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Conserved domains on  [gi|530379106|ref|XP_005248467|]
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ras GTPase-activating-like protein IQGAP2 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RasGAP_IQGAP2 cd05131
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...
 889-1247 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: 711.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  889 DTVIFTLYNYASNQREEYLLLKLFKTALEEEIKSKVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIDD 968
Cdd:cd05131     1 DTVIFTLYNYASNQREEYLLLKLFETALEEEIKSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  969 KSLIINTNPVEVYKAWVNQLETQTGEASKLPYDVTTEQALTYPEVKNKLEASIENLRRVTDKVLNSIISSLDLLPYGLRY 1048
Cdd:cd05131    81 KSLIINTNPVEVYKAWVNQLETATGEASKLPYDVTTEQALTHPEVVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1049 IAKVLKNSIHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQINSDQRRNLGSVAKVLQHAASNKLFE 1128
Cdd:cd05131   161 IAKVLKNSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHSEQRRNLGSVAKVLQHAASNKLFE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1129 GENEHLSSMNNYLSETYQEFRKYFKEACNVPEPEEKFNMDKYTDLVTVSKPVIYISIEEIISTHSLLLEHQDAIAPEKND 1208
Cdd:cd05131   241 GENAHLSSMNSYLSQTYQKFRKFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIAPDQND 320

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 530379106 1209 LLSELLGSLGEVPTVESFLGEGAVDPNDPNKANTLSQLS 1247
Cdd:cd05131   321 LLHELLKDLGEVPDVESFLGEGTVDPNDPNKENTLSQLG 359
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 1-139 5.63e-103

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).


The actual alignment was detected with superfamily member cd21275:

Pssm-ID: 469584 [Multi-domain]  Cd Length: 156  Bit Score: 325.05  E-value: 5.63e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106    1 MDERRRQNIAYEYLCHLEEAKRWMEVCLVEELPPTTELEEGLRNGVYLAKLAKFFAPKMVSEKKIYDVEQTRYKKSGLHF 80
Cdd:cd21275    18 MDERRRQNIAYEYLCHLEEAKQWIEACLNEELPPTTELEEGLRNGVYLVKLAKFFAPKLVSEKKIYDVDQVRYKRSGLHF 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530379106   81 RHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGIAPQIQ 139
Cdd:cd21275    98 RHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNMPRVIYCIHALSLYLFKLGIAPQIQ 156
IQG1 super family cl34962
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
 757-1548 1.64e-58

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


The actual alignment was detected with superfamily member COG5261:

Pssm-ID: 227586 [Multi-domain]  Cd Length: 1054  Bit Score: 221.30  E-value: 1.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  757 IRKFVYLLDQSDLD---------FQEELEVARLREEVVTKIRANQQLEKDLNLMDIK----IGLLVKNRITLEDVISHSK 823
Cdd:COG5261   274 TRRSTSVFYTISLEmisnveqafFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFAE 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  824 KLNkkkggemEILNNTDnqgiKSLSKERRktLETYQQLFYLLQTN-PLYL--------------AKLIFQMPQNKSTKFM 888
Cdd:COG5261   354 RLQ-------SNINGRK----KYFPLDRR--LSLFGPLFFLLQSSiPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE 420

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  889 dtvIFTLYNYASNQREEYLLLKLFKTALEEEIKSKVDqVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIDD 968
Cdd:COG5261   421 ---IRKLYSLGKSNCEEHLSVSLFQMLLRTEVEATSL-VQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIH 496

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  969 KSLIINTNPVEVYKAWVNQLETQTGEASKLpyDVTTEQALTYPEVKNKL-EASIENLRRVTDKVLNSIISSLDLLPYGLR 1047
Cdd:COG5261   497 EDLEVDINPLLVYRALLNKGQLSPDKDLEL--LTSNEEVSEFLAVMNAVqESSAKLLELSTERILDAVYNSLDEIGYGIR 574

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1048 YIAKVLK-------NSIHEKFPDA--------TEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQINSDQRRnLG 1112
Cdd:COG5261   575 FVCELIRvvfeltpNRLFPSISDSrclrticfAEIDSLGLIGGFFFLRFVNEALVSPQTSMLKD----SCPSDNVRK-LA 649

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1113 SVAKVLQhaasnKLFEGEN--EHLSSMNNYLSETYQEFRKYFKEACNVPEPEEKFNMDKYTDLVTVSKPVIYISIEEIIS 1190
Cdd:COG5261   650 TLSKILQ-----SVFEITSsdKFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYLVNEIYLT 724

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1191 THSLLLEHQDAIAPEkndllsellgslGEVPTVESFLGEGAVDPNDPNKantlsqlskTEISLVLTSKYDIEDGEAidsR 1270
Cdd:COG5261   725 HEIIIEYLDNLYDPD------------SLVDLLLQELGELCSFPQDQRD---------TLNCLVTLPLFNRSDDPI---R 780

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1271 SLMIKTKKLIIDVIRNQPGNTLTEIL--ETP---ATAQQEVDHATDMVSRAMIDSRTPEEMKHsqsmiedaqlpleqKKR 1345
Cdd:COG5261   781 DLKQQLKRTRVYIIYVDAGTNLFEQLlrLLPsdePATRNPLDLNPNIRDDPSVSSLKSMSLMK--------------LKI 846

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1346 KIQRNLRTLEQTGHVSSENKYQDILNEIAKDIRNQRIYRKLRKAELAKLQQTLNALNKKAAFYEEQINYYDTYIKTCLDN 1425
Cdd:COG5261   847 RAIELLDELETLGFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQ 926

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1426 LKRKNTRR---SIKLDGKGEPKGAKRAKPVKYTAAKLHEKGVLLDIDDLQTNqFKNVTFdIIATEDVGIF--DVRSKFLG 1500
Cdd:COG5261   927 LQPKKSKLkgfSRGVGVVRDKPKSISSGTFKYSAQQLYKRGVLVNITIPEPN-VSNIYF-TFSSDSTDNFviEVYQPGHS 1004

                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....*...
gi 530379106 1501 VEMEKVQLNIQDLLQMQYEGVAVMKMFDKVKVNVNLLIYLLNKKFYGK 1548
Cdd:COG5261  1005 VSLPEVSFCFDDLLKRQYNKNPVVDLGGFLTFNANKLLHLIESKFYRK 1052
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 662-683 1.84e-04

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 40.00  E-value: 1.84e-04
                            10        20
                    ....*....|....*....|..
gi 530379106    662 EQEENVVKIQAFWKGYKQRKEY 683
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
 
