NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|971437588|ref|XP_015132809|]
View 

ras GTPase-activating-like protein IQGAP2 isoform X4 [Gallus gallus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
914-1272 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: 730.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  914 DTVIFTLYNYASNQREEYLLLKLFKTALEEEINSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDD 993
Cdd:cd05131     1 DTVIFTLYNYASNQREEYLLLKLFETALEEEIKSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  994 KSLIINTSPVDVYKSWVNQLEMQTGEASKLPYDVTTEQALTHTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRY 1073
Cdd:cd05131    81 KSLIINTNPVEVYKAWVNQLETATGEASKLPYDVTTEQALTHPEVVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1074 IAKVLKSSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHPDQRRNLGCVAKVLQHAASNKLFE 1153
Cdd:cd05131   161 IAKVLKNSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHSEQRRNLGSVAKVLQHAASNKLFE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1154 GESEHLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIATEPND 1233
Cdd:cd05131   241 GENAHLSSMNSYLSQTYQKFRKFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIAPDQND 320
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 971437588 1234 LLNELLEGLGPVPDVESFLGEGSVDPNDPNRESTLNQLA 1272
Cdd:cd05131   321 LLHELLKDLGEVPDVESFLGEGTVDPNDPNKENTLSQLG 359
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
11-166 4.56e-114

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: 356.25  E-value: 4.56e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588   11 RPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKRWMEVCLEEELPPTTELEEGLRNGVYLAKLAKFFAPNLVSDK 90
Cdd:cd21275     1 RPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKQWIEACLNEELPPTTELEEGLRNGVYLVKLAKFFAPKLVSEK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 971437588   91 KIYDVKQERYKRSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGLAPQIQ 166
Cdd:cd21275    81 KIYDVDQVRYKRSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNMPRVIYCIHALSLYLFKLGIAPQIQ 156
IQG1 super family cl34962
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
783-1575 7.90e-61

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: 228.62  E-value: 7.90e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  783 RKFAYLLDQSDLD---------FQEELEVTRLREEVVTKIRSNQQLEKDLNLMDIK----IGLLVKNRITLQDVVLHSkk 849
Cdd:COG5261   275 RRSTSVFYTISLEmisnveqafFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFA-- 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  850 lnkksknqleEMVMVDKQGIKGLSKERRKkLEAYQHLFYLLQTN-PMYL--------------AKLIFQMPQNKSTKFMd 914
Cdd:COG5261   353 ----------ERLQSNINGRKKYFPLDRR-LSLFGPLFFLLQSSiPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE- 420
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  915 tvIFTLYNYASNQREEYLLLKLFKTALEEEINSKVDqIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDDK 994
Cdd:COG5261   421 --IRKLYSLGKSNCEEHLSVSLFQMLLRTEVEATSL-VQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHE 497
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  995 SLIINTSPVDVYKSWVNQLEMQTGEASKLpyDVTTEQALTHTEVVNKL-ESSIQSLRAVTDKVLTSIFSSLNMMPYGMRY 1073
Cdd:COG5261   498 DLEVDINPLLVYRALLNKGQLSPDKDLEL--LTSNEEVSEFLAVMNAVqESSAKLLELSTERILDAVYNSLDEIGYGIRF 575
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1074 IAKVLKS-------SLHEKFPDA--------TEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQIHPDQRRnLGC 1138
Cdd:COG5261   576 VCELIRVvfeltpnRLFPSISDSrclrticfAEIDSLGLIGGFFFLRFVNEALVSPQTSMLKD----SCPSDNVRK-LAT 650
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1139 VAKVLQhaasnKLFEGES--EHLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYIsIEEIINT 1216
Cdd:COG5261   651 LSKILQ-----SVFEITSsdKFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYL-VNEIYLT 724
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1217 HSLLLEHQDAIaTEPNDLlnelleglgpVPDVESFLGEGSVDPNDPNResTLNQLAkteislsltSKYELREGEDQdLKS 1296
Cdd:COG5261   725 HEIIIEYLDNL-YDPDSL----------VDLLLQELGELCSFPQDQRD--TLNCLV---------TLPLFNRSDDP-IRD 781
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1297 LMIKTKRLIVDMIRTQPGDTLPEILETTATAQQESEHSKLVEKRAILDSKTPEKMKrSQSIFEdgqlpieqKKRKIQRNL 1376
Cdd:COG5261   782 LKQQLKRTRVYIIYVDAGTNLFEQLLRLLPSDEPATRNPLDLNPNIRDDPSVSSLK-SMSLMK--------LKIRAIELL 852
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1377 RTLEQAGLVSSATKYQEIINEIAKDIRNQRRYRHHRKAELVKLQQTLNALNSKTAFYEEQINYYNTYIKTCLDNLTRKNS 1456
Cdd:COG5261   853 DELETLGFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKS 932
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1457 RRSIKLDGKEEVKGSKKLKQA-SLKYTAARLHEKGVILEIEDLQTNqFKNVMFDITpGEEVGDFEIKAKFLG--VEMEKV 1533
Cdd:COG5261   933 KLKGFSRGVGVVRDKPKSISSgTFKYSAQQLYKRGVLVNITIPEPN-VSNIYFTFS-SDSTDNFVIEVYQPGhsVSLPEV 1010
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|..
gi 971437588 1534 QLHFQDLLQMQYEGVAVMKMFDKAKVNVNLLIFLLNKKFYGK 1575
Cdd:COG5261  1011 SFCFDDLLKRQYNKNPVVDLGGFLTFNANKLLHLIESKFYRK 1052
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
720-739 1.55e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


:

Pssm-ID: 459869  Cd Length: 21  Bit Score: 37.30  E-value: 1.55e-03
                           10        20
                   ....*....|....*....|
gi 971437588   720 AAIVKIQSWVKMWLARRAYR 739
Cdd:pfam00612    2 KAAIKIQAAWRGYLARKRYK 21
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
688-708 2.85e-03

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


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.53  E-value: 2.85e-03
                            10        20
                    ....*....|....*....|.
gi 971437588    688 QEPSAIKIQAFWKGFKQRKSY 708
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRY 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 ...
914-1272 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: 730.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  914 DTVIFTLYNYASNQREEYLLLKLFKTALEEEINSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDD 993
Cdd:cd05131     1 DTVIFTLYNYASNQREEYLLLKLFETALEEEIKSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  994 KSLIINTSPVDVYKSWVNQLEMQTGEASKLPYDVTTEQALTHTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRY 1073
Cdd:cd05131    81 KSLIINTNPVEVYKAWVNQLETATGEASKLPYDVTTEQALTHPEVVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1074 IAKVLKSSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHPDQRRNLGCVAKVLQHAASNKLFE 1153
Cdd:cd05131   161 IAKVLKNSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHSEQRRNLGSVAKVLQHAASNKLFE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1154 GESEHLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIATEPND 1233
Cdd:cd05131   241 GENAHLSSMNSYLSQTYQKFRKFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIAPDQND 320
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 971437588 1234 LLNELLEGLGPVPDVESFLGEGSVDPNDPNRESTLNQLA 1272
Cdd:cd05131   321 LLHELLKDLGEVPDVESFLGEGTVDPNDPNKENTLSQLG 359
CH_IQGAP2 cd21275
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP2; IQ motif ...
11-166 4.56e-114

