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Conserved domains on  [gi|19921564|ref|NP_610002|]
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Cd GTPase activating protein-related, isoform A [Drosophila melanogaster]

Protein Classification

Rho GTPase-activating protein( domain architecture ID 10246376)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
420-613 2.78e-109

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: 345.64  E-value: 2.78e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  420 RVFNCDLSEHLLNSGQDIPMVLRSCAEFIENYGVIDGIYRLSGITSNIQRLRRAFDEERVPDLGNPEMKQDIHAVSSLLK 499
Cdd:cd04384    1 RVFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGIVDGIYRLSGIASNIQRLRHEFDSEQIPDLTKDVYIQDIHSVSSLCK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  500 MYFRELPNPLCTYQLYDNFVEAIQvkADEADERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVW 579
Cdd:cd04384   81 LYFRELPNPLLTYQLYEKFSEAVS--AASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVW 158
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 19921564  580 APNLLRSPALESG---GVAALRGVGVQAVVTEYLIRN 613
Cdd:cd04384  159 APNLLRSKQIESAcfsGTAAFMEVRIQSVVVEFILNH 195
SH3_ARHGAP32_33 cd11835
Src homology 3 domain of Rho GTPase-activating proteins 32 and 33, and similar proteins; ...
299-358 4.79e-29

Src homology 3 domain of Rho GTPase-activating proteins 32 and 33, and similar proteins; Members of this family contain N-terminal PX and Src Homology 3 (SH3) domains, a central Rho GAP domain, and C-terminal extensions. RhoGAPs (or ARHGAPs) bind to Rho proteins and enhance the hydrolysis rates of bound GTP. ARHGAP32 is also called RICS, PX-RICS, p250GAP, or p200RhoGAP. It is a Rho GTPase-activating protein for Cdc42 and Rac1, and is implicated in the regulation of postsynaptic signaling and neurite outgrowth. PX-RICS, a variant of RICS that contain PX and SH3 domains, is the main isoform expressed during neural development. It is involved in neural functions including axon and dendrite extension, postnatal remodeling, and fine-tuning of neural circuits during early brain development. ARHGAP33, also called sorting nexin 26 or TCGAP (Tc10/CDC42 GTPase-activating protein), is widely expressed in the brain where it is involved in regulating the outgrowth of axons and dendrites and is regulated by the protein tyrosine kinase Fyn. It is translocated to the plasma membrane in adipocytes in response to insulin and may be involved in the regulation of insulin-stimulated glucose transport. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


:

Pssm-ID: 212769 [Multi-domain]  Cd Length: 54  Bit Score: 110.62  E-value: 4.79e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  299 AAYGVRRYQAQAPDEINIEVGDMISVIDMPSPAESIWWRGKKShlqkslYEVGFFPQSCV 358
Cdd:cd11835    1 AAHVIKRYTAQAPDELSLEVGDIVSVIDMPPPEESTWWRGKKG------FQVGFFPSECV 54
PX_domain super family cl02563
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
168-274 2.07e-16

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


The actual alignment was detected with superfamily member cd07278:

Pssm-ID: 470617  Cd Length: 114  Bit Score: 76.76  E-value: 2.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  168 SLGGDLPHSSLRSFSPESCWFIIRVCPQRCepFLIKRSFENMQLLDEMLHRCVYDRKISGLRNMEELAAELPSESDVEYA 247
Cdd:cd07278   10 VLSDDGSLKSYKNSGKELVYLVQVQCQGKS--WLVKRSYDDFRMLDKHLHQCIYDRKFSQLTELPEECIEKREQQNLHQV 87
                         90       100
                 ....*....|....*....|....*..
gi 19921564  248 VAKYLERFSKIASDSLTCGTILTWLQL 274
Cdd:cd07278   88 LSDYLKRLSSIAGNLLNCGPVLNWLEL 114
 
Name Accession Description Interval E-value
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
420-613 2.78e-109

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: 345.64  E-value: 2.78e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  420 RVFNCDLSEHLLNSGQDIPMVLRSCAEFIENYGVIDGIYRLSGITSNIQRLRRAFDEERVPDLGNPEMKQDIHAVSSLLK 499
Cdd:cd04384    1 RVFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGIVDGIYRLSGIASNIQRLRHEFDSEQIPDLTKDVYIQDIHSVSSLCK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  500 MYFRELPNPLCTYQLYDNFVEAIQvkADEADERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVW 579
Cdd:cd04384   81 LYFRELPNPLLTYQLYEKFSEAVS--AASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVW 158
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 19921564  580 APNLLRSPALESG---GVAALRGVGVQAVVTEYLIRN 613
Cdd:cd04384  159 APNLLRSKQIESAcfsGTAAFMEVRIQSVVVEFILNH 195
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
438-588 9.30e-57

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 193.53  E-value: 9.30e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564    438 PMVLRSCAEFIENYGV-IDGIYRLSGITSNIQRLRRAFDEERVPDLgnPEMKQDIHAVSSLLKMYFRELPNPLCTYQLYD 516
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLdTEGIFRVSGSASRIKELREAFDRGPDVDL--DLEEEDVHVVASLLKLFLRELPEPLLTFELYE 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921564    517 NFVEAIQVKADEadERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWAPNLLRSPA 588
Cdd:pfam00620   79 EFIEAAKLPDEE--ERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
435-614 5.41e-54

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


Pssm-ID: 214618  Cd Length: 174  Bit Score: 186.70  E-value: 5.41e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564     435 QDIPMVLRSCAEFIENYGV-IDGIYRLSGITSNIQRLRRAFDEErvPDLGNPEMKQDIHAVSSLLKMYFRELPNPLCTYQ 513
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLdTEGIYRVSGSKSRVKELRDAFDSG--PDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYE 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564     514 LYDNFVEAIQVkaDEADERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWAPNLLRSPALEsgg 593
Cdd:smart00324   79 LYEEFIEAAKL--EDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGE--- 153
                           170       180
                    ....*....|....*....|.
gi 19921564     594 VAALRGVGVQAVVTEYLIRNC 614
Cdd:smart00324  154 VASLKDIRHQNTVIEFLIENA 174
SH3_ARHGAP32_33 cd11835
Src homology 3 domain of Rho GTPase-activating proteins 32 and 33, and similar proteins; ...
299-358 4.79e-29

Src homology 3 domain of Rho GTPase-activating proteins 32 and 33, and similar proteins; Members of this family contain N-terminal PX and Src Homology 3 (SH3) domains, a central Rho GAP domain, and C-terminal extensions. RhoGAPs (or ARHGAPs) bind to Rho proteins and enhance the hydrolysis rates of bound GTP. ARHGAP32 is also called RICS, PX-RICS, p250GAP, or p200RhoGAP. It is a Rho GTPase-activating protein for Cdc42 and Rac1, and is implicated in the regulation of postsynaptic signaling and neurite outgrowth. PX-RICS, a variant of RICS that contain PX and SH3 domains, is the main isoform expressed during neural development. It is involved in neural functions including axon and dendrite extension, postnatal remodeling, and fine-tuning of neural circuits during early brain development. ARHGAP33, also called sorting nexin 26 or TCGAP (Tc10/CDC42 GTPase-activating protein), is widely expressed in the brain where it is involved in regulating the outgrowth of axons and dendrites and is regulated by the protein tyrosine kinase Fyn. It is translocated to the plasma membrane in adipocytes in response to insulin and may be involved in the regulation of insulin-stimulated glucose transport. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212769 [Multi-domain]  Cd Length: 54  Bit Score: 110.62  E-value: 4.79e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  299 AAYGVRRYQAQAPDEINIEVGDMISVIDMPSPAESIWWRGKKShlqkslYEVGFFPQSCV 358
Cdd:cd11835    1 AAHVIKRYTAQAPDELSLEVGDIVSVIDMPPPEESTWWRGKKG------FQVGFFPSECV 54
PX_RICS_like cd07278
The phosphoinositide binding Phox Homology domain of PX-RICS-like proteins; The PX domain is a ...
168-274 2.07e-16

