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Conserved domains on  [gi|6325014|ref|NP_015082|]
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Iqg1p [Saccharomyces cerevisiae S288C]

Protein Classification

Ras GTPase-activating protein( domain architecture ID 11474206)

Ras GTPase-activating protein accelerates the GTPase activity of Ras

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
1-1494 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: 1156.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014     1 MTAYSGSpskpgnnnsyLNRYVENLGtnvtpplRPqssskinsslnIASPSHLKTKTSASNSSAtilskkvessvsklkp 80
Cdd:COG5261    1 MTAYSGS----------LNRYVENLG-------RP-----------IGTPSHLKTKTSAKNRSA---------------- 36
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014    81 slpnklvgkytvdlsnyskieLRYYEFLCRVSEVKIWIEAVIEEALPseiELCVGDSLRNGVFLAKLTQRINPDLTTVIF 160
Cdd:COG5261   37 ---------------------LRAYEYLCRVSEAKIWIEEVIEEALP---ELCFEDSLRNGVFLAKLTQRFNPDLTTVIF 92
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   161 PAgDKLQFKHTQNINAFFGLVEHVGVPDSFRFELQDLYNKKNIPQVFETLHILISMInkKWPGKTPaLTNVSGQISFTKE 240
Cdd:COG5261   93 PA-DKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISML--SWPGKTP-LINSSGQISFTKE 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   241 EIAACKKAWPRIRDFKSLGTNINTApASPEEPKEKRSGLIKDFNKFERPNIPVEEILITPRKNITDANCsdfsNTPSPYN 320
Cdd:COG5261  169 DIAACKKAWPRIPDFKSLGTNINTA-ASPEEPKEKRSGLIKKFAKFQRPNIPVESILITPRKSITDANC----STPSDYL 243
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   321 EApkmsnldvvVEKRKftPIEPsllgPTPSLEYSPIKNKSLSYYSpTISKYLTYDTEFytrrsraREEDLNYYQTFKYsp 400
Cdd:COG5261  244 KA---------TLKRF--PYKR----HSGTLEDSVLPQTSLSLFS-TRRSTSVFYTIS-------LEMISNVEQAFFH-- 298
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   401 sHYSPMRRERMTEEQFLEKVVQLQNICRgvntrfnLYIQKRllnlfeqdilrfqaclrGNKFRVLSSMYLPIrraKIDVP 480
Cdd:COG5261  299 -LDRELHRLKQSISSQSKQVVVLERDIR-------LLIQKR-----------------GNKIRLLIQNRMPQ---EEDTK 350
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   481 HVEAIQSRIKGsriRYKYDKLKFTLSRFSCTVELLQaycrskllkttvntklndieiSHYPLTKlqsymrasyvrkkvms 560
Cdd:COG5261  351 FAERLQSNING---RKKYFPLDRRLSLFGPLFFLLQ---------------------SSIPLFS---------------- 390
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   561 lntklnderesimkfSAIIRGNVVRCSEDailsavhdvHKENISKLQSLIRGIFTRsclasIIYSLGKENCNIiqlsaci 640
Cdd:COG5261  391 ---------------IAICVGRVKRFSID---------ALLNIVKLQILGNGYEIR-----KLYSLGKSNCEE------- 434
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   641 rgnavrhkvqslfapennlSETVHDLQGLVRgilvrytldlvdDIVEYNNLalFQAFSRGALVresldqkssfYKRNVRS 720
Cdd:COG5261  435 -------------------HLSVSLFQMLLR------------TEVEATSL--VQSLLRGNLP----------VHRNMTN 471
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   721 vimiqsWIRKSLQRSAYLElldcpnpslwavkkfvhllngtatieevqnqlesCQASLDSENMKKERLLKSIRQQLNING 800
Cdd:COG5261  472 ------YFRRSQGQAALRE----------------------------------IRYQIINDVAIHEDLEVDINPLLVYRA 511
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   801 VLDKFGLLKDKDHELGisdstipKSKYQKYEKLFYMLQVDPSYWKLLYLkEPEFVAKNVYMTFGTVNQRMndrersyftR 880
Cdd:COG5261  512 LLNKGQLSPDKDLELL-------TSNEEVSEFLAVMNAVQESSAKLLEL-STERILDAVYNSLDEIGYGI---------R 574
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   881 FVCEMLQnaineapsiesfldnrsqfwqtilqdflrrespeffsiivpvldylsdpvVDFESDPYKIYQEIhgfsspqhc 960
Cdd:COG5261  575 FVCELIR--------------------------------------------------VVFELTPNRLFPSI--------- 595
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   961 spvddastknKFIdnlRCLWHAIemvaeiytrkvhtipveirylctkifcyaadknIEEIDSLRAISSILVNVFVSEYLV 1040
Cdd:COG5261  596 ----------SDS---RCLRTIC---------------------------------FAEIDSLGLIGGFFFLRFVNEALV 629
                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014  1041 NREYYGYKDSNVQKNNQKIDILMKSLATVFEIKNFDGFLDPLNQYANEIKPHIKDVLYNVLVDPEYEQEGDRLIYLDMVS 1120
Cdd:COG5261  630 SPQTSMLKDSCPSDNVRKLATLSKILQSVFEITSSDKFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVK 709
                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014  1121 PSPKLELLTEKVLEISGKFEEYLNEFPEADILHDILEKNLDNS-SFPRSGRVTLELDASAYRFLVSDDKMRKIYDQVKRA 1199
Cdd:COG5261  710 KSRALEYLVNEIYLTHEIIIEYLDNLYDPDSLVDLLLQELGELcSFPQDQRDTLNCLVTLPLFNRSDDPIRDLKQQLKRT 789
                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014  1200 FVYMMQIEDVDtNLYDLSIStILPQDEPNFANFLEQNPKIRDDPMIQKLKPLKYFTLKNVTLKKIHELESTGtFCSSDNK 1279
Cdd:COG5261  790 RVYIIYVDAGT-NLFEQLLR-LLPSDEPATRNPLDLNPNIRDDPSVSSLKSMSLMKLKIRAIELLDELETLG-FVSRENR 866
                       1290      1300      1310      1320      1330      1340      1350      1360
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014  1280 LQNFLNDIANTIKNPNYAIDYVTQEIYITKETLTKISEMNHSLDIELSRLKKHVDHTIKDFQKAkdfspvhKSKFGNFKN 1359
Cdd:COG5261  867 YQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPK-------KSKLKGFSR 939
                       1370      1380      1390      1400      1410      1420      1430      1440
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014  1360 AVKKVQGRERSElQGMKFKWNTKQLYERGVLKTIRGEklaeltvkvfgssGPKFPDIIFKISTSDGSRFGIQMIdkrkGP 1439
Cdd:COG5261  940 GVGVVRDKPKSI-SSGTFKYSAQQLYKRGVLVNITIP-------------EPNVSNIYFTFSSDSTDNFVIEVY----QP 1001
                       1450      1460      1470      1480      1490
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6325014  1440 DKRYSDDVDSFSFKDLIKTQVEpKIETWKLFhSNVVVNNSQLLHLIVSFFYKRNA 1494
Cdd:COG5261 1002 GHSVSLPEVSFCFDDLLKRQYN-KNPVVDLG-GFLTFNANKLLHLIESKFYRKNA 1054
 