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: 356.25  E-value: 4.56e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588   11 RPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKRWMEVCLEEELPPTTELEEGLRNGVYLAKLAKFFAPNLVSDK 90
Cdd:cd21275     1 RPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKQWIEACLNEELPPTTELEEGLRNGVYLVKLAKFFAPKLVSEK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 971437588   91 KIYDVKQERYKRSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGLAPQIQ 166
Cdd:cd21275    81 KIYDVDQVRYKRSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNMPRVIYCIHALSLYLFKLGIAPQIQ 156
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
903-1230 6.32e-79

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: 264.94  E-value: 6.32e-79
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588    903 QMPQNKSTKFMDTVIFTLYNYASNQREEYLLLKLFKTALEeeINSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQL 982
Cdd:smart00323    1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLS--LASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRAL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588    983 LAPVVKEIMDD----KSLIINTSPVDVYKSWVNQLEMQTGEASKLPYDVTTEQALTHTEVVNK---LESSIQSLRAVTDK 1055
Cdd:smart00323   79 IDPEVERTDDPntifRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEgedLETNLENLLQYVER 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588   1056 VLTSIFSSLNMMPYGMRYIAKVLKSSLHEKFPDAteDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMtaggQIHPDQRRN 1135
Cdd:smart00323  159 LFDAIINSSDRLPYGLRDICKQLRQAAEKRFPDA--DVIYKAVSSFVFLRFFCPAIVSPKLFNLVDE----HPDPTTRRT 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588   1136 LGCVAKVLQHAASNKLFEGESEHLSSMNTYLSQTYQKFRNFFQAACDVPEPeekfNIDEYSDMVTLskpviyiSIEEIIN 1215
Cdd:smart00323  233 LTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEI----LVDKVSDSTTI-------SGRELSL 301
                           330
                    ....*....|....*
gi 971437588   1216 THSLLLEHQDAIATE 1230
Cdd:smart00323  302 LHSLLLENGDALKRE 316
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
936-1148 2.38e-70

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: 234.49  E-value: 2.38e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588   936 LFKTALEEEINSkVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDDKSLIINTSPVDVYKSWVNQLEM 1015
Cdd:pfam00616    1 LISELIEEEIES-SDNPNDLLRGNSLVSKLLETYNRRPRGQEYLKKVLGPLVRKIIEDEDLDLESDPRKIYESLINQEEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  1016 QTGEaSKLPYDVTTEQALTHTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRYIAKVLKSSLHEKFPDATEDELL 1095
Cdd:pfam00616   80 KTGR-SDLPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEIL 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 971437588  1096 KIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQIHPDQRRNLGCVAKVLQHAAS 1148
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVD----HQISPKQRRNLTLIAKVLQNLAN 207
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
783-1575 7.90e-61

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


Pssm-ID: 227586 [Multi-domain]  Cd Length: 1054  Bit Score: 228.62  E-value: 7.90e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  783 RKFAYLLDQSDLD---------FQEELEVTRLREEVVTKIRSNQQLEKDLNLMDIK----IGLLVKNRITLQDVVLHSkk 849
Cdd:COG5261   275 RRSTSVFYTISLEmisnveqafFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFA-- 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  850 lnkksknqleEMVMVDKQGIKGLSKERRKkLEAYQHLFYLLQTN-PMYL--------------AKLIFQMPQNKSTKFMd 914
Cdd:COG5261   353 ----------ERLQSNINGRKKYFPLDRR-LSLFGPLFFLLQSSiPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE- 420
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  915 tvIFTLYNYASNQREEYLLLKLFKTALEEEINSKVDqIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDDK 994
Cdd:COG5261   421 --IRKLYSLGKSNCEEHLSVSLFQMLLRTEVEATSL-VQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHE 497
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  995 SLIINTSPVDVYKSWVNQLEMQTGEASKLpyDVTTEQALTHTEVVNKL-ESSIQSLRAVTDKVLTSIFSSLNMMPYGMRY 1073
Cdd:COG5261   498 DLEVDINPLLVYRALLNKGQLSPDKDLEL--LTSNEEVSEFLAVMNAVqESSAKLLELSTERILDAVYNSLDEIGYGIRF 575
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1074 IAKVLKS-------SLHEKFPDA--------TEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQIHPDQRRnLGC 1138
Cdd:COG5261   576 VCELIRVvfeltpnRLFPSISDSrclrticfAEIDSLGLIGGFFFLRFVNEALVSPQTSMLKD----SCPSDNVRK-LAT 650
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1139 VAKVLQhaasnKLFEGES--EHLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYIsIEEIINT 1216
Cdd:COG5261   651 LSKILQ-----SVFEITSsdKFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYL-VNEIYLT 724
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1217 HSLLLEHQDAIaTEPNDLlnelleglgpVPDVESFLGEGSVDPNDPNResTLNQLAkteislsltSKYELREGEDQdLKS 1296
Cdd:COG5261   725 HEIIIEYLDNL-YDPDSL----------VDLLLQELGELCSFPQDQRD--TLNCLV---------TLPLFNRSDDP-IRD 781
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1297 LMIKTKRLIVDMIRTQPGDTLPEILETTATAQQESEHSKLVEKRAILDSKTPEKMKrSQSIFEdgqlpieqKKRKIQRNL 1376
Cdd:COG5261   782 LKQQLKRTRVYIIYVDAGTNLFEQLLRLLPSDEPATRNPLDLNPNIRDDPSVSSLK-SMSLMK--------LKIRAIELL 852
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1377 RTLEQAGLVSSATKYQEIINEIAKDIRNQRRYRHHRKAELVKLQQTLNALNSKTAFYEEQINYYNTYIKTCLDNLTRKNS 1456
Cdd:COG5261   853 DELETLGFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKS 932
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1457 RRSIKLDGKEEVKGSKKLKQA-SLKYTAARLHEKGVILEIEDLQTNqFKNVMFDITpGEEVGDFEIKAKFLG--VEMEKV 1533
Cdd:COG5261   933 KLKGFSRGVGVVRDKPKSISSgTFKYSAQQLYKRGVLVNITIPEPN-VSNIYFTFS-SDSTDNFVIEVYQPGhsVSLPEV 1010
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|..
gi 971437588 1534 QLHFQDLLQMQYEGVAVMKMFDKAKVNVNLLIFLLNKKFYGK 1575
Cdd:COG5261  1011 SFCFDDLLKRQYNKNPVVDLGGFLTFNANKLLHLIESKFYRK 1052
RasGAP_C pfam03836
RasGAP C-terminus; This domain can be found in the C terminus of the IQGAP family members, ...
1365-1499 2.68e-48

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: 168.50  E-value: 2.68e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  1365 IEQKKRKIQRNLRTLEQAGLVSSATKYQEIINEIAKDIRNQRRYRHHRKAELVKLQQTLNALNSKTAFYEEQINYYNTYI 1444
Cdd:pfam03836    1 YVELKKKALENLLELESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYI 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 971437588  1445 KTCLDNLTRKNSRR--SIKLDGKEEVKGSKKLKQASLKYTAARLHEKGVILEIEDLQ 1499
Cdd:pfam03836   81 ENCLDNLQKKKKKLfsKQYFHYRKLQKRGKLPKFGSYKYSARQLYEKGVLLEIEGVP 137
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
4-211 2.14e-35