Name Accession Description Interval E-value
RasGAP_IQGAP2 cd05131
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...
 889-1247 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: 711.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  889 DTVIFTLYNYASNQREEYLLLKLFKTALEEEIKSKVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIDD 968
Cdd:cd05131     1 DTVIFTLYNYASNQREEYLLLKLFETALEEEIKSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  969 KSLIINTNPVEVYKAWVNQLETQTGEASKLPYDVTTEQALTYPEVKNKLEASIENLRRVTDKVLNSIISSLDLLPYGLRY 1048
Cdd:cd05131    81 KSLIINTNPVEVYKAWVNQLETATGEASKLPYDVTTEQALTHPEVVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1049 IAKVLKNSIHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQINSDQRRNLGSVAKVLQHAASNKLFE 1128
Cdd:cd05131   161 IAKVLKNSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHSEQRRNLGSVAKVLQHAASNKLFE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1129 GENEHLSSMNNYLSETYQEFRKYFKEACNVPEPEEKFNMDKYTDLVTVSKPVIYISIEEIISTHSLLLEHQDAIAPEKND 1208
Cdd:cd05131   241 GENAHLSSMNSYLSQTYQKFRKFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIAPDQND 320

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 530379106 1209 LLSELLGSLGEVPTVESFLGEGAVDPNDPNKANTLSQLS 1247
Cdd:cd05131   321 LLHELLKDLGEVPDVESFLGEGTVDPNDPNKENTLSQLG 359
CH_IQGAP2 cd21275
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP2; IQ motif ...
 1-139 5.63e-103

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: 325.05  E-value: 5.63e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106    1 MDERRRQNIAYEYLCHLEEAKRWMEVCLVEELPPTTELEEGLRNGVYLAKLAKFFAPKMVSEKKIYDVEQTRYKKSGLHF 80
Cdd:cd21275    18 MDERRRQNIAYEYLCHLEEAKQWIEACLNEELPPTTELEEGLRNGVYLVKLAKFFAPKLVSEKKIYDVDQVRYKRSGLHF 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530379106   81 RHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGIAPQIQ 139
Cdd:cd21275    98 RHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNMPRVIYCIHALSLYLFKLGIAPQIQ 156
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
 878-1207 8.95e-91

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: 298.45  E-value: 8.95e-91
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106    878 QMPQNKSTKFMDTVIFTLYNYASNQREEYLLLKLFKTALEeeIKSKVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQL 957
Cdd:smart00323    1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLS--LASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRAL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106    958 LAPVVKEIIDD----KSLIINTNPVEVYKAWVNQLETQTGEASKLPYDVTTEQALTYPEVKNK---LEASIENLRRVTDK 1030
Cdd:smart00323   79 IDPEVERTDDPntifRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEgedLETNLENLLQYVER 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106   1031 VLNSIISSLDLLPYGLRYIAKVLKNSIHEKFPDAteDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMtaggQINSDQRRN 1110
Cdd:smart00323  159 LFDAIINSSDRLPYGLRDICKQLRQAAEKRFPDA--DVIYKAVSSFVFLRFFCPAIVSPKLFNLVDE----HPDPTTRRT 232

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106   1111 LGSVAKVLQHAASNKLFEGENEHLSSMNNYLSETYQEFRKYFKEACNVPEPeekfNMDKYTDLVTVSKPviyisieEIIS 1190
Cdd:smart00323  233 LTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEI----LVDKVSDSTTISGR-------ELSL 301

                           330
                    ....*....|....*..
gi 530379106   1191 THSLLLEHQDAIAPEKN 1207
Cdd:smart00323  302 LHSLLLENGDALKRELN 318
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
 911-1123 2.18e-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: 2.18e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106   911 LFKTALEEEIKSkVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIDDKSLIINTNPVEVYKAWVNQLET 990
Cdd:pfam00616    1 LISELIEEEIES-SDNPNDLLRGNSLVSKLLETYNRRPRGQEYLKKVLGPLVRKIIEDEDLDLESDPRKIYESLINQEEL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106   991 QTGEaSKLPYDVTTEQALTYPEVKNKLEASIENLRRVTDKVLNSIISSLDLLPYGLRYIAKVLKNSIHEKFPDATEDELL 1070
Cdd:pfam00616   80 KTGR-SDLPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEIL 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 530379106  1071 KIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQINSDQRRNLGSVAKVLQHAAS 1123
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVD----HQISPKQRRNLTLIAKVLQNLAN 207
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
 757-1548 1.64e-58

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: 221.30  E-value: 1.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  757 IRKFVYLLDQSDLD---------FQEELEVARLREEVVTKIRANQQLEKDLNLMDIK----IGLLVKNRITLEDVISHSK 823
Cdd:COG5261   274 TRRSTSVFYTISLEmisnveqafFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFAE 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  824 KLNkkkggemEILNNTDnqgiKSLSKERRktLETYQQLFYLLQTN-PLYL--------------AKLIFQMPQNKSTKFM 888
Cdd:COG5261   354 RLQ-------SNINGRK----KYFPLDRR--LSLFGPLFFLLQSSiPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE 420

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  889 dtvIFTLYNYASNQREEYLLLKLFKTALEEEIKSKVDqVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIDD 968
Cdd:COG5261   421 ---IRKLYSLGKSNCEEHLSVSLFQMLLRTEVEATSL-VQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIH 496

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  969 KSLIINTNPVEVYKAWVNQLETQTGEASKLpyDVTTEQALTYPEVKNKL-EASIENLRRVTDKVLNSIISSLDLLPYGLR 1047
Cdd:COG5261   497 EDLEVDINPLLVYRALLNKGQLSPDKDLEL--LTSNEEVSEFLAVMNAVqESSAKLLELSTERILDAVYNSLDEIGYGIR 574

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1048 YIAKVLK-------NSIHEKFPDA--------TEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQINSDQRRnLG 1112
Cdd:COG5261   575 FVCELIRvvfeltpNRLFPSISDSrclrticfAEIDSLGLIGGFFFLRFVNEALVSPQTSMLKD----SCPSDNVRK-LA 649

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1113 SVAKVLQhaasnKLFEGEN--EHLSSMNNYLSETYQEFRKYFKEACNVPEPEEKFNMDKYTDLVTVSKPVIYISIEEIIS 1190
Cdd:COG5261   650 TLSKILQ-----SVFEITSsdKFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYLVNEIYLT 724

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1191 THSLLLEHQDAIAPEkndllsellgslGEVPTVESFLGEGAVDPNDPNKantlsqlskTEISLVLTSKYDIEDGEAidsR 1270
Cdd:COG5261   725 HEIIIEYLDNLYDPD------------SLVDLLLQELGELCSFPQDQRD---------TLNCLVTLPLFNRSDDPI---R 780

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1271 SLMIKTKKLIIDVIRNQPGNTLTEIL--ETP---ATAQQEVDHATDMVSRAMIDSRTPEEMKHsqsmiedaqlpleqKKR 1345
Cdd:COG5261   781 DLKQQLKRTRVYIIYVDAGTNLFEQLlrLLPsdePATRNPLDLNPNIRDDPSVSSLKSMSLMK--------------LKI 846

