|
Name |
Accession |
Description |
Interval |
E-value |
| RasGAP_IQGAP2 |
cd05131 |
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ... |
916-1274 |
0e+00 |
|
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: 744.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 916 DTVIFTLYNYASNQREEYLLLKLFKTALEEEIKSKVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 995
Cdd:cd05131 1 DTVIFTLYNYASNQREEYLLLKLFETALEEEIKSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 996 KALVINTNPVEVYKAWVNQLETQTGEASKLPYDVTTEQALTYPEVKNKLEASIENLRKVTDKVLGSIISSLDLLPYGLRY 1075
Cdd:cd05131 81 KSLIINTNPVEVYKAWVNQLETATGEASKLPYDVTTEQALTHPEVVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1076 IAKVLKNSIREKFPDATEEELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQINSNQRRNLGSVAKVLQHAASNKLFE 1155
Cdd:cd05131 161 IAKVLKNSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHSEQRRNLGSVAKVLQHAASNKLFE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1156 GENEHLSSMNNYLSETYQEFRKYFQEACDVPEPEEKFNMDKYTDLVTVSKPVIYISIEEIINTHLLLLEHQDAIATEKSD 1235
Cdd:cd05131 241 GENAHLSSMNSYLSQTYQKFRKFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIAPDQND 320
|
330 340 350
....*....|....*....|....*....|....*....
gi 118344444 1236 LLNELLESLGEVPTVESFLGEGAVDPNDPNKENTLNQLS 1274
Cdd:cd05131 321 LLHELLKDLGEVPDVESFLGEGTVDPNDPNKENTLSQLG 359
|
|
| CH_IQGAP2 |
cd21275 |
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP2; IQ motif ... |
11-166 |
6.34e-117 |
|
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: 363.95 E-value: 6.34e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 11 RPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKRWMEVCLVEELPPTTELEEGLRNGVYLAKLAKFFAPKMVSEK 90
Cdd:cd21275 1 RPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKQWIEACLNEELPPTTELEEGLRNGVYLVKLAKFFAPKLVSEK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118344444 91 KIYDVEQTRYKKSGLHFRHTDNTVQWLRAMEAIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGIAPQIQ 166
Cdd:cd21275 81 KIYDVDQVRYKRSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNMPRVIYCIHALSLYLFKLGIAPQIQ 156
|
|
| RasGAP |
smart00323 |
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ... |
905-1257 |
1.34e-90 |
|
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: 298.07 E-value: 1.34e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 905 QMPQNKSTKFMDTVIFTLYNYASNQREEYLLLKLFKTALEeeIKSKVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQL 984
Cdd:smart00323 1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLS--LASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 985 LAPVVKEIIED----KALVINTNPVEVYKAWVNQLETQTGEASKLPYDVTTEQALTYPEVKNK---LEASIENLRKVTDK 1057
Cdd:smart00323 79 IDPEVERTDDPntifRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEgedLETNLENLLQYVER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1058 VLGSIISSLDLLPYGLRYIAKVLKNSIREKFPDAteEELLKIVGNLLYYRYMNPAIVAPDGFDIIDMtaggQINSNQRRN 1137
Cdd:smart00323 159 LFDAIINSSDRLPYGLRDICKQLRQAAEKRFPDA--DVIYKAVSSFVFLRFFCPAIVSPKLFNLVDE----HPDPTTRRT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1138 LGSVAKVLQHAASNKLFEGENEHLSSMNNYLSETYQEFRKYFQEACDVPEPeekfNMDKYTDLVTVskpviyiSIEEIIN 1217
Cdd:smart00323 233 LTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEI----LVDKVSDSTTI-------SGRELSL 301
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 118344444 1218 THLLLLEHQDAIATEKS--DLLNELLESLGEVPTVESFLGEG 1257
Cdd:smart00323 302 LHSLLLENGDALKRELNneDPLGKLLFKLRYFGLTTHELTYG 343
|
|
| RasGAP |
pfam00616 |
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ... |
938-1150 |
2.50e-73 |
|
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: 243.35 E-value: 2.50e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 938 LFKTALEEEIKSkVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIEDKALVINTNPVEVYKAWVNQLET 1017
Cdd:pfam00616 1 LISELIEEEIES-SDNPNDLLRGNSLVSKLLETYNRRPRGQEYLKKVLGPLVRKIIEDEDLDLESDPRKIYESLINQEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1018 QTGEaSKLPYDVTTEQALTYPEVKNKLEASIENLRKVTDKVLGSIISSLDLLPYGLRYIAKVLKNSIREKFPDATEEELL 1097
Cdd:pfam00616 80 KTGR-SDLPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 118344444 1098 KIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQINSNQRRNLGSVAKVLQHAAS 1150
Cdd:pfam00616 159 NAIGGFLFLRFFCPAIVNPDLFGLVD----HQISPKQRRNLTLIAKVLQNLAN 207
|
|
| IQG1 |
COG5261 |
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ... |
784-1575 |
3.23e-61 |
|
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: 229.77 E-value: 3.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 784 IRKFVYLLDQSDLD---------FQEELEVARLREEVVTKIRANQQLEKDLNLMDIK----IGLLVKNRITLEDVISHRK 850
Cdd:COG5261 274 TRRSTSVFYTISLEmisnveqafFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFAE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 851 KLNkkkggeiEILNNTDnkgiKSLSKERRktLETYQQLFYLLQTK-PSYL--------------AKLIFQMPQNKSTKFM 915
Cdd:COG5261 354 RLQ-------SNINGRK----KYFPLDRR--LSLFGPLFFLLQSSiPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 916 dtvIFTLYNYASNQREEYLLLKLFKTALEEEIKSKVDqVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 995
Cdd:COG5261 421 ---IRKLYSLGKSNCEEHLSVSLFQMLLRTEVEATSL-VQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIH 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 996 KALVINTNPVEVYKAWVNQLETQTGEASKLpyDVTTEQALTYPEVKNKL-EASIENLRKVTDKVLGSIISSLDLLPYGLR 1074
Cdd:COG5261 497 EDLEVDINPLLVYRALLNKGQLSPDKDLEL--LTSNEEVSEFLAVMNAVqESSAKLLELSTERILDAVYNSLDEIGYGIR 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1075 YIAKVLK-------NSIREKFPDA--------TEEELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQINSNQRRnLG 1139
