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Conserved domains on  [gi|19114772|ref|NP_593860|]
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IQ motif containing GTPase activating protein [Schizosaccharomyces pombe]

Protein Classification

Ras GTPase-activating protein( domain architecture ID 11474206)

Ras GTPase-activating protein accelerates the GTPase activity of Ras

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
1-1489 0e+00

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: 1140.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772    1 MDVNVG-LSRLQSQAGAPVGTKGSN-TRLAAKQRETLQAYDYLCRVDEAKKWIEECLGTDLgPTSTFEQSLRNGVVLALL 78
Cdd:COG5261    1 MTAYSGsLNRYVENLGRPIGTPSHLkTKTSAKNRSALRAYEYLCRVSEAKIWIEEVIEEAL-PELCFEDSLRNGVFLAKL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   79 VQKFQPDKLIKIFYSNELQFRHSDNINKFLDFIHGIGLPEIFHFELTDIYEGKNLPKVIYCIHALSYFLSMQDLAPpLIK 158
Cdd:COG5261   80 TQRFNPDLTTVIFPADKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTP-LIN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  159 SDENLSFTDEDVSIIVRRLRQsnviLPNFKALSADFMLRASPVSSRTPSPTRFPKHARFQTLNSSDSASIYSsPYTSPTL 238
Cdd:COG5261  159 SSGQISFTKEDIAACKKAWPR----IPDFKSLGTNINTAASPEEPKEKRSGLIKKFAKFQRPNIPVESILIT-PRKSITD 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  239 EFSKkdasARSDILKMhrrtksatpSLEQFnePYKQtlpsHSIEFEDSFFQPPSqkghmqrsfLTTFSapTRRREALFST 318
Cdd:COG5261  234 ANCS----TPSDYLKA---------TLKRF--PYKR----HSGTLEDSVLPQTS---------LSLFS--TRRSTSVFYT 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  319 TSglsqrspvDEKIVNAIQACGRgvlVRLRLVDMLQSLVEQSSSVVLLQAVIRgyisrntYRIRKkaydelvnwvtsiqs 398
Cdd:COG5261  284 IS--------LEMISNVEQAFFH---LDRELHRLKQSISSQSKQVVVLERDIR-------LLIQK--------------- 330
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  399 isRAYLIRAQYRKVVLQEEATKSIQTLQSIIRGgfyRRKYHSLIERLDLFTPSFVLIQssalgfltrhaivnmldnlyNY 478
Cdd:COG5261  331 --RGNKIRLLIQNRMPQEEDTKFAERLQSNING---RKKYFPLDRRLSLFGPLFFLLQ--------------------SS 385
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  479 IPLFNrmqsilranmfrnewsnfldsvqsfpvsfHSICKGRLIRDSINrlngsllgELDNFIKLQNLSRGFMIRrafkeK 558
Cdd:COG5261  386 IPLFS-----------------------------IAICVGRVKRFSID--------ALLNIVKLQILGNGYEIR-----K 423
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  559 LEKLKASTSsfialqaivrafllrknlesiydsfqKSHLSVIKAQSLYRgfitrtkidycndyllkrlpdivfmqsavra 638
Cdd:COG5261  424 LYSLGKSNC--------------------------EEHLSVSLFQMLLR------------------------------- 446
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  639 illrddvnyTEVQLDSfipeivLLQSLIRGYLSrnkfsrklqnFHKNMENpivaksIFRGRQEGLAYRElataknppvmt 718
Cdd:COG5261  447 ---------TEVEATS------LVQSLLRGNLP----------VHRNMTN------YFRRSQGQAALRE----------- 484
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  719 vknfvhllddtnfdfeeevllekMRKEIVQQVRDNEEIEVHINELDVKIALLVKNKISLDDVLKHHnkykfgkQSTEYLK 798
Cdd:COG5261  485 -----------------------IRYQIINDVAIHEDLEVDINPLLVYRALLNKGQLSPDKDLELL-------TSNEEVS 534
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  799 INTLSMKSLNNSSRKFLELyqcffyvlqtnemylanyfqalktegtSSVKIRHAVYLVLQIFGHGsnrreevllLRFISQ 878
Cdd:COG5261  535 EFLAVMNAVQESSAKLLEL---------------------------STERILDAVYNSLDEIGYG---------IRFVCE 578
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  879 VIKLEaalvnssqdllsddcvwkllftgyrgdvrevklwktilgrihkvlvadnhldFEINPLTLFKSFnpevasqtdsp 958
Cdd:COG5261  579 LIRVV----------------------------------------------------FELTPNRLFPSI----------- 595
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  959 kltlslamqhpptrnlyvSRLRELRKLCqsFLVAlsknienipyalcytaaqlknslqryfpaahkeEIFGVIGKFVYWA 1038
Cdd:COG5261  596 ------------------SDSRCLRTIC--FAEI---------------------------------DSLGLIGGFFFLR 622
                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1039 YVAPVLVSPDNFKLVDGSITALQRKnLYTLSSILSEIFSIESCDskqlGFFRPLSEFIEVSKQDTMLMLERLVDVVDPEV 1118
Cdd:COG5261  623 FVNEALVSPQTSMLKDSCPSDNVRK-LATLSKILQSVFEITSSD----KFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEE 697
                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1119 YFEFDAFEDLVNTKRPVIYMKRDDILGIYSSIAYVIDSIAPPDVNDPLRAVVNSLgPVSEQDndfvQDETDVKLELNPKF 1198
Cdd:COG5261  698 YFEFDQYIDLVKKSRALEYLVNEIYLTHEIIIEYLDNLYDPDSLVDLLLQELGEL-CSFPQD----QRDTLNCLVTLPLF 772
                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1199 CTIENPvaqERTLIVQTKRYILFIIRIQNGLNLLEILVKpVTDSDEAAWQNLLAEEseKNARNyDLFDDSIFSMSFAELK 1278
Cdd:COG5261  773 NRSDDP---IRDLKQQLKRTRVYIIYVDAGTNLFEQLLR-LLPSDEPATRNPLDLN--PNIRD-DPSVSSLKSMSLMKLK 845
                       1290      1300      1310      1320      1330      1340      1350      1360
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1279 YTALSNIVEMEKLGFANRRNNYQDMVNSIALDIRNKSRRRMQRQRELDAGHQSLLNLREKRAFLDSQLKSYNEYIEQAME 1358
Cdd:COG5261  846 IRAIELLDELETLGFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARS 925
                       1370      1380      1390      1400      1410      1420      1430      1440
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1359 TLQSKkgKKKLIPFSKQYFHMRDLRKSGrvpRFGSFKYPALKLYDRGVLVSISHM-PQKEKLYITISADEVGKFILEATS 1437
Cdd:COG5261  926 QLQPK--KSKLKGFSRGVGVVRDKPKSI---SSGTFKYSAQQLYKRGVLVNITIPePNVSNIYFTFSSDSTDNFVIEVYQ 1000
                       1450      1460      1470      1480      1490
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19114772 1438 PTVKVSSPRCELHLDDLLSAQYNKVLTLDVLdGRLKLNTNMFLHLIFSKFYS 1489
Cdd:COG5261 1001 PGHSVSLPEVSFCFDDLLKRQYNKNPVVDLG-GFLTFNANKLLHLIESKFYR 1051
 
Name Accession Description Interval E-value
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
1-1489 0e+00

