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Conserved domains on  [gi|1023177826|ref|XP_016295099|]
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RasGAP protein, C-terminal [Kalmanozyma brasiliensis GHG001]

Protein Classification

Ras GTPase-activating protein( domain architecture ID 13424543)

Ras GTPase-activating protein accelerates the GTPase activity of Ras

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RasGAP_GAPA cd05132
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...
160-512 0e+00

Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to bind to small GTPases, which are yet to be identified. IQGAP proteins are integral components of cytoskeletal regulation. Results from truncated GAPAs indicated that almost the entire region of GAPA homologous to IQGAP is required for cytokinesis in Dictyostelium. More members of the IQGAP family are emerging, and evidence suggests that there are both similarities and differences in their function.


:

Pssm-ID: 213334  Cd Length: 352  Bit Score: 666.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 160 EIDTLLQTVMFTLYGNQYESREEHLLLTMFQSVLSAQFETATEFGSLLRANTPVSRMMTTYTRRGPGQSYLKSVLAERIN 239
Cdd:cd05132     1 EIDSLLQTVMFTLYGNQYESREEHLLLSMFQSVLTYEFDETTEFGSLLRANTAVSRMMTTYTRRGPGQSYLKTVLADRIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 240 SLIEHKDLNLEINPLKVYEQMTNQIEEDTGsLPPNLPRGVPAEVASENADVQAIIAPRLTMLMEIANSFLQTIINSIEEV 319
Cdd:cd05132    81 DLISLKDLNLEINPLKVYEQMINDIELDTG-LPSNLPRGITPEEAAENPAVQNIIEPRLEMLEEITNSFLEAIINSLDEV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 320 PYGIRWICKQIRSLTKRKYPDATDLAICSLIGGFFFLRFINPAIVTPQAYMLVDGPPAKHPRRTLTLIAKMLQNLANKPS 399
Cdd:cd05132   160 PYGIRWICKQIRSLTRRKFPDASDETICSLIGGFFLLRFINPAIVSPQAYMLVDGKPSDNTRRTLTLIAKLLQNLANKPS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 400 YAKEQYMMSLEPFVENNKTRMNAFLNALCDVGDFYETLEMDQYMALSKKDLQIQITLNELYNTHSLVAQHLDILAPNDKH 479
Cdd:cd05132   240 YSKEPYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQYIALSKKDLSINITLNEIYNTHSLLVKHLAELAPDHND 319
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1023177826 480 HLRILIDELGGSPGQVPRKENRTLDLPLFSRWE 512
Cdd:cd05132   320 HLRLILQELGPAPPQVPRKENRTIELPLYSRWE 352
IQG1 super family cl34962
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
37-788 1.96e-114

Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and chromosome partitioning / Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5261:

Pssm-ID: 227586 [Multi-domain]  Cd Length: 1054  Bit Score: 371.91  E-value: 1.96e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826   37 TNRYSVTALYSMAAEQDVEVEDDLARAQKRLRELKGRISAQSKKNFVLERDVRYLDSR----IALLIANRMALDEQNEVA 112
Cdd:COG5261    273 STRRSTSVFYTISLEMISNVEQAFFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFA 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  113 STLEETDSSTVGTSLDDRKMQQYGNFFFLLQS-EPRHIAALC-RLVSLAEIDTLLQTVMFTLYGNQYESR---------- 180
Cdd:COG5261    353 ERLQSNINGRKKYFPLDRRLSLFGPLFFLLQSsIPLFSIAICvGRVKRFSIDALLNIVKLQILGNGYEIRklyslgksnc 432
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  181 EEHLLLTMFQSVLSAQFETATEFGSLLRANTPVSRMMTTYTRRGPGQSYLKSVLAERINSLIEHKDLNLEINPLKVYEQM 260
Cdd:COG5261    433 EEHLSVSLFQMLLRTEVEATSLVQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHEDLEVDINPLLVYRAL 512
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  261 TNQIEEdtgSLPPNLPRGVPAEVASENADVQAIIAPRLTMLMEIA-NSFLQTIINSIEEVPYGIRWICKQIRSLTK---- 335
Cdd:COG5261    513 LNKGQL---SPDKDLELLTSNEEVSEFLAVMNAVQESSAKLLELStERILDAVYNSLDEIGYGIRFVCELIRVVFEltpn 589
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  336 RKYPDATD-----------LAICSLIGGFFFLRFINPAIVTPQAYMLVDGPPAKHPRRTLTLiAKMLQNLANKPSYAKeq 404
Cdd:COG5261    590 RLFPSISDsrclrticfaeIDSLGLIGGFFFLRFVNEALVSPQTSMLKDSCPSDNVRKLATL-SKILQSVFEITSSDK-- 666
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  405 YMMSLEPFVENNKTRMNAFLNALCDVGDFYETLEMDQYMALSKKDLQIQITLNELYNTH-SLVAQHLDILAPNDKHHlri 483
Cdd:COG5261    667 FDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYLVNEIYLTHeIIIEYLDNLYDPDSLVD--- 743
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  484 LIDELGGSPGQVPRKENRTLDL----PLFSRWETPIQDlttaFMSENNVTQNDILYMETK-SIFVQLLRSIPT------- 551
Cdd:COG5261    744 LLLQELGELCSFPQDQRDTLNClvtlPLFNRSDDPIRD----LKQQLKRTRVYIIYVDAGtNLFEQLLRLLPSdepatrn 819
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  552 LAEKRPINLPQIAerAATTKDATLVRKGIKVKEMLRELEELKVVDRRDGYSLMTDEVATELTHLGNMREKVMQEMGSLES 631
Cdd:COG5261    820 PLDLNPNIRDDPS--VSSLKSMSLMKLKIRAIELLDELETLGFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQD 897
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  632 VYKTICEHNNYMRSQLDTYKSYLQNVRMTSGSAKDKSaggVGVISVGGKEKKAPKTQALGPYRFTHAQMEKDGIIVESNV 711
Cdd:COG5261    898 SLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKSKL---KGFSRGVGVVRDKPKSISSGTFKYSAQQLYKRGVLVNITI 974
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1023177826  712 PDNRRANIYFNITSPSPGTFIIALHYKGREKAILEMDLKLDDLLEKQKDDVQLLDL-EYVQLNVSKILQLLNKTFTKR 788
Cdd:COG5261    975 PEPNVSNIYFTFSSDSTDNFVIEVYQPGHSVSLPEVSFCFDDLLKRQYNKNPVVDLgGFLTFNANKLLHLIESKFYRK 1052
 
Name Accession Description Interval E-value
RasGAP_GAPA cd05132
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...
160-512 0e+00

Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to bind to small GTPases, which are yet to be identified. IQGAP proteins are integral components of cytoskeletal regulation. Results from truncated GAPAs indicated that almost the entire region of GAPA homologous to IQGAP is required for cytokinesis in Dictyostelium. More members of the IQGAP family are emerging, and evidence suggests that there are both similarities and differences in their function.