Cdd:COG5261 575 FVCELIRvvfeltpNRLFPSISDSrclrticfAEIDSLGLIGGFFFLRFVNEALVSPQTSMLKD----SCPSDNVRK-LA 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1140 SVAKVLQhaasnKLFEGEN--EHLSSMNNYLSETYQEFRKYFQEACDVPEPEEKFNMDKYTDLVTVSKPVIYIsIEEIIN 1217
Cdd:COG5261 650 TLSKILQ-----SVFEITSsdKFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYL-VNEIYL 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1218 THLLLLEHQDAIaTEKSDLLNELLESLGEVPTVesflgegavdPNDPNKentlnqlskTEISLSLTSKYDVKDGEAvdgR 1297
Cdd:COG5261 724 THEIIIEYLDNL-YDPDSLVDLLLQELGELCSF----------PQDQRD---------TLNCLVTLPLFNRSDDPI---R 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1298 SLMIKTKKLIIDVTRNQPGSTLTEIL------ETPATgQQELEHAKDMESRAVVDSRTPEEgkqsqaviedarlpLEQKK 1371
Cdd:COG5261 781 DLKQQLKRTRVYIIYVDAGTNLFEQLlrllpsDEPAT-RNPLDLNPNIRDDPSVSSLKSMS--------------LMKLK 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1372 RKIQRNLRTLEQTGHVSSKNKYQDILNEIAKDIRNQRIHRKLRKAELSKLQQTLNALNKKAAFYEDQINYYDTYIKTCVD 1451
Cdd:COG5261 846 IRAIELLDELETLGFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARS 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1452 NLKRKNSrrsiKLDGKAEPKGTKRVKP-------VRYTAAKLHDKGVLLGIDDLQTNqFKNVMFDIIATE-DMGIFDVRS 1523
Cdd:COG5261 926 QLQPKKS----KLKGFSRGVGVVRDKPksissgtFKYSAQQLYKRGVLVNITIPEPN-VSNIYFTFSSDStDNFVIEVYQ 1000
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 118344444 1524 KFLGVEMEKVQLNIQDLLQMQYEGVAVMKMFDKVKVNVNLLIYLLNKKFYGK 1575
Cdd:COG5261 1001 PGHSVSLPEVSFCFDDLLKRQYNKNPVVDLGGFLTFNANKLLHLIESKFYRK 1052
|
|
| RasGAP_C |
pfam03836 |
RasGAP C-terminus; This domain can be found in the C terminus of the IQGAP family members, ... |
1367-1499 |
2.01e-43 |
|
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: 154.63 E-value: 2.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1367 LEQKKRKIQRNLRTLEQTGHVSSKNKYQDILNEIAKDIRNQRIHRKLRKAELSKLQQTLNALNKKAAFYEDQINYYDTYI 1446
Cdd:pfam03836 1 YVELKKKALENLLELESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 118344444 1447 KTCVDNLKRKNSRR--SIKLDGKAEPKGTKRVK--PVRYTAAKLHDKGVLLGIDDLQ 1499
Cdd:pfam03836 81 ENCLDNLQKKKKKLfsKQYFHYRKLQKRGKLPKfgSYKYSARQLYEKGVLLEIEGVP 137
|
|
| IQG1 |
COG5261 |
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ... |
4-211 |
3.76e-34 |
|
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: 143.10 E-value: 3.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 4 EELPSLQRPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKRWMEVCLVEELPpTTELEEGLRNGVYLAKLAKFFA 83
Cdd:COG5261 6 GSLNRYVENLGRPIGTPSHLKTKTSAKNRSALRAYEYLCRVSEAKIWIEEVIEEALP-ELCFEDSLRNGVFLAKLTQRFN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 84 PKMVseKKIYdveqtryKKSGLHFRHTDNTVQWLRAMEAIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGIAP 163
Cdd:COG5261 85 PDLT--TVIF-------PADKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 118344444 164 QIQDLLGKVdFTEEEISNMRKELEkygiQMPAFSKIGGILANELSVDE 211
Cdd:COG5261 156 LINSSGQIS-FTKEDIAACKKAWP----RIPDFKSLGTNINTAASPEE 198
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
45-152 |
2.80e-11 |
|
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: 61.56 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 45 EEAKRWMEVCLVEELPPT-TELEEGLRNGVYLAKLAKFFAPKMVSEKKIydveqtryKKSGLHFRHTDNTVQWLRAMEAI 123
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPvTNFSSDLKDGVALCALLNSLSPGLVDKKKV--------AASLSRFKKIENINLALSFAEKL 72
|
90 100 110
....*....|....*....|....*....|
gi 118344444 124 GlPKIFYPETTDVYD-RKNIPRMIYCIHAL 152
Cdd:smart00033 73 G-GKVVLFEPEDLVEgPKLILGVIWTLISL 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
45-155 |
3.28e-11 |
|
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: 61.53 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 45 EEAKRWMEVCLVEELPPT--TELEEGLRNGVYLAKLAKFFAPKMVSEKKIYDVEqtrykksglhFRHTDNTVQWLR-AME 121
Cdd:pfam00307 5 KELLRWINSHLAEYGPGVrvTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSE----------FDKLENINLALDvAEK 74
|
90 100 110
....*....|....*....|....*....|....
gi 118344444 122 AIGLPKIFyPETTDVYDRKNIpRMIYCIHALSLY 155
Cdd:pfam00307 75 KLGVPKVL-IEPEDLVEGDNK-SVLTYLASLFRR 106
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
689-710 |
1.23e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 37.69 E-value: 1.23e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RasGAP_IQGAP2 |
cd05131 |
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ... |
916-1274 |
0e+00 |
|
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: 744.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 916 DTVIFTLYNYASNQREEYLLLKLFKTALEEEIKSKVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 995
Cdd:cd05131 1 DTVIFTLYNYASNQREEYLLLKLFETALEEEIKSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 996 KALVINTNPVEVYKAWVNQLETQTGEASKLPYDVTTEQALTYPEVKNKLEASIENLRKVTDKVLGSIISSLDLLPYGLRY 1075
Cdd:cd05131 81 KSLIINTNPVEVYKAWVNQLETATGEASKLPYDVTTEQALTHPEVVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1076 IAKVLKNSIREKFPDATEEELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQINSNQRRNLGSVAKVLQHAASNKLFE 1155
Cdd:cd05131 161 IAKVLKNSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHSEQRRNLGSVAKVLQHAASNKLFE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1156 GENEHLSSMNNYLSETYQEFRKYFQEACDVPEPEEKFNMDKYTDLVTVSKPVIYISIEEIINTHLLLLEHQDAIATEKSD 1235
Cdd:cd05131 241 GENAHLSSMNSYLSQTYQKFRKFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIAPDQND 320
|
330 340 350
....*....|....*....|....*....|....*....