The phosphoinositide binding Phox Homology domain of PX-RICS-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this family include PX-RICS, TCGAP (Tc10/Cdc42 GTPase-activating protein), and similar proteins. They contain N-terminal PX and Src Homology 3 (SH3) domains, a central Rho GAP domain, and C-terminal extensions. They act as Rho GTPase-activating proteins. PX-RICS is the main isoform expressed during neural development. It is involved in neural functions including axon and dendrite extension, postnatal remodeling, and fine-tuning of neural circuits during early brain development. The PX domain of PX-RICS specifically binds phosphatidylinositol 3-phosphate (PI3P), PI4P, and PI5P. TCGAP is widely expressed in the brain where it is involved in regulating the outgrowth of axons and dendrites and is regulated by the protein tyrosine kinase Fyn. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132811  Cd Length: 114  Bit Score: 76.76  E-value: 2.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  168 SLGGDLPHSSLRSFSPESCWFIIRVCPQRCepFLIKRSFENMQLLDEMLHRCVYDRKISGLRNMEELAAELPSESDVEYA 247
Cdd:cd07278   10 VLSDDGSLKSYKNSGKELVYLVQVQCQGKS--WLVKRSYDDFRMLDKHLHQCIYDRKFSQLTELPEECIEKREQQNLHQV 87
                         90       100
                 ....*....|....*....|....*..
gi 19921564  248 VAKYLERFSKIASDSLTCGTILTWLQL 274
Cdd:cd07278   88 LSDYLKRLSSIAGNLLNCGPVLNWLEL 114
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
306-359 1.34e-06

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 47.15  E-value: 1.34e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 19921564     306 YQAQAPDEINIEVGDMISVIDMPSPAesiWWRGKKSHLQkslyeVGFFPQSCVA 359
Cdd:smart00326   11 YTAQDPDELSFKKGDIITVLEKSDDG---WWKGRLGRGK-----EGLFPSNYVE 56
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
306-354 5.38e-05

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 42.19  E-value: 5.38e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 19921564    306 YQAQAPDEINIEVGDMISVIDMPspaESIWWRGKKSHLQkslyeVGFFP 354
Cdd:pfam00018    6 YTAQEPDELSFKKGDIIIVLEKS---EDGWWKGRNKGGK-----EGLIP 46
 
Name Accession Description Interval E-value
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
420-613 2.78e-109

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: 345.64  E-value: 2.78e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  420 RVFNCDLSEHLLNSGQDIPMVLRSCAEFIENYGVIDGIYRLSGITSNIQRLRRAFDEERVPDLGNPEMKQDIHAVSSLLK 499
Cdd:cd04384    1 RVFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGIVDGIYRLSGIASNIQRLRHEFDSEQIPDLTKDVYIQDIHSVSSLCK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  500 MYFRELPNPLCTYQLYDNFVEAIQvkADEADERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVW 579
Cdd:cd04384   81 LYFRELPNPLLTYQLYEKFSEAVS--AASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVW 158
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 19921564  580 APNLLRSPALESG---GVAALRGVGVQAVVTEYLIRN 613
Cdd:cd04384  159 APNLLRSKQIESAcfsGTAAFMEVRIQSVVVEFILNH 195
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
438-588 9.30e-57

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 193.53  E-value: 9.30e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564    438 PMVLRSCAEFIENYGV-IDGIYRLSGITSNIQRLRRAFDEERVPDLgnPEMKQDIHAVSSLLKMYFRELPNPLCTYQLYD 516
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLdTEGIFRVSGSASRIKELREAFDRGPDVDL--DLEEEDVHVVASLLKLFLRELPEPLLTFELYE 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921564    517 NFVEAIQVKADEadERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWAPNLLRSPA 588
Cdd:pfam00620   79 EFIEAAKLPDEE--ERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
435-614 5.41e-54

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


Pssm-ID: 214618  Cd Length: 174  Bit Score: 186.70  E-value: 5.41e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564     435 QDIPMVLRSCAEFIENYGV-IDGIYRLSGITSNIQRLRRAFDEErvPDLGNPEMKQDIHAVSSLLKMYFRELPNPLCTYQ 513
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLdTEGIYRVSGSKSRVKELRDAFDSG--PDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYE 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564     514 LYDNFVEAIQVkaDEADERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWAPNLLRSPALEsgg 593
Cdd:smart00324   79 LYEEFIEAAKL--EDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGE--- 153
                           170       180
                    ....*....|....*....|.
gi 19921564     594 VAALRGVGVQAVVTEYLIRNC 614
Cdd:smart00324  154 VASLKDIRHQNTVIEFLIENA 174
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
438-613 2.75e-51

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


Pssm-ID: 238090 [Multi-domain]  Cd Length: 169  Bit Score: 178.65  E-value: 2.75e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  438 PMVLRSCAEFIENYGV-IDGIYRLSGITSNIQRLRRAFDEERVPDlgnPEMKQDIHAVSSLLKMYFRELPNPLCTYQLYD 516
Cdd:cd00159    1 PLIIEKCIEYLEKNGLnTEGIFRVSGSASKIEELKKKFDRGEDID---DLEDYDVHDVASLLKLYLRELPEPLIPFELYD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  517 NFVEAIQVKADEadERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWAPNLLRSPALEsggVAA 596
Cdd:cd00159   78 EFIELAKIEDEE--ERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSD---DEL 152
                        170
                 ....*....|....*..
gi 19921564  597 LRGVGVQAVVTEYLIRN 613
Cdd:cd00159  153 LEDIKKLNEIVEFLIEN 169
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
422-618 8.85e-44

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: 157.95  E-value: 8.85e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  422 FNCDLSEHLLNSGQDIPMVLRSCAEFIENYGV-IDGIYRLSGITSNIQRLRRAFDEE--RVPDLGNPEMKQDIHAVSSLL 498
Cdd:cd04398    1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLnLEGIYRLSGNVSRVNKLKELFDKDplNVLLISPEDYESDIHSVASLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  499 KMYFRELPNPLCTYQLYDNFVEAIQVKadeaDERLR--LMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLA 576
Cdd:cd04398   81 KLFFRELPEPLLTKALSREFIEAAKIE----DESRRrdALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLA 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 19921564  577 IVWAPNLLRSPaleSGGVAAlrgVGVQAVVTEYLIRNCHNIF 618
Cdd:cd04398  157 IIWGPTLMNAA---PDNAAD---MSFQSRVIETLLDNAYQIF 192
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
422-618 1.80e-43

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: 157.29  E-value: 1.80e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  422 FNCDLSEHLLNSGQDIPMVLRSCAEFIENYGVI-DGIYRLSGITSNIQRLRRAFDEERVPDLGNPEMKQDIHAVSSLLKM 500
Cdd:cd04372    1 YGCDLTTLVKAHNTQRPMVVDMCIREIEARGLQsEGLYRVSGFAEEIEDVKMAFDRDGEKADISATVYPDINVITGALKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  501 YFRELPNPLCTYQLYDNFVEAIQVKadEADERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWA 580
Cdd:cd04372   81 YFRDLPIPVITYDTYPKFIDAAKIS--NPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFG 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 19921564  581 PNLLRSPalESGGVAALRGVGVQAVVTEYLIRNCHNIF 618
Cdd:cd04372  159 PTLMRPP--EDSALTTLNDMRYQILIVQLLITNEDVLF 194
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
422-596 5.97e-41

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: 149.85  E-value: 5.97e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  422 FNCDLSEHLLNSGQDIPMVLRSCAEFIENYGV-IDGIYRLSGITSNIQRLRRAFDEERVPDLgNPEMKQDIHAVSSLLKM 500
Cdd:cd04403    1 FGCHLEALCQRENSTVPKFVRLCIEAVEKRGLdVDGIYRVSGNLAVIQKLRFAVDHDEKLDL-DDSKWEDIHVITGALKL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  501 YFRELPNPLCTYQLYDNFVEAIqvKADEADERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWA 580
Cdd:cd04403   80 FFRELPEPLFPYSLFNDFVAAI--KLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFG 157
                        170
                 ....*....|....*.
gi 19921564  581 PNLLRsPALESGGVAA 596
Cdd:cd04403  158 PTLLR-PEQETGNIAV 172
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
420-619 1.49e-38

RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Nadrin-like proteins. Nadrin, also named Rich-1, has been shown to be involved in the regulation of Ca2+-dependent exocytosis in neurons and recently has been implicated in tight junction maintenance in mammalian epithelium. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239851  Cd Length: 203  Bit Score: 143.37  E-value: 1.49e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  420 RVFNCDLSEHLLNSGQDIPMVLRSCAEFIENYGVID-GIYRLSGITSNIQRLRRAFDEERVpDLGNPEMKQDIHAVSSLL 498
Cdd:cd04386    3 PVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEeGLFRVGGGASKLKRLKAALDAGTF-SLPLDEFYSDPHAVASAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  499 KMYFRELPNPLCTYQLYDNFVEAIQVKADeaDERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIV 578
Cdd:cd04386   82 KSYLRELPDPLLTYNLYEDWVQAANKPDE--DERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIV 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 19921564  579 WAPNLLRSPALESGGVAALrGVGVQAV-VTEYLIRNCHNIFD 619
Cdd:cd04386  160 LAPNLLWAKNEGSLAEMAA-GTSVHVVaIVELIISHADWFFP 200
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
437-587 1.73e-34

RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP21-like proteins. ArhGAP21 is a multi-domain protein, containing RhoGAP, PH and PDZ domains, and is believed to play a role in the organization of the cell-cell junction complex. It has been shown to function as a GAP of Cdc42 and RhoA, and to interact with alpha-catenin and Arf6. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239860  Cd Length: 196  Bit Score: 131.75  E-value: 1.73e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  437 IPMVLRSCAEFIENYGV-IDGIYRLSG----ITSNIQRLRRAFDEERVPDlgnpEMKQDIHAVSSLLKMYFRELPNPLCT 511
Cdd:cd04395   18 VPLIVEVCCNIVEARGLeTVGIYRVPGnnaaISALQEELNRGGFDIDLQD----PRWRDVNVVSSLLKSFFRKLPEPLFT 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19921564  512 YQLYDNFVEAiqVKADEADERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWAPNLLRSP 587
Cdd:cd04395   94 NELYPDFIEA--NRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIVFGPTLVRTS 167
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
433-614 3.38e-33

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: 3.38e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  433 SGQDIPMVLRSCAEFIENYGV-IDGIYRLSGITSNIQRLRRAFDEervpDLGNPEM---KQDIHAVSSLLKMYFRELPNP 508
Cdd:cd04385   11 TDNDIPVIVDKCIDFITQHGLmSEGIYRKNGKNSSVKKLLEAFRK----DARSVQLregEYTVHDVADVLKRFLRDLPDP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  509 LCTYQLYDNFVEAIQVKadEADERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWAPNLLRSPA 588
Cdd:cd04385   87 LLTSELHAEWIEAAELE--NKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLFQTDE 164
                        170       180
                 ....*....|....*....|....*..
gi 19921564  589 LESGGvaalrgvGVQAV-VTEYLIRNC 614
Cdd:cd04385  165 HSVGQ-------TSHEVkVIEDLIDNY 184
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
422-613 9.22e-33

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: 126.77  E-value: 9.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  422 FNCDLSEHLLNSGQDIPMVLRSCAEFIENYGV-IDGIYRLSGITSNIQRLRRAFDEERvpDLgnPEMKQ-DIHAVSSLLK 499
Cdd:cd04378    1 FGVDFSQVPRDFPDEVPFIIKKCTSEIENRALgVQGIYRVSGSKARVEKLCQAFENGK--DL--VELSElSPHDISSVLK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  500 MYFRELPNPLCTYQLYDNFV---EAIQvKADEADER----------LRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHG 566
Cdd:cd04378   77 LFLRQLPEPLILFRLYNDFIalaKEIQ-RDTEEDKApntpievnriIRKLKDLLRQLPASNYNTLQHLIAHLYRVAEQFE 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 19921564  567 RTGMTDKNLAIVWAPNLLRSPALESG-GVAALRGVGVQAVVTEYLIRN 613
Cdd:cd04378  156 ENKMSPNNLGIVFGPTLIRPRPGDADvSLSSLVDYGYQARLVEFLITN 203
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
439-613 9.61e-32

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: 124.04  E-value: 9.61e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  439 MVLRSCAEFIENYGVID-GIYRLSGITSNIQRLRRAFDEERVPDLGNPEMKQ---DIHAVSSLLKMYFRELPNPLCTYQL 514
Cdd:cd04374   30 KFVRKCIEAVETRGINEqGLYRVVGVNSKVQKLLSLGLDPKTSTPGDVDLDNsewEIKTITSALKTYLRNLPEPLMTYEL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  515 YDNFVEAiqVKADEADERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWAPNLLRsPALESggV 594
Cdd:cd04374  110 HNDFINA--AKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLR-PQEET--V 184
                        170
                 ....*....|....*....
gi 19921564  595 AALRGVGVQAVVTEYLIRN 613
Cdd:cd04374  185 AAIMDIKFQNIVVEILIEN 203
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
437-585 3.82e-31

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: 121.41  E-value: 3.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  437 IPMVLRSCAEFIENYGV-IDGIYRLSGITSNIQRLRRAFDEERVPDLGnpEMKQDIHAVSSLLKMYFRELPNPLCTYQLY 515
Cdd:cd04373   15 IPIFLEKCVEFIEATGLeTEGIYRVSGNKTHLDSLQKQFDQDHNLDLV--SKDFTVNAVAGALKSFFSELPDPLIPYSMH 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  516 DNFVEAIQVKADEadERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWAPNLLR 585
Cdd:cd04373   93 LELVEAAKINDRE--QRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLMR 160
SH3_ARHGAP32_33 cd11835
Src homology 3 domain of Rho GTPase-activating proteins 32 and 33, and similar proteins; ...
299-358 4.79e-29

Src homology 3 domain of Rho GTPase-activating proteins 32 and 33, and similar proteins; Members of this family contain N-terminal PX and Src Homology 3 (SH3) domains, a central Rho GAP domain, and C-terminal extensions. RhoGAPs (or ARHGAPs) bind to Rho proteins and enhance the hydrolysis rates of bound GTP. ARHGAP32 is also called RICS, PX-RICS, p250GAP, or p200RhoGAP. It is a Rho GTPase-activating protein for Cdc42 and Rac1, and is implicated in the regulation of postsynaptic signaling and neurite outgrowth. PX-RICS, a variant of RICS that contain PX and SH3 domains, is the main isoform expressed during neural development. It is involved in neural functions including axon and dendrite extension, postnatal remodeling, and fine-tuning of neural circuits during early brain development. ARHGAP33, also called sorting nexin 26 or TCGAP (Tc10/CDC42 GTPase-activating protein), is widely expressed in the brain where it is involved in regulating the outgrowth of axons and dendrites and is regulated by the protein tyrosine kinase Fyn. It is translocated to the plasma membrane in adipocytes in response to insulin and may be involved in the regulation of insulin-stimulated glucose transport. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212769 [Multi-domain]  Cd Length: 54  Bit Score: 110.62  E-value: 4.79e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  299 AAYGVRRYQAQAPDEINIEVGDMISVIDMPSPAESIWWRGKKShlqkslYEVGFFPQSCV 358
Cdd:cd11835    1 AAHVIKRYTAQAPDELSLEVGDIVSVIDMPPPEESTWWRGKKG------FQVGFFPSECV 54
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
430-611 5.52e-29

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: 115.23  E-value: 5.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  430 LLNSGQDIPMVLRSCAEFIENYGV-IDGIYRLSGITSNIQRLRRAFDEErvPDLGNPEmKQDIHAVSSLLKMYFRELPNP 508
Cdd:cd04377    8 LTSEDRSVPLVLEKLLEHIEMHGLyTEGIYRKSGSANKIKELRQGLDTD--PDSVNLE-DYPIHVITSVLKQWLRELPEP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  509 LCTYQLYDNFVEAIQVKadEADERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWAPNLLR--- 585
Cdd:cd04377   85 LMTFELYENFLRAMELE--EKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCILRcpd 162
                        170       180
                 ....*....|....*....|....*..
gi 19921564  586 -SPALESggvaaLRGVGVQAVVTEYLI 611
Cdd:cd04377  163 tADPLQS-----LQDVSKTTTCVETLI 184
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
426-583 7.91e-29

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: 115.15  E-value: 7.91e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  426 LSEHLLNsGQDIPMVLRSCAEFIENYGVI--DGIYRLSGITSNIQRLRRAFDEERVPDLGNPEMKQDIHAVSSLLKMYFR 503
Cdd:cd04400   12 LSSHKYN-GRDLPSVVYRCIEYLDKNRAIyeEGIFRLSGSASVIKQLKERFNTEYDVDLFSSSLYPDVHTVAGLLKLYLR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  504 ELPNPLCTYQLYDNFVEAIQVKADEAdERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWAPNL 583
Cdd:cd04400   91 ELPTLILGGELHNDFKRLVEENHDRS-QRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLRNVCIVFSPTL 169
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
422-613 5.29e-28