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: 147.34  E-value: 2.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588    4 EELAPLQRPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKRWMEVCLEEELPpTTELEEGLRNGVYLAKLAKFFA 83
Cdd:COG5261     6 GSLNRYVENLGRPIGTPSHLKTKTSAKNRSALRAYEYLCRVSEAKIWIEEVIEEALP-ELCFEDSLRNGVFLAKLTQRFN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588   84 PNLVsdKKIYdvkqeryKRSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGLAP 163
Cdd:COG5261    85 PDLT--TVIF-------PADKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTP 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 971437588  164 QIQDLLGKVdFTEEEISNMSKELEkygiQMPSFSKIGGILASELSVDE 211
Cdd:COG5261   156 LINSSGQIS-FTKEDIAACKKAWP----RIPDFKSLGTNINTAASPEE 198
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
45-152 1.50e-12

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: 65.03  E-value: 1.50e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588     45 EEAKRWMEVCLEEELPPT-TELEEGLRNGVYLAKLAKFFAPNLVSDKKIydvkqeryKRSGLHFRHTDNTVQWLRAMESI 123
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPvTNFSSDLKDGVALCALLNSLSPGLVDKKKV--------AASLSRFKKIENINLALSFAEKL 72
                            90       100       110
                    ....*....|....*....|....*....|
gi 971437588    124 GlPKIFYPETTDVYD-RKNIPRMIYCIHAL 152
Cdd:smart00033   73 G-GKVVLFEPEDLVEgPKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
45-155 6.23e-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: 60.76  E-value: 6.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588    45 EEAKRWMEVCLEEELPPT--TELEEGLRNGVYLAKLAKFFAPNLVSDKKIydvkqerykrSGLHFRHTDNTVQWLR-AME 121
Cdd:pfam00307    5 KELLRWINSHLAEYGPGVrvTNFTTDLRDGLALCALLNKLAPGLVDKKKL----------NKSEFDKLENINLALDvAEK 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 971437588   122 SIGLPKIFyPETTDVYDRKNIpRMIYCIHALSLY 155
Cdd:pfam00307   75 KLGVPKVL-IEPEDLVEGDNK-SVLTYLASLFRR 106
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
720-739 1.55e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 37.30  E-value: 1.55e-03
                           10        20
                   ....*....|....*....|
gi 971437588   720 AAIVKIQSWVKMWLARRAYR 739
Cdd:pfam00612    2 KAAIKIQAAWRGYLARKRYK 21
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
688-708 2.85e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.53  E-value: 2.85e-03
                            10        20
                    ....*....|....*....|.
gi 971437588    688 QEPSAIKIQAFWKGFKQRKSY 708
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRY 22
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
720-739 3.47e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.15  E-value: 3.47e-03
                            10        20
                    ....*....|....*....|
gi 971437588    720 AAIVKIQSWVKMWLARRAYR 739
Cdd:smart00015    4 RAAIIIQAAWRGYLARKRYK 23
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
720-743 3.93e-03

calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).


Pssm-ID: 409646 [Multi-domain]  Cd Length: 149  Bit Score: 39.41  E-value: 3.93e-03
                          10        20
                  ....*....|....*....|....
gi 971437588  720 AAIVKIQSWVKMWLARRAYRKRLQ 743
Cdd:cd21759    46 EALIKIQKTVRGYLARKKHRPRIK 69
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
691-708 9.90e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.99  E-value: 9.90e-03
                           10
                   ....*....|....*...
gi 971437588   691 SAIKIQAFWKGFKQRKSY 708
Cdd:pfam00612    3 AAIKIQAAWRGYLARKRY 20
 
Name Accession Description Interval E-value
RasGAP_IQGAP2 cd05131
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...
914-1272 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: 730.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  914 DTVIFTLYNYASNQREEYLLLKLFKTALEEEINSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDD 993
Cdd:cd05131     1 DTVIFTLYNYASNQREEYLLLKLFETALEEEIKSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  994 KSLIINTSPVDVYKSWVNQLEMQTGEASKLPYDVTTEQALTHTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRY 1073
Cdd:cd05131    81 KSLIINTNPVEVYKAWVNQLETATGEASKLPYDVTTEQALTHPEVVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1074 IAKVLKSSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHPDQRRNLGCVAKVLQHAASNKLFE 1153
Cdd:cd05131   161 IAKVLKNSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHSEQRRNLGSVAKVLQHAASNKLFE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1154 GESEHLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIATEPND 1233
Cdd:cd05131   241 GENAHLSSMNSYLSQTYQKFRKFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIAPDQND 320
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 971437588 1234 LLNELLEGLGPVPDVESFLGEGSVDPNDPNRESTLNQLA 1272
Cdd:cd05131   321 LLHELLKDLGEVPDVESFLGEGTVDPNDPNKENTLSQLG 359
RasGAP_IQGAP1 cd05133
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...
914-1296 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: 598.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  914 DTVIFTLYNYASNQREEYLLLKLFKTALEEEINSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDD 993
Cdd:cd05133     1 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  994 KSLIINTSPVDVYKSWVNQLEMQTGEASKLPYDVTTEQALTHTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRY 1073
Cdd:cd05133    81 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQAMSHEEVRTRLDASIKNMRMVTDKFLSAIISSVDKIPYGMRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1074 IAKVLKSSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHPDQRRNLGCVAKVLQHAASNKLFE 1153
Cdd:cd05133   161 IAKVLKDTLHEKFPDAGEDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1154 GESEHLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIATEPND 1233
Cdd:cd05133   241 GDNAHLSPINEYLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971437588 1234 LLNELLEGLGPVPDVESFLGEGSVDPNDPNREStlnqLAKTEISLSLTSKYELREGEDQDLKS 1296
Cdd:cd05133   321 PIHELLDDLGEVPTIESLIGENPGPPGDPNRET----LAKTEVSLTLTNKFDVPGDENAEMDA 379
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
924-1254 0e+00

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


Pssm-ID: 213329 [Multi-domain]  Cd Length: 331  Bit Score: 547.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  924 ASNQREEYLLLKLFKTALEEEINSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDDKSLIINTSPV 1003
Cdd:cd05127     1 ASNRREEYLLLKLFKTALREEIESKVSLPEDIVTGNPTVIKLVVNYNRGPRGQKYLRELLGPVVKEILDDDDLDLETDPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1004 DVYKSWVNQLEMQTGEASKLPYDVTTEQALTHTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRYIAKVLKSSLH 1083
Cdd:cd05127    81 DIYKAWINQEESRTGEPSKLPYDVTREQALKDPEVRKRLIEHLEKLRAITDKFLTAITESLDKMPYGMRYIAKVLKEALR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1084 EKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHPDQRRNLGCVAKVLQHAASNKLFEGESEHLSSMN 1163
Cdd:cd05127   161 EKFPDAPEEEILKIVGNLLYYRYMNPAIVAPEAFDIIDLSVGGQLSPLQRRNLGSIAKVLQQAASGKLFGGENPYLSPLN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1164 TYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIATEPNDLLNELLEGLG 1243
Cdd:cd05127   241 PYISESHEKFKKFFLEACTVPEAEEHFNIDEYSDLTMLTKPTIYISLQEIFATHKLLLEHQDEIAPDPDDPLRELLDDLG 320
                         330
                  ....*....|.
gi 971437588 1244 PVPDVESFLGE 1254
Cdd:cd05127   321 PAPTIESLLGS 331
RasGAP_IQGAP3 cd12207
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ...
914-1261 1.74e-173