Pssm-ID: 213334  Cd Length: 352  Bit Score: 666.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 160 EIDTLLQTVMFTLYGNQYESREEHLLLTMFQSVLSAQFETATEFGSLLRANTPVSRMMTTYTRRGPGQSYLKSVLAERIN 239
Cdd:cd05132     1 EIDSLLQTVMFTLYGNQYESREEHLLLSMFQSVLTYEFDETTEFGSLLRANTAVSRMMTTYTRRGPGQSYLKTVLADRIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 240 SLIEHKDLNLEINPLKVYEQMTNQIEEDTGsLPPNLPRGVPAEVASENADVQAIIAPRLTMLMEIANSFLQTIINSIEEV 319
Cdd:cd05132    81 DLISLKDLNLEINPLKVYEQMINDIELDTG-LPSNLPRGITPEEAAENPAVQNIIEPRLEMLEEITNSFLEAIINSLDEV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 320 PYGIRWICKQIRSLTKRKYPDATDLAICSLIGGFFFLRFINPAIVTPQAYMLVDGPPAKHPRRTLTLIAKMLQNLANKPS 399
Cdd:cd05132   160 PYGIRWICKQIRSLTRRKFPDASDETICSLIGGFFLLRFINPAIVSPQAYMLVDGKPSDNTRRTLTLIAKLLQNLANKPS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 400 YAKEQYMMSLEPFVENNKTRMNAFLNALCDVGDFYETLEMDQYMALSKKDLQIQITLNELYNTHSLVAQHLDILAPNDKH 479
Cdd:cd05132   240 YSKEPYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQYIALSKKDLSINITLNEIYNTHSLLVKHLAELAPDHND 319
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1023177826 480 HLRILIDELGGSPGQVPRKENRTLDLPLFSRWE 512
Cdd:cd05132   320 HLRLILQELGPAPPQVPRKENRTIELPLYSRWE 352
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
37-788 1.96e-114

Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and chromosome partitioning / Signal transduction mechanisms];


Pssm-ID: 227586 [Multi-domain]  Cd Length: 1054  Bit Score: 371.91  E-value: 1.96e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826   37 TNRYSVTALYSMAAEQDVEVEDDLARAQKRLRELKGRISAQSKKNFVLERDVRYLDSR----IALLIANRMALDEQNEVA 112
Cdd:COG5261    273 STRRSTSVFYTISLEMISNVEQAFFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFA 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  113 STLEETDSSTVGTSLDDRKMQQYGNFFFLLQS-EPRHIAALC-RLVSLAEIDTLLQTVMFTLYGNQYESR---------- 180
Cdd:COG5261    353 ERLQSNINGRKKYFPLDRRLSLFGPLFFLLQSsIPLFSIAICvGRVKRFSIDALLNIVKLQILGNGYEIRklyslgksnc 432
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  181 EEHLLLTMFQSVLSAQFETATEFGSLLRANTPVSRMMTTYTRRGPGQSYLKSVLAERINSLIEHKDLNLEINPLKVYEQM 260
Cdd:COG5261    433 EEHLSVSLFQMLLRTEVEATSLVQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHEDLEVDINPLLVYRAL 512
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  261 TNQIEEdtgSLPPNLPRGVPAEVASENADVQAIIAPRLTMLMEIA-NSFLQTIINSIEEVPYGIRWICKQIRSLTK---- 335
Cdd:COG5261    513 LNKGQL---SPDKDLELLTSNEEVSEFLAVMNAVQESSAKLLELStERILDAVYNSLDEIGYGIRFVCELIRVVFEltpn 589
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  336 RKYPDATD-----------LAICSLIGGFFFLRFINPAIVTPQAYMLVDGPPAKHPRRTLTLiAKMLQNLANKPSYAKeq 404
Cdd:COG5261    590 RLFPSISDsrclrticfaeIDSLGLIGGFFFLRFVNEALVSPQTSMLKDSCPSDNVRKLATL-SKILQSVFEITSSDK-- 666
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  405 YMMSLEPFVENNKTRMNAFLNALCDVGDFYETLEMDQYMALSKKDLQIQITLNELYNTH-SLVAQHLDILAPNDKHHlri 483
Cdd:COG5261    667 FDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYLVNEIYLTHeIIIEYLDNLYDPDSLVD--- 743
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  484 LIDELGGSPGQVPRKENRTLDL----PLFSRWETPIQDlttaFMSENNVTQNDILYMETK-SIFVQLLRSIPT------- 551
Cdd:COG5261    744 LLLQELGELCSFPQDQRDTLNClvtlPLFNRSDDPIRD----LKQQLKRTRVYIIYVDAGtNLFEQLLRLLPSdepatrn 819
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  552 LAEKRPINLPQIAerAATTKDATLVRKGIKVKEMLRELEELKVVDRRDGYSLMTDEVATELTHLGNMREKVMQEMGSLES 631
Cdd:COG5261    820 PLDLNPNIRDDPS--VSSLKSMSLMKLKIRAIELLDELETLGFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQD 897
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  632 VYKTICEHNNYMRSQLDTYKSYLQNVRMTSGSAKDKSaggVGVISVGGKEKKAPKTQALGPYRFTHAQMEKDGIIVESNV 711
Cdd:COG5261    898 SLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKSKL---KGFSRGVGVVRDKPKSISSGTFKYSAQQLYKRGVLVNITI 974
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1023177826  712 PDNRRANIYFNITSPSPGTFIIALHYKGREKAILEMDLKLDDLLEKQKDDVQLLDL-EYVQLNVSKILQLLNKTFTKR 788
Cdd:COG5261    975 PEPNVSNIYFTFSSDSTDNFVIEVYQPGHSVSLPEVSFCFDDLLKRQYNKNPVVDLgGFLTFNANKLLHLIESKFYRK 1052
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
188-396 1.65e-83

GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position.


Pssm-ID: 459871  Cd Length: 207  Bit Score: 264.53  E-value: 1.65e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 188 MFQSVLSAQFETATEFGSLLRANTPVSRMMTTYTRRGPGQSYLKSVLAERINSLIEHKDLNLEINPLKVYEQMTNQIEED 267
Cdd:pfam00616   1 LISELIEEEIESSDNPNDLLRGNSLVSKLLETYNRRPRGQEYLKKVLGPLVRKIIEDEDLDLESDPRKIYESLINQEELK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 268 TGSlpPNLPRGVPAEVASENADVQAIIAPRLTMLMEIANSFLQTIINSIEEVPYGIRWICKQIRSLTKRKYPDATDLAIC 347
Cdd:pfam00616  81 TGR--SDLPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEIL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1023177826 348 SLIGGFFFLRFINPAIVTPQAYMLVDGPPAKHPRRTLTLIAKMLQNLAN 396
Cdd:pfam00616 159 NAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
155-479 1.03e-64

GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position. Improved domain limits from structure.


Pssm-ID: 214617  Cd Length: 344  Bit Score: 219.49  E-value: 1.03e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  155 LVSLAEIDTLLQTVMFTLYGNQYESREEHLLLTMFQSVLSAQFETAtEFGSLLRANTPVSRMMTTYTRRGPGQSYLKSVL 234
Cdd:smart00323   1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLSLASALS-EVCSGLDKDELATKLVRLFLRRGRGHPFLRALI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  235 AERINSLIE----HKDLNLEINPLKVYEQMTNQIEEDTGsLPPNLPRGV---------PAEVASENadvqaiIAPRLTML 301
Cdd:smart00323  80 DPEVERTDDpntiFRGNSLATKSMEVYMKLVGNQYLHTT-LKPVLKKIVeskkscevdPAKLEGED------LETNLENL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  302 MEIANSFLQTIINSIEEVPYGIRWICKQIRSLTKRKYPDatDLAICSLIGGFFFLRFINPAIVTPQAYMLVDGPPAKHPR 381
Cdd:smart00323 153 LQYVERLFDAIINSSDRLPYGLRDICKQLRQAAEKRFPD--ADVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTR 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  382 RTLTLIAKMLQNLAN-KPSYAKEQYMMSLEPFVENNKTRMNAFLNALCDVGDFyetlemdqymALSKKDLQIQITLNELY 460
Cdd:smart00323 231 RTLTLIAKVLQNLANlSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEI----------LVDKVSDSTTISGRELS 300
                          330
                   ....*....|....*....
gi 1023177826  461 NTHSLVAQHLDILAPNDKH 479
Cdd:smart00323 301 LLHSLLLENGDALKRELNN 319
RasGAP_C pfam03836
RasGAP C-terminus; This domain can be found in the C terminus of the IQGAP family members, ...
575-708 7.02e-36

RasGAP C-terminus; This domain can be found in the C terminus of the IQGAP family members, including human IQGAP1/2/3, S. cerevisiae Iqg1 and S. pombe Rng2. Some members function in cytoskeletal remodelling. Human IQGAP1 is a scaffolding protein that can assemble multi-protein complexes involved in cell-cell interaction, cell adherence, and movement via actin/tubulin-based cytoskeletal reorganization. IQGAP1 is also a regulator of the MAPK and Wnt/beta-catenin signaling pathways.Iqg1 and Rng2 are required for actomyosin ring construction during cytokinesis.