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: 1140.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772    1 MDVNVG-LSRLQSQAGAPVGTKGSN-TRLAAKQRETLQAYDYLCRVDEAKKWIEECLGTDLgPTSTFEQSLRNGVVLALL 78
Cdd:COG5261    1 MTAYSGsLNRYVENLGRPIGTPSHLkTKTSAKNRSALRAYEYLCRVSEAKIWIEEVIEEAL-PELCFEDSLRNGVFLAKL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   79 VQKFQPDKLIKIFYSNELQFRHSDNINKFLDFIHGIGLPEIFHFELTDIYEGKNLPKVIYCIHALSYFLSMQDLAPpLIK 158
Cdd:COG5261   80 TQRFNPDLTTVIFPADKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTP-LIN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  159 SDENLSFTDEDVSIIVRRLRQsnviLPNFKALSADFMLRASPVSSRTPSPTRFPKHARFQTLNSSDSASIYSsPYTSPTL 238
Cdd:COG5261  159 SSGQISFTKEDIAACKKAWPR----IPDFKSLGTNINTAASPEEPKEKRSGLIKKFAKFQRPNIPVESILIT-PRKSITD 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  239 EFSKkdasARSDILKMhrrtksatpSLEQFnePYKQtlpsHSIEFEDSFFQPPSqkghmqrsfLTTFSapTRRREALFST 318
Cdd:COG5261  234 ANCS----TPSDYLKA---------TLKRF--PYKR----HSGTLEDSVLPQTS---------LSLFS--TRRSTSVFYT 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  319 TSglsqrspvDEKIVNAIQACGRgvlVRLRLVDMLQSLVEQSSSVVLLQAVIRgyisrntYRIRKkaydelvnwvtsiqs 398
Cdd:COG5261  284 IS--------LEMISNVEQAFFH---LDRELHRLKQSISSQSKQVVVLERDIR-------LLIQK--------------- 330
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  399 isRAYLIRAQYRKVVLQEEATKSIQTLQSIIRGgfyRRKYHSLIERLDLFTPSFVLIQssalgfltrhaivnmldnlyNY 478
Cdd:COG5261  331 --RGNKIRLLIQNRMPQEEDTKFAERLQSNING---RKKYFPLDRRLSLFGPLFFLLQ--------------------SS 385
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  479 IPLFNrmqsilranmfrnewsnfldsvqsfpvsfHSICKGRLIRDSINrlngsllgELDNFIKLQNLSRGFMIRrafkeK 558
Cdd:COG5261  386 IPLFS-----------------------------IAICVGRVKRFSID--------ALLNIVKLQILGNGYEIR-----K 423
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  559 LEKLKASTSsfialqaivrafllrknlesiydsfqKSHLSVIKAQSLYRgfitrtkidycndyllkrlpdivfmqsavra 638
Cdd:COG5261  424 LYSLGKSNC--------------------------EEHLSVSLFQMLLR------------------------------- 446
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  639 illrddvnyTEVQLDSfipeivLLQSLIRGYLSrnkfsrklqnFHKNMENpivaksIFRGRQEGLAYRElataknppvmt 718
Cdd:COG5261  447 ---------TEVEATS------LVQSLLRGNLP----------VHRNMTN------YFRRSQGQAALRE----------- 484
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  719 vknfvhllddtnfdfeeevllekMRKEIVQQVRDNEEIEVHINELDVKIALLVKNKISLDDVLKHHnkykfgkQSTEYLK 798
Cdd:COG5261  485 -----------------------IRYQIINDVAIHEDLEVDINPLLVYRALLNKGQLSPDKDLELL-------TSNEEVS 534
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  799 INTLSMKSLNNSSRKFLELyqcffyvlqtnemylanyfqalktegtSSVKIRHAVYLVLQIFGHGsnrreevllLRFISQ 878
Cdd:COG5261  535 EFLAVMNAVQESSAKLLEL---------------------------STERILDAVYNSLDEIGYG---------IRFVCE 578
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  879 VIKLEaalvnssqdllsddcvwkllftgyrgdvrevklwktilgrihkvlvadnhldFEINPLTLFKSFnpevasqtdsp 958
Cdd:COG5261  579 LIRVV----------------------------------------------------FELTPNRLFPSI----------- 595
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  959 kltlslamqhpptrnlyvSRLRELRKLCqsFLVAlsknienipyalcytaaqlknslqryfpaahkeEIFGVIGKFVYWA 1038
Cdd:COG5261  596 ------------------SDSRCLRTIC--FAEI---------------------------------DSLGLIGGFFFLR 622
                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1039 YVAPVLVSPDNFKLVDGSITALQRKnLYTLSSILSEIFSIESCDskqlGFFRPLSEFIEVSKQDTMLMLERLVDVVDPEV 1118
Cdd:COG5261  623 FVNEALVSPQTSMLKDSCPSDNVRK-LATLSKILQSVFEITSSD----KFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEE 697
                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1119 YFEFDAFEDLVNTKRPVIYMKRDDILGIYSSIAYVIDSIAPPDVNDPLRAVVNSLgPVSEQDndfvQDETDVKLELNPKF 1198
Cdd:COG5261  698 YFEFDQYIDLVKKSRALEYLVNEIYLTHEIIIEYLDNLYDPDSLVDLLLQELGEL-CSFPQD----QRDTLNCLVTLPLF 772
                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1199 CTIENPvaqERTLIVQTKRYILFIIRIQNGLNLLEILVKpVTDSDEAAWQNLLAEEseKNARNyDLFDDSIFSMSFAELK 1278
Cdd:COG5261  773 NRSDDP---IRDLKQQLKRTRVYIIYVDAGTNLFEQLLR-LLPSDEPATRNPLDLN--PNIRD-DPSVSSLKSMSLMKLK 845
                       1290      1300      1310      1320      1330      1340      1350      1360
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1279 YTALSNIVEMEKLGFANRRNNYQDMVNSIALDIRNKSRRRMQRQRELDAGHQSLLNLREKRAFLDSQLKSYNEYIEQAME 1358
Cdd:COG5261  846 IRAIELLDELETLGFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARS 925
                       1370      1380      1390      1400      1410      1420      1430      1440
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1359 TLQSKkgKKKLIPFSKQYFHMRDLRKSGrvpRFGSFKYPALKLYDRGVLVSISHM-PQKEKLYITISADEVGKFILEATS 1437
Cdd:COG5261  926 QLQPK--KSKLKGFSRGVGVVRDKPKSI---SSGTFKYSAQQLYKRGVLVNITIPePNVSNIYFTFSSDSTDNFVIEVYQ 1000
                       1450      1460      1470      1480      1490
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19114772 1438 PTVKVSSPRCELHLDDLLSAQYNKVLTLDVLdGRLKLNTNMFLHLIFSKFYS 1489
Cdd:COG5261 1001 PGHSVSLPEVSFCFDDLLKRQYNKNPVVDLG-GFLTFNANKLLHLIESKFYR 1051
RasGAP_IQGAP_related cd12206
Ras-GTPase Activating Domain of proteins related to IQGAPs; RasGAP: Ras-GTPase Activating ...
846-1217 2.62e-93

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: 306.18  E-value: 2.62e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  846 SVKIRHAVYLVLQIF----GHGSNRREEVLLLRFISQVIKLEAALVNSSQDLL-SDDCVWKLLFTGYRGDvREVKLWKTI 920
Cdd:cd12206    1 SEFIEKNVYVTLPIFqkptNGKMDSREEFLFIKFILELLKSDIENSNSNQDFLaNSDNFWILLLVTFNNL-RERSELKSI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  921 LGRIHKVLVADNHLDFEINPLTLFKSFNPevasqtdSPKLTLSLAMQHPPTRNLYVSRLRELRKLCQSFLVALSKNIENI 1000
Cdd:cd12206   80 FGPLLVQYLENQEIDFESDPSVIYKSLHG-------RPPLSSEEAIEDDRVSDKFVENLTNLREAVEMVAEIIFKNVDKI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1001 PYALCYTAAQLKNSLQRYFPAAHKEEIFGVIGKFVYWAYVAPVLVSPDNFKLVDGsitalQRKNLYTLSSILSEIFSIES 1080
Cdd:cd12206  153 PVEIRYLCTKAYIAFADKFPDESEEDILRAISKILIKSYVAPILVNPENYGFVDN-----EEDNLNEKARVLLQILSMVF 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1081 CDSKQLGFFRPLSEFIEVSKQDTMLMLERLVDVVDPEVYFEFDAFEDLVNTKRPVIYMKRDDILGIYSSIAYVIDSIAPp 1160
Cdd:cd12206  228 FLKNFDGYLKPLNQYIEEIKPSIRDLLKELLDVPEEEQEYDKLIYYDIMSTTRPCLEILLDKVIEIIQILKENLDEFTP- 306
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 19114772 1161 dvNDPLRAVVNSLGPVSEQDNDfvQDETDVKLELNPKFCTIENPVAQERTLIVQTKR 1217
Cdd:cd12206  307 --DDQLVQLLEKIVDLSSSSND--KRSGRVTLELNPSAYQFLVNDDKERKLYDQVKR 359
RasGAP_C pfam03836
RasGAP C-terminus; This domain can be found in the C terminus of the IQGAP family members, ...
1274-1414 6.12e-53

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: 181.98  E-value: 6.12e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   1274 FAELKYTALSNIVEMEKLGFANRRNNYQDMVNSIALDIRNKSRRRMQRQRELDAGHQSLLNLREKRAFLDSQLKSYNEYI 1353
Cdd:pfam03836    1 YVELKKKALENLLELESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYI 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114772   1354 EQAMETLQSKKGKKklipFSKQYFHMRDLRKSGRVPRFGSFKYPALKLYDRGVLVSISHMP 1414
Cdd:pfam03836   81 ENCLDNLQKKKKKL----FSKQYFHYRKLQKRGKLPKFGSYKYSARQLYEKGVLLEIEGVP 137
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
978-1130 1.65e-16