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: 524.01  E-value: 1.74e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  914 DTVIFTLYNYASNQREEYLLLKLFKTALEEEINSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDD 993
Cdd:cd12207     1 ESVIFSLYNYASNRREAYLLLQLFKTALQEEISSKVEKPQDVITGNPTVIRLLVSFYRSARGQNALRHILGPVVQDVLQD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  994 KSLIINTSPVDVYKSWVNQLEMQTGEASKLPYDVTTEQALTHTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRY 1073
Cdd:cd12207    81 KGLSIRTDPVQIYKAWINQTETQSGCRSSLPYEVSPEQALSHPEVQRRLDIAIRNLLAVTDKFLSAITSSVDKIPYGMRY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1074 IAKVLKSSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHPDQRRNLGCVAKVLQHAASNKLFE 1153
Cdd:cd12207   161 VAKVLRDSLQEKFPGASEDEVYKVVGNLLYYRFMNPAVVAPDGFDIVDCSAGGALQPEQRRMLGSVAKVLQHAAANKHFQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1154 GESEHLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIATEPND 1233
Cdd:cd12207   241 GDSEHLQALNQYLEETHVKFRKFILQACCVPEPEERFNVDEYSEMVAVAKPVIYITVGELINTHKLLLEHQDSIAPDHSD 320
                         330       340
                  ....*....|....*....|....*...
gi 971437588 1234 LLNELLEGLGPVPDVESFLGEGSVDPND 1261
Cdd:cd12207   321 PLHELLEDLGEVPTVQSLIGESWADLGD 348
CH_IQGAP2 cd21275
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP2; IQ motif ...
11-166 4.56e-114

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: 356.25  E-value: 4.56e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588   11 RPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKRWMEVCLEEELPPTTELEEGLRNGVYLAKLAKFFAPNLVSDK 90
Cdd:cd21275     1 RPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKQWIEACLNEELPPTTELEEGLRNGVYLVKLAKFFAPKLVSEK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 971437588   91 KIYDVKQERYKRSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGLAPQIQ 166
Cdd:cd21275    81 KIYDVDQVRYKRSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNMPRVIYCIHALSLYLFKLGIAPQIQ 156
CH_IQGAP1 cd21274
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif ...
34-187 3.38e-90

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: 289.20  E-value: 3.38e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588   34 QNIAYEYLCHLEEAKRWMEVCLEEELPPTTELEEGLRNGVYLAKLAKFFAPNLVSDKKIYDVKQERYKRSGLHFRHTDNT 113
Cdd:cd21274     1 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971437588  114 VQWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGLAPQIQDLLGKVDFTEEEISNMSKELE 187
Cdd:cd21274    81 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTELE 154
CH_IQGAP3 cd21276
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP3; IQ motif ...
35-186 3.50e-89

calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP3; IQ motif containing GTPase activating protein 3 (IQGAP3) associates with Ras GTP-binding proteins. It regulates the organization of the cytoskeleton under the regulation of Rac1 and Cdc42 in neuronal cells. The depletion of IQGAP3 is shown to impair neurite or axon outgrowth in neuronal cells with disorganized cytoskeleton. It belongs to the IQGAP family, which consists of multi-domain proteins having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP3 contains a single copy of the CH domain at the N-terminus.


Pssm-ID: 409125 [Multi-domain]  Cd Length: 152  Bit Score: 286.10  E-value: 3.50e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588   35 NIAYEYLCHLEEAKRWMEVCLEEELPPTTELEEGLRNGVYLAKLAKFFAPNLVSDKKIYDVKQERYKRSGLHFRHTDNTV 114
Cdd:cd21276     1 NVAYQYLCRLEEAKRWMEACLKEELPPPTELEESLRNGVYLAKLGHCFAPRVVPLKKIYDLEQMRYQATGLHFRHTDNIN 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 971437588  115 QWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGLAPQIQDLLGKVDFTEEEISNMSKEL 186
Cdd:cd21276    81 HWRNAMMHIGLPSIFHPETTDIYDKKNMPRVVYCIHALSLYLFRLGLAPQIHDLYGKVKFTEEEINNMKLEL 152
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
903-1230 6.32e-79

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: 264.94  E-value: 6.32e-79
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588    903 QMPQNKSTKFMDTVIFTLYNYASNQREEYLLLKLFKTALEeeINSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQL 982
Cdd:smart00323    1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLS--LASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRAL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588    983 LAPVVKEIMDD----KSLIINTSPVDVYKSWVNQLEMQTGEASKLPYDVTTEQALTHTEVVNK---LESSIQSLRAVTDK 1055
Cdd:smart00323   79 IDPEVERTDDPntifRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEgedLETNLENLLQYVER 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588   1056 VLTSIFSSLNMMPYGMRYIAKVLKSSLHEKFPDAteDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMtaggQIHPDQRRN 1135
Cdd:smart00323  159 LFDAIINSSDRLPYGLRDICKQLRQAAEKRFPDA--DVIYKAVSSFVFLRFFCPAIVSPKLFNLVDE----HPDPTTRRT 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588   1136 LGCVAKVLQHAASNKLFEGESEHLSSMNTYLSQTYQKFRNFFQAACDVPEPeekfNIDEYSDMVTLskpviyiSIEEIIN 1215
Cdd:smart00323  233 LTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEI----LVDKVSDSTTI-------SGRELSL 301
                           330
                    ....*....|....*
gi 971437588   1216 THSLLLEHQDAIATE 1230
Cdd:smart00323  302 LHSLLLENGDALKRE 316
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
936-1148 2.38e-70

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: 234.49  E-value: 2.38e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588   936 LFKTALEEEINSkVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDDKSLIINTSPVDVYKSWVNQLEM 1015
Cdd:pfam00616    1 LISELIEEEIES-SDNPNDLLRGNSLVSKLLETYNRRPRGQEYLKKVLGPLVRKIIEDEDLDLESDPRKIYESLINQEEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  1016 QTGEaSKLPYDVTTEQALTHTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRYIAKVLKSSLHEKFPDATEDELL 1095
Cdd:pfam00616   80 KTGR-SDLPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEIL 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 971437588  1096 KIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQIHPDQRRNLGCVAKVLQHAAS 1148
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVD----HQISPKQRRNLTLIAKVLQNLAN 207
CH_IQGAP cd21206
calponin homology (CH) domain found in the IQ motif containing GTPase activating protein ...
35-160 7.35e-69