gi 118344444 1236 LLNELLESLGEVPTVESFLGEGAVDPNDPNKENTLNQLS 1274
Cdd:cd05131 321 LLHELLKDLGEVPDVESFLGEGTVDPNDPNKENTLSQLG 359
|
|
| RasGAP_IQGAP1 |
cd05133 |
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ... |
916-1288 |
0e+00 |
|
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: 602.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 916 DTVIFTLYNYASNQREEYLLLKLFKTALEEEIKSKVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 995
Cdd:cd05133 1 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 996 KALVINTNPVEVYKAWVNQLETQTGEASKLPYDVTTEQALTYPEVKNKLEASIENLRKVTDKVLGSIISSLDLLPYGLRY 1075
Cdd:cd05133 81 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQAMSHEEVRTRLDASIKNMRMVTDKFLSAIISSVDKIPYGMRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1076 IAKVLKNSIREKFPDATEEELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQINSNQRRNLGSVAKVLQHAASNKLFE 1155
Cdd:cd05133 161 IAKVLKDTLHEKFPDAGEDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1156 GENEHLSSMNNYLSETYQEFRKYFQEACDVPEPEEKFNMDKYTDLVTVSKPVIYISIEEIINTHLLLLEHQDAIATEKSD 1235
Cdd:cd05133 241 GDNAHLSPINEYLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 118344444 1236 LLNELLESLGEVPTVESFLGEGAVDPNDPNKENtlnqLSKTEISLSLTSKYDV 1288
Cdd:cd05133 321 PIHELLDDLGEVPTIESLIGENPGPPGDPNRET----LAKTEVSLTLTNKFDV 369
|
|
| RasGAP_IQGAP_like |
cd05127 |
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ... |
926-1256 |
0e+00 |
|
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: 569.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 926 ASNQREEYLLLKLFKTALEEEIKSKVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIEDKALVINTNPV 1005
Cdd:cd05127 1 ASNRREEYLLLKLFKTALREEIESKVSLPEDIVTGNPTVIKLVVNYNRGPRGQKYLRELLGPVVKEILDDDDLDLETDPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1006 EVYKAWVNQLETQTGEASKLPYDVTTEQALTYPEVKNKLEASIENLRKVTDKVLGSIISSLDLLPYGLRYIAKVLKNSIR 1085
Cdd:cd05127 81 DIYKAWINQEESRTGEPSKLPYDVTREQALKDPEVRKRLIEHLEKLRAITDKFLTAITESLDKMPYGMRYIAKVLKEALR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1086 EKFPDATEEELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQINSNQRRNLGSVAKVLQHAASNKLFEGENEHLSSMN 1165
Cdd:cd05127 161 EKFPDAPEEEILKIVGNLLYYRYMNPAIVAPEAFDIIDLSVGGQLSPLQRRNLGSIAKVLQQAASGKLFGGENPYLSPLN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1166 NYLSETYQEFRKYFQEACDVPEPEEKFNMDKYTDLVTVSKPVIYISIEEIINTHLLLLEHQDAIATEKSDLLNELLESLG 1245
Cdd:cd05127 241 PYISESHEKFKKFFLEACTVPEAEEHFNIDEYSDLTMLTKPTIYISLQEIFATHKLLLEHQDEIAPDPDDPLRELLDDLG 320
|
330
....*....|.
gi 118344444 1246 EVPTVESFLGE 1256
Cdd:cd05127 321 PAPTIESLLGS 331
|
|
| RasGAP_IQGAP3 |
cd12207 |
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ... |
916-1263 |
2.14e-180 |
|
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: 542.50 E-value: 2.14e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 916 DTVIFTLYNYASNQREEYLLLKLFKTALEEEIKSKVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 995
Cdd:cd12207 1 ESVIFSLYNYASNRREAYLLLQLFKTALQEEISSKVEKPQDVITGNPTVIRLLVSFYRSARGQNALRHILGPVVQDVLQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 996 KALVINTNPVEVYKAWVNQLETQTGEASKLPYDVTTEQALTYPEVKNKLEASIENLRKVTDKVLGSIISSLDLLPYGLRY 1075
Cdd:cd12207 81 KGLSIRTDPVQIYKAWINQTETQSGCRSSLPYEVSPEQALSHPEVQRRLDIAIRNLLAVTDKFLSAITSSVDKIPYGMRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1076 IAKVLKNSIREKFPDATEEELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQINSNQRRNLGSVAKVLQHAASNKLFE 1155
Cdd:cd12207 161 VAKVLRDSLQEKFPGASEDEVYKVVGNLLYYRFMNPAVVAPDGFDIVDCSAGGALQPEQRRMLGSVAKVLQHAAANKHFQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1156 GENEHLSSMNNYLSETYQEFRKYFQEACDVPEPEEKFNMDKYTDLVTVSKPVIYISIEEIINTHLLLLEHQDAIATEKSD 1235
Cdd:cd12207 241 GDSEHLQALNQYLEETHVKFRKFILQACCVPEPEERFNVDEYSEMVAVAKPVIYITVGELINTHKLLLEHQDSIAPDHSD 320
|
330 340
....*....|....*....|....*...
gi 118344444 1236 LLNELLESLGEVPTVESFLGEGAVDPND 1263
Cdd:cd12207 321 PLHELLEDLGEVPTVQSLIGESWADLGD 348
|
|
| CH_IQGAP2 |
cd21275 |
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP2; IQ motif ... |
11-166 |
6.34e-117 |
|
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: 363.95 E-value: 6.34e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 11 RPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKRWMEVCLVEELPPTTELEEGLRNGVYLAKLAKFFAPKMVSEK 90
Cdd:cd21275 1 RPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKQWIEACLNEELPPTTELEEGLRNGVYLVKLAKFFAPKLVSEK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118344444 91 KIYDVEQTRYKKSGLHFRHTDNTVQWLRAMEAIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGIAPQIQ 166
Cdd:cd21275 81 KIYDVDQVRYKRSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNMPRVIYCIHALSLYLFKLGIAPQIQ 156
|
|
| CH_IQGAP1 |
cd21274 |
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif ... |
34-187 |
2.80e-91 |
|
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: 292.28 E-value: 2.80e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 34 QNIAYEYLCHLEEAKRWMEVCLVEELPPTTELEEGLRNGVYLAKLAKFFAPKMVSEKKIYDVEQTRYKKSGLHFRHTDNT 113
Cdd:cd21274 1 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118344444 114 VQWLRAMEAIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGIAPQIQDLLGKVDFTEEEISNMRKELE 187
Cdd:cd21274 81 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTELE 154
|
|
| RasGAP |
smart00323 |
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ... |
905-1257 |
1.34e-90 |
|
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: 298.07 E-value: 1.34e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 905 QMPQNKSTKFMDTVIFTLYNYASNQREEYLLLKLFKTALEeeIKSKVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQL 984
Cdd:smart00323 1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLS--LASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 985 LAPVVKEIIED----KALVINTNPVEVYKAWVNQLETQTGEASKLPYDVTTEQALTYPEVKNK---LEASIENLRKVTDK 1057
Cdd:smart00323 79 IDPEVERTDDPntifRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEgedLETNLENLLQYVER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1058 VLGSIISSLDLLPYGLRYIAKVLKNSIREKFPDAteEELLKIVGNLLYYRYMNPAIVAPDGFDIIDMtaggQINSNQRRN 1137