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: 82.74  E-value: 1.65e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772     978 RLRELRKLCQSFLVALSKNIENIPYALCYTAAQLKNSLQRYFPAAHkeEIFGVIGKFVYWAYVAPVLVSPDNFKLVDGSI 1057
Cdd:smart00323  148 NLENLLQYVERLFDAIINSSDRLPYGLRDICKQLRQAAEKRFPDAD--VIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHP 225
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19114772    1058 TALQRKNLYTLSSILSEIFSIESCDSKQlGFFRPLSEFIEVSKQDTMLMLERLVDVVDPEVYFEFDAFEDLVN 1130
Cdd:smart00323  226 DPTTRRTLTLIAKVLQNLANLSEFGSKE-PWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDSTTISGR 297
 
Name Accession Description Interval E-value
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
1-1489 0e+00

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: 1140.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772    1 MDVNVG-LSRLQSQAGAPVGTKGSN-TRLAAKQRETLQAYDYLCRVDEAKKWIEECLGTDLgPTSTFEQSLRNGVVLALL 78
Cdd:COG5261    1 MTAYSGsLNRYVENLGRPIGTPSHLkTKTSAKNRSALRAYEYLCRVSEAKIWIEEVIEEAL-PELCFEDSLRNGVFLAKL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   79 VQKFQPDKLIKIFYSNELQFRHSDNINKFLDFIHGIGLPEIFHFELTDIYEGKNLPKVIYCIHALSYFLSMQDLAPpLIK 158
Cdd:COG5261   80 TQRFNPDLTTVIFPADKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTP-LIN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  159 SDENLSFTDEDVSIIVRRLRQsnviLPNFKALSADFMLRASPVSSRTPSPTRFPKHARFQTLNSSDSASIYSsPYTSPTL 238
Cdd:COG5261  159 SSGQISFTKEDIAACKKAWPR----IPDFKSLGTNINTAASPEEPKEKRSGLIKKFAKFQRPNIPVESILIT-PRKSITD 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  239 EFSKkdasARSDILKMhrrtksatpSLEQFnePYKQtlpsHSIEFEDSFFQPPSqkghmqrsfLTTFSapTRRREALFST 318
Cdd:COG5261  234 ANCS----TPSDYLKA---------TLKRF--PYKR----HSGTLEDSVLPQTS---------LSLFS--TRRSTSVFYT 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  319 TSglsqrspvDEKIVNAIQACGRgvlVRLRLVDMLQSLVEQSSSVVLLQAVIRgyisrntYRIRKkaydelvnwvtsiqs 398
Cdd:COG5261  284 IS--------LEMISNVEQAFFH---LDRELHRLKQSISSQSKQVVVLERDIR-------LLIQK--------------- 330
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  399 isRAYLIRAQYRKVVLQEEATKSIQTLQSIIRGgfyRRKYHSLIERLDLFTPSFVLIQssalgfltrhaivnmldnlyNY 478
Cdd:COG5261  331 --RGNKIRLLIQNRMPQEEDTKFAERLQSNING---RKKYFPLDRRLSLFGPLFFLLQ--------------------SS 385
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  479 IPLFNrmqsilranmfrnewsnfldsvqsfpvsfHSICKGRLIRDSINrlngsllgELDNFIKLQNLSRGFMIRrafkeK 558
Cdd:COG5261  386 IPLFS-----------------------------IAICVGRVKRFSID--------ALLNIVKLQILGNGYEIR-----K 423
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  559 LEKLKASTSsfialqaivrafllrknlesiydsfqKSHLSVIKAQSLYRgfitrtkidycndyllkrlpdivfmqsavra 638
Cdd:COG5261  424 LYSLGKSNC--------------------------EEHLSVSLFQMLLR------------------------------- 446
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  639 illrddvnyTEVQLDSfipeivLLQSLIRGYLSrnkfsrklqnFHKNMENpivaksIFRGRQEGLAYRElataknppvmt 718
Cdd:COG5261  447 ---------TEVEATS------LVQSLLRGNLP----------VHRNMTN------YFRRSQGQAALRE----------- 484
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  719 vknfvhllddtnfdfeeevllekMRKEIVQQVRDNEEIEVHINELDVKIALLVKNKISLDDVLKHHnkykfgkQSTEYLK 798
Cdd:COG5261  485 -----------------------IRYQIINDVAIHEDLEVDINPLLVYRALLNKGQLSPDKDLELL-------TSNEEVS 534
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  799 INTLSMKSLNNSSRKFLELyqcffyvlqtnemylanyfqalktegtSSVKIRHAVYLVLQIFGHGsnrreevllLRFISQ 878
Cdd:COG5261  535 EFLAVMNAVQESSAKLLEL---------------------------STERILDAVYNSLDEIGYG---------IRFVCE 578
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  879 VIKLEaalvnssqdllsddcvwkllftgyrgdvrevklwktilgrihkvlvadnhldFEINPLTLFKSFnpevasqtdsp 958
Cdd:COG5261  579 LIRVV----------------------------------------------------FELTPNRLFPSI----------- 595
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  959 kltlslamqhpptrnlyvSRLRELRKLCqsFLVAlsknienipyalcytaaqlknslqryfpaahkeEIFGVIGKFVYWA 1038
Cdd:COG5261  596 ------------------SDSRCLRTIC--FAEI---------------------------------DSLGLIGGFFFLR 622
                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1039 YVAPVLVSPDNFKLVDGSITALQRKnLYTLSSILSEIFSIESCDskqlGFFRPLSEFIEVSKQDTMLMLERLVDVVDPEV 1118
Cdd:COG5261  623 FVNEALVSPQTSMLKDSCPSDNVRK-LATLSKILQSVFEITSSD----KFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEE 697
                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1119 YFEFDAFEDLVNTKRPVIYMKRDDILGIYSSIAYVIDSIAPPDVNDPLRAVVNSLgPVSEQDndfvQDETDVKLELNPKF 1198
Cdd:COG5261  698 YFEFDQYIDLVKKSRALEYLVNEIYLTHEIIIEYLDNLYDPDSLVDLLLQELGEL-CSFPQD----QRDTLNCLVTLPLF 772
                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1199 CTIENPvaqERTLIVQTKRYILFIIRIQNGLNLLEILVKpVTDSDEAAWQNLLAEEseKNARNyDLFDDSIFSMSFAELK 1278
Cdd:COG5261  773 NRSDDP---IRDLKQQLKRTRVYIIYVDAGTNLFEQLLR-LLPSDEPATRNPLDLN--PNIRD-DPSVSSLKSMSLMKLK 845
                       1290      1300      1310      1320      1330      1340      1350      1360
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1279 YTALSNIVEMEKLGFANRRNNYQDMVNSIALDIRNKSRRRMQRQRELDAGHQSLLNLREKRAFLDSQLKSYNEYIEQAME 1358
Cdd:COG5261  846 IRAIELLDELETLGFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARS 925
                       1370      1380      1390      1400      1410      1420      1430      1440
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1359 TLQSKkgKKKLIPFSKQYFHMRDLRKSGrvpRFGSFKYPALKLYDRGVLVSISHM-PQKEKLYITISADEVGKFILEATS 1437
Cdd:COG5261  926 QLQPK--KSKLKGFSRGVGVVRDKPKSI---SSGTFKYSAQQLYKRGVLVNITIPePNVSNIYFTFSSDSTDNFVIEVYQ 1000
                       1450      1460      1470      1480      1490
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19114772 1438 PTVKVSSPRCELHLDDLLSAQYNKVLTLDVLdGRLKLNTNMFLHLIFSKFYS 1489
Cdd:COG5261 1001 PGHSVSLPEVSFCFDDLLKRQYNKNPVVDLG-GFLTFNANKLLHLIESKFYR 1051
RasGAP_IQGAP_related cd12206
Ras-GTPase Activating Domain of proteins related to IQGAPs; RasGAP: Ras-GTPase Activating ...
846-1217 2.62e-93