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1346 KIQRNLRTLEQTGHVSSENKYQDILNEIAKDIRNQRIYRKLRKAELAKLQQTLNALNKKAAFYEEQINYYDTYIKTCLDN 1425
Cdd:COG5261   847 RAIELLDELETLGFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQ 926

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1426 LKRKNTRR---SIKLDGKGEPKGAKRAKPVKYTAAKLHEKGVLLDIDDLQTNqFKNVTFdIIATEDVGIF--DVRSKFLG 1500
Cdd:COG5261   927 LQPKKSKLkgfSRGVGVVRDKPKSISSGTFKYSAQQLYKRGVLVNITIPEPN-VSNIYF-TFSSDSTDNFviEVYQPGHS 1004

                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....*...
gi 530379106 1501 VEMEKVQLNIQDLLQMQYEGVAVMKMFDKVKVNVNLLIYLLNKKFYGK 1548
Cdd:COG5261  1005 VSLPEVSFCFDDLLKRQYNKNPVVDLGGFLTFNANKLLHLIESKFYRK 1052
RasGAP_C pfam03836
RasGAP C-terminus; This domain can be found in the C terminus of the IQGAP family members, ...
 1340-1472 9.97e-47

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: 164.26  E-value: 9.97e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  1340 LEQKKRKIQRNLRTLEQTGHVSSENKYQDILNEIAKDIRNQRIYRKLRKAELAKLQQTLNALNKKAAFYEEQINYYDTYI 1419
Cdd:pfam03836    1 YVELKKKALENLLELESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYI 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 530379106  1420 KTCLDNLKRKNTRR--SIKLDGKGEPKGAKRAK--PVKYTAAKLHEKGVLLDIDDLQ 1472
Cdd:pfam03836   81 ENCLDNLQKKKKKLfsKQYFHYRKLQKRGKLPKfgSYKYSARQLYEKGVLLEIEGVP 137
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
 1-184 6.03e-33

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: 139.25  E-value: 6.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106    1 MDERRRQNIAYEYLCHLEEAKRWMEVCLVEELPpTTELEEGLRNGVYLAKLAKFFAPKMVseKKIYdveqtryKKSGLHF 80
Cdd:COG5261    30 SAKNRSALRAYEYLCRVSEAKIWIEEVIEEALP-ELCFEDSLRNGVFLAKLTQRFNPDLT--TVIF-------PADKLQF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106   81 RHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGIAPQIQDLLGKVdFTEEEISNMRKELE 160
Cdd:COG5261   100 RHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTPLINSSGQIS-FTKEDIAACKKAWP 178

                         170       180
                  ....*....|....*....|....
gi 530379106  161 kygiQMPSFSKIGGILANELSVDE 184
Cdd:COG5261   179 ----RIPDFKSLGTNINTAASPEE 198
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 18-125 3.31e-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: 61.18  E-value: 3.31e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106     18 EEAKRWMEVCLVEELPPT-TELEEGLRNGVYLAKLAKFFAPKMVSEKKIydveqtryKKSGLHFRHTDNTVQWLRAMESI 96
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPvTNFSSDLKDGVALCALLNSLSPGLVDKKKV--------AASLSRFKKIENINLALSFAEKL 72

                            90       100       110
                    ....*....|....*....|....*....|
gi 530379106     97 GlPKIFYPETTDVYD-RKNIPRMIYCIHAL 125
Cdd:smart00033   73 G-GKVVLFEPEDLVEgPKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 18-128 4.23e-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: 61.15  E-value: 4.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106    18 EEAKRWMEVCLVEELPPT--TELEEGLRNGVYLAKLAKFFAPKMVSEKKIYDVEqtrykksglhFRHTDNTVQWLR-AME 94
Cdd:pfam00307    5 KELLRWINSHLAEYGPGVrvTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSE----------FDKLENINLALDvAEK 74

                           90       100       110
                   ....*....|....*....|....*....|....
gi 530379106    95 SIGLPKIFyPETTDVYDRKNIpRMIYCIHALSLY 128
Cdd:pfam00307   75 KLGVPKVL-IEPEDLVEGDNK-SVLTYLASLFRR 106
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 662-683 1.84e-04

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 40.00  E-value: 1.84e-04
                            10        20
                    ....*....|....*....|..
gi 530379106    662 EQEENVVKIQAFWKGYKQRKEY 683
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
 
Name Accession Description Interval E-value
RasGAP_IQGAP2 cd05131
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...
 889-1247 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: 711.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  889 DTVIFTLYNYASNQREEYLLLKLFKTALEEEIKSKVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIDD 968
Cdd:cd05131     1 DTVIFTLYNYASNQREEYLLLKLFETALEEEIKSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  969 KSLIINTNPVEVYKAWVNQLETQTGEASKLPYDVTTEQALTYPEVKNKLEASIENLRRVTDKVLNSIISSLDLLPYGLRY 1048
Cdd:cd05131    81 KSLIINTNPVEVYKAWVNQLETATGEASKLPYDVTTEQALTHPEVVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1049 IAKVLKNSIHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQINSDQRRNLGSVAKVLQHAASNKLFE 1128
Cdd:cd05131   161 IAKVLKNSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHSEQRRNLGSVAKVLQHAASNKLFE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1129 GENEHLSSMNNYLSETYQEFRKYFKEACNVPEPEEKFNMDKYTDLVTVSKPVIYISIEEIISTHSLLLEHQDAIAPEKND 1208
Cdd:cd05131   241 GENAHLSSMNSYLSQTYQKFRKFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIAPDQND 320

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 530379106 1209 LLSELLGSLGEVPTVESFLGEGAVDPNDPNKANTLSQLS 1247
Cdd:cd05131   321 LLHELLKDLGEVPDVESFLGEGTVDPNDPNKENTLSQLG 359
RasGAP_IQGAP1 cd05133
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...
 889-1270 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: 571.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  889 DTVIFTLYNYASNQREEYLLLKLFKTALEEEIKSKVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIDD 968
Cdd:cd05133     1 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  969 KSLIINTNPVEVYKAWVNQLETQTGEASKLPYDVTTEQALTYPEVKNKLEASIENLRRVTDKVLNSIISSLDLLPYGLRY 1048
Cdd:cd05133    81 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQAMSHEEVRTRLDASIKNMRMVTDKFLSAIISSVDKIPYGMRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1049 IAKVLKNSIHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQINSDQRRNLGSVAKVLQHAASNKLFE 1128
Cdd:cd05133   161 IAKVLKDTLHEKFPDAGEDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1129 GENEHLSSMNNYLSETYQEFRKYFKEACNVPEPEEKFNMDKYTDLVTVSKPVIYISIEEIISTHSLLLEHQDAIAPEKND 1208
Cdd:cd05133   241 GDNAHLSPINEYLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530379106 1209 LLSELLGSLGEVPTVESFLGEGAVDPNDPNKantlSQLSKTEISLVLTSKYDI--EDGEAIDSR 1270
Cdd:cd05133   321 PIHELLDDLGEVPTIESLIGENPGPPGDPNR----ETLAKTEVSLTLTNKFDVpgDENAEMDAR 380
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
 899-1229 1.02e-177