Name Accession Description Interval E-value
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
1-1494 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: 1156.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014     1 MTAYSGSpskpgnnnsyLNRYVENLGtnvtpplRPqssskinsslnIASPSHLKTKTSASNSSAtilskkvessvsklkp 80
Cdd:COG5261    1 MTAYSGS----------LNRYVENLG-------RP-----------IGTPSHLKTKTSAKNRSA---------------- 36
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014    81 slpnklvgkytvdlsnyskieLRYYEFLCRVSEVKIWIEAVIEEALPseiELCVGDSLRNGVFLAKLTQRINPDLTTVIF 160
Cdd:COG5261   37 ---------------------LRAYEYLCRVSEAKIWIEEVIEEALP---ELCFEDSLRNGVFLAKLTQRFNPDLTTVIF 92
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   161 PAgDKLQFKHTQNINAFFGLVEHVGVPDSFRFELQDLYNKKNIPQVFETLHILISMInkKWPGKTPaLTNVSGQISFTKE 240
Cdd:COG5261   93 PA-DKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISML--SWPGKTP-LINSSGQISFTKE 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   241 EIAACKKAWPRIRDFKSLGTNINTApASPEEPKEKRSGLIKDFNKFERPNIPVEEILITPRKNITDANCsdfsNTPSPYN 320
Cdd:COG5261  169 DIAACKKAWPRIPDFKSLGTNINTA-ASPEEPKEKRSGLIKKFAKFQRPNIPVESILITPRKSITDANC----STPSDYL 243
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   321 EApkmsnldvvVEKRKftPIEPsllgPTPSLEYSPIKNKSLSYYSpTISKYLTYDTEFytrrsraREEDLNYYQTFKYsp 400
Cdd:COG5261  244 KA---------TLKRF--PYKR----HSGTLEDSVLPQTSLSLFS-TRRSTSVFYTIS-------LEMISNVEQAFFH-- 298
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   401 sHYSPMRRERMTEEQFLEKVVQLQNICRgvntrfnLYIQKRllnlfeqdilrfqaclrGNKFRVLSSMYLPIrraKIDVP 480
Cdd:COG5261  299 -LDRELHRLKQSISSQSKQVVVLERDIR-------LLIQKR-----------------GNKIRLLIQNRMPQ---EEDTK 350
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   481 HVEAIQSRIKGsriRYKYDKLKFTLSRFSCTVELLQaycrskllkttvntklndieiSHYPLTKlqsymrasyvrkkvms 560
Cdd:COG5261  351 FAERLQSNING---RKKYFPLDRRLSLFGPLFFLLQ---------------------SSIPLFS---------------- 390
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   561 lntklnderesimkfSAIIRGNVVRCSEDailsavhdvHKENISKLQSLIRGIFTRsclasIIYSLGKENCNIiqlsaci 640
Cdd:COG5261  391 ---------------IAICVGRVKRFSID---------ALLNIVKLQILGNGYEIR-----KLYSLGKSNCEE------- 434
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   641 rgnavrhkvqslfapennlSETVHDLQGLVRgilvrytldlvdDIVEYNNLalFQAFSRGALVresldqkssfYKRNVRS 720
Cdd:COG5261  435 -------------------HLSVSLFQMLLR------------TEVEATSL--VQSLLRGNLP----------VHRNMTN 471
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   721 vimiqsWIRKSLQRSAYLElldcpnpslwavkkfvhllngtatieevqnqlesCQASLDSENMKKERLLKSIRQQLNING 800
Cdd:COG5261  472 ------YFRRSQGQAALRE----------------------------------IRYQIINDVAIHEDLEVDINPLLVYRA 511
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   801 VLDKFGLLKDKDHELGisdstipKSKYQKYEKLFYMLQVDPSYWKLLYLkEPEFVAKNVYMTFGTVNQRMndrersyftR 880
Cdd:COG5261  512 LLNKGQLSPDKDLELL-------TSNEEVSEFLAVMNAVQESSAKLLEL-STERILDAVYNSLDEIGYGI---------R 574
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   881 FVCEMLQnaineapsiesfldnrsqfwqtilqdflrrespeffsiivpvldylsdpvVDFESDPYKIYQEIhgfsspqhc 960
Cdd:COG5261  575 FVCELIR--------------------------------------------------VVFELTPNRLFPSI--------- 595
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   961 spvddastknKFIdnlRCLWHAIemvaeiytrkvhtipveirylctkifcyaadknIEEIDSLRAISSILVNVFVSEYLV 1040
Cdd:COG5261  596 ----------SDS---RCLRTIC---------------------------------FAEIDSLGLIGGFFFLRFVNEALV 629
                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014  1041 NREYYGYKDSNVQKNNQKIDILMKSLATVFEIKNFDGFLDPLNQYANEIKPHIKDVLYNVLVDPEYEQEGDRLIYLDMVS 1120
Cdd:COG5261  630 SPQTSMLKDSCPSDNVRKLATLSKILQSVFEITSSDKFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVK 709
                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014  1121 PSPKLELLTEKVLEISGKFEEYLNEFPEADILHDILEKNLDNS-SFPRSGRVTLELDASAYRFLVSDDKMRKIYDQVKRA 1199
Cdd:COG5261  710 KSRALEYLVNEIYLTHEIIIEYLDNLYDPDSLVDLLLQELGELcSFPQDQRDTLNCLVTLPLFNRSDDPIRDLKQQLKRT 789
                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014  1200 FVYMMQIEDVDtNLYDLSIStILPQDEPNFANFLEQNPKIRDDPMIQKLKPLKYFTLKNVTLKKIHELESTGtFCSSDNK 1279
Cdd:COG5261  790 RVYIIYVDAGT-NLFEQLLR-LLPSDEPATRNPLDLNPNIRDDPSVSSLKSMSLMKLKIRAIELLDELETLG-FVSRENR 866
                       1290      1300      1310      1320      1330      1340      1350      1360
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014  1280 LQNFLNDIANTIKNPNYAIDYVTQEIYITKETLTKISEMNHSLDIELSRLKKHVDHTIKDFQKAkdfspvhKSKFGNFKN 1359
Cdd:COG5261  867 YQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPK-------KSKLKGFSR 939
                       1370      1380      1390      1400      1410      1420      1430      1440
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014  1360 AVKKVQGRERSElQGMKFKWNTKQLYERGVLKTIRGEklaeltvkvfgssGPKFPDIIFKISTSDGSRFGIQMIdkrkGP 1439
Cdd:COG5261  940 GVGVVRDKPKSI-SSGTFKYSAQQLYKRGVLVNITIP-------------EPNVSNIYFTFSSDSTDNFVIEVY----QP 1001
                       1450      1460      1470      1480      1490
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6325014  1440 DKRYSDDVDSFSFKDLIKTQVEpKIETWKLFhSNVVVNNSQLLHLIVSFFYKRNA 1494
Cdd:COG5261 1002 GHSVSLPEVSFCFDDLLKRQYN-KNPVVDLG-GFLTFNANKLLHLIESKFYRKNA 1054
RasGAP_IQGAP_related cd12206
Ras-GTPase Activating Domain of proteins related to IQGAPs; RasGAP: Ras-GTPase Activating ...
852-1198 4.66e-129

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: 404.79  E-value: 4.66e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   852 PEFVAKNVYMTFGTV----NQRMNDRERSYFTRFVCEMLQNAINEAPSIESFLDNRSQFWQTILQDFL-RRESPEFFSII 926
Cdd:cd12206    1 SEFIEKNVYVTLPIFqkptNGKMDSREEFLFIKFILELLKSDIENSNSNQDFLANSDNFWILLLVTFNnLRERSELKSIF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   927 VPVL-DYLSDPVVDFESDPYKIYQEIHGFSSPQHCSPVDDASTKNKFIDNLRCLWHAIEMVAEIYTRKVHTIPVEIRYLC 1005
Cdd:cd12206   81 GPLLvQYLENQEIDFESDPSVIYKSLHGRPPLSSEEAIEDDRVSDKFVENLTNLREAVEMVAEIIFKNVDKIPVEIRYLC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014  1006 TKIFCYAADKNIEE--IDSLRAISSILVNVFVSEYLVNREYYGYKDSNVQKNNQKIDILMKSLATVFEIKNFDGFLDPLN 1083
Cdd:cd12206  161 TKAYIAFADKFPDEseEDILRAISKILIKSYVAPILVNPENYGFVDNEEDNLNEKARVLLQILSMVFFLKNFDGYLKPLN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014  1084 QYANEIKPHIKDVLYNVLVDPEYEQEGDRLIYLDMVS-PSPKLELLTEKVLEISGKFEEYLNEFPEADILHDILEKNLDN 1162
Cdd:cd12206  241 QYIEEIKPSIRDLLKELLDVPEEEQEYDKLIYYDIMStTRPCLEILLDKVIEIIQILKENLDEFTPDDQLVQLLEKIVDL 320
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 6325014  1163 SSFP---RSGRVTLELDASAYRFLVSDDKMRKIYDQVKR 1198
Cdd:cd12206  321 SSSSndkRSGRVTLELNPSAYQFLVNDDKERKLYDQVKR 359
RasGAP_C pfam03836
RasGAP C-terminus; This domain can be found in the C terminus of the IQGAP family members, ...
1253-1397 4.64e-31