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: 306.18  E-value: 2.62e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  846 SVKIRHAVYLVLQIF----GHGSNRREEVLLLRFISQVIKLEAALVNSSQDLL-SDDCVWKLLFTGYRGDvREVKLWKTI 920
Cdd:cd12206    1 SEFIEKNVYVTLPIFqkptNGKMDSREEFLFIKFILELLKSDIENSNSNQDFLaNSDNFWILLLVTFNNL-RERSELKSI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  921 LGRIHKVLVADNHLDFEINPLTLFKSFNPevasqtdSPKLTLSLAMQHPPTRNLYVSRLRELRKLCQSFLVALSKNIENI 1000
Cdd:cd12206   80 FGPLLVQYLENQEIDFESDPSVIYKSLHG-------RPPLSSEEAIEDDRVSDKFVENLTNLREAVEMVAEIIFKNVDKI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1001 PYALCYTAAQLKNSLQRYFPAAHKEEIFGVIGKFVYWAYVAPVLVSPDNFKLVDGsitalQRKNLYTLSSILSEIFSIES 1080
Cdd:cd12206  153 PVEIRYLCTKAYIAFADKFPDESEEDILRAISKILIKSYVAPILVNPENYGFVDN-----EEDNLNEKARVLLQILSMVF 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1081 CDSKQLGFFRPLSEFIEVSKQDTMLMLERLVDVVDPEVYFEFDAFEDLVNTKRPVIYMKRDDILGIYSSIAYVIDSIAPp 1160
Cdd:cd12206  228 FLKNFDGYLKPLNQYIEEIKPSIRDLLKELLDVPEEEQEYDKLIYYDIMSTTRPCLEILLDKVIEIIQILKENLDEFTP- 306
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 19114772 1161 dvNDPLRAVVNSLGPVSEQDNDfvQDETDVKLELNPKFCTIENPVAQERTLIVQTKR 1217
Cdd:cd12206  307 --DDQLVQLLEKIVDLSSSSND--KRSGRVTLELNPSAYQFLVNDDKERKLYDQVKR 359
CH_IQGAP cd21206
calponin homology (CH) domain found in the IQ motif containing GTPase activating protein ...
35-151 1.59e-57

calponin homology (CH) domain found in the IQ motif containing GTPase activating protein family; Members of the IQ motif containing GTPase activating protein (IQGAP) family are associated with the Ras GTP-binding protein and act as essential regulators of cytoskeletal function. There are three known IQGAP family members: IQGAP1, IQGAP2, and IQGAP3. They 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. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity. It lacks GAP activity. Both IQGAP1 and IQGAP2 specifically bind to Cdc42 and Rac1, but not to RhoA. Despite similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP3 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: 409055 [Multi-domain]  Cd Length: 118  Bit Score: 193.98  E-value: 1.59e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   35 LQAYDYLCRVDEAKKWIEECLGTDLGPTSTFEQSLRNGVVLALLVQKFQPDKLIKIF-YSNELQFRHSDNINKFLDFIHG 113
Cdd:cd21206    1 TIAYEYLCRLEEAKQWIEACLNEELPPTTEFEEELRNGVVLAKLANKFAPKLVPLKKiYDVGLQFRHTDNINHFLRALKK 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 19114772  114 IGLPEIFHFELTDIYEGKNLPKVIYCIHALSYFLSMQD 151
Cdd:cd21206   81 IGLPKIFHFETTDLYEKKNIPKVIYCLHALSLLLFKLG 118
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
863-1182 1.41e-55

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: 197.04  E-value: 1.41e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  863 GSNRREEVLLLRFISQVIKLE-AALVNSSQDLLSDDCVW-KLLFTGYRGDvREVKLWKTILGRIHKVLVADNHLDFEINP 940
Cdd:cd05127    1 ASNRREEYLLLKLFKTALREEiESKVSLPEDIVTGNPTViKLVVNYNRGP-RGQKYLRELLGPVVKEILDDDDLDLETDP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  941 LTLFKSFNPEVASQTDSP-KLTLSL----AMQHPPTRNLYVSRLRELRKLCQSFLVALSKNIENIPYALCYTAAQLKNSL 1015
Cdd:cd05127   80 VDIYKAWINQEESRTGEPsKLPYDVtreqALKDPEVRKRLIEHLEKLRAITDKFLTAITESLDKMPYGMRYIAKVLKEAL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1016 QRYFPAAHKEEIFGVIGKFVYWAYVAPVLVSPDNFKLVD----GSITALQRKNLYTLSSILSEI-----FSIEScdskql 1086
Cdd:cd05127  160 REKFPDAPEEEILKIVGNLLYYRYMNPAIVAPEAFDIIDlsvgGQLSPLQRRNLGSIAKVLQQAasgklFGGEN------ 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1087 GFFRPLSEFIEVSKQDTMLMLERLVDVVDPEVYFEFDAFEDLVNTKRPVIYMKRDDILGIYSSIAYVIDSIApPDVNDPL 1166
Cdd:cd05127  234 PYLSPLNPYISESHEKFKKFFLEACTVPEAEEHFNIDEYSDLTMLTKPTIYISLQEIFATHKLLLEHQDEIA-PDPDDPL 312
                        330
                 ....*....|....*.
gi 19114772 1167 RAVVNSLGPVSEQDND 1182
Cdd:cd05127  313 RELLDDLGPAPTIESL 328
RasGAP_C pfam03836
RasGAP C-terminus; This domain can be found in the C terminus of the IQGAP family members, ...
1274-1414 6.12e-53

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: 181.98  E-value: 6.12e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   1274 FAELKYTALSNIVEMEKLGFANRRNNYQDMVNSIALDIRNKSRRRMQRQRELDAGHQSLLNLREKRAFLDSQLKSYNEYI 1353
Cdd:pfam03836    1 YVELKKKALENLLELESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYI 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114772   1354 EQAMETLQSKKGKKklipFSKQYFHMRDLRKSGRVPRFGSFKYPALKLYDRGVLVSISHMP 1414
Cdd:pfam03836   81 ENCLDNLQKKKKKL----FSKQYFHYRKLQKRGKLPKFGSYKYSARQLYEKGVLLEIEGVP 137
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
875-1077 2.21e-47

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: 168.62  E-value: 2.21e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772    875 FISQVIKLEAALVNSSQDLLSDDCVWKLLFTGY-RGDVREVKLWKTILGRIHKVlVADNHLDFEINPLTLFKSFNPEVAS 953
Cdd:pfam00616    1 LISELIEEEIESSDNPNDLLRGNSLVSKLLETYnRRPRGQEYLKKVLGPLVRKI-IEDEDLDLESDPRKIYESLINQEEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772    954 QTD----SPKLTLSLAMQHPPTRNLYVSRLRELRKLCQSFLVALSKNIENIPYALCYTAAQLKNSLQRYFPAAHKEEIFG 1029
Cdd:pfam00616   80 KTGrsdlPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEILN 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 19114772   1030 VIGKFVYWAYVAPVLVSPDNFKLVDGSITALQRKNLYTLSSILSEIFS 1077
Cdd:pfam00616  160 AIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
RasGAP_IQGAP2 cd05131
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...
855-1181 2.04e-42

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: 159.78  E-value: 2.04e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  855 LVLQIFGHGSNRREEVLLLRFISQVIKLE-AALVNSSQDLLSDD-CVWKLLFTGYRGdVREVKLWKTILGRIHKVLVADN 932
Cdd:cd05131    3 VIFTLYNYASNQREEYLLLKLFETALEEEiKSKVDQIQDIVTGNpTVIKMVVSFNRG-ARGQNTLRQLLAPVVKEIIEDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  933 HLDFEINPLTLFKSFNPEVASQT-DSPKL----TLSLAMQHPPTRNLYVSRLRELRKLCQSFLVALSKNIENIPYALCYT 1007
Cdd:cd05131   82 SLIINTNPVEVYKAWVNQLETATgEASKLpydvTTEQALTHPEVVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRYI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1008 AAQLKNSLQRYFPAAHKEEIFGVIGKFVYWAYVAPVLVSPDNFKLVD----GSITALQRKNLYTLSSILSEIFSIESCDS 1083
Cdd:cd05131  162 AKVLKNSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQIHSEQRRNLGSVAKVLQHAASNKLFEG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1084 KQlGFFRPLSEFIEVSKQDTMLMLERLVDVVDPEVYFEFDAFEDLVNTKRPVIYMKRDDILGIYSSIAYVIDSIApPDVN 1163
Cdd:cd05131  242 EN-AHLSSMNSYLSQTYQKFRKFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIA-PDQN 319
                        330
                 ....*....|....*...
gi 19114772 1164 DPLRAVVNSLGPVSEQDN 1181
Cdd:cd05131  320 DLLHELLKDLGEVPDVES 337
CH_IQGAP3 cd21276
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP3; IQ motif ...
37-177 4.23e-42

calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP3; IQ motif containing GTPase activating protein 3 (IQGAP3) associates with Ras GTP-binding proteins. It 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. It belongs to the IQGAP family, which consists of multi-domain proteins 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. IQGAP3 contains a single copy of the CH domain at the N-terminus.


