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Conserved domains on  [gi|754348057|ref|XP_011270414|]
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hypothetical protein CAOG_08784 [Capsaspora owczarzaki ATCC 30864]

Protein Classification

PX and BAR domain-containing protein; BAR and SH3 domain-containing protein( domain architecture ID 10311773)

PX (Phox homology) and BAR (Bin/Amphiphysin/Rvs) domain-containing protein, similar to sorting nexins that are involved in regulating membrane traffic and protein sorting in the endosomal system| BAR (Bin/Amphiphysin/Rvs) and SH3 (Src homology 3) domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
552-725 3.15e-55

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: 188.66  E-value: 3.15e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 552 PLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDPLVNEEYcqqNIHAVAGVLKLYFRELPTPLFPFEFYE 631
Cdd:cd00159    1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDY---DVHDVASLLKLYLRELPEPLIPFELYD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 632 PLINIIRyTTDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGPTLIRAPADNLAAMVaD 711
Cdd:cd00159   78 EFIELAK-IEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDDELLE-D 155
                        170
                 ....*....|....
gi 754348057 712 TGSQCQIVSMIIQE 725
Cdd:cd00159  156 IKKLNEIVEFLIEN 169
BAR super family cl12013
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
35-308 1.34e-30

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


The actual alignment was detected with superfamily member cd07656:

Pssm-ID: 472257 [Multi-domain]  Cd Length: 241  Bit Score: 120.90  E-value: 1.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057  35 SQEVEQLKLFQHRTESKVAFMQDVQEFLKKRAEVEQEYAQKLDKVAEKFAHKLKHTSYGRYtllhnnslsspadgsaspl 114
Cdd:cd07656    1 QQLSEQLKCLDLRTEAQVQLLADLQDYFRRRAEIELEYSRSLEKLADRFSSKHKNEKSKRE------------------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 115 vigaagaslpsplvsptslenAVHPQTPVDVWTVLIENCRKTSRSRAALATRYGTELLDFTAEMERETVAGARQCHDYGL 194
Cdd:cd07656   62 ---------------------DWSLLSPVNCWNTLLVQTKQESRDHSTLSDIYSNNLVQRLGQMSEDLQRISKKCREIGS 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 195 KLHAELSESLAHLET---TAHSFHGLSAKAASAKAKVEDAKKKLESGSVNSKIISMLGKNVEKELHKREDTAAVQERRAS 271
Cdd:cd07656  121 QLHDELLRVLNELQTamkTYHTYHAESKSAERKLKEAEKQEEKQEQSPEKKLERSRSSKKIEKEVEKRQAKYSEAKLKCT 200
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 754348057 272 NAFNDYLFAIDVANAHKNQFFEHEIVELTALHDRFYH 308
Cdd:cd07656  201 KARNEYLLNLAAANATIHKYFVQDLSDLIDCMDLGFH 237
 
Name Accession Description Interval E-value
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
552-725 3.15e-55

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: 188.66  E-value: 3.15e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 552 PLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDPLVNEEYcqqNIHAVAGVLKLYFRELPTPLFPFEFYE 631
Cdd:cd00159    1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDY---DVHDVASLLKLYLRELPEPLIPFELYD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 632 PLINIIRyTTDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGPTLIRAPADNLAAMVaD 711
Cdd:cd00159   78 EFIELAK-IEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDDELLE-D 155
                        170
                 ....*....|....
gi 754348057 712 TGSQCQIVSMIIQE 725
Cdd:cd00159  156 IKKLNEIVEFLIEN 169
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
552-726 1.98e-54

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


Pssm-ID: 214618  Cd Length: 174  Bit Score: 186.70  E-value: 1.98e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057   552 PLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDPLVNEEycQQNIHAVAGVLKLYFRELPTPLFPFEFYE 631
Cdd:smart00324   4 PIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDLS--EYDVHDVAGLLKLFLRELPEPLITYELYE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057   632 PLINIIRyTTDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGPTLIRAPaDNLAAMVAD 711
Cdd:smart00324  82 EFIEAAK-LEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPP-DGEVASLKD 159
                          170
                   ....*....|....*
gi 754348057   712 TGSQCQIVSMIIQEH 726
Cdd:smart00324 160 IRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
552-702 2.05e-54

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 185.44  E-value: 2.05e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057  552 PLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDPLVNEEYcqQNIHAVAGVLKLYFRELPTPLFPFEFYE 631
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDLEE--EDVHVVASLLKLFLRELPEPLLTFELYE 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754348057  632 PLINIIRYTtDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGPTLIRAPA 702
Cdd:pfam00620  79 EFIEAAKLP-DEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
F-BAR_srGAP cd07656
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
35-308 1.34e-30

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs, all of which are expressed during embryonic and early development in the nervous system but with different localization and timing. srGAPs contain an N-terminal F-BAR domain, a Rho GAP 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.


Pssm-ID: 153340 [Multi-domain]  Cd Length: 241  Bit Score: 120.90  E-value: 1.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057  35 SQEVEQLKLFQHRTESKVAFMQDVQEFLKKRAEVEQEYAQKLDKVAEKFAHKLKHTSYGRYtllhnnslsspadgsaspl 114
Cdd:cd07656    1 QQLSEQLKCLDLRTEAQVQLLADLQDYFRRRAEIELEYSRSLEKLADRFSSKHKNEKSKRE------------------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 115 vigaagaslpsplvsptslenAVHPQTPVDVWTVLIENCRKTSRSRAALATRYGTELLDFTAEMERETVAGARQCHDYGL 194
Cdd:cd07656   62 ---------------------DWSLLSPVNCWNTLLVQTKQESRDHSTLSDIYSNNLVQRLGQMSEDLQRISKKCREIGS 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 195 KLHAELSESLAHLET---TAHSFHGLSAKAASAKAKVEDAKKKLESGSVNSKIISMLGKNVEKELHKREDTAAVQERRAS 271
Cdd:cd07656  121 QLHDELLRVLNELQTamkTYHTYHAESKSAERKLKEAEKQEEKQEQSPEKKLERSRSSKKIEKEVEKRQAKYSEAKLKCT 200
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 754348057 272 NAFNDYLFAIDVANAHKNQFFEHEIVELTALHDRFYH 308
Cdd:cd07656  201 KARNEYLLNLAAANATIHKYFVQDLSDLIDCMDLGFH 237
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
40-97 2.52e-10

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: 57.28  E-value: 2.52e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 754348057   40 QLKLFQHRTESKVAFMQDVQEFLKKRAEVEQEYAQKLDKVAEKFAHKLKHTSYGRYTL 97
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKKKKPEDDGGTL 58
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
34-93 5.03e-06