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: 226.72  E-value: 7.35e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588   35 NIAYEYLCHLEEAKRWMEVCLEEELPPTTELEEGLRNGVYLAKLAKFFAPNLVSDKKIYDVkqerykrsGLHFRHTDNTV 114
Cdd:cd21206     1 TIAYEYLCRLEEAKQWIEACLNEELPPTTEFEEELRNGVVLAKLANKFAPKLVPLKKIYDV--------GLQFRHTDNIN 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 971437588  115 QWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLG 160
Cdd:cd21206    73 HFLRALKKIGLPKIFHFETTDLYEKKNIPKVIYCLHALSLLLFKLG 118
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
783-1575 7.90e-61

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


Pssm-ID: 227586 [Multi-domain]  Cd Length: 1054  Bit Score: 228.62  E-value: 7.90e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  783 RKFAYLLDQSDLD---------FQEELEVTRLREEVVTKIRSNQQLEKDLNLMDIK----IGLLVKNRITLQDVVLHSkk 849
Cdd:COG5261   275 RRSTSVFYTISLEmisnveqafFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFA-- 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  850 lnkksknqleEMVMVDKQGIKGLSKERRKkLEAYQHLFYLLQTN-PMYL--------------AKLIFQMPQNKSTKFMd 914
Cdd:COG5261   353 ----------ERLQSNINGRKKYFPLDRR-LSLFGPLFFLLQSSiPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE- 420
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  915 tvIFTLYNYASNQREEYLLLKLFKTALEEEINSKVDqIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDDK 994
Cdd:COG5261   421 --IRKLYSLGKSNCEEHLSVSLFQMLLRTEVEATSL-VQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHE 497
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  995 SLIINTSPVDVYKSWVNQLEMQTGEASKLpyDVTTEQALTHTEVVNKL-ESSIQSLRAVTDKVLTSIFSSLNMMPYGMRY 1073
Cdd:COG5261   498 DLEVDINPLLVYRALLNKGQLSPDKDLEL--LTSNEEVSEFLAVMNAVqESSAKLLELSTERILDAVYNSLDEIGYGIRF 575
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1074 IAKVLKS-------SLHEKFPDA--------TEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQIHPDQRRnLGC 1138
Cdd:COG5261   576 VCELIRVvfeltpnRLFPSISDSrclrticfAEIDSLGLIGGFFFLRFVNEALVSPQTSMLKD----SCPSDNVRK-LAT 650
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1139 VAKVLQhaasnKLFEGES--EHLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYIsIEEIINT 1216
Cdd:COG5261   651 LSKILQ-----SVFEITSsdKFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYL-VNEIYLT 724
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1217 HSLLLEHQDAIaTEPNDLlnelleglgpVPDVESFLGEGSVDPNDPNResTLNQLAkteislsltSKYELREGEDQdLKS 1296
Cdd:COG5261   725 HEIIIEYLDNL-YDPDSL----------VDLLLQELGELCSFPQDQRD--TLNCLV---------TLPLFNRSDDP-IRD 781
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1297 LMIKTKRLIVDMIRTQPGDTLPEILETTATAQQESEHSKLVEKRAILDSKTPEKMKrSQSIFEdgqlpieqKKRKIQRNL 1376
Cdd:COG5261   782 LKQQLKRTRVYIIYVDAGTNLFEQLLRLLPSDEPATRNPLDLNPNIRDDPSVSSLK-SMSLMK--------LKIRAIELL 852
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1377 RTLEQAGLVSSATKYQEIINEIAKDIRNQRRYRHHRKAELVKLQQTLNALNSKTAFYEEQINYYNTYIKTCLDNLTRKNS 1456
Cdd:COG5261   853 DELETLGFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKS 932
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1457 RRSIKLDGKEEVKGSKKLKQA-SLKYTAARLHEKGVILEIEDLQTNqFKNVMFDITpGEEVGDFEIKAKFLG--VEMEKV 1533
Cdd:COG5261   933 KLKGFSRGVGVVRDKPKSISSgTFKYSAQQLYKRGVLVNITIPEPN-VSNIYFTFS-SDSTDNFVIEVYQPGhsVSLPEV 1010
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|..
gi 971437588 1534 QLHFQDLLQMQYEGVAVMKMFDKAKVNVNLLIFLLNKKFYGK 1575
Cdd:COG5261  1011 SFCFDDLLKRQYNKNPVVDLGGFLTFNANKLLHLIESKFYRK 1052
RasGAP_GAPA cd05132
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...
912-1247 1.11e-57

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: 203.74  E-value: 1.11e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  912 FMDTVIFTLYNYASNQREEYLLLKLFKTALEEEInSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIM 991
Cdd:cd05132     5 LLQTVMFTLYGNQYESREEHLLLSMFQSVLTYEF-DETTEFGSLLRANTAVSRMMTTYTRRGPGQSYLKTVLADRINDLI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  992 DDKSLIINTSPVDVYKSWVNQLEMQTGEASKLPYDVTTEQALTHTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGM 1071
Cdd:cd05132    84 SLKDLNLEINPLKVYEQMINDIELDTGLPSNLPRGITPEEAAENPAVQNIIEPRLEMLEEITNSFLEAIINSLDEVPYGI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1072 RYIAKVLKSSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQIHPDQRRNLGCVAKVLQHAASNKL 1151
Cdd:cd05132   164 RWICKQIRSLTRRKFPDASDETICSLIGGFFLLRFINPAIVSPQAYMLVD----GKPSDNTRRTLTLIAKLLQNLANKPS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1152 FEGESeHLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYsdmVTLSKPVIYISI--EEIINTHSLLLEHQDAIAT 1229
Cdd:cd05132   240 YSKEP-YMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQY---IALSKKDLSINItlNEIYNTHSLLVKHLAELAP 315
                         330
                  ....*....|....*...
gi 971437588 1230 EPNDLLNELLEGLGPVPD 1247
Cdd:cd05132   316 DHNDHLRLILQELGPAPP 333
RasGAP_C pfam03836
RasGAP C-terminus; This domain can be found in the C terminus of the IQGAP family members, ...
1365-1499 2.68e-48

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: 168.50  E-value: 2.68e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  1365 IEQKKRKIQRNLRTLEQAGLVSSATKYQEIINEIAKDIRNQRRYRHHRKAELVKLQQTLNALNSKTAFYEEQINYYNTYI 1444
Cdd:pfam03836    1 YVELKKKALENLLELESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYI 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 971437588  1445 KTCLDNLTRKNSRR--SIKLDGKEEVKGSKKLKQASLKYTAARLHEKGVILEIEDLQ 1499
Cdd:pfam03836   81 ENCLDNLQKKKKKLfsKQYFHYRKLQKRGKLPKFGSYKYSARQLYEKGVLLEIEGVP 137
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
929-1182 2.86e-37