Cdd:smart00323 159 LFDAIINSSDRLPYGLRDICKQLRQAAEKRFPDA--DVIYKAVSSFVFLRFFCPAIVSPKLFNLVDE----HPDPTTRRT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1138 LGSVAKVLQHAASNKLFEGENEHLSSMNNYLSETYQEFRKYFQEACDVPEPeekfNMDKYTDLVTVskpviyiSIEEIIN 1217
Cdd:smart00323 233 LTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEI----LVDKVSDSTTI-------SGRELSL 301
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 118344444 1218 THLLLLEHQDAIATEKS--DLLNELLESLGEVPTVESFLGEG 1257
Cdd:smart00323 302 LHSLLLENGDALKRELNneDPLGKLLFKLRYFGLTTHELTYG 343
|
|
| CH_IQGAP3 |
cd21276 |
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP3; IQ motif ... |
35-186 |
1.02e-89 |
|
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: 287.65 E-value: 1.02e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 35 NIAYEYLCHLEEAKRWMEVCLVEELPPTTELEEGLRNGVYLAKLAKFFAPKMVSEKKIYDVEQTRYKKSGLHFRHTDNTV 114
Cdd:cd21276 1 NVAYQYLCRLEEAKRWMEACLKEELPPPTELEESLRNGVYLAKLGHCFAPRVVPLKKIYDLEQMRYQATGLHFRHTDNIN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118344444 115 QWLRAMEAIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGIAPQIQDLLGKVDFTEEEISNMRKEL 186
Cdd:cd21276 81 HWRNAMMHIGLPSIFHPETTDIYDKKNMPRVVYCIHALSLYLFRLGLAPQIHDLYGKVKFTEEEINNMKLEL 152
|
|
| RasGAP |
pfam00616 |
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ... |
938-1150 |
2.50e-73 |
|
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: 243.35 E-value: 2.50e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 938 LFKTALEEEIKSkVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIEDKALVINTNPVEVYKAWVNQLET 1017
Cdd:pfam00616 1 LISELIEEEIES-SDNPNDLLRGNSLVSKLLETYNRRPRGQEYLKKVLGPLVRKIIEDEDLDLESDPRKIYESLINQEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1018 QTGEaSKLPYDVTTEQALTYPEVKNKLEASIENLRKVTDKVLGSIISSLDLLPYGLRYIAKVLKNSIREKFPDATEEELL 1097
Cdd:pfam00616 80 KTGR-SDLPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 118344444 1098 KIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQINSNQRRNLGSVAKVLQHAAS 1150
Cdd:pfam00616 159 NAIGGFLFLRFFCPAIVNPDLFGLVD----HQISPKQRRNLTLIAKVLQNLAN 207
|
|
| CH_IQGAP |
cd21206 |
calponin homology (CH) domain found in the IQ motif containing GTPase activating protein ... |
35-160 |
3.24e-68 |
|
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: 224.80 E-value: 3.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 35 NIAYEYLCHLEEAKRWMEVCLVEELPPTTELEEGLRNGVYLAKLAKFFAPKMVSEKKIYDVeqtrykksGLHFRHTDNTV 114
Cdd:cd21206 1 TIAYEYLCRLEEAKQWIEACLNEELPPTTEFEEELRNGVVLAKLANKFAPKLVPLKKIYDV--------GLQFRHTDNIN 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 118344444 115 QWLRAMEAIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLG 160
Cdd:cd21206 73 HFLRALKKIGLPKIFHFETTDLYEKKNIPKVIYCLHALSLLLFKLG 118
|
|
| RasGAP_GAPA |
cd05132 |
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ... |
914-1287 |
2.54e-65 |
|
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: 225.69 E-value: 2.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 914 FMDTVIFTLYNYASNQREEYLLLKLFKTALEEEIKSKVDqVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEII 993
Cdd:cd05132 5 LLQTVMFTLYGNQYESREEHLLLSMFQSVLTYEFDETTE-FGSLLRANTAVSRMMTTYTRRGPGQSYLKTVLADRINDLI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 994 EDKALVINTNPVEVYKAWVNQLETQTGEASKLPYDVTTEQALTYPEVKNKLEASIENLRKVTDKVLGSIISSLDLLPYGL 1073
Cdd:cd05132 84 SLKDLNLEINPLKVYEQMINDIELDTGLPSNLPRGITPEEAAENPAVQNIIEPRLEMLEEITNSFLEAIINSLDEVPYGI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1074 RYIAKVLKNSIREKFPDATEEELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQINSNQRRNLGSVAKVLQHAASNKL 1153
Cdd:cd05132 164 RWICKQIRSLTRRKFPDASDETICSLIGGFFLLRFINPAIVSPQAYMLVD----GKPSDNTRRTLTLIAKLLQNLANKPS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1154 FEGEnEHLSSMNNYLSETYQEFRKYFQEACDVPEPEEKFNMDKYtdlVTVSKPVIYISI--EEIINTHLLLLEHQDAIAT 1231
Cdd:cd05132 240 YSKE-PYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQY---IALSKKDLSINItlNEIYNTHSLLVKHLAELAP 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 118344444 1232 EKSDLLNELLESLGEVPtvesflgegavdPNDPNKENTLnqlskteISLSLTSKYD 1287
Cdd:cd05132 316 DHNDHLRLILQELGPAP------------PQVPRKENRT-------IELPLYSRWE 352
|
|
| IQG1 |
COG5261 |
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ... |
784-1575 |
3.23e-61 |
|
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: 229.77 E-value: 3.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 784 IRKFVYLLDQSDLD---------FQEELEVARLREEVVTKIRANQQLEKDLNLMDIK----IGLLVKNRITLEDVISHRK 850
Cdd:COG5261 274 TRRSTSVFYTISLEmisnveqafFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFAE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 851 KLNkkkggeiEILNNTDnkgiKSLSKERRktLETYQQLFYLLQTK-PSYL--------------AKLIFQMPQNKSTKFM 915
Cdd:COG5261 354 RLQ-------SNINGRK----KYFPLDRR--LSLFGPLFFLLQSSiPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 916 dtvIFTLYNYASNQREEYLLLKLFKTALEEEIKSKVDqVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 995
Cdd:COG5261 421 ---IRKLYSLGKSNCEEHLSVSLFQMLLRTEVEATSL-VQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIH 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 996 KALVINTNPVEVYKAWVNQLETQTGEASKLpyDVTTEQALTYPEVKNKL-EASIENLRKVTDKVLGSIISSLDLLPYGLR 1074
Cdd:COG5261 497 EDLEVDINPLLVYRALLNKGQLSPDKDLEL--LTSNEEVSEFLAVMNAVqESSAKLLELSTERILDAVYNSLDEIGYGIR 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1075 YIAKVLK-------NSIREKFPDA--------TEEELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQINSNQRRnLG 1139
Cdd:COG5261 575 FVCELIRvvfeltpNRLFPSISDSrclrticfAEIDSLGLIGGFFFLRFVNEALVSPQTSMLKD----SCPSDNVRK-LA 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1140 SVAKVLQhaasnKLFEGEN--EHLSSMNNYLSETYQEFRKYFQEACDVPEPEEKFNMDKYTDLVTVSKPVIYIsIEEIIN 1217
Cdd:COG5261 650 TLSKILQ-----SVFEITSsdKFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYL-VNEIYL 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1218 THLLLLEHQDAIaTEKSDLLNELLESLGEVPTVesflgegavdPNDPNKentlnqlskTEISLSLTSKYDVKDGEAvdgR 1297
