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Conserved domains on  [gi|2201823352|ref|XP_046791004|]
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ras GTPase-activating-like protein IQGAP2 isoform X5 [Gallus gallus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RasGAP_IQGAP2 cd05131
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...
849-1207 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: 731.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  849 DTVIFTLYNYASNQREEYLLLKLFKTALEEEINSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDD 928
Cdd:cd05131      1 DTVIFTLYNYASNQREEYLLLKLFETALEEEIKSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  929 KSLIINTSPVDVYKSWVNQLEMQTGEASKLPYDVTTEQALTHTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRY 1008
Cdd:cd05131     81 KSLIINTNPVEVYKAWVNQLETATGEASKLPYDVTTEQALTHPEVVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1009 IAKVLKSSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHPDQRRNLGCVAKVLQHAASNKLFE 1088
Cdd:cd05131    161 IAKVLKNSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHSEQRRNLGSVAKVLQHAASNKLFE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1089 GESEHLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIATEPND 1168
Cdd:cd05131    241 GENAHLSSMNSYLSQTYQKFRKFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIAPDQND 320
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2201823352 1169 LLNELLEGLGPVPDVESFLGEGSVDPNDPNRESTLNQLA 1207
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 4.50e-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: 355.48  E-value: 4.50e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   11 RPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKRWMEVCLEEELPPTTELEEGLRNGVYLAKLAKFFAPNLVSDK 90
Cdd:cd21275      1 RPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKQWIEACLNEELPPTTELEEGLRNGVYLVKLAKFFAPKLVSEK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2201823352   91 KIYDVKQERYKRSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGLAPQIQ 166
Cdd:cd21275     81 KIYDVDQVRYKRSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNMPRVIYCIHALSLYLFKLGIAPQIQ 156
IQG1 super family cl34962
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
718-1510 4.99e-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: 229.00  E-value: 4.99e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  718 RKFAYLLDQSDLD---------FQEELEVTRLREEVVTKIRSNQQLEKDLNLMDIK----IGLLVKNRITLQDVVLHSkk 784
Cdd:COG5261    275 RRSTSVFYTISLEmisnveqafFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFA-- 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  785 lnkksknqleEMVMVDKQGIKGLSKERRKkLEAYQHLFYLLQTN-PMYL--------------AKLIFQMPQNKSTKFMd 849
Cdd:COG5261    353 ----------ERLQSNINGRKKYFPLDRR-LSLFGPLFFLLQSSiPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE- 420
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  850 tvIFTLYNYASNQREEYLLLKLFKTALEEEINSKVDqIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDDK 929
Cdd:COG5261    421 --IRKLYSLGKSNCEEHLSVSLFQMLLRTEVEATSL-VQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHE 497
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  930 SLIINTSPVDVYKSWVNQLEMQTGEASKLpyDVTTEQALTHTEVVNKL-ESSIQSLRAVTDKVLTSIFSSLNMMPYGMRY 1008
Cdd:COG5261    498 DLEVDINPLLVYRALLNKGQLSPDKDLEL--LTSNEEVSEFLAVMNAVqESSAKLLELSTERILDAVYNSLDEIGYGIRF 575
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1009 IAKVLKS-------SLHEKFPDA--------TEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQIHPDQRRnLGC 1073
Cdd:COG5261    576 VCELIRVvfeltpnRLFPSISDSrclrticfAEIDSLGLIGGFFFLRFVNEALVSPQTSMLKD----SCPSDNVRK-LAT 650
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1074 VAKVLQhaasnKLFEGES--EHLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYIsIEEIINT 1151
Cdd:COG5261    651 LSKILQ-----SVFEITSsdKFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYL-VNEIYLT 724
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1152 HSLLLEHQDAIaTEPNDLlnelleglgpVPDVESFLGEGSVDPNDPNResTLNQLAkteislsltSKYELREGEDQdLKS 1231
Cdd:COG5261    725 HEIIIEYLDNL-YDPDSL----------VDLLLQELGELCSFPQDQRD--TLNCLV---------TLPLFNRSDDP-IRD 781
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1232 LMIKTKRLIVDMIRTQPGDTLPEILETTATAQQESEHSKLVEKRAILDSKTPEKMKrSQSIFEdgqlpieqKKRKIQRNL 1311
Cdd:COG5261    782 LKQQLKRTRVYIIYVDAGTNLFEQLLRLLPSDEPATRNPLDLNPNIRDDPSVSSLK-SMSLMK--------LKIRAIELL 852
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1312 RTLEQAGLVSSATKYQEIINEIAKDIRNQRRYRHHRKAELVKLQQTLNALNSKTAFYEEQINYYNTYIKTCLDNLTRKNS 1391
Cdd:COG5261    853 DELETLGFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKS 932
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1392 RRSIKLDGKEEVKGSKKLKQA-SLKYTAARLHEKGVILEIEDLQTNqFKNVMFDITpGEEVGDFEIKAKFLG--VEMEKV 1468
Cdd:COG5261    933 KLKGFSRGVGVVRDKPKSISSgTFKYSAQQLYKRGVLVNITIPEPN-VSNIYFTFS-SDSTDNFVIEVYQPGhsVSLPEV 1010
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|..
gi 2201823352 1469 QLHFQDLLQMQYEGVAVMKMFDKAKVNVNLLIFLLNKKFYGK 1510
Cdd:COG5261   1011 SFCFDDLLKRQYNKNPVVDLGGFLTFNANKLLHLIESKFYRK 1052
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
655-674 1.58e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


:

Pssm-ID: 459869  Cd Length: 21  Bit Score: 37.30  E-value: 1.58e-03
                           10        20
                   ....*....|....*....|
gi 2201823352  655 AAIVKIQSWVKMWLARRAYR 674
Cdd:pfam00612    2 KAAIKIQAAWRGYLARKRYK 21
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
623-643 2.99e-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: 2.99e-03
                            10        20
                    ....*....|....*....|.
gi 2201823352   623 QEPSAIKIQAFWKGFKQRKSY 643
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 ...
849-1207 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: 731.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  849 DTVIFTLYNYASNQREEYLLLKLFKTALEEEINSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDD 928
Cdd:cd05131      1 DTVIFTLYNYASNQREEYLLLKLFETALEEEIKSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  929 KSLIINTSPVDVYKSWVNQLEMQTGEASKLPYDVTTEQALTHTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRY 1008
Cdd:cd05131     81 KSLIINTNPVEVYKAWVNQLETATGEASKLPYDVTTEQALTHPEVVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1009 IAKVLKSSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHPDQRRNLGCVAKVLQHAASNKLFE 1088
Cdd:cd05131    161 IAKVLKNSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHSEQRRNLGSVAKVLQHAASNKLFE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1089 GESEHLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIATEPND 1168
Cdd:cd05131    241 GENAHLSSMNSYLSQTYQKFRKFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIAPDQND 320
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2201823352 1169 LLNELLEGLGPVPDVESFLGEGSVDPNDPNRESTLNQLA 1207
Cdd:cd05131    321 LLHELLKDLGEVPDVESFLGEGTVDPNDPNKENTLSQLG 359
CH_IQGAP2 cd21275
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP2; IQ motif ...
11-166 4.50e-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: 355.48  E-value: 4.50e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   11 RPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKRWMEVCLEEELPPTTELEEGLRNGVYLAKLAKFFAPNLVSDK 90
Cdd:cd21275      1 RPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKQWIEACLNEELPPTTELEEGLRNGVYLVKLAKFFAPKLVSEK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2201823352   91 KIYDVKQERYKRSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGLAPQIQ 166
Cdd:cd21275     81 KIYDVDQVRYKRSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNMPRVIYCIHALSLYLFKLGIAPQIQ 156
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
838-1165 4.20e-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: 265.33  E-value: 4.20e-79
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   838 QMPQNKSTKFMDTVIFTLYNYASNQREEYLLLKLFKTALEeeINSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQL 917
Cdd:smart00323    1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLS--LASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRAL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   918 LAPVVKEIMDD----KSLIINTSPVDVYKSWVNQLEMQTGEASKLPYDVTTEQALTHTEVVNK---LESSIQSLRAVTDK 990
Cdd:smart00323   79 IDPEVERTDDPntifRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEgedLETNLENLLQYVER 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   991 VLTSIFSSLNMMPYGMRYIAKVLKSSLHEKFPDAteDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMtaggQIHPDQRRN 1070
Cdd:smart00323  159 LFDAIINSSDRLPYGLRDICKQLRQAAEKRFPDA--DVIYKAVSSFVFLRFFCPAIVSPKLFNLVDE----HPDPTTRRT 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  1071 LGCVAKVLQHAASNKLFEGESEHLSSMNTYLSQTYQKFRNFFQAACDVPEPeekfNIDEYSDMVTLskpviyiSIEEIIN 1150
Cdd:smart00323  233 LTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEI----LVDKVSDSTTI-------SGRELSL 301
                           330
                    ....*....|....*
gi 2201823352  1151 THSLLLEHQDAIATE 1165
Cdd:smart00323  302 LHSLLLENGDALKRE 316
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
871-1083 1.39e-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: 235.26  E-value: 1.39e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  871 LFKTALEEEINSkVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDDKSLIINTSPVDVYKSWVNQLEM 950
Cdd:pfam00616    1 LISELIEEEIES-SDNPNDLLRGNSLVSKLLETYNRRPRGQEYLKKVLGPLVRKIIEDEDLDLESDPRKIYESLINQEEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  951 QTGEaSKLPYDVTTEQALTHTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRYIAKVLKSSLHEKFPDATEDELL 1030
Cdd:pfam00616   80 KTGR-SDLPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEIL 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2201823352 1031 KIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQIHPDQRRNLGCVAKVLQHAAS 1083
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVD----HQISPKQRRNLTLIAKVLQNLAN 207
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
718-1510 4.99e-61

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


Pssm-ID: 227586 [Multi-domain]  Cd Length: 1054  Bit Score: 229.00  E-value: 4.99e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  718 RKFAYLLDQSDLD---------FQEELEVTRLREEVVTKIRSNQQLEKDLNLMDIK----IGLLVKNRITLQDVVLHSkk 784
Cdd:COG5261    275 RRSTSVFYTISLEmisnveqafFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFA-- 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  785 lnkksknqleEMVMVDKQGIKGLSKERRKkLEAYQHLFYLLQTN-PMYL--------------AKLIFQMPQNKSTKFMd 849
Cdd:COG5261    353 ----------ERLQSNINGRKKYFPLDRR-LSLFGPLFFLLQSSiPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE- 420
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  850 tvIFTLYNYASNQREEYLLLKLFKTALEEEINSKVDqIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDDK 929
Cdd:COG5261    421 --IRKLYSLGKSNCEEHLSVSLFQMLLRTEVEATSL-VQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHE 497
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  930 SLIINTSPVDVYKSWVNQLEMQTGEASKLpyDVTTEQALTHTEVVNKL-ESSIQSLRAVTDKVLTSIFSSLNMMPYGMRY 1008
Cdd:COG5261    498 DLEVDINPLLVYRALLNKGQLSPDKDLEL--LTSNEEVSEFLAVMNAVqESSAKLLELSTERILDAVYNSLDEIGYGIRF 575
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1009 IAKVLKS-------SLHEKFPDA--------TEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQIHPDQRRnLGC 1073
Cdd:COG5261    576 VCELIRVvfeltpnRLFPSISDSrclrticfAEIDSLGLIGGFFFLRFVNEALVSPQTSMLKD----SCPSDNVRK-LAT 650
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1074 VAKVLQhaasnKLFEGES--EHLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYIsIEEIINT 1151
Cdd:COG5261    651 LSKILQ-----SVFEITSsdKFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYL-VNEIYLT 724
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1152 HSLLLEHQDAIaTEPNDLlnelleglgpVPDVESFLGEGSVDPNDPNResTLNQLAkteislsltSKYELREGEDQdLKS 1231
Cdd:COG5261    725 HEIIIEYLDNL-YDPDSL----------VDLLLQELGELCSFPQDQRD--TLNCLV---------TLPLFNRSDDP-IRD 781
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1232 LMIKTKRLIVDMIRTQPGDTLPEILETTATAQQESEHSKLVEKRAILDSKTPEKMKrSQSIFEdgqlpieqKKRKIQRNL 1311
Cdd:COG5261    782 LKQQLKRTRVYIIYVDAGTNLFEQLLRLLPSDEPATRNPLDLNPNIRDDPSVSSLK-SMSLMK--------LKIRAIELL 852
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1312 RTLEQAGLVSSATKYQEIINEIAKDIRNQRRYRHHRKAELVKLQQTLNALNSKTAFYEEQINYYNTYIKTCLDNLTRKNS 1391
Cdd:COG5261    853 DELETLGFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKS 932
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1392 RRSIKLDGKEEVKGSKKLKQA-SLKYTAARLHEKGVILEIEDLQTNqFKNVMFDITpGEEVGDFEIKAKFLG--VEMEKV 1468
Cdd:COG5261    933 KLKGFSRGVGVVRDKPKSISSgTFKYSAQQLYKRGVLVNITIPEPN-VSNIYFTFS-SDSTDNFVIEVYQPGhsVSLPEV 1010
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|..
gi 2201823352 1469 QLHFQDLLQMQYEGVAVMKMFDKAKVNVNLLIFLLNKKFYGK 1510
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, ...
1300-1434 3.50e-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: 168.11  E-value: 3.50e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1300 IEQKKRKIQRNLRTLEQAGLVSSATKYQEIINEIAKDIRNQRRYRHHRKAELVKLQQTLNALNSKTAFYEEQINYYNTYI 1379
Cdd:pfam03836    1 YVELKKKALENLLELESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYI 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2201823352 1380 KTCLDNLTRKNSRR--SIKLDGKEEVKGSKKLKQASLKYTAARLHEKGVILEIEDLQ 1434
Cdd:pfam03836   81 ENCLDNLQKKKKKLfsKQYFHYRKLQKRGKLPKFGSYKYSARQLYEKGVLLEIEGVP 137
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
4-211 1.85e-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: 1.85e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352    4 EELAPLQRPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKRWMEVCLEEELPpTTELEEGLRNGVYLAKLAKFFA 83
Cdd:COG5261      6 GSLNRYVENLGRPIGTPSHLKTKTSAKNRSALRAYEYLCRVSEAKIWIEEVIEEALP-ELCFEDSLRNGVFLAKLTQRFN 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   84 PNLVsdKKIYdvkqeryKRSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGLAP 163
Cdd:COG5261     85 PDLT--TVIF-------PADKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTP 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2201823352  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 1.23e-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: 65.41  E-value: 1.23e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352    45 EEAKRWMEVCLEEELPPT-TELEEGLRNGVYLAKLAKFFAPNLVSDKKIydvkqeryKRSGLHFRHTDNTVQWLRAMESI 123
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPvTNFSSDLKDGVALCALLNSLSPGLVDKKKV--------AASLSRFKKIENINLALSFAEKL 72
                            90       100       110
                    ....*....|....*....|....*....|
gi 2201823352   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 5.10e-11