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: 112.99  E-value: 5.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  422 FNCDLSEHLLNSGQDIPMVLRSCAEFIENYGV-IDGIYRLSGITSNIQRLRRAFDEER-VPDLGNpemkQDIHAVSSLLK 499
Cdd:cd04408    1 FGVDFSQLPRDFPEEVPFVVVRCTAEIENRALgVQGIYRISGSKARVEKLCQAFENGRdLVDLSG----HSPHDITSVLK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  500 MYFRELPNPLCTYQLYDNFV-------EAIQVKADE---ADERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTG 569
Cdd:cd04408   77 HFLKELPEPVLPFQLYDDFIalakelqRDSEKAAESpsiVENIIRSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNK 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 19921564  570 MTDKNLAIVWAPNLLRSPALESGGVAALRGVGVQAVVTEYLIRN 613
Cdd:cd04408  157 MSPNNLGIVFGPTLLRPLVGGDVSMICLLDTGYQAQLVEFLISN 200
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
428-618 2.64e-27

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: 110.89  E-value: 2.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  428 EHLL--NSGQD-IPMVLRSCAEFIENYGV-IDGIYRLSGITSNIQRLrrafdEERVpDLGNPEMKQ---DIHAVSSLLKM 500
Cdd:cd04404   11 QFLKekNPEQEpIPPVVRETVEYLQAHALtTEGIFRRSANTQVVKEV-----QQKY-NMGEPVDFDqyeDVHLPAVILKT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  501 YFRELPNPLCTYQLYDNFVEAIQVkadEADERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWA 580
Cdd:cd04404   85 FLRELPEPLLTFDLYDDIVGFLNV---DKEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFG 161
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 19921564  581 PNLLRSPAlesgGVAALRGVGVQAVVTEYLIRNCHNIF 618
Cdd:cd04404  162 PNLLWAKD----ASMSLSAINPINTFTKFLLDHQDEIF 195
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
422-613 2.66e-27

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: 110.79  E-value: 2.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  422 FNCDLSEHLLNSGQDIPMVLRSCAEFIENYGVID-GIYRLSGITSNIQRLRRAFDEERvPDLGNPEMKQDIHAVSSLLKM 500
Cdd:cd04387    1 FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEvGIYRISGVATDIQALKAAFDTNN-KDVSVMLSEMDVNAIAGTLKL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  501 YFRELPNPLCTYQLYDNFVEAIQVKADEADErlRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWA 580
Cdd:cd04387   80 YFRELPEPLFTDELYPNFAEGIALSDPVAKE--SCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFG 157
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 19921564  581 PNLLRSPALESGGVAALRG------VGVQAVVTEYLIRN 613
Cdd:cd04387  158 PTLLRPSEKESKIPTNTMTdswsleVMSQVQVLLYFLQL 196
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
420-587 1.24e-26

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: 108.66  E-value: 1.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  420 RVFNCDLSEHLLNSGQDIPMVLRSCAEFIENYGVI-DGIYRLSGITSNIQRLRRAFdeERVPD-LGNPEMKQDIHAVSSL 497
Cdd:cd04383    1 KLFNGSLEEYIQDSGQAIPLVVESCIRFINLYGLQhQGIFRVSGSQVEVNDIKNAF--ERGEDpLADDQNDHDINSVAGV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  498 LKMYFRELPNPLCTYQLYDNFVEAIQVkaDEADERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAI 577
Cdd:cd04383   79 LKLYFRGLENPLFPKERFEDLMSCVKL--ENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAI 156
                        170
                 ....*....|
gi 19921564  578 VWAPNLLRSP 587
Cdd:cd04383  157 CFGPTLMPVP 166
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
437-618 6.01e-25

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: 104.06  E-value: 6.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  437 IPMVLRSCAEFIENYGVID-GIYRLSGITSNIQRLRRAFDEERVPDLgnpEMKQDIHAVSSLLKMYFRELPNPLCTYQLY 515
Cdd:cd04390   22 VPILVEQCVDFIREHGLKEeGLFRLPGQANLVKQLQDAFDAGERPSF---DSDTDVHTVASLLKLYLRELPEPVIPWAQY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  516 DNFVEAIQ-VKADEADERLRLMKEtVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWAPNLLRsPALESgGV 594
Cdd:cd04390   99 EDFLSCAQlLSKDEEKGLGELMKQ-VSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLATVFGPNILR-PKVED-PA 175
                        170       180
                 ....*....|....*....|....*
gi 19921564  595 AALRG-VGVQAVVTeYLIRNCHNIF 618
Cdd:cd04390  176 TIMEGtPQIQQLMT-VMISKHEPLF 199
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
437-618 9.66e-25

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: 104.06  E-value: 9.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  437 IPMVLRSCAEFIENYGVID-GIYRLSGITSNIQRLRRAFDeerVPDLGNPEMKQDIHAVSSLLKMYFRELPNPLCTYQLY 515
Cdd:cd04376    9 VPRLVESCCQHLEKHGLQTvGIFRVGSSKKRVRQLREEFD---RGIDVVLDENHSVHDVAALLKEFFRDMPDPLLPRELY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  516 DNFVEAIQVKADEADERLRLMketVLKLPPPHYRTLKYLAEHLYKVSQH----HGRTG-------MTDKNLAIVWAPNLL 584
Cdd:cd04376   86 TAFIGTALLEPDEQLEALQLL---IYLLPPCNCDTLHRLLKFLHTVAEHaadsIDEDGqevsgnkMTSLNLATIFGPNLL 162
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 19921564  585 R--SPALESGGVAALRGVGVQAV--VTEYLIRNCHNIF 618
Cdd:cd04376  163 HkqKSGEREFVQASLRIEESTAIinVVQTMIDNYEELF 200
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
420-583 3.06e-24

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: 101.77  E-value: 3.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  420 RVFNCDLSEhLLNSGQ---DIPMVLRSCAEFIENYGVI-DGIYRLSGITSNIQRLRRAFDEERVPDLGNPEmkqDIHAVS 495
Cdd:cd04393    1 KVFGVPLQE-LQQAGQpenGVPAVVRHIVEYLEQHGLEqEGLFRVNGNAETVEWLRQRLDSGEEVDLSKEA---DVCSAA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  496 SLLKMYFRELPNPLCTYQLYDNFVEAIQvKADEADERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNL 575
Cdd:cd04393   77 SLLRLFLQELPEGLIPASLQIRLMQLYQ-DYNGEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENL 155

                 ....*...
gi 19921564  576 AIVWAPNL 583
Cdd:cd04393  156 AAVFGPDV 163
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
422-611 1.38e-23

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: 100.65  E-value: 1.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  422 FNCDLSEHLLNSGQDIPMVLRSCAEFIENYGV-IDGIYRLSGITSNIQRLRRAFdeERVPDLgnPEMKQ-DIHAVSSLLK 499
Cdd:cd04409    1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALcLKGIYRVNGAKSRVEKLCQAF--ENGKDL--VELSElSPHDISNVLK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  500 MYFRELPNPLCTYQLYDNFV----------EAIQVKADEADERLRL----------MKETVLKLPPPHYRTLKYLAEHLY 559
Cdd:cd04409   77 LYLRQLPEPLILFRLYNEFIglakesqhvnETQEAKKNSDKKWPNMctelnrillkSKDLLRQLPAPNYNTLQFLIVHLH 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19921564  560 KVSQHHGRTGMTDKNLAIVWAPNLLRSPALESG-GVAALRGVGVQAVVTEYLI 611
Cdd:cd04409  157 RVSEQAEENKMSASNLGIIFGPTLIRPRPTDATvSLSSLVDYPHQARLVELLI 209
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
437-610 1.41e-22

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: 97.36  E-value: 1.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  437 IPMVLRSCAEFIENYGVID-GIYRLSGITSNIQRLRRAF-DEERVPDLGnpemKQDIHAVSSLLKMYFRELPNPLCTYQL 514
Cdd:cd04382   17 IPALIVHCVNEIEARGLTEeGLYRVSGSEREVKALKEKFlRGKTVPNLS----KVDIHVICGCLKDFLRSLKEPLITFAL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  515 YDNFVEAIQVkADEADERLrLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHgRTGMTDKNLAIVWAPNLLRSPALESGGV 594
Cdd:cd04382   93 WKEFMEAAEI-LDEDNSRA-ALYQAISELPQPNRDTLAFLILHLQRVAQSP-ECKMDINNLARVFGPTIVGYSVPNPDPM 169
                        170
                 ....*....|....*.
gi 19921564  595 AALRGVGVQAVVTEYL 610
Cdd:cd04382  170 TILQDTVRQPRVVERL 185
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
434-583 1.61e-22