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: 534.09  E-value: 1.02e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  899 ASNQREEYLLLKLFKTALEEEIKSKVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIDDKSLIINTNPV 978
Cdd:cd05127     1 ASNRREEYLLLKLFKTALREEIESKVSLPEDIVTGNPTVIKLVVNYNRGPRGQKYLRELLGPVVKEILDDDDLDLETDPV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  979 EVYKAWVNQLETQTGEASKLPYDVTTEQALTYPEVKNKLEASIENLRRVTDKVLNSIISSLDLLPYGLRYIAKVLKNSIH 1058
Cdd:cd05127    81 DIYKAWINQEESRTGEPSKLPYDVTREQALKDPEVRKRLIEHLEKLRAITDKFLTAITESLDKMPYGMRYIAKVLKEALR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1059 EKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQINSDQRRNLGSVAKVLQHAASNKLFEGENEHLSSMN 1138
Cdd:cd05127   161 EKFPDAPEEEILKIVGNLLYYRYMNPAIVAPEAFDIIDLSVGGQLSPLQRRNLGSIAKVLQQAASGKLFGGENPYLSPLN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1139 NYLSETYQEFRKYFKEACNVPEPEEKFNMDKYTDLVTVSKPVIYISIEEIISTHSLLLEHQDAIAPEKNDLLSELLGSLG 1218
Cdd:cd05127   241 PYISESHEKFKKFFLEACTVPEAEEHFNIDEYSDLTMLTKPTIYISLQEIFATHKLLLEHQDEIAPDPDDPLRELLDDLG 320

                         330
                  ....*....|.
gi 530379106 1219 EVPTVESFLGE 1229
Cdd:cd05127   321 PAPTIESLLGS 331
RasGAP_IQGAP3 cd12207
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ...
 889-1236 3.49e-167

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: 507.06  E-value: 3.49e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  889 DTVIFTLYNYASNQREEYLLLKLFKTALEEEIKSKVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIDD 968
Cdd:cd12207     1 ESVIFSLYNYASNRREAYLLLQLFKTALQEEISSKVEKPQDVITGNPTVIRLLVSFYRSARGQNALRHILGPVVQDVLQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  969 KSLIINTNPVEVYKAWVNQLETQTGEASKLPYDVTTEQALTYPEVKNKLEASIENLRRVTDKVLNSIISSLDLLPYGLRY 1048
Cdd:cd12207    81 KGLSIRTDPVQIYKAWINQTETQSGCRSSLPYEVSPEQALSHPEVQRRLDIAIRNLLAVTDKFLSAITSSVDKIPYGMRY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1049 IAKVLKNSIHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQINSDQRRNLGSVAKVLQHAASNKLFE 1128
Cdd:cd12207   161 VAKVLRDSLQEKFPGASEDEVYKVVGNLLYYRFMNPAVVAPDGFDIVDCSAGGALQPEQRRMLGSVAKVLQHAAANKHFQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1129 GENEHLSSMNNYLSETYQEFRKYFKEACNVPEPEEKFNMDKYTDLVTVSKPVIYISIEEIISTHSLLLEHQDAIAPEKND 1208
Cdd:cd12207   241 GDSEHLQALNQYLEETHVKFRKFILQACCVPEPEERFNVDEYSEMVAVAKPVIYITVGELINTHKLLLEHQDSIAPDHSD 320

                         330       340
                  ....*....|....*....|....*...
gi 530379106 1209 LLSELLGSLGEVPTVESFLGEGAVDPND 1236
Cdd:cd12207   321 PLHELLEDLGEVPTVQSLIGESWADLGD 348
CH_IQGAP2 cd21275
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP2; IQ motif ...
 1-139 5.63e-103

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: 325.05  E-value: 5.63e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106    1 MDERRRQNIAYEYLCHLEEAKRWMEVCLVEELPPTTELEEGLRNGVYLAKLAKFFAPKMVSEKKIYDVEQTRYKKSGLHF 80
Cdd:cd21275    18 MDERRRQNIAYEYLCHLEEAKQWIEACLNEELPPTTELEEGLRNGVYLVKLAKFFAPKLVSEKKIYDVDQVRYKRSGLHF 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530379106   81 RHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGIAPQIQ 139
Cdd:cd21275    98 RHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNMPRVIYCIHALSLYLFKLGIAPQIQ 156
CH_IQGAP1 cd21274
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif ...
 7-160 3.12e-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: 291.90  E-value: 3.12e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106    7 QNIAYEYLCHLEEAKRWMEVCLVEELPPTTELEEGLRNGVYLAKLAKFFAPKMVSEKKIYDVEQTRYKKSGLHFRHTDNT 86
Cdd:cd21274     1 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530379106   87 VQWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGIAPQIQDLLGKVDFTEEEISNMRKELE 160
Cdd:cd21274    81 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTELE 154
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
 878-1207 8.95e-91

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: 298.45  E-value: 8.95e-91
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106    878 QMPQNKSTKFMDTVIFTLYNYASNQREEYLLLKLFKTALEeeIKSKVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQL 957
Cdd:smart00323    1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLS--LASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRAL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106    958 LAPVVKEIIDD----KSLIINTNPVEVYKAWVNQLETQTGEASKLPYDVTTEQALTYPEVKNK---LEASIENLRRVTDK 1030
Cdd:smart00323   79 IDPEVERTDDPntifRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEgedLETNLENLLQYVER 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106   1031 VLNSIISSLDLLPYGLRYIAKVLKNSIHEKFPDAteDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMtaggQINSDQRRN 1110
Cdd:smart00323  159 LFDAIINSSDRLPYGLRDICKQLRQAAEKRFPDA--DVIYKAVSSFVFLRFFCPAIVSPKLFNLVDE----HPDPTTRRT 232

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106   1111 LGSVAKVLQHAASNKLFEGENEHLSSMNNYLSETYQEFRKYFKEACNVPEPeekfNMDKYTDLVTVSKPviyisieEIIS 1190
Cdd:smart00323  233 LTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEI----LVDKVSDSTTISGR-------ELSL 301

                           330
                    ....*....|....*..
gi 530379106   1191 THSLLLEHQDAIAPEKN 1207
Cdd:smart00323  302 LHSLLLENGDALKRELN 318
CH_IQGAP3 cd21276
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP3; IQ motif ...
 8-159 9.93e-90