Pssm-ID: 409125 [Multi-domain]  Cd Length: 152  Bit Score: 151.28  E-value: 4.23e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   37 AYDYLCRVDEAKKWIEECLGTDLGPTSTFEQSLRNGVVLALLVQKFQPDKL-IKIFYSNE--------LQFRHSDNINKF 107
Cdd:cd21276    3 AYQYLCRLEEAKRWMEACLKEELPPPTELEESLRNGVYLAKLGHCFAPRVVpLKKIYDLEqmryqatgLHFRHTDNINHW 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  108 LDFIHGIGLPEIFHFELTDIYEGKNLPKVIYCIHALSYFLSMQDLAPPLIKSDENLSFTDEDVSIIVRRL 177
Cdd:cd21276   83 RNAMMHIGLPSIFHPETTDIYDKKNMPRVVYCIHALSLYLFRLGLAPQIHDLYGKVKFTEEEINNMKLEL 152
RasGAP_IQGAP1 cd05133
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...
855-1176 2.43e-38

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: 148.27  E-value: 2.43e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  855 LVLQIFGHGSNRREEVLLLRFISQVIKLE-AALVNSSQDLLSDD-CVWKLLFTGYRGdVREVKLWKTILGRIHKVLVADN 932
Cdd:cd05133    3 VIFTLYNYASNQREEYLLLRLFKTALQEEiKSKVDQIQEIVTGNpTVIKMVVSFNRG-ARGQNALRQILAPVVKEIMDDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  933 HLDFEINPLTLFKSFNPEVASQT-DSPKL----TLSLAMQHPPTRNLYVSRLRELRKLCQSFLVALSKNIENIPYALCYT 1007
Cdd:cd05133   82 SLNIKTDPVDIYKSWVNQMESQTgEASKLpydvTPEQAMSHEEVRTRLDASIKNMRMVTDKFLSAIISSVDKIPYGMRFI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1008 AAQLKNSLQRYFPAAHKEEIFGVIGKFVYWAYVAPVLVSPDNFKLVD----GSITALQRKNLYTLSSILSEIFSIESC-- 1081
Cdd:cd05133  162 AKVLKDTLHEKFPDAGEDELLKIVGNLLYYRYMNPAIVAPDAFDIIDlsagGQLTTDQRRNLGSIAKMLQHAASNKMFlg 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1082 DSKQLGffrPLSEFIEVSKQDTMLMLERLVDVVDPEVYFEFDAFEDLVNTKRPVIYMKRDDILGIYSSIAYVIDSIApPD 1161
Cdd:cd05133  242 DNAHLS---PINEYLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIA-PE 317
                        330
                 ....*....|....*
gi 19114772 1162 VNDPLRAVVNSLGPV 1176
Cdd:cd05133  318 HNDPIHELLDDLGEV 332
RasGAP_IQGAP3 cd12207
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ...
855-1176 5.47e-38

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: 146.51  E-value: 5.47e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  855 LVLQIFGHGSNRREEVLLLRFISQVIKLEAAL-VNSSQDLLSDD-CVWKLLFTGYRGDVREVKLwKTILGRIHKVLVADN 932
Cdd:cd12207    3 VIFSLYNYASNRREAYLLLQLFKTALQEEISSkVEKPQDVITGNpTVIRLLVSFYRSARGQNAL-RHILGPVVQDVLQDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  933 HLDFEINPLTLFKSFNPEVASQTDSP-----KLTLSLAMQHPPTRNLYVSRLRELRKLCQSFLVALSKNIENIPYALCYT 1007
Cdd:cd12207   82 GLSIRTDPVQIYKAWINQTETQSGCRsslpyEVSPEQALSHPEVQRRLDIAIRNLLAVTDKFLSAITSSVDKIPYGMRYV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1008 AAQLKNSLQRYFPAAHKEEIFGVIGKFVYWAYVAPVLVSPDNFKLVD----GSITALQRKNLYTLSSILSEIFSIE--SC 1081
Cdd:cd12207  162 AKVLRDSLQEKFPGASEDEVYKVVGNLLYYRFMNPAVVAPDGFDIVDcsagGALQPEQRRMLGSVAKVLQHAAANKhfQG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1082 DSKQLGFfrpLSEFIEVSKQDTMLMLERLVDVVDPEVYFEFDAFEDLVNTKRPVIYMKRDDILGIYSSIAYVIDSIApPD 1161
Cdd:cd12207  242 DSEHLQA---LNQYLEETHVKFRKFILQACCVPEPEERFNVDEYSEMVAVAKPVIYITVGELINTHKLLLEHQDSIA-PD 317
                        330
                 ....*....|....*
gi 19114772 1162 VNDPLRAVVNSLGPV 1176
Cdd:cd12207  318 HSDPLHELLEDLGEV 332
CH_IQGAP2 cd21275
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP2; IQ motif ...
19-154 2.88e-37

calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP2; IQ motif containing GTPase activating protein 2 (IQGAP2) is a member of the IQGAP family, which consists of multi-domain proteins 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. IQGAP2 binds to activated Cdc42 and Rac1 but does not seem to stimulate their GTPase activity. It associates with calmodulin. IQGAP2 contains a single copy of the CH domain at the N-terminus.


Pssm-ID: 409124 [Multi-domain]  Cd Length: 156  Bit Score: 137.84  E-value: 2.88e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   19 GTKGSNTRLAAKQ----RETLQAYDYLCRVDEAKKWIEECLGTDLGPTSTFEQSLRNGVVLALLVQKFQPdKLI---KIF 91
Cdd:cd21275    5 GSIVDDERLSAEEmderRRQNIAYEYLCHLEEAKQWIEACLNEELPPTTELEEGLRNGVYLVKLAKFFAP-KLVsekKIY 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   92 YSNE-------LQFRHSDNINKFLDFIHGIGLPEIFHFELTDIYEGKNLPKVIYCIHALSYFLSMQDLAP 154
Cdd:cd21275   84 DVDQvrykrsgLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNMPRVIYCIHALSLYLFKLGIAP 153
CH_IQGAP1 cd21274
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif ...
37-171 1.46e-36

calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif containing GTPase activating protein 1 (IQGAP1), also called p195, is a homodimeric protein that is widely expressed among vertebrate cell types from early embryogenesis. It plays a crucial role in regulating the dynamics and assembly of the actin cytoskeleton. It belongs to the IQGAP family, which consists of multi-domain proteins 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. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity. It lacks GAP activity. Both, IQGAP1 and IQGAP2, specifically bind to Cdc42 and Rac1, but not to RhoA. Despite similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP1 contains a single copy of the CH domain at the N-terminus.


Pssm-ID: 409123 [Multi-domain]  Cd Length: 154  Bit Score: 135.89  E-value: 1.46e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   37 AYDYLCRVDEAKKWIEECLGTDLGPTSTFEQSLRNGVVLALLVQKFQPDKL-IKIFYSNE--------LQFRHSDNINKF 107
Cdd:cd21274    4 AYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVsLKKIYDREqtrykatgLHFRHTDNVIQW 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19114772  108 LDFIHGIGLPEIFHFELTDIYEGKNLPKVIYCIHALSYFLSMQDLAPPLIKSDENLSFTDEDVS 171
Cdd:cd21274   84 LNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEIN 147
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
44-144 5.88e-29

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 112.05  E-value: 5.88e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   44 VDEAKKWIEECLGTDLGPTST-FEQSLRNGVVLALLVQKFQPDKLIKIFYSNELQFRHSDNINKFLDFIHGIGLPEIFHF 122
Cdd:cd00014    1 EEELLKWINEVLGEELPVSITdLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKLGLPELDLF 80
                         90       100
                 ....*....|....*....|..
gi 19114772  123 ELTDIYEGKNLPKVIYCIHALS 144
Cdd:cd00014   81 EPEDLYEKGNLKKVLGTLWALA 102
RasGAP_GAPA cd05132
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...
859-1179 4.34e-22

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: 99.73  E-value: 4.34e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  859 IFGHGSNRREEVLLLRFISQVIKLEAALVNSSQDLLSDDCVWKLLFTGY--RGDVREvkLWKTILGRIHKVLVADNHLDF 936
Cdd:cd05132   13 LYGNQYESREEHLLLSMFQSVLTYEFDETTEFGSLLRANTAVSRMMTTYtrRGPGQS--YLKTVLADRINDLISLKDLNL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  937 EINPLTLFKSFNPEVASQTDSP-----KLTLSLAMQHPPTRNLYVSRLRELRKLCQSFLVALSKNIENIPYALCYTAAQL 1011
Cdd:cd05132   91 EINPLKVYEQMINDIELDTGLPsnlprGITPEEAAENPAVQNIIEPRLEMLEEITNSFLEAIINSLDEVPYGIRWICKQI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1012 KNSLQRYFPAAHKEEIFGVIGKFVYWAYVAPVLVSPDNFKLVDGSITALQRKNLYTLSSILSEI-----FSIEScdskql 1086
Cdd:cd05132  171 RSLTRRKFPDASDETICSLIGGFFLLRFINPAIVSPQAYMLVDGKPSDNTRRTLTLIAKLLQNLankpsYSKEP------ 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772 1087 gFFRPLSEFIEVSKQDTMLMLERLVDVVDPEVYFEFDAFeDLVNTKRPVIYMKRDDILGIYSSIAYVIDSIApPDVNDPL 1166
Cdd:cd05132  245 -YMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQY-IALSKKDLSINITLNEIYNTHSLLVKHLAELA-PDHNDHL 321
                        330
                 ....*....|...
gi 19114772 1167 RAVVNSLGPVSEQ 1179
Cdd:cd05132  322 RLILQELGPAPPQ 334
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
43-143 1.02e-18

calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 (dMP20) and similar domains; This subfamily contains Drosophila melanogaster muscle-specific protein 20 (dMP20), Echinococcus granulosus myophilin, Dictyostelium discoideum Rac guanine nucleotide exchange factor B (also called Trix), and similar proteins. dMP20 is present only in the synchronous muscles of D. melanogaster. It may be involved in the system linking the nerve impulse with the contraction or the relaxation process. Trix is involved in the regulation of the late steps of the endocytic pathway. dMP20 contains a single copy of the CH domain, while Trix (triple CH-domain array exchange factor) contains three, two type 3 CH domains which are included in this model, and one type 1 CH domain that is not included in this subfamily, but is part of the superfamily. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409056 [Multi-domain]  Cd Length: 107  Bit Score: 82.74  E-value: 1.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   43 RVDEAKKWIEECLGTDLGPTSTFEQSLRNGVVLALLVQKFQPDKLIKIfYSNELQFRHSDNINKFLDFIHGIGLPEIFHF 122
Cdd:cd21207    6 LEAEALDWIEAVTGEKLDDGKDYEDVLKDGVILCKLINILKPGSVKKI-NTSKMAFKLMENIENFLTACKGYGVPKTDLF 84
                         90       100
                 ....*....|....*....|.
gi 19114772  123 ELTDIYEGKNLPKVIYCIHAL 143
Cdd:cd21207   85 QTVDLYEKKNIPQVTNCLFAL 105
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
978-1130 1.65e-16

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: 82.74  E-value: 1.65e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772     978 RLRELRKLCQSFLVALSKNIENIPYALCYTAAQLKNSLQRYFPAAHkeEIFGVIGKFVYWAYVAPVLVSPDNFKLVDGSI 1057
Cdd:smart00323  148 NLENLLQYVERLFDAIINSSDRLPYGLRDICKQLRQAAEKRFPDAD--VIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHP 225
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19114772    1058 TALQRKNLYTLSSILSEIFSIESCDSKQlGFFRPLSEFIEVSKQDTMLMLERLVDVVDPEVYFEFDAFEDLVN 1130
Cdd:smart00323  226 DPTTRRTLTLIAKVLQNLANLSEFGSKE-PWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDSTTISGR 297
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
45-143 3.74e-14

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 69.65  E-value: 3.74e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772      45 DEAKKWIEECLGTDLGPTST-FEQSLRNGVVLALLVQKFQPDKLIKIFYSNEL-QFRHSDNINKFLDFIHGIGlPEIFHF 122
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTnFSSDLKDGVALCALLNSLSPGLVDKKKVAASLsRFKKIENINLALSFAEKLG-GKVVLF 79
                            90       100
                    ....*....|....*....|..
gi 19114772     123 ELTDIYEG-KNLPKVIYCIHAL 143
Cdd:smart00033   80 EPEDLVEGpKLILGVIWTLISL 101
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
46-144 5.49e-14

calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar proteins; The family includes transgelins from Saccharomyces cerevisiae and Schizosaccharomyces pombe, which are also called SCP1 and STG1, respectively. Transgelin, also called calponin homolog 1, has actin-binding and actin-bundling activity. It stabilizes actin filaments against disassembly. Transgelin contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409059 [Multi-domain]  Cd Length: 101  Bit Score: 69.32  E-value: 5.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   46 EAKKWIEECLGTDLGPtSTFEQSLRNGVVLALLVQKFQPDKLIKIFYSNeLQFRHSDNINKFLDFIHGIGLPEIFHFELT 125
Cdd:cd21210    4 EAREWIEEVLGEKLAQ-GDLLDALKDGVVLCKLANRILPADIRKYKESK-MPFVQMENISAFLNAARKLGVPENDLFQTV 81
                         90
                 ....*....|....*....
gi 19114772  126 DIYEGKNLPKVIYCIHALS 144
Cdd:cd21210   82 DLFERKNPAQVLQCLHALS 100
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
41-144 2.54e-13

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 67.70  E-value: 2.54e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772     41 LCRVDEAKKWIEECLGTDLGPTST--FEQSLRNGVVLALLVQKFQPDKLIKIFySNELQFRHSDNINKFLDFIHG-IGLP 117
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGPGVRVtnFTTDLRDGLALCALLNKLAPGLVDKKK-LNKSEFDKLENINLALDVAEKkLGVP 79
                           90       100
                   ....*....|....*....|....*..
gi 19114772    118 EIFhFELTDIYEGKNLpKVIYCIHALS 144
Cdd:pfam00307   80 KVL-IEPEDLVEGDNK-SVLTYLASLF 104
SCP1 COG5199
Calponin [Cytoskeleton];
46-148 4.51e-12

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 66.10  E-value: 4.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   46 EAKKWIEECLGTDLGPTSTFEQSLRNGVVLALLVQKFQPdklIKIFY-SNELQFRHSDNINKFLDFIHGIGLPEIFHFEL 124
Cdd:COG5199   17 EVTLWIETVLGEKFEPPGDLLSLLKDGVRLCRILNEASP---LDIKYkESKMPFVQMENISSFINGLKKLRVPEYELFQT 93
                         90       100
                 ....*....|....*....|....
gi 19114772  125 TDIYEGKNLPKVIYCIHALSYFLS 148
Cdd:COG5199   94 NDLFEAKDLRQVVICLYSLSRYAQ 117
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
969-1102 1.59e-11

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: 66.36  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  969 PPTRNLYVSRLRELRKLCQSFLVALSKNIENIPYALCYTAAQLKNSLQRYFPAaHKEEIFGVIGKFVYWAYVAPVLVSPD 1048
Cdd:cd04519  115 LPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILREFLAERFPE-EPDEAYQAVSGFLFLRFICPAIVSPE 193
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 19114772 1049 NFKLVDGSITALQRKNLYTLSSILSEIFSIESCDSKQlGFFRPLSEFIEVSKQD 1102
Cdd:cd04519  194 LFGLVPDEPSEQARRNLTLISKVLQSLANGVEFGDKE-PFMKPLNDFIKSNKPK 246
CH_GAS2-like cd21204
calponin homology (CH) domain found in the growth arrest-specific protein 2 family; The growth ...
36-145 3.41e-10

calponin homology (CH) domain found in the growth arrest-specific protein 2 family; The growth arrest-specific protein 2 (GAS-2) family includes GAS-2, and GAS-2 like proteins, GAS2L1-3. GAS-2 may play a role in apoptosis by acting as a cell death substrate for caspases. GAS2L1 (also called GAS2-related protein on chromosome 22 or growth arrest-specific protein 2-like 1) and GAS2L2 (also called GAS2-related protein on chromosome 17 or growth arrest-specific protein 2-like 2) may be involved in the cross-linking of microtubules and microfilaments. GAS2L3, also called GAS2-like protein 3, is a cytoskeletal linker protein that may promote and stabilize the formation of the actin and microtubule network. Members of this family contain a single copy of the CH domain at the N-terminal region. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409053  Cd Length: 131  Bit Score: 59.20  E-value: 3.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   36 QAYDYLCRVDEAKkWIEECLGTDLGPTsTFEQSLRNGVVLALLVQKFQP--------DKLIKIFYSNELQFRHS------ 101
Cdd:cd21204    1 EEALLPMKEDLAE-WLNDLLGDDLTPD-NFLDELRNGVVLCQLAQKIQEaaekareaGKKNGPPPSYKLKCNENakpgsf 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 19114772  102 ---DNINKFLDFIHGIGLPEIFHFELTDIYEGKNLPKVIYCIHALSY 145
Cdd:cd21204   79 farDNVANFLRWCRKLGVDEVLLFESEDLVLHKNPRQVLLCLLELAR 125
CH_CNN3 cd21284
calponin homology (CH) domain found in calponin-3; Calponin-3 (CNN3), also called acidic ...
45-144 4.37e-10

calponin homology (CH) domain found in calponin-3; Calponin-3 (CNN3), also called acidic isoform calponin, is an F-actin-binding protein that is expressed in the brain and has been shown to control dendritic spine morphology, density, and plasticity by regulating actin cytoskeletal reorganization and dynamics. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409133 [Multi-domain]  Cd Length: 111  Bit Score: 58.38  E-value: 4.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   45 DEAKKWIEECLGTDLGPTstFEQSLRNGVVLALLVQKFQPDKLIKIFYSnELQFRHSDNINKFLDFIHGIGLPEIFHFEL 124
Cdd:cd21284    8 EELRNWIEEVTGMSIGEN--FQKGLKDGVILCELINKLQPGSIRKINES-KLNWHQLENIGNFIKAIQAYGMKPHDIFEA 84
                         90       100
                 ....*....|....*....|
gi 19114772  125 TDIYEGKNLPKVIYCIHALS 144
Cdd:cd21284   85 NDLFENGNMTQVQTTLLALA 104
CH_CNN2 cd21283
calponin homology (CH) domain found in calponin-2; Calponin-2 (CNN2), also called neutral ...
46-144 3.26e-09