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: 96.74  E-value: 1.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  434 GQDIPMVLRSCAEFIENYGV-IDGIYRLSGITSNIQRLRRAFDEERVPDLGNpemkQDIHAVSSLLKMYFRELPNPLCTY 512
Cdd:cd04381   17 GIDLPLVFRECIDYVEKHGMkCEGIYKVSGIKSKVDELKAAYNRRESPNLEE----YEPPTVASLLKQYLRELPEPLLTK 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19921564  513 QLYDNFVEA--IQVKADEADERLRLMKEtvlkLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWAPNL 583
Cdd:cd04381   93 ELMPRFEEAcgRPTEAEREQELQRLLKE----LPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVLSPTV 161
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
430-612 3.87e-22

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


Pssm-ID: 239872 [Multi-domain]  Cd Length: 186  Bit Score: 95.83  E-value: 3.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  430 LLNSGQDIPMVLRSCAEFIENYGV-IDGIYRLSGITSNIQRLRRAF--DEERVPDLGNPemkqdIHAVSSLLKMYFRELP 506
Cdd:cd04407    8 LTSNKTSVPIVLEKLLEHVEMHGLyTEGIYRKSGSANRMKELHQLLqaDPENVKLENYP-----IHAITGLLKQWLRELP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  507 NPLCTYQLYDNFVEAIQVKadEADERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWAPNLLRS 586
Cdd:cd04407   83 EPLMTFAQYNDFLRAVELP--EKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRC 160
                        170       180
                 ....*....|....*....|....*.
gi 19921564  587 PAlESGGVAALRGVGVQAVVTEYLIR 612
Cdd:cd04407  161 PD-SSDPLTSMKDVAKTTTCVEMLIK 185
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
455-618 6.11e-21

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: 92.36  E-value: 6.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  455 DGIYRLSGITSNIQRLRRAFDEERVPDLGnpemKQDIHAVSSLLKMYFRELPNPLCTYQLYDNFVEAIQVKADEadERLR 534
Cdd:cd04402   34 EGIFRRSANAKACKELKEKLNSGVEVDLK----AEPVLLLASVLKDFLRNIPGSLLSSDLYEEWMSALDQENEE--EKIA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  535 LMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWAPNLLRSPALESGGVAALRGVgvqAVVTEYLIRNC 614
Cdd:cd04402  108 ELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLWPPASSELQNEDLKKV---TSLVQFLIENC 184

                 ....
gi 19921564  615 HNIF 618
Cdd:cd04402  185 QEIF 188
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
422-587 2.61e-19

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: 87.75  E-value: 2.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  422 FNCDLSEhLLNSGQDIPMVLRSCAEFIENYGV-IDGIYRLSGITSNIQRLRRAFDEervpDLGNPEMKQ-DIHAVSSLLK 499
Cdd:cd04406    1 FGVELSR-LTSEDRSVPLVVEKLINYIEMHGLyTEGIYRKSGSTNKIKELRQGLDT----DANSVNLDDyNIHVIASVFK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  500 MYFRELPNPLCTYQLYDNFVEAIQVKadEADERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVW 579
Cdd:cd04406   76 QWLRDLPNPLMTFELYEEFLRAMGLQ--ERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVF 153

                 ....*...
gi 19921564  580 APNLLRSP 587
Cdd:cd04406  154 APCILRCP 161
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
421-583 2.69e-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: 88.63  E-value: 2.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  421 VFNCDLSEHLLNSGQDIPMVLRSCAEFIENYgVID--GIYRLSGITSNIQRLRRAFdeERVPDLGNPEmKQDIHAVSSLL 498
Cdd:cd04375    4 VFGVPLLVNLQRTGQPLPRSIQQAMRWLRNN-ALDqvGLFRKSGVKSRIQKLRSMI--ESSTDNVNYD-GQQAYDVADML 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  499 KMYFRELPNPLCTYQLYDNFVEAIQVKADEadERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIV 578
Cdd:cd04375   80 KQYFRDLPEPLLTNKLSETFIAIFQYVPKE--QRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVC 157

                 ....*
gi 19921564  579 WAPNL 583
Cdd:cd04375  158 LAPSL 162
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
436-584 2.02e-18

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: 85.60  E-value: 2.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  436 DIPMVLRSCAEFIENYGV-IDGIYRLSGITSNIQRLRRAFDEERVPDLGNPEMKQDIHAVSSLLKMYFRELPNPLCTYQL 514
Cdd:cd04379   17 DVPIVLQKCVQEIERRGLdVIGLYRLCGSAAKKKELRDAFERNSAAVELSEELYPDINVITGVLKDYLRELPEPLITPQL 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19921564  515 YDNFVEAIQVKADEADERLRLMKETVLKLPPPHYR-TLKYLAEHLYKVSQHHGRTGMTDKNLAIVWAPNLL 584
Cdd:cd04379   97 YEMVLEALAVALPNDVQTNTHLTLSIIDCLPLSAKaTLLLLLDHLSLVLSNSERNKMTPQNLAVCFGPVLM 167
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
422-617 4.20e-18

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: 4.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  422 FNCDLSEHLLNSGqDIPMVLRSCAEFIENYGVIDGIYRLSGITSNIQRLRRAFDEErvpdlGNPEMKQDIHAVSSLLKMY 501
Cdd:cd04394    6 LHSLPHSTVPEYG-NVPKFLVDACTFLLDHLSTEGLFRKSGSVVRQKELKAKLEGG-----EACLSSALPCDVAGLLKQF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  502 FRELPNPLCTYQLYDNFVEAIQVKADEadERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWAP 581
Cdd:cd04394   80 FRELPEPLLPYDLHEALLKAQELPTDE--ERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVIFAP 157
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 19921564  582 NLLRSP-ALESGGVAALRGVGVQAVVTEYLIRNCHNI 617
Cdd:cd04394  158 NLFQSEeGGEKMSSSTEKRLRLQAAVVQTLIDNASNI 194
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
421-613 3.73e-17

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: 82.39  E-value: 3.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  421 VFNCDLSEHLLNS-----GQDIPMVLRSCAEFIENYGV-IDGIYRLSGITSNIQRLRRAFDEERVPDLGNPE-MKQdiHA 493
Cdd:cd04391    1 LFGVPLSTLLERDqkkvpGSKVPLIFQKLINKLEERGLeTEGILRIPGSAQRVKFLCQELEAKFYEGTFLWDqVKQ--HD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  494 VSSLLKMYFRELPNPLCTYQLYDNF--VEAI-----QVKAdeaderLRLMketVLKLPPPHYRTLKYLAEHLYKVSQHHG 566
Cdd:cd04391   79 AASLLKLFIRELPQPLLTVEYLPAFysVQGLpskkdQLQA------LNLL---VLLLPEANRDTLKALLEFLQKVVDHEE 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 19921564  567 RTGMTDKNLAIVWAPNLLRSPALESGGVAAL----RGVGVQAVVTEYLIRN 613
Cdd:cd04391  150 KNKMNLWNVAMIMAPNLFPPRGKHSKDNESLqeevNMAAGCANIMRLLIRY 200
PX_RICS_like cd07278
The phosphoinositide binding Phox Homology domain of PX-RICS-like proteins; The PX domain is a ...
168-274 2.07e-16

The phosphoinositide binding Phox Homology domain of PX-RICS-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this family include PX-RICS, TCGAP (Tc10/Cdc42 GTPase-activating protein), and similar proteins. They contain N-terminal PX and Src Homology 3 (SH3) domains, a central Rho GAP domain, and C-terminal extensions. They act as Rho GTPase-activating proteins. PX-RICS is the main isoform expressed during neural development. It is involved in neural functions including axon and dendrite extension, postnatal remodeling, and fine-tuning of neural circuits during early brain development. The PX domain of PX-RICS specifically binds phosphatidylinositol 3-phosphate (PI3P), PI4P, and PI5P. TCGAP is widely expressed in the brain where it is involved in regulating the outgrowth of axons and dendrites and is regulated by the protein tyrosine kinase Fyn. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132811  Cd Length: 114  Bit Score: 76.76  E-value: 2.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  168 SLGGDLPHSSLRSFSPESCWFIIRVCPQRCepFLIKRSFENMQLLDEMLHRCVYDRKISGLRNMEELAAELPSESDVEYA 247
Cdd:cd07278   10 VLSDDGSLKSYKNSGKELVYLVQVQCQGKS--WLVKRSYDDFRMLDKHLHQCIYDRKFSQLTELPEECIEKREQQNLHQV 87
                         90       100
                 ....*....|....*....|....*..
gi 19921564  248 VAKYLERFSKIASDSLTCGTILTWLQL 274
Cdd:cd07278   88 LSDYLKRLSSIAGNLLNCGPVLNWLEL 114
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
454-613 1.53e-15