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: 9.93e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106    8 NIAYEYLCHLEEAKRWMEVCLVEELPPTTELEEGLRNGVYLAKLAKFFAPKMVSEKKIYDVEQTRYKKSGLHFRHTDNTV 87
Cdd:cd21276     1 NVAYQYLCRLEEAKRWMEACLKEELPPPTELEESLRNGVYLAKLGHCFAPRVVPLKKIYDLEQMRYQATGLHFRHTDNIN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530379106   88 QWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGIAPQIQDLLGKVDFTEEEISNMRKEL 159
Cdd:cd21276    81 HWRNAMMHIGLPSIFHPETTDIYDKKNMPRVVYCIHALSLYLFRLGLAPQIHDLYGKVKFTEEEINNMKLEL 152
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
 911-1123 2.18e-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: 2.18e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106   911 LFKTALEEEIKSkVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIDDKSLIINTNPVEVYKAWVNQLET 990
Cdd:pfam00616    1 LISELIEEEIES-SDNPNDLLRGNSLVSKLLETYNRRPRGQEYLKKVLGPLVRKIIEDEDLDLESDPRKIYESLINQEEL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106   991 QTGEaSKLPYDVTTEQALTYPEVKNKLEASIENLRRVTDKVLNSIISSLDLLPYGLRYIAKVLKNSIHEKFPDATEDELL 1070
Cdd:pfam00616   80 KTGR-SDLPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEIL 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 530379106  1071 KIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQINSDQRRNLGSVAKVLQHAAS 1123
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVD----HQISPKQRRNLTLIAKVLQNLAN 207
CH_IQGAP cd21206
calponin homology (CH) domain found in the IQ motif containing GTPase activating protein ...
 8-133 3.79e-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: 224.41  E-value: 3.79e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106    8 NIAYEYLCHLEEAKRWMEVCLVEELPPTTELEEGLRNGVYLAKLAKFFAPKMVSEKKIYDVeqtrykksGLHFRHTDNTV 87
Cdd:cd21206     1 TIAYEYLCRLEEAKQWIEACLNEELPPTTEFEEELRNGVVLAKLANKFAPKLVPLKKIYDV--------GLQFRHTDNIN 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 530379106   88 QWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLG 133
Cdd:cd21206    73 HFLRALKKIGLPKIFHFETTDLYEKKNIPKVIYCLHALSLLLFKLG 118
RasGAP_GAPA cd05132
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...
 887-1208 1.45e-58

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: 206.43  E-value: 1.45e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  887 FMDTVIFTLYNYASNQREEYLLLKLFKTALEEEIKSKVDqVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEII 966
Cdd:cd05132     5 LLQTVMFTLYGNQYESREEHLLLSMFQSVLTYEFDETTE-FGSLLRANTAVSRMMTTYTRRGPGQSYLKTVLADRINDLI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  967 DDKSLIINTNPVEVYKAWVNQLETQTGEASKLPYDVTTEQALTYPEVKNKLEASIENLRRVTDKVLNSIISSLDLLPYGL 1046
Cdd:cd05132    84 SLKDLNLEINPLKVYEQMINDIELDTGLPSNLPRGITPEEAAENPAVQNIIEPRLEMLEEITNSFLEAIINSLDEVPYGI 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1047 RYIAKVLKNSIHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQINSDQRRNLGSVAKVLQHAASNKL 1126
Cdd:cd05132   164 RWICKQIRSLTRRKFPDASDETICSLIGGFFLLRFINPAIVSPQAYMLVD----GKPSDNTRRTLTLIAKLLQNLANKPS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1127 FEGEnEHLSSMNNYLSETYQEFRKYFKEACNVPEPEEKFNMDKYTDLVTVSKPViYISIEEIISTHSLLLEHQDAIAPEK 1206
Cdd:cd05132   240 YSKE-PYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQYIALSKKDLSI-NITLNEIYNTHSLLVKHLAELAPDH 317


                  ..
gi 530379106 1207 ND 1208
Cdd:cd05132   318 ND 319
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
 757-1548 1.64e-58

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: 221.30  E-value: 1.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  757 IRKFVYLLDQSDLD---------FQEELEVARLREEVVTKIRANQQLEKDLNLMDIK----IGLLVKNRITLEDVISHSK 823
Cdd:COG5261   274 TRRSTSVFYTISLEmisnveqafFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFAE 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  824 KLNkkkggemEILNNTDnqgiKSLSKERRktLETYQQLFYLLQTN-PLYL--------------AKLIFQMPQNKSTKFM 888
Cdd:COG5261   354 RLQ-------SNINGRK----KYFPLDRR--LSLFGPLFFLLQSSiPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE 420

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  889 dtvIFTLYNYASNQREEYLLLKLFKTALEEEIKSKVDqVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIDD 968
Cdd:COG5261   421 ---IRKLYSLGKSNCEEHLSVSLFQMLLRTEVEATSL-VQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIH 496

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  969 KSLIINTNPVEVYKAWVNQLETQTGEASKLpyDVTTEQALTYPEVKNKL-EASIENLRRVTDKVLNSIISSLDLLPYGLR 1047
Cdd:COG5261   497 EDLEVDINPLLVYRALLNKGQLSPDKDLEL--LTSNEEVSEFLAVMNAVqESSAKLLELSTERILDAVYNSLDEIGYGIR 574

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1048 YIAKVLK-------NSIHEKFPDA--------TEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQINSDQRRnLG 1112
Cdd:COG5261   575 FVCELIRvvfeltpNRLFPSISDSrclrticfAEIDSLGLIGGFFFLRFVNEALVSPQTSMLKD----SCPSDNVRK-LA 649

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1113 SVAKVLQhaasnKLFEGEN--EHLSSMNNYLSETYQEFRKYFKEACNVPEPEEKFNMDKYTDLVTVSKPVIYISIEEIIS 1190
Cdd:COG5261   650 TLSKILQ-----SVFEITSsdKFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYLVNEIYLT 724

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1191 THSLLLEHQDAIAPEkndllsellgslGEVPTVESFLGEGAVDPNDPNKantlsqlskTEISLVLTSKYDIEDGEAidsR 1270
Cdd:COG5261   725 HEIIIEYLDNLYDPD------------SLVDLLLQELGELCSFPQDQRD---------TLNCLVTLPLFNRSDDPI---R 780

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1271 SLMIKTKKLIIDVIRNQPGNTLTEIL--ETP---ATAQQEVDHATDMVSRAMIDSRTPEEMKHsqsmiedaqlpleqKKR 1345
Cdd:COG5261   781 DLKQQLKRTRVYIIYVDAGTNLFEQLlrLLPsdePATRNPLDLNPNIRDDPSVSSLKSMSLMK--------------LKI 846

