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Conserved domains on  [gi|1007393347|ref|NP_001308161|]
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rho GTPase-activating protein 45 isoform 5 [Homo sapiens]

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 ...
 763-973 3.81e-105

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 cd04378:

Pssm-ID: 470621  Cd Length: 203  Bit Score: 328.61  E-value: 3.81e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  763 FGQDFSHAARSAPDGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHDISNVLKLYLR 842
Cdd:cd04378      1 FGVDFSQVPRDFPDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  843 QLPEPLISFRLYHELVGLAKDSLKAEAEakaasrGRQDGSESEAVAVALagRLRELLRDLPPENRASLQYLLRHLRRIVE 922
Cdd:cd04378     81 QLPEPLILFRLYNDFIALAKEIQRDTEE------DKAPNTPIEVNRIIR--KLKDLLRQLPASNYNTLQHLIAHLYRVAE 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1007393347  923 VEQDNKMTPGNLGIVFGPTLLRPRPTEATVSLSSLVDYPHQARVIETLIVH 973
Cdd:cd04378    153 QFEENKMSPNNLGIVFGPTLIRPRPGDADVSLSSLVDYGYQARLVEFLITN 203
C1_GMIP-like cd20816
protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP) ...
 705-755 7.26e-29

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: 109.65  E-value: 7.26e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1007393347  705 RTHRLRKLRTPAKCRECNSYVYFQGAECEECCLACHKKCLETLAIQCGHKK 755
Cdd:cd20816      1 QTHRFRRLRTPSKCRECDSYVYFNGAECEECGLACHKKCLETLAIQCGHKR 51
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 285-360 9.28e-16

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: 73.53  E-value: 9.28e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1007393347   285 GVDAALLYAKNMAKYMKDLISYLEKRTTLEMEFAKGLQKIAHNCRQSVMQEPHM-PLLSIYSLALEQDLEFGHSMVQ 360
Cdd:smart00055   10 GFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKLRAVRDTEPEYgSLSKAWEVLLSETDALAKQHLE 86
 
Name Accession Description Interval E-value
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 763-973 3.81e-105

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: 328.61  E-value: 3.81e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  763 FGQDFSHAARSAPDGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHDISNVLKLYLR 842
Cdd:cd04378      1 FGVDFSQVPRDFPDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  843 QLPEPLISFRLYHELVGLAKDSLKAEAEakaasrGRQDGSESEAVAVALagRLRELLRDLPPENRASLQYLLRHLRRIVE 922
Cdd:cd04378     81 QLPEPLILFRLYNDFIALAKEIQRDTEE------DKAPNTPIEVNRIIR--KLKDLLRQLPASNYNTLQHLIAHLYRVAE 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1007393347  923 VEQDNKMTPGNLGIVFGPTLLRPRPTEATVSLSSLVDYPHQARVIETLIVH 973
Cdd:cd04378    153 QFEENKMSPNNLGIVFGPTLIRPRPGDADVSLSSLVDYGYQARLVEFLITN 203
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 778-974 2.78e-60

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: 204.04  E-value: 2.78e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347   778 VPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELV-ELSQASPHDISNVLKLYLRQLPEPLISFRLYHE 856
Cdd:smart00324    3 IPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDlDLSEYDVHDVAGLLKLFLRELPEPLITYELYEE 82

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347   857 LVGLAKDSlkaeaeakaasrgrqdgSESEAVAvalagRLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGNLGI 936
Cdd:smart00324   83 FIEAAKLE-----------------DETERLR-----ALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAI 140

                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1007393347   937 VFGPTLLRPRPTEATvslsSLVDYPHQARVIETLIVHY 974
Cdd:smart00324  141 VFGPTLLRPPDGEVA----SLKDIRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 779-947 1.03e-53

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 184.29  E-value: 1.03e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  779 PFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELV-ELSQASPHDISNVLKLYLRQLPEPLISFRLYHEL 857
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDlDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  858 VGLAKDSlkaeaeakaasrgrqdgSESEAVAvalagRLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGNLGIV 937
Cdd:pfam00620   81 IEAAKLP-----------------DEEERLE-----ALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIV 138

                          170
                   ....*....|
gi 1007393347  938 FGPTLLRPRP 947
Cdd:pfam00620  139 FGPTLLRPPD 148
C1_GMIP-like cd20816
protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP) ...
 705-755 7.26e-29

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: 109.65  E-value: 7.26e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1007393347  705 RTHRLRKLRTPAKCRECNSYVYFQGAECEECCLACHKKCLETLAIQCGHKK 755
Cdd:cd20816      1 QTHRFRRLRTPSKCRECDSYVYFNGAECEECGLACHKKCLETLAIQCGHKR 51
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 285-360 9.28e-16

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: 73.53  E-value: 9.28e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1007393347   285 GVDAALLYAKNMAKYMKDLISYLEKRTTLEMEFAKGLQKIAHNCRQSVMQEPHM-PLLSIYSLALEQDLEFGHSMVQ 360
Cdd:smart00055   10 GFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKLRAVRDTEPEYgSLSKAWEVLLSETDALAKQHLE 86
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
 300-534 6.10e-15

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: 75.46  E-value: 6.10e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  300 MKDLISYLEKRTTLEMEFAKGLQKIAHNCRQsVMQEPHMpLLSIYSLALEQDLEFGHSMVQAVGTLQT--QTFMQPLTLR 377
Cdd:cd07652     21 AKEFATFLKKRAAIEEEHARGLKKLARTTLD-TYKRPDH-KQGSFSNAYHSSLEFHEKLADNGLRFAKalNEMSDELSSL 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  378 RLEHEKRRKEIKEAWHRAQRKLQEAESNLRKAKQGYVQRCEDHDKarflvAKAEEEQAGSapGAGSTATKTL-----DKR 452
Cdd:cd07652     99 AKTVEKSRKSIKETGKRAEKKVQDAEAAAEKAKARYDSLADDLER-----VKTGDPGKKL--KFGLKGNKSAaqhedELL 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  453 RRLEEEAKnkaeeamaTYRTCVADAKTQKQELEDT-KVTALRQIQEVIRQSDQTIKsatisyyqmMHMQtaplpvHFQML 531
Cdd:cd07652    172 RKVQAADQ--------DYASKVNAAQALRQELLSRhRPEAVKDLFDLILEIDAALR---------LQYQ------KYALP 228


                   ...
gi 1007393347  532 CES 534
Cdd:cd07652    229 NEL 231
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 706-751 2.43e-09

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: 54.01  E-value: 2.43e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1007393347   706 THRLRKLRTPAKCRECNSYVYF---QGAECEECCLACHKKCLETLAIQC 751
Cdd:smart00109    2 KHVFRTFTKPTFCCVCRKSIWGsfkQGLRCSECKVKCHKKCADKVPKAC 50
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 710-752 1.61e-06

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: 46.28  E-value: 1.61e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1007393347  710 RKLRTPAKCRECNSYVYF---QGAECEECCLACHKKCLETLAIQCG 752
Cdd:pfam00130    6 RNFKQPTFCDHCGEFLWGlgkQGLKCSWCKLNVHKRCHEKVPPECG 51
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 275-325 2.30e-04

Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The cytosolic endocytic adaptor proteins in fungi carry this domain at the N-terminus; several of these have been referred to as muniscin proteins. These N-terminal BAR, N-BAR, and EFC/F-BAR domains are found in proteins that regulate membrane trafficking events by inducing membrane tubulation. The domain dimerizes into a curved structure that binds to liposomes and either senses or induces the curvature of the membrane bilayer to cause biophysical changes to the shape of the bilayer; it also thereby recruits other trafficking factors, such as the GTPase dynamin. Most EFC/F-BAR domain-family members localize to actin-rich structures.


