDCDGI---VMFPGVECEECLLVCHRKCLENLVIIC 659
Cdd:cd20807   10 TPTYCYECEGLlwgIARQGVRCTECGVKCHEKCKDLLNADC 50
C1_PIK3R-like_rpt2 cd20830
second protein kinase C conserved region 1 (C1 domain) found in uncharacterized ...
 615-661 4.99e-03

second protein kinase C conserved region 1 (C1 domain) found in uncharacterized phosphatidylinositol 3-kinase regulatory subunit-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate phosphatidylinositol 3-kinase regulatory subunits (PIK3Rs), which bind to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulate their kinase activity. Unlike typical PIK3Rs, members of this family have two C1 domains. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410380  Cd Length: 52  Bit Score: 36.46  E-value: 4.99e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 81900344  615 HKFrKLRSPTKCRDCD--GIVMF----PGVECEECLLVCHRKCLENLVIICGH 661
Cdd:cd20830    1 HRF-VEQSFSTLQWCDkcGKFLFglvhQGLQCQDCGLVCHRTCAATGLPKCEP 52
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 219-428 6.87e-03

The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a dimerization module that binds and bends membranes; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. F-BAR domain containing proteins, also known as Pombe Cdc15 homology (PCH) family proteins, include Fes and Fer tyrosine kinases, PACSINs/Syndapins, FCHO, PSTPIP, CIP4-like proteins and srGAPs. Many members also contain an SH3 domain and play roles in endocytosis. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. These tubules have diameters larger than those observed with N-BARs. The F-BAR domains of some members such as NOSTRIN and Rgd1 are important for the subcellular localization of the protein.


Pssm-ID: 153294 [Multi-domain]  Cd Length: 191  Bit Score: 39.25  E-value: 6.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  219 TKNIVSWVEKKLNLELESTRNIVKLAEatRSSIGIQEFMPLQSLFTNAL--LSDIHSSHLLQqtIAALQANKFVQPLLGR 296
Cdd:cd07610   16 LKDLREFLKKRAAIEEEYAKNLQKLAK--KFSKKPESGKTSLGTSWNSLreETESAATVHEE--LSEKLSQLIREPLEKV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344  297 KNEMEKQRKEIKDLWKQQQNKLLETETALKKakllcmQRQDEYekakssmfraeeeqlsssvglAKNLNKQLEKRRRLEE 376
Cdd:cd07610   92 KEDKEQARKKELAEGEKLKKKLQELWAKLAK------KADEEY---------------------REQVEKLNPAQSEYEE 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 81900344  377 EALQKVEEANEHYkvcvtnvEERRNDLENTKREILTQLRTLVFQCDLTLKAV 428
Cdd:cd07610  145 EKLNKIQAEQERE-------EERLEILKDNLKNYINAIKEIPQKIQQELEQS 189
CRIK cd20814
protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) ...
 615-660 6.94e-03

protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) and similar proteins; CRIK, also called serine/threonine-protein kinase 21, is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger (C1 domain), and a pleckstrin homology (PH) domain, in addition to other motifs. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410364  Cd Length: 56  Bit Score: 36.07  E-value: 6.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 81900344  615 HKFRKLR--SPTKCRDCDGIVMF--PGVECEECLLVCHRKCLENLVIICG 660
Cdd:cd20814    5 HRFTTGLnmRATKCAVCLDGVPFgrQASKCSECGIVCHPKCSSSLPNTCG 54
C1_RASSF1-like cd20820
protein kinase C conserved region 1 (C1 domain) found in the Ras association domain-containing ...
 615-659 8.79e-03

protein kinase C conserved region 1 (C1 domain) found in the Ras association domain-containing protein 1 (RASSF1)-like family; The RASSF1-like family includes RASSF1 and RASSF5. RASSF1 and RASSF5 are members of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. RASSF1 has eight transcripts (A-H) arising from alternative splicing and differential promoter usage. RASSF1A and 1C are the most extensively studied RASSF1; both are localized to microtubules and involved in the regulation of growth and migration. RASSF1 is a potential tumor suppressor that is required for death receptor-dependent apoptosis. RASSF5, also called new ras effector 1 (NORE1), or regulator for cell adhesion and polarization enriched in lymphoid tissues (RAPL), is expressed as three transcripts (A-C) via differential promoter usage and alternative splicing. RASSF5A is a pro-apoptotic Ras effector and functions as a Ras regulated tumor suppressor. RASSF5C is regulated by Ras related protein and modulates cellular adhesion. RASSF5 is a potential tumor suppressor that seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. RASSF1 and RASSF5 contain a C1 domain, which is descibed in this model. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410370  Cd Length: 52  Bit Score: 35.50  E-value: 8.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 81900344  615 HKFR--KLRSPTKCRDCDGIV--MFP-GVECEECLLVCHRKCLENLVIIC 659
Cdd:cd20820    2 HRFVplELEQPTWCDLCGSVIlgLFRkCLRCANCKMTCHPRCRSLVCLTC 51
PRK00106 PRK00106
ribonuclease Y;
293-415 9.61e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 40.24  E-value: 9.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81900344   293 LLGRKNEMEKQRKEIKDLWKQQQNKLLETETALKKaKLLCMQRQDEYEKAKSSMFRAEEEQLSSSvglAKNLNKQLEKRR 372
Cdd:PRK00106   74 LLEAKEEARKYREEIEQEFKSERQELKQIESRLTE-RATSLDRKDENLSSKEKTLESKEQSLTDK---SKHIDEREEQVE 149

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 81900344   373 RLEEealQKVEEANehyKVCVTNVEERRNDL-----ENTKREILTQLR 415
Cdd:PRK00106  150 KLEE---QKKAELE---RVAALSQAEAREIIlaeteNKLTHEIATRIR 191
 
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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