Cdd:COG5261 724 THEIIIEYLDNL-YDPDSLVDLLLQELGELCSF----------PQDQRD---------TLNCLVTLPLFNRSDDPI---R 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1298 SLMIKTKKLIIDVTRNQPGSTLTEIL------ETPATgQQELEHAKDMESRAVVDSRTPEEgkqsqaviedarlpLEQKK 1371
Cdd:COG5261 781 DLKQQLKRTRVYIIYVDAGTNLFEQLlrllpsDEPAT-RNPLDLNPNIRDDPSVSSLKSMS--------------LMKLK 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1372 RKIQRNLRTLEQTGHVSSKNKYQDILNEIAKDIRNQRIHRKLRKAELSKLQQTLNALNKKAAFYEDQINYYDTYIKTCVD 1451
Cdd:COG5261 846 IRAIELLDELETLGFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARS 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1452 NLKRKNSrrsiKLDGKAEPKGTKRVKP-------VRYTAAKLHDKGVLLGIDDLQTNqFKNVMFDIIATE-DMGIFDVRS 1523
Cdd:COG5261 926 QLQPKKS----KLKGFSRGVGVVRDKPksissgtFKYSAQQLYKRGVLVNITIPEPN-VSNIYFTFSSDStDNFVIEVYQ 1000
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 118344444 1524 KFLGVEMEKVQLNIQDLLQMQYEGVAVMKMFDKVKVNVNLLIYLLNKKFYGK 1575
Cdd:COG5261 1001 PGHSVSLPEVSFCFDDLLKRQYNKNPVVDLGGFLTFNANKLLHLIESKFYRK 1052
|
|
| RasGAP_C |
pfam03836 |
RasGAP C-terminus; This domain can be found in the C terminus of the IQGAP family members, ... |
1367-1499 |
2.01e-43 |
|
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: 154.63 E-value: 2.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1367 LEQKKRKIQRNLRTLEQTGHVSSKNKYQDILNEIAKDIRNQRIHRKLRKAELSKLQQTLNALNKKAAFYEDQINYYDTYI 1446
Cdd:pfam03836 1 YVELKKKALENLLELESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 118344444 1447 KTCVDNLKRKNSRR--SIKLDGKAEPKGTKRVK--PVRYTAAKLHDKGVLLGIDDLQ 1499
Cdd:pfam03836 81 ENCLDNLQKKKKKLfsKQYFHYRKLQKRGKLPKfgSYKYSARQLYEKGVLLEIEGVP 137
|
|
| RasGAP |
cd04519 |
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ... |
931-1184 |
3.63e-38 |
|
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: 144.17 E-value: 3.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 931 EEYLLLKLFKTALEEEIKSKVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIEDKALV----INTNPVE 1006
Cdd:cd04519 1 EEYRLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNTKNPNTLFrgnsLATKLLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1007 VYKAWVNQlETQTGEASKLPYDVTTEQAL----TYPEVKNKLEASIENLRKVTDKVLGSIISSLDLLPYGLRYIAKVLKN 1082
Cdd:cd04519 81 QYMKLVGQ-EYLKETLSPLIREILESKESceidTKLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILRE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1083 SIREKFPDATEEElLKIVGNLLYYRYMNPAIVAPDGFDIIDMtaggQINSNQRRNLGSVAKVLQHAASNKLFEGENEHLS 1162
Cdd:cd04519 160 FLAERFPEEPDEA-YQAVSGFLFLRFICPAIVSPELFGLVPD----EPSEQARRNLTLISKVLQSLANGVEFGDKEPFMK 234
|
250 260
....*....|....*....|..
gi 118344444 1163 SMNNYLSETYQEFRKYFQEACD 1184
Cdd:cd04519 235 PLNDFIKSNKPKLKQFLDELSS 256
|
|
| RasGAP_IQGAP_related |
cd12206 |
Ras-GTPase Activating Domain of proteins related to IQGAPs; RasGAP: Ras-GTPase Activating ... |
912-1276 |
1.06e-35 |
|
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: 140.16 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 912 TKFMDTVIFTLYNYASN----QREEYLLLKLFKTALEEEIKsKVDQVQDIVTGNPTV-IKMVVSFNRgaRGQNTLRQ-LL 985
Cdd:cd12206 4 IEKNVYVTLPIFQKPTNgkmdSREEFLFIKFILELLKSDIE-NSNSNQDFLANSDNFwILLLVTFNN--LRERSELKsIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 986 APVVKEIIEDKALVINTNPVEVYKawvnQLETQTGEASklpydvttEQALTYPEVKNKLEASIENLRKVTDKVLGSIISS 1065
Cdd:cd12206 81 GPLLVQYLENQEIDFESDPSVIYK----SLHGRPPLSS--------EEAIEDDRVSDKFVENLTNLREAVEMVAEIIFKN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1066 LDLLPYGLRYIAKVLKNSIREKFPDATEEELLKIVGNLLYYRYMNPAIVAPDGFDiidmtaggqINSNQRRNLGSVAKVL 1145
Cdd:cd12206 149 VDKIPVEIRYLCTKAYIAFADKFPDESEEDILRAISKILIKSYVAPILVNPENYG---------FVDNEEDNLNEKARVL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1146 QHAASNKLFEGE-NEHLSSMNNYLSETYQEFRKYFQEACDVPEPEEKFNMDKYTDLVTVSKPVIYISIEEIINTHLLLLE 1224
Cdd:cd12206 220 LQILSMVFFLKNfDGYLKPLNQYIEEIKPSIRDLLKELLDVPEEEQEYDKLIYYDIMSTTRPCLEILLDKVIEIIQILKE 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 118344444 1225 HQDAIAteKSDLLNELLESLGEVPTVESFLGEGAVDPN-DPNKENTLNQLSKT 1276
Cdd:cd12206 300 NLDEFT--PDDQLVQLLEKIVDLSSSSNDKRSGRVTLElNPSAYQFLVNDDKE 350
|
|
| IQG1 |
COG5261 |
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ... |
4-211 |
3.76e-34 |
|
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: 143.10 E-value: 3.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 4 EELPSLQRPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKRWMEVCLVEELPpTTELEEGLRNGVYLAKLAKFFA 83
Cdd:COG5261 6 GSLNRYVENLGRPIGTPSHLKTKTSAKNRSALRAYEYLCRVSEAKIWIEEVIEEALP-ELCFEDSLRNGVFLAKLTQRFN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 84 PKMVseKKIYdveqtryKKSGLHFRHTDNTVQWLRAMEAIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGIAP 163
Cdd:COG5261 85 PDLT--TVIF-------PADKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 118344444 164 QIQDLLGKVdFTEEEISNMRKELEkygiQMPAFSKIGGILANELSVDE 211
Cdd:COG5261 156 LINSSGQIS-FTKEDIAACKKAWP----RIPDFKSLGTNINTAASPEE 198
|
|
| RasGAP_Neurofibromin_like |
cd05392 |
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ... |
918-1193 |
1.11e-32 |
|
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: 130.10 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 918 VIFTLYNYASNqreeylLLKLFKTALEEEIkSKVDQVQDIVTGNPTVIKMVVSFNRgARGQNTLRQLLAPVVKEIIEDKA 997
Cdd:cd05392 38 SLLNLFETRNR------LLPLISWLIEDEI-SHTSRAADLFRRNSVATRLLTLYAK-SVGNKYLRKVLRPLLTEIVDNKD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 998 --LVINTNPVEVykawvnqletqtgeasklpydvtteqaltypevknKLEASIENLRKVTDKVLGSIISSLDLLPYGLRY 1075
Cdd:cd05392 110 yfEVEKIKPDDE-----------------------------------NLEENADLLMKYAQMLLDSITDSVDQLPPSFRY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1076 IAKVLKNSIREKFPDATeeelLKIVGNLLYYRYMNPAIVAPDGFDIIDMTaggqINSNQRRNLGSVAKVLQHAASNKLFE 1155
Cdd:cd05392 155 ICNTIYESVSKKFPDAA----LIAVGGFLFLRFICPAIVSPESENLLDPP----PTPEARRSLILIAKVLQNIANGVLFS 226
|
250 260 270
....*....|....*....|....*....|....*...