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: 141.47  E-value: 2.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  929 EEYLLLKLFKTALEEEINSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDDKSL----IINTSPVD 1004
Cdd:cd04519     1 EEYRLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNTKNPNTLfrgnSLATKLLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1005 VYKSWVNQlEMQTGEASKLPYDVTTEQAL----THTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRYIAKVLKS 1080
Cdd:cd04519    81 QYMKLVGQ-EYLKETLSPLIREILESKESceidTKLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILRE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1081 SLHEKFPDATeDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMtaggQIHPDQRRNLGCVAKVLQHAASNKLFEGESEHLS 1160
Cdd:cd04519   160 FLAERFPEEP-DEAYQAVSGFLFLRFICPAIVSPELFGLVPD----EPSEQARRNLTLISKVLQSLANGVEFGDKEPFMK 234
                         250       260
                  ....*....|....*....|..
gi 971437588 1161 SMNTYLSQTYQKFRNFFQAACD 1182
Cdd:cd04519   235 PLNDFIKSNKPKLKQFLDELSS 256
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
4-211 2.14e-35

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: 147.34  E-value: 2.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588    4 EELAPLQRPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKRWMEVCLEEELPpTTELEEGLRNGVYLAKLAKFFA 83
Cdd:COG5261     6 GSLNRYVENLGRPIGTPSHLKTKTSAKNRSALRAYEYLCRVSEAKIWIEEVIEEALP-ELCFEDSLRNGVFLAKLTQRFN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588   84 PNLVsdKKIYdvkqeryKRSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGLAP 163
Cdd:COG5261    85 PDLT--TVIF-------PADKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTP 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 971437588  164 QIQDLLGKVdFTEEEISNMSKELEkygiQMPSFSKIGGILASELSVDE 211
Cdd:COG5261   156 LINSSGQIS-FTKEDIAACKKAWP----RIPDFKSLGTNINTAASPEE 198
RasGAP_Neurofibromin_like cd05392
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...
916-1230 2.12e-31

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: 126.24  E-value: 2.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  916 VIFTLYNYASNqreeylLLKLFKTALEEEINsKVDQIQDIVTGNPTVIKMVVSFNRgARGQNTLRQLLAPVVKEIMDDKS 995
Cdd:cd05392    38 SLLNLFETRNR------LLPLISWLIEDEIS-HTSRAADLFRRNSVATRLLTLYAK-SVGNKYLRKVLRPLLTEIVDNKD 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  996 --LIINTSPVDVykswvnqlemqtgeasklpydvtteqalthtevvnKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRY 1073
Cdd:cd05392   110 yfEVEKIKPDDE-----------------------------------NLEENADLLMKYAQMLLDSITDSVDQLPPSFRY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1074 IAKVLKSSLHEKFPDATedelLKIVGNLLYYRYMNPAIVAPDGFDIIDMTaggqIHPDQRRNLGCVAKVLQHAASNKLFE 1153
Cdd:cd05392   155 ICNTIYESVSKKFPDAA----LIAVGGFLFLRFICPAIVSPESENLLDPP----PTPEARRSLILIAKVLQNIANGVLFS 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 971437588 1154 GESEHLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNideysdmVTLSKPViyisIEEIINTHSLLLEHQDAIATE 1230
Cdd:cd05392   227 LKEPYLESLNEFLKKNSDRIQQFLSEVSTIPPTDPIFD-------ESDEEPI----TADLRYLHKFLYLHFLEIRKE 292
RasGAP_IQGAP_related cd12206
Ras-GTPase Activating Domain of proteins related to IQGAPs; RasGAP: Ras-GTPase Activating ...
910-1233 3.84e-28

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: 117.81  E-value: 3.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  910 TKFMDTVIFTLYNYASN----QREEYLLLKLFKTALEEEINsKVDQIQDIVTGNPTV-IKMVVSFNRgaRGQNTLRQ-LL 983
Cdd:cd12206     4 IEKNVYVTLPIFQKPTNgkmdSREEFLFIKFILELLKSDIE-NSNSNQDFLANSDNFwILLLVTFNN--LRERSELKsIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  984 APVVKEIMDDKSLIINTSPVDVYKSWVNQLEMQTgeasklpydvttEQALTHTEVVNKLESSIQSLRAVTDKVLTSIFSS 1063
Cdd:cd12206    81 GPLLVQYLENQEIDFESDPSVIYKSLHGRPPLSS------------EEAIEDDRVSDKFVENLTNLREAVEMVAEIIFKN 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1064 LNMMPYGMRYIAKVLKSSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtaggqihpDQRRNLGCVAKVL 1143
Cdd:cd12206   149 VDKIPVEIRYLCTKAYIAFADKFPDESEEDILRAISKILIKSYVAPILVNPENYGFVD---------NEEDNLNEKARVL 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1144 QHAASNKLFEGESE-HLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLE 1222
Cdd:cd12206   220 LQILSMVFFLKNFDgYLKPLNQYIEEIKPSIRDLLKELLDVPEEEQEYDKLIYYDIMSTTRPCLEILLDKVIEIIQILKE 299
                         330
                  ....*....|.
gi 971437588 1223 HQDAIAtePND 1233
Cdd:cd12206   300 NLDEFT--PDD 308
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
44-154 2.67e-23

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: 95.87  E-value: 2.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588   44 LEEAKRWMEVCLEEELP-PTTELEEGLRNGVYLAKLAKFFAPNLVSdkkiydvkqERYKRSGLHFRHTDNTVQWLRAMES 122
Cdd:cd00014     1 EEELLKWINEVLGEELPvSITDLFESLRDGVLLCKLINKLSPGSIP---------KINKKPKSPFKKRENINLFLNACKK 71
                          90       100       110
                  ....*....|....*....|....*....|..
gi 971437588  123 IGLPKIFYPETTDVYDRKNIPRMIYCIHALSL 154
Cdd:cd00014    72 LGLPELDLFEPEDLYEKGNLKKVLGTLWALAL 103
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
932-1228 4.73e-15

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


Pssm-ID: 213332 [Multi-domain]  Cd Length: 332  Bit Score: 78.13  E-value: 4.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  932 LLLKLFKTALEeeinsKVDQIQDIVTGNPTVIK-MVVSFNrgARGQNTLRQLLAPVVKEIMddksliinTSPvDVYKSWV 1010
Cdd:cd05130    59 LLWNMFSKEVE-----LADSMQTLFRGNSLASKiMTFCFK--VYGATYLQSLLEPLLRTMI--------TSS-EWVSYEV 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1011 NQLEMQTGEasklpydvtteqalthtevvnKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRYIAKVLKSSLHEKFPDat 1090
Cdd:cd05130   123 DPTRLEGNE---------------------NLEENQRNLLQLTEKFFHAIISSSDEFPPQLRSVCHCLYQVVSHRFPN-- 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1091 edELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQIHPDQRRNLGCVAKVLQHAASNKLFEGEsEHLSSMNTYLSQTY 1170
Cdd:cd05130   180 --SGLGAVGSAIFLRFINPAIVSPYEYGILD----REPPPRVKRGLKLMSKILQNIANHVLFTKE-AHMLPFNDFLRNHF 252
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 971437588 1171 QKFRNFFQAACDVPEPEEKFNideysdmvtlSKPVIYISIEEIINTHSLLLEHQDAIA 1228
Cdd:cd05130   253 EAGRRFFSSIASDCGAVDGPS----------SKYLSFINDANVLALHRLLWNNQEKIG 300
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
46-152 1.27e-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: 65.41  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588   46 EAKRWMEVCLEEELPPTTELEEGLRNGVYLAKLAKFFAPNLVsdKKIYDvkqerykrSGLHFRHTDNTVQWLRAMESIGL 125
Cdd:cd21207     9 EALDWIEAVTGEKLDDGKDYEDVLKDGVILCKLINILKPGSV--KKINT--------SKMAFKLMENIENFLTACKGYGV 78
                          90       100
                  ....*....|....*....|....*..
gi 971437588  126 PKIFYPETTDVYDRKNIPRMIYCIHAL 152
Cdd:cd21207    79 PKTDLFQTVDLYEKKNIPQVTNCLFAL 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
45-152 1.50e-12