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: 77.41  E-value: 1.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  454 IDGIYRLSGitsNIQRLRRAFDE-----ERVPDLGnpemKQDIHAVSSLLKMYFRELPNPLCTYQLYDNFVEAiqVKADE 528
Cdd:cd04397   45 VEGVFRKNG---NIRRLKELTEEidknpTEVPDLS----KENPVQLAALLKKFLRELPDPLLTFKLYRLWISS--QKIED 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  529 ADERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHH---GRTG--MTDKNLAIVWAPNLLRSPALESGGVAALRGvGVQ 603
Cdd:cd04397  116 EEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSFShidEETGskMDIHNLATVITPNILYSKTDNPNTGDEYFL-AIE 194
                        170
                 ....*....|
gi 19921564  604 AVvtEYLIRN 613
Cdd:cd04397  195 AV--NYLIEN 202
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
422-585 1.04e-14

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: 74.35  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  422 FNCDLSEhLLNSGQD------IPMVLRSCAEFIENYGV--IDGIYRLSGITSNIQRLRRAFDEERVPDLGnpemKQDIHA 493
Cdd:cd04389    1 FGSSLEE-IMDRQKEkypelkLPWILTFLSEKVLALGGfqTEGIFRVPGDIDEVNELKLRVDQWDYPLSG----LEDPHV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  494 VSSLLKMYFRELPNPLCTYQLYDNFVEAIQvKADEAderlrlmKETVLKLPPPHYRTLKYLAEHLYKVSQHH--GRTGMT 571
Cdd:cd04389   76 PASLLKLWLRELEEPLIPDALYQQCISASE-DPDKA-------VEIVQKLPIINRLVLCYLINFLQVFAQPEnvAHTKMD 147
                        170
                 ....*....|....
gi 19921564  572 DKNLAIVWAPNLLR 585
Cdd:cd04389  148 VSNLAMVFAPNILR 161
PX_RICS cd07298
The phosphoinositide binding Phox Homology domain of PX-RICS; The PX domain is a ...
143-274 6.71e-14

The phosphoinositide binding Phox Homology domain of PX-RICS; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. RICS is a Rho GTPase-activating protein for cdc42 and Rac1. It is implicated in the regulation of postsynaptic signaling and neurite outgrowth. An N-terminal splicing variant of RICS containing additional PX and Src Homology 3 (SH3) domains, also called PX-RICS, is the main isoform expressed during neural development. PX-RICS is involved in neural functions including axon and dendrite extension, postnatal remodeling, and fine-tuning of neural circuits during early brain development. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. The PX domain of PX-RICS specifically binds phosphatidylinositol 3-phosphate (PI3P), PI4P, and PI5P.


Pssm-ID: 132831  Cd Length: 115  Bit Score: 69.62  E-value: 6.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  143 VQLGPLSVQLLDDKSEHMGSSIASQSLggdlphsslrsfspescWFIIRVCPQRcEPFLIKRSFENMQLLDEMLHRCVYD 222
Cdd:cd07298    2 VDFGSIQLSLGEEQNEVMRNGCESKEL-----------------VYLVQIACQG-RSWIVKRSYEDFRVLDKHLHLCIYD 63
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19921564  223 RKISGLRNMEELAAELPSESDVEYAVAKYLERFSKIASDSLTCGTILTWLQL 274
Cdd:cd07298   64 RRFSQLPELPRSDSLKDSPESVTQMLMAYLSRLSAIAGNKINCGPALTWMEI 115
PX_TCGAP cd07299
The phosphoinositide binding Phox Homology domain of Tc10/Cdc42 GTPase-activating protein; The ...
143-274 3.80e-12

The phosphoinositide binding Phox Homology domain of Tc10/Cdc42 GTPase-activating protein; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. TCGAP (Tc10/Cdc42 GTPase-activating protein) contains N-terminal PX and Src Homology 3 (SH3) domains, a central Rho GAP domain, and C-terminal proline-rich regions. It is widely expressed in the brain where it is involved in regulating the outgrowth of axons and dendrites and is regulated by the protein tyrosine kinase Fyn. It interacts with cdc42 and TC10beta through its GAP domain and with phosphatidylinositol-(4,5)-bisphosphate [PI(4,5)P2] through its PX domain. It is translocated to the plasma membrane in adipocytes in response to insulin and may be involved in the regulation of insulin-stimulated glucose transport. TCGAP has also been named sorting nexins 26 (SNX26). SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. It is unknown whether TCGAP also functions as a SNX.


Pssm-ID: 132832  Cd Length: 113  Bit Score: 64.49  E-value: 3.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  143 VQLGPLSVQLLDDKSEHMGSSiasqslGGDLPhsslrsfspescwFIIRV-CPQRCEPFLikRSFENMQLLDEMLHRCVY 221
Cdd:cd07299    2 VDFGSIQLQLSNERSDWTSSS------EKDLV-------------FLVQVtCQGRSWMVL--RSYEDFRTLDAHLHRCIF 60
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  222 DRKISGLrnmeelaAELPSESDVEYA-------VAKYLERFSKIASDSLTCGTILTWLQL 274
Cdd:cd07299   61 DRRFSQL-------LELPPLCEIGDRlqiltplLSEYLNRLTGIVDSNLNCGPVLTWMEI 113
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
437-590 3.82e-11

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: 64.74  E-value: 3.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  437 IPMVLRSCAEFI-ENYGVIDGIYRLSGITSNIQRLRRAFDEErvPDLGNP--EMKQDIHAVSSLLKMYFRELPNPLCTYQ 513
Cdd:cd04396   32 IPVVVAKCGVYLkENATEVEGIFRVAGSSKRIRELQLIFSTP--PDYGKSfdWDGYTVHDAASVLRRYLNNLPEPLVPLD 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  514 LYDNF----------VEAIQVKADEA-----DERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIV 578
Cdd:cd04396  110 LYEEFrnplrkrpriLQYMKGRINEPlntdiDQAIKEYRDLITRLPNLNRQLLLYLLDLLAVFARNSDKNLMTASNLAAI 189
                        170
                 ....*....|..
gi 19921564  579 WAPNLLRSPALE 590
Cdd:cd04396  190 FQPGILSHPDHE 201
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
446-584 2.25e-10

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: 62.09  E-value: 2.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  446 EFIENYGVIDGIYRLSGITSNIQRLRRAFDEERVPDLGNPEMKqdIHAVSSLLKMYFRELPNPLCTY----------QLY 515
Cdd:cd04392   18 EYLEKNLRVEGLFRKPGNSARQQELRDLLNSGTDLDLESGGFH--AHDCATVLKGFLGELPEPLLTHahypahlqiaDLC 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19921564  516 DNFVEAIQVKADEADERLRLMKETVLKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWAPNLL 584
Cdd:cd04392   96 QFDEKGNKTSAPDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLI 164
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
425-588 1.13e-08

RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in the p85 isoforms of the regulatory subunit of the class IA PI3K (phosphatidylinositol 3'-kinase). This domain is also called Bcr (breakpoint cluster region protein) homology (BH) domain. Class IA PI3Ks are heterodimers, containing a regulatory subunit (p85) and a catalytic subunit (p110) and are activated by growth factor receptor tyrosine kinases (RTKs); this activation is mediated by the p85 subunit. p85 isoforms, alpha and beta, contain a C-terminal p110-binding domain flanked by two SH2 domains, an N-terminal SH3 domain, and a RhoGAP domain flanked by two proline-rich regions. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239853  Cd Length: 200  Bit Score: 57.19  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  425 DLSEHLlnSGQDI-PMVLRSCAEFIENYGVIDGIYRLSGITSNIQRLRRAFDEervpDLGNPEMKQ-DIHAVSSLLKMYF 502
Cdd:cd04388    4 DLTEQF--SPPDVaPPLLIKLVEAIEKKGLESSTLYRTQSSSSLTELRQILDC----DAASVDLEQfDVAALADALKRYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  503 RELPNPLCTYQLYDNFVEAIQ--VKADEADERLRLMKETVlKLPPPHYRTLKYLAEHLYKVSQHHGRTGMTDKNLAIVWA 580
Cdd:cd04388   78 LDLPNPVIPAPVYSEMISRAQevQSSDEYAQLLRKLIRSP-NLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFS 156

                 ....*...
gi 19921564  581 PNLLRSPA 588
Cdd:cd04388  157 PLLFRFQP 164
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
306-359 1.34e-06

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 47.15  E-value: 1.34e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 19921564     306 YQAQAPDEINIEVGDMISVIDMPSPAesiWWRGKKSHLQkslyeVGFFPQSCVA 359
Cdd:smart00326   11 YTAQDPDELSFKKGDIITVLEKSDDG---WWKGRLGRGK-----EGLFPSNYVE 56
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
306-357 2.07e-06

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


Pssm-ID: 212690 [Multi-domain]  Cd Length: 51  Bit Score: 46.30  E-value: 2.07e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19921564  306 YQAQAPDEINIEVGDMISVIDMPSPAesiWWRGKKSHLQKslyevGFFPQSC 357
Cdd:cd00174    8 YEAQDDDELSFKKGDIITVLEKDDDG---WWEGELNGGRE-----GLFPANY 51
SH3_GRAP_C cd11951
C-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor ...
306-358 2.45e-05

C-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor protein that is highly expressed in lymphoid tissues. It acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. It has been identified as a regulator of TGFbeta signaling in diabetic kidney tubules and may have a role in the pathogenesis of the disease. GRAP contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domains (SH3c) of the related proteins, GRB2 and GRAP2, have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212884  Cd Length: 53  Bit Score: 43.25  E-value: 2.45e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19921564  306 YQAQAPDEINIEVGDMISVIDMPSPAesiWWRGKKSHlqkslyEVGFFPQSCV 358
Cdd:cd11951    8 FSAEDPSQLSFRRGDIIEVLDCPDPN---WWRGRISG------RVGFFPRNYV 51
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
306-354 5.38e-05

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 42.19  E-value: 5.38e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 19921564    306 YQAQAPDEINIEVGDMISVIDMPspaESIWWRGKKSHLQkslyeVGFFP 354
Cdd:pfam00018    6 YTAQEPDELSFKKGDIIIVLEKS---EDGWWKGRNKGGK-----EGLIP 46
SH3_OSTF1 cd11772
Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or ...
306-339 5.97e-05

Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or SH3P2, is a signaling protein containing SH3 and ankyrin-repeat domains. It acts through a Src-related pathway to enhance the formation of osteoclasts and bone resorption. It also acts as a negative regulator of cell motility. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212706 [Multi-domain]  Cd Length: 53  Bit Score: 42.29  E-value: 5.97e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 19921564  306 YQAQAPDEINIEVGDMISVIDMPSPAesiWWRGK 339
Cdd:cd11772    8 YEAQHPDELSFEEGDLLYISDKSDPN---WWKAT 38
SH3_ASPP cd11807
Src homology 3 domain of Apoptosis Stimulating of p53 proteins (ASPP); The ASPP family of ...
298-336 7.86e-05

Src homology 3 domain of Apoptosis Stimulating of p53 proteins (ASPP); The ASPP family of proteins bind to important regulators of apoptosis (p53, Bcl-2, and RelA) and cell growth (APCL, PP1). They share similarity at their C-termini, where they harbor a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain. Vertebrates contain three members of the family: ASPP1, ASPP2, and iASPP. ASPP1 and ASPP2 activate the apoptotic function of the p53 family of tumor suppressors (p53, p63, and p73), while iASPP is an oncoprotein that specifically inhibits p53-induced apoptosis. The expression of ASPP proteins is altered in tumors; ASPP1 and ASPP2 are downregulated whereas iASPP is upregulated is some cancer types. ASPP proteins also bind and regulate protein phosphatase 1 (PP1), and this binding is competitive with p53 binding. The SH3 domain and the ANK repeats of ASPP contribute to the p53 binding site; they bind to the DNA binding domain of p53. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212741 [Multi-domain]  Cd Length: 57  Bit Score: 41.98  E-value: 7.86e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 19921564  298 GAAYGVRRYQAQAPDEINIEVGDMISVIDMPSPAESIWW 336
Cdd:cd11807    1 GVVYALFDYEAENGDELSFREGDELTVLRKGDDDETEWW 39
SH3_Nck_2 cd11766
Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin ...
305-354 8.55e-05

Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The second SH3 domain of Nck appears to prefer ligands containing the APxxPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212700 [Multi-domain]  Cd Length: 53  Bit Score: 41.87  E-value: 8.55e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 19921564  305 RYQAQAPDEINIEVGDMISVIDMPSPAesiWWRGKKSHlqkslyEVGFFP 354
Cdd:cd11766    7 NYEAQREDELSLRKGDRVLVLEKSSDG---WWRGECNG------QVGWFP 47
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
470-560 8.57e-05

RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD2-like proteins. Yeast Rgd2 is a GAP protein for Cdc42 and Rho5. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239864  Cd Length: 212  Bit Score: 45.79  E-value: 8.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  470 LRRAFDEERVPDLGNPEMKQ-DIHAVSSLLKMYFRELPNPLCTYQLYDNFVEAIQ----VKADEADERLRLMKETVLKLP 544
Cdd:cd04399   56 LRNLLNKPKKPDKEVIILKKfEPSTVASVLKLYLLELPDSLIPHDIYDLIRSLYSayppSQEDSDTARIQGLQSTLSQLP 135
                         90
                 ....*....|....*.
gi 19921564  545 PPHYRTLKYLAEHLYK 560
Cdd:cd04399  136 KSHIATLDAIITHFYR 151
SH3_iASPP cd11952
Src Homology 3 (SH3) domain of Inhibitor of ASPP protein (iASPP); iASPP, also called ...
298-336 1.84e-04

Src Homology 3 (SH3) domain of Inhibitor of ASPP protein (iASPP); iASPP, also called RelA-associated inhibitor (RAI), is an oncoprotein that inhibits the apoptotic transactivation potential of p53. It is upregulated in human breast cancers expressing wild-type p53, in acute leukemias regardless of the p53 mutation status, as well as in ovarian cancer where it is associated with poor patient outcome and chemoresistance. iASPP is also a binding partner and negative regulator of p65RelA, which promotes cell proliferation and inhibits apoptosis; p65RelA has the opposite effect on cell growth compared to the p53 family. It contains a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain at its C-terminal half. The SH3 domain and the ANK repeats of iASPP contribute to the p53 binding site; they bind to the DNA binding domain of p53. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212885 [Multi-domain]  Cd Length: 56  Bit Score: 41.07  E-value: 1.84e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 19921564  298 GAAYGVRRYQAQAPDEINIEVGDMISVIDMPSPAESIWW 336
Cdd:cd11952    1 GVVYALWDYSAEFPDELSFKEGDMVTVLRKDGEGTDWWW 39
SH3_SNX9_like cd11763
Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox ...
306-358 1.86e-04

Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. This subfamily consists of SH3 domain containing SNXs including SNX9, SNX18, SNX33, and similar proteins. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis, while SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212697 [Multi-domain]  Cd Length: 55  Bit Score: 40.77  E-value: 1.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19921564  306 YQAQAPDEINIEVGDMISVIDmpSPAESIWWRGKKSHlqkslYEVGFFPQSCV 358
Cdd:cd11763    8 FDSQPSGELSLRAGEVLTITR--QDVGDGWLEGRNSR-----GEVGLFPSSYV 53
SH3_9 pfam14604
Variant SH3 domain;
305-359 4.29e-04

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 39.52  E-value: 4.29e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 19921564    305 RYQAQAPDEINIEVGDMISVIDMpspAESIWWRGKKSHLqkslyeVGFFPQSCVA 359
Cdd:pfam14604    4 PYEPKDDDELSLQRGDVITVIEE---SEDGWWEGINTGR------TGLVPANYVE 49
SH3_CD2AP-like_2 cd11874
Second Src Homology 3 domain (SH3B) of CD2-associated protein and similar proteins; This ...
305-358 8.90e-04

Second Src Homology 3 domain (SH3B) of CD2-associated protein and similar proteins; This subfamily is composed of the second SH3 domain (SH3B) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3B of both proteins have been shown to bind to Cbl. In the case of CD2AP, its SH3B binds to Cbl at a site distinct from the c-Cbl/SH3A binding site. The CIN85 SH3B also binds ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212807 [Multi-domain]  Cd Length: 53  Bit Score: 38.85  E-value: 8.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 19921564  305 RYQAQAPDEINIEVGDMISVIDMPspaESIWWRGKKSHlqkslyEVGFFPQSCV 358
Cdd:cd11874    7 SYTPQNEDELELKVGDTIEVLGEV---EEGWWEGKLNG------KVGVFPSNFV 51
SH3_CD2AP-like_1 cd11873
First Src Homology 3 domain (SH3A) of CD2-associated protein and similar proteins; This ...
306-358 9.05e-04

First Src Homology 3 domain (SH3A) of CD2-associated protein and similar proteins; This subfamily is composed of the first SH3 domain (SH3A) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3A of both proteins bind to an atypical PXXXPR motif at the C-terminus of Cbl and the cytoplasmic domain of the cell adhesion protein CD2. CIN85 SH3A binds to internal proline-rich motifs within the proline-rich region; this intramolecular interaction serves as a regulatory mechanism to keep CIN85 in a closed conformation, preventing the recruitment of other proteins. CIN85 SH3A has also been shown to bind ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212806 [Multi-domain]  Cd Length: 53  Bit Score: 38.79  E-value: 9.05e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19921564  306 YQAQAPDEINIEVGDMISVIdmpSPAESIWWRGKKSHlqkslyEVGFFPQSCV 358
Cdd:cd11873    8 YDAEEPDELTLKVGDIITNV---KKMEEGWWEGTLNG------KRGMFPDNFV 51
SH3_ephexin1 cd11939
Src homology 3 domain of the Rho guanine nucleotide exchange factor, ephexin-1 (also called ...
303-358 9.24e-04

Src homology 3 domain of the Rho guanine nucleotide exchange factor, ephexin-1 (also called NGEF or ARHGEF27); Ephexin-1, also called NGEF (neuronal GEF) or ARHGEF27, activates RhoA, Tac1, and Cdc42 by exchanging bound GDP for free GTP. It is expressed mainly in the brain in a region associated with movement control. It regulates the stability of postsynaptic acetylcholine receptor (AChR) clusters and thus, plays a critical role in the maturation and neurotransmission of neuromuscular junctions. Ephexin-1 directly interacts with the ephrin receptor EphA4 and their coexpression enhances the ability of ephexin-1 to activate RhoA. It is required for normal axon growth and EphA-induced growth cone collapse. Ephexin-1 contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), and SH3 domains. The SH3 domains of ARHGEFs play an autoinhibitory role through intramolecular interactions with a proline-rich region N-terminal to the DH domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212872 [Multi-domain]  Cd Length: 55  Bit Score: 39.16  E-value: 9.24e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19921564  303 VRRYQAQAPDEINIEVGDMISVIDmpsPAESIWWRGKKSHLQkslyEVGFFPQSCV 358
Cdd:cd11939    5 VHPYVSQEPDELSLELADVLNILD---KTDDGWIFGERLHDQ----ERGWFPSSVV 53
SH3_ASPP1 cd11954
Src Homology 3 domain of Apoptosis Stimulating of p53 protein 1; ASPP1, like ASPP2, activates ...
298-339 9.32e-04

Src Homology 3 domain of Apoptosis Stimulating of p53 protein 1; ASPP1, like ASPP2, activates the apoptotic function of the p53 family of tumor suppressors (p53, p63, and p73). In addition, it functions in the cytoplasm to regulate the nuclear localization of the transcriptional cofactors YAP and TAZ by inihibiting their phosphorylation; YAP and TAZ are important regulators of cell expansion, differentiation, migration, and invasion. ASPP1 is downregulated in breast tumors expressing wild-type p53. It contains a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain at its C-terminal half. The SH3 domain and the ANK repeats of ASPP1 contribute to the p53 binding site; they bind to the DNA binding domain of p53. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212887 [Multi-domain]  Cd Length: 57  Bit Score: 39.23  E-value: 9.32e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 19921564  298 GAAYGVRRYQAQAPDEINIEVGDMISVIDMPSPAESIWWRGK 339
Cdd:cd11954    1 GMVYALWDYEAQNADELSFQEGDAITILRRKDDSETEWWWAR 42
SH3_FCHSD_1 cd11761
First Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of ...
305-356 1.06e-03

First Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of FCH and double SH3 domains protein 1 (FCHSD1) and FCHSD2. These proteins have a common domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. They have only been characterized in silico and their functions remain unknown. This group also includes the insect protein, nervous wreck, which acts as a regulator of synaptic growth signaling. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212695 [Multi-domain]  Cd Length: 57  Bit Score: 38.88  E-value: 1.06e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19921564  305 RYQAQAPDEINIEVGDMISVIDMPSPAESIWWRGKKShlqkslyEVGFFPQS 356
Cdd:cd11761    9 SYEAQRPDELTITEGEELEVIEDGDGDGWVKARNKSG-------EVGYVPEN 53
SH3_CD2AP-like_3 cd11875
Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This ...
306-338 1.16e-03

Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This subfamily is composed of the third SH3 domain (SH3C) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3C of both proteins have been shown to bind to ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212808 [Multi-domain]  Cd Length: 55  Bit Score: 38.87  E-value: 1.16e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 19921564  306 YQAQAPDEINIEVGDMISVIDMPSPaESIWWRG 338
Cdd:cd11875    8 YEAENEDELTLREGDIVTILSKDCE-DKGWWKG 39
SH3_D21-like cd12142
Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; ...
306-358 1.27e-03

Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; N-terminal SH3 domain of the uncharacterized protein SH3 domain-containing protein 21, and similar uncharacterized domains, it belongs to the CD2AP-like_3 subfamily of proteins. The CD2AP-like_3 subfamily is composed of the third SH3 domain (SH3C) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3C of both proteins have been shown to bind to ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 213018 [Multi-domain]  Cd Length: 55  Bit Score: 38.60  E-value: 1.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19921564  306 YQAQAPDEINIEVGDMISVIDMPSPAESiWWRGKKSHlqkslyEVGFFPQSCV 358
Cdd:cd12142    8 YNPVAPDELALKKGDVIEVISKETEDEG-WWEGELNG------RRGFFPDNFV 53
SH3_Intersectin_5 cd11840
Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor ...
306-359 3.27e-03

Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The fifth SH3 domain (or SH3E) of ITSN1 has been shown to bind many protein partners including SGIP1, Sos1, dynamin1/2, CIN85, c-Cbl, SHIP2, N-WASP, and synaptojanin-1, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212774 [Multi-domain]  Cd Length: 53  Bit Score: 37.40  E-value: 3.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 19921564  306 YQAQAPDEINIEVGDMISVIDMPSPAesiWWRGKKSHLqkslyeVGFFPQSCVA 359
Cdd:cd11840    8 YTAQNEDELSFQKGDIINVLSKDDPD---WWRGELNGQ------TGLFPSNYVE 52
SH3_GRAP2_C cd11950
C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ...
306-359 3.79e-03

C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS (GRB2-related adapter downstream of Shc), GrpL, GRB2L, Mona, or GRID (Grb2-related protein with insert domain). It is expressed specifically in the hematopoietic system. It plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. It also has roles in antigen-receptor and tyrosine kinase mediated signaling. GRAP2 is unique from other GRB2-like adaptor proteins in that it can be regulated by caspase cleavage. It contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domain of GRAP2 binds to different motifs found in substrate peptides including the typical PxxP motif in hematopoietic progenitor kinase 1 (HPK1), the RxxK motif in SLP-76 and HPK1, and the RxxxxK motif in phosphatase-like protein HD-PTP. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212883 [Multi-domain]  Cd Length: 53  Bit Score: 37.11  E-value: 3.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 19921564  306 YQAQAPDEINIEVGDMISVIDMPSPAesiWWRGKKSHlqkslyEVGFFPQSCVA 359
Cdd:cd11950    8 FEALEDDELGFNSGDVIEVLDSSNPS---WWKGRLHG------KLGLFPANYVA 52
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
410-613 4.54e-03

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: 40.79  E-value: 4.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  410 RLKQSGIyreRVFNCDLSEHLLNSGQD----IPMVLRSCAEFIENYGVID-GIYRLSGITSN----IQRLRRAFDEERVP 480
Cdd:cd04380   22 RLPDPGI---RNLIDQLELGDNPDYSEvplsIPKEIWRLVDYLYTRGLAQeGLFEEPGLPSEpgelLAEIRDALDTGSPF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921564  481 DLGNPemkqdIHAVSSLLKMYFRELPNPLCTYQLYDNFVEAIQVKADEADERLRLMketvlkLPPPHYRTLKYLAEHLYK 560
Cdd:cd04380   99 NSPGS-----AESVAEALLLFLESLPDPIIPYSLYERLLEAVANNEEDKRQVIRIS------LPPVHRNVFVYLCSFLRE 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19921564  561 VSQHHGRTGMTDKNLAIVWAPNLLRSPALESGGVAALRGVGVQAVVTEYLIRN 613
Cdd:cd04380  168 LLSESADRGLDENTLATIFGRVLLRDPPRAGGKERRAERDRKRAFIEQFLLND 220
 
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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