calponin homology (CH) domain found in calponin-2; Calponin-2 (CNN2), also called neutral calponin, or smooth muscle calponin H2, is an actin cytoskeleton-associated regulatory protein that inhibits the activity of myosin-ATPase and cytoskeleton dynamics. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409132 [Multi-domain]  Cd Length: 109  Bit Score: 56.09  E-value: 3.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   46 EAKKWIEECLGTDLGPTstFEQSLRNGVVLALLVQKFQPDKLIKIFYSNElQFRHSDNINKFLDFIHGIGLPEIFHFELT 125
Cdd:cd21283    7 ELRTWIEGLTGRSIGPD--FQKGLKDGVILCELMNKLQPGSVPKINRSMQ-NWHQLENLSNFIKAMVSYGMKPVDLFEAN 83
                         90
                 ....*....|....*....
gi 19114772  126 DIYEGKNLPKVIYCIHALS 144
Cdd:cd21283   84 DLFESGNMTQVQVSLLALA 102
CH_CNN cd21211
calponin homology (CH) domain found in the calponin family; Calponin is an actin ...
43-144 4.82e-09

calponin homology (CH) domain found in the calponin family; Calponin is an actin filament-associated regulatory protein expressed in smooth muscle and many types of non-muscle cells. There are three calponin isoforms, calponin-1, -2, -3. All of them are actin-binding proteins with functions in inhibiting actin-activated myosin ATPase and stabilizing the actin cytoskeleton. Calponin-1 is specifically expressed in smooth muscle cells and plays a role in fine-tuning smooth muscle contractility. Calponin-2 is expressed in both smooth muscle and non-muscle cells and regulates multiple actin cytoskeleton-based functions. Calponin-3 is expressed in the brain and participates in actin cytoskeleton-based activities in embryonic development and myogenesis. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409060 [Multi-domain]  Cd Length: 108  Bit Score: 55.39  E-value: 4.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   43 RVDEAKKWIEECLGTDLGPtsTFEQSLRNGVVLALLVQKFQPDKLIKIFYSNeLQFRHSDNINKFLDFIHGIGLPEIFHF 122
Cdd:cd21211    4 KEAELRTWIEGVTGLSIGP--NFQKGLKDGIILCELINKLQPGSVKKINESM-QNWHQLENIGNFIKAIVSYGMKPHDIF 80
                         90       100
                 ....*....|....*....|..
gi 19114772  123 ELTDIYEGKNLPKVIYCIHALS 144
Cdd:cd21211   81 EANDLFENGNMTQVQVTLLALA 102
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
44-129 1.11e-08

calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This family includes LIM domain only protein 7 (LMO-7) and LIM and calponin homology domains-containing protein 1 (LIMCH1), and similar proteins. LMO-7, also called F-box only protein 20, or LOMP, is a transcription regulator for expression of many Emery-Dreifuss muscular dystrophy (EDMD)-relevant genes. It binds to alpha-actinin and AF6/afadin at adherens junctions for epithelial cell-cell adhesion. LIMCH1 acts as an actin stress fiber-associated protein that activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. It positively regulates actin stress fiber assembly and stabilizes focal adhesions, and therefore negatively regulates cell spreading and cell migration. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409057 [Multi-domain]  Cd Length: 119  Bit Score: 54.65  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   44 VDEAKKWIEECLGTDLGPTStFEQSLRNGVVLALLVQKFQPDKLIKIfysNELQ--FRHSDNINKFLDFIHGIGLPEIFH 121
Cdd:cd21208    2 LKEARTWIEAVTGKKFPSDD-FRESLEDGILLCELINAIKPGSIKKI---NRLPtpIAGLDNLNLFLKACEDLGLKDSQL 77

                 ....*...
gi 19114772  122 FELTDIYE 129
Cdd:cd21208   78 FDPTDLQD 85
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
43-143 1.44e-08

calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. This family includes a group of kinesin-like proteins belonging to KIN-14 protein family. They all contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409052 [Multi-domain]  Cd Length: 112  Bit Score: 53.96  E-value: 1.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   43 RVDEAKKWIEECLGTDLGPTST---FEQSLRNGVVLALLVQKFQPDKLIKIFYSNELQ-------FRHSDNINKFLDFIH 112
Cdd:cd21203    1 RRYEAAEWIQNVLGVLVLPDPSeeeFRLCLRDGVVLCKLLNKLQPGAVPKVVESPDDPdgaagsaFQYFENVRNFLVAIE 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 19114772  113 GIGLPEifhFELTDI--YEGKNLPKVIYCIHAL 143
Cdd:cd21203   81 EMGLPT---FEASDLeqGGGGSRPRVVDCILAL 110
CH_VAV cd21201
calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic ...
65-144 1.66e-07

calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and as scaffold proteins, and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the CH domain, an actin-binding domain which is present as a single copy in VAV proteins.


Pssm-ID: 409050  Cd Length: 117  Bit Score: 51.10  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   65 FEQSLRNGVVLALLVQKFQPDKLIKIFYSN---ELQFRHSDNINKFLDFIHG-IGLPEIFHFELTDIYEGKNLPKVIYCI 140
Cdd:cd21201   32 LAQALRDGVLLCQLLNRLSPGSVDDREINLrpqMSQFLCLKNIRTFLQACRTvFGLRSADLFEPEDLYDVTNFGKVIRTL 111

                 ....
gi 19114772  141 HALS 144
Cdd:cd21201  112 SKLS 115
CH_CNN1 cd21282
calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), ...
46-144 1.08e-06

calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), also called basic calponin, or smooth muscle calponin H1, is a thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C, and tropomyosin. Calponin-1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409131 [Multi-domain]  Cd Length: 108  Bit Score: 48.72  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   46 EAKKWIEECLGTDLGptSTFEQSLRNGVVLALLVQKFQPDKLIKIfySNELQFRHS-DNINKFLDFIHGIGLPEIFHFEL 124
Cdd:cd21282    7 ELRVWIEGVTGRRIG--DNFMDGLKDGVILCELINKLQPGSVRKI--NESTQNWHKlENIGNFIKAIMHYGVKPHDIFEA 82
                         90       100
                 ....*....|....*....|
gi 19114772  125 TDIYEGKNLPKVIYCIHALS 144
Cdd:cd21282   83 NDLFENTNHTQVQSTLIALA 102
CH_betaPIX cd21266
calponin homology (CH) domain found in beta-Pak Interactive eXchange factor; Beta-Pak ...
61-144 2.59e-06

calponin homology (CH) domain found in beta-Pak Interactive eXchange factor; Beta-Pak Interactive eXchange factor (beta-PIX), also called PAK-interacting exchange factor beta, Rho guanine nucleotide exchange factor 7 (ARHGEF7), p85, or Cool (Cloned out of Library)-1, activates small GTPases by exchanging bound GDP for free GTP. It acts as a GEF for both Cdc42 and Rac1, and plays important roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. Beta-PIX contains a single copy of the CH domain at its N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409115  Cd Length: 112  Bit Score: 47.61  E-value: 2.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   61 PTSTFEQSLRNGVVLALLVQKFQPDKLIKIFYSNELQFRHSDNINKFLdfiHGIGLPEIFHFELTDIYEGKNLPKVIYCI 140
Cdd:cd21266   25 PEGFLQASLKDGVVLCRLLERLLPGSIDKVYPEPRTESECLSNIREFL---RGCGALRLETFDANDLYQGQNFNKVLSSL 101

                 ....
gi 19114772  141 HALS 144
Cdd:cd21266  102 VALN 105
RasGAP_Neurofibromin_like cd05392
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...
872-1072 9.65e-06