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 61.15  E-value: 5.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   45 EEAKRWMEVCLEEELPPT--TELEEGLRNGVYLAKLAKFFAPNLVSDKKIydvkqerykrSGLHFRHTDNTVQWLR-AME 121
Cdd:pfam00307    5 KELLRWINSHLAEYGPGVrvTNFTTDLRDGLALCALLNKLAPGLVDKKKL----------NKSEFDKLENINLALDvAEK 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2201823352  122 SIGLPKIFyPETTDVYDRKNIpRMIYCIHALSLY 155
Cdd:pfam00307   75 KLGVPKVL-IEPEDLVEGDNK-SVLTYLASLFRR 106
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
655-674 1.58e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 37.30  E-value: 1.58e-03
                           10        20
                   ....*....|....*....|
gi 2201823352  655 AAIVKIQSWVKMWLARRAYR 674
Cdd:pfam00612    2 KAAIKIQAAWRGYLARKRYK 21
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
623-643 2.99e-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: 2.99e-03
                            10        20
                    ....*....|....*....|.
gi 2201823352   623 QEPSAIKIQAFWKGFKQRKSY 643
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRY 22
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
655-674 3.67e-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: 3.67e-03
                            10        20
                    ....*....|....*....|
gi 2201823352   655 AAIVKIQSWVKMWLARRAYR 674
Cdd:smart00015    4 RAAIIIQAAWRGYLARKRYK 23
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
655-678 4.10e-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: 4.10e-03
                           10        20
                   ....*....|....*....|....
gi 2201823352  655 AAIVKIQSWVKMWLARRAYRKRLQ 678
Cdd:cd21759     46 EALIKIQKTVRGYLARKKHRPRIK 69
 
Name Accession Description Interval E-value
RasGAP_IQGAP2 cd05131
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...
849-1207 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: 731.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  849 DTVIFTLYNYASNQREEYLLLKLFKTALEEEINSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDD 928
Cdd:cd05131      1 DTVIFTLYNYASNQREEYLLLKLFETALEEEIKSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  929 KSLIINTSPVDVYKSWVNQLEMQTGEASKLPYDVTTEQALTHTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRY 1008
Cdd:cd05131     81 KSLIINTNPVEVYKAWVNQLETATGEASKLPYDVTTEQALTHPEVVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1009 IAKVLKSSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHPDQRRNLGCVAKVLQHAASNKLFE 1088
Cdd:cd05131    161 IAKVLKNSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHSEQRRNLGSVAKVLQHAASNKLFE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1089 GESEHLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIATEPND 1168
Cdd:cd05131    241 GENAHLSSMNSYLSQTYQKFRKFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIAPDQND 320
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2201823352 1169 LLNELLEGLGPVPDVESFLGEGSVDPNDPNRESTLNQLA 1207
Cdd:cd05131    321 LLHELLKDLGEVPDVESFLGEGTVDPNDPNKENTLSQLG 359
RasGAP_IQGAP1 cd05133
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...
849-1231 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: 598.95  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  849 DTVIFTLYNYASNQREEYLLLKLFKTALEEEINSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDD 928
Cdd:cd05133      1 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  929 KSLIINTSPVDVYKSWVNQLEMQTGEASKLPYDVTTEQALTHTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRY 1008
Cdd:cd05133     81 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQAMSHEEVRTRLDASIKNMRMVTDKFLSAIISSVDKIPYGMRF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1009 IAKVLKSSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHPDQRRNLGCVAKVLQHAASNKLFE 1088
Cdd:cd05133    161 IAKVLKDTLHEKFPDAGEDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1089 GESEHLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIATEPND 1168
Cdd:cd05133    241 GDNAHLSPINEYLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 320
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2201823352 1169 LLNELLEGLGPVPDVESFLGEGSVDPNDPNREStlnqLAKTEISLSLTSKYELREGEDQDLKS 1231
Cdd:cd05133    321 PIHELLDDLGEVPTIESLIGENPGPPGDPNRET----LAKTEVSLTLTNKFDVPGDENAEMDA 379
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
859-1189 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 2201823352  859 ASNQREEYLLLKLFKTALEEEINSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDDKSLIINTSPV 938
Cdd:cd05127      1 ASNRREEYLLLKLFKTALREEIESKVSLPEDIVTGNPTVIKLVVNYNRGPRGQKYLRELLGPVVKEILDDDDLDLETDPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  939 DVYKSWVNQLEMQTGEASKLPYDVTTEQALTHTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRYIAKVLKSSLH 1018
Cdd:cd05127     81 DIYKAWINQEESRTGEPSKLPYDVTREQALKDPEVRKRLIEHLEKLRAITDKFLTAITESLDKMPYGMRYIAKVLKEALR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1019 EKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHPDQRRNLGCVAKVLQHAASNKLFEGESEHLSSMN 1098
Cdd:cd05127    161 EKFPDAPEEEILKIVGNLLYYRYMNPAIVAPEAFDIIDLSVGGQLSPLQRRNLGSIAKVLQQAASGKLFGGENPYLSPLN 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1099 TYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIATEPNDLLNELLEGLG 1178
Cdd:cd05127    241 PYISESHEKFKKFFLEACTVPEAEEHFNIDEYSDLTMLTKPTIYISLQEIFATHKLLLEHQDEIAPDPDDPLRELLDDLG 320
                          330
                   ....*....|.
gi 2201823352 1179 PVPDVESFLGE 1189
Cdd:cd05127    321 PAPTIESLLGS 331
RasGAP_IQGAP3 cd12207
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ...
849-1196 6.78e-174