gi 118344444 1156 GENEHLSSMNNYLSETYQEFRKYFQEACDVPEPEEKFN 1193
Cdd:cd05392 227 LKEPYLESLNEFLKKNSDRIQQFLSEVSTIPPTDPIFD 264
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
44-154 |
1.04e-22 |
|
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: 94.33 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 44 LEEAKRWMEVCLVEELP-PTTELEEGLRNGVYLAKLAKFFAPKMVSEKKiydveqtryKKSGLHFRHTDNTVQWLRAMEA 122
Cdd:cd00014 1 EEELLKWINEVLGEELPvSITDLFESLRDGVLLCKLINKLSPGSIPKIN---------KKPKSPFKKRENINLFLNACKK 71
|
90 100 110
....*....|....*....|....*....|..
gi 118344444 123 IGLPKIFYPETTDVYDRKNIPRMIYCIHALSL 154
Cdd:cd00014 72 LGLPELDLFEPEDLYEKGNLKKVLGTLWALAL 103
|
|
| RasGAP_Neurofibromin |
cd05130 |
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ... |
1043-1230 |
5.33e-15 |
|
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the neurofibromatosis type 1 gene (NF1) and shares a region of similarity with catalytic domain of the mammalian p120RasGAP protein and an extended similarity with the Saccharomyces cerevisiae RasGAP proteins Ira1 and Ira2. Neurofibromin has been shown to function as a GAP (GTPase-activating protein) which inhibits low molecular weight G proteins such as Ras by stimulating their intrinsic GTPase activity. NF1 is a common genetic disorder characterized by various symptoms ranging from predisposition for the development of tumors to learning disability or mental retardation. Loss of neurofibromin activity can be correlated to the increase in Ras-GTP concentration in neurofibromas of NF1 of patients, supporting the notion that unregulated Ras signaling may contribute to their development.
Pssm-ID: 213332 [Multi-domain] Cd Length: 332 Bit Score: 78.13 E-value: 5.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1043 KLEASIENLRKVTDKVLGSIISSLDLLPYGLRYIAKVLKNSIREKFPdateEELLKIVGNLLYYRYMNPAIVAPDGFDII 1122
Cdd:cd05130 132 NLEENQRNLLQLTEKFFHAIISSSDEFPPQLRSVCHCLYQVVSHRFP----NSGLGAVGSAIFLRFINPAIVSPYEYGIL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1123 DmtagGQINSNQRRNLGSVAKVLQHAASNKLFEGEnEHLSSMNNYLSETYQEFRKYFQEACDVPEPEEKFNmdkytdlvt 1202
Cdd:cd05130 208 D----REPPPRVKRGLKLMSKILQNIANHVLFTKE-AHMLPFNDFLRNHFEAGRRFFSSIASDCGAVDGPS--------- 273
|
170 180
....*....|....*....|....*...
gi 118344444 1203 vSKPVIYISIEEIINTHLLLLEHQDAIA 1230
Cdd:cd05130 274 -SKYLSFINDANVLALHRLLWNNQEKIG 300
|
|
| CH_SCP1-like |
cd21210 |
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ... |
45-153 |
2.14e-13 |
|
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: 67.78 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 45 EEAKRWMEVCLVEELPPTTeLEEGLRNGVYLAKLAKFFAPKMVSekkiydveqtRYKKSGLHFRHTDNTVQWLRAMEAIG 124
Cdd:cd21210 3 QEAREWIEEVLGEKLAQGD-LLDALKDGVVLCKLANRILPADIR----------KYKESKMPFVQMENISAFLNAARKLG 71
|
90 100
....*....|....*....|....*....
gi 118344444 125 LPKIFYPETTDVYDRKNIPRMIYCIHALS 153
Cdd:cd21210 72 VPENDLFQTVDLFERKNPAQVLQCLHALS 100
|
|
| CH_dMP20-like |
cd21207 |
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ... |
46-152 |
4.16e-12 |
|
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: 64.25 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 46 EAKRWMEVCLVEELPPTTELEEGLRNGVYLAKLAKFFAPKMVseKKIYDveqtrykkSGLHFRHTDNTVQWLRAMEAIGL 125
Cdd:cd21207 9 EALDWIEAVTGEKLDDGKDYEDVLKDGVILCKLINILKPGSV--KKINT--------SKMAFKLMENIENFLTACKGYGV 78
|
90 100
....*....|....*....|....*..
gi 118344444 126 PKIFYPETTDVYDRKNIPRMIYCIHAL 152
Cdd:cd21207 79 PKTDLFQTVDLYEKKNIPQVTNCLFAL 105
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
45-152 |
2.80e-11 |
|
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: 61.56 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 45 EEAKRWMEVCLVEELPPT-TELEEGLRNGVYLAKLAKFFAPKMVSEKKIydveqtryKKSGLHFRHTDNTVQWLRAMEAI 123
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPvTNFSSDLKDGVALCALLNSLSPGLVDKKKV--------AASLSRFKKIENINLALSFAEKL 72
|
90 100 110
....*....|....*....|....*....|
gi 118344444 124 GlPKIFYPETTDVYD-RKNIPRMIYCIHAL 152
Cdd:smart00033 73 G-GKVVLFEPEDLVEgPKLILGVIWTLISL 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
45-155 |
3.28e-11 |
|
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: 61.53 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 45 EEAKRWMEVCLVEELPPT--TELEEGLRNGVYLAKLAKFFAPKMVSEKKIYDVEqtrykksglhFRHTDNTVQWLR-AME 121
Cdd:pfam00307 5 KELLRWINSHLAEYGPGVrvTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSE----------FDKLENINLALDvAEK 74
|
90 100 110
....*....|....*....|....*....|....
gi 118344444 122 AIGLPKIFyPETTDVYDRKNIpRMIYCIHALSLY 155
Cdd:pfam00307 75 KLGVPKVL-IEPEDLVEGDNK-SVLTYLASLFRR 106
|
|
| RasGAP_RAP6 |
cd05129 |
Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is ... |
881-1245 |
2.59e-10 |
|
Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is an endosomal protein with a role in the regulation of receptor-mediated endocytosis. RAP6 contains a Vps9 domain, which is involved in the activation of Rab5, and a Ras GAP domain (RGD). Rab5 is a small GTPase required for the control of the endocytic route, and its activity is regulated by guanine nucleotide exchange factor, such as Rabex5, and GAPs, such as RN-tre. Human Rap6 protein is localized on the plasma membrane and on the endosome. RAP6 binds to Rab5 and Ras through the Vps9 and RGD domains, respectively.