Pssm-ID: 461071  Cd Length: 137  Bit Score: 132.29  E-value: 7.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 575 LVRKGIKVKEMLRELEELKVVDRRDGYSLMTDEVATELTHLGNMREKVMQEMGSLESVYKTICEHNNYMRSQLDTYKSYL 654
Cdd:pfam03836   1 YVELKKKALENLLELESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1023177826 655 QNVRMTSGSAKDKsaGGVGVISVGGKEKKAPKTQALGPYRFTHAQMEKDGIIVE 708
Cdd:pfam03836  81 ENCLDNLQKKKKK--LFSKQYFHYRKLQKRGKLPKFGSYKYSARQLYEKGVLLE 132
 
Name Accession Description Interval E-value
RasGAP_GAPA cd05132
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...
160-512 0e+00

Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to bind to small GTPases, which are yet to be identified. IQGAP proteins are integral components of cytoskeletal regulation. Results from truncated GAPAs indicated that almost the entire region of GAPA homologous to IQGAP is required for cytokinesis in Dictyostelium. More members of the IQGAP family are emerging, and evidence suggests that there are both similarities and differences in their function.


Pssm-ID: 213334  Cd Length: 352  Bit Score: 666.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 160 EIDTLLQTVMFTLYGNQYESREEHLLLTMFQSVLSAQFETATEFGSLLRANTPVSRMMTTYTRRGPGQSYLKSVLAERIN 239
Cdd:cd05132     1 EIDSLLQTVMFTLYGNQYESREEHLLLSMFQSVLTYEFDETTEFGSLLRANTAVSRMMTTYTRRGPGQSYLKTVLADRIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 240 SLIEHKDLNLEINPLKVYEQMTNQIEEDTGsLPPNLPRGVPAEVASENADVQAIIAPRLTMLMEIANSFLQTIINSIEEV 319
Cdd:cd05132    81 DLISLKDLNLEINPLKVYEQMINDIELDTG-LPSNLPRGITPEEAAENPAVQNIIEPRLEMLEEITNSFLEAIINSLDEV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 320 PYGIRWICKQIRSLTKRKYPDATDLAICSLIGGFFFLRFINPAIVTPQAYMLVDGPPAKHPRRTLTLIAKMLQNLANKPS 399
Cdd:cd05132   160 PYGIRWICKQIRSLTRRKFPDASDETICSLIGGFFLLRFINPAIVSPQAYMLVDGKPSDNTRRTLTLIAKLLQNLANKPS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 400 YAKEQYMMSLEPFVENNKTRMNAFLNALCDVGDFYETLEMDQYMALSKKDLQIQITLNELYNTHSLVAQHLDILAPNDKH 479
Cdd:cd05132   240 YSKEPYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQYIALSKKDLSINITLNEIYNTHSLLVKHLAELAPDHND 319
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1023177826 480 HLRILIDELGGSPGQVPRKENRTLDLPLFSRWE 512
Cdd:cd05132   320 HLRLILQELGPAPPQVPRKENRTIELPLYSRWE 352
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
37-788 1.96e-114

Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and chromosome partitioning / Signal transduction mechanisms];


Pssm-ID: 227586 [Multi-domain]  Cd Length: 1054  Bit Score: 371.91  E-value: 1.96e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826   37 TNRYSVTALYSMAAEQDVEVEDDLARAQKRLRELKGRISAQSKKNFVLERDVRYLDSR----IALLIANRMALDEQNEVA 112
Cdd:COG5261    273 STRRSTSVFYTISLEMISNVEQAFFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFA 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  113 STLEETDSSTVGTSLDDRKMQQYGNFFFLLQS-EPRHIAALC-RLVSLAEIDTLLQTVMFTLYGNQYESR---------- 180
Cdd:COG5261    353 ERLQSNINGRKKYFPLDRRLSLFGPLFFLLQSsIPLFSIAICvGRVKRFSIDALLNIVKLQILGNGYEIRklyslgksnc 432
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  181 EEHLLLTMFQSVLSAQFETATEFGSLLRANTPVSRMMTTYTRRGPGQSYLKSVLAERINSLIEHKDLNLEINPLKVYEQM 260
Cdd:COG5261    433 EEHLSVSLFQMLLRTEVEATSLVQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHEDLEVDINPLLVYRAL 512
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  261 TNQIEEdtgSLPPNLPRGVPAEVASENADVQAIIAPRLTMLMEIA-NSFLQTIINSIEEVPYGIRWICKQIRSLTK---- 335
Cdd:COG5261    513 LNKGQL---SPDKDLELLTSNEEVSEFLAVMNAVQESSAKLLELStERILDAVYNSLDEIGYGIRFVCELIRVVFEltpn 589
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  336 RKYPDATD-----------LAICSLIGGFFFLRFINPAIVTPQAYMLVDGPPAKHPRRTLTLiAKMLQNLANKPSYAKeq 404
Cdd:COG5261    590 RLFPSISDsrclrticfaeIDSLGLIGGFFFLRFVNEALVSPQTSMLKDSCPSDNVRKLATL-SKILQSVFEITSSDK-- 666
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  405 YMMSLEPFVENNKTRMNAFLNALCDVGDFYETLEMDQYMALSKKDLQIQITLNELYNTH-SLVAQHLDILAPNDKHHlri 483
Cdd:COG5261    667 FDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYLVNEIYLTHeIIIEYLDNLYDPDSLVD--- 743
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  484 LIDELGGSPGQVPRKENRTLDL----PLFSRWETPIQDlttaFMSENNVTQNDILYMETK-SIFVQLLRSIPT------- 551
Cdd:COG5261    744 LLLQELGELCSFPQDQRDTLNClvtlPLFNRSDDPIRD----LKQQLKRTRVYIIYVDAGtNLFEQLLRLLPSdepatrn 819
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  552 LAEKRPINLPQIAerAATTKDATLVRKGIKVKEMLRELEELKVVDRRDGYSLMTDEVATELTHLGNMREKVMQEMGSLES 631
Cdd:COG5261    820 PLDLNPNIRDDPS--VSSLKSMSLMKLKIRAIELLDELETLGFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQD 897
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  632 VYKTICEHNNYMRSQLDTYKSYLQNVRMTSGSAKDKSaggVGVISVGGKEKKAPKTQALGPYRFTHAQMEKDGIIVESNV 711
Cdd:COG5261    898 SLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKSKL---KGFSRGVGVVRDKPKSISSGTFKYSAQQLYKRGVLVNITI 974
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1023177826  712 PDNRRANIYFNITSPSPGTFIIALHYKGREKAILEMDLKLDDLLEKQKDDVQLLDL-EYVQLNVSKILQLLNKTFTKR 788
Cdd:COG5261    975 PEPNVSNIYFTFSSDSTDNFVIEVYQPGHSVSLPEVSFCFDDLLKRQYNKNPVVDLgGFLTFNANKLLHLIESKFYRK 1052
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
188-396 1.65e-83

GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position.


Pssm-ID: 459871  Cd Length: 207  Bit Score: 264.53  E-value: 1.65e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 188 MFQSVLSAQFETATEFGSLLRANTPVSRMMTTYTRRGPGQSYLKSVLAERINSLIEHKDLNLEINPLKVYEQMTNQIEED 267
Cdd:pfam00616   1 LISELIEEEIESSDNPNDLLRGNSLVSKLLETYNRRPRGQEYLKKVLGPLVRKIIEDEDLDLESDPRKIYESLINQEELK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 268 TGSlpPNLPRGVPAEVASENADVQAIIAPRLTMLMEIANSFLQTIINSIEEVPYGIRWICKQIRSLTKRKYPDATDLAIC 347
Cdd:pfam00616  81 TGR--SDLPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEIL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1023177826 348 SLIGGFFFLRFINPAIVTPQAYMLVDGPPAKHPRRTLTLIAKMLQNLAN 396
Cdd:pfam00616 159 NAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
180-492 4.73e-67

Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family represents IQ motif containing GTPase activating protein (IQGAP) which associated with the Ras GTP-binding protein. A primary function of IQGAP proteins is to modulate cytoskeletal architecture. There are three known IQGAP family members: IQGAP1, IQGAP2 and IQGAP3. Human IQGAP1 and IQGAP2 share 62% identity. IQGAPs are multi-domain molecules having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP is an essential regulator of cytoskeletal function. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity, the protein actually lacks GAP activity. Both IQGAP1 and IQGAP2 specifically bind to Cdc42 and Rac1, but not to RhoA. Despite of their similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP3, only present in mammals, regulates the organization of the cytoskeleton under the regulation of Rac1 and Cdc42 in neuronal cells. The depletion of IQGAP3 is shown to impair neurite or axon outgrowth in neuronal cells with disorganized cytoskeleton.