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1346 KIQRNLRTLEQTGHVSSENKYQDILNEIAKDIRNQRIYRKLRKAELAKLQQTLNALNKKAAFYEEQINYYDTYIKTCLDN 1425
Cdd:COG5261   847 RAIELLDELETLGFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQ 926

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1426 LKRKNTRR---SIKLDGKGEPKGAKRAKPVKYTAAKLHEKGVLLDIDDLQTNqFKNVTFdIIATEDVGIF--DVRSKFLG 1500
Cdd:COG5261   927 LQPKKSKLkgfSRGVGVVRDKPKSISSGTFKYSAQQLYKRGVLVNITIPEPN-VSNIYF-TFSSDSTDNFviEVYQPGHS 1004

                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....*...
gi 530379106 1501 VEMEKVQLNIQDLLQMQYEGVAVMKMFDKVKVNVNLLIYLLNKKFYGK 1548
Cdd:COG5261  1005 VSLPEVSFCFDDLLKRQYNKNPVVDLGGFLTFNANKLLHLIESKFYRK 1052
RasGAP_C pfam03836
RasGAP C-terminus; This domain can be found in the C terminus of the IQGAP family members, ...
 1340-1472 9.97e-47

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: 164.26  E-value: 9.97e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  1340 LEQKKRKIQRNLRTLEQTGHVSSENKYQDILNEIAKDIRNQRIYRKLRKAELAKLQQTLNALNKKAAFYEEQINYYDTYI 1419
Cdd:pfam03836    1 YVELKKKALENLLELESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYI 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 530379106  1420 KTCLDNLKRKNTRR--SIKLDGKGEPKGAKRAK--PVKYTAAKLHEKGVLLDIDDLQ 1472
Cdd:pfam03836   81 ENCLDNLQKKKKKLfsKQYFHYRKLQKRGKLPKfgSYKYSARQLYEKGVLLEIEGVP 137
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
 904-1157 7.77e-40

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: 148.79  E-value: 7.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  904 EEYLLLKLFKTALEEEIKSKVDQVQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIDDKSL----IINTNPVE 979
Cdd:cd04519     1 EEYRLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNTKNPNTLfrgnSLATKLLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  980 VYKAWVNQlETQTGEASKLPYDVTTEQAL----TYPEVKNKLEASIENLRRVTDKVLNSIISSLDLLPYGLRYIAKVLKN 1055
Cdd:cd04519    81 QYMKLVGQ-EYLKETLSPLIREILESKESceidTKLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILRE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1056 SIHEKFPDATeDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMtaggQINSDQRRNLGSVAKVLQHAASNKLFEGENEHLS 1135
Cdd:cd04519   160 FLAERFPEEP-DEAYQAVSGFLFLRFICPAIVSPELFGLVPD----EPSEQARRNLTLISKVLQSLANGVEFGDKEPFMK 234

                         250       260
                  ....*....|....*....|..
gi 530379106 1136 SMNNYLSETYQEFRKYFKEACN 1157
Cdd:cd04519   235 PLNDFIKSNKPKLKQFLDELSS 256
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
 1-184 6.03e-33

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: 139.25  E-value: 6.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106    1 MDERRRQNIAYEYLCHLEEAKRWMEVCLVEELPpTTELEEGLRNGVYLAKLAKFFAPKMVseKKIYdveqtryKKSGLHF 80
Cdd:COG5261    30 SAKNRSALRAYEYLCRVSEAKIWIEEVIEEALP-ELCFEDSLRNGVFLAKLTQRFNPDLT--TVIF-------PADKLQF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106   81 RHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGIAPQIQDLLGKVdFTEEEISNMRKELE 160
Cdd:COG5261   100 RHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTPLINSSGQIS-FTKEDIAACKKAWP 178

                         170       180
                  ....*....|....*....|....
gi 530379106  161 kygiQMPSFSKIGGILANELSVDE 184
Cdd:COG5261   179 ----RIPDFKSLGTNINTAASPEE 198
RasGAP_Neurofibromin_like cd05392
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...
 891-1166 8.79e-33

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: 130.48  E-value: 8.79e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  891 VIFTLYNYASNqreeylLLKLFKTALEEEIkSKVDQVQDIVTGNPTVIKMVVSFNRgARGQNTLRQLLAPVVKEIIDDKS 970
Cdd:cd05392    38 SLLNLFETRNR------LLPLISWLIEDEI-SHTSRAADLFRRNSVATRLLTLYAK-SVGNKYLRKVLRPLLTEIVDNKD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  971 --LIINTNPVEVykawvnqletqtgeasklpydvtteqaltypevknKLEASIENLRRVTDKVLNSIISSLDLLPYGLRY 1048
Cdd:cd05392   110 yfEVEKIKPDDE-----------------------------------NLEENADLLMKYAQMLLDSITDSVDQLPPSFRY 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1049 IAKVLKNSIHEKFPDATedelLKIVGNLLYYRYMNPAIVAPDGFDIIDMTaggqINSDQRRNLGSVAKVLQHAASNKLFE 1128
Cdd:cd05392   155 ICNTIYESVSKKFPDAA----LIAVGGFLFLRFICPAIVSPESENLLDPP----PTPEARRSLILIAKVLQNIANGVLFS 226

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 530379106 1129 GENEHLSSMNNYLSETYQEFRKYFKEACNVPEPEEKFN 1166
Cdd:cd05392   227 LKEPYLESLNEFLKKNSDRIQQFLSEVSTIPPTDPIFD 264
RasGAP_IQGAP_related cd12206
Ras-GTPase Activating Domain of proteins related to IQGAPs; RasGAP: Ras-GTPase Activating ...
 885-1205 2.13e-27

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: 115.50  E-value: 2.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  885 TKFMDTVIFTLYNYASN----QREEYLLLKLFKTALEEEIKsKVDQVQDIVTGNPTV-IKMVVSFNRgaRGQNTLRQ-LL 958
Cdd:cd12206     4 IEKNVYVTLPIFQKPTNgkmdSREEFLFIKFILELLKSDIE-NSNSNQDFLANSDNFwILLLVTFNN--LRERSELKsIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  959 APVVKEIIDDKSLIINTNPVEVYKawvnQLETQTGEASklpydvttEQALTYPEVKNKLEASIENLRRVTDKVLNSIISS 1038
Cdd:cd12206    81 GPLLVQYLENQEIDFESDPSVIYK----SLHGRPPLSS--------EEAIEDDRVSDKFVENLTNLREAVEMVAEIIFKN 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1039 LDLLPYGLRYIAKVLKNSIHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDiidmtaggqINSDQRRNLGSVAKVL 1118
Cdd:cd12206   149 VDKIPVEIRYLCTKAYIAFADKFPDESEEDILRAISKILIKSYVAPILVNPENYG---------FVDNEEDNLNEKARVL 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1119 QHAASNKLFEGE-NEHLSSMNNYLSETYQEFRKYFKEACNVPEPEEKFNMDKYTDLVTVSKPVIYISIEEIISTHSLLLE 1197
Cdd:cd12206   220 LQILSMVFFLKNfDGYLKPLNQYIEEIKPSIRDLLKELLDVPEEEQEYDKLIYYDIMSTTRPCLEILLDKVIEIIQILKE 299