Pssm-ID: 459868 [Multi-domain]  Cd Length: 78  Bit Score: 40.72  E-value: 2.30e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1007393347  275 VDVLLQRCEGGVDAallyaknmakyMKDLISYLEKRTTLEMEFAKGLQKIA 325
Cdd:pfam00611    2 FKVLLKRLKQGIKL-----------LEELASFLKERAEIEEEYAKKLQKLA 41
 
Name Accession Description Interval E-value
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 763-973 3.81e-105

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: 328.61  E-value: 3.81e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  763 FGQDFSHAARSAPDGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHDISNVLKLYLR 842
Cdd:cd04378      1 FGVDFSQVPRDFPDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  843 QLPEPLISFRLYHELVGLAKDSLKAEAEakaasrGRQDGSESEAVAVALagRLRELLRDLPPENRASLQYLLRHLRRIVE 922
Cdd:cd04378     81 QLPEPLILFRLYNDFIALAKEIQRDTEE------DKAPNTPIEVNRIIR--KLKDLLRQLPASNYNTLQHLIAHLYRVAE 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1007393347  923 VEQDNKMTPGNLGIVFGPTLLRPRPTEATVSLSSLVDYPHQARVIETLIVH 973
Cdd:cd04378    153 QFEENKMSPNNLGIVFGPTLIRPRPGDADVSLSSLVDYGYQARLVEFLITN 203
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 763-973 2.06e-101

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: 318.68  E-value: 2.06e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  763 FGQDFSHAARSAPDGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHDISNVLKLYLR 842
Cdd:cd04409      1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLKLYLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  843 QLPEPLISFRLYHELVGLAKDSLK--AEAEAKAASRGRQDGSESEAVAVALagRLRELLRDLPPENRASLQYLLRHLRRI 920
Cdd:cd04409     81 QLPEPLILFRLYNEFIGLAKESQHvnETQEAKKNSDKKWPNMCTELNRILL--KSKDLLRQLPAPNYNTLQFLIVHLHRV 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1007393347  921 VEVEQDNKMTPGNLGIVFGPTLLRPRPTEATVSLSSLVDYPHQARVIETLIVH 973
Cdd:cd04409    159 SEQAEENKMSASNLGIIFGPTLIRPRPTDATVSLSSLVDYPHQARLVELLITY 211
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 763-973 2.14e-67

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: 225.08  E-value: 2.14e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  763 FGQDFSHAARSAPDGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHDISNVLKLYLR 842
Cdd:cd04408      1 FGVDFSQLPRDFPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  843 QLPEPLISFRLYHELVGLAKDSLkaeaeakaasRGRQDGSESEAVAVALAGRLRELLRDLPPENRASLQYLLRHLRRIVE 922
Cdd:cd04408     81 ELPEPVLPFQLYDDFIALAKELQ----------RDSEKAAESPSIVENIIRSLKELLGRLPVSNYNTLRHLMAHLYRVAE 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1007393347  923 VEQDNKMTPGNLGIVFGPTLLRPRPTEAtVSLSSLVDYPHQARVIETLIVH 973
Cdd:cd04408    151 RFEDNKMSPNNLGIVFGPTLLRPLVGGD-VSMICLLDTGYQAQLVEFLISN 200
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 778-974 2.78e-60

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: 204.04  E-value: 2.78e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347   778 VPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELV-ELSQASPHDISNVLKLYLRQLPEPLISFRLYHE 856
Cdd:smart00324    3 IPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDlDLSEYDVHDVAGLLKLFLRELPEPLITYELYEE 82

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347   857 LVGLAKDSlkaeaeakaasrgrqdgSESEAVAvalagRLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGNLGI 936
Cdd:smart00324   83 FIEAAKLE-----------------DETERLR-----ALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAI 140

                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1007393347   937 VFGPTLLRPRPTEATvslsSLVDYPHQARVIETLIVHY 974
Cdd:smart00324  141 VFGPTLLRPPDGEVA----SLKDIRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 779-947 1.03e-53

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 184.29  E-value: 1.03e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  779 PFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELV-ELSQASPHDISNVLKLYLRQLPEPLISFRLYHEL 857
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDlDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  858 VGLAKDSlkaeaeakaasrgrqdgSESEAVAvalagRLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGNLGIV 937
Cdd:pfam00620   81 IEAAKLP-----------------DEEERLE-----ALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIV 138

                          170
                   ....*....|
gi 1007393347  938 FGPTLLRPRP 947
Cdd:pfam00620  139 FGPTLLRPPD 148
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 779-973 2.22e-51

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: 178.26  E-value: 2.22e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  779 PFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHDISNVLKLYLRQLPEPLISFRLYHELV 858
Cdd:cd00159      1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  859 GLAKDSlkaeaeakaasrgrqdgSESEAVAvalagRLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGNLGIVF 938
Cdd:cd00159     81 ELAKIE-----------------DEEERIE-----ALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVF 138

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1007393347  939 GPTLLRPRPTeatvSLSSLVDYPHQARVIETLIVH 973
Cdd:cd00159    139 APTLLRPPDS----DDELLEDIKKLNEIVEFLIEN 169
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 776-974 8.75e-38

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: 139.75  E-value: 8.75e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  776 DGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVEL--SQASPHDISNVLKLYLRQLPEPLISFRL 853
Cdd:cd04385     13 NDIPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARSVQLreGEYTVHDVADVLKRFLRDLPDPLLTSEL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  854 YHELVGLAKDSlkaeaeakaasrgrqdgSESEAVAvalagRLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGN 933
Cdd:cd04385     93 HAEWIEAAELE-----------------NKDERIA-----RYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHN 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1007393347  934 LGIVFGPTLLRPRPTEATvslsslvDYPHQARVIETLIVHY 974
Cdd:cd04385    151 LALVFGPTLFQTDEHSVG-------QTSHEVKVIEDLIDNY 184
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 763-978 1.73e-37

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: 139.57  E-value: 1.73e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  763 FGQDFSHAARSAPDGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHD---ISNVLKL 839
Cdd:cd04372      1 YGCDLTTLVKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKADISATVYPDinvITGALKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  840 YLRQLPEPLISFRLYHELVGLAKdslkaeaeakaasRGRQDgSESEAVAvalagrlrELLRDLPPENRASLQYLLRHLRR 919
Cdd:cd04372     81 YFRDLPIPVITYDTYPKFIDAAK-------------ISNPD-ERLEAVH--------EALMLLPPAHYETLRYLMEHLKR 138

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1007393347  920 IVEVEQDNKMTPGNLGIVFGPTLLRPrPTEATvsLSSLVDYPHQARVIETLIVHYGLVF 978
Cdd:cd04372    139 VTLHEKDNKMNAENLGIVFGPTLMRP-PEDSA--LTTLNDMRYQILIVQLLITNEDVLF 194
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 778-978 8.48e-35

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: 131.75  E-value: 8.48e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  778 VPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHD---ISNVLKLYLRQLPEPLISFRLY 854
Cdd:cd04395     18 VPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGFDIDLQDPRWRDvnvVSSLLKSFFRKLPEPLFTNELY 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  855 HELVglakdslkaeaeakaaSRGRQDGSESEAVAvalagrLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGNL 934
Cdd:cd04395     98 PDFI----------------EANRIEDPVERLKE------LRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNL 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1007393347  935 GIVFGPTLLRPrpteATVSLSSLV-DYPHQARVIETLIVHYGLVF 978
Cdd:cd04395    156 AIVFGPTLVRT----SDDNMETMVtHMPDQCKIVETLIQHYDWFF 196
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 778-959 1.06e-34

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: 131.59  E-value: 1.06e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  778 VPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFE-NGKE-LVELSQASPHDISNVLKLYLRQLPEPLISFRLYH 855
Cdd:cd04387     16 VPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDtNNKDvSVMLSEMDVNAIAGTLKLYFRELPEPLFTDELYP 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  856 ELvglakdslkaeaeakaasrgrqdgSESEAVA--VALAGRLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGN 933
Cdd:cd04387     96 NF------------------------AEGIALSdpVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHN 151

                          170       180
                   ....*....|....*....|....*.
gi 1007393347  934 LGIVFGPTLLRPRPTEATVSLSSLVD 959
Cdd:cd04387    152 LATVFGPTLLRPSEKESKIPTNTMTD 177
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 778-964 1.67e-34

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: 130.59  E-value: 1.67e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  778 VPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKL-CQAfeNGKELVELSQASPHDI---SNVLKLYLRQLPEPLISFRL 853
Cdd:cd04403     16 VPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLrFAV--DHDEKLDLDDSKWEDIhviTGALKLFFRELPEPLFPYSL 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  854 YHELVGLAKDSlkaeaeaKAASRGRQdgseseavavalagrLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGN 933
Cdd:cd04403     94 FNDFVAAIKLS-------DYEQRVSA---------------VKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQN 151

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1007393347  934 LGIVFGPTLLRPRPTEATVSLSSLvdYPHQA 964
Cdd:cd04403    152 LAIVFGPTLLRPEQETGNIAVHMV--YQNQI 180
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 761-978 2.62e-33

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: 127.45  E-value: 2.62e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  761 QLFGQDFSHAARSAP--DGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHDISNVLK 838
Cdd:cd04404      4 QQFGVSLQFLKEKNPeqEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGEPVDFDQYEDVHLPAVILK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  839 LYLRQLPEPLISFRLYHELVGLakdslkaeaeakaasrgrQDGSESEAVAvalagRLRELLRDLPPENRASLQYLLRHLR 918
Cdd:cd04404     84 TFLRELPEPLLTFDLYDDIVGF------------------LNVDKEERVE-----RVKQLLQTLPEENYQVLKYLIKFLV 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  919 RIVEVEQDNKMTPGNLGIVFGPTLLRPRPTEATVSLSSLVDyphqaRVIETLIVHYGLVF 978
Cdd:cd04404    141 QVSAHSDQNKMTNSNLAVVFGPNLLWAKDASMSLSAINPIN-----TFTKFLLDHQDEIF 195
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
 781-971 3.55e-33

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: 127.51  E-value: 3.55e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  781 IVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHD------ISNVLKLYLRQLPEPLISFRLY 854
Cdd:cd04374     31 FVRKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLGLDPKTSTPGDVDLDNSeweiktITSALKTYLRNLPEPLMTYELH 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  855 HELVGLAKdslkaeaeakaasrgrQDGSESEAVAValagrlRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGNL 934
Cdd:cd04374    111 NDFINAAK----------------SENLESRVNAI------HSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNL 168