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: 6.78e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  849 DTVIFTLYNYASNQREEYLLLKLFKTALEEEINSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDD 928
Cdd:cd12207      1 ESVIFSLYNYASNRREAYLLLQLFKTALQEEISSKVEKPQDVITGNPTVIRLLVSFYRSARGQNALRHILGPVVQDVLQD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  929 KSLIINTSPVDVYKSWVNQLEMQTGEASKLPYDVTTEQALTHTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRY 1008
Cdd:cd12207     81 KGLSIRTDPVQIYKAWINQTETQSGCRSSLPYEVSPEQALSHPEVQRRLDIAIRNLLAVTDKFLSAITSSVDKIPYGMRY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1009 IAKVLKSSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHPDQRRNLGCVAKVLQHAASNKLFE 1088
Cdd:cd12207    161 VAKVLRDSLQEKFPGASEDEVYKVVGNLLYYRFMNPAVVAPDGFDIVDCSAGGALQPEQRRMLGSVAKVLQHAAANKHFQ 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1089 GESEHLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIATEPND 1168
Cdd:cd12207    241 GDSEHLQALNQYLEETHVKFRKFILQACCVPEPEERFNVDEYSEMVAVAKPVIYITVGELINTHKLLLEHQDSIAPDHSD 320
                          330       340
                   ....*....|....*....|....*...
gi 2201823352 1169 LLNELLEGLGPVPDVESFLGEGSVDPND 1196
Cdd:cd12207    321 PLHELLEDLGEVPTVQSLIGESWADLGD 348
CH_IQGAP2 cd21275
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP2; IQ motif ...
11-166 4.50e-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: 355.48  E-value: 4.50e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   11 RPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKRWMEVCLEEELPPTTELEEGLRNGVYLAKLAKFFAPNLVSDK 90
Cdd:cd21275      1 RPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKQWIEACLNEELPPTTELEEGLRNGVYLVKLAKFFAPKLVSEK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2201823352   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 2.63e-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: 2.63e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   34 QNIAYEYLCHLEEAKRWMEVCLEEELPPTTELEEGLRNGVYLAKLAKFFAPNLVSDKKIYDVKQERYKRSGLHFRHTDNT 113
Cdd:cd21274      1 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2201823352  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 3.45e-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: 3.45e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   35 NIAYEYLCHLEEAKRWMEVCLEEELPPTTELEEGLRNGVYLAKLAKFFAPNLVSDKKIYDVKQERYKRSGLHFRHTDNTV 114
Cdd:cd21276      1 NVAYQYLCRLEEAKRWMEACLKEELPPPTELEESLRNGVYLAKLGHCFAPRVVPLKKIYDLEQMRYQATGLHFRHTDNIN 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2201823352  115 QWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGLAPQIQDLLGKVDFTEEEISNMSKEL 186
Cdd:cd21276     81 HWRNAMMHIGLPSIFHPETTDIYDKKNMPRVVYCIHALSLYLFRLGLAPQIHDLYGKVKFTEEEINNMKLEL 152
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
838-1165 4.20e-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: 265.33  E-value: 4.20e-79
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   838 QMPQNKSTKFMDTVIFTLYNYASNQREEYLLLKLFKTALEeeINSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQL 917
Cdd:smart00323    1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLS--LASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRAL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   918 LAPVVKEIMDD----KSLIINTSPVDVYKSWVNQLEMQTGEASKLPYDVTTEQALTHTEVVNK---LESSIQSLRAVTDK 990
Cdd:smart00323   79 IDPEVERTDDPntifRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEgedLETNLENLLQYVER 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   991 VLTSIFSSLNMMPYGMRYIAKVLKSSLHEKFPDAteDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMtaggQIHPDQRRN 1070
Cdd:smart00323  159 LFDAIINSSDRLPYGLRDICKQLRQAAEKRFPDA--DVIYKAVSSFVFLRFFCPAIVSPKLFNLVDE----HPDPTTRRT 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  1071 LGCVAKVLQHAASNKLFEGESEHLSSMNTYLSQTYQKFRNFFQAACDVPEPeekfNIDEYSDMVTLskpviyiSIEEIIN 1150
Cdd:smart00323  233 LTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEI----LVDKVSDSTTI-------SGRELSL 301
                           330
                    ....*....|....*
gi 2201823352  1151 THSLLLEHQDAIATE 1165
Cdd:smart00323  302 LHSLLLENGDALKRE 316
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
871-1083 1.39e-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: 235.26  E-value: 1.39e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  871 LFKTALEEEINSkVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDDKSLIINTSPVDVYKSWVNQLEM 950
Cdd:pfam00616    1 LISELIEEEIES-SDNPNDLLRGNSLVSKLLETYNRRPRGQEYLKKVLGPLVRKIIEDEDLDLESDPRKIYESLINQEEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  951 QTGEaSKLPYDVTTEQALTHTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRYIAKVLKSSLHEKFPDATEDELL 1030
Cdd:pfam00616   80 KTGR-SDLPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEIL 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2201823352 1031 KIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQIHPDQRRNLGCVAKVLQHAAS 1083
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVD----HQISPKQRRNLTLIAKVLQNLAN 207
CH_IQGAP cd21206
calponin homology (CH) domain found in the IQ motif containing GTPase activating protein ...
35-160 5.36e-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: 227.11  E-value: 5.36e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   35 NIAYEYLCHLEEAKRWMEVCLEEELPPTTELEEGLRNGVYLAKLAKFFAPNLVSDKKIYDVkqerykrsGLHFRHTDNTV 114
Cdd:cd21206      1 TIAYEYLCRLEEAKQWIEACLNEELPPTTEFEEELRNGVVLAKLANKFAPKLVPLKKIYDV--------GLQFRHTDNIN 72
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2201823352  115 QWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLG 160
Cdd:cd21206     73 HFLRALKKIGLPKIFHFETTDLYEKKNIPKVIYCLHALSLLLFKLG 118
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
718-1510 4.99e-61