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: 119.19  E-value: 4.64e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014    1253 YFTLKNVTLKKIHELESTGTfCSSDNKLQNFLNDIANTIKNPNYAIDYVTQEIYITKETLTKISEMNHSLDIELSRLKKH 1332
Cdd:pfam03836    1 YVELKKKALENLLELESLGV-ISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDY 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325014    1333 VDHTIKDFQKAKdfspvhKSKFGNFKNAVKKVQGRERSELQGmKFKWNTKQLYERGVLKTIRGEK 1397
Cdd:pfam03836   80 IENCLDNLQKKK------KKLFSKQYFHYRKLQKRGKLPKFG-SYKYSARQLYEKGVLLEIEGVP 137
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
113-213 1.34e-13

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: 68.11  E-value: 1.34e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014      113 EVKIWIEAVIEEALPSEIElCVGDSLRNGVFLAKLTQRINPDLTTVIFPAGDKLQFKHTQNINAFFGLVEHVGvPDSFRF 192
Cdd:smart00033    2 TLLRWVNSLLAEYDKPPVT-NFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLG-GKVVLF 79
                            90       100
                    ....*....|....*....|..
gi 6325014      193 ELQDLY-NKKNIPQVFETLHIL 213
Cdd:smart00033   80 EPEDLVeGPKLILGVIWTLISL 101
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
1013-1362 4.36e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 41.96  E-value: 4.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014    1013 ADKNIEE--IDSLRAISSILVNVFVSEYLVNREYYGYKDSNVQKNNQKIDILMKSLATVF-EIK------NFDGFLDPLN 1083
Cdd:TIGR01612 1027 ATNDIEQkiEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAEINITNFnEIKeklkhyNFDDFGKEEN 1106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014    1084 -QYANEIKpHIKDVLYNVlvdpeyEQEGDRLIyldmvspspklelltEKVLEISGKFEEYLNEF-PEADILHDILEKNLD 1161
Cdd:TIGR01612 1107 iKYADEIN-KIKDDIKNL------DQKIDHHI---------------KALEEIKKKSENYIDEIkAQINDLEDVADKAIS 1164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014    1162 NSSFPrsgrvtlELDASAYRFLVSDDKMRKIYDQVKRAFVYMMQIEDVDTNL---------YDLSISTIlpqdepnfanF 1232
Cdd:TIGR01612 1165 NDDPE-------EIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLeevkginlsYGKNLGKL----------F 1227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014    1233 LEQ--NPKIRDDPMIQKLKplKYFTLKNVTLKKIHELESTGTFCSSDNKLQNFLNdiantIKNPNYAIDYVT-----QEI 1305
Cdd:TIGR01612 1228 LEKidEEKKKSEHMIKAME--AYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFN-----ISHDDDKDHHIIskkhdENI 1300
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 6325014    1306 YITKETLTKISEMNhSLDIELSRLKKHVDHTIKDFQKAKDFSPVHKSKFGNFKNAVK 1362
Cdd:TIGR01612 1301 SDIREKSLKIIEDF-SEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILK 1356
 
Name Accession Description Interval E-value
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
1-1494 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: 1156.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014     1 MTAYSGSpskpgnnnsyLNRYVENLGtnvtpplRPqssskinsslnIASPSHLKTKTSASNSSAtilskkvessvsklkp 80
Cdd:COG5261    1 MTAYSGS----------LNRYVENLG-------RP-----------IGTPSHLKTKTSAKNRSA---------------- 36
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014    81 slpnklvgkytvdlsnyskieLRYYEFLCRVSEVKIWIEAVIEEALPseiELCVGDSLRNGVFLAKLTQRINPDLTTVIF 160
Cdd:COG5261   37 ---------------------LRAYEYLCRVSEAKIWIEEVIEEALP---ELCFEDSLRNGVFLAKLTQRFNPDLTTVIF 92
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   161 PAgDKLQFKHTQNINAFFGLVEHVGVPDSFRFELQDLYNKKNIPQVFETLHILISMInkKWPGKTPaLTNVSGQISFTKE 240
Cdd:COG5261   93 PA-DKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISML--SWPGKTP-LINSSGQISFTKE 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   241 EIAACKKAWPRIRDFKSLGTNINTApASPEEPKEKRSGLIKDFNKFERPNIPVEEILITPRKNITDANCsdfsNTPSPYN 320
Cdd:COG5261  169 DIAACKKAWPRIPDFKSLGTNINTA-ASPEEPKEKRSGLIKKFAKFQRPNIPVESILITPRKSITDANC----STPSDYL 243
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   321 EApkmsnldvvVEKRKftPIEPsllgPTPSLEYSPIKNKSLSYYSpTISKYLTYDTEFytrrsraREEDLNYYQTFKYsp 400
Cdd:COG5261  244 KA---------TLKRF--PYKR----HSGTLEDSVLPQTSLSLFS-TRRSTSVFYTIS-------LEMISNVEQAFFH-- 298
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   401 sHYSPMRRERMTEEQFLEKVVQLQNICRgvntrfnLYIQKRllnlfeqdilrfqaclrGNKFRVLSSMYLPIrraKIDVP 480
Cdd:COG5261  299 -LDRELHRLKQSISSQSKQVVVLERDIR-------LLIQKR-----------------GNKIRLLIQNRMPQ---EEDTK 350
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   481 HVEAIQSRIKGsriRYKYDKLKFTLSRFSCTVELLQaycrskllkttvntklndieiSHYPLTKlqsymrasyvrkkvms 560
Cdd:COG5261  351 FAERLQSNING---RKKYFPLDRRLSLFGPLFFLLQ---------------------SSIPLFS---------------- 390
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   561 lntklnderesimkfSAIIRGNVVRCSEDailsavhdvHKENISKLQSLIRGIFTRsclasIIYSLGKENCNIiqlsaci 640
Cdd:COG5261  391 ---------------IAICVGRVKRFSID---------ALLNIVKLQILGNGYEIR-----KLYSLGKSNCEE------- 434
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   641 rgnavrhkvqslfapennlSETVHDLQGLVRgilvrytldlvdDIVEYNNLalFQAFSRGALVresldqkssfYKRNVRS 720
Cdd:COG5261  435 -------------------HLSVSLFQMLLR------------TEVEATSL--VQSLLRGNLP----------VHRNMTN 471
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   721 vimiqsWIRKSLQRSAYLElldcpnpslwavkkfvhllngtatieevqnqlesCQASLDSENMKKERLLKSIRQQLNING 800
Cdd:COG5261  472 ------YFRRSQGQAALRE----------------------------------IRYQIINDVAIHEDLEVDINPLLVYRA 511
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   801 VLDKFGLLKDKDHELGisdstipKSKYQKYEKLFYMLQVDPSYWKLLYLkEPEFVAKNVYMTFGTVNQRMndrersyftR 880
Cdd:COG5261  512 LLNKGQLSPDKDLELL-------TSNEEVSEFLAVMNAVQESSAKLLEL-STERILDAVYNSLDEIGYGI---------R 574
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   881 FVCEMLQnaineapsiesfldnrsqfwqtilqdflrrespeffsiivpvldylsdpvVDFESDPYKIYQEIhgfsspqhc 960
Cdd:COG5261  575 FVCELIR--------------------------------------------------VVFELTPNRLFPSI--------- 595
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   961 spvddastknKFIdnlRCLWHAIemvaeiytrkvhtipveirylctkifcyaadknIEEIDSLRAISSILVNVFVSEYLV 1040
Cdd:COG5261  596 ----------SDS---RCLRTIC---------------------------------FAEIDSLGLIGGFFFLRFVNEALV 629
                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014  1041 NREYYGYKDSNVQKNNQKIDILMKSLATVFEIKNFDGFLDPLNQYANEIKPHIKDVLYNVLVDPEYEQEGDRLIYLDMVS 1120
Cdd:COG5261  630 SPQTSMLKDSCPSDNVRKLATLSKILQSVFEITSSDKFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVK 709
                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014  1121 PSPKLELLTEKVLEISGKFEEYLNEFPEADILHDILEKNLDNS-SFPRSGRVTLELDASAYRFLVSDDKMRKIYDQVKRA 1199
Cdd:COG5261  710 KSRALEYLVNEIYLTHEIIIEYLDNLYDPDSLVDLLLQELGELcSFPQDQRDTLNCLVTLPLFNRSDDPIRDLKQQLKRT 789
                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014  1200 FVYMMQIEDVDtNLYDLSIStILPQDEPNFANFLEQNPKIRDDPMIQKLKPLKYFTLKNVTLKKIHELESTGtFCSSDNK 1279
Cdd:COG5261  790 RVYIIYVDAGT-NLFEQLLR-LLPSDEPATRNPLDLNPNIRDDPSVSSLKSMSLMKLKIRAIELLDELETLG-FVSRENR 866
                       1290      1300      1310      1320      1330      1340      1350      1360
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014  1280 LQNFLNDIANTIKNPNYAIDYVTQEIYITKETLTKISEMNHSLDIELSRLKKHVDHTIKDFQKAkdfspvhKSKFGNFKN 1359
Cdd:COG5261  867 YQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPK-------KSKLKGFSR 939
                       1370      1380      1390      1400      1410      1420      1430      1440
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014  1360 AVKKVQGRERSElQGMKFKWNTKQLYERGVLKTIRGEklaeltvkvfgssGPKFPDIIFKISTSDGSRFGIQMIdkrkGP 1439
Cdd:COG5261  940 GVGVVRDKPKSI-SSGTFKYSAQQLYKRGVLVNITIP-------------EPNVSNIYFTFSSDSTDNFVIEVY----QP 1001
                       1450      1460      1470      1480      1490
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6325014  1440 DKRYSDDVDSFSFKDLIKTQVEpKIETWKLFhSNVVVNNSQLLHLIVSFFYKRNA 1494
Cdd:COG5261 1002 GHSVSLPEVSFCFDDLLKRQYN-KNPVVDLG-GFLTFNANKLLHLIESKFYRKNA 1054
RasGAP_IQGAP_related cd12206
Ras-GTPase Activating Domain of proteins related to IQGAPs; RasGAP: Ras-GTPase Activating ...
852-1198 4.66e-129

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: 404.79  E-value: 4.66e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   852 PEFVAKNVYMTFGTV----NQRMNDRERSYFTRFVCEMLQNAINEAPSIESFLDNRSQFWQTILQDFL-RRESPEFFSII 926
Cdd:cd12206    1 SEFIEKNVYVTLPIFqkptNGKMDSREEFLFIKFILELLKSDIENSNSNQDFLANSDNFWILLLVTFNnLRERSELKSIF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   927 VPVL-DYLSDPVVDFESDPYKIYQEIHGFSSPQHCSPVDDASTKNKFIDNLRCLWHAIEMVAEIYTRKVHTIPVEIRYLC 1005
Cdd:cd12206   81 GPLLvQYLENQEIDFESDPSVIYKSLHGRPPLSSEEAIEDDRVSDKFVENLTNLREAVEMVAEIIFKNVDKIPVEIRYLC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014  1006 TKIFCYAADKNIEE--IDSLRAISSILVNVFVSEYLVNREYYGYKDSNVQKNNQKIDILMKSLATVFEIKNFDGFLDPLN 1083
Cdd:cd12206  161 TKAYIAFADKFPDEseEDILRAISKILIKSYVAPILVNPENYGFVDNEEDNLNEKARVLLQILSMVFFLKNFDGYLKPLN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014  1084 QYANEIKPHIKDVLYNVLVDPEYEQEGDRLIYLDMVS-PSPKLELLTEKVLEISGKFEEYLNEFPEADILHDILEKNLDN 1162
Cdd:cd12206  241 QYIEEIKPSIRDLLKELLDVPEEEQEYDKLIYYDIMStTRPCLEILLDKVIEIIQILKENLDEFTPDDQLVQLLEKIVDL 320
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 6325014  1163 SSFP---RSGRVTLELDASAYRFLVSDDKMRKIYDQVKR 1198
Cdd:cd12206  321 SSSSndkRSGRVTLELNPSAYQFLVNDDKERKLYDQVKR 359
CH_IQGAP cd21206
calponin homology (CH) domain found in the IQ motif containing GTPase activating protein ...
102-221 1.96e-48

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: 168.17  E-value: 1.96e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   102 LRYYEFLCRVSEVKIWIEAVIEEALPSEIELcvGDSLRNGVFLAKLTQRINPDLTTVIFPAGDKLQFKHTQNINAFFGLV 181
Cdd:cd21206    1 TIAYEYLCRLEEAKQWIEACLNEELPPTTEF--EEELRNGVVLAKLANKFAPKLVPLKKIYDVGLQFRHTDNINHFLRAL 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 6325014   182 EHVGVPDSFRFELQDLYNKKNIPQVFETLHILISMINKKW 221
Cdd:cd21206   79 KKIGLPKIFHFETTDLYEKKNIPKVIYCLHALSLLLFKLG 118
RasGAP_C pfam03836
RasGAP C-terminus; This domain can be found in the C terminus of the IQGAP family members, ...
1253-1397 4.64e-31

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: 119.19  E-value: 4.64e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014    1253 YFTLKNVTLKKIHELESTGTfCSSDNKLQNFLNDIANTIKNPNYAIDYVTQEIYITKETLTKISEMNHSLDIELSRLKKH 1332
Cdd:pfam03836    1 YVELKKKALENLLELESLGV-ISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDY 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325014    1333 VDHTIKDFQKAKdfspvhKSKFGNFKNAVKKVQGRERSELQGmKFKWNTKQLYERGVLKTIRGEK 1397
Cdd:pfam03836   80 IENCLDNLQKKK------KKLFSKQYFHYRKLQKRGKLPKFG-SYKYSARQLYEKGVLLEIEGVP 137
CH_IQGAP3 cd21276
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP3; IQ motif ...
105-246 6.08e-27

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: 108.14  E-value: 6.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   105 YEFLCRVSEVKIWIEAVIEEALPSEIELcvGDSLRNGVFLAKLTQRINP---------DLTTVIFPAGDkLQFKHTQNIN 175
Cdd:cd21276    4 YQYLCRLEEAKRWMEACLKEELPPPTEL--EESLRNGVYLAKLGHCFAPrvvplkkiyDLEQMRYQATG-LHFRHTDNIN 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6325014   176 AFFGLVEHVGVPDSFRFELQDLYNKKNIPQVFETLHILISMINKKwpGKTPALTNVSGQISFTKEEIAACK 246
Cdd:cd21276   81 HWRNAMMHIGLPSIFHPETTDIYDKKNMPRVVYCIHALSLYLFRL--GLAPQIHDLYGKVKFTEEEINNMK 149
CH_IQGAP1 cd21274
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif ...
105-242 1.44e-20

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: 90.05  E-value: 1.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   105 YEFLCRVSEVKIWIEAVIEEALPSEIELCVGdsLRNGVFLAKLTQRINPDLTTV--IFP------AGDKLQFKHTQNINA 176
Cdd:cd21274    5 YEYLCHLEEAKRWMEACLGEDLPPTTELEEG--LRNGVYLAKLGNFFSPKVVSLkkIYDreqtryKATGLHFRHTDNVIQ 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325014   177 FFGLVEHVGVPDSFRFELQDLYNKKNIPQVFETLHILISMINKKwpGKTPALTNVSGQISFTKEEI 242
Cdd:cd21274   83 WLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKL--GLAPQIQDLYGKVDFTEEEI 146
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
111-215 4.83e-20

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: 86.62  E-value: 4.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   111 VSEVKIWIEAVIEEALPSEIElCVGDSLRNGVFLAKLTQRINPDLTTVIFPAGdKLQFKHTQNINAFFGLVEHVGVPDSF 190
Cdd:cd00014    1 EEELLKWINEVLGEELPVSIT-DLFESLRDGVLLCKLINKLSPGSIPKINKKP-KSPFKKRENINLFLNACKKLGLPELD 78
                         90       100
                 ....*....|....*....|....*
gi 6325014   191 RFELQDLYNKKNIPQVFETLHILIS 215
Cdd:cd00014   79 LFEPEDLYEKGNLKKVLGTLWALAL 103
CH_IQGAP2 cd21275
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP2; IQ motif ...
105-213 1.21e-19

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: 87.38  E-value: 1.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   105 YEFLCRVSEVKIWIEAVIEEALPSEIELcvGDSLRNGVFLAKLTQRINPDLTT--VIFPAGDK------LQFKHTQNINA 176
Cdd:cd21275   28 YEYLCHLEEAKQWIEACLNEELPPTTEL--EEGLRNGVYLVKLAKFFAPKLVSekKIYDVDQVrykrsgLHFRHTDNTVQ 105
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 6325014   177 FFGLVEHVGVPDSFRFELQDLYNKKNIPQVFETLHIL 213
Cdd:cd21275  106 WLRAMESIGLPKIFYPETTDVYDRKNMPRVIYCIHAL 142
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
113-213 3.13e-17

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: 78.51  E-value: 3.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   113 EVKIWIEAVIEEALPSEieLCVGDSLRNGVFLAKLTQRINPDLTTVIfpAGDKLQFKHTQNINAFFGLVEHVGVPDSFRF 192
Cdd:cd21207    9 EALDWIEAVTGEKLDDG--KDYEDVLKDGVILCKLINILKPGSVKKI--NTSKMAFKLMENIENFLTACKGYGVPKTDLF 84
                         90       100
                 ....*....|....*....|.
gi 6325014   193 ELQDLYNKKNIPQVFETLHIL 213
Cdd:cd21207   85 QTVDLYEKKNIPQVTNCLFAL 105
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
871-1100 3.34e-14

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: 74.45  E-value: 3.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   871 NDRERSYFTRFVCEMLQNAINEAPSiesfLDNRSQFWQTILQDFLRR--ESPEFFSIIVPVLDYLSDPVV-----DFESD 943
Cdd:cd04519    2 EYRLLSLLLTESPLALLRELSQVLP----VKDKEEVATALLRIFESRglALEFLRYLVRSEVKNTKNPNTlfrgnSLATK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   944 PYKIYQEIHGFSS-PQHCSPVDDA-----------STKNKFIDNLRCLWHAIEMVAEIYTRKVHTI---PVEIRYLCTKI 1008
Cdd:cd04519   78 LLDQYMKLVGQEYlKETLSPLIREileskesceidTKLPVGEDLEENLENLLELVNKLVDRILSSLdrlPPELRYVFKIL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014  1009 FCYAADKNIEE-IDSLRAISSILVNVFVSEYLVNREYYGYKDSNVQKNNQK----IDILMKSLATVFEIKNFDGFLDPLN 1083
Cdd:cd04519  158 REFLAERFPEEpDEAYQAVSGFLFLRFICPAIVSPELFGLVPDEPSEQARRnltlISKVLQSLANGVEFGDKEPFMKPLN 237
                        250
                 ....*....|....*..
gi 6325014  1084 QYANEIKPHIKDVLYNV 1100
Cdd:cd04519  238 DFIKSNKPKLKQFLDEL 254
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
113-213 1.34e-13

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: 68.11  E-value: 1.34e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014      113 EVKIWIEAVIEEALPSEIElCVGDSLRNGVFLAKLTQRINPDLTTVIFPAGDKLQFKHTQNINAFFGLVEHVGvPDSFRF 192
Cdd:smart00033    2 TLLRWVNSLLAEYDKPPVT-NFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLG-GKVVLF 79
                            90       100
                    ....*....|....*....|..
gi 6325014      193 ELQDLY-NKKNIPQVFETLHIL 213
Cdd:smart00033   80 EPEDLVeGPKLILGVIWTLISL 101
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
113-213 9.58e-12

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: 62.77  E-value: 9.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   113 EVKIWIEAVIEEALPsEIELCvgDSLRNGVFLAKLTQRINPDLTTVIFPAgdKLQFKHTQNINAFFGLVEHVGVPDSFRF 192
Cdd:cd21210    4 EAREWIEEVLGEKLA-QGDLL--DALKDGVVLCKLANRILPADIRKYKES--KMPFVQMENISAFLNAARKLGVPENDLF 78
                         90       100
                 ....*....|....*....|.
gi 6325014   193 ELQDLYNKKNIPQVFETLHIL 213
Cdd:cd21210   79 QTVDLFERKNPAQVLQCLHAL 99
SCP1 COG5199
Calponin [Cytoskeleton];
113-228 1.78e-10

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 61.47  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   113 EVKIWIEAVIEEALPSEIELCvgDSLRNGVFLAKLtqrINPDLTTVIFPAGDKLQFKHTQNINAFFGLVEHVGVPDSFRF 192
Cdd:COG5199   17 EVTLWIETVLGEKFEPPGDLL--SLLKDGVRLCRI---LNEASPLDIKYKESKMPFVQMENISSFINGLKKLRVPEYELF 91
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 6325014   193 ELQDLYNKKNIPQVFETLHILISMINKKWPGKTPAL 228
Cdd:COG5199   92 QTNDLFEAKDLRQVVICLYSLSRYAQKERMFSGPFL 127
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
108-219 1.31e-09

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: 56.91  E-value: 1.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014     108 LCRVSEVKIWIEAVIEEALPSEIELCVGDSLRNGVFLAKLTQRINPDLTTVIFPAGDklQFKHTQNINAFFGLVE-HVGV 186
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS--EFDKLENINLALDVAEkKLGV 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 6325014     187 PDSFRfELQDLYNKKNIpQVFETLHILISMINK 219
Cdd:pfam00307   79 PKVLI-EPEDLVEGDNK-SVLTYLASLFRRFQA 109
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
884-1058 2.26e-08

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: 56.14  E-value: 2.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014     884 EMLQNAINEAPSIESFLDNRSqFWQTILQDFLRRESPEFF--SIIVPVL-DYLSDPVVDFESDPYKIYQEIHGFSSPQHC 960
Cdd:pfam00616    4 ELIEEEIESSDNPNDLLRGNS-LVSKLLETYNRRPRGQEYlkKVLGPLVrKIIEDEDLDLESDPRKIYESLINQEELKTG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014     961 SPV-----------DDASTKNKFIDNLRCL-------WHAIEmvaeiytRKVHTIPVEIRYLCTKIF----CYAADKNIE 1018
Cdd:pfam00616   83 RSDlprdvspeeaiEDPEVRQIFEDNLQKLreladefLDAIY-------SSLNQLPYGIRYICKQLYelleEKFPDASEE 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 6325014    1019 EIdsLRAISSILVNVFVSEYLVNREYYGYKDSNVQKNNQK 1058
Cdd:pfam00616  156 EI--LNAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRR 193
CH_VAV cd21201
calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic ...
125-213 7.16e-08

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: 52.26  E-value: 7.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   125 ALPSEIELCVGDS--------LRNGVFLAKLTQRINP---DLTTvIFPAGDKLQFKHTQNINAFFG-LVEHVGVPDSFRF 192
Cdd:cd21201   15 VLPPDHRATQPNAtvfdlaqaLRDGVLLCQLLNRLSPgsvDDRE-INLRPQMSQFLCLKNIRTFLQaCRTVFGLRSADLF 93
                         90       100
                 ....*....|....*....|.
gi 6325014   193 ELQDLYNKKNIPQVFETLHIL 213
Cdd:cd21201   94 EPEDLYDVTNFGKVIRTLSKL 114
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
111-198 7.59e-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: 52.34  E-value: 7.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   111 VSEVKIWIEAVIEEALPSEIelcVGDSLRNGVFLAKLTQRINPDLTTVIfpagDKLQ--FKHTQNINAFFGLVEHVGVPD 188
Cdd:cd21208    2 LKEARTWIEAVTGKKFPSDD---FRESLEDGILLCELINAIKPGSIKKI----NRLPtpIAGLDNLNLFLKACEDLGLKD 74
                         90
                 ....*....|
gi 6325014   189 SFRFELQDLY 198
Cdd:cd21208   75 SQLFDPTDLQ 84
CH_CNN3 cd21284
calponin homology (CH) domain found in calponin-3; Calponin-3 (CNN3), also called acidic ...
113-220 2.34e-04

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: 42.20  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   113 EVKIWIEAVIEEALPSEIELcvgdSLRNGVFLAKLTQRINPDLTTVIFPAgdKLQFKHTQNINAFFGLVEHVGVPDSFRF 192
Cdd:cd21284    9 ELRNWIEEVTGMSIGENFQK----GLKDGVILCELINKLQPGSIRKINES--KLNWHQLENIGNFIKAIQAYGMKPHDIF 82
                         90       100
                 ....*....|....*....|....*...
gi 6325014   193 ELQDLYNKKNIPQVFETLHILISMINKK 220
Cdd:cd21284   83 EANDLFENGNMTQVQTTLLALAGLAKTK 110
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
117-197 8.11e-04

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: 40.48  E-value: 8.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   117 WIEAVIEEAL---PSEIELCVgdSLRNGVFLAKLTQRINPD-----LTTVIFPAGDKLQFKHTQ-NINAFFGLVEHVGVP 187
Cdd:cd21203    8 WIQNVLGVLVlpdPSEEEFRL--CLRDGVVLCKLLNKLQPGavpkvVESPDDPDGAAGSAFQYFeNVRNFLVAIEEMGLP 85
                         90
                 ....*....|
gi 6325014   188 dsfRFELQDL 197
Cdd:cd21203   86 ---TFEASDL 92
CH_CNN1 cd21282
calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), ...
113-220 3.25e-03

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: 38.70  E-value: 3.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014   113 EVKIWIEAVIEEALPSEIElcvgDSLRNGVFLAKLTQRINPDLTTVIfpaGDKLQFKHT-QNINAFFGLVEHVGVPDSFR 191
Cdd:cd21282    7 ELRVWIEGVTGRRIGDNFM----DGLKDGVILCELINKLQPGSVRKI---NESTQNWHKlENIGNFIKAIMHYGVKPHDI 79
                         90       100
                 ....*....|....*....|....*....
gi 6325014   192 FELQDLYNKKNIPQVFETLHILISMINKK 220
Cdd:cd21282   80 FEANDLFENTNHTQVQSTLIALASMAKTK 108
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
1013-1362 4.36e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 41.96  E-value: 4.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014    1013 ADKNIEE--IDSLRAISSILVNVFVSEYLVNREYYGYKDSNVQKNNQKIDILMKSLATVF-EIK------NFDGFLDPLN 1083
Cdd:TIGR01612 1027 ATNDIEQkiEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAEINITNFnEIKeklkhyNFDDFGKEEN 1106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014    1084 -QYANEIKpHIKDVLYNVlvdpeyEQEGDRLIyldmvspspklelltEKVLEISGKFEEYLNEF-PEADILHDILEKNLD 1161
Cdd:TIGR01612 1107 iKYADEIN-KIKDDIKNL------DQKIDHHI---------------KALEEIKKKSENYIDEIkAQINDLEDVADKAIS 1164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014    1162 NSSFPrsgrvtlELDASAYRFLVSDDKMRKIYDQVKRAFVYMMQIEDVDTNL---------YDLSISTIlpqdepnfanF 1232
Cdd:TIGR01612 1165 NDDPE-------EIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLeevkginlsYGKNLGKL----------F 1227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325014    1233 LEQ--NPKIRDDPMIQKLKplKYFTLKNVTLKKIHELESTGTFCSSDNKLQNFLNdiantIKNPNYAIDYVT-----QEI 1305
Cdd:TIGR01612 1228 LEKidEEKKKSEHMIKAME--AYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFN-----ISHDDDKDHHIIskkhdENI 1300
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 6325014    1306 YITKETLTKISEMNhSLDIELSRLKKHVDHTIKDFQKAKDFSPVHKSKFGNFKNAVK 1362
Cdd:TIGR01612 1301 SDIREKSLKIIEDF-SEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILK 1356
 
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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