Pssm-ID: 213329 [Multi-domain]  Cd Length: 331  Bit Score: 225.54  E-value: 4.73e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 180 REEHLLLTMFQSVL----SAQFETATEFgslLRANTPVSRMMTTYTRRGPGQSYLKSVLAERINSLIEHKDLNLEINPLK 255
Cdd:cd05127     5 REEYLLLKLFKTALreeiESKVSLPEDI---VTGNPTVIKLVVNYNRGPRGQKYLRELLGPVVKEILDDDDLDLETDPVD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 256 VYEQMTNQIEEDTGSlPPNLPRGVPAEVASENADVQAIIAPRLTMLMEIANSFLQTIINSIEEVPYGIRWICKQIRSLTK 335
Cdd:cd05127    82 IYKAWINQEESRTGE-PSKLPYDVTREQALKDPEVRKRLIEHLEKLRAITDKFLTAITESLDKMPYGMRYIAKVLKEALR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 336 RKYPDATDLAICSLIGGFFFLRFINPAIVTPQAYMLVDGPPAK----HPRRTLTLIAKMLQNLANKPSYAKE-QYMMSLE 410
Cdd:cd05127   161 EKFPDAPEEEILKIVGNLLYYRYMNPAIVAPEAFDIIDLSVGGqlspLQRRNLGSIAKVLQQAASGKLFGGEnPYLSPLN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 411 PFVENNKTRMNAFLNALCDVGDFYETLEMDQY---MALSKKdlQIQITLNELYNTHSLVAQHLDILAPNDKHHLRILIDE 487
Cdd:cd05127   241 PYISESHEKFKKFFLEACTVPEAEEHFNIDEYsdlTMLTKP--TIYISLQEIFATHKLLLEHQDEIAPDPDDPLRELLDD 318

                  ....*
gi 1023177826 488 LGGSP 492
Cdd:cd05127   319 LGPAP 323
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
155-479 1.03e-64

GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position. Improved domain limits from structure.


Pssm-ID: 214617  Cd Length: 344  Bit Score: 219.49  E-value: 1.03e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  155 LVSLAEIDTLLQTVMFTLYGNQYESREEHLLLTMFQSVLSAQFETAtEFGSLLRANTPVSRMMTTYTRRGPGQSYLKSVL 234
Cdd:smart00323   1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLSLASALS-EVCSGLDKDELATKLVRLFLRRGRGHPFLRALI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  235 AERINSLIE----HKDLNLEINPLKVYEQMTNQIEEDTGsLPPNLPRGV---------PAEVASENadvqaiIAPRLTML 301
Cdd:smart00323  80 DPEVERTDDpntiFRGNSLATKSMEVYMKLVGNQYLHTT-LKPVLKKIVeskkscevdPAKLEGED------LETNLENL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  302 MEIANSFLQTIINSIEEVPYGIRWICKQIRSLTKRKYPDatDLAICSLIGGFFFLRFINPAIVTPQAYMLVDGPPAKHPR 381
Cdd:smart00323 153 LQYVERLFDAIINSSDRLPYGLRDICKQLRQAAEKRFPD--ADVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTR 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826  382 RTLTLIAKMLQNLAN-KPSYAKEQYMMSLEPFVENNKTRMNAFLNALCDVGDFyetlemdqymALSKKDLQIQITLNELY 460
Cdd:smart00323 231 RTLTLIAKVLQNLANlSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEI----------LVDKVSDSTTISGRELS 300
                          330
                   ....*....|....*....
gi 1023177826  461 NTHSLVAQHLDILAPNDKH 479
Cdd:smart00323 301 LLHSLLLENGDALKRELNN 319
RasGAP_IQGAP2 cd05131
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...
167-500 1.97e-54

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a member of the IQGAP family that contains a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeat, a single WW domain, four IQ motifs which mediate interactions with calmodulin, and a Ras-GTPase-activating protein (GAP)-related domain that binds Rho family GTPases. IQGAP2 and IQGAP3 play important roles in the regulation of the cytoskeleton for axon outgrowth in hippocampal neurons and are thought to stay in a common regulatory pathway. The results of RNA interference studies indicated that IQGAP3 partially compensates functions of IQGAP2, but has lesser ability than IQGAP2 to promote axon outgrowth in hippocampal neuron. Moreover, IQGAP2 is required for the cadherin-mediated cell-to-cell adhesion in Xenopus laevis embryos.


Pssm-ID: 213333 [Multi-domain]  Cd Length: 359  Bit Score: 192.13  E-value: 1.97e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 167 TVMFTLYGNQYESREEHLLLTMFQSVLSAQFETATE-FGSLLRANTPVSRMMTTYTRRGPGQSYLKSVLAERINSLIEHK 245
Cdd:cd05131     2 TVIFTLYNYASNQREEYLLLKLFETALEEEIKSKVDqIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIEDK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 246 DLNLEINPLKVYEQMTNQIEEDTGSlPPNLPRGVPAEVASENADVQAIIAPRLTMLMEIANSFLQTIINSIEEVPYGIRW 325
Cdd:cd05131    82 SLIINTNPVEVYKAWVNQLETATGE-ASKLPYDVTTEQALTHPEVVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 326 ICKQIRSLTKRKYPDATDLAICSLIGGFFFLRFINPAIVTPQAYMLVD----GPPAKHPRRTLTLIAKMLQNLA-NKPSY 400
Cdd:cd05131   161 IAKVLKNSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQIHSEQRRNLGSVAKVLQHAAsNKLFE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 401 AKEQYMMSLEPFVENNKTRMNAFLNALCDVGDFYETLEMDQY---MALSKKdlQIQITLNELYNTHSLVAQHLDILAPND 477
Cdd:cd05131   241 GENAHLSSMNSYLSQTYQKFRKFFQAACDVPEPEEKFNIDEYsdmVTLSKP--VIYISIEEIINTHSLLLEHQDAIAPDQ 318
                         330       340
                  ....*....|....*....|...
gi 1023177826 478 KHhlriLIDELGGSPGQVPRKEN 500
Cdd:cd05131   319 ND----LLHELLKDLGEVPDVES 337
RasGAP_Neurofibromin_like cd05392
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...
131-430 2.12e-51

Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins include the Saccharomyces cerevisiae RasGAP proteins Ira1 and Ira2, the closest homolog of neurofibromin, which is responsible for the human autosomal dominant disease neurofibromatosis type I (NF1). The RasGAP Ira1/2 proteins are negative regulators of the Ras-cAMP signaling pathway and conserved from yeast to human. In yeast Ras proteins are activated by GEFs, and inhibited by two GAPs, Ira1 and Ira2. Ras proteins activate the cAMP/protein kinase A (PKA) pathway, which controls metabolism, stress resistance, growth, and meiosis. Recent studies showed that the kelch proteins Gpb1 and Gpb2 inhibit Ras activity via association with Ira1 and Ira2. Gpb1/2 bind to a conserved C-terminal domain of Ira1/2, and loss of Gpb1/2 results in a destabilization of Ira1 and Ira2, leading to elevated levels of Ras2-GTP and uninhibited cAMP-PKA signaling. Since the Gpb1/2 binding domain on Ira1/2 is conserved in the human neurofibromin protein, the studies suggest that an analogous signaling mechanism may contribute to the neoplastic development of NF1.