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: 65.03  E-value: 1.50e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588     45 EEAKRWMEVCLEEELPPT-TELEEGLRNGVYLAKLAKFFAPNLVSDKKIydvkqeryKRSGLHFRHTDNTVQWLRAMESI 123
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPvTNFSSDLKDGVALCALLNSLSPGLVDKKKV--------AASLSRFKKIENINLALSFAEKL 72
                            90       100       110
                    ....*....|....*....|....*....|
gi 971437588    124 GlPKIFYPETTDVYD-RKNIPRMIYCIHAL 152
Cdd:smart00033   73 G-GKVVLFEPEDLVEgPKLILGVIWTLISL 101
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
45-153 5.12e-12

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


Pssm-ID: 409059 [Multi-domain]  Cd Length: 101  Bit Score: 63.54  E-value: 5.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588   45 EEAKRWMEVCLEEELPPTTeLEEGLRNGVYLAKLAKFFAPNLVSdkkiydvkqeRYKRSGLHFRHTDNTVQWLRAMESIG 124
Cdd:cd21210     3 QEAREWIEEVLGEKLAQGD-LLDALKDGVVLCKLANRILPADIR----------KYKESKMPFVQMENISAFLNAARKLG 71
                          90       100
                  ....*....|....*....|....*....
gi 971437588  125 LPKIFYPETTDVYDRKNIPRMIYCIHALS 153
Cdd:cd21210    72 VPENDLFQTVDLFERKNPAQVLQCLHALS 100
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
45-155 6.23e-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: 60.76  E-value: 6.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588    45 EEAKRWMEVCLEEELPPT--TELEEGLRNGVYLAKLAKFFAPNLVSDKKIydvkqerykrSGLHFRHTDNTVQWLR-AME 121
Cdd:pfam00307    5 KELLRWINSHLAEYGPGVrvTNFTTDLRDGLALCALLNKLAPGLVDKKKL----------NKSEFDKLENINLALDvAEK 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 971437588   122 SIGLPKIFyPETTDVYDRKNIpRMIYCIHALSLY 155
Cdd:pfam00307   75 KLGVPKVL-IEPEDLVEGDNK-SVLTYLASLFRR 106
SCP1 COG5199
Calponin [Cytoskeleton];
45-165 4.92e-08

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 54.54  E-value: 4.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588   45 EEAKRWMEVCLEEELPPTTELEEGLRNGVYLAKLAKFFAPNLVsdkkiydvkqeRYKRSGLHFRHTDNTVQWLRAMESIG 124
Cdd:COG5199    16 KEVTLWIETVLGEKFEPPGDLLSLLKDGVRLCRILNEASPLDI-----------KYKESKMPFVQMENISSFINGLKKLR 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 971437588  125 LPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKL------GLAPQI 165
Cdd:COG5199    85 VPEYELFQTNDLFEAKDLRQVVICLYSLSRYAQKErmfsgpFLGPHL 131
RasGAP_RASAL cd05135
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...
979-1183 9.99e-08

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: 55.20  E-value: 9.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  979 LRQLLAPVVKEIMDDKSLIintsPVDVYKswvnqLEMQTGEASKLPYDVTTEQALthtevvnklESSIQSLRAVTDKVLT 1058
Cdd:cd05135   101 LHEVLKPVINRIFEEKKYV----ELDPCK-----IDLNRTRRISFKGSLSEAQVR---------ESSLELLQGYLGSIID 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1059 SIFSSLNMMPYGMRYIAKVLKSSLHEKFPDATEDEL--LKIVGnLLYYRYMNPAIVAPDGFDIIDMtaggqiHPDQR--R 1134
Cdd:cd05135   163 AIVGSVDQCPPVMRVAFKQLHKRVEERFPEAEHQDVkyLAISG-FLFLRFFAPAILTPKLFQLREQ------HADPRtsR 235
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 971437588 1135 NLGCVAKVLQHAAS--NKLFEGESEHLSSMNTYLSQTYQKFRNFFQAACDV 1183
Cdd:cd05135   236 TLLLLAKAVQSIGNlgLQLGQGKEQWMAPLHPFILQSVARVKDFLDRLIDI 286
RasGAP_GAP1_like cd05128
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...
932-1183 1.03e-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: 54.95  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  932 LLLKLFKTALEEEInSKVDQIQDIVTGNPTVIKMVVSFNRGArGQNTLRQLLAPVVKEIMDD-KSLIINtspvdvykswv 1010
Cdd:cd05128    51 QIVPLLRALASREI-SKTQDPNTLFRGNSLASKCMDEFMKLV-GMQYLHETLKPVIDEIFSEkKSCEID----------- 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1011 nqlemqtgeASKLPYDVTTEQALTHtevvnklessiqsLRAVTDKVLTSIFSSLNMMPYGMRYIAKVLKSSLHEKFPDAT 1090
Cdd:cd05128   118 ---------PSKLKDGEVLETNLAN-------------LRGYVERVFKAITSSARRCPTLMCEIFSDLRESAAQRFPDNE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1091 EDELLKIVGnLLYYRYMNPAIVAPDGFDIIDMtaggqiHPDQR--RNLGCVAKVLQH----AASNKLFEGESEHLSSM-N 1163
Cdd:cd05128   176 DVPYTAVSG-FIFLRFFAPAILNPKLFGLREE------HPDPQtaRTLTLISKTIQTlgnlGSSSSGLGVKEAYMSPLyE 248
                         250       260
                  ....*....|....*....|.
gi 971437588 1164 TYLSQTY-QKFRNFFQAACDV 1183
Cdd:cd05128   249 RFTDEQHvDAVKKFLDRISSV 269
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
1042-1222 1.25e-07

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: 55.28  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1042 LESSIQSLRAVTDKVLTSIFSSLNMMPygmryiaKVLK---SSLHEKFPDATEDELL-KIVGNLLYYRYMNPAIVAPDGF 1117
Cdd:cd05136   132 LSRNQANLRRSVELAWCKILSSHCVFP-------RELRevfSSWRERLEERGREDIAdRLISASLFLRFLCPAILSPSLF 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1118 DIIdmtaggQIHPDQR--RNLGCVAKVLQHAASNKLFEGESEHLSSMNTYLSQTYQKFRNFFQaacDVPEPEEKFNIDEY 1195
Cdd:cd05136   205 NLT------QEYPSERaaRNLTLIAKVIQNLANFTRFGGKEEYMEFMNDFVEQEWPNMKQFLQ---EISSPSPSSNSSDF 275
                         170       180
                  ....*....|....*....|....*..
gi 971437588 1196 SDMVTLSKpviyisieEIINTHSLLLE 1222
Cdd:cd05136   276 DGYIDLGR--------ELSLLHSLLVE 294
RasGAP_RAP6 cd05129
Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is ...
881-1233 1.91e-07