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


Pssm-ID: 227586 [Multi-domain]  Cd Length: 1054  Bit Score: 229.00  E-value: 4.99e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  718 RKFAYLLDQSDLD---------FQEELEVTRLREEVVTKIRSNQQLEKDLNLMDIK----IGLLVKNRITLQDVVLHSkk 784
Cdd:COG5261    275 RRSTSVFYTISLEmisnveqafFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFA-- 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  785 lnkksknqleEMVMVDKQGIKGLSKERRKkLEAYQHLFYLLQTN-PMYL--------------AKLIFQMPQNKSTKFMd 849
Cdd:COG5261    353 ----------ERLQSNINGRKKYFPLDRR-LSLFGPLFFLLQSSiPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE- 420
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  850 tvIFTLYNYASNQREEYLLLKLFKTALEEEINSKVDqIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDDK 929
Cdd:COG5261    421 --IRKLYSLGKSNCEEHLSVSLFQMLLRTEVEATSL-VQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHE 497
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  930 SLIINTSPVDVYKSWVNQLEMQTGEASKLpyDVTTEQALTHTEVVNKL-ESSIQSLRAVTDKVLTSIFSSLNMMPYGMRY 1008
Cdd:COG5261    498 DLEVDINPLLVYRALLNKGQLSPDKDLEL--LTSNEEVSEFLAVMNAVqESSAKLLELSTERILDAVYNSLDEIGYGIRF 575
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1009 IAKVLKS-------SLHEKFPDA--------TEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQIHPDQRRnLGC 1073
Cdd:COG5261    576 VCELIRVvfeltpnRLFPSISDSrclrticfAEIDSLGLIGGFFFLRFVNEALVSPQTSMLKD----SCPSDNVRK-LAT 650
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1074 VAKVLQhaasnKLFEGES--EHLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYIsIEEIINT 1151
Cdd:COG5261    651 LSKILQ-----SVFEITSsdKFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYL-VNEIYLT 724
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1152 HSLLLEHQDAIaTEPNDLlnelleglgpVPDVESFLGEGSVDPNDPNResTLNQLAkteislsltSKYELREGEDQdLKS 1231
Cdd:COG5261    725 HEIIIEYLDNL-YDPDSL----------VDLLLQELGELCSFPQDQRD--TLNCLV---------TLPLFNRSDDP-IRD 781
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1232 LMIKTKRLIVDMIRTQPGDTLPEILETTATAQQESEHSKLVEKRAILDSKTPEKMKrSQSIFEdgqlpieqKKRKIQRNL 1311
Cdd:COG5261    782 LKQQLKRTRVYIIYVDAGTNLFEQLLRLLPSDEPATRNPLDLNPNIRDDPSVSSLK-SMSLMK--------LKIRAIELL 852
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1312 RTLEQAGLVSSATKYQEIINEIAKDIRNQRRYRHHRKAELVKLQQTLNALNSKTAFYEEQINYYNTYIKTCLDNLTRKNS 1391
Cdd:COG5261    853 DELETLGFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKS 932
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1392 RRSIKLDGKEEVKGSKKLKQA-SLKYTAARLHEKGVILEIEDLQTNqFKNVMFDITpGEEVGDFEIKAKFLG--VEMEKV 1468
Cdd:COG5261    933 KLKGFSRGVGVVRDKPKSISSgTFKYSAQQLYKRGVLVNITIPEPN-VSNIYFTFS-SDSTDNFVIEVYQPGhsVSLPEV 1010
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|..
gi 2201823352 1469 QLHFQDLLQMQYEGVAVMKMFDKAKVNVNLLIFLLNKKFYGK 1510
Cdd:COG5261   1011 SFCFDDLLKRQYNKNPVVDLGGFLTFNANKLLHLIESKFYRK 1052
RasGAP_GAPA cd05132
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...
847-1182 7.06e-58

Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to bind to small GTPases, which are yet to be identified. IQGAP proteins are integral components of cytoskeletal regulation. Results from truncated GAPAs indicated that almost the entire region of GAPA homologous to IQGAP is required for cytokinesis in Dictyostelium. More members of the IQGAP family are emerging, and evidence suggests that there are both similarities and differences in their function.


Pssm-ID: 213334  Cd Length: 352  Bit Score: 204.12  E-value: 7.06e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  847 FMDTVIFTLYNYASNQREEYLLLKLFKTALEEEInSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIM 926
Cdd:cd05132      5 LLQTVMFTLYGNQYESREEHLLLSMFQSVLTYEF-DETTEFGSLLRANTAVSRMMTTYTRRGPGQSYLKTVLADRINDLI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  927 DDKSLIINTSPVDVYKSWVNQLEMQTGEASKLPYDVTTEQALTHTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGM 1006
Cdd:cd05132     84 SLKDLNLEINPLKVYEQMINDIELDTGLPSNLPRGITPEEAAENPAVQNIIEPRLEMLEEITNSFLEAIINSLDEVPYGI 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1007 RYIAKVLKSSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQIHPDQRRNLGCVAKVLQHAASNKL 1086
Cdd:cd05132    164 RWICKQIRSLTRRKFPDASDETICSLIGGFFLLRFINPAIVSPQAYMLVD----GKPSDNTRRTLTLIAKLLQNLANKPS 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1087 FEGESeHLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYsdmVTLSKPVIYISI--EEIINTHSLLLEHQDAIAT 1164
Cdd:cd05132    240 YSKEP-YMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQY---IALSKKDLSINItlNEIYNTHSLLVKHLAELAP 315
                          330
                   ....*....|....*...
gi 2201823352 1165 EPNDLLNELLEGLGPVPD 1182
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, ...
1300-1434 3.50e-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: 168.11  E-value: 3.50e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1300 IEQKKRKIQRNLRTLEQAGLVSSATKYQEIINEIAKDIRNQRRYRHHRKAELVKLQQTLNALNSKTAFYEEQINYYNTYI 1379
Cdd:pfam03836    1 YVELKKKALENLLELESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYI 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2201823352 1380 KTCLDNLTRKNSRR--SIKLDGKEEVKGSKKLKQASLKYTAARLHEKGVILEIEDLQ 1434
Cdd:pfam03836   81 ENCLDNLQKKKKKLfsKQYFHYRKLQKRGKLPKFGSYKYSARQLYEKGVLLEIEGVP 137
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
864-1117 1.58e-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: 142.25  E-value: 1.58e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  864 EEYLLLKLFKTALEEEINSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIMDDKSL----IINTSPVD 939
Cdd:cd04519      1 EEYRLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNTKNPNTLfrgnSLATKLLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  940 VYKSWVNQlEMQTGEASKLPYDVTTEQAL----THTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRYIAKVLKS 1015
Cdd:cd04519     81 QYMKLVGQ-EYLKETLSPLIREILESKESceidTKLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILRE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1016 SLHEKFPDATeDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMtaggQIHPDQRRNLGCVAKVLQHAASNKLFEGESEHLS 1095
Cdd:cd04519    160 FLAERFPEEP-DEAYQAVSGFLFLRFICPAIVSPELFGLVPD----EPSEQARRNLTLISKVLQSLANGVEFGDKEPFMK 234
                          250       260
                   ....*....|....*....|..
gi 2201823352 1096 SMNTYLSQTYQKFRNFFQAACD 1117
Cdd:cd04519    235 PLNDFIKSNKPKLKQFLDELSS 256
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
4-211 1.85e-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: 1.85e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352    4 EELAPLQRPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKRWMEVCLEEELPpTTELEEGLRNGVYLAKLAKFFA 83
Cdd:COG5261      6 GSLNRYVENLGRPIGTPSHLKTKTSAKNRSALRAYEYLCRVSEAKIWIEEVIEEALP-ELCFEDSLRNGVFLAKLTQRFN 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   84 PNLVsdKKIYdvkqeryKRSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKLGLAP 163
Cdd:COG5261     85 PDLT--TVIF-------PADKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTP 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2201823352  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 ...
851-1165 1.37e-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: 127.02  E-value: 1.37e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  851 VIFTLYNYASNqreeylLLKLFKTALEEEINsKVDQIQDIVTGNPTVIKMVVSFNRgARGQNTLRQLLAPVVKEIMDDKS 930
Cdd:cd05392     38 SLLNLFETRNR------LLPLISWLIEDEIS-HTSRAADLFRRNSVATRLLTLYAK-SVGNKYLRKVLRPLLTEIVDNKD 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  931 --LIINTSPVDVykswvnqlemqtgeasklpydvtteqalthtevvnKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRY 1008
Cdd:cd05392    110 yfEVEKIKPDDE-----------------------------------NLEENADLLMKYAQMLLDSITDSVDQLPPSFRY 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1009 IAKVLKSSLHEKFPDATedelLKIVGNLLYYRYMNPAIVAPDGFDIIDMTaggqIHPDQRRNLGCVAKVLQHAASNKLFE 1088
Cdd:cd05392    155 ICNTIYESVSKKFPDAA----LIAVGGFLFLRFICPAIVSPESENLLDPP----PTPEARRSLILIAKVLQNIANGVLFS 226
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201823352 1089 GESEHLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNideysdmVTLSKPViyisIEEIINTHSLLLEHQDAIATE 1165
Cdd:cd05392    227 LKEPYLESLNEFLKKNSDRIQQFLSEVSTIPPTDPIFD-------ESDEEPI----TADLRYLHKFLYLHFLEIRKE 292
RasGAP_IQGAP_related cd12206
Ras-GTPase Activating Domain of proteins related to IQGAPs; RasGAP: Ras-GTPase Activating ...
845-1168 2.16e-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: 118.58  E-value: 2.16e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  845 TKFMDTVIFTLYNYASN----QREEYLLLKLFKTALEEEINsKVDQIQDIVTGNPTV-IKMVVSFNRgaRGQNTLRQ-LL 918
Cdd:cd12206      4 IEKNVYVTLPIFQKPTNgkmdSREEFLFIKFILELLKSDIE-NSNSNQDFLANSDNFwILLLVTFNN--LRERSELKsIF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  919 APVVKEIMDDKSLIINTSPVDVYKSWVNQLEMQTgeasklpydvttEQALTHTEVVNKLESSIQSLRAVTDKVLTSIFSS 998
Cdd:cd12206     81 GPLLVQYLENQEIDFESDPSVIYKSLHGRPPLSS------------EEAIEDDRVSDKFVENLTNLREAVEMVAEIIFKN 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  999 LNMMPYGMRYIAKVLKSSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtaggqihpDQRRNLGCVAKVL 1078
Cdd:cd12206    149 VDKIPVEIRYLCTKAYIAFADKFPDESEEDILRAISKILIKSYVAPILVNPENYGFVD---------NEEDNLNEKARVL 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1079 QHAASNKLFEGESE-HLSSMNTYLSQTYQKFRNFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLE 1157
Cdd:cd12206    220 LQILSMVFFLKNFDgYLKPLNQYIEEIKPSIRDLLKELLDVPEEEQEYDKLIYYDIMSTTRPCLEILLDKVIEIIQILKE 299
                          330
                   ....*....|.
gi 2201823352 1158 HQDAIAtePND 1168
Cdd:cd12206    300 NLDEFT--PDD 308
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
44-154 2.07e-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: 96.25  E-value: 2.07e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   44 LEEAKRWMEVCLEEELP-PTTELEEGLRNGVYLAKLAKFFAPNLVSdkkiydvkqERYKRSGLHFRHTDNTVQWLRAMES 122
Cdd:cd00014      1 EEELLKWINEVLGEELPvSITDLFESLRDGVLLCKLINKLSPGSIP---------KINKKPKSPFKKRENINLFLNACKK 71
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2201823352  123 IGLPKIFYPETTDVYDRKNIPRMIYCIHALSL 154
Cdd:cd00014     72 LGLPELDLFEPEDLYEKGNLKKVLGTLWALAL 103
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
867-1163 3.71e-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: 78.52  E-value: 3.71e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  867 LLLKLFKTALEeeinsKVDQIQDIVTGNPTVIK-MVVSFNrgARGQNTLRQLLAPVVKEIMddksliinTSPvDVYKSWV 945
Cdd:cd05130     59 LLWNMFSKEVE-----LADSMQTLFRGNSLASKiMTFCFK--VYGATYLQSLLEPLLRTMI--------TSS-EWVSYEV 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  946 NQLEMQTGEasklpydvtteqalthtevvnKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRYIAKVLKSSLHEKFPDat 1025
Cdd:cd05130    123 DPTRLEGNE---------------------NLEENQRNLLQLTEKFFHAIISSSDEFPPQLRSVCHCLYQVVSHRFPN-- 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1026 edELLKIVGNLLYYRYMNPAIVAPDGFDIIDmtagGQIHPDQRRNLGCVAKVLQHAASNKLFEGEsEHLSSMNTYLSQTY 1105
Cdd:cd05130    180 --SGLGAVGSAIFLRFINPAIVSPYEYGILD----REPPPRVKRGLKLMSKILQNIANHVLFTKE-AHMLPFNDFLRNHF 252
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2201823352 1106 QKFRNFFQAACDVPEPEEKFNideysdmvtlSKPVIYISIEEIINTHSLLLEHQDAIA 1163
Cdd:cd05130    253 EAGRRFFSSIASDCGAVDGPS----------SKYLSFINDANVLALHRLLWNNQEKIG 300
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
46-152 1.18e-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: 65.79  E-value: 1.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   46 EAKRWMEVCLEEELPPTTELEEGLRNGVYLAKLAKFFAPNLVsdKKIYDvkqerykrSGLHFRHTDNTVQWLRAMESIGL 125
Cdd:cd21207      9 EALDWIEAVTGEKLDDGKDYEDVLKDGVILCKLINILKPGSV--KKINT--------SKMAFKLMENIENFLTACKGYGV 78
                           90       100
                   ....*....|....*....|....*..
gi 2201823352  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 1.23e-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: 65.41  E-value: 1.23e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352    45 EEAKRWMEVCLEEELPPT-TELEEGLRNGVYLAKLAKFFAPNLVSDKKIydvkqeryKRSGLHFRHTDNTVQWLRAMESI 123
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPvTNFSSDLKDGVALCALLNSLSPGLVDKKKV--------AASLSRFKKIENINLALSFAEKL 72
                            90       100       110
                    ....*....|....*....|....*....|
gi 2201823352   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 4.85e-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: 4.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   45 EEAKRWMEVCLEEELPPTTeLEEGLRNGVYLAKLAKFFAPNLVSdkkiydvkqeRYKRSGLHFRHTDNTVQWLRAMESIG 124
Cdd:cd21210      3 QEAREWIEEVLGEKLAQGD-LLDALKDGVVLCKLANRILPADIR----------KYKESKMPFVQMENISAFLNAARKLG 71
                           90       100
                   ....*....|....*....|....*....
gi 2201823352  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 5.10e-11

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 61.15  E-value: 5.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   45 EEAKRWMEVCLEEELPPT--TELEEGLRNGVYLAKLAKFFAPNLVSDKKIydvkqerykrSGLHFRHTDNTVQWLR-AME 121
Cdd:pfam00307    5 KELLRWINSHLAEYGPGVrvTNFTTDLRDGLALCALLNKLAPGLVDKKKL----------NKSEFDKLENINLALDvAEK 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2201823352  122 SIGLPKIFyPETTDVYDRKNIpRMIYCIHALSLY 155
Cdd:pfam00307   75 KLGVPKVL-IEPEDLVEGDNK-SVLTYLASLFRR 106
SCP1 COG5199
Calponin [Cytoskeleton];
45-165 5.85e-08

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 54.16  E-value: 5.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   45 EEAKRWMEVCLEEELPPTTELEEGLRNGVYLAKLAKFFAPNLVsdkkiydvkqeRYKRSGLHFRHTDNTVQWLRAMESIG 124
Cdd:COG5199     16 KEVTLWIETVLGEKFEPPGDLLSLLKDGVRLCRILNEASPLDI-----------KYKESKMPFVQMENISSFINGLKKLR 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2201823352  125 LPKIFYPETTDVYDRKNIPRMIYCIHALSLYLFKL------GLAPQI 165
Cdd:COG5199     85 VPEYELFQTNDLFEAKDLRQVVICLYSLSRYAQKErmfsgpFLGPHL 131
RasGAP_GAP1_like cd05128
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...
867-1118 9.18e-08

Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras GTPase-activating proteins includes GAP1(m) (or RASA2), GAP1_IP4BP (or RASA3), Ca2+ -promoted Ras inactivator (CAPRI, or RASAL4), and Ras GTPase activating-like proteins (RASAL) or RASAL1. The members are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin homology domain that is associated with a Bruton's tyrosine kinase motif. While this domain structure is conserved, a small change in the function of each individual domain and the interaction between domains has a marked effect on the regulation of each protein.


Pssm-ID: 213330  Cd Length: 269  Bit Score: 55.33  E-value: 9.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  867 LLLKLFKTALEEEInSKVDQIQDIVTGNPTVIKMVVSFNRGArGQNTLRQLLAPVVKEIMDD-KSLIINtspvdvykswv 945
Cdd:cd05128     51 QIVPLLRALASREI-SKTQDPNTLFRGNSLASKCMDEFMKLV-GMQYLHETLKPVIDEIFSEkKSCEID----------- 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  946 nqlemqtgeASKLPYDVTTEQALTHtevvnklessiqsLRAVTDKVLTSIFSSLNMMPYGMRYIAKVLKSSLHEKFPDAT 1025
Cdd:cd05128    118 ---------PSKLKDGEVLETNLAN-------------LRGYVERVFKAITSSARRCPTLMCEIFSDLRESAAQRFPDNE 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1026 EDELLKIVGnLLYYRYMNPAIVAPDGFDIIDMtaggqiHPDQR--RNLGCVAKVLQH----AASNKLFEGESEHLSSM-N 1098
Cdd:cd05128    176 DVPYTAVSG-FIFLRFFAPAILNPKLFGLREE------HPDPQtaRTLTLISKTIQTlgnlGSSSSGLGVKEAYMSPLyE 248
                          250       260
                   ....*....|....*....|.
gi 2201823352 1099 TYLSQTY-QKFRNFFQAACDV 1118
Cdd:cd05128    249 RFTDEQHvDAVKKFLDRISSV 269
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
977-1157 1.13e-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: 55.67  E-value: 1.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  977 LESSIQSLRAVTDKVLTSIFSSLNMMPygmryiaKVLK---SSLHEKFPDATEDELL-KIVGNLLYYRYMNPAIVAPDGF 1052
Cdd:cd05136    132 LSRNQANLRRSVELAWCKILSSHCVFP-------RELRevfSSWRERLEERGREDIAdRLISASLFLRFLCPAILSPSLF 204
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1053 DIIdmtaggQIHPDQR--RNLGCVAKVLQHAASNKLFEGESEHLSSMNTYLSQTYQKFRNFFQaacDVPEPEEKFNIDEY 1130
Cdd:cd05136    205 NLT------QEYPSERaaRNLTLIAKVIQNLANFTRFGGKEEYMEFMNDFVEQEWPNMKQFLQ---EISSPSPSSNSSDF 275
                          170       180
                   ....*....|....*....|....*..
gi 2201823352 1131 SDMVTLSKpviyisieEIINTHSLLLE 1157
Cdd:cd05136    276 DGYIDLGR--------ELSLLHSLLVE 294
RasGAP_RASAL cd05135
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...
914-1118 1.13e-07