                  ....*...
gi 530379106 1198 HQDAIAPE 1205
Cdd:cd12206   300 NLDEFTPD 307
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 17-127 1.21e-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: 93.94  E-value: 1.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106   17 LEEAKRWMEVCLVEELP-PTTELEEGLRNGVYLAKLAKFFAPKMVSEKKiydveqtryKKSGLHFRHTDNTVQWLRAMES 95
Cdd:cd00014     1 EEELLKWINEVLGEELPvSITDLFESLRDGVLLCKLINKLSPGSIPKIN---------KKPKSPFKKRENINLFLNACKK 71

                          90       100       110
                  ....*....|....*....|....*....|..
gi 530379106   96 IGLPKIFYPETTDVYDRKNIPRMIYCIHALSL 127
Cdd:cd00014    72 LGLPELDLFEPEDLYEKGNLKKVLGTLWALAL 103
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
 1016-1203 1.39e-13

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: 73.90  E-value: 1.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1016 KLEASIENLRRVTDKVLNSIISSLDLLPYGLRYIAKVLKNSIHEKFPDatedELLKIVGNLLYYRYMNPAIVAPDGFDII 1095
Cdd:cd05130   132 NLEENQRNLLQLTEKFFHAIISSSDEFPPQLRSVCHCLYQVVSHRFPN----SGLGAVGSAIFLRFINPAIVSPYEYGIL 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1096 DmtagGQINSDQRRNLGSVAKVLQHAASNKLFEGEnEHLSSMNNYLSETYQEFRKYFK----EACNVPEPEEKFnmdkyt 1171
Cdd:cd05130   208 D----REPPPRVKRGLKLMSKILQNIANHVLFTKE-AHMLPFNDFLRNHFEAGRRFFSsiasDCGAVDGPSSKY------ 276

                         170       180       190
                  ....*....|....*....|....*....|..
gi 530379106 1172 dLVTVSKPVIYISieeiistHSLLLEHQDAIA 1203
Cdd:cd05130   277 -LSFINDANVLAL-------HRLLWNNQEKIG 300
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
 18-126 2.90e-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: 67.39  E-value: 2.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106   18 EEAKRWMEVCLVEELPPTTeLEEGLRNGVYLAKLAKFFAPKMVSekkiydveqtRYKKSGLHFRHTDNTVQWLRAMESIG 97
Cdd:cd21210     3 QEAREWIEEVLGEKLAQGD-LLDALKDGVVLCKLANRILPADIR----------KYKESKMPFVQMENISAFLNAARKLG 71

                          90       100
                  ....*....|....*....|....*....
gi 530379106   98 LPKIFYPETTDVYDRKNIPRMIYCIHALS 126
Cdd:cd21210    72 VPENDLFQTVDLFERKNPAQVLQCLHALS 100
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
 19-125 4.83e-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: 63.87  E-value: 4.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106   19 EAKRWMEVCLVEELPPTTELEEGLRNGVYLAKLAKFFAPKMVseKKIYDveqtrykkSGLHFRHTDNTVQWLRAMESIGL 98
Cdd:cd21207     9 EALDWIEAVTGEKLDDGKDYEDVLKDGVILCKLINILKPGSV--KKINT--------SKMAFKLMENIENFLTACKGYGV 78

                          90       100
                  ....*....|....*....|....*..
gi 530379106   99 PKIFYPETTDVYDRKNIPRMIYCIHAL 125
Cdd:cd21207    79 PKTDLFQTVDLYEKKNIPQVTNCLFAL 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 18-125 3.31e-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: 61.18  E-value: 3.31e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106     18 EEAKRWMEVCLVEELPPT-TELEEGLRNGVYLAKLAKFFAPKMVSEKKIydveqtryKKSGLHFRHTDNTVQWLRAMESI 96
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPvTNFSSDLKDGVALCALLNSLSPGLVDKKKV--------AASLSRFKKIENINLALSFAEKL 72

                            90       100       110
                    ....*....|....*....|....*....|
gi 530379106     97 GlPKIFYPETTDVYD-RKNIPRMIYCIHAL 125
Cdd:smart00033   73 G-GKVVLFEPEDLVEgPKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 18-128 4.23e-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: 61.15  E-value: 4.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106    18 EEAKRWMEVCLVEELPPT--TELEEGLRNGVYLAKLAKFFAPKMVSEKKIYDVEqtrykksglhFRHTDNTVQWLR-AME 94
Cdd:pfam00307    5 KELLRWINSHLAEYGPGVrvTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSE----------FDKLENINLALDvAEK 74

                           90       100       110
                   ....*....|....*....|....*....|....
gi 530379106    95 SIGLPKIFyPETTDVYDRKNIpRMIYCIHALSLY 128
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 ...
 854-1163 1.75e-08

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: 58.51  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  854 TLETYQQLFYLLQTNPLYLAKLIFQMPQ--NKSTK-FMDTVIFTLYNYASNQREEYLLLKLFKTALEEEIKSKVDQVQDI 930
Cdd:cd05129     9 QLSHYGEFLRILRENPQLLAECLARGEKlsLEQTQnVIQTIVTSLYGNCIMPEDERLLLQLLRELMELQLKKSDNPRRLL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  931 VTGNPTVIKMVVSFNRGA-RGQNTLRQLLAPVVKEIIDDKSLIINTNPvevYKAWVNqleTQTGEASKLPYDVTTeqalt 1009
Cdd:cd05129    89 RKGSCAFSRVFKLFTELLfSAKLYLTAALHKPIMQVLVDDEIFLETDP---QKALCR---FSPAEQEKRFGEEGT----- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1010 yPEVKNKL-EASIENLRRV---TDKVLNSIISSLDLLPYGLRYIAKVLKNSIHEKFpDATEDELLKIVGNLLYYRYMNPA 1085
Cdd:cd05129   158 -PEQQRKLqQYRAEFLSRLvalVNKFISSLRQSVYCFPQSLRWIVRQLRKILTRSG-DDEEAEARALCTDLLFTNFICPA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1086 IVAPDGFDIIDmtaGGQINSDQRRNLGSVAKVLQHAASNKLFEGENEhlssmnnyLSETYQEFRK----YFKEACNVPEP 1161
Cdd:cd05129   236 IVNPEQYGIIS---DAPISEVARHNLMQVAQILQVLALTEFESPDPR--------LKELLSKFDKdcvsAFLDVVIVGRA 304