Pssm-ID: 213331 Cd Length: 365 Bit Score: 64.29 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 881 TLETYQQLFYLLQTKPSYLAKLIFQMPQ--NKSTK-FMDTVIFTLYNYASNQREEYLLLKLFKTALEEEIKSKVDQVQDI 957
Cdd:cd05129 9 QLSHYGEFLRILRENPQLLAECLARGEKlsLEQTQnVIQTIVTSLYGNCIMPEDERLLLQLLRELMELQLKKSDNPRRLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 958 VTGNPTVIKMVVSFNRGA-RGQNTLRQLLAPVVKEIIEDKALVINTNPvevYKAWVNqleTQTGEASKLPYDVTTeqalt 1036
Cdd:cd05129 89 RKGSCAFSRVFKLFTELLfSAKLYLTAALHKPIMQVLVDDEIFLETDP---QKALCR---FSPAEQEKRFGEEGT----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1037 yPEVKNKL-EASIENLRKV---TDKVLGSIISSLDLLPYGLRYIAKVLKNSIREKFpDATEEELLKIVGNLLYYRYMNPA 1112
Cdd:cd05129 158 -PEQQRKLqQYRAEFLSRLvalVNKFISSLRQSVYCFPQSLRWIVRQLRKILTRSG-DDEEAEARALCTDLLFTNFICPA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1113 IVAPDGFDIIDmtaGGQINSNQRRNLGSVAKVLQHAASNKLFEGENEhlssmnnyLSETYQEFRK----YFQEACDVPEP 1188
Cdd:cd05129 236 IVNPEQYGIIS---DAPISEVARHNLMQVAQILQVLALTEFESPDPR--------LKELLSKFDKdcvsAFLDVVIVGRA 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1189 EEKFNMdkYT-DLVTVSKPVIYISIEEiINTHLLLLEHQDAIATEKSDLLN--ELLESLG 1245
Cdd:cd05129 305 VETPPP--SSsALLEGSRTAVLITESD-LATLVEFLRSVKTGDEEKEDQMAldNLLKNLP 361
|
|
| RasGAP_GAP1_like |
cd05128 |
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ... |
934-1185 |
1.23e-08 |
|
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras GTPase-activating proteins includes GAP1(m) (or RASA2), GAP1_IP4BP (or RASA3), Ca2+ -promoted Ras inactivator (CAPRI, or RASAL4), and Ras GTPase activating-like proteins (RASAL) or RASAL1. The members are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin homology domain that is associated with a Bruton's tyrosine kinase motif. While this domain structure is conserved, a small change in the function of each individual domain and the interaction between domains has a marked effect on the regulation of each protein.
Pssm-ID: 213330 Cd Length: 269 Bit Score: 58.03 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 934 LLLKLFKTALEEEIkSKVDQVQDIVTGNPTVIKMVVSFNRGArGQNTLRQLLAPVVKEIIEDKAlvintnPVEVykawvn 1013
Cdd:cd05128 51 QIVPLLRALASREI-SKTQDPNTLFRGNSLASKCMDEFMKLV-GMQYLHETLKPVIDEIFSEKK------SCEI------ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1014 qletqtgEASKLPYdvtteqaltypevKNKLEASIENLRKVTDKVLGSIISSLDLLPYGLRYIAKVLKNSIREKFPDATE 1093
Cdd:cd05128 117 -------DPSKLKD-------------GEVLETNLANLRGYVERVFKAITSSARRCPTLMCEIFSDLRESAAQRFPDNED 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1094 EELLKIVGnLLYYRYMNPAIVAPDGFDIIDMtaggQINSNQRRNLGSVAKVLQH-----AASNKLFEGEnEHLSSMNNY- 1167
Cdd:cd05128 177 VPYTAVSG-FIFLRFFAPAILNPKLFGLREE----HPDPQTARTLTLISKTIQTlgnlgSSSSGLGVKE-AYMSPLYERf 250
|
250
....*....|....*....
gi 118344444 1168 LSETYQE-FRKYFQEACDV 1185
Cdd:cd05128 251 TDEQHVDaVKKFLDRISSV 269
|
|
| SCP1 |
COG5199 |
Calponin [Cytoskeleton]; |
45-165 |
2.63e-08 |
|
Calponin [Cytoskeleton];
Pssm-ID: 227526 [Multi-domain] Cd Length: 178 Bit Score: 55.31 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 45 EEAKRWMEVCLVEELPPTTELEEGLRNGVYLAKLAKFFAPKMVsekkiydveqtRYKKSGLHFRHTDNTVQWLRAMEAIG 124
Cdd:COG5199 16 KEVTLWIETVLGEKFEPPGDLLSLLKDGVRLCRILNEASPLDI-----------KYKESKMPFVQMENISSFINGLKKLR 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 118344444 125 LPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKL------GIAPQI 165
Cdd:COG5199 85 VPEYELFQTNDLFEAKDLRQVVICLYSLSRYAQKErmfsgpFLGPHL 131
|
|
| RasGAP_CLA2_BUD2 |
cd05137 |
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ... |
1038-1186 |
3.40e-08 |
|
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein (GAP) for BUD1/RSR1 and is necessary for proper bud-site selection in yeast. BUD2 has sequence similarity to the catalytic domain of RasGAPs, and stimulates the hydrolysis of BUD1-GTP to BUD1-GDP. Elimination of Bud2p activity by mutation causes a random budding pattern with no growth defect. Overproduction of Bud2p also alters the budding pattern.
Pssm-ID: 213339 [Multi-domain] Cd Length: 356 Bit Score: 57.57 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1038 PEVKNKLEASIENLRKVTDKVLGSIISSLDLLPYGLRyiaKVLKNsIREKFPDATEEELLKI----VGNLLYYRYMNPAI 1113
Cdd:cd05137 149 IEKEEDLEENWENLISLTEEIWNSIYITSNDCPPELR---KILKH-IRAKVEDRYGDFLRTVtlnsVSGFLFLRFFCPAI 224
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118344444 1114 VAPDGFDIIDmtagGQINSNQRRNLGSVAKVLQHAASNKLFEGENEHLSSMNNYLSETYQEFRKYFQEACDVP 1186
Cdd:cd05137 225 LNPKLFGLLK----DHPRPRAQRTLTLIAKVLQNLANLTTFGQKEPWMEPMNEFLTTHREELKDYIDKITGIK 293
|
|
| RasGAP_p120GAP |
cd05391 |
Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ... |
1046-1200 |
1.26e-07 |
|
Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates hydrolysis of bound GTP to GDP. Once the Ras regulator p120GAP, a member of the GAP protein family, is recruited to the membrane, it is transiently immobilized to interact with Ras-GTP. The down-regulation of Ras by p120GAP is a critical step in the regulation of many cellular processes, which is disrupted in approximately 30% of human cancers. p120GAP contains SH2, SH3, PH, calcium- and lipid-binding domains, suggesting its involvement in a complex network of cellular interactions in vivo.