Pssm-ID: 213341  Cd Length: 317  Bit Score: 182.10  E-value: 2.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 131 KMQQYGNFFFLLQSEPRHIAALCRLVSLAEIDTLLQtVMFTLYgnqyESReeHLLLTMFQSVLSAQFETATEFGSLLRAN 210
Cdd:cd05392     2 KSEAYDELLELLIEDPQLLLAIAEVCPSSEVDLLAQ-SLLNLF----ETR--NRLLPLISWLIEDEISHTSRAADLFRRN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 211 TPVSRMMTTYTRRgPGQSYLKSVLAERINSLIEHKDLNLEINPLKVYEQMTnqieedtgslppnlprgvpaevasENADV 290
Cdd:cd05392    75 SVATRLLTLYAKS-VGNKYLRKVLRPLLTEIVDNKDYFEVEKIKPDDENLE------------------------ENADL 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 291 qaiiaprltmLMEIANSFLQTIINSIEEVPYGIRWICKQIRSLTKRKYPDATDLAIcsliGGFFFLRFINPAIVTPQAYM 370
Cdd:cd05392   130 ----------LMKYAQMLLDSITDSVDQLPPSFRYICNTIYESVSKKFPDAALIAV----GGFLFLRFICPAIVSPESEN 195
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1023177826 371 LVDGPPAKHPRRTLTLIAKMLQNLANKPSY-AKEQYMMSLEPFVENNKTRMNAFLNALCDV 430
Cdd:cd05392   196 LLDPPPTPEARRSLILIAKVLQNIANGVLFsLKEPYLESLNEFLKKNSDRIQQFLSEVSTI 256
RasGAP_IQGAP1 cd05133
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...
167-492 7.33e-51

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a homodimeric protein that is widely expressed among vertebrate cell types from early embryogenesis. Mammalian IQGAP1 protein is the best characterized member of the IQGAP family, and contains several protein-interacting domains. Human IQGAP1 is most similar to mouse Iqgap1 (94% identity) and has 62% identity to human IQGAP2. IQGAP1 binds and cross-links actin filaments in vitro and has been implicated in Ca2+/calmodulin signaling, E-cadherin-dependent cell adhesion, cell motility, and invasion. Yeast IQGAP homologs have a role in the recruitment of actin filaments, are components of the spindle pole body, and are required for actomyosin ring assembly and cytokinesis. Furthermore, IQGAP1 over-expression has also been detected in gastric and colorectal carcinomas and gastric cancer cell lines.


Pssm-ID: 213335  Cd Length: 380  Bit Score: 182.55  E-value: 7.33e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 167 TVMFTLYGNQYESREEHLLLTMFQSVLSAQFETAT-EFGSLLRANTPVSRMMTTYTRRGPGQSYLKSVLAERINSLIEHK 245
Cdd:cd05133     2 SVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVdQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 246 DLNLEINPLKVYEQMTNQIEEDTGSlPPNLPRGVPAEVASENADVQAIIAPRLTMLMEIANSFLQTIINSIEEVPYGIRW 325
Cdd:cd05133    82 SLNIKTDPVDIYKSWVNQMESQTGE-ASKLPYDVTPEQAMSHEEVRTRLDASIKNMRMVTDKFLSAIISSVDKIPYGMRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 326 ICKQIRSLTKRKYPDATDLAICSLIGGFFFLRFINPAIVTPQAYMLVD----GPPAKHPRRTLTLIAKMLQNLA-NKPSY 400
Cdd:cd05133   161 IAKVLKDTLHEKFPDAGEDELLKIVGNLLYYRYMNPAIVAPDAFDIIDlsagGQLTTDQRRNLGSIAKMLQHAAsNKMFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 401 AKEQYMMSLEPFVENNKTRMNAFLNALCDVGDFYETLEMDQYMAL-SKKDLQIQITLNELYNTHSLVAQHLDILAPNDKH 479
Cdd:cd05133   241 GDNAHLSPINEYLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDLvTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 320
                         330
                  ....*....|...
gi 1023177826 480 HLRILIDELGGSP 492
Cdd:cd05133   321 PIHELLDDLGEVP 333
RasGAP_IQGAP3 cd12207
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ...
166-492 1.56e-50

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family represents the IQ motif containing GTPase activating protein 3 (IQGAP3), which associates with Ras GTP-binding proteins. A primary function of IQGAP proteins is to modulate cytoskeletal architecture. There are three known IQGAP family members: IQGAP1, IQGAP2 and IQGAP3. Human IQGAP1 and IQGAP2 share 62% identity. IQGAPs are multi-domain molecules having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP is an essential regulator of cytoskeletal function. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity, the protein actually lacks GAP activity. Both IQGAP1 and IQGAP2 specifically bind to Cdc42 and Rac1, but not to RhoA. Despite of their similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP3, only present in mammals, regulates the organization of the cytoskeleton under the regulation of Rac1 and Cdc42 in neuronal cells. The depletion of IQGAP3 is shown to impair neurite or axon outgrowth in neuronal cells with disorganized cytoskeleton.


Pssm-ID: 213346 [Multi-domain]  Cd Length: 350  Bit Score: 180.80  E-value: 1.56e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 166 QTVMFTLYGNQYESREEHLLLTMFQSVLSAQFETATE-FGSLLRANTPVSRMMTTYTRRGPGQSYLKSVLAERINSLIEH 244
Cdd:cd12207     1 ESVIFSLYNYASNRREAYLLLQLFKTALQEEISSKVEkPQDVITGNPTVIRLLVSFYRSARGQNALRHILGPVVQDVLQD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 245 KDLNLEINPLKVYEQMTNQIEEDTGSlPPNLPRGVPAEVASENADVQAIIAPRLTMLMEIANSFLQTIINSIEEVPYGIR 324
Cdd:cd12207    81 KGLSIRTDPVQIYKAWINQTETQSGC-RSSLPYEVSPEQALSHPEVQRRLDIAIRNLLAVTDKFLSAITSSVDKIPYGMR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 325 WICKQIRSLTKRKYPDATDLAICSLIGGFFFLRFINPAIVTPQAYMLVD--GPPAKHP--RRTLTLIAKMLQN-LANKPS 399
Cdd:cd12207   160 YVAKVLRDSLQEKFPGASEDEVYKVVGNLLYYRFMNPAVVAPDGFDIVDcsAGGALQPeqRRMLGSVAKVLQHaAANKHF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 400 YAKEQYMMSLEPFVENNKTRMNAFLNALCDVGDFYETLEMDQY---MALSKKdlQIQITLNELYNTHSLVAQHLDILAPN 476
Cdd:cd12207   240 QGDSEHLQALNQYLEETHVKFRKFILQACCVPEPEERFNVDEYsemVAVAKP--VIYITVGELINTHKLLLEHQDSIAPD 317
                         330
                  ....*....|....*.
gi 1023177826 477 DKHHLRILIDELGGSP 492
Cdd:cd12207   318 HSDPLHELLEDLGEVP 333
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
181-429 3.79e-44

Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Proteins having a RasGAP domain include p120GAP, IQGAP, Rab5-activating protein 6, and Neurofibromin, among others. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP exhibit no similarity at their amino acid sequence level. RasGTPases function as molecular switches in a large number of signaling pathways. They are in the on state when bound to GTP, and in the off state when bound to GDP. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator.