                  ..
gi 530379106 1162 EE 1163
Cdd:cd05129   305 VE 306
SCP1 COG5199
Calponin [Cytoskeleton];
18-138 2.07e-08

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 55.70  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106   18 EEAKRWMEVCLVEELPPTTELEEGLRNGVYLAKLAKFFAPKMVsekkiydveqtRYKKSGLHFRHTDNTVQWLRAMESIG 97
Cdd:COG5199    16 KEVTLWIETVLGEKFEPPGDLLSLLKDGVRLCRILNEASPLDI-----------KYKESKMPFVQMENISSFINGLKKLR 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 530379106   98 LPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKL------GIAPQI 138
Cdd:COG5199    85 VPEYELFQTNDLFEAKDLRQVVICLYSLSRYAQKErmfsgpFLGPHL 131
RasGAP_p120GAP cd05391
Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ...
 1019-1173 1.02e-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: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1019 ASIENLRRVTDKVLNSIISSLDLLPYGLRYIAKVLKNSIHEKFPDATEDElLKIVGNLLYYRYMNPAIVAPDGFDIID-- 1096
Cdd:cd05391   130 TNLEHLLNILSELVEKIFMAAEILPPTLRYIYGCLQKSVQQKWPTNTTVR-TRVVSGFVFLRLICPAILNPRMFNIISet 208

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379106 1097 --MTAGgqinsdqrRNLGSVAKVLQHAASNKLFEGENEHLSSMNNYLSETYQEFRKYFKEACNVPEPEEKFNMDKyTDL 1173
Cdd:cd05391   209 psPTAA--------RTLTLVAKSLQNLANLVEFGAKEPYMEGVNPFIKKNKERMIMFLDELGNVPELPDTTEHSR-TDL 278
RasGAP_GAP1_like cd05128
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...
 907-1120 3.66e-07

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: 53.41  E-value: 3.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  907 LLLKLFKTALEEEIkSKVDQVQDIVTGNPTVIKMVVSFNRGArGQNTLRQLLAPVVKEIIDDKSliintnPVEVykawvn 986
Cdd:cd05128    51 QIVPLLRALASREI-SKTQDPNTLFRGNSLASKCMDEFMKLV-GMQYLHETLKPVIDEIFSEKK------SCEI------ 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  987 qletqtgEASKLPYdvtteqaltypevKNKLEASIENLRRVTDKVLNSIISSLDLLPYGLRYIAKVLKNSIHEKFPDATE 1066
Cdd:cd05128   117 -------DPSKLKD-------------GEVLETNLANLRGYVERVFKAITSSARRCPTLMCEIFSDLRESAAQRFPDNED 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530379106 1067 DELLKIVGnLLYYRYMNPAIVAPDGFDIIDMTAGGQINsdqrRNLGSVAKVLQH 1120
Cdd:cd05128   177 VPYTAVSG-FIFLRFFAPAILNPKLFGLREEHPDPQTA----RTLTLISKTIQT 225
RasGAP_CLA2_BUD2 cd05137
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ...
 1011-1159 4.45e-07

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: 53.72  E-value: 4.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1011 PEVKNKLEASIENLRRVTDKVLNSIISSLDLLPYGLRyiaKVLKNsIHEKFPDATEDELLKI----VGNLLYYRYMNPAI 1086
Cdd:cd05137   149 IEKEEDLEENWENLISLTEEIWNSIYITSNDCPPELR---KILKH-IRAKVEDRYGDFLRTVtlnsVSGFLFLRFFCPAI 224

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530379106 1087 VAPDGFDIIDmtagGQINSDQRRNLGSVAKVLQHAASNKLFEGENEHLSSMNNYLSETYQEFRKYFKEACNVP 1159
Cdd:cd05137   225 LNPKLFGLLK----DHPRPRAQRTLTLIAKVLQNLANLTTFGQKEPWMEPMNEFLTTHREELKDYIDKITGIK 293
RasGAP_RASAL cd05135
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...
 954-1119 3.75e-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: 50.58  E-value: 3.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106  954 LRQLLAPVVKEIIDDKSLIintnpvEVYKAWVNQLETQTgeasklpydVTTEQALTYPEVknkLEASIENLRRVTDKVLN 1033
Cdd:cd05135   101 LHEVLKPVINRIFEEKKYV------ELDPCKIDLNRTRR---------ISFKGSLSEAQV---RESSLELLQGYLGSIID 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1034 SIISSLDLLPYGLRYIAKVLKNSIHEKFPDATEDEL--LKIVGnLLYYRYMNPAIVAPDGFDIIDMTAGGQINsdqrRNL 1111
Cdd:cd05135   163 AIVGSVDQCPPVMRVAFKQLHKRVEERFPEAEHQDVkyLAISG-FLFLRFFAPAILTPKLFQLREQHADPRTS----RTL 237


                  ....*...
gi 530379106 1112 GSVAKVLQ 1119
Cdd:cd05135   238 LLLAKAVQ 245
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
 18-125 5.98e-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: 5.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106   18 EEAKRWMEVCLVEELPPTT---ELEEGLRNGVYLAKLAKFFAPKMVSekKIYDVEQTRYKKSGLHFRHTDNTVQWLRAME 94
Cdd:cd21203     3 YEAAEWIQNVLGVLVLPDPseeEFRLCLRDGVVLCKLLNKLQPGAVP--KVVESPDDPDGAAGSAFQYFENVRNFLVAIE 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 530379106   95 SIGLPkIFYPETTDVYDRKNIPRMIYCIHAL 125
Cdd:cd21203    81 EMGLP-TFEASDLEQGGGGSRPRVVDCILAL 110
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
 1023-1208 1.72e-04

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: 45.65  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1023 NLRRVTDKVLNSIISSLDLLPYGLRYIAKVLKNSIHE-KFPDATEdellKIVGNLLYYRYMNPAIVAPDGFDIIdmtagg 1101
Cdd:cd05136   138 NLRRSVELAWCKILSSHCVFPRELREVFSSWRERLEErGREDIAD----RLISASLFLRFLCPAILSPSLFNLT------ 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379106 1102 QINSDQR--RNLGSVAKVLQHAASNKLFEGENEHLSSMNNYLSETYQEFRKYFKEACNVPEPEEKFNMDKYTDLVTVSKP 1179
Cdd:cd05136   208 QEYPSERaaRNLTLIAKVIQNLANFTRFGGKEEYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSL 287

                         170       180
                  ....*....|....*....|....*....
gi 530379106 1180 ViyisieeiistHSLLLEHQDAIAPEKND 1208
Cdd:cd05136   288 L-----------HSLLVEIISKLNQTTLD 305
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 662-683 1.84e-04

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 40.00  E-value: 1.84e-04
                            10        20
                    ....*....|....*....|..
gi 530379106    662 EQEENVVKIQAFWKGYKQRKEY 683
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
 
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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