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1007393347  935 GIVFGPTLLRPRptEATVslSSLVDYPHQARVIETLI 971
Cdd:cd04374    169 GVVFGPTLLRPQ--EETV--AAIMDIKFQNIVVEILI 201
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 763-978 2.34e-30

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: 119.05  E-value: 2.34e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  763 FGQDFSHAARSAPDGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVEL--SQASPHDISNV---L 837
Cdd:cd04398      1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLLisPEDYESDIHSVaslL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  838 KLYLRQLPEPLISFRLYHELVGLAKdslkaeaeakaasrgrqdgSESEavaVALAGRLRELLRDLPPENRASLQYLLRHL 917
Cdd:cd04398     81 KLFFRELPEPLLTKALSREFIEAAK-------------------IEDE---SRRRDALHGLINDLPDANYATLRALMFHL 138

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1007393347  918 RRIVEVEQDNKMTPGNLGIVFGPTLLRPRPTeatvslsSLVDYPHQARVIETLIVHYGLVF 978
Cdd:cd04398    139 ARIKEHESVNRMSVNNLAIIWGPTLMNAAPD-------NAADMSFQSRVIETLLDNAYQIF 192
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 773-970 1.05e-29

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: 117.01  E-value: 1.05e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  773 SAPDGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHDISNVLKLYLRQLPEPLISFR 852
Cdd:cd04382     12 STSPMIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVDIHVICGCLKDFLRSLKEPLITFA 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  853 LYHELVgLAKDSLkaeaeakaasrgrqDGSESEAVavalagrLRELLRDLPPENRASLQYLLRHLRRIVEVEqDNKMTPG 932
Cdd:cd04382     92 LWKEFM-EAAEIL--------------DEDNSRAA-------LYQAISELPQPNRDTLAFLILHLQRVAQSP-ECKMDIN 148

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1007393347  933 NLGIVFGPTL---LRPRPTEATvslsSLVDYPHQARVIETL 970
Cdd:cd04382    149 NLARVFGPTIvgySVPNPDPMT----ILQDTVRQPRVVERL 185
C1_GMIP-like cd20816
protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP) ...
 705-755 7.26e-29

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: 109.65  E-value: 7.26e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1007393347  705 RTHRLRKLRTPAKCRECNSYVYFQGAECEECCLACHKKCLETLAIQCGHKK 755
Cdd:cd20816      1 QTHRFRRLRTPSKCRECDSYVYFNGAECEECGLACHKKCLETLAIQCGHKR 51
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 778-972 1.31e-28

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: 113.69  E-value: 1.31e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  778 VPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHDISNVLKLYLRQLPEPLISFRLYHEL 857
Cdd:cd04377     15 VPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLKQWLRELPEPLMTFELYENF 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  858 VGLAkdslkaeaeakaasrGRQDGSESeavavaLAGrLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGNLGIV 937
Cdd:cd04377     95 LRAM---------------ELEEKQER------VRA-LYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIV 152

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1007393347  938 FGPTLLRpRPtEATVSLSSLVDYPHQARVIETLIV 972
Cdd:cd04377    153 FAPCILR-CP-DTADPLQSLQDVSKTTTCVETLIK 185
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 778-971 8.99e-27

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: 109.09  E-value: 8.99e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  778 VPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHD---ISNVLKLYLRQLPEPLISFRLY 854
Cdd:cd04379     18 VPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELSEELYPDinvITGVLKDYLRELPEPLITPQLY 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  855 HELVglakdslkaeaeakaasrgrqdgsesEAVAVALAGR-------LRELLRDLPPENRASLQYLLRHLRRIVEVEQDN 927
Cdd:cd04379     98 EMVL--------------------------EALAVALPNDvqtnthlTLSIIDCLPLSAKATLLLLLDHLSLVLSNSERN 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1007393347  928 KMTPGNLGIVFGPTLLRPR--PTEATVSLS------SLVDYPHQARVIETLI 971
Cdd:cd04379    152 KMTPQNLAVCFGPVLMFCSqeFSRYGISPTskmaavSTVDFKQHIEVLHYLL 203
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 778-978 9.78e-27

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: 108.70  E-value: 9.78e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  778 VPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENG--KELVELSQASPHDISNVLKLYLRQLPEPLISFRLYH 855
Cdd:cd04386     20 IALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGtfSLPLDEFYSDPHAVASALKSYLRELPDPLLTYNLYE 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  856 ELVGLAKdslkaeaeakaasrgRQDGSEseavavalagRLRELLR---DLPPENRASLQYLLRHLRRIVEVEQDNKMTPG 932
Cdd:cd04386    100 DWVQAAN---------------KPDEDE----------RLQAIWRilnKLPRENRDNLRYLIKFLSKLAQKSDENKMSPS 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1007393347  933 NLGIVFGPTLLRPRpTEATVSLSSLVDYPHQARVIETLIVHYGLVF 978
Cdd:cd04386    155 NIAIVLAPNLLWAK-NEGSLAEMAAGTSVHVVAIVELIISHADWFF 199
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 778-978 2.08e-26

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: 107.91  E-value: 2.08e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  778 VPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHDISNVLKLYLRQLPEPLISFRLYHEL 857
Cdd:cd04376      9 VPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENHSVHDVAALLKEFFRDMPDPLLPRELYTAF 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  858 VGLAKDSLkaeaeakaasrgrQDGSESeavavalagrLRELLRDLPPENRASLQYLLRHLRRIVEVEQD----------- 926
Cdd:cd04376     89 IGTALLEP-------------DEQLEA----------LQLLIYLLPPCNCDTLHRLLKFLHTVAEHAADsidedgqevsg 145

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1007393347  927 NKMTPGNLGIVFGPTLLR-PRPTEATVSLSSL--VDYPHQARVIETLIVHYGLVF 978
Cdd:cd04376    146 NKMTSLNLATIFGPNLLHkQKSGEREFVQASLriEESTAIINVVQTMIDNYEELF 200
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 763-973 1.47e-25

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: 105.28  E-value: 1.47e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  763 FGQDFSHAARSAPDGVPFIVKKCVCEIERRALRTkGIYRVNGVKTRVEKLCQAFENGKE---LVELSQASPHDISNVLKL 839
Cdd:cd04384      3 FGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDSEQIpdlTKDVYIQDIHSVSSLCKL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  840 YLRQLPEPLISFRLYHELvglakdslkaeaeakaaSRGRQDGSESEAVAvalagRLRELLRDLPPENRASLQYLLRHLRR 919
Cdd:cd04384     82 YFRELPNPLLTYQLYEKF-----------------SEAVSAASDEERLE-----KIHDVIQQLPPPHYRTLEFLMRHLSR 139

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1007393347  920 IVEVEQDNKMTPGNLGIVFGPTLLRPRPTEATV--SLSSLVDYPHQARVIETLIVH 973
Cdd:cd04384    140 LAKYCSITNMHAKNLAIVWAPNLLRSKQIESACfsGTAAFMEVRIQSVVVEFILNH 195
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 778-972 1.82e-24

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: 101.99  E-value: 1.82e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  778 VPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHDISNVLKLYLRQLPEPLISFRLYHEL 857
Cdd:cd04407     15 VPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRELPEPLMTFAQYNDF 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  858 VglakdslkaeaeakaasRGRQDGSESEAVAVALAgrlreLLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGNLGIV 937
Cdd:cd04407     95 L-----------------RAVELPEKQEQLQAIYR-----VLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIV 152

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1007393347  938 FGPTLLR-PRPTEatvSLSSLVDYPHQARVIETLIV 972
Cdd:cd04407    153 FAPCLLRcPDSSD---PLTSMKDVAKTTTCVEMLIK 185
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 773-945 1.42e-23

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: 99.07  E-value: 1.42e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  773 SAPDGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASP-HDISNVLKLYLRQLPEPLISF 851
Cdd:cd04373     10 TSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHNLDLVSKDFTvNAVAGALKSFFSELPDPLIPY 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  852 RLYHELVGLAKDSlkaeaeakaasrgrqDGSESeavavaLAGrLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTP 931
Cdd:cd04373     90 SMHLELVEAAKIN---------------DREQR------LHA-LKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTS 147

                          170
                   ....*....|....
gi 1007393347  932 GNLGIVFGPTLLRP 945
Cdd:cd04373    148 ENLSICFWPTLMRP 161
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 778-978 8.26e-23

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: 97.80  E-value: 8.26e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  778 VPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFEN--GKELVELSQASPHDISNVLKLYLRQLPEPLisfrLYH 855
Cdd:cd04391     22 VPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAkfYEGTFLWDQVKQHDAASLLKLFIRELPQPL----LTV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  856 ELVGLAKDSlkaeaeakaasrgrQDGSESEAVAVALagRLRELLrdLPPENRASLQYLLRHLRRIVEVEQDNKMTPGNLG 935
Cdd:cd04391     98 EYLPAFYSV--------------QGLPSKKDQLQAL--NLLVLL--LPEANRDTLKALLEFLQKVVDHEEKNKMNLWNVA 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1007393347  936 IVFGPTL---LRPRPTEATVSLSSLVDYPHQARVIETLIVHYGLVF 978
Cdd:cd04391    160 MIMAPNLfppRGKHSKDNESLQEEVNMAAGCANIMRLLIRYQDLLW 205
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 761-973 2.73e-22

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: 95.57  E-value: 2.73e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  761 QLFGQDFSHAARSAPDGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQaSPHDISN---VL 837
Cdd:cd04383      1 KLFNGSLEEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPLADDQ-NDHDINSvagVL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  838 KLYLRQLPEPLISFRLYHELVGLAKdslkaeaeakaasrgrqdgSESEAvavALAGRLRELLRDLPPENRASLQYLLRHL 917
Cdd:cd04383     80 KLYFRGLENPLFPKERFEDLMSCVK-------------------LENPT---ERVHQIREILSTLPRSVIIVMRYLFAFL 137

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1007393347  918 RRIVEVEQDNKMTPGNLGIVFGPTLLRPRPTEATVSLSSLVDyphqaRVIETLIVH 973
Cdd:cd04383    138 NHLSQFSDENMMDPYNLAICFGPTLMPVPEGQDQVSCQAHVN-----ELIKTIIIH 188
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 776-947 3.06e-22

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: 95.61  E-value: 3.06e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  776 DGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGkELVELSQ-ASPHDISNVLKLYLRQLPEPLISFRLY 854
Cdd:cd04393     18 NGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSG-EEVDLSKeADVCSAASLLRLFLQELPEGLIPASLQ 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  855 HELVGLAKDSlkaeaeakaasrGRQDGSESeavavalagRLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGNL 934
Cdd:cd04393     97 IRLMQLYQDY------------NGEDEFGR---------KLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENL 155

                          170
                   ....*....|...
gi 1007393347  935 GIVFGPTLLRPRP 947
Cdd:cd04393    156 AAVFGPDVFHVYT 168
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
 762-942 5.00e-22

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: 94.73  E-value: 5.00e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  762 LFGQDFSHAAR-SAPD----GVPFIVKKCVCEIE-RRALRTKGIYRVNGVKTRVEKLCQAFENGKElVELSQAS----PH 831
Cdd:cd04400      1 IFGSPLEEAVElSSHKyngrDLPSVVYRCIEYLDkNRAIYEEGIFRLSGSASVIKQLKERFNTEYD-VDLFSSSlypdVH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  832 DISNVLKLYLRQLPEPLISFRLYHELVGLAkdslkaeaeakaasrgrqdgsESEAVAVALAGRLRELLRDLPPENRASLQ 911
Cdd:cd04400     80 TVAGLLKLYLRELPTLILGGELHNDFKRLV---------------------EENHDRSQRALELKDLVSQLPQANYDLLY 138

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1007393347  912 YLLRHLRRIVEVEQDNKMTPGNLGIVFGPTL 942
Cdd:cd04400    139 VLFSFLRKIIEHSDVNKMNLRNVCIVFSPTL 169
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 762-978 2.14e-21

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: 93.28  E-value: 2.14e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  762 LFGQDFS----HAARSAPDGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHDISNVL 837
Cdd:cd04390      2 VFGQRLEdtvaYERKFGPRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASLL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  838 KLYLRQLPEPLISFRLYHELVGLAKdslkaeaeakaasrgRQDGSESEAVavalaGRLRELLRDLPPENRASLQYLLRHL 917
Cdd:cd04390     82 KLYLRELPEPVIPWAQYEDFLSCAQ---------------LLSKDEEKGL-----GELMKQVSILPKVNYNLLSYICRFL 141

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1007393347  918 RRIVEVEQDNKMTPGNLGIVFGPTLLRPRpTEATVSLssLVDYPHQARVIETLIVHYGLVF 978
Cdd:cd04390    142 DEVQSNSSVNKMSVQNLATVFGPNILRPK-VEDPATI--MEGTPQIQQLMTVMISKHEPLF 199
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 776-942 7.92e-21

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: 91.34  E-value: 7.92e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  776 DGV--PFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFeNGKELVELSQASPHDISNVLKLYLRQLPEPLisfrL 853
Cdd:cd04381     16 DGIdlPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAY-NRRESPNLEEYEPPTVASLLKQYLRELPEPL----L 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  854 YHELVGLAKDSLkaeaeakaasrGRQDGSESEAvavalagRLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGN 933
Cdd:cd04381     91 TKELMPRFEEAC-----------GRPTEAEREQ-------ELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQN 152


                   ....*....
gi 1007393347  934 LGIVFGPTL 942
Cdd:cd04381    153 ISIVLSPTV 161
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 778-973 4.40e-20

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: 90.16  E-value: 4.40e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  778 VPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFEN----GKELVElSQASPHDISNVLKLYLRQLPEPLISFRL 853
Cdd:cd04396     32 IPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTppdyGKSFDW-DGYTVHDAASVLRRYLNNLPEPLVPLDL 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  854 YHELvglaKDSLKAEAEAKAASRGRQDGSESEAVAVALAgRLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGN 933
Cdd:cd04396    111 YEEF----RNPLRKRPRILQYMKGRINEPLNTDIDQAIK-EYRDLITRLPNLNRQLLLYLLDLLAVFARNSDKNLMTASN 185

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1007393347  934 LGIVFGPTLLR-------PRPTEATVSlsslvdyphqarVIETLIVH 973
Cdd:cd04396    186 LAAIFQPGILShpdhemdPKEYKLSRL------------VVEFLIEH 220
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 763-972 1.92e-17

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: 81.59  E-value: 1.92e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  763 FGQDFSHAArSAPDGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHDISNVLKLYLR 842
Cdd:cd04406      1 FGVELSRLT-SEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  843 QLPEPLISFRLYHELVglakdslkaeaeakaASRGRQDGSESeavavalAGRLRELLRDLPPENRASLQYLLRHLRRIVE 922
Cdd:cd04406     80 DLPNPLMTFELYEEFL---------------RAMGLQERRET-------VRGVYSVIDQLSRTHLNTLERLIFHLVRIAL 137

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1007393347  923 VEQDNKMTPGNLGIVFGPTLLRPRPTeaTVSLSSLVDYPHQARVIETLIV 972
Cdd:cd04406    138 QEETNRMSANALAIVFAPCILRCPDT--TDPLQSVQDISKTTTCVELIVC 185
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 777-978 1.16e-16

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: 80.15  E-value: 1.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  777 GVPFIVK---------KCVCE----IERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHDISNVLKLYLRQ 843
Cdd:cd04375      6 GVPLLVNlqrtgqplpRSIQQamrwLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQAYDVADMLKQYFRD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  844 LPEPLISFRLYHELVG----LAKDslkaeaeakaasrgrqdgSESEAVAVALagrlreLLrdLPPENRASLQYLLRHLRR 919
Cdd:cd04375     86 LPEPLLTNKLSETFIAifqyVPKE------------------QRLEAVQCAI------LL--LPDENREVLQTLLYFLSD 139

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1007393347  920 IVEVEQDNKMTPGNLGIVFGPTL--LRPRPTEATVSLSSL-----VDYPHQARVIETLIVHYGLVF 978
Cdd:cd04375    140 VAANSQENQMTATNLAVCLAPSLfhLNTSRRENSSPARRMqrkksLGKPDQKELSENKAAHQCLAY 205
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 794-946 2.45e-16

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: 79.04  E-value: 2.45e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  794 LRTKGIYRVNGVKTRVEKLCQAFENGKEL-VELSQASPHDISNVLKLYLRQLPEPLISFRLYHELVGLAKDSLKAEAEAK 872
Cdd:cd04392     24 LRVEGLFRKPGNSARQQELRDLLNSGTDLdLESGGFHAHDCATVLKGFLGELPEPLLTHAHYPAHLQIADLCQFDEKGNK 103

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1007393347  873 AASRGRQDGSESeavavalagrLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGNLGIVFGPTLLRPR 946
Cdd:cd04392    104 TSAPDKERLLEA----------LQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLICPR 167
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 285-360 9.28e-16

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: 73.53  E-value: 9.28e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1007393347   285 GVDAALLYAKNMAKYMKDLISYLEKRTTLEMEFAKGLQKIAHNCRQSVMQEPHM-PLLSIYSLALEQDLEFGHSMVQ 360
Cdd:smart00055   10 GFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKLRAVRDTEPEYgSLSKAWEVLLSETDALAKQHLE 86
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
 300-534 6.10e-15

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: 75.46  E-value: 6.10e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  300 MKDLISYLEKRTTLEMEFAKGLQKIAHNCRQsVMQEPHMpLLSIYSLALEQDLEFGHSMVQAVGTLQT--QTFMQPLTLR 377
Cdd:cd07652     21 AKEFATFLKKRAAIEEEHARGLKKLARTTLD-TYKRPDH-KQGSFSNAYHSSLEFHEKLADNGLRFAKalNEMSDELSSL 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  378 RLEHEKRRKEIKEAWHRAQRKLQEAESNLRKAKQGYVQRCEDHDKarflvAKAEEEQAGSapGAGSTATKTL-----DKR 452
Cdd:cd07652     99 AKTVEKSRKSIKETGKRAEKKVQDAEAAAEKAKARYDSLADDLER-----VKTGDPGKKL--KFGLKGNKSAaqhedELL 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  453 RRLEEEAKnkaeeamaTYRTCVADAKTQKQELEDT-KVTALRQIQEVIRQSDQTIKsatisyyqmMHMQtaplpvHFQML 531
Cdd:cd07652    172 RKVQAADQ--------DYASKVNAAQALRQELLSRhRPEAVKDLFDLILEIDAALR---------LQYQ------KYALP 228


                   ...
gi 1007393347  532 CES 534
Cdd:cd07652    229 NEL 231
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 794-971 2.64e-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: 72.89  E-value: 2.64e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  794 LRTKGIYRVNGVKTRVEKLCQAFENGKELveLSQASPHDISNVLKLYLRQLPEPLISFRlYHELVGLAKdslkaeaeakA 873
Cdd:cd04394     35 LSTEGLFRKSGSVVRQKELKAKLEGGEAC--LSSALPCDVAGLLKQFFRELPEPLLPYD-LHEALLKAQ----------E 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  874 ASRGRQDGSeseavAVALAGRLrellrdLPPENRASLQYLLRHLRRIVEVEQDNKMTPGNLGIVFGPTLLRPRPTEATVS 953
Cdd:cd04394    102 LPTDEERKS-----ATLLLTCL------LPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVIFAPNLFQSEEGGEKMS 170

                          170
                   ....*....|....*...
gi 1007393347  954 LSSLVDYPHQARVIETLI 971
Cdd:cd04394    171 SSTEKRLRLQAAVVQTLI 188
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 773-971 4.28e-14

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: 72.21  E-value: 4.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  773 SAPDGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEkLCQAFENGKELVELSQASPHDISNVLKLYLRQLPEPLISFR 852
Cdd:cd04388     10 SPPDVAPPLLIKLVEAIEKKGLESSTLYRTQSSSSLTE-LRQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPAP 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  853 LYHELVGLAKDSLkaeaeakaasrgrqdgSESEAvavalAGRLRELLR--DLPPENRASLQYLLRHLRRIVEVEQDNKMT 930
Cdd:cd04388     89 VYSEMISRAQEVQ----------------SSDEY-----AQLLRKLIRspNLPHQYWLTLQYLLKHFFRLCQSSSKNLLS 147

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1007393347  931 PGNLGIVFGPTLLRPRPTEAtvslsslvDYP-HQARVIETLI 971
Cdd:cd04388    148 ARALAEIFSPLLFRFQPASS--------DSPeFHIRIIEVLI 181
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 762-945 6.96e-14

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: 71.56  E-value: 6.96e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  762 LFGQDFSHAARSapDGVPFIVKKCVCEIERRALRTKGIYRVNG-VKTRVEKLCQaFENGKElVELSQASPHDISNVLKLY 840
Cdd:cd04402      1 LFGQPLSNICED--DNLPKPILDMLSLLYQKGPSTEGIFRRSAnAKACKELKEK-LNSGVE-VDLKAEPVLLLASVLKDF 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  841 LRQLPEPLISFRLYHELVGLAkdslkaeaeakaasrgrQDGSESEAVAvalagRLRELLRDLPPENRASLQYLLRHLRRI 920
Cdd:cd04402     77 LRNIPGSLLSSDLYEEWMSAL-----------------DQENEEEKIA-----ELQRLLDKLPRPNVLLLKHLICVLHNI 134

                          170       180
                   ....*....|....*....|....*
gi 1007393347  921 VEVEQDNKMTPGNLGIVFGPTLLRP 945
Cdd:cd04402    135 SQNSETNKMDAFNLAVCIAPSLLWP 159
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 795-973 4.15e-12

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: 66.26  E-value: 4.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  795 RTKGIYRVNGVKTRVEKLCQAFENGKelVELSQAS-PHDISNVLKLYLRQLPEPLISFRLYHELVglakdslkaeaeaka 873
Cdd:cd04389     39 QTEGIFRVPGDIDEVNELKLRVDQWD--YPLSGLEdPHVPASLLKLWLRELEEPLIPDALYQQCI--------------- 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  874 asrgrqDGSESEAVAValagrlrELLRDLPPENRASLQYLLRHLRRIV--EVEQDNKMTPGNLGIVFGPTLLRPRPTEAT 951
Cdd:cd04389    102 ------SASEDPDKAV-------EIVQKLPIINRLVLCYLINFLQVFAqpENVAHTKMDVSNLAMVFAPNILRCTSDDPR 168

                          170       180
                   ....*....|....*....|..
gi 1007393347  952 VSLSSLvdyPHQARVIETLIVH 973
Cdd:cd04389    169 VIFENT---RKEMSFLRTLIEH 187
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 778-973 2.10e-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: 2.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  778 VPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFE-NGKELVELSQASPHDISNVLKLYLRQLPEPLISFRLYHE 856
Cdd:cd04397     27 IPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDkNPTEVPDLSKENPVQLAALLKKFLRELPDPLLTFKLYRL 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  857 LVGLAKDSlkaeaeakaasrgrqDGSESEAVavalagrLRELLRDLPPENRASLQYLLRHLRRI-----VEVEQDNKMTP 931
Cdd:cd04397    107 WISSQKIE---------------DEEERKRV-------LHLVYCLLPKYHRDTMEVLFSFLKWVssfshIDEETGSKMDI 164

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1007393347  932 GNLGIVFGPTLLRPRPTEatvslSSLVDYPHQA-RVIETLIVH 973
Cdd:cd04397    165 HNLATVITPNILYSKTDN-----PNTGDEYFLAiEAVNYLIEN 202
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 706-751 2.43e-09

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: 54.01  E-value: 2.43e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1007393347   706 THRLRKLRTPAKCRECNSYVYF---QGAECEECCLACHKKCLETLAIQC 751
Cdd:smart00109    2 KHVFRTFTKPTFCCVCRKSIWGsfkQGLRCSECKVKCHKKCADKVPKAC 50
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 776-971 7.02e-08

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: 54.27  E-value: 7.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  776 DGVPFIVKK----CVCEIERRALRTKGIYRVNGVKTRVEKLCQ----AFENGKelVELSQASPHDISNVLKLYLRQLPEP 847
Cdd:cd04380     44 SEVPLSIPKeiwrLVDYLYTRGLAQEGLFEEPGLPSEPGELLAeirdALDTGS--PFNSPGSAESVAEALLLFLESLPDP 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  848 LISFRLYHELvglakdslkaeaeakaasrgrqdgseSEAVAvALAGRLRELLRD-LPPENRASLQYLLRHLRRIVEVEQD 926
Cdd:cd04380    122 IIPYSLYERL--------------------------LEAVA-NNEEDKRQVIRIsLPPVHRNVFVYLCSFLRELLSESAD 174

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1007393347  927 NKMTPGNLGIVFGPTLLRPRPTEATVSLSslVDYPHQARVIETLI 971
Cdd:cd04380    175 RGLDENTLATIFGRVLLRDPPRAGGKERR--AERDRKRAFIEQFL 217
F-BAR_PSTPIP cd07647
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 285-435 1.22e-07

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Vetebrates contain two Proline-Serine-Threonine Phosphatase-Interacting Proteins (PSTPIPs), PSTPIP1 and PSTPIP2. PSTPIPs are mainly expressed in hematopoietic cells and are involved in the regulation of cell adhesion and motility. Mutations in PSTPIPs have been shown to cause autoinflammatory disorders. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain, while PSTPIP2 contains only the N-terminal F-BAR domain. 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: 153331 [Multi-domain]  Cd Length: 239  Bit Score: 54.02  E-value: 1.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  285 GVDAALLYAKNMAKYMKDLISYLEKRTTLEMEFAKGLQKIAHncrqsvmqephmpllsiysLALEQDlEFGhSMVQAVGT 364
Cdd:cd07647      6 GFDTLLQRLKEGKKMCKELEDFLKQRAKAEEDYGKALLKLSK-------------------SAGPGD-EIG-TLKSSWDS 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  365 LQTQT---------FMQPLT--LRRLE-----HEKRRKEIKEAWHRAQRKLQEAESNLRKAKQGYVQRCEDHDKA----- 423
Cdd:cd07647     65 LRKETenvanahiqLAQSLReeAEKLEefrekQKEERKKTEDIMKRSQKNKKELYKKTMKAKKSYEQKCREKDKAeqaye 144

                          170
                   ....*....|....
gi 1007393347  424 --RFLVAKAEEEQA 435
Cdd:cd07647    145 ksSSGAQPKEAEKL 158
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 707-751 1.86e-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: 48.67  E-value: 1.86e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1007393347  707 HRLRK--LRTPAKCRECNSYVYF---QGAECEECCLACHKKCLETLAIQC 751
Cdd:cd00029      1 HRFVPttFSSPTFCDVCGKLIWGlfkQGLKCSDCGLVCHKKCLDKAPSPC 50
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 820-978 5.61e-07

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: 51.56  E-value: 5.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  820 KELVELSQASPHDISNVLKLYLRQLPEPLISFRLYHELVGLAkdslkaeaeakaasrgRQDGSESEAVAVALAGRLRELL 899
Cdd:cd04399     68 KEVIILKKFEPSTVASVLKLYLLELPDSLIPHDIYDLIRSLY----------------SAYPPSQEDSDTARIQGLQSTL 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  900 RDLPPENRASLQYLLRHLRRIVEV----EQDNKMTPgNLGIVFGPTLLRPRpTEATVSLSSlvdyPHQARVIETLIVHYG 975
Cdd:cd04399    132 SQLPKSHIATLDAIITHFYRLIEItkmgESEEEYAD-KLATSLSREILRPI-IESLLTIGD----KHGYKFFRDLLTHKD 205


                   ...
gi 1007393347  976 LVF 978
Cdd:cd04399    206 QIF 208
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 710-752 1.61e-06

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: 46.28  E-value: 1.61e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1007393347  710 RKLRTPAKCRECNSYVYF---QGAECEECCLACHKKCLETLAIQCG 752
Cdd:pfam00130    6 RNFKQPTFCDHCGEFLWGlgkQGLKCSWCKLNVHKRCHEKVPPECG 51
C1_ScPKC1-like_rpt1 cd20822
first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...
 705-751 1.88e-06

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: 45.74  E-value: 1.88e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1007393347  705 RTHRLRKLR--TPAKCRECNSYVYFQGAECEECCLACHKKCLETLAIQC 751
Cdd:cd20822      1 RGHKFVQKQfyQIMRCAVCGEFLVNAGYQCEDCKYTCHKKCYEKVVTKC 49
C1_TNS2-like cd20826
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ...
 708-753 2.38e-06

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: 45.46  E-value: 2.38e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1007393347  708 RLRKLRTPAKCRECNSYVYFQGAECEECCLACHKKCLETLAIQCGH 753
Cdd:cd20826      6 KEKSFRKPRTCDVCKQIIWNEGSSCRVCKYACHRKCEPKVTAACSP 51
C1_cPKC_nPKC_rpt1 cd20792
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
 708-751 4.68e-06

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: 44.93  E-value: 4.68e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1007393347  708 RLRKLRTPAKCRECNSYVY---FQGAECEECCLACHKKCLETLAIQC 751
Cdd:cd20792      5 VATFFKQPTFCSHCKDFIWglgKQGYQCQVCRFVVHKRCHEYVVFKC 51
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 275-415 1.49e-05

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: 46.95  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  275 VDVLLQRCEGGVDaallyaknmakYMKDLISYLEKRTTLEMEFAKGLQKIAhncrQSVMQEPHMPLLSIYSlaLEQDLEF 354
Cdd:cd07610      2 FELLEKRTELGLD-----------LLKDLREFLKKRAAIEEEYAKNLQKLA----KKFSKKPESGKTSLGT--SWNSLRE 64

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1007393347  355 GHSMVQAVGTLQTQTFMQ----PLTLRRLEHEKRRKEIKEAWHRAQRKLQEAESNL-RKAKQGYVQ 415
Cdd:cd07610     65 ETESAATVHEELSEKLSQlirePLEKVKEDKEQARKKELAEGEKLKKKLQELWAKLaKKADEEYRE 130
F-BAR_NOSTRIN cd07658
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Nitric Oxide Synthase TRaffic ...
 292-513 1.68e-05

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Nitric Oxide Synthase TRaffic INducer (NOSTRIN); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Nitric Oxide Synthase TRaffic INducer (NOSTRIN) is expressed in endothelial and epithelial cells and is involved in the regulation, trafficking and targeting of endothelial NOS (eNOS). NOSTRIN facilitates the endocytosis of eNOS by coordinating the functions of dynamin and the Wiskott-Aldrich syndrome protein (WASP). Increased expression of NOSTRIN may be correlated to preeclampsia. NOSTRIN contains an N-terminal F-BAR domain and a C-terminal SH3 domain. 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. The F-BAR domain of NOSTRIN is necessary and sufficient for its membrane association and is responsible for its subcellular localization.


Pssm-ID: 153342 [Multi-domain]  Cd Length: 239  Bit Score: 47.38  E-value: 1.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  292 YAKNMAKYMKDLISYLEKRTTLEMEFAKGLQKIAHN----------------CRQSVMQEPHMPLLSIYSLALEQDLefg 355
Cdd:cd07658     13 YVKQGGDFCKELATVLQERAELELNYAKGLSKLSGKlskasksvsgtlssawTCVAEEMESEADIHRNLGSALTEEA--- 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  356 hsmvqavgtlqtqtfMQPLTLRRLEHEKRRKEIKEAWHRAQRKLQEAESNLRKAKQGYVQRCEDHDKARFLV-------- 427
Cdd:cd07658     90 ---------------IKPLRQVLDEQHKTRKPVENEVDKAAKLLTDWRSEQIKVKKKLHGLARENEKLQDQVednkqsct 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  428 -AKAEEEQAGSAPGAGSTATKTLDKRRRLEEEAKNKAEeamaTYRTCVADAKTQKQELEDTKVTALRQIQEVIRQSDQTI 506
Cdd:cd07658    155 kQKMLNKLKKSAEVQDKEDEKLEAKRKKGEESRLKAEN----EYYTCCVRLERLRLEWESALRKGLNQYESLEEERLQHL 230


                   ....*..
gi 1007393347  507 KSATISY 513
Cdd:cd07658    231 KHSLSQY 237
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 276-423 2.66e-05

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 1 (PSTPIP1), also known as CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain. 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: 153355 [Multi-domain]  Cd Length: 242  Bit Score: 46.88  E-value: 2.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  276 DVLLQRceggvdaaLLYAKNMAKYMKDLisyLEKRTTLEMEFAKGLQKIAhncRQSVMQEPHMPLLSIYSLALEQDLEFG 355
Cdd:cd07671      8 EILLQR--------LLDGRKMCKDVEEL---LKQRAQAEERYGKELVQIA---RKAGGQTEINTLKASFDQLKQQIENIG 73

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1007393347  356 HSMVQAVGTLQTQtfmqpltLRRLEH-EKRRKEIKEAWHRAQRKLQEAESNLRK----AKQGYVQRCEDHDKA 423
Cdd:cd07671     74 NSHIQLAGMLREE-------LKSLEEfRERQKEQRKKYEAVMERVQKSKVSLYKktmeSKKTYEQRCREADEA 139
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
 705-752 4.93e-05

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: 42.01  E-value: 4.93e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1007393347  705 RTHRL--RKLRTPAKCRECNSYVYFQGAE--CEECCLACHKKCLETLAIQCG 752
Cdd:cd20821      1 RPHRFvsKTVIKPETCVVCGKRIKFGKKAlkCKDCRVVCHPDCKDKLPLPCV 52
C1_RASGRP2 cd20861
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 2 ...
 715-751 8.41e-05

protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 2 (RASGRP2) and similar proteins; RASGRP2, also called calcium and DAG-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), Cdc25-like protein (CDC25L), or F25B3.3 kinase-like protein, functions as a calcium- and DAG-regulated nucleotide exchange factor specifically activating Rap through the exchange of bound GDP for GTP. It may also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. RASGRP2 is also involved in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation, as well as in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. 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: 410411  Cd Length: 56  Bit Score: 41.41  E-value: 8.41e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1007393347  715 PAKCRECNSYV---YFQGAECEECCLACHKKCLETLAIQC 751
Cdd:cd20861     14 PVACRHCKNLIlgiYKQGLKCRACGVNCHKQCKDHLSIEC 53
C1_VAV cd20810
protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function ...
 715-752 1.63e-04

protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and as scaffold proteins, and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. 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: 410360  Cd Length: 52  Bit Score: 40.32  E-value: 1.63e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1007393347  715 PAKCRECNSY---VYFQGAECEECCLACHKKCLETLAiQCG 752
Cdd:cd20810     13 PTTCSVCKKLlkgLFFQGYKCSVCGAAVHKECIAKVK-RCG 52
C1_nPKC_theta-like_rpt2 cd20837
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 707-751 1.93e-04

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: 40.11  E-value: 1.93e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1007393347  707 HRLR--KLRTPAKCRECNSYVY---FQGAECEECCLACHKKCLETLAIQC 751
Cdd:cd20837      1 HRFKvyNYMSPTFCDHCGSLLWglfRQGLKCEECGMNVHHKCQKKVANLC 50
C1_KSR cd20812
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ...
 707-752 1.95e-04

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: 40.00  E-value: 1.95e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1007393347  707 HRL-RKLRTPAKCRECNSYVYFqGAECEECCLACHKKCLETLAIQCG 752
Cdd:cd20812      3 HRFsKKLFMRQTCDYCHKQMFF-GLKCKDCKYKCHKKCAKKAPPSCG 48
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 275-325 2.30e-04

Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The cytosolic endocytic adaptor proteins in fungi carry this domain at the N-terminus; several of these have been referred to as muniscin proteins. These N-terminal BAR, N-BAR, and EFC/F-BAR domains are found in proteins that regulate membrane trafficking events by inducing membrane tubulation. The domain dimerizes into a curved structure that binds to liposomes and either senses or induces the curvature of the membrane bilayer to cause biophysical changes to the shape of the bilayer; it also thereby recruits other trafficking factors, such as the GTPase dynamin. Most EFC/F-BAR domain-family members localize to actin-rich structures.


Pssm-ID: 459868 [Multi-domain]  Cd Length: 78  Bit Score: 40.72  E-value: 2.30e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1007393347  275 VDVLLQRCEGGVDAallyaknmakyMKDLISYLEKRTTLEMEFAKGLQKIA 325
Cdd:pfam00611    2 FKVLLKRLKQGIKL-----------LEELASFLKERAEIEEEYAKKLQKLA 41
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
 707-752 2.53e-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: 39.95  E-value: 2.53e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1007393347  707 HRL--RKLRTPAKCRECNSYVY---FQGAECEECCLACHKKCLETLAIQCG 752
Cdd:cd20809      1 HKFivRTFSTPTKCNHCTSLMVglvRQGLVCEVCGYACHVSCADKAPQVCP 51
C1_nPKC_theta-like_rpt1 cd20834
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 713-751 3.94e-04

first 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 domains. 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 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: 410384  Cd Length: 61  Bit Score: 39.61  E-value: 3.94e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1007393347  713 RTPAKCRECNSYVY-F--QGAECEECCLACHKKCLETLAIQC 751
Cdd:cd20834     16 RQPTFCSVCKEFLWgFnkQGYQCRQCNAAVHKKCHDKILGKC 57
C1_Munc13-1 cd20858
protein kinase C conserved region 1 (C1 domain) found in Munc13-1 and similar proteins; ...
 714-751 3.95e-04

protein kinase C conserved region 1 (C1 domain) found in Munc13-1 and similar proteins; Munc13-1, also called protein unc-13 homolog A (Unc13A), is a diacylglycerol (DAG) receptor that plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. It is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Loss of MUNC13-1 function causes microcephaly, cortical hyperexcitability, and fatal myasthenia. 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: 410408  Cd Length: 60  Bit Score: 39.69  E-value: 3.95e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1007393347  714 TPAKCRECNSYVY---FQGAECEECCLACHKKCLETLAIQC 751
Cdd:cd20858     17 TPTYCYECEGLLWgiaRQGMRCTECGVKCHEKCQDLLNADC 57
C1_PIK3R-like_rpt2 cd20830
second protein kinase C conserved region 1 (C1 domain) found in uncharacterized ...
 718-753 5.90e-04

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: 38.77  E-value: 5.90e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1007393347  718 CRECNSY---VYFQGAECEECCLACHKKCLETLAIQCGH 753
Cdd:cd20830     14 CDKCGKFlfgLVHQGLQCQDCGLVCHRTCAATGLPKCEP 52
C1_RASSF1-like cd20820
protein kinase C conserved region 1 (C1 domain) found in the Ras association domain-containing ...
 712-751 7.57e-04

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: 38.58  E-value: 7.57e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1007393347  712 LRTPAKCRECNSY---VYFQGAECEECCLACHKKCLETLAIQC 751
Cdd:cd20820      9 LEQPTWCDLCGSVilgLFRKCLRCANCKMTCHPRCRSLVCLTC 51
C1_Munc13 cd20807
protein kinase C conserved region 1 (C1 domain) found in the Munc13 family; The Munc13 gene ...
 714-751 1.49e-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: 37.84  E-value: 1.49e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1007393347  714 TPAKCRECNSYVY---FQGAECEECCLACHKKCLETLAIQC 751
Cdd:cd20807     10 TPTYCYECEGLLWgiaRQGVRCTECGVKCHEKCKDLLNADC 50
C1_cPKC_rpt2 cd20836
second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
 714-753 1.55e-03

second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. 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: 410386  Cd Length: 54  Bit Score: 37.70  E-value: 1.55e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1007393347  714 TPAKCRECNSYVY---FQGAECEECCLACHKKCLETLAIQCGH 753
Cdd:cd20836     10 SPTFCDHCGSLLYgliHQGMKCDTCDMNVHKRCVKNVPSLCGT 52
C1_RASGRP cd20808
protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein ...
 713-751 1.59e-03

protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein (RASGRP) family; The RASGRP family includes RASGRP1-4. They function as cation-, usually calcium-, and diacylglycerol (DAG)-regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. RASGRP1, also called calcium and DAG-regulated guanine nucleotide exchange factor II (CalDAG-GEFII) or Ras guanyl-releasing protein, activates the Erk/MAP kinase cascade and regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. RASGRP1 also regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways. RASGRP2, also called calcium and DAG-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), Cdc25-like protein (CDC25L), or F25B3.3 kinase-like protein, specifically activates Rap and may also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. RASGRP2 is involved in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation, as well as in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. RASGRP3, also called calcium and DAG-regulated guanine nucleotide exchange factor III (CalDAG-GEFIII), or guanine nucleotide exchange factor for Rap1, is a guanine nucleotide-exchange factor activating H-Ras, R-Ras and Ras-associated protein-1/2. It functions as an important mediator of signaling downstream from receptor coupled phosphoinositide turnover in B and T cells. RASGRP4 may function in mast cell differentiation. 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: 410358  Cd Length: 52  Bit Score: 37.70  E-value: 1.59e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1007393347  713 RTPAKCRECNSY---VYFQGAECEECCLACHKKCLETLAIQC 751
Cdd:cd20808     10 FKPTFCDHCTGLlwgLIKQGYKCKDCGINCHKHCKDLVVVEC 51
C1_RASGRP4 cd20863
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 4 ...
 713-751 1.68e-03

protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 4 (RASGRP4) and similar proteins; RASGRP4 functions as a cation- and diacylglycerol (DAG)-regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. It may function in mast cell differentiation. 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: 410413  Cd Length: 57  Bit Score: 37.83  E-value: 1.68e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1007393347  713 RTPAKCRECNSY---VYFQGAECEECCLACHKKCLETLAIQC 751
Cdd:cd20863     12 KKPTFCDSCSGFlwgVTKQGYRCQDCGINCHKHCKDQVDVEC 53
C1_Sbf-like cd20827
protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf ...
 706-751 1.96e-03

protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf and similar proteins; This group includes Drosophila melanogaster SET domain binding factor (Sbf), the single homolog of human MTMR5/MTMR13, and similar proteins, that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs) which may function as guanine nucleotide exchange factors (GEFs). Sbf is a pseudophosphatase that coordinates both phosphatidylinositol 3-phosphate (PI(3)P) turnover and Rab21 GTPase activation in an endosomal pathway that controls macrophage remodeling. It also functions as a GEF that promotes Rab21 GTPase activation associated with PI(3)P endosomes. Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 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: 410377  Cd Length: 53  Bit Score: 37.40  E-value: 1.96e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1007393347  706 THRLRK--LRTPAKCRECNSYVY---FQGAECEECCLACHKKCLETLAIQC 751
Cdd:cd20827      1 PHRFEKhnFTTPTYCDYCSSLLWglvKTGMRCADCGYSCHEKCLEHVPKNC 51
C1_MRCKalpha cd20864
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related ...
 705-751 2.06e-03

protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related Cdc42-binding kinase alpha (MRCK alpha) and similar proteins; MRCK alpha, also called Cdc42-binding protein kinase alpha, DMPK-like alpha, or myotonic dystrophy protein kinase-like alpha, is a serine/threonine-protein kinase expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK alpha is an important downstream effector of Cdc42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. 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: 410414  Cd Length: 60  Bit Score: 37.69  E-value: 2.06e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1007393347  705 RTHR--LRKLRTPAKCRECNSYVY---FQGAECEECCLACHKKCLETLAIQC 751
Cdd:cd20864      1 KAHQfvVKSFTTPTKCNQCTSLMVgliRQGCTCEVCGFSCHVTCADKAPSVC 52
F-BAR_FCHO cd07648
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; ...
 291-432 2.47e-03

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: 41.17  E-value: 2.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  291 LYaKNMAK---YMKDLISYLEKRTTLEMEFAKGLQKIAHNCRQSVMQEPHMPLLSIYSLALEQDLEFGHSMVQavgtlQT 367
Cdd:cd07648     10 LY-HNMKHgqiAVKELADFLRERATIEETYSKALNKLAKQASNSSQLGTFAPLWLVLRVSTEKLSELHLQLVQ-----KL 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1007393347  368 QTFMQPLTLRRLEHEKRRKEIKEAWHRAQRKLQEAES---NLRKAKQGYVQRCEDHDKARFLVAKAEE 432
Cdd:cd07648     84 QELIKDVQKYGEEQHKKHKKVKEEESGTAEAVQAIQTttaALQKAKEAYHARCLELERLRRENASPKE 151
C1_cPKC_rpt1 cd20833
first protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
 710-751 3.48e-03

first protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. 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: 410383  Cd Length: 58  Bit Score: 37.00  E-value: 3.48e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1007393347  710 RKLRTPAKCRECNSYVY---FQGAECEECCLACHKKCLETLAIQC 751
Cdd:cd20833      8 RFFKQPTFCSHCTDFIWgfgKQGFQCQVCSFVVHKRCHEFVTFSC 52
C1_RASGRP1 cd20860
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 1 ...
 715-754 3.73e-03

protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 1 (RASGRP1) and similar proteins; RASGRP1, also called calcium and DAG-regulated guanine nucleotide exchange factor II (CalDAG-GEFII) or Ras guanyl-releasing protein, functions as a calcium- and diacylglycerol (DAG)-regulated nucleotide exchange factor specifically activating Ras through the exchange of bound GDP for GTP. It activates the Erk/MAP kinase cascade and regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. RASGRP1 also regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways. 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: 410410  Cd Length: 55  Bit Score: 36.83  E-value: 3.73e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1007393347  715 PAKCRECNSYVY---FQGAECEECCLACHKKCLETLAIQCGHK 754
Cdd:cd20860     13 PTFCDNCAGFLWgviKQGYRCKDCGMNCHKQCKDLVVFECKKR 55
C1_MTMR-like cd20828
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to ...
 714-752 4.32e-03

protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to myotubularin-related proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs), such as MTMR5 and MTMR13. MTMRs may function as guanine nucleotide exchange factors (GEFs). Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 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: 410378  Cd Length: 57  Bit Score: 36.65  E-value: 4.32e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1007393347  714 TPAKCRECNS---YVYFQGAECEECCLACHKKCLETLAIQCG 752
Cdd:cd20828     15 TPTNCDYCLQilwGIVKKGMKCSECGYNCHEKCQPQVPKQCS 56
F-BAR_FCHO2 cd07673
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; ...
 301-516 4.58e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. The specific function of FCH domain Only 2 (FCHO2) is still unknown. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO1 and 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: 153357 [Multi-domain]  Cd Length: 269  Bit Score: 40.43  E-value: 4.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  301 KDLISYLEKRTTLEMEFAKGLQKIAHNCRQSVMQEPHMPLLSIYSLALEQDLEFGHSMVQAVGTLQTQtfMQPLTLRRLE 380
Cdd:cd07673     29 KELSDFIRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLANCHLELVRKLQELIKE--VQKYGEEQVK 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  381 HEKRRKEIKEAWHRAQRKLQEAESNLRKAKQGYVQRCEDHDKArflvaKAEEEQAGSAPGAGSTATKTLDkrrrleeeak 460
Cdd:cd07673    107 SHKKTKEEVAGTLEAVQNIQSITQALQKSKENYNAKCLEQERL-----KKEGATQREIEKAAVKSKKATE---------- 171

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1007393347  461 nkaeeamaTYRTCV---ADAKT---QK-----QELEDTKVTALRQIQEVIRQSDQTIKSATISYYQM 516
Cdd:cd07673    172 --------SYKLYVekyALAKAdfeQKmtetaQKFQDIEETHLIRIKEIIGSYSNSVKEIHIQIGQV 230
C1_TNS3_v cd20889
protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar ...
 706-752 5.36e-03

protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar proteins; 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. This model corresponds to the C1 domain found in TNS3 variant. Typical TNS3 does not contain 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: 410439  Cd Length: 56  Bit Score: 36.40  E-value: 5.36e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1007393347  706 THRLRKLRTPAKCRECNSYVYFQGAECEECCLACHKKCLETLAIQCG 752
Cdd:cd20889      4 TFKNKTFKKPKVCSICKQVIDSQGISCRVCKYACHKKCEAKVVTPCF 50
C1_DGKtheta_typeV_rpt1 cd20803
first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
 707-751 5.59e-03

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: 36.13  E-value: 5.59e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1007393347  707 HRLRK--LRTPAKCRECNSYVY---FQGAECEECCLACHKKCLETLAIQC 751
Cdd:cd20803      2 HSFRKktFHKPTYCHHCTDLLWgllNQGYQCEVCNFVSHERCLKTVVTPC 51
C1_PKD_rpt2 cd20796
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D ...
 715-751 5.76e-03

second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D (PKD); PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain 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: 410346  Cd Length: 54  Bit Score: 36.11  E-value: 5.76e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1007393347  715 PAKCRECNSY---VYFQGAECEECCLACHKKCLETLAIQC 751
Cdd:cd20796     12 PTVCQHCKKLlkgLFRQGLQCKDCKFNCHKKCAEKVPKDC 51
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 294-413 6.26e-03

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.


Pssm-ID: 153271 [Multi-domain]  Cd Length: 194  Bit Score: 39.35  E-value: 6.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  294 KNMAKYMKDLISYLEKRTTLEMEFAKGLQKIAHNCRQSVMQEPHMPLLSIYSLALEQDlEFGHSMVQAVgtlqTQTFMQP 373
Cdd:cd07307     10 KKLIKDTKKLLDSLKELPAAAEKLSEALQELGKELPDLSNTDLGEALEKFGKIQKELE-EFRDQLEQKL----ENKVIEP 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  374 LTL-----------RRLEHEKRRKEI---KEAWHRAQRK------LQEAESNLRKAKQGY 413
Cdd:cd07307     85 LKEylkkdlkeikkRRKKLDKARLDYdaaREKLKKLRKKkkdsskLAEAEEELQEAKEKY 144
C1_Myosin-IXa cd20883
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar ...
 715-754 6.96e-03

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar proteins; Myosin-IXa, also called unconventional myosin-9a (Myo9a), is a single-headed, actin-dependent motor protein of the unconventional myosin IX class. It is expressed in several tissues and is enriched in the brain and testes. Myosin-IXa contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating domain (RhoGAP). Myosin-IXa binds the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor (AMPAR) GluA2 subunit, and plays a key role in controlling the molecular structure and function of hippocampal synapses. Moreover, Myosin-IXa functions in epithelial cell morphology and differentiation, such that its knockout mice develop hydrocephalus and kidney dysfunction. Myosin-IXa regulates collective epithelial cell migration by targeting RhoGAP activity to cell-cell junctions. Myosin-IXa negatively regulates Rho GTPase signaling, and functions as a regulator of kidney tubule function. 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: 410433  Cd Length: 58  Bit Score: 36.10  E-value: 6.96e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1007393347  715 PAKCRECNSYVYF--QGAECEECCLACHKKCLETLAIQCGHK 754
Cdd:cd20883     16 PTYCEYCSSLIWMmdRAYVCKLCRYACHKKCCLKTTTKCSKK 57
F-BAR_PSTPIP2 cd07672
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 284-429 7.95e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 2; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 2 (PSTPIP2), also known as Macrophage Actin-associated tYrosine Phosphorylated protein (MAYP), is mostly expressed in hematopoietic cells but is also expressed in the brain. It is involved in regulating cell adhesion and motility. Mutations in the gene encoding murine PSTPIP2 can cause autoinflammatory disorders such as chronic multifocal osteomyelitis and macrophage autoinflammatory disease. PSTPIP2 contains an N-terminal F-BAR domain and lacks the PEST motifs and SH3 domain that are found in PSTPIP1. 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: 153356 [Multi-domain]  Cd Length: 240  Bit Score: 39.55  E-value: 7.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393347  284 GGVDAALLYAKNMAKYMKDLISYLEKRTTLEMEFAKGLQKIAHN--CRQSVMQEPHMPLlSIYSLALEQdleFGHSMVQA 361
Cdd:cd07672      5 GGYDCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELLNLSKKkpCGQTEINTLKRSL-DVFKQQIDN---VGQSHIQL 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1007393347  362 VGTLQTQTF-MQPLTLRRLEHEKRRKEIKEAWHRaQRKLQEAESnlRKAKQGYVQRCEDHDKARFLVAK 429
Cdd:cd07672     81 AQTLRDEAKkMEDFRERQKLARKKIELIMDAIHK-QRAMQFKKT--MESKKNYEQKCRDKDEAEQAVNR 146
C1_nPKC_epsilon-like_rpt2 cd20838
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 707-754 8.12e-03

second 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 domain. 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 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: 410388  Cd Length: 55  Bit Score: 35.71  E-value: 8.12e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1007393347  707 HR--LRKLRTPAKCRECNSYVY---FQGAECEECCLACHKKCLETLAIQCGHK 754
Cdd:cd20838      3 HRfsVHNYKRPTFCDHCGSLLYglyKQGLQCKVCKMNVHKRCQKNVANNCGVN 55
 
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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