Pssm-ID: 213328  Cd Length: 256  Bit Score: 159.96  E-value: 3.79e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 181 EEHLLLTMFQSVLSAQFETA-TEFGSLLRANTPVSRMMTTYTRRGPGQSYLKSVLAERINSLIEHKDL----NLEINPLK 255
Cdd:cd04519     1 EEYRLLSLLLTESPLALLRElSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNTKNPNTLfrgnSLATKLLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 256 VYEQMTNQ--IEEDTGSLPPNLPRGVPAEVASENADVQAIIAPRLTMLMEIANSFLQTIINSIEEVPYGIRWICKQIRSL 333
Cdd:cd04519    81 QYMKLVGQeyLKETLSPLIREILESKESCEIDTKLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILREF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 334 TKRKYPDATDLAIcSLIGGFFFLRFINPAIVTPQAYMLVDGPPAKHPRRTLTLIAKMLQNLANKPSY-AKEQYMMSLEPF 412
Cdd:cd04519   161 LAERFPEEPDEAY-QAVSGFLFLRFICPAIVSPELFGLVPDEPSEQARRNLTLISKVLQSLANGVEFgDKEPFMKPLNDF 239
                         250
                  ....*....|....*..
gi 1023177826 413 VENNKTRMNAFLNALCD 429
Cdd:cd04519   240 IKSNKPKLKQFLDELSS 256
RasGAP_C pfam03836
RasGAP C-terminus; This domain can be found in the C terminus of the IQGAP family members, ...
575-708 7.02e-36

RasGAP C-terminus; This domain can be found in the C terminus of the IQGAP family members, including human IQGAP1/2/3, S. cerevisiae Iqg1 and S. pombe Rng2. Some members function in cytoskeletal remodelling. Human IQGAP1 is a scaffolding protein that can assemble multi-protein complexes involved in cell-cell interaction, cell adherence, and movement via actin/tubulin-based cytoskeletal reorganization. IQGAP1 is also a regulator of the MAPK and Wnt/beta-catenin signaling pathways.Iqg1 and Rng2 are required for actomyosin ring construction during cytokinesis.


Pssm-ID: 461071  Cd Length: 137  Bit Score: 132.29  E-value: 7.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 575 LVRKGIKVKEMLRELEELKVVDRRDGYSLMTDEVATELTHLGNMREKVMQEMGSLESVYKTICEHNNYMRSQLDTYKSYL 654
Cdd:pfam03836   1 YVELKKKALENLLELESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1023177826 655 QNVRMTSGSAKDKsaGGVGVISVGGKEKKAPKTQALGPYRFTHAQMEKDGIIVE 708
Cdd:pfam03836  81 ENCLDNLQKKKKK--LFSKQYFHYRKLQKRGKLPKFGSYKYSARQLYEKGVLLE 132
RasGAP_p120GAP cd05391
Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ...
141-464 1.11e-29

Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates hydrolysis of bound GTP to GDP. Once the Ras regulator p120GAP, a member of the GAP protein family, is recruited to the membrane, it is transiently immobilized to interact with Ras-GTP. The down-regulation of Ras by p120GAP is a critical step in the regulation of many cellular processes, which is disrupted in approximately 30% of human cancers. p120GAP contains SH2, SH3, PH, calcium- and lipid-binding domains, suggesting its involvement in a complex network of cellular interactions in vivo.


Pssm-ID: 213340  Cd Length: 328  Bit Score: 120.67  E-value: 1.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 141 LLQSEPRHIAALCRLVslAEIDTLLQTVMFTLYgnQYESREEHLLLTMFQSVLSAQFETATefgsLLRANTPVSRMMTTY 220
Cdd:cd05391    17 ILQKELHVVYALAHVC--GQDRTLLASILLRIF--RHEKLESLLLRTLNDREISMEDEATT----LFRATTLASTLMEQY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 221 TRrGPGQSYLKSVLAERINSLIEHKDlNLEINPLKVyeqmtnqieedtgslppnlprgvpaevaSENADVQAiiapRLTM 300
Cdd:cd05391    89 MK-ATATPFVHHALKDTILKILESKQ-SCELNPSKL----------------------------EKNEDVNT----NLEH 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 301 LMEIANSFLQTIINSIEEVPYGIRWICKQIRSLTKRKYPDATDLAIcSLIGGFFFLRFINPAIVTPQAYMLVDGPPAKHP 380
Cdd:cd05391   135 LLNILSELVEKIFMAAEILPPTLRYIYGCLQKSVQQKWPTNTTVRT-RVVSGFVFLRLICPAILNPRMFNIISETPSPTA 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 381 RRTLTLIAKMLQNLANKPSY-AKEQYMMSLEPFVENNKTRMNAFLNALCDVGDFYETLEmdqymaLSKKDLQIQI-TLNE 458
Cdd:cd05391   214 ARTLTLVAKSLQNLANLVEFgAKEPYMEGVNPFIKKNKERMIMFLDELGNVPELPDTTE------HSRTDLSRDLaALHE 287

                  ....*.
gi 1023177826 459 LYNTHS 464
Cdd:cd05391   288 ICVAHS 293
RasGAP_CLA2_BUD2 cd05137
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ...
202-428 3.23e-29

Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein (GAP) for BUD1/RSR1 and is necessary for proper bud-site selection in yeast. BUD2 has sequence similarity to the catalytic domain of RasGAPs, and stimulates the hydrolysis of BUD1-GTP to BUD1-GDP. Elimination of Bud2p activity by mutation causes a random budding pattern with no growth defect. Overproduction of Bud2p also alters the budding pattern.


Pssm-ID: 213339 [Multi-domain]  Cd Length: 356  Bit Score: 119.98  E-value: 3.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 202 EFGSLLRANTPVSRMMTTYTRRgPGQSYLKSVLAERINSLIEhKDLNLEINPLKVYEQMTNQIEEDTgslppnlprgvpa 281
Cdd:cd05137    91 EANLLFRGNSLLTKSLEKYMRR-IGKEYLEKSIGDVIRKICE-ENKDCEVDPSRVKESDSIEKEEDL------------- 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 282 evaseNADVQAiiaprltmLMEIANSFLQTIINSIEEVPYGIRWICKQIRSLTKRKYPDATDLAICSLIGGFFFLRFINP 361
Cdd:cd05137   156 -----EENWEN--------LISLTEEIWNSIYITSNDCPPELRKILKHIRAKVEDRYGDFLRTVTLNSVSGFLFLRFFCP 222
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1023177826 362 AIVTPQAYMLVDGPPAKHPRRTLTLIAKMLQNLANKPSYA-KEQYMMSLEPFVENNKTRMNAFLNALC 428
Cdd:cd05137   223 AILNPKLFGLLKDHPRPRAQRTLTLIAKVLQNLANLTTFGqKEPWMEPMNEFLTTHREELKDYIDKIT 290
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
151-482 6.40e-29

Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the neurofibromatosis type 1 gene (NF1) and shares a region of similarity with catalytic domain of the mammalian p120RasGAP protein and an extended similarity with the Saccharomyces cerevisiae RasGAP proteins Ira1 and Ira2. Neurofibromin has been shown to function as a GAP (GTPase-activating protein) which inhibits low molecular weight G proteins such as Ras by stimulating their intrinsic GTPase activity. NF1 is a common genetic disorder characterized by various symptoms ranging from predisposition for the development of tumors to learning disability or mental retardation. Loss of neurofibromin activity can be correlated to the increase in Ras-GTP concentration in neurofibromas of NF1 of patients, supporting the notion that unregulated Ras signaling may contribute to their development.


Pssm-ID: 213332 [Multi-domain]  Cd Length: 332  Bit Score: 118.19  E-value: 6.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 151 ALCRLVSLAEIDTLLQtVMFTLYgnqyESReeHLLLTMFQSVLSAQFETATEFGSLLRANTPVSRMMTtYTRRGPGQSYL 230
Cdd:cd05130    29 ALANVVPCSQMDELAR-VLVTLF----DSK--HLLYQLLWNMFSKEVELADSMQTLFRGNSLASKIMT-FCFKVYGATYL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 231 KSVLAERINSLIEHKD-LNLEINPLKVyeQMTNQIEEDTGSLppnlprgvpaevasenadvqaiiaprltmlMEIANSFL 309
Cdd:cd05130   101 QSLLEPLLRTMITSSEwVSYEVDPTRL--EGNENLEENQRNL------------------------------LQLTEKFF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 310 QTIINSIEEVPYGIRWICKQIRSLTKRKYPDATDLAICSLIggffFLRFINPAIVTPQAYMLVDGPPAKHPRRTLTLIAK 389
Cdd:cd05130   149 HAIISSSDEFPPQLRSVCHCLYQVVSHRFPNSGLGAVGSAI----FLRFINPAIVSPYEYGILDREPPPRVKRGLKLMSK 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 390 MLQNLANKPSYAKEQYMMSLEPFVENNKTRMNAFlnaLCDVGDFYETLE--MDQYMALskkdlqiqITLNELYNTHSLVA 467
Cdd:cd05130   225 ILQNIANHVLFTKEAHMLPFNDFLRNHFEAGRRF---FSSIASDCGAVDgpSSKYLSF--------INDANVLALHRLLW 293
                         330
                  ....*....|....*....
gi 1023177826 468 QHLDI----LAPNDKHHLR 482
Cdd:cd05130   294 NNQEKigqyLASSRDHKAV 312
RasGAP_IQGAP_related cd12206
Ras-GTPase Activating Domain of proteins related to IQGAPs; RasGAP: Ras-GTPase Activating ...
161-539 1.58e-23

Ras-GTPase Activating Domain of proteins related to IQGAPs; RasGAP: Ras-GTPase Activating Domain. RasGAP functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Proteins having a RasGAP domain include p120GAP, IQGAP, Rab5-activating protein 6, and Neurofibromin. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a myriad of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGap domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator.


Pssm-ID: 213345 [Multi-domain]  Cd Length: 359  Bit Score: 103.18  E-value: 1.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 161 IDTLLQTVMFTLyGNQYESREEHLLLTMFQSVLSAQFETATEFGSLLRANTPVSRMMTTYTRRGPGQSYLKSVLAERINS 240
Cdd:cd12206     8 VYVTLPIFQKPT-NGKMDSREEFLFIKFILELLKSDIENSNSNQDFLANSDNFWILLLVTFNNLRERSELKSIFGPLLVQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 241 LIEHKDLNLEINPLKVYEQMTNQIEEDtgslppnlprgvpAEVASENADVQAIIAPRLTMLMEIANSFLQTIINSIEEVP 320
Cdd:cd12206    87 YLENQEIDFESDPSVIYKSLHGRPPLS-------------SEEAIEDDRVSDKFVENLTNLREAVEMVAEIIFKNVDKIP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 321 YGIRWICKQIRSLTKRKYPDATDLAICSLIGGFFFLRFINPAIVTPQAYMLVDGppakHPRRTLTLIAKMLQNLANKPSY 400
Cdd:cd12206   154 VEIRYLCTKAYIAFADKFPDESEEDILRAISKILIKSYVAPILVNPENYGFVDN----EEDNLNEKARVLLQILSMVFFL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 401 AKEQ-YMMSLEPFVENNKTR-MNAFLNALCDVGDFYETLEMDQYMALSKKDLQIQITLNELYNTHSLVAQHLDILAPNDK 478
Cdd:cd12206   230 KNFDgYLKPLNQYIEEIKPSiRDLLKELLDVPEEEQEYDKLIYYDIMSTTRPCLEILLDKVIEIIQILKENLDEFTPDDQ 309
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1023177826 479 hhLRILIDELGGSPGQVPRKENRTLDLPLFSrweTPIQDLttafmseNNVTQNDILYMETK 539
Cdd:cd12206   310 --LVQLLEKIVDLSSSSNDKRSGRVTLELNP---SAYQFL-------VNDDKERKLYDQVK 358
RasGAP_RASAL cd05135
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...
200-430 1.67e-23

Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like protein (RASAL) or RASAL1 is a member of the GAP1 family, and a Ca2+ sensor responding in-phase to repetitive Ca2+ signals by associating with the plasma membrane and deactivating Ras. It contains a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. RASAL, like Ca2+ -promoted Ras inactivator (CAPRI, or RASAL4), is a cytosolic protein that undergoes a rapid translocation to the plasma membrane in response to receptor-mediated elevation in the concentration of intracellular free Ca2+, a translocation that activates its ability to function as a RasGAP. However, unlike RASAL4, RASAL undergoes an oscillatory translocation to the plasma membrane that occurs in synchrony with repetitive Ca2+ spikes.


Pssm-ID: 213337  Cd Length: 287  Bit Score: 101.43  E-value: 1.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 200 ATEFGSLLRANTPVSRMMTTYTRrGPGQSYLKSVLAERINSLIEHKDLnLEINPLKVyEQMTNQIEEDTGSLppnlprgv 279
Cdd:cd05135    72 TTDPNTLFRSNSLASKSMEQFMK-VVGMPYLHEVLKPVINRIFEEKKY-VELDPCKI-DLNRTRRISFKGSL-------- 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 280 paevaSENAdvqaIIAPRLTMLMEIANSFLQTIINSIEEVPYGIRWICKQIRSLTKRKYPDATDLAICSL-IGGFFFLRF 358
Cdd:cd05135   141 -----SEAQ----VRESSLELLQGYLGSIIDAIVGSVDQCPPVMRVAFKQLHKRVEERFPEAEHQDVKYLaISGFLFLRF 211
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1023177826 359 INPAIVTPQAYMLVDGPPAKHPRRTLTLIAKMLQ---NLANKPSYAKEQYMMSLEPFVENNKTRMNAFLNALCDV 430
Cdd:cd05135   212 FAPAILTPKLFQLREQHADPRTSRTLLLLAKAVQsigNLGLQLGQGKEQWMAPLHPFILQSVARVKDFLDRLIDI 286
RasGAP_RAP6 cd05129
Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is ...
135-427 4.45e-23

Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is an endosomal protein with a role in the regulation of receptor-mediated endocytosis. RAP6 contains a Vps9 domain, which is involved in the activation of Rab5, and a Ras GAP domain (RGD). Rab5 is a small GTPase required for the control of the endocytic route, and its activity is regulated by guanine nucleotide exchange factor, such as Rabex5, and GAPs, such as RN-tre. Human Rap6 protein is localized on the plasma membrane and on the endosome. RAP6 binds to Rab5 and Ras through the Vps9 and RGD domains, respectively.


Pssm-ID: 213331  Cd Length: 365  Bit Score: 101.65  E-value: 4.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 135 YGNFFFLLQSEPRHIAAL---CRLVSLAEIDTLLQTVMFTLYGNQYESREEHLLLTMFQSVLSAQFETATEFGSLLRANT 211
Cdd:cd05129    13 YGEFLRILRENPQLLAEClarGEKLSLEQTQNVIQTIVTSLYGNCIMPEDERLLLQLLRELMELQLKKSDNPRRLLRKGS 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 212 PVSRMMTTYTRRG--PGQSYLKSVLAERINSLIEHKDLNLEINPLKVYEQMT-NQIEEDTGSlppnlpRGVPAEvaseNA 288
Cdd:cd05129    93 CAFSRVFKLFTELlfSAKLYLTAALHKPIMQVLVDDEIFLETDPQKALCRFSpAEQEKRFGE------EGTPEQ----QR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 289 DVQAIIAPRLTMLMEIANSFLQTIINSIEEVPYGIRWICKQIRSLTKRKYpDATDLAICSLIGGFFFLRFINPAIVTPQA 368
Cdd:cd05129   163 KLQQYRAEFLSRLVALVNKFISSLRQSVYCFPQSLRWIVRQLRKILTRSG-DDEEAEARALCTDLLFTNFICPAIVNPEQ 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1023177826 369 YMLVDGPP----AKHprrTLTLIAKMLQNLA-NKPSYAKEQYMMSLEPFvenNKTRMNAFLNAL 427
Cdd:cd05129   242 YGIISDAPisevARH---NLMQVAQILQVLAlTEFESPDPRLKELLSKF---DKDCVSAFLDVV 299
RasGAP_GAP1_like cd05128
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...
205-430 1.04e-22

Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras GTPase-activating proteins includes GAP1(m) (or RASA2), GAP1_IP4BP (or RASA3), Ca2+ -promoted Ras inactivator (CAPRI, or RASAL4), and Ras GTPase activating-like proteins (RASAL) or RASAL1. The members are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin homology domain that is associated with a Bruton's tyrosine kinase motif. While this domain structure is conserved, a small change in the function of each individual domain and the interaction between domains has a marked effect on the regulation of each protein.


Pssm-ID: 213330  Cd Length: 269  Bit Score: 98.48  E-value: 1.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 205 SLLRANTPVSRMMTTYTRRGpGQSYLKSVLAERINSLIEHKdLNLEINPLKVyeqmtnqieEDTGSLPPNLprgvpaeva 284
Cdd:cd05128    72 TLFRGNSLASKCMDEFMKLV-GMQYLHETLKPVIDEIFSEK-KSCEIDPSKL---------KDGEVLETNL--------- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 285 sENadvqaiiaprLTMLMEIAnsfLQTIINSIEEVPYGIRWICKQIRSLTKRKYPDATDLAIcSLIGGFFFLRFINPAIV 364
Cdd:cd05128   132 -AN----------LRGYVERV---FKAITSSARRCPTLMCEIFSDLRESAAQRFPDNEDVPY-TAVSGFIFLRFFAPAIL 196
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1023177826 365 TPQAYMLVDGPPAKHPRRTLTLIAKMLQNLAN-----KPSYAKEQYMMSL--EPFVENNKTRMNAFLNALCDV 430
Cdd:cd05128   197 NPKLFGLREEHPDPQTARTLTLISKTIQTLGNlgsssSGLGVKEAYMSPLyeRFTDEQHVDAVKKFLDRISSV 269
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
207-424 2.33e-18

Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras GTPase-activating proteins includes DAB2IP, nGAP, and Syn GAP. Disabled 2 interactive protein, (DAB2IP; also known as ASK-interacting protein 1 (AIP1)), is a member of the GTPase-activating proteins, down-regulates Ras-mediated signal pathways, and mediates TNF-induced activation of ASK1-JNK signaling pathways. The mechanism by which TNF signaling is coupled to DAB2IP is not known.


Pssm-ID: 213338  Cd Length: 324  Bit Score: 86.87  E-value: 2.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 207 LRANTPVSRMMTTYTRRgPGQSYLKSVLAERINSLIEHKDlNLEINPLKVyeqmtnqieedtgslppnlprgVPAEVASE 286
Cdd:cd05136    79 FRGNTLATKAMEAYLKL-VGQKYLQETLGEFIRALYESEE-DCEVDPSKC----------------------PPSASLSR 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 287 NadvQAiiapRLTMLMEIAnsfLQTIINSIEEVPYGIRWICKQIR-SLTKRKYPDATDLAICSLIggffFLRFINPAIVT 365
Cdd:cd05136   135 N---QA----NLRRSVELA---WCKILSSHCVFPRELREVFSSWReRLEERGREDIADRLISASL----FLRFLCPAILS 200
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 366 PQAYMLVDGPPAKHPRRTLTLIAKMLQNLANKPSY-AKEQYMMSLEPFVENNKTRMNAFL 424
Cdd:cd05136   201 PSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFgGKEEYMEFMNDFVEQEWPNMKQFL 260
RasGAP_RASA4 cd05395
Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also ...
143-430 9.73e-14

Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also known as Ca2+ -promoted Ras inactivator (CAPRI), is a member of the GAP1 family. Members of the GAP1 family are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. RASAL4, like RASAL, is a cytosolic protein that undergoes a rapid translocation to the plasma membrane in response to a receptor-mediated elevation in the concentration of intracellular free Ca2+ ([Ca2+]i). However, unlike RASAL, RASAL4 does not sense oscillations in [Ca2+]i.


Pssm-ID: 213343 [Multi-domain]  Cd Length: 287  Bit Score: 72.60  E-value: 9.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 143 QSEPRHIAALCRLVSLAEIDTLLQTVMFTLYGNQYESREehLLLTMFQSVLSAQFETATefgsLLRANTPVSRMMTTYTR 222
Cdd:cd05395    21 QAGPVQLISLIDETTTAECRQEVATNLVKLFLGQGLAKE--FLDLLFQLELDKTTEPNT----LFRSNSLASKSMESFLK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 223 RGpGQSYLKSVLAERINSLIEHKDLnLEINPLKVyeqmtnQIEEDTGSlppNLPR-GVPAEVASENAdvqaiiaprlTML 301
Cdd:cd05395    95 VA-GMQYLHSVLGPTINRVFEEKKY-VELDPSKV------EIKDVGCS---GLHRiQTESEVIEQSA----------QLL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 302 MEIANSFLQTIINSIEEVPYGIRWICKQIRSLTKRKYPDATD-----LAICSliggFFFLRFINPAIVTPQAYMLVDGPP 376
Cdd:cd05395   154 QSYLGELLSAISKSVKYCPAVIRATFRQLFKRVQERFPENQHqnvkfIAVTS----FLCLRFFSPAIMSPKLFHLREKHA 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1023177826 377 AKHPRRTLTLIAKMLQNLANK---PSYAKEQYMMSLEPFVENNKTRMNAFLNALCDV 430
Cdd:cd05395   230 DARTSRTLLLLAKAVQNVGNMdtlASRAKEAWMAPLQPAIQQGVAQLKDFITKLVDI 286
RasGAP_RASA2 cd05394
Ras-GTPase Activating Domain of RASA2; RASA2 (or GAP1(m)) is a member of the GAP1 family of ...
183-406 8.42e-08

Ras-GTPase Activating Domain of RASA2; RASA2 (or GAP1(m)) is a member of the GAP1 family of Ras GTPase-activating proteins that includes GAP1_IP4BP (or RASA3), CAPRI, and RASAL. In vitro, RASA2 has been shown to bind inositol 1,3,4,5-tetrakisphosphate (IP4), the water soluble inositol head group of the lipid second messenger phosphatidylinositol 3,4,5-trisphosphate (PIP3). In vivo studies also demonstrated that RASA2 binds PIP3, and it is recruited to the plasma membrane following agonist stimulation of PI 3-kinase. Furthermore, the membrane translocation is a consequence of the ability of its pleckstrin homology (PH) domain to bind PIP3.


Pssm-ID: 213342  Cd Length: 272  Bit Score: 54.51  E-value: 8.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 183 HLLLTMFQSVLSAQFETATEFGSLLRANTPVSR----MMTTYtrrgpGQSYLKSVLAERINSLIEHKDlNLEINPLKVYE 258
Cdd:cd05394    50 NKLVPFVAAVAALDLKDTQEANTIFRGNSLATRcldeMMKIV-----GKHYLKVTLKPVLDEICESPK-PCEIDPIKLKE 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 259 qmtnqieedtgslppnlprGVPAEVASENadvqaiiaprltmLMEIANSFLQTIINSIEEVPYGIRWICKQIRSLTKRKY 338
Cdd:cd05394   124 -------------------GDNVENNKEN-------------LRYYVDKVFFSIVKSSMSCPTLMCDVFRSLRHLAVKRF 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1023177826 339 PDATDLAIcSLIGGFFFLRFINPAIVTPQAYMLVDGPPAKHPRRTLTLIAKMLQNLA-------NKPSYAKEQYM 406
Cdd:cd05394   172 PNDPHVQY-SAVSSFVFLRFFAVAVVSPHTFQLRPHHPDAQTSRTLTLISKTIQTLGswgslskSKLSSFKETFM 245
RasGAP_RASA3 cd05134
Ras-GTPase Activating Domain of RASA3; RASA3 (or GAP1_IP4BP) is a member of the GAP1 family ...
339-417 1.38e-07

Ras-GTPase Activating Domain of RASA3; RASA3 (or GAP1_IP4BP) is a member of the GAP1 family and has been shown to specifically bind 1,3,4,5-tetrakisphosphate (IP4). Thus, RASA3 may function as an IP4 receptor. The members of GAP1 family are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. Purified RASA3 stimulates GAP activity on Ras with about a five-fold lower potency than p120RasGAP, but shows no GAP-stimulating activity at all against Rac or Rab3A.


Pssm-ID: 213336  Cd Length: 269  Bit Score: 53.87  E-value: 1.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023177826 339 PDATDLAICSliggFFFLRFINPAIVTPQAYMLVDGPPAKHPRRTLTLIAKMLQNLA----NKPSYAKEQYMMSLEPFVE 414
Cdd:cd05134   175 PDVRYTAVSS----FIFLRFFAPAILSPNLFQLTPHHPDPQTSRTLTLISKTIQTLGslskSKSANFKESYMAAFYDYFN 250

                  ...
gi 1023177826 415 NNK 417
Cdd:cd05134   251 EQK 253
 
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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