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: 1.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  914 LRQLLAPVVKEIMDDKSLIintsPVDVYKswvnqLEMQTGEASKLPYDVTTEQALthtevvnklESSIQSLRAVTDKVLT 993
Cdd:cd05135    101 LHEVLKPVINRIFEEKKYV----ELDPCK-----IDLNRTRRISFKGSLSEAQVR---------ESSLELLQGYLGSIID 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  994 SIFSSLNMMPYGMRYIAKVLKSSLHEKFPDATEDEL--LKIVGnLLYYRYMNPAIVAPDGFDIIDMtaggqiHPDQR--R 1069
Cdd:cd05135    163 AIVGSVDQCPPVMRVAFKQLHKRVEERFPEAEHQDVkyLAISG-FLFLRFFAPAILTPKLFQLREQ------HADPRtsR 235
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2201823352 1070 NLGCVAKVLQHAAS--NKLFEGESEHLSSMNTYLSQTYQKFRNFFQAACDV 1118
Cdd:cd05135    236 TLLLLAKAVQSIGNlgLQLGQGKEQWMAPLHPFILQSVARVKDFLDRLIDI 286
RasGAP_RAP6 cd05129
Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is ...
816-1168 1.46e-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: 55.43  E-value: 1.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  816 EAYQHLFY----------LLQTNPMYLAKLIFQMPQ--NKSTK-FMDTVIFTLYNYASNQREEYLLLKLFKTALEEEINS 882
Cdd:cd05129      1 DAYKLLGYqlshygeflrILRENPQLLAECLARGEKlsLEQTQnVIQTIVTSLYGNCIMPEDERLLLQLLRELMELQLKK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  883 KVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQ--LLAPVVKEIMDDksliINTSPVDVYKSWVNqleMQTGEASKLPY 960
Cdd:cd05129     81 SDNPRRLLRKGSCAFSRVFKLFTELLFSAKLYLTaaLHKPIMQVLVDD----EIFLETDPQKALCR---FSPAEQEKRFG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  961 DVTTEQAltHTEVVNKLESSIQSLRAVTDKVLTSIFSSLNMMPYGMRYIAKVLKSSLHEKFpDATEDELLKIVGNLLYYR 1040
Cdd:cd05129    154 EEGTPEQ--QRKLQQYRAEFLSRLVALVNKFISSLRQSVYCFPQSLRWIVRQLRKILTRSG-DDEEAEARALCTDLLFTN 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352 1041 YMNPAIVAPDGFDIIDmtaGGQIHPDQRRNLGCVAKVLQHAASNKLFEGESEhlssmntyLSQTYQKFRN----FFQAAC 1116
Cdd:cd05129    231 FICPAIVNPEQYGIIS---DAPISEVARHNLMQVAQILQVLALTEFESPDPR--------LKELLSKFDKdcvsAFLDVV 299
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2201823352 1117 DVPEPEEKFNIDEySDMVTLSKPVIYISIEEiINTHSLLLEHQDAIATEPND 1168
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 1.99e-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: 1.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352   45 EEAKRWMEVCLEEELPPTT---ELEEGLRNGVYLAKLAKFFAPNLVSdkKIYDVKQERYKRSGLHFRHTDNTVQWLRAME 121
Cdd:cd21203      3 YEAAEWIQNVLGVLVLPDPseeEFRLCLRDGVVLCKLLNKLQPGAVP--KVVESPDDPDGAAGSAFQYFENVRNFLVAIE 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2201823352  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 ...
982-1123 1.50e-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: 1.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  982 QSLRAVTDKVLTSIFSSLNMMPYGMRYIAKVLKSSLHEKFPDATEDElLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGg 1061
Cdd:cd05391    133 EHLLNILSELVEKIFMAAEILPPTLRYIYGCLQKSVQQKWPTNTTVR-TRVVSGFVFLRLICPAILNPRMFNIISETPS- 210
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2201823352 1062 qihPDQRRNLGCVAKVLQHAASNKLFEGESEHLSSMNTYLSQTYQKFRNFFQAACDVPEPEE 1123
Cdd:cd05391    211 ---PTAARTLTLVAKSLQNLANLVEFGAKEPYMEGVNPFIKKNKERMIMFLDELGNVPELPD 269
RasGAP_CLA2_BUD2 cd05137
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ...
977-1119 2.59e-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: 48.33  E-value: 2.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  977 LESSIQSLRAVTDKVLTSIFSSLNMMPYGMRYIAKVLKSSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIId 1056
Cdd:cd05137    155 LEENWENLISLTEEIWNSIYITSNDCPPELRKILKHIRAKVEDRYGDFLRTVTLNSVSGFLFLRFFCPAILNPKLFGLL- 233
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201823352 1057 mtaggQIHPD--QRRNLGCVAKVLQHAASNKLFEGESEHLSSMNTYLSQTYQKFRNFFQAACDVP 1119
Cdd:cd05137    234 -----KDHPRprAQRTLTLIAKVLQNLANLTTFGQKEPWMEPMNEFLTTHREELKDYIDKITGIK 293
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
655-674 1.58e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 37.30  E-value: 1.58e-03
                           10        20
                   ....*....|....*....|
gi 2201823352  655 AAIVKIQSWVKMWLARRAYR 674
Cdd:pfam00612    2 KAAIKIQAAWRGYLARKRYK 21
RasGAP_RASA4 cd05395
Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also ...
910-1079 1.85e-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: 1.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  910 GQNTLRQLLAPVVKEIMDDKSLI-INTSPVDVYKSWVNQLEMQTGEAsklpydvtteqalthtEVvnkLESSIQSLRAVT 988
Cdd:cd05395     97 GMQYLHSVLGPTINRVFEEKKYVeLDPSKVEIKDVGCSGLHRIQTES----------------EV---IEQSAQLLQSYL 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201823352  989 DKVLTSIFSSLNMMPYGMRYIAKVLKSSLHEKFPDATEDELLKI-VGNLLYYRYMNPAIVAPDGFDIIDMtaggqiHPDQ 1067
Cdd:cd05395    158 GELLSAISKSVKYCPAVIRATFRQLFKRVQERFPENQHQNVKFIaVTSFLCLRFFSPAIMSPKLFHLREK------HADA 231
                          170
                   ....*....|....
gi 2201823352 1068 R--RNLGCVAKVLQ 1079
Cdd:cd05395    232 RtsRTLLLLAKAVQ 245
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
623-643 2.99e-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: 2.99e-03
                            10        20
                    ....*....|....*....|.
gi 2201823352   623 QEPSAIKIQAFWKGFKQRKSY 643
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRY 22
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
655-674 3.67e-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: 3.67e-03
                            10        20
                    ....*....|....*....|
gi 2201823352   655 AAIVKIQSWVKMWLARRAYR 674
Cdd:smart00015    4 RAAIIIQAAWRGYLARKRYK 23
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
655-678 4.10e-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: 4.10e-03
                           10        20
                   ....*....|....*....|....
gi 2201823352  655 AAIVKIQSWVKMWLARRAYRKRLQ 678
Cdd:cd21759     46 EALIKIQKTVRGYLARKKHRPRIK 69
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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