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: 49.20  E-value: 9.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  872 LLRFISQVIKLEAALVNSSQDLL-SDDCVWKLLFTgYRGDVREVKLWKTiLGRIHKVLVADNHLDFEINPltlfKSFNPE 950
Cdd:cd05392   49 LLPLISWLIEDEISHTSRAADLFrRNSVATRLLTL-YAKSVGNKYLRKV-LRPLLTEIVDNKDYFEVEKI----KPDDEN 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772  951 VASQTDSpkltlslamqhpptrnlyvsrlreLRKLCQSFLVALSKNIENIPYALCYTAAQLKNSLQRYFP-AAHKeeifg 1029
Cdd:cd05392  123 LEENADL------------------------LMKYAQMLLDSITDSVDQLPPSFRYICNTIYESVSKKFPdAALI----- 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 19114772 1030 VIGKFVYWAYVAPVLVSPDNFKLVDGSITALQRKNLYTLSSIL 1072
Cdd:cd05392  174 AVGGFLFLRFICPAIVSPESENLLDPPPTPEARRSLILIAKVL 216
CH_TAGLN cd21279
calponin homology (CH) domain found in transgelin; Transgelin, also called 22 kDa ...
49-143 1.01e-05

calponin homology (CH) domain found in transgelin; Transgelin, also called 22 kDa actin-binding protein, protein WS3-10, or smooth muscle protein 22-alpha (SM22-alpha), acts as an actin cross-linking/gelling protein that may be involved in calcium interactions and in regulating contractile properties of the cell. It may also contribute to replicative senescence. Transgelin contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409128 [Multi-domain]  Cd Length: 121  Bit Score: 46.15  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   49 KWIEECLGTDLGPTST----FEQSLRNGVVLALLVQKFQPD--KLIKIFYSN-ELQFRHSDNINKFLDFIHGIGLPEIFH 121
Cdd:cd21279   10 EWIVVQCGPDVGRPDRgrlgFQVWLKNGVVLSKLVNSLYPDgsKPVKIPDNPpSMVFKQMEQVAQFLKAAEDYGVVKTDM 89
                         90       100
                 ....*....|....*....|..
gi 19114772  122 FELTDIYEGKNLPKVIYCIHAL 143
Cdd:cd21279   90 FQTVDLYEGKDMAAVQRTLVAL 111
CH_LMO7 cd21277
calponin homology (CH) domain found in LIM domain only protein 7; LIM domain only protein 7 ...
46-121 4.76e-05

calponin homology (CH) domain found in LIM domain only protein 7; LIM domain only protein 7 (LMO-7), also called F-box only protein 20, or LOMP, is a transcription regulator for expression of many Emery-Dreifuss muscular dystrophy (EDMD)-relevant genes. It binds to alpha-actinin and AF6/afadin at adherens junctions for epithelial cell-cell adhesion. It contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409126 [Multi-domain]  Cd Length: 116  Bit Score: 44.06  E-value: 4.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   46 EAKKWIEECLGTDLGpTSTFEQSLRNGVVLALLVQKFQPDKLIKIfysNELQ--FRHSDNINKFLDFIHGIGLPE--IFH 121
Cdd:cd21277    4 EAQRWIEAVTGKNFG-NKDFRSALENGVLLCDLINKIKPGIIKKI---NRLStpIAGLDNINVFLKACEKLGLKEaqLFH 79
CH_TAGLN-like cd21209
calponin homology (CH) domain found in the transgelin family; The transgelin (TAGLN) family ...
50-143 1.21e-04

calponin homology (CH) domain found in the transgelin family; The transgelin (TAGLN) family includes transgelin, transgelin-2 and transgelin-3. Transgelin, also called 22 kDa actin-binding protein, protein WS3-10, or smooth muscle protein 22-alpha (SM22-alpha), acts as an actin cross-linking/gelling protein that may be involved in calcium interactions and in regulating contractile properties of the cell. Transgelin-2, also called epididymis tissue protein Li 7e, or SM22-alpha homolog, acts as an actin-binding protein that induces actin gelation and regulates actin cytoskeleton. It may participate in the development and progression of multiple cancers. Transgelin-3, also called neuronal protein 22 (NP22), or neuronal protein NP25, may have a role in alcohol-related adaptations and may mediate regulatory signal transduction pathways in neurons. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409058 [Multi-domain]  Cd Length: 119  Bit Score: 43.27  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   50 WIEECLGTDLG----PTSTFEQSLRNGVVLALLVQKFQPD--KLIKIFYSNELQFRHSDNINKFLDFIHGIGLPEIFHFE 123
Cdd:cd21209   11 WIVAQCGSDVGrpdpGRLGFQKWLKDGTVLCKLINSLYPEgsKPVKKIQSSKMAFKQMEQISQFLKAAEDYGVRTTDIFQ 90
                         90       100
                 ....*....|....*....|
gi 19114772  124 LTDIYEGKNLPKVIYCIHAL 143
Cdd:cd21209   91 TVDLWEGKDMAAVQRTLMAL 110
CH_TAGLN2 cd21280
calponin homology (CH) domain found in transgelin-2; Transgelin-2, also called epididymis ...
49-136 1.94e-04

calponin homology (CH) domain found in transgelin-2; Transgelin-2, also called epididymis tissue protein Li 7e, or SM22-alpha homolog, acts as an actin-binding protein that induces actin gelation and regulates the actin cytoskeleton. It may participate in the development and progression of multiple cancers. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409129 [Multi-domain]  Cd Length: 137  Bit Score: 42.94  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   49 KWIEECLGTDLGPT----STFEQSLRNGVVLALLVQKFQPDKL--IKIFYSNELQFRHSDNINKFLDFIHGIGLPEIFHF 122
Cdd:cd21280   15 QWITAQCGKQVGRPqpgrENFQNWLKDGTVLCHLINSLYPKGQapVKKIQASTMAFKQMEQISQFLQAAERYGINTTDIF 94
                         90
                 ....*....|....
gi 19114772  123 ELTDIYEGKNLPKV 136
Cdd:cd21280   95 QTVDLWEGKNMASV 108
CH_alphaPIX cd21265
calponin homology (CH) domain found in alpha-Pak Interactive eXchange factor; Alpha-Pak ...
61-143 1.05e-03

calponin homology (CH) domain found in alpha-Pak Interactive eXchange factor; Alpha-Pak Interactive eXchange factor (alpha-PIX), also called PAK-interacting exchange factor alpha, Rho guanine nucleotide exchange factor 6 (ARHGEF6), Rac/Cdc42 guanine nucleotide exchange factor 6, or Cool (Cloned out of Library)-2, activates small GTPases by exchanging bound GDP for free GTP. It acts as a GEF for both Cdc42 and Rac1, and is localized in dendritic spines where it regulates spine morphogenesis. It controls dendritic length and spine density in the hippocampus. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. Alpha-PIX contains a single copy of the CH domain at its N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409114  Cd Length: 117  Bit Score: 40.57  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   61 PTSTFEQSLRNGVVLALLVQKFQPDKLIKifYSNELQfRHSDNINKFLDFIHGIGLPEIFHFELTDIYEGKNLPKVIYCI 140
Cdd:cd21265   27 PEEFLKSSLKDGVVLCKLIERLLPGSVEK--YCLEPK-TEADCIGNIKEFLKGCAALKVETFEPDDLYTGENFSKVLSTL 103

                 ...
gi 19114772  141 HAL 143
Cdd:cd21265  104 LAV 106
CH_PIX cd21202
calponin homology (CH) domain found in the Pak Interactive eXchange factor family; Pak ...
30-146 4.93e-03

calponin homology (CH) domain found in the Pak Interactive eXchange factor family; Pak Interactive eXchange factor (PIX) proteins are Rho guanine nucleotide exchange factors (GEFs), which activate small GTPases by exchanging bound GDP for free GTP. They act as GEFs for both Cdc42 and Rac1, and have been implicated in cell motility, adhesion, neurite outgrowth, and cell polarity. Vertebrates contain two proteins from the PIX family, alpha-PIX and beta-PIX. Alpha-PIX, also called Rho guanine nucleotide exchange factor 6 (ARHGEF6), is localized in dendritic spines where it regulates spine morphogenesis. It controls dendritic length and spine density in the hippocampus. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. Beta-PIX, also called Rho guanine nucleotide exchange factor 7 (ARHGEF7), plays important roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. Both alpha-PIX and beta-PIX contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409051 [Multi-domain]  Cd Length: 114  Bit Score: 38.28  E-value: 4.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   30 KQRETLQAYDYLCRVDEAKKwieeclGTDLGPTSTFEQSLRNGVVLALLVQKFQPDKLIKIFYSNELQFRHSDNINKFLD 109
Cdd:cd21202    1 SAEQIVTWLISLGLLESPKK------ETIEDPERFLSESLKNGVVLCRLVNRLKPGTVEKIYDEPTTEEECLYNFESFLK 74
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 19114772  110 FIHGIGLPEIFHFELTDIYEGKNLPKVIYCIHALSYF 146
Cdd:cd21202   75 ACQELGILAEEIFDPNDLYSGGNFQKVLSTLERLEKV 111
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
61-143 9.99e-03

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409062  Cd Length: 107  Bit Score: 37.28  E-value: 9.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114772   61 PTSTFEQSLRNGVVLALLVQKFQPDKLIKIFYSNELQFRHSDNINKFLDFI--HGIGLPeifHFELTDIYEGkNLPKVIY 138
Cdd:cd21213   21 PVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMasKRIRMH---QTSAKDIVDG-NLKAIMR 96

                 ....*
gi 19114772  139 CIHAL 143
Cdd:cd21213   97 LILAL 101
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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