Pssm-ID: 213340 Cd Length: 328 Bit Score: 55.57 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1046 ASIENLRKVTDKVLGSIISSLDLLPYGLRYIAKVLKNSIREKFPDATEEElLKIVGNLLYYRYMNPAIVAPDGFDIID-- 1123
Cdd:cd05391 130 TNLEHLLNILSELVEKIFMAAEILPPTLRYIYGCLQKSVQQKWPTNTTVR-TRVVSGFVFLRLICPAILNPRMFNIISet 208
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118344444 1124 --MTAGgqinsnqrRNLGSVAKVLQHAASNKLFEGENEHLSSMNNYLSETYQEFRKYFQEACDVPEPEEKFNMDKyTDL 1200
Cdd:cd05391 209 psPTAA--------RTLTLVAKSLQNLANLVEFGAKEPYMEGVNPFIKKNKERMIMFLDELGNVPELPDTTEHSR-TDL 278
|
|
| RasGAP_RASAL |
cd05135 |
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ... |
1044-1146 |
5.82e-06 |
|
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like protein (RASAL) or RASAL1 is a member of the GAP1 family, and a Ca2+ sensor responding in-phase to repetitive Ca2+ signals by associating with the plasma membrane and deactivating Ras. It contains a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. RASAL, like Ca2+ -promoted Ras inactivator (CAPRI, or RASAL4), is a cytosolic protein that undergoes a rapid translocation to the plasma membrane in response to receptor-mediated elevation in the concentration of intracellular free Ca2+, a translocation that activates its ability to function as a RasGAP. However, unlike RASAL4, RASAL undergoes an oscillatory translocation to the plasma membrane that occurs in synchrony with repetitive Ca2+ spikes.
Pssm-ID: 213337 Cd Length: 287 Bit Score: 49.81 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1044 LEASIENLRKVTDKVLGSIISSLDLLPYGLRYIAKVLKNSIREKFPDATEEEL--LKIVGnLLYYRYMNPAIVAPDGFDI 1121
Cdd:cd05135 146 RESSLELLQGYLGSIIDAIVGSVDQCPPVMRVAFKQLHKRVEERFPEAEHQDVkyLAISG-FLFLRFFAPAILTPKLFQL 224
|
90 100
....*....|....*....|....*
gi 118344444 1122 IDMTAGGQINsnqrRNLGSVAKVLQ 1146
Cdd:cd05135 225 REQHADPRTS----RTLLLLAKAVQ 245
|
|
| CH_AtKIN14-like |
cd21203 |
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ... |
45-152 |
6.45e-06 |
|
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: 46.64 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 45 EEAKRWMEVCLVEELPPTT---ELEEGLRNGVYLAKLAKFFAPKMVSekKIYDVEQTRYKKSGLHFRHTDNTVQWLRAME 121
Cdd:cd21203 3 YEAAEWIQNVLGVLVLPDPseeEFRLCLRDGVVLCKLLNKLQPGAVP--KVVESPDDPDGAAGSAFQYFENVRNFLVAIE 80
|
90 100 110
....*....|....*....|....*....|.
gi 118344444 122 AIGLPkIFYPETTDVYDRKNIPRMIYCIHAL 152
Cdd:cd21203 81 EMGLP-TFEASDLEQGGGGSRPRVVDCILAL 110
|
|
| RasGAP_DAB2IP |
cd05136 |
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ... |
1050-1200 |
2.89e-05 |
|
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras GTPase-activating proteins includes DAB2IP, nGAP, and Syn GAP. Disabled 2 interactive protein, (DAB2IP; also known as ASK-interacting protein 1 (AIP1)), is a member of the GTPase-activating proteins, down-regulates Ras-mediated signal pathways, and mediates TNF-induced activation of ASK1-JNK signaling pathways. The mechanism by which TNF signaling is coupled to DAB2IP is not known.
Pssm-ID: 213338 Cd Length: 324 Bit Score: 47.96 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1050 NLRKVTDKVLGSIISSLDLLPYGLRyiaKVLkNSIREKFPDATEEELL-KIVGNLLYYRYMNPAIVAPDGFDII-----D 1123
Cdd:cd05136 138 NLRRSVELAWCKILSSHCVFPRELR---EVF-SSWRERLEERGREDIAdRLISASLFLRFLCPAILSPSLFNLTqeypsE 213
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118344444 1124 MTAggqinsnqrRNLGSVAKVLQHAASNKLFEGENEHLSSMNNYLSETYQEFRKYFQEACDVPEPEEKFNMDKYTDL 1200
Cdd:cd05136 214 RAA---------RNLTLIAKVIQNLANFTRFGGKEEYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDL 281
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
689-710 |
1.23e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 37.69 E-value: 1.23e-03
|
| RasGAP_RASA4 |
cd05395 |
Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also ... |
977-1146 |
1.31e-03 |
|
Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also known as Ca2+ -promoted Ras inactivator (CAPRI), is a member of the GAP1 family. Members of the GAP1 family are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. RASAL4, like RASAL, is a cytosolic protein that undergoes a rapid translocation to the plasma membrane in response to a receptor-mediated elevation in the concentration of intracellular free Ca2+ ([Ca2+]i). However, unlike RASAL, RASAL4 does not sense oscillations in [Ca2+]i.
Pssm-ID: 213343 [Multi-domain] Cd Length: 287 Bit Score: 42.55 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 977 GQNTLRQLLAPVVKEIIEDKALV-INTNPVEVYKAWVNQLETQTGEAsklpydvtteqaltypEVknkLEASIENLRKVT 1055
Cdd:cd05395 97 GMQYLHSVLGPTINRVFEEKKYVeLDPSKVEIKDVGCSGLHRIQTES----------------EV---IEQSAQLLQSYL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344444 1056 DKVLGSIISSLDLLPYGLRYIAKVLKNSIREKFPDATEEELLKI-VGNLLYYRYMNPAIVAPDGFDIIDMTAggqiNSNQ 1134
Cdd:cd05395 158 GELLSAISKSVKYCPAVIRATFRQLFKRVQERFPENQHQNVKFIaVTSFLCLRFFSPAIMSPKLFHLREKHA----DART 233
|
170
....*....|..
gi 118344444 1135 RRNLGSVAKVLQ 1146
Cdd:cd05395 234 SRTLLLLAKAVQ 245
|
|
| |