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: 45.41  E-value: 5.03e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754348057    34 RSQEVEQLKLFQHRTESKVAFMQDVQEFLKKRAEVEQEYAQKLDKVAEKF-AHKLKHTSYG 93
Cdd:smart00055   4 WSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKLrAVRDTEPEYG 64
 
Name Accession Description Interval E-value
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
552-725 3.15e-55

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: 188.66  E-value: 3.15e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 552 PLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDPLVNEEYcqqNIHAVAGVLKLYFRELPTPLFPFEFYE 631
Cdd:cd00159    1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDY---DVHDVASLLKLYLRELPEPLIPFELYD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 632 PLINIIRyTTDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGPTLIRAPADNLAAMVaD 711
Cdd:cd00159   78 EFIELAK-IEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDDELLE-D 155
                        170
                 ....*....|....
gi 754348057 712 TGSQCQIVSMIIQE 725
Cdd:cd00159  156 IKKLNEIVEFLIEN 169
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
552-726 1.98e-54

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


Pssm-ID: 214618  Cd Length: 174  Bit Score: 186.70  E-value: 1.98e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057   552 PLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDPLVNEEycQQNIHAVAGVLKLYFRELPTPLFPFEFYE 631
Cdd:smart00324   4 PIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDLS--EYDVHDVAGLLKLFLRELPEPLITYELYE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057   632 PLINIIRyTTDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGPTLIRAPaDNLAAMVAD 711
Cdd:smart00324  82 EFIEAAK-LEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPP-DGEVASLKD 159
                          170
                   ....*....|....*
gi 754348057   712 TGSQCQIVSMIIQEH 726
Cdd:smart00324 160 IRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
552-702 2.05e-54

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 185.44  E-value: 2.05e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057  552 PLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDPLVNEEYcqQNIHAVAGVLKLYFRELPTPLFPFEFYE 631
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDLEE--EDVHVVASLLKLFLRELPEPLLTFELYE 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754348057  632 PLINIIRYTtDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGPTLIRAPA 702
Cdd:pfam00620  79 EFIEAAKLP-DEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
534-701 2.29e-41

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: 149.88  E-value: 2.29e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 534 KVFGVELADHLRVVERSTPLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDPLVNEEYcQQNIHAVAGVL 613
Cdd:cd04383    1 KLFNGSLEEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPLADDQN-DHDINSVAGVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 614 KLYFRELPTPLFPFEFYEPLINIIRyTTDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVF 693
Cdd:cd04383   80 KLYFRGLENPLFPKERFEDLMSCVK-LENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICF 158

                 ....*...
gi 754348057 694 GPTLIRAP 701
Cdd:cd04383  159 GPTLMPVP 166
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
535-730 4.79e-41

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: 149.47  E-value: 4.79e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 535 VFGVELADHLRV-VERSTPLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLD--PLVNEEYcqQNIHAVAG 611
Cdd:cd04395    1 TFGVPLDDCPPSsENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGFdiDLQDPRW--RDVNVVSS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 612 VLKLYFRELPTPLFPFEFYEPLINIIRyTTDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAI 691
Cdd:cd04395   79 LLKSFFRKLPEPLFTNELYPDFIEANR-IEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAI 157
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 754348057 692 VFGPTLIRAPADNLAAMVADTGSQCQIVSMIIQEHAFLF 730
Cdd:cd04395  158 VFGPTLVRTSDDNMETMVTHMPDQCKIVETLIQHYDWFF 196
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
548-725 5.76e-39

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: 143.30  E-value: 5.76e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 548 ERST-PLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRglDPLVNEEYCQ-QNIHAVAGVLKLYFRELPTPLF 625
Cdd:cd04403   12 ENSTvPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDH--DEKLDLDDSKwEDIHVITGALKLFFRELPEPLF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 626 PFEFYEPLINIIRyTTDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGPTLIRaPADNL 705
Cdd:cd04403   90 PYSLFNDFVAAIK-LSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGPTLLR-PEQET 167
                        170       180
                 ....*....|....*....|
gi 754348057 706 AAMVADTGSQCQIVSMIIQE 725
Cdd:cd04403  168 GNIAVHMVYQNQIVELILLE 187
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
536-730 8.04e-39

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: 143.04  E-value: 8.04e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 536 FGVELADHLRVVERSTPLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDPLVNEEYCQQNIHAVAGVLKL 615
Cdd:cd04372    1 YGCDLTTLVKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKADISATVYPDINVITGALKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 616 YFRELPTPLFPFEFYEPLINIIRyTTDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGP 695
Cdd:cd04372   81 YFRDLPIPVITYDTYPKFIDAAK-ISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGP 159
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 754348057 696 TLIRAPADNLAAMVADTGSQCQIVSMIIQEHAFLF 730
Cdd:cd04372  160 TLMRPPEDSALTTLNDMRYQILIVQLLITNEDVLF 194
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
536-724 1.33e-38

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: 142.16  E-value: 1.33e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 536 FGVELADHLRVVERSTPLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRglDP----LVNEEYCQQNIHAVAG 611
Cdd:cd04398    1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDK--DPlnvlLISPEDYESDIHSVAS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 612 VLKLYFRELPTPLFPFEFYEPLINIIRYTTDHKsRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAI 691
Cdd:cd04398   79 LLKLFFRELPEPLLTKALSREFIEAAKIEDESR-RRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAI 157
                        170       180       190
                 ....*....|....*....|....*....|...
gi 754348057 692 VFGPTLIRAPADNlaamVADTGSQCQIVSMIIQ 724
Cdd:cd04398  158 IWGPTLMNAAPDN----AADMSFQSRVIETLLD 186
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
535-730 1.77e-38

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: 142.21  E-value: 1.77e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 535 VFGVELADHLRVVERSTPLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRG-LDPLVNEEYCqqNIHAVAGVL 613
Cdd:cd04386    4 VFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGtFSLPLDEFYS--DPHAVASAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 614 KLYFRELPTPLFPFEFYEPLINIIRYTTDHKsRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVF 693
Cdd:cd04386   82 KSYLRELPDPLLTYNLYEDWVQAANKPDEDE-RLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 754348057 694 GPTLIRAPADNLAAMVADTGSQ--CQIVSMIIQEHAFLF 730
Cdd:cd04386  161 APNLLWAKNEGSLAEMAAGTSVhvVAIVELIISHADWFF 199
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
536-725 8.53e-38

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: 139.88  E-value: 8.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 536 FGVELaDHLRVVERSTPLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDPLVNEEYcqqNIHAVAGVLKL 615
Cdd:cd04377    1 FGVSL-SSLTSEDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDY---PIHVITSVLKQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 616 YFRELPTPLFPFEFYEPLINIIRyTTDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGP 695
Cdd:cd04377   77 WLRELPEPLMTFELYENFLRAME-LEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAP 155
                        170       180       190
                 ....*....|....*....|....*....|..
gi 754348057 696 TLIRAP--ADNLAAMvADTGSQCQIVSMIIQE 725
Cdd:cd04377  156 CILRCPdtADPLQSL-QDVSKTTTCVETLIKE 186
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
534-702 2.63e-36

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: 135.71  E-value: 2.63e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 534 KVFGVELADHLRVVERSTPLLVDSCIATIEDFGILqEGIFRLSGSAVAIKEMRASFDRGLDPLVNEEYCQQNIHAVAGVL 613
Cdd:cd04384    1 RVFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGIV-DGIYRLSGIASNIQRLRHEFDSEQIPDLTKDVYIQDIHSVSSLC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 614 KLYFRELPTPLFPFEFYEPLINIIRYTTDhKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVF 693
Cdd:cd04384   80 KLYFRELPNPLLTYQLYEKFSEAVSAASD-EERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVW 158

                 ....*....
gi 754348057 694 GPTLIRAPA 702
Cdd:cd04384  159 APNLLRSKQ 167
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
535-697 2.86e-35

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: 132.48  E-value: 2.86e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 535 VFGVELADHLRV-----VERSTPLLVDSCIATIEDFG-ILQEGIFRLSGSAVAIKEMRASFDRGLDPLVNEEYCQQNIHA 608
Cdd:cd04400    1 IFGSPLEEAVELsshkyNGRDLPSVVYRCIEYLDKNRaIYEEGIFRLSGSASVIKQLKERFNTEYDVDLFSSSLYPDVHT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 609 VAGVLKLYFRELPTPLFPFEFYEPLINIIRYTTDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHN 688
Cdd:cd04400   81 VAGLLKLYLRELPTLILGGELHNDFKRLVEENHDRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLRN 160

                 ....*....
gi 754348057 689 LAIVFGPTL 697
Cdd:cd04400  161 VCIVFSPTL 169
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
536-724 4.61e-34

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: 129.46  E-value: 4.61e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 536 FGVELADHLRVVERSTPLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDpLVneEYCQQNIHAVAGVLKL 615
Cdd:cd04378    1 FGVDFSQVPRDFPDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKD-LV--ELSELSPHDISSVLKL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 616 YFRELPTPLFPFEFYEPLINIIR-------------YTTDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELN 682
Cdd:cd04378   78 FLRQLPEPLILFRLYNDFIALAKeiqrdteedkapnTPIEVNRIIRKLKDLLRQLPASNYNTLQHLIAHLYRVAEQFEEN 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 754348057 683 KMKAHNLAIVFGPTLIR---APADNLAAMVADTGSQCQIVSMIIQ 724
Cdd:cd04378  158 KMSPNNLGIVFGPTLIRprpGDADVSLSSLVDYGYQARLVEFLIT 202
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
548-730 6.32e-33

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: 126.20  E-value: 6.32e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 548 ERS-TPLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDPLVNEeYCQQNIHAVAGVLKLYFRELPTPLFP 626
Cdd:cd04387   12 ERSkVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVM-LSEMDVNAIAGTLKLYFRELPEPLFT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 627 FEFYEPLINIIRyTTDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGPTLIRaPADNLA 706
Cdd:cd04387   91 DELYPNFAEGIA-LSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTLLR-PSEKES 168
                        170       180
                 ....*....|....*....|....
gi 754348057 707 AMVADTGSQCQIVSMIIQEHAFLF 730
Cdd:cd04387  169 KIPTNTMTDSWSLEVMSQVQVLLY 192
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
536-701 6.47e-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: 125.91  E-value: 6.47e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 536 FGVELaDHLRvvERS-----TPLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDplvneEYCQQ--NIHA 608
Cdd:cd04404    6 FGVSL-QFLK--EKNpeqepIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGEP-----VDFDQyeDVHL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 609 VAGVLKLYFRELPTPLFPFEFYEPLINIIRYTTDHKSRAVslRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHN 688
Cdd:cd04404   78 PAVILKTFLRELPEPLLTFDLYDDIVGFLNVDKEERVERV--KQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSN 155
                        170
                 ....*....|...
gi 754348057 689 LAIVFGPTLIRAP 701
Cdd:cd04404  156 LAVVFGPNLLWAK 168
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
535-730 8.08e-33

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: 126.02  E-value: 8.08e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 535 VFGVELADHL----RVVERSTPLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDPLVNEEycqQNIHAVA 610
Cdd:cd04390    2 VFGQRLEDTVayerKFGPRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSD---TDVHTVA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 611 GVLKLYFRELPTPLFPFEFYEP-LINIIRYTTDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNL 689
Cdd:cd04390   79 SLLKLYLRELPEPVIPWAQYEDfLSCAQLLSKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNL 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 754348057 690 AIVFGPTLIRAPADNLAAMVADTGSQCQIVSMIIQEHAFLF 730
Cdd:cd04390  159 ATVFGPNILRPKVEDPATIMEGTPQIQQLMTVMISKHEPLF 199
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
552-697 2.70e-31

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: 120.88  E-value: 2.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 552 PLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFD---RGLDPLVNEEycqqNIHAVAGVLKLYFRELPTPLFPFE 628
Cdd:cd04385   16 PVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRkdaRSVQLREGEY----TVHDVADVLKRFLRDLPDPLLTSE 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 629 FYEPLINIIryTTDHKSRAVS-LRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGPTL 697
Cdd:cd04385   92 LHAEWIEAA--ELENKDERIArYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTL 159
F-BAR_srGAP cd07656
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
35-308 1.34e-30

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs, all of which are expressed during embryonic and early development in the nervous system but with different localization and timing. srGAPs contain an N-terminal F-BAR domain, a Rho GAP 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.


Pssm-ID: 153340 [Multi-domain]  Cd Length: 241  Bit Score: 120.90  E-value: 1.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057  35 SQEVEQLKLFQHRTESKVAFMQDVQEFLKKRAEVEQEYAQKLDKVAEKFAHKLKHTSYGRYtllhnnslsspadgsaspl 114
Cdd:cd07656    1 QQLSEQLKCLDLRTEAQVQLLADLQDYFRRRAEIELEYSRSLEKLADRFSSKHKNEKSKRE------------------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 115 vigaagaslpsplvsptslenAVHPQTPVDVWTVLIENCRKTSRSRAALATRYGTELLDFTAEMERETVAGARQCHDYGL 194
Cdd:cd07656   62 ---------------------DWSLLSPVNCWNTLLVQTKQESRDHSTLSDIYSNNLVQRLGQMSEDLQRISKKCREIGS 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 195 KLHAELSESLAHLET---TAHSFHGLSAKAASAKAKVEDAKKKLESGSVNSKIISMLGKNVEKELHKREDTAAVQERRAS 271
Cdd:cd07656  121 QLHDELLRVLNELQTamkTYHTYHAESKSAERKLKEAEKQEEKQEQSPEKKLERSRSSKKIEKEVEKRQAKYSEAKLKCT 200
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 754348057 272 NAFNDYLFAIDVANAHKNQFFEHEIVELTALHDRFYH 308
Cdd:cd07656  201 KARNEYLLNLAAANATIHKYFVQDLSDLIDCMDLGFH 237
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
536-725 4.46e-30

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: 117.56  E-value: 4.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 536 FGVELADhLRVVERSTPLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRglDPLVNEEYCQQNIHAVAGVLKL 615
Cdd:cd04373    1 FGVPLAN-VVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQ--DHNLDLVSKDFTVNAVAGALKS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 616 YFRELPTPLFPFEFYEPLINIIRyTTDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGP 695
Cdd:cd04373   78 FFSELPDPLIPYSMHLELVEAAK-INDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWP 156
                        170       180       190
                 ....*....|....*....|....*....|
gi 754348057 696 TLIRAPADNLAAMVADTGSQcQIVSMIIQE 725
Cdd:cd04373  157 TLMRPDFTSMEALSATRIYQ-TIIETFIQQ 185
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
536-724 9.30e-30

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: 117.22  E-value: 9.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 536 FGVELADHLRVVERSTPLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDpLVneEYCQQNIHAVAGVLKL 615
Cdd:cd04408    1 FGVDFSQLPRDFPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRD-LV--DLSGHSPHDITSVLKH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 616 YFRELPTPLFPFEFYEPLINIIRYTTDHKSRAV-----------SLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKM 684
Cdd:cd04408   78 FLKELPEPVLPFQLYDDFIALAKELQRDSEKAAespsiveniirSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKM 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 754348057 685 KAHNLAIVFGPTLIRAPADNLAAMVA--DTGSQCQIVSMIIQ 724
Cdd:cd04408  158 SPNNLGIVFGPTLLRPLVGGDVSMICllDTGYQAQLVEFLIS 199
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
547-730 1.70e-29

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: 116.77  E-value: 1.70e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 547 VERSTPLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDPLVNEEycqQNIHAVAGVLKLYFRELPTPLFP 626
Cdd:cd04376    5 IARQVPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDEN---HSVHDVAALLKEFFRDMPDPLLP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 627 FEFYEPLINIIRYTTDHKSRAvsLRELLKSLPKSNLLVLERLFDLLVQIAQQ--------GEL---NKMKAHNLAIVFGP 695
Cdd:cd04376   82 RELYTAFIGTALLEPDEQLEA--LQLLIYLLPPCNCDTLHRLLKFLHTVAEHaadsidedGQEvsgNKMTSLNLATIFGP 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 754348057 696 TLIRAPADNL------AAMVADTGSQCQIVSMIIQEHAFLF 730
Cdd:cd04376  160 NLLHKQKSGErefvqaSLRIEESTAIINVVQTMIDNYEELF 200
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
536-725 1.96e-28

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: 112.79  E-value: 1.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 536 FGVELAdHLRVVERSTPLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDPLVNEEYcqqNIHAVAGVLKL 615
Cdd:cd04406    1 FGVELS-RLTSEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDY---NIHVIASVFKQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 616 YFRELPTPLFPFEFYEPLINIIRYTtDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGP 695
Cdd:cd04406   77 WLRDLPNPLMTFELYEEFLRAMGLQ-ERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAP 155
                        170       180       190
                 ....*....|....*....|....*....|..
gi 754348057 696 TLIRAP--ADNLAAmVADTGSQCQIVSMIIQE 725
Cdd:cd04406  156 CILRCPdtTDPLQS-VQDISKTTTCVELIVCE 186
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
536-725 1.42e-26

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: 107.38  E-value: 1.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 536 FGVELaDHLRVVERSTPLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDPLVNEEYcqqNIHAVAGVLKL 615
Cdd:cd04407    1 FGVRV-GSLTSNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENY---PIHAITGLLKQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 616 YFRELPTPLFPFEFYEPLINIIRYTtDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGP 695
Cdd:cd04407   77 WLRELPEPLMTFAQYNDFLRAVELP-EKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAP 155
                        170       180       190
                 ....*....|....*....|....*....|..
gi 754348057 696 TLIRAP--ADNLAAMvADTGSQCQIVSMIIQE 725
Cdd:cd04407  156 CLLRCPdsSDPLTSM-KDVAKTTTCVEMLIKE 186
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
536-723 1.31e-25

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: 105.66  E-value: 1.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 536 FGVELADHLRVVERSTPLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDpLVneEYCQQNIHAVAGVLKL 615
Cdd:cd04409    1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKD-LV--ELSELSPHDISNVLKL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 616 YFRELPTPLFPFEFYEPLINIIRYT---------------------TDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQ 674
Cdd:cd04409   78 YLRQLPEPLILFRLYNEFIGLAKESqhvnetqeakknsdkkwpnmcTELNRILLKSKDLLRQLPAPNYNTLQFLIVHLHR 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 754348057 675 IAQQGELNKMKAHNLAIVFGPTLIRA-PADNLAAM--VADTGSQCQIVSMII 723
Cdd:cd04409  158 VSEQAEENKMSASNLGIIFGPTLIRPrPTDATVSLssLVDYPHQARLVELLI 209
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
534-703 3.97e-25

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: 103.31  E-value: 3.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 534 KVFGVELAD--HLRVVERSTPLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDPLVNEEycqQNIHAVAG 611
Cdd:cd04393    1 KVFGVPLQElqQAGQPENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSKE---ADVCSAAS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 612 VLKLYFRELPTPLFPFEFYEPLINIIRYTTDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAI 691
Cdd:cd04393   78 LLRLFLQELPEGLIPASLQIRLMQLYQDYNGEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAA 157
                        170
                 ....*....|..
gi 754348057 692 VFGPTLIRAPAD 703
Cdd:cd04393  158 VFGPDVFHVYTD 169
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
566-732 4.08e-24

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: 100.84  E-value: 4.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 566 GILQEGIFRLSGSAVAIKEMRASFDRGLDplVNEEycQQNIHAVAGVLKLYFRELPTPLFPFEFYEPLINIIRyTTDHKS 645
Cdd:cd04402   30 GPSTEGIFRRSANAKACKELKEKLNSGVE--VDLK--AEPVLLLASVLKDFLRNIPGSLLSSDLYEEWMSALD-QENEEE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 646 RAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGPTLIRAPADNLAAMvADTGSQCQIVSMIIQE 725
Cdd:cd04402  105 KIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLWPPASSELQN-EDLKKVTSLVQFLIEN 183

                 ....*..
gi 754348057 726 HAFLFGE 732
Cdd:cd04402  184 CQEIFGE 190
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
570-724 8.15e-24

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: 99.77  E-value: 8.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 570 EGIFRLSGSAVAIKEMRASFDRGLDPLVNEEycqqNIHAVAGVLKLYFRELPTPLFPFEFYEPLINiiryTTDHKSRAVs 649
Cdd:cd04389   41 EGIFRVPGDIDEVNELKLRVDQWDYPLSGLE----DPHVPASLLKLWLRELEEPLIPDALYQQCIS----ASEDPDKAV- 111
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754348057 650 lrELLKSLPKSNLLVLERLFDLLVQIAQQG--ELNKMKAHNLAIVFGPTLIRAPADNLAAMVADTGSQCQIVSMIIQ 724
Cdd:cd04389  112 --EIVQKLPIINRLVLCYLINFLQVFAQPEnvAHTKMDVSNLAMVFAPNILRCTSDDPRVIFENTRKEMSFLRTLIE 186
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
535-737 2.61e-23

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: 98.70  E-value: 2.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 535 VFGVEL----ADHLRVVERSTPLLVDSCiATIEDFgILQEGIFRLSGSAVAIKEMRASFDRGLDPLVNEEYCQqnihaVA 610
Cdd:cd04394    1 VFGVPLhslpHSTVPEYGNVPKFLVDAC-TFLLDH-LSTEGLFRKSGSVVRQKELKAKLEGGEACLSSALPCD-----VA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 611 GVLKLYFRELPTPLFPFEFYEPLINIIRYTTDH-KSRAVSLRELLksLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNL 689
Cdd:cd04394   74 GLLKQFFRELPEPLLPYDLHEALLKAQELPTDEeRKSATLLLTCL--LPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNL 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 754348057 690 AIVFGPTLIrAPADNLAAMVADT----GSQCQIVSMIIqEHAFLFGETNEFV 737
Cdd:cd04394  152 AVIFAPNLF-QSEEGGEKMSSSTekrlRLQAAVVQTLI-DNASNIGIVPDFI 201
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
536-698 3.77e-21

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: 92.53  E-value: 3.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 536 FGVELAdhlRVVERS-----TPLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRG--LDPLVNEEYCQQNIha 608
Cdd:cd04379    1 FGVPLS---RLVEREgesrdVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNsaAVELSEELYPDINV-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 609 VAGVLKLYFRELPTPLFPFEFYEPLINI--IRYTTDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKA 686
Cdd:cd04379   76 ITGVLKDYLRELPEPLITPQLYEMVLEAlaVALPNDVQTNTHLTLSIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTP 155
                        170
                 ....*....|..
gi 754348057 687 HNLAIVFGPTLI 698
Cdd:cd04379  156 QNLAVCFGPVLM 167
F-BAR_srGAP3 cd07684
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
35-311 4.96e-21

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating Protein 3; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs. srGAP3, also called MEGAP (MEntal disorder associated GTPase-Activating Protein), is a Rho GAP with activity towards Rac1 and Cdc42. It impacts cell migration by regulating actin and microtubule cytoskeletal dynamics. The association between srGAP3 haploinsufficiency and mental retardation is under debate. srGAP3 contains an N-terminal F-BAR domain, a Rho GAP 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.


Pssm-ID: 153368 [Multi-domain]  Cd Length: 253  Bit Score: 93.62  E-value: 4.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057  35 SQEVEQLKLFQHRTESKVAFMQDVQEFLKKRAEVEQEYAQKLDKVAEKFAHKLKhTSYGRYTLLHNNSLSspadgsaspl 114
Cdd:cd07684    1 TQLVEQFKCLEQQSESRLQLLQDLQEFFRRKAEIELEYSRSLEKLAERFSSKIR-TSREHQFKKDQQLLS---------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 115 vigaagaslpsplvsptslenavhpqtPVDVWTVLIENCRKTSRSRAALATRYGTELLDFTAEMERETVAGARQCHDYGL 194
Cdd:cd07684   70 ---------------------------PVNCWYLVLEQTRRESRDHATLNDIFNNNVIVRLSQISEDVIRLFKKSKEIGL 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 195 KLHAELSESLAHLETTAHSFHGLSAKAASAKAKVEDAKKKLESGSVNSKIISML-------------GKNVEKELHKRED 261
Cdd:cd07684  123 QMHEELLKVTNELYTVMKTYHMYHAESISAESKLKEAEKQEEKQFNKSGDISSNllrheerpqrrssVKKIEKMKEKRQA 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 754348057 262 TAAVQERRASNAFNDYLFAIDVANAHKNQFFEHEIVELTALHDRFYHENM 311
Cdd:cd07684  203 KYSENKLKCTKARNDYLLNLAATNAAVSKYYIHDVSDLIDCCDLGFHASL 252
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
555-708 6.00e-21

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: 91.69  E-value: 6.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 555 VDSCIATIEDFGILQEGIFRLSGSAVAI-KEMRASFD-RGLDPL-VNEEYCQQNIHAVAGVLKLYFRELPTPLFPFEFYE 631
Cdd:cd04374   32 VRKCIEAVETRGINEQGLYRVVGVNSKVqKLLSLGLDpKTSTPGdVDLDNSEWEIKTITSALKTYLRNLPEPLMTYELHN 111
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754348057 632 PLINIIRyTTDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGPTLIRAPADNLAAM 708
Cdd:cd04374  112 DFINAAK-SENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQEETVAAI 187
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
552-720 1.46e-20

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: 90.43  E-value: 1.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 552 PLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRG-LDPLVNeeycQQNIHAVAGVLKLYFRELPTPLFPFEFY 630
Cdd:cd04382   18 PALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGkTVPNLS----KVDIHVICGCLKDFLRSLKEPLITFALW 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 631 EPLINIIRYTTDHKSRAvSLRELLKSLPKSNLLVLERLFDLLVQIAQQGElNKMKAHNLAIVFGPTLIRAPADNL--AAM 708
Cdd:cd04382   94 KEFMEAAEILDEDNSRA-ALYQAISELPQPNRDTLAFLILHLQRVAQSPE-CKMDINNLARVFGPTIVGYSVPNPdpMTI 171
                        170
                 ....*....|..
gi 754348057 709 VADTGSQCQIVS 720
Cdd:cd04382  172 LQDTVRQPRVVE 183
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
535-730 1.52e-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: 91.32  E-value: 1.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 535 VFGVELADHLRV--VERST-------------PLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDPLVNE 599
Cdd:cd04396    1 VFGVSLEESLKYasVAISIvdedgeqyvygyiPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPDYGKSF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 600 EYCQQNIHAVAGVLKLYFRELPTPLFPFEFYE----PLIN---IIRYTTD--------HKSRAVSL-RELLKSLPKSNLL 663
Cdd:cd04396   81 DWDGYTVHDAASVLRRYLNNLPEPLVPLDLYEefrnPLRKrprILQYMKGrineplntDIDQAIKEyRDLITRLPNLNRQ 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754348057 664 VLERLFDLLVQIAQQGELNKMKAHNLAIVFGPTLIRAPADNLaaMVADTG-SQCQIVSMIiqEHAFLF 730
Cdd:cd04396  161 LLLYLLDLLAVFARNSDKNLMTASNLAAIFQPGILSHPDHEM--DPKEYKlSRLVVEFLI--EHQDKF 224
F-BAR_srGAP1 cd07683
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
35-312 6.46e-20

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating 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. Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs. srGAP1, also called Rho GTPase-Activating Protein 13 (ARHGAP13), is a Cdc42- and RhoA-specific GAP and is expressed later in the development of CNS (central nervous system) tissues. It is an important downstream signaling molecule of Robo1. srGAP1 contains an N-terminal F-BAR domain, a Rho GAP 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.


Pssm-ID: 153367 [Multi-domain]  Cd Length: 253  Bit Score: 90.13  E-value: 6.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057  35 SQEVEQLKLFQHRTESKVAFMQDVQEFLKKRAEVEQEYAQKLDKVAEKFAHKLKHTSYGRYTLLHNNSLSspadgsaspl 114
Cdd:cd07683    1 AQLVEQQKCLEQQTEMRVQLLQDLQDFFRKKAEIESEYSRNLEKLAERFMAKTRSTKDHQQYKKDQNLLS---------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 115 vigaagaslpsplvsptslenavhpqtPVDVWTVLIENCRKTSRSRAALATRYGTELLDFTAEMERETVAGARQCHDYGL 194
Cdd:cd07683   71 ---------------------------PVNCWYLLLNQVRRESKDHATLSDIYLNNVIMRFMQISEDSTRMFKKSKEIAF 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 195 KLHAELSESLAHLETTAHSFHGLSAKAASAKAKVEDAKKKLES--GSVNSKIISM----------LGKNVEKELHKREDT 262
Cdd:cd07683  124 QLHEDLMKVLNELYTVMKTYHMYHTESISAESKLKEAEKQEEKqiGRSGDPVFHIrledrhqrrsSVKKIEKMKEKRQAK 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 754348057 263 AAVQERRASNAFNDYLFAIDVANAHKNQFFEHEIVELTALHDRFYHENMN 312
Cdd:cd07683  204 YSENKLKSIKARNEYLLTLEATNASVFKYYIHDLSDLIDCCDLGYHASLN 253
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
536-697 2.87e-19

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: 86.34  E-value: 2.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 536 FGVELADhlrVVERST-------PLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRGLDPLVnEEYcqqNIHA 608
Cdd:cd04381    1 FGASLSL---AVERSRchdgidlPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRESPNL-EEY---EPPT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 609 VAGVLKLYFRELPTPLFPFEFyeplinIIRY-----TTDHKSRAVSLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNK 683
Cdd:cd04381   74 VASLLKQYLRELPEPLLTKEL------MPRFeeacgRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETK 147
                        170
                 ....*....|....
gi 754348057 684 MKAHNLAIVFGPTL 697
Cdd:cd04381  148 MNIQNISIVLSPTV 161
F-BAR_srGAP2 cd07682
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
35-312 8.21e-19

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating 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. Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs. srGAP2 is expressed in zones of neuronal differentiation. It plays a role in the regeneration of neurons and axons. srGAP2 contains an N-terminal F-BAR domain, a Rho GAP 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.


Pssm-ID: 153366 [Multi-domain]  Cd Length: 263  Bit Score: 87.44  E-value: 8.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057  35 SQEVEQLKLFQHRTESKVAFMQDVQEFLKKRAEVEQEYAQKLDKVAEKFAHKLKHTSYGRYTLlHNNSLSspadgsaspl 114
Cdd:cd07682    1 AQLVEQLKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRSTKDQQFKK-DQNVLS---------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 115 vigaagaslpsplvsptslenavhpqtPVDVWTVLIENCRKTSRSRAALATRYGTELLDFTAEMERETVAGARQCHDYGL 194
Cdd:cd07682   70 ---------------------------PVNCWNLLLNQVKRESRDHATLSDIYLNNIIPRFVQISEDSGRLFKKSKEVGL 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 195 KLHAELSESLAHLETTAHSFHGLSAKAASAKAKVEDAKKKLE---SGSVNSK--------------------IISMLGKN 251
Cdd:cd07682  123 QLQEDLMKVLNELYTVMKTYHMYNADSISAQSKLKEAEKQEEkqmSRSVRQEdrqtprspdsttnirieekhVRRSSVKK 202
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754348057 252 VEKELHKREDTAAVQERRASNAFNDYLFAIDVANAHKNQFFEHEIVELTALHDRFYHENMN 312
Cdd:cd07682  203 IEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDLIDCCDLGYHASLN 263
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
534-697 5.48e-17

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: 80.92  E-value: 5.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 534 KVFGVELADHLRVVERSTPLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRaSFDRGLDPLVNeeYCQQNIHAVAGVL 613
Cdd:cd04375    3 NVFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLR-SMIESSTDNVN--YDGQQAYDVADML 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 614 KLYFRELPTPLFPFEFYEPLINIIRYT-TDHKSRAVSLRELLksLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIV 692
Cdd:cd04375   80 KQYFRDLPEPLLTNKLSETFIAIFQYVpKEQRLEAVQCAILL--LPDENREVLQTLLYFLSDVAANSQENQMTATNLAVC 157

                 ....*
gi 754348057 693 FGPTL 697
Cdd:cd04375  158 LAPSL 162
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
535-697 2.25e-16

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: 78.93  E-value: 2.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 535 VFGVELA-----DHLRVVERSTPLLVDSCIATIEDFGILQEGIFRLSGSAVAIK----EMRASFDRGLDPLvnEEYCQqn 605
Cdd:cd04391    1 LFGVPLStllerDQKKVPGSKVPLIFQKLINKLEERGLETEGILRIPGSAQRVKflcqELEAKFYEGTFLW--DQVKQ-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 606 iHAVAGVLKLYFRELPTPLFPFEFYEPLINIIRY-TTDHKSRAVSLRELLksLPKSNLLVLERLFDLLVQIAQQGELNKM 684
Cdd:cd04391   77 -HDAASLLKLFIRELPQPLLTVEYLPAFYSVQGLpSKKDQLQALNLLVLL--LPEANRDTLKALLEFLQKVVDHEEKNKM 153
                        170
                 ....*....|...
gi 754348057 685 KAHNLAIVFGPTL 697
Cdd:cd04391  154 NLWNVAMIMAPNL 166
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
567-698 1.75e-15

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: 76.35  E-value: 1.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 567 ILQEGIFRLSGSAVAIKEMRASFDRGLD-PLVNEEYcqqNIHAVAGVLKLYFRELPTPLFPFEFYEPLINII-------- 637
Cdd:cd04392   24 LRVEGLFRKPGNSARQQELRDLLNSGTDlDLESGGF---HAHDCATVLKGFLGELPEPLLTHAHYPAHLQIAdlcqfdek 100
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754348057 638 --RYTTDHKSRAV-SLRELLKSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGPTLI 698
Cdd:cd04392  101 gnKTSAPDKERLLeALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLI 164
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
543-704 2.05e-14

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: 73.17  E-value: 2.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 543 HLRVverstPLLVDSCIATIEDFGILQEGIFRLSGSAVAIKEMRASFDRglDPLVNEEYCQQNIHAVAGVLKLYFRELPT 622
Cdd:cd04397   24 KLRI-----PALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDK--NPTEVPDLSKENPVQLAALLKKFLRELPD 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 623 PLFPFEFYEPLINIIRYTTDHKSRAVsLRELLKSLPKSNLLVLERLFDLLVQIAQQGEL-----NKMKAHNLAIVFGPTL 697
Cdd:cd04397   97 PLLTFKLYRLWISSQKIEDEEERKRV-LHLVYCLLPKYHRDTMEVLFSFLKWVSSFSHIdeetgSKMDIHNLATVITPNI 175

                 ....*..
gi 754348057 698 IRAPADN 704
Cdd:cd04397  176 LYSKTDN 182
F-BAR_FCHSD cd07654
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains ...
38-327 1.30e-10

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains proteins (FCHSD); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of FCH and double SH3 domain (FCHSD) proteins, so named as they contain an N-terminal F-BAR domain and two SH3 domains at the C-terminus. Vertebrates harbor two subfamily members, FCHSD1 and FCHSD2, which have been characterized only in silico. Their biological function is still unknown. 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: 153338 [Multi-domain]  Cd Length: 264  Bit Score: 62.99  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057  38 VEQLKLFQHRTESKVAFMQDVQEFLKKRAEVEQEYAQKLDKVAEKFahkLKHtsygrytllhnnslSSPADGSASPlvig 117
Cdd:cd07654    4 LEQLSKLQAKHQTECDLLEDIRTYSQKKAAIEREYGQALQKLASQF---LKR--------------EWPGSGELKP---- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 118 aagaslpsplvsptSLENAVHPqtpvdVWTVLIENCRKTSRSRAALATRYGTELLDFTAEMERETVAGARQCHDYGLKLH 197
Cdd:cd07654   63 --------------EDDRSGYT-----VWGAWLEGLDAVAQSRQNRCEAYRRYISEPAKTGRSAKEQQLKKCTEQLQRAQ 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 198 AELSESLAHLETTAHSFHGLSAKAASAKAKVEDAKKKL---ESGSVNSKiiSMLGKNVEKeLHKREDTAavqERRASNAF 274
Cdd:cd07654  124 AEVQQTVRELSKSRKTYFEREQVAHLAREKAADVQAREarsDLSIFQSR--TSLQKASVK-LSARKAEC---SSKATAAR 197
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 754348057 275 NDYLFAIDVANAHKNQFFEHEIVELTALHDRFYHENMNHFFNEYAHIEGECAT 327
Cdd:cd07654  198 NDYLLNLAATNAHQDRYYQTDLPAIIKALDGELYDHLKDFLISLSHTELETAQ 250
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
40-97 2.52e-10

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: 57.28  E-value: 2.52e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 754348057   40 QLKLFQHRTESKVAFMQDVQEFLKKRAEVEQEYAQKLDKVAEKFAHKLKHTSYGRYTL 97
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKKKKPEDDGGTL 58
F-BAR_FCHSD2 cd07677
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 2 ...
37-337 1.47e-09

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 2 (FCHSD2); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH and double SH3 domains 2 (FCHSD2) contains an N-terminal F-BAR domain and two SH3 domains at the C-terminus. It has been characterized only in silico, and its biological function is still unknown. 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: 153361 [Multi-domain]  Cd Length: 260  Bit Score: 59.76  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057  37 EVEQLKLFQHRTESKVAFMQDVQEFLKKRAEVEQEYAQKLDKVAEKFahklkhtsygrytlLHNNSLSSPADGSASplvi 116
Cdd:cd07677    3 QVEQMTKLQAKHQAECKLLEDEREFSQKIAAIESEYAQKEQKLASQY--------------LKSDWRGMKADERAD---- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 117 gaagaslpsplvsptslENAVHPqtpvdVWTVLIENCRKTSRSRAALATRYGtellDFTAEMERETVAGARQ----CHDY 192
Cdd:cd07677   65 -----------------YRSMYT-----VWKSFLEGTMQVAQSRINICENYK----NLISEPARTVRLYKEQqlkrCVDQ 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 193 GLKLHAELSESLAHLETTAHSFHGLSAKAASAKAKVE-DAKKKLesgSVNSKIISMLGKNVEKELHKREDTAavqerRAS 271
Cdd:cd07677  119 LTKIQAELQETVKDLAKGKKKYFETEQMAHAVREKADiEAKSKL---SLFQSRISLQKASVKLKARRSECNS-----KAT 190
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754348057 272 NAFNDYLFAIDVANAHKNQFFEHEIVELTALHDRFYHENMNHFFNEYAHIEGE-CATDSSSMVHLLK 337
Cdd:cd07677  191 HARNDYLLTLAAANAHQDRYYQTDLVNIMKALDGNVYDHLKDYLMAFSRTELEtCQAVQNTFQFLLE 257
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
552-726 5.41e-09

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: 57.19  E-value: 5.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 552 PLLVdSCIATIEDFGILQEGIFRlSGSAVAIKEMRASFDrglDPLVNEEYCQQNIHAVAGVLKLYFRELPTPLFPFEFYE 631
Cdd:cd04388   17 PLLI-KLVEAIEKKGLESSTLYR-TQSSSSLTELRQILD---CDAASVDLEQFDVAALADALKRYLLDLPNPVIPAPVYS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 632 PLINIIRYTTDHKSRAVSLRELLKS--LPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGPTLIRAPadnlAAMV 709
Cdd:cd04388   92 EMISRAQEVQSSDEYAQLLRKLIRSpnLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLFRFQ----PASS 167
                        170
                 ....*....|....*..
gi 754348057 710 ADTGSQCQIVSMIIQEH 726
Cdd:cd04388  168 DSPEFHIRIIEVLITSE 184
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
553-718 9.97e-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: 53.50  E-value: 9.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 553 LLVDSciatIEDFGILQEGIFRLSG----SAVAIKEMRASFDRGLDPLVNEeycqqNIHAVAGVLKLYFRELPTPLFPFE 628
Cdd:cd04380   56 RLVDY----LYTRGLAQEGLFEEPGlpsePGELLAEIRDALDTGSPFNSPG-----SAESVAEALLLFLESLPDPIIPYS 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 629 FYEPLINIIRYTTDHKSRAVSLrellkSLPKSNLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGPTLIRAPaDNLAAM 708
Cdd:cd04380  127 LYERLLEAVANNEEDKRQVIRI-----SLPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDP-PRAGGK 200
                        170
                 ....*....|
gi 754348057 709 VADTGSQCQI 718
Cdd:cd04380  201 ERRAERDRKR 210
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
40-90 9.13e-07

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: 50.42  E-value: 9.13e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 754348057  40 QLKLFQHRTESKVAFMQDVQEFLKKRAEVEQEYAQKLDKVAEKFAHKLKHT 90
Cdd:cd07610    1 GFELLEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQKLAKKFSKKPESG 51
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
609-715 1.28e-06

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: 50.02  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 609 VAGVLKLYFRELPTPLFPFEFYEplinIIR--YT-------TDHKSRAVSLRELLKSLPKSNLLVLERL---FDLLVQIA 676
Cdd:cd04399   81 VASVLKLYLLELPDSLIPHDIYD----LIRslYSayppsqeDSDTARIQGLQSTLSQLPKSHIATLDAIithFYRLIEIT 156
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 754348057 677 QQGELNKMKAHNLAIVFGPTLIRAPADNLAAMVADTGSQ 715
Cdd:cd04399  157 KMGESEEEYADKLATSLSREILRPIIESLLTIGDKHGYK 195
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
34-93 5.03e-06

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: 45.41  E-value: 5.03e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754348057    34 RSQEVEQLKLFQHRTESKVAFMQDVQEFLKKRAEVEQEYAQKLDKVAEKF-AHKLKHTSYG 93
Cdd:smart00055   4 WSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKLrAVRDTEPEYG 64
F-BAR_FCHSD1 cd07678
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 1 ...
39-326 6.32e-06

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 1 (FCHSD1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH and double SH3 domains 1 (FCHSD1) contains an N-terminal F-BAR domain and two SH3 domains at the C-terminus. It has been characterized only in silico, and its biological function is still unknown. 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: 153362 [Multi-domain]  Cd Length: 263  Bit Score: 48.85  E-value: 6.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057  39 EQLKLFQHRTESKVAFMQDVQEFLKKRAEVEQEYAQKLDKVAEKFAHKLKHTsyGRYTLLHNNSL----SSPADGSASpl 114
Cdd:cd07678    5 EQLSILQTKQQRDAELLEDIRSYSKQRAAIEREYGQALQRLASQFLKRDWHR--GGNETEMDRSVrtvwGAWREGTAA-- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 115 vIGAAGAslpsplvspTSLENavhpqtpvdvWTVLIENCRKTSRSRAALATRYGTELLdftaemeretvagarqchdygL 194
Cdd:cd07678   81 -TGQGRV---------TRLEA----------YRRLRDEAGKTGRSAKEQVLKKSTEQL---------------------Q 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 195 KLHAELSESLAHLETTAHSFHGLSAKAASAKAKVEDAKKKL---ESGSVNSKiismlgKNVEKELHKREDTAAVQERRAS 271
Cdd:cd07678  120 KAQAELLETVKELSKSKKLYGQLERVSEVAKEKAADVEARLnksDHGIFHSK------ASLQKLSAKFSAQSAEYSQQLQ 193
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 754348057 272 NAFNDYLFAIDVANAHKNQFFEHEIVELTALHDRFYHENMNHFFNEYAHIEGECA 326
Cdd:cd07678  194 AARNEYLLNLVAANAHLDHYYQEELPAIMKALDGDLYERLRDPLTSLSHTELEAC 248
RhoGAP_fMSB1 cd04401
RhoGAP_fMSB1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
572-695 3.97e-04

RhoGAP_fMSB1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal MSB1-like proteins. Msb1 was originally identified as a multicopy suppressor of temperature sensitive cdc42 mutation. Msb1 is a positive regulator of the Pkc1p-MAPK pathway and 1,3-beta-glucan synthesis, both pathways involve Rho1 regulation. 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: 239866  Cd Length: 198  Bit Score: 42.72  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348057 572 IFRLSGSAVAIKE-MRASFDRGLDPLVNEEYCQQ-----NIHAVAGVLKLYFRELPTPLFP-FEFYEpliNIIRYTTDHK 644
Cdd:cd04401   30 PFRPELSPDKVRSlINSFFPSQNGQLQGTAELLDelryaDPHTLILVLKWIWSRLPGSKVIwWEVYE---EFKARERRSN 106
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 754348057 645 SRAVSLRELLKSLPKS--NLLVLERLFDLLVQIAQQGELNKMKAHNLAIVFGP 695
Cdd:cd04401  107 YPADAFLDLLPQCLSSpaHASILYDFFDLLSSIAAHSSVNGMSGRKLSKMAGP 159
F-BAR_CIP4-like cd07653
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ...
40-89 1.69e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 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. This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4), Formin Binding Protein 17 (FBP17), FormiN Binding Protein 1-Like (FNBP1L), and similar proteins. CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. Members of this subfamily typically contain an N-terminal F-BAR domain and a C-terminal SH3 domain. In addition, some members such as FNBP1L contain a central Cdc42-binding HR1 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: 153337 [Multi-domain]  Cd Length: 251  Bit Score: 41.08  E-value: 1.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 754348057  40 QLKLFQHRTESKVAFMQDVQEFLKKRAEVEQEYAQKLDKVAEKFAHKLKH 89
Cdd:cd07653    6 QFDNLEKHTQKGIDFLERYGKFVKERAAIEQEYAKKLRKLVKKYLPKKKE 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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