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: 55.04  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  881 EAYQHLFY----------LLQTNPMYLAKLIFQMPQ--NKSTK-FMDTVIFTLYNYASNQREEYLLLKLFKTALEEEINS 947
Cdd:cd05129     1 DAYKLLGYqlshygeflrILRENPQLLAECLARGEKlsLEQTQnVIQTIVTSLYGNCIMPEDERLLLQLLRELMELQLKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  948 KVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQ--LLAPVVKEIMDDksliINTSPVDVYKSWVNqleMQTGEASKLPY 1025
Cdd:cd05129    81 SDNPRRLLRKGSCAFSRVFKLFTELLFSAKLYLTaaLHKPIMQVLVDD----EIFLETDPQKALCR---FSPAEQEKRFG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1026 DVTTEQAltHTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRYIAKVLKSSLHEKFpDATEDELLKIVGNLLYYR 1105
Cdd:cd05129   154 EEGTPEQ--QRKLQQYRAEFLSRLVALVNKFISSLRQSVYCFPQSLRWIVRQLRKILTRSG-DDEEAEARALCTDLLFTN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1106 YMNPAIVAPDGFDIIDmtaGGQIHPDQRRNLGCVAKVLQHAASNKLFEGESEhlssmntyLSQTYQKFRN----FFQAAC 1181
Cdd:cd05129   231 FICPAIVNPEQYGIIS---DAPISEVARHNLMQVAQILQVLALTEFESPDPR--------LKELLSKFDKdcvsAFLDVV 299
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 971437588 1182 DVPEPEEKFNIDEySDMVTLSKPVIYISIEEiINTHSLLLEHQDAIATEPND 1233
Cdd:cd05129   300 IVGRAVETPPPSS-SALLEGSRTAVLITESD-LATLVEFLRSVKTGDEEKED 349
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
45-152 2.08e-07

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: 50.88  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588   45 EEAKRWMEVCLEEELPPTT---ELEEGLRNGVYLAKLAKFFAPNLVSdkKIYDVKQERYKRSGLHFRHTDNTVQWLRAME 121
Cdd:cd21203     3 YEAAEWIQNVLGVLVLPDPseeEFRLCLRDGVVLCKLLNKLQPGAVP--KVVESPDDPDGAAGSAFQYFENVRNFLVAIE 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 971437588  122 SIGLPkIFYPETTDVYDRKNIPRMIYCIHAL 152
Cdd:cd21203    81 EMGLP-TFEASDLEQGGGGSRPRVVDCILAL 110
RasGAP_p120GAP cd05391
Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ...
1047-1188 1.62e-06

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: 52.10  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1047 QSLRAVTDKVLTSIFSSLNMMPYGMRYIAKVLKSSLHEKFPDATEDElLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGg 1126
Cdd:cd05391   133 EHLLNILSELVEKIFMAAEILPPTLRYIYGCLQKSVQQKWPTNTTVR-TRVVSGFVFLRLICPAILNPRMFNIISETPS- 210
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 971437588 1127 qihPDQRRNLGCVAKVLQHAASNKLFEGESEHLSSMNTYLSQTYQKFRNFFQAACDVPEPEE 1188
Cdd:cd05391   211 ---PTAARTLTLVAKSLQNLANLVEFGAKEPYMEGVNPFIKKNKERMIMFLDELGNVPELPD 269
RasGAP_CLA2_BUD2 cd05137
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ...
1042-1184 3.07e-05

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: 47.94  E-value: 3.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1042 LESSIQSLRAVTDKVLTSIFSSLNMMPYGMRYIAKVLKSSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIId 1121
Cdd:cd05137   155 LEENWENLISLTEEIWNSIYITSNDCPPELRKILKHIRAKVEDRYGDFLRTVTLNSVSGFLFLRFFCPAILNPKLFGLL- 233
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 971437588 1122 mtaggQIHPD--QRRNLGCVAKVLQHAASNKLFEGESEHLSSMNTYLSQTYQKFRNFFQAACDVP 1184
Cdd:cd05137   234 -----KDHPRprAQRTLTLIAKVLQNLANLTTFGQKEPWMEPMNEFLTTHREELKDYIDKITGIK 293
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
720-739 1.55e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 37.30  E-value: 1.55e-03
                           10        20
                   ....*....|....*....|
gi 971437588   720 AAIVKIQSWVKMWLARRAYR 739
Cdd:pfam00612    2 KAAIKIQAAWRGYLARKRYK 21
RasGAP_RASA4 cd05395
Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also ...
975-1144 1.82e-03

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


Pssm-ID: 213343 [Multi-domain]  Cd Length: 287  Bit Score: 42.17  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588  975 GQNTLRQLLAPVVKEIMDDKSLI-INTSPVDVYKSWVNQLEMQTGEAsklpydvtteqalthtEVvnkLESSIQSLRAVT 1053
Cdd:cd05395    97 GMQYLHSVLGPTINRVFEEKKYVeLDPSKVEIKDVGCSGLHRIQTES----------------EV---IEQSAQLLQSYL 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971437588 1054 DKVLTSIFSSLNMMPYGMRYIAKVLKSSLHEKFPDATEDELLKI-VGNLLYYRYMNPAIVAPDGFDIIDMtaggqiHPDQ 1132
Cdd:cd05395   158 GELLSAISKSVKYCPAVIRATFRQLFKRVQERFPENQHQNVKFIaVTSFLCLRFFSPAIMSPKLFHLREK------HADA 231
                         170
                  ....*....|....
gi 971437588 1133 R--RNLGCVAKVLQ 1144
Cdd:cd05395   232 RtsRTLLLLAKAVQ 245
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
688-708 2.85e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.53  E-value: 2.85e-03
                            10        20
                    ....*....|....*....|.
gi 971437588    688 QEPSAIKIQAFWKGFKQRKSY 708
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRY 22
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
720-739 3.47e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.15  E-value: 3.47e-03
                            10        20
                    ....*....|....*....|
gi 971437588    720 AAIVKIQSWVKMWLARRAYR 739
Cdd:smart00015    4 RAAIIIQAAWRGYLARKRYK 23
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
720-743 3.93e-03

calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).


Pssm-ID: 409646 [Multi-domain]  Cd Length: 149  Bit Score: 39.41  E-value: 3.93e-03
                          10        20
                  ....*....|....*....|....
gi 971437588  720 AAIVKIQSWVKMWLARRAYRKRLQ 743
Cdd:cd21759    46 EALIKIQKTVRGYLARKKHRPRIK 69
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
691-708 9.90e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.99  E-value: 9.90e-03
                           10
                   ....*....|....*...
gi 971437588   691 SAIKIQAFWKGFKQRKSY 708
Cdd:pfam00612    3 AAIKIQAAWRGYLARKRY 20
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH