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Conserved domains on  [gi|568967400|ref|XP_006513634|]
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rho GTPase-activating protein 9 isoform X2 [Mus musculus]

Protein Classification

Rho GTPase-activating protein( domain architecture ID 10192492)

Rho GTPase-activating protein for Rho/Rac/Cdc42-like small GTPases that act as molecular switches, active in their GTP-bound form but inactive when bound to GDP; contains a Pleckstrin homology (PH) domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 196-400 4.47e-121

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: 349.00  E-value: 4.47e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 196 FGCQLESLCQREGDTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDRERavtsdgrymfpeqagqegKLDL 275
Cdd:cd04403    1 FGCHLEALCQRENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDE------------------KLDL 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 276 DSAEWDDIHVVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIAHS 355
Cdd:cd04403   63 DDSKWEDIHVITGALKLFFRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHG 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568967400 356 DKNRMTAHNLGIVFGPTLFRPEQEASDMAAHVFYPGQLVQLMLNN 400
Cdd:cd04403  143 EKNRMTTQNLAIVFGPTLLRPEQETGNIAVHMVYQNQIVELILLE 187
PH_ARHGAP9-like cd13233
Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like ...
 1-107 7.09e-50

Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with RhoGAP domain. The ARHGAP members here all have a PH domain upstream of their C-terminal RhoGAP domain. Some have additional N-terminal SH3 and WW domains. The members here include: ARHGAP9, ARHGAP12, ARHGAP15, and ARHGAP27. ARHGAP27 and ARHGAP12 shared the common-domain structure, consisting of SH3, WW, PH, and RhoGAP domains. The PH domain of ArhGAP9 employs a non-canonical phosphoinositide binding mechanism, a variation of the spectrin- Ins(4,5)P2-binding mode, that gives rise to a unique PI binding profile, namely a preference for both PI(4,5)P2 and the PI 3-kinase products PI(3,4,5)P3 and PI(3,4)P2. This lipid binding mechanism is also employed by the PH domain of Tiam1 and Slm1. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 270053  Cd Length: 110  Bit Score: 163.99  E-value: 7.09e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400   1 MTKIAQGGRKLRKNWGPAWVVLTGSSLVFYRErpPQSAslQGWARAGSRPESSVDLRGAALASGRQLSSRRNVLHIRTVP 80
Cdd:cd13233    8 KTKIAENGKKLRKNWSTSWVVLTSSHLLFYKD--AKSA--AKSGNPYSKPESSVDLRGASIEWAKEKSSRKNVFQISTVT 83

                         90       100
                 ....*....|....*....|....*..
gi 568967400  81 GHEFLLQSDEETELRDWHRALRTVIER 107
Cdd:cd13233   84 GTEFLLQSDNDTEIREWFDAIKAVIQR 110
 
Name Accession Description Interval E-value
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 196-400 4.47e-121

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: 349.00  E-value: 4.47e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 196 FGCQLESLCQREGDTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDRERavtsdgrymfpeqagqegKLDL 275
Cdd:cd04403    1 FGCHLEALCQRENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDE------------------KLDL 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 276 DSAEWDDIHVVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIAHS 355
Cdd:cd04403   63 DDSKWEDIHVITGALKLFFRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHG 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568967400 356 DKNRMTAHNLGIVFGPTLFRPEQEASDMAAHVFYPGQLVQLMLNN 400
Cdd:cd04403  143 EKNRMTTQNLAIVFGPTLLRPEQETGNIAVHMVYQNQIVELILLE 187
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 212-378 2.41e-60

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 192.37  E-value: 2.41e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400  212 PSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDRERAVTSDgrymfpeqagqegkldldsAEWDDIHVVTGALK 291
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLD-------------------LEEEDVHVVASLLK 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400  292 LFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIAHSDKNRMTAHNLGIVFGP 371
Cdd:pfam00620  62 LFLRELPEPLLTFELYEEFIEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGP 141


                  ....*..
gi 568967400  372 TLFRPEQ 378
Cdd:pfam00620 142 TLLRPPD 148
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 209-400 1.91e-56

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: 183.24  E-value: 1.91e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400   209 DTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRflvdreravtsdgrymfpEQAGQEGKLDLDSAEWDdIHVVTG 288
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELR------------------DAFDSGPDPDLDLSEYD-VHDVAG 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400   289 ALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIAHSDKNRMTAHNLGIV 368
Cdd:smart00324  62 LLKLFLRELPEPLITYELYEEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIV 141

                          170       180       190
                   ....*....|....*....|....*....|..
gi 568967400   369 FGPTLFRPEQEASDMAAHVFYPGQLVQLMLNN 400
Cdd:smart00324 142 FGPTLLRPPDGEVASLKDIRHQNTVIEFLIEN 173
PH_ARHGAP9-like cd13233
Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like ...
 1-107 7.09e-50

Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with RhoGAP domain. The ARHGAP members here all have a PH domain upstream of their C-terminal RhoGAP domain. Some have additional N-terminal SH3 and WW domains. The members here include: ARHGAP9, ARHGAP12, ARHGAP15, and ARHGAP27. ARHGAP27 and ARHGAP12 shared the common-domain structure, consisting of SH3, WW, PH, and RhoGAP domains. The PH domain of ArhGAP9 employs a non-canonical phosphoinositide binding mechanism, a variation of the spectrin- Ins(4,5)P2-binding mode, that gives rise to a unique PI binding profile, namely a preference for both PI(4,5)P2 and the PI 3-kinase products PI(3,4,5)P3 and PI(3,4)P2. This lipid binding mechanism is also employed by the PH domain of Tiam1 and Slm1. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270053  Cd Length: 110  Bit Score: 163.99  E-value: 7.09e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400   1 MTKIAQGGRKLRKNWGPAWVVLTGSSLVFYRErpPQSAslQGWARAGSRPESSVDLRGAALASGRQLSSRRNVLHIRTVP 80
Cdd:cd13233    8 KTKIAENGKKLRKNWSTSWVVLTSSHLLFYKD--AKSA--AKSGNPYSKPESSVDLRGASIEWAKEKSSRKNVFQISTVT 83

                         90       100
                 ....*....|....*....|....*..
gi 568967400  81 GHEFLLQSDEETELRDWHRALRTVIER 107
Cdd:cd13233   84 GTEFLLQSDNDTEIREWFDAIKAVIQR 110
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 8-105 3.38e-10

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 56.79  E-value: 3.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400     8 GRKLRKNWGPAWVVLTGSSLVFYRERPpqsaslqgwARAGSRPESSVDLRGA--ALASGRQLSSRRNVLHIRTVPGHEFL 85
Cdd:smart00233  11 SGGGKKSWKKRYFVLFNSTLLYYKSKK---------DKKSYKPKGSIDLSGCtvREAPDPDSSKKPHCFEIKTSDRKTLL 81

                           90       100
                   ....*....|....*....|
gi 568967400    86 LQSDEETELRDWHRALRTVI 105
Cdd:smart00233  82 LQAESEEEREKWVEALRKAI 101
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 8-106 1.92e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 54.88  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400    8 GRKLRKNWGPAWVVLTGSSLVFYRERPPQSAslqgwaragSRPESSVDLRGAALASGRQLSS--RRNVLHIRTV---PGH 82
Cdd:pfam00169  11 GGGKKKSWKKRYFVLFDGSLLYYKDDKSGKS---------KEPKGSISLSGCEVVEVVASDSpkRKFCFELRTGertGKR 81

                          90       100
                  ....*....|....*....|....
gi 568967400   83 EFLLQSDEETELRDWHRALRTVIE 106
Cdd:pfam00169  82 TYLLQAESEEERKDWIKAIQSAIR 105
 
Name Accession Description Interval E-value
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 196-400 4.47e-121

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: 349.00  E-value: 4.47e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 196 FGCQLESLCQREGDTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDRERavtsdgrymfpeqagqegKLDL 275
Cdd:cd04403    1 FGCHLEALCQRENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDE------------------KLDL 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 276 DSAEWDDIHVVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIAHS 355
Cdd:cd04403   63 DDSKWEDIHVITGALKLFFRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHG 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568967400 356 DKNRMTAHNLGIVFGPTLFRPEQEASDMAAHVFYPGQLVQLMLNN 400
Cdd:cd04403  143 EKNRMTTQNLAIVFGPTLLRPEQETGNIAVHMVYQNQIVELILLE 187
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 212-378 2.41e-60

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 192.37  E-value: 2.41e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400  212 PSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDRERAVTSDgrymfpeqagqegkldldsAEWDDIHVVTGALK 291
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLD-------------------LEEEDVHVVASLLK 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400  292 LFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIAHSDKNRMTAHNLGIVFGP 371
Cdd:pfam00620  62 LFLRELPEPLLTFELYEEFIEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGP 141


                  ....*..
gi 568967400  372 TLFRPEQ 378
Cdd:pfam00620 142 TLLRPPD 148
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 209-400 1.91e-56

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: 183.24  E-value: 1.91e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400   209 DTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRflvdreravtsdgrymfpEQAGQEGKLDLDSAEWDdIHVVTG 288
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELR------------------DAFDSGPDPDLDLSEYD-VHDVAG 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400   289 ALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIAHSDKNRMTAHNLGIV 368
Cdd:smart00324  62 LLKLFLRELPEPLITYELYEEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIV 141

                          170       180       190
                   ....*....|....*....|....*....|..
gi 568967400   369 FGPTLFRPEQEASDMAAHVFYPGQLVQLMLNN 400
Cdd:smart00324 142 FGPTLLRPPDGEVASLKDIRHQNTVIEFLIEN 173
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 212-400 1.25e-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: 180.96  E-value: 1.25e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 212 PSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDRERavtsdgrymfpeqagqegklDLDSAEWDDIHVVTGALK 291
Cdd:cd00159    1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGE--------------------DIDDLEDYDVHDVASLLK 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 292 LFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIAHSDKNRMTAHNLGIVFGP 371
Cdd:cd00159   61 LYLRELPEPLIPFELYDEFIELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAP 140

                        170       180
                 ....*....|....*....|....*....
gi 568967400 372 TLFRPEQEASDMAAHVFYPGQLVQLMLNN 400
Cdd:cd00159  141 TLLRPPDSDDELLEDIKKLNEIVEFLIEN 169
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 196-405 4.55e-53

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: 175.28  E-value: 4.55e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 196 FGCQLESLCQREGDTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDREravtsdgrymfpeqagqEGKLDL 275
Cdd:cd04398    1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKD-----------------PLNVLL 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 276 DSAE-WD-DIHVVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIA 353
Cdd:cd04398   64 ISPEdYEsDIHSVASLLKLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKE 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568967400 354 HSDKNRMTAHNLGIVFGPTLFrpeQEASDMAAHVFYPGQLVQLMLNNFASLF 405
Cdd:cd04398  144 HESVNRMSVNNLAIIWGPTLM---NAAPDNAADMSFQSRVIETLLDNAYQIF 192
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 195-405 4.16e-51

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: 170.27  E-value: 4.16e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 195 VFGCQLESlCQ--REGDTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDReravtsdgrymfpeqagQEGK 272
Cdd:cd04395    1 TFGVPLDD-CPpsSENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNR-----------------GGFD 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 273 LDLDSAEWDDIHVVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVI 352
Cdd:cd04395   63 IDLQDPRWRDVNVVSSLLKSFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVA 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568967400 353 AHSDKNRMTAHNLGIVFGPTLFRPEQEA-SDMAAHVFYPGQLVQLMLNNFASLF 405
Cdd:cd04395  143 DNSEVNKMEPRNLAIVFGPTLVRTSDDNmETMVTHMPDQCKIVETLIQHYDWFF 196
PH_ARHGAP9-like cd13233
Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like ...
 1-107 7.09e-50

Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with RhoGAP domain. The ARHGAP members here all have a PH domain upstream of their C-terminal RhoGAP domain. Some have additional N-terminal SH3 and WW domains. The members here include: ARHGAP9, ARHGAP12, ARHGAP15, and ARHGAP27. ARHGAP27 and ARHGAP12 shared the common-domain structure, consisting of SH3, WW, PH, and RhoGAP domains. The PH domain of ArhGAP9 employs a non-canonical phosphoinositide binding mechanism, a variation of the spectrin- Ins(4,5)P2-binding mode, that gives rise to a unique PI binding profile, namely a preference for both PI(4,5)P2 and the PI 3-kinase products PI(3,4,5)P3 and PI(3,4)P2. This lipid binding mechanism is also employed by the PH domain of Tiam1 and Slm1. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270053  Cd Length: 110  Bit Score: 163.99  E-value: 7.09e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400   1 MTKIAQGGRKLRKNWGPAWVVLTGSSLVFYRErpPQSAslQGWARAGSRPESSVDLRGAALASGRQLSSRRNVLHIRTVP 80
Cdd:cd13233    8 KTKIAENGKKLRKNWSTSWVVLTSSHLLFYKD--AKSA--AKSGNPYSKPESSVDLRGASIEWAKEKSSRKNVFQISTVT 83

                         90       100
                 ....*....|....*....|....*..
gi 568967400  81 GHEFLLQSDEETELRDWHRALRTVIER 107
Cdd:cd13233   84 GTEFLLQSDNDTEIREWFDAIKAVIQR 110
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 196-405 5.36e-46

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: 156.91  E-value: 5.36e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 196 FGCQLESLCQREGDTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDReravtsDGRymfpeqagqegKLDL 275
Cdd:cd04372    1 YGCDLTTLVKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDR------DGE-----------KADI 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 276 DSAEWDDIHVVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIAHS 355
Cdd:cd04372   64 SATVYPDINVITGALKLYFRDLPIPVITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHE 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568967400 356 DKNRMTAHNLGIVFGPTLFR-PEQEASDMAAHVFYPGQLVQLMLNNFASLF 405
Cdd:cd04372  144 KDNKMNAENLGIVFGPTLMRpPEDSALTTLNDMRYQILIVQLLITNEDVLF 194
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 196-400 2.15e-39

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: 139.87  E-value: 2.15e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 196 FGCQLESLCQREGDTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRflvdreravtsdgrymfpeQAGQEGKLDL 275
Cdd:cd04378    1 FGVDFSQVPRDFPDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLC-------------------QAFENGKDLV 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 276 DSAEWDDiHVVTGALKLFFRELPQPLVPALLLPDF----RDALELSE----PEQC------LSKIQKLIDSLPRPNHDTL 341
Cdd:cd04378   62 ELSELSP-HDISSVLKLFLRQLPEPLILFRLYNDFialaKEIQRDTEedkaPNTPievnriIRKLKDLLRQLPASNYNTL 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967400 342 KYILEHLCRVIAHSDKNRMTAHNLGIVFGPTLFRPEQEASD--MAAHVFYPGQ--LVQLMLNN 400
Cdd:cd04378  141 QHLIAHLYRVAEQFEENKMSPNNLGIVFGPTLIRPRPGDADvsLSSLVDYGYQarLVEFLITN 203
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 196-397 1.32e-37

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: 135.06  E-value: 1.32e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 196 FGCQLESLCQREGDTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVD-RERAVTSDGRYMfpeqagqegkld 274
Cdd:cd04387    1 FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDtNNKDVSVMLSEM------------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 275 ldsaewdDIHVVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIAH 354
Cdd:cd04387   69 -------DVNAIAGTLKLYFRELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAER 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568967400 355 SDKNRMTAHNLGIVFGPTLFRPEQEASDMAAHVFYPGQLVQLM 397
Cdd:cd04387  142 EEVNKMSLHNLATVFGPTLLRPSEKESKIPTNTMTDSWSLEVM 184
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 195-378 2.57e-37

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: 134.17  E-value: 2.57e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 195 VFGCQLESLCQREGDTVPSFVRLCVEAVDKKGLdVDGIYRVSGNLAVVQKLRFLVDRERAvtsdgrymfPEQAGQEGKld 274
Cdd:cd04384    2 VFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGI-VDGIYRLSGIASNIQRLRHEFDSEQI---------PDLTKDVYI-- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 275 ldsaewDDIHVVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIAH 354
Cdd:cd04384   70 ------QDIHSVSSLCKLYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKY 143

                        170       180
                 ....*....|....*....|....
gi 568967400 355 SDKNRMTAHNLGIVFGPTLFRPEQ 378
Cdd:cd04384  144 CSITNMHAKNLAIVWAPNLLRSKQ 167
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
 213-379 3.55e-37

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: 134.06  E-value: 3.55e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 213 SFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKL-RFLVDRERAvtsdgrymfpeqagQEGKLDLDSAEWDdIHVVTGALK 291
Cdd:cd04374   30 KFVRKCIEAVETRGINEQGLYRVVGVNSKVQKLlSLGLDPKTS--------------TPGDVDLDNSEWE-IKTITSALK 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 292 LFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIAHSDKNRMTAHNLGIVFGP 371
Cdd:cd04374   95 TYLRNLPEPLMTYELHNDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGP 174


                 ....*...
gi 568967400 372 TLFRPEQE 379
Cdd:cd04374  175 TLLRPQEE 182
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 196-401 7.26e-37

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: 132.58  E-value: 7.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 196 FGCQLESLCQREGDtVPSFVRLCVEAVDKKGLDVDGIYRVSGN---LAVVQKlRFLvdreravtsdgrymfpeqagQEGK 272
Cdd:cd04373    1 FGVPLANVVTSEKP-IPIFLEKCVEFIEATGLETEGIYRVSGNkthLDSLQK-QFD--------------------QDHN 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 273 LDLDSAEWDdIHVVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVI 352
Cdd:cd04373   59 LDLVSKDFT-VNAVAGALKSFFSELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVS 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568967400 353 AHSDKNRMTAHNLGIVFGPTLFRPeqEASDMAAhvFYPGQLVQLMLNNF 401
Cdd:cd04373  138 QNSKVNLMTSENLSICFWPTLMRP--DFTSMEA--LSATRIYQTIIETF 182
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 205-386 6.18e-35

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: 127.42  E-value: 6.18e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 205 QREGDTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKL--RFLVDrERAVTSDgrymfpeqagqEGKldldsaewDD 282
Cdd:cd04385    9 QLTDNDIPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLleAFRKD-ARSVQLR-----------EGE--------YT 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 283 IHVVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIAHSDKNRMTA 362
Cdd:cd04385   69 VHDVADVLKRFLRDLPDPLLTSELHAEWIEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSV 148

                        170       180
                 ....*....|....*....|....
gi 568967400 363 HNLGIVFGPTLFRPEQEASDMAAH 386
Cdd:cd04385  149 HNLALVFGPTLFQTDEHSVGQTSH 172
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 194-405 3.83e-33

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: 123.34  E-value: 3.83e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 194 QVFGCQLESLCQREGDTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDreravtsdgrymfpeqAGQEgKL 273
Cdd:cd04386    3 PVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALD----------------AGTF-SL 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 274 DLDSaEWDDIHVVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIA 353
Cdd:cd04386   66 PLDE-FYSDPHAVASALKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQ 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568967400 354 HSDKNRMTAHNLGIVFGPTLFRPEQEASD------MAAHVfypGQLVQLMLNNFASLF 405
Cdd:cd04386  145 KSDENKMSPSNIAIVLAPNLLWAKNEGSLaemaagTSVHV---VAIVELIISHADWFF 199
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 194-385 4.57e-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: 122.83  E-value: 4.57e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 194 QVFGCQLESLCQR--EGDTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDReravtsdgrymfpeqagqeg 271
Cdd:cd04404    4 QQFGVSLQFLKEKnpEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNM-------------------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 272 KLDLDSAEWDDIHVVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQcLSKIQKLIDSLPRPNHDTLKYILEHLCRV 351
Cdd:cd04404   64 GEPVDFDQYEDVHLPAVILKTFLRELPEPLLTFDLYDDIVGFLNVDKEER-VERVKQLLQTLPEENYQVLKYLIKFLVQV 142

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568967400 352 IAHSDKNRMTAHNLGIVFGPTLFRPEQEASDMAA 385
Cdd:cd04404  143 SAHSDQNKMTNSNLAVVFGPNLLWAKDASMSLSA 176
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 196-375 7.42e-32

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: 119.08  E-value: 7.42e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 196 FGCQLESLCQrEGDTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDReravtsdgrymfpeqagqegklDL 275
Cdd:cd04377    1 FGVSLSSLTS-EDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDT----------------------DP 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 276 DSAEWDD--IHVVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIA 353
Cdd:cd04377   58 DSVNLEDypIHVITSVLKQWLRELPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVAL 137

                        170       180
                 ....*....|....*....|..
gi 568967400 354 HSDKNRMTAHNLGIVFGPTLFR 375
Cdd:cd04377  138 QEEVNRMSANALAIVFAPCILR 159
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 196-381 1.16e-31

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: 119.49  E-value: 1.16e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 196 FGCQLESLCQREGDT--VPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDRERAVTsdgrymfpeqagqegkl 273
Cdd:cd04379    1 FGVPLSRLVEREGESrdVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAV----------------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 274 DLDSAEWDDIHVVTGALKLFFRELPQPLVPALLLPDFRDALEL---SEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCR 350
Cdd:cd04379   64 ELSEELYPDINVITGVLKDYLRELPEPLITPQLYEMVLEALAValpNDVQTNTHLTLSIIDCLPLSAKATLLLLLDHLSL 143

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568967400 351 VIAHSDKNRMTAHNLGIVFGPTLFRPEQEAS 381
Cdd:cd04379  144 VLSNSERNKMTPQNLAVCFGPVLMFCSQEFS 174
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
 195-406 1.37e-30

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: 115.92  E-value: 1.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 195 VFGCQLE-----SLCQREGDTVPSFVRLCVEAVDKKG-LDVDGIYRVSGNLAVVQKLRflvdreravtsdgrymfpEQAG 268
Cdd:cd04400    1 IFGSPLEeavelSSHKYNGRDLPSVVYRCIEYLDKNRaIYEEGIFRLSGSASVIKQLK------------------ERFN 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 269 QEGKLDL-DSAEWDDIHVVTGALKLFFRELPQPLVPALLLPDFRDALEL-SEPEQCLSKIQKLIDSLPRPNHDTLKYILE 346
Cdd:cd04400   63 TEYDVDLfSSSLYPDVHTVAGLLKLYLRELPTLILGGELHNDFKRLVEEnHDRSQRALELKDLVSQLPQANYDLLYVLFS 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 347 HLCRVIAHSDKNRMTAHNLGIVFGPTLfrpeqeasDMAAHVFypgqlvQLMLNNFASLFT 406
Cdd:cd04400  143 FLRKIIEHSDVNKMNLRNVCIVFSPTL--------NIPAGIF------VLFLTDFDCIFG 188
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 211-374 3.16e-30

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: 115.08  E-value: 3.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 211 VPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLR--FLvdRERAVTSDGRYmfpeqagqegkldldsaewdDIHVVTG 288
Cdd:cd04382   17 IPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKekFL--RGKTVPNLSKV--------------------DIHVICG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 289 ALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRViAHSDKNRMTAHNLGIV 368
Cdd:cd04382   75 CLKDFLRSLKEPLITFALWKEFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRV-AQSPECKMDINNLARV 153


                 ....*.
gi 568967400 369 FGPTLF 374
Cdd:cd04382  154 FGPTIV 159
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 196-398 4.29e-30

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: 115.29  E-value: 4.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 196 FGCQLESLCQREGDTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRflvdreravtsdgrymfpeQAGQEGKLDL 275
Cdd:cd04409    1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLC-------------------QAFENGKDLV 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 276 DSAEWDDiHVVTGALKLFFRELPQPLVPALLLPDF-------------RDALELSEPEQ---------CLSKIQKLIDSL 333
Cdd:cd04409   62 ELSELSP-HDISNVLKLYLRQLPEPLILFRLYNEFiglakesqhvnetQEAKKNSDKKWpnmctelnrILLKSKDLLRQL 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568967400 334 PRPNHDTLKYILEHLCRVIAHSDKNRMTAHNLGIVFGPTLFRPEQEASD--MAAHVFYPGQ--LVQLML 398
Cdd:cd04409  141 PAPNYNTLQFLIVHLHRVSEQAEENKMSASNLGIIFGPTLIRPRPTDATvsLSSLVDYPHQarLVELLI 209
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 196-400 1.68e-29

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: 113.37  E-value: 1.68e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 196 FGCQLESLCQREGDTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRflvdreravtsdgrymfpeQAGQEGKLDL 275
Cdd:cd04408    1 FGVDFSQLPRDFPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLC-------------------QAFENGRDLV 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 276 DSAEwDDIHVVTGALKLFFRELPQPLVPALLLPDF----RDALELSE--------PEQCLSKIQKLIDSLPRPNHDTLKY 343
Cdd:cd04408   62 DLSG-HSPHDITSVLKHFLKELPEPVLPFQLYDDFialaKELQRDSEkaaespsiVENIIRSLKELLGRLPVSNYNTLRH 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967400 344 ILEHLCRVIAHSDKNRMTAHNLGIVFGPTLFRPeQEASDMAAHVF----YPGQLVQLMLNN 400
Cdd:cd04408  141 LMAHLYRVAERFEDNKMSPNNLGIVFGPTLLRP-LVGGDVSMICLldtgYQAQLVEFLISN 200
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 195-406 7.87e-28

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: 109.36  E-value: 7.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 195 VFGCQLESLCQR-----EGDTVPSFVRLCVEAVDKKGLDVDGIYRVSGnlaVVQKLRFLvdreravtsdgrYMFPEQAGQ 269
Cdd:cd04391    1 LFGVPLSTLLERdqkkvPGSKVPLIFQKLINKLEERGLETEGILRIPG---SAQRVKFL------------CQELEAKFY 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 270 EGKLDLDSAEwddIHVVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLC 349
Cdd:cd04391   66 EGTFLWDQVK---QHDAASLLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQ 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568967400 350 RVIAHSDKNRMTAHNLGIVFGPTLFRP----------EQEASDMAAHVfypGQLVQLMLNNFASLFT 406
Cdd:cd04391  143 KVVDHEEKNKMNLWNVAMIMAPNLFPPrgkhskdnesLQEEVNMAAGC---ANIMRLLIRYQDLLWT 206
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 195-405 4.79e-27

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: 106.76  E-value: 4.79e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 195 VFGCQLESLCQREGD----TVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDreravtsdgrymfpeqAGQE 270
Cdd:cd04390    2 VFGQRLEDTVAYERKfgprLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFD----------------AGER 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 271 GKLDLDSaewdDIHVVTGALKLFFRELPQPLVPALLLPDFRDA--LELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHL 348
Cdd:cd04390   66 PSFDSDT----DVHTVASLLKLYLRELPEPVIPWAQYEDFLSCaqLLSKDEEKGLGELMKQVSILPKVNYNLLSYICRFL 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568967400 349 CRVIAHSDKNRMTAHNLGIVFGPTLFRPEQE--ASDMAAHVFYPgQLVQLMLNNFASLF 405
Cdd:cd04390  142 DEVQSNSSVNKMSVQNLATVFGPNILRPKVEdpATIMEGTPQIQ-QLMTVMISKHEPLF 199
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 196-375 1.24e-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: 105.07  E-value: 1.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 196 FGCQLESLCQrEGDTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVdreravtsdgrymfpeQAGQEG-KLd 274
Cdd:cd04407    1 FGVRVGSLTS-NKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLL----------------QADPENvKL- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 275 ldsaEWDDIHVVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIAH 354
Cdd:cd04407   63 ----ENYPIHAITGLLKQWLRELPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALE 138

                        170       180
                 ....*....|....*....|.
gi 568967400 355 SDKNRMTAHNLGIVFGPTLFR 375
Cdd:cd04407  139 EDVNRMSPNALAIVFAPCLLR 159
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 194-374 1.32e-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: 102.54  E-value: 1.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 194 QVFGCQLESLcQREG---DTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFlvdreravtsdgRYmfpeqagqE 270
Cdd:cd04393    1 KVFGVPLQEL-QQAGqpeNGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQ------------RL--------D 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 271 GKLDLDSAEWDDIHVVTGALKLFFRELPQPLVPALLLPDF-RDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLC 349
Cdd:cd04393   60 SGEEVDLSKEADVCSAASLLRLFLQELPEGLIPASLQIRLmQLYQDYNGEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLS 139

                        170       180
                 ....*....|....*....|....*
gi 568967400 350 RVIAHSDKNRMTAHNLGIVFGPTLF 374
Cdd:cd04393  140 NVASQHHENRMTAENLAAVFGPDVF 164
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 196-387 6.59e-23

RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in srGAPs. srGAPs are components of the intracellular part of Slit-Robo signalling pathway that is important for axon guidance and cell migration. srGAPs contain an N-terminal FCH domain, a central RhoGAP domain and a C-terminal SH3 domain; this SH3 domain interacts with the intracellular proline-rich-tail of the Roundabout receptor (Robo). This interaction with Robo then activates the rhoGAP domain which in turn inhibits Cdc42 activity. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239848  Cd Length: 188  Bit Score: 95.18  E-value: 6.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 196 FGCQLESLCQREGDTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDReravtsdgrymfpeqaGQEGKLDL 275
Cdd:cd04383    3 FNGSLEEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFER----------------GEDPLADD 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 276 DSAEwdDIHVVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYI---LEHLCRvi 352
Cdd:cd04383   67 QNDH--DINSVAGVLKLYFRGLENPLFPKERFEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLfafLNHLSQ-- 142

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568967400 353 aHSDKNRMTAHNLGIVFGPTLFR-PE-QEASDMAAHV 387
Cdd:cd04383  143 -FSDENMMDPYNLAICFGPTLMPvPEgQDQVSCQAHV 178
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 196-405 2.34e-22

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: 93.52  E-value: 2.34e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 196 FGCQLESLCqrEGDTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRflvdreravtsdgrymfpEQAGQEGKLDL 275
Cdd:cd04402    2 FGQPLSNIC--EDDNLPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELK------------------EKLNSGVEVDL 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 276 DSaewDDIHVVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIAHS 355
Cdd:cd04402   62 KA---EPVLLLASVLKDFLRNIPGSLLSSDLYEEWMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNS 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568967400 356 DKNRMTAHNLGIVFGPTLFRPEQEASDMAAHVFYPGQLVQLMLNNFASLF 405
Cdd:cd04402  139 ETNKMDAFNLAVCIAPSLLWPPASSELQNEDLKKVTSLVQFLIENCQEIF 188
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 211-406 2.93e-22

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: 93.66  E-value: 2.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 211 VPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDReravtsdgrymfpeqaGQEGKLDldsaEWDDIHVVTGAL 290
Cdd:cd04376    9 VPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDR----------------GIDVVLD----ENHSVHDVAALL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 291 KLFFRELPQPLVPALLLPDFRDALELsEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIAHSDK-----------NR 359
Cdd:cd04376   69 KEFFRDMPDPLLPRELYTAFIGTALL-EPDEQLEALQLLIYLLPPCNCDTLHRLLKFLHTVAEHAADsidedgqevsgNK 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568967400 360 MTAHNLGIVFGPTLFRPEQ-------EASDMAAHVFYPGQLVQLMLNNFASLFT 406
Cdd:cd04376  148 MTSLNLATIFGPNLLHKQKsgerefvQASLRIEESTAIINVVQTMIDNYEELFM 201
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 196-373 1.14e-20

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: 88.65  E-value: 1.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 196 FGCQLESLCQR----EGDTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDRERAVTSDgrymfpeqagqeg 271
Cdd:cd04381    1 FGASLSLAVERsrchDGIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRESPNLE------------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 272 klDLDSaewddiHVVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRV 351
Cdd:cd04381   68 --EYEP------PTVASLLKQYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHV 139

                        170       180
                 ....*....|....*....|..
gi 568967400 352 IAHSDKNRMTAHNLGIVFGPTL 373
Cdd:cd04381  140 IAQELETKMNIQNISIVLSPTV 161
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 195-374 3.52e-19

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: 85.55  E-value: 3.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 195 VFGCQLESLCQREGDTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVdreravtsdgrymfpEQAGQEGKLD 274
Cdd:cd04375    4 VFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMI---------------ESSTDNVNYD 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 275 LDSAewddiHVVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIAH 354
Cdd:cd04375   69 GQQA-----YDVADMLKQYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAAN 143

                        170       180
                 ....*....|....*....|
gi 568967400 355 SDKNRMTAHNLGIVFGPTLF 374
Cdd:cd04375  144 SQENQMTATNLAVCLAPSLF 163
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 195-383 6.36e-19

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: 84.45  E-value: 6.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 195 VFGCQLESL----CQREGDtVPSF-VRLCVEAVDKkgLDVDGIYRVSGNLAVVQKLRFLVDRERAVtsdgrymfpeqagq 269
Cdd:cd04394    1 VFGVPLHSLphstVPEYGN-VPKFlVDACTFLLDH--LSTEGLFRKSGSVVRQKELKAKLEGGEAC-------------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 270 egkldLDSAEWDDihvVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLC 349
Cdd:cd04394   64 -----LSSALPCD---VAGLLKQFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLY 135

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568967400 350 RVIAHSDKNRMTAHNLGIVFGPTLFRPEQEASDM 383
Cdd:cd04394  136 DVAQRCSENKMDSSNLAVIFAPNLFQSEEGGEKM 169
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 196-384 2.27e-18

RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXA. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239871  Cd Length: 186  Bit Score: 82.36  E-value: 2.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 196 FGCQLESLCQREgDTVPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDReravtsdgrymfpeqagqegklDL 275
Cdd:cd04406    1 FGVELSRLTSED-RSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDT----------------------DA 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 276 DSAEWDD--IHVVTGALKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIA 353
Cdd:cd04406   58 NSVNLDDynIHVIASVFKQWLRDLPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIAL 137

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568967400 354 HSDKNRMTAHNLGIVFGPTLFR------PEQEASDMA 384
Cdd:cd04406  138 QEETNRMSANALAIVFAPCILRcpdttdPLQSVQDIS 174
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 224-405 5.30e-17

RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP19-like proteins. The function of ArhGAP19 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239857  Cd Length: 208  Bit Score: 79.04  E-value: 5.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 224 KKGLDVDGIYRVSGNLAVVQKLRFLVDRERAvtsdgrymfpeqagqegkLDLDSAEWDdIHVVTGALKLFFRELPQPLVP 303
Cdd:cd04392   21 EKNLRVEGLFRKPGNSARQQELRDLLNSGTD------------------LDLESGGFH-AHDCATVLKGFLGELPEPLLT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 304 ALLLPDFRDALELS------------EPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRVIAHSDKNRMTAHNLGIVFGP 371
Cdd:cd04392   82 HAHYPAHLQIADLCqfdekgnktsapDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTP 161

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568967400 372 TLFRPEQ-EASDMAAHVFYPGQLVQLMLNNFASLF 405
Cdd:cd04392  162 HLICPRNlTPEDLHENAQKLNSIVTFMIKHSQKLF 196
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 209-398 1.09e-16

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: 77.99  E-value: 1.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 209 DTVPSFVRLCVEAVDKKGLDVDGIYR--VSGNLAvvqKLRFLVDRERAvtsdgrymfpeqagqegklDLDSAEWDdIHVV 286
Cdd:cd04388   13 DVAPPLLIKLVEAIEKKGLESSTLYRtqSSSSLT---ELRQILDCDAA-------------------SVDLEQFD-VAAL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 287 TGALKLFFRELPQPLVPALLLPD-FRDALELSEPEQCLSKIQKLIDSLPRPNHD--TLKYILEHLCRVIAHSDKNRMTAH 363
Cdd:cd04388   70 ADALKRYLLDLPNPVIPAPVYSEmISRAQEVQSSDEYAQLLRKLIRSPNLPHQYwlTLQYLLKHFFRLCQSSSKNLLSAR 149

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568967400 364 NLGIVFGPTLFRPEQEASDMAAHvfyPGQLVQLML 398
Cdd:cd04388  150 ALAEIFSPLLFRFQPASSDSPEF---HIRIIEVLI 181
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 211-405 1.10e-15

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: 75.52  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 211 VPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDreravtSDGRYmfpeqagqeGKldldSAEWDD--IHVVTG 288
Cdd:cd04396   32 IPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFS------TPPDY---------GK----SFDWDGytVHDAAS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 289 ALKLFFRELPQPLVPALLLPDFRDAL-----------------ELSEPEQCLSKIQKLIDSLPRPNHDTLKYILEHLCRV 351
Cdd:cd04396   93 VLRRYLNNLPEPLVPLDLYEEFRNPLrkrprilqymkgrinepLNTDIDQAIKEYRDLITRLPNLNRQLLLYLLDLLAVF 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568967400 352 IAHSDKNRMTAHNLGIVFGPTLFrpEQEASDMAAHVFYPGQLVQLMLNNFASLF 405
Cdd:cd04396  173 ARNSDKNLMTASNLAAIFQPGIL--SHPDHEMDPKEYKLSRLVVEFLIEHQDKF 224
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 196-379 2.02e-13

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: 68.19  E-value: 2.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 196 FGCQLESLCQREGDTVPSF------VRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDReravtsdGRYmfpeqagq 269
Cdd:cd04389    1 FGSSLEEIMDRQKEKYPELklpwilTFLSEKVLALGGFQTEGIFRVPGDIDEVNELKLRVDQ-------WDY-------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 270 egkldlDSAEWDDIHVVTGALKLFFRELPQPLVPALLlpdFRDALELSE-PEqclsKIQKLIDSLPRPNHDTLKYILEHL 348
Cdd:cd04389   66 ------PLSGLEDPHVPASLLKLWLRELEEPLIPDAL---YQQCISASEdPD----KAVEIVQKLPIINRLVLCYLINFL 132

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568967400 349 --CRVIAHSDKNRMTAHNLGIVFGPTLFRPEQE 379
Cdd:cd04389  133 qvFAQPENVAHTKMDVSNLAMVFAPNILRCTSD 165
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 196-401 2.45e-13

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: 68.55  E-value: 2.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 196 FGCQLESLCQREG-DT----------VPSFVRLCVEAVDKKGLDVDGIYRVSGNLAVVQKLRFLVDRERAVTSDgryMFP 264
Cdd:cd04397    1 FGVPLEILVEKFGaDStlgvgpgklrIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVPD---LSK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 265 EQAGQEGKLdldsaewddihvvtgaLKLFFRELPQPLVPALLLPDFRDALELSEPEQCLSKIQKLIDSLPRPNHDTLKYI 344
Cdd:cd04397   78 ENPVQLAAL----------------LKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVL 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568967400 345 LEHLCRV--IAHSDK---NRMTAHNLGIVFGPTLFRPEQEASDMAAHVFYPGQLVQLMLNNF 401
Cdd:cd04397  142 FSFLKWVssFSHIDEetgSKMDIHNLATVITPNILYSKTDNPNTGDEYFLAIEAVNYLIENN 203
PH_ARHGAP21-like cd01253
ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho ...
 7-102 5.77e-12

ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with a RhoGAP domain. These proteins functions as a GTPase-activating protein (GAP) for RHOA and CDC42. ARHGAP21 controls the Arp2/3 complex and F-actin dynamics at the Golgi complex by regulating the activity of the small GTPase Cdc42. It is recruited to the Golgi by to GTPase, ARF1, through its PH domain and its helical motif. It is also required for CTNNA1 recruitment to adherens junctions. ARHGAP21 and it related proteins all contains a PH domain and a RhoGAP domain. Some of the members have additional N-terminal domains including PDZ, SH3, and SPEC. The ARHGAP21 PH domain interacts with the GTPbound forms of both ARF1 and ARF6 ARF-binding domain/ArfBD. The members here include: ARHGAP15, ARHGAP21, and ARHGAP23. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269955  Cd Length: 113  Bit Score: 62.00  E-value: 5.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400   7 GGRKLRKNWGPAWVVLTGSSLVFYRERPPQSASLQGWARAGSRpessVDLRGAALASGRQLSSRRNVLHIRTVPGHEFLL 86
Cdd:cd01253   16 GKRVSDRSWKQAWAVLRGHSLYLYKDKREQTPALSIELGSEQR----ISIRGCIVDIAYSYTKRKHVFRLTTSDFSEYLF 91

                         90
                 ....*....|....*.
gi 568967400  87 QSDEETELRDWHRALR 102
Cdd:cd01253   92 QAEDRDDMLGWIKAIQ 107
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 8-105 3.38e-10

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 56.79  E-value: 3.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400     8 GRKLRKNWGPAWVVLTGSSLVFYRERPpqsaslqgwARAGSRPESSVDLRGA--ALASGRQLSSRRNVLHIRTVPGHEFL 85
Cdd:smart00233  11 SGGGKKSWKKRYFVLFNSTLLYYKSKK---------DKKSYKPKGSIDLSGCtvREAPDPDSSKKPHCFEIKTSDRKTLL 81

                           90       100
                   ....*....|....*....|
gi 568967400    86 LQSDEETELRDWHRALRTVI 105
Cdd:smart00233  82 LQAESEEEREKWVEALRKAI 101
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 8-106 1.92e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 54.88  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400    8 GRKLRKNWGPAWVVLTGSSLVFYRERPPQSAslqgwaragSRPESSVDLRGAALASGRQLSS--RRNVLHIRTV---PGH 82
Cdd:pfam00169  11 GGGKKKSWKKRYFVLFDGSLLYYKDDKSGKS---------KEPKGSISLSGCEVVEVVASDSpkRKFCFELRTGertGKR 81

                          90       100
                  ....*....|....*....|....
gi 568967400   83 EFLLQSDEETELRDWHRALRTVIE 106
Cdd:pfam00169  82 TYLLQAESEEERKDWIKAIQSAIR 105
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 196-381 4.85e-08

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: 53.11  E-value: 4.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 196 FGCQLESLCQREGDTVPSFVRLCVEAVDKKGLDVDG------IYRVSGNLAVVQKLRFLVDREravtsdgrymFPEQAGQ 269
Cdd:cd04399    1 FGVDLETRCRLDKKVVPLIVSAILSYLDQLYPDLINdevrrnVWTDPVSLKETHQLRNLLNKP----------KKPDKEV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 270 EGKLDLDSAewddihVVTGALKLFFRELPQPLVPA-------LLLPDFRDALELSEPEQcLSKIQKLIDSLPRPNHDTLK 342
Cdd:cd04399   71 IILKKFEPS------TVASVLKLYLLELPDSLIPHdiydlirSLYSAYPPSQEDSDTAR-IQGLQSTLSQLPKSHIATLD 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568967400 343 YILEHLCRVI---AHSDKNRMTAHNLGIVFGPTLFRPEQEAS 381
Cdd:cd04399  144 AIITHFYRLIeitKMGESEEEYADKLATSLSREILRPIIESL 185
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 8-101 7.90e-08

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 49.85  E-value: 7.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400   8 GRKLRKNWGPAWVVLTGSSLVFYRERPpqsaslqgwaRAGSRPESSVDLRGAALASGRQLSSRRNVLHIRTVPGHEFLLQ 87
Cdd:cd00821    9 GGGGLKSWKKRWFVLFEGVLLYYKSKK----------DSSYKPKGSIPLSGILEVEEVSPKERPHCFELVTPDGRTYYLQ 78

                         90
                 ....*....|....
gi 568967400  88 SDEETELRDWHRAL 101
Cdd:cd00821   79 ADSEEERQEWLKAL 92
PH_beta_spectrin cd10571
Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a ...
 7-104 1.39e-06

Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a major component of the cytoskeleton underlying cellular membranes. Beta spectrin consists of multiple spectrin repeats followed by a PH domain, which binds to inositol-1,4,5-trisphosphate. The PH domain of beta-spectrin is thought to play a role in the association of spectrin with the plasma membrane of cells. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269975  Cd Length: 106  Bit Score: 46.45  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400   7 GGRK-LRKNWGPAWVVLTGSSLVFYRERppQSASlqgwARAGSRPESSVDLRGAA--LASGRQlsSRRNVLHIRTVPGHE 83
Cdd:cd10571   14 GGKKaSNRSWKNVYTVLRGQELSFYKDQ--KAAK----SGITYAAEPPLNLYNAVceVASDYT--KKKHVFRLKLSDGAE 85

                         90       100
                 ....*....|....*....|.
gi 568967400  84 FLLQSDEETELRDWHRALRTV 104
Cdd:cd10571   86 FLFQAKDEEEMNQWVKKISFA 106
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 282-380 1.20e-05

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: 46.18  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 282 DIHVVTGALKLFFRELPQPLVPALLlpdFRDALE-LSEPEQCLSKIqkLIDSLPRPNHDTLKYILEHLCRVIAHSDKNRM 360
Cdd:cd04380  103 SAESVAEALLLFLESLPDPIIPYSL---YERLLEaVANNEEDKRQV--IRISLPPVHRNVFVYLCSFLRELLSESADRGL 177

                         90       100
                 ....*....|....*....|
gi 568967400 361 TAHNLGIVFGPTLFRPEQEA 380
Cdd:cd04380  178 DENTLATIFGRVLLRDPPRA 197
PH1_Pleckstrin_2 cd13301
Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in ...
 11-110 1.79e-05

Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in platelets. This name is derived from platelet and leukocyte C kinase substrate and the KSTR string of amino acids. Pleckstrin 2 contains two PH domains and a DEP (dishvelled, egl-10, and pleckstrin) domain. Unlike pleckstrin 1, pleckstrin 2 does not contain obvious sites of PKC phosphorylation. Pleckstrin 2 plays a role in actin rearrangement, large lamellipodia and peripheral ruffle formation, and may help orchestrate cytoskeletal arrangement. The PH domains of pleckstrin 2 are thought to contribute to lamellipodia formation. This cd contains the first PH domain repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270113  Cd Length: 108  Bit Score: 43.52  E-value: 1.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400  11 LRKNWGPAWVVLTGSSLVFY---RERPPqsaslQGWaragsrpessVDLRGAALASG-RQLSSRRNVLHIRTVPGHEFLL 86
Cdd:cd13301   15 VVNNWKARWFVLKEDGLEYYkkkTDSSP-----KGM----------IPLKGCTITSPcLEYGKRPLVFKLTTAKGQEHFF 79

                         90       100
                 ....*....|....*....|....*..
gi 568967400  87 Q--SDEEtelRD-WHRALRTVIERLDR 110
Cdd:cd13301   80 QacSREE---RDaWAKDITKAITCLEG 103
RhoGAP_fMSB1 cd04401
RhoGAP_fMSB1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 253-374 3.54e-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: 41.56  E-value: 3.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400 253 RAVTSDGRYMFPEQAGQ---EGKLDLDSAEwDDIHVVTGALKLFFRELPQPLVPAL-LLPDFRDALELSE-PEQCLSKIQ 327
Cdd:cd04401   38 DKVRSLINSFFPSQNGQlqgTAELLDELRY-ADPHTLILVLKWIWSRLPGSKVIWWeVYEEFKARERRSNyPADAFLDLL 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568967400 328 KLidSLPRPNHDTLKY-ILEHLCRVIAHSDKNRMTAHNLGIVFGPTLF 374
Cdd:cd04401  117 PQ--CLSSPAHASILYdFFDLLSSIAAHSSVNGMSGRKLSKMAGPWAF 162
PH1_PLEKHH1_PLEKHH2 cd13282
Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 ...
 1-109 1.07e-03

Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 (PLEKHH1) PH domain, repeat 1; PLEKHH1 and PLEKHH2 (also called PLEKHH1L) are thought to function in phospholipid binding and signal transduction. There are 3 Human PLEKHH genes: PLEKHH1, PLEKHH2, and PLEKHH3. There are many isoforms, the longest of which contain a FERM domain, a MyTH4 domain, two PH domains, a peroximal domain, a vacuolar domain, and a coiled coil stretch. The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241436  Cd Length: 96  Bit Score: 38.05  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400   1 MTKIaqGGRKlrKNWGPAWVVLTGSSLVFYRERppqsaslqgwARAGSRPESSVDLRGAAlasGRQLSSRRNVLHIRTvP 80
Cdd:cd13282    5 LTKL--GGKV--KTWKRRWFVLKNGELFYYKSP----------NDVIRKPQGQIALDGSC---EIARAEGAQTFEIVT-E 66

                         90       100
                 ....*....|....*....|....*....
gi 568967400  81 GHEFLLQSDEETELRDWHRALRTVIERLD 109
Cdd:cd13282   67 KRTYYLTADSENDLDEWIRVIQNVLRRQA 95
PH_AtPH1 cd13276
Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all ...
 13-110 7.96e-03

Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all plant tissue and is proposed to be the plant homolog of human pleckstrin. Pleckstrin consists of two PH domains separated by a linker region, while AtPH has a single PH domain with a short N-terminal extension. AtPH1 binds PtdIns3P specifically and is thought to be an adaptor molecule since it has no obvious catalytic functions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270095  Cd Length: 106  Bit Score: 35.76  E-value: 7.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967400  13 KNWGPAWVVLTGSSLVFYRERPPQSaslqgwaraGSRPESSVDLRGA-ALASGRQLSSRRNVLHIRTvPGHEFLLQSDEE 91
Cdd:cd13276   13 KTWRRRWFVLKQGKLFWFKEPDVTP---------YSKPRGVIDLSKClTVKSAEDATNKENAFELST-PEETFYFIADNE 82

                         90
                 ....*....|....*....
gi 568967400  92 TELRDWHRALRTVIERLDR 110
Cdd:cd13276   83 KEKEEWIGAIGRAIVKHSR 101
 
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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