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Conserved domains on  [gi|1370451976|ref|XP_024309044|]
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ras GTPase-activating-like protein IQGAP3 isoform X5 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RasGAP_IQGAP3 cd12207
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ...
860-1209 0e+00

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  Cd Length: 350  Bit Score: 663.06  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  860 EAVIFSLYNYASSRREAYLLLQLFKTALQEEIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLED 939
Cdd:cd12207      1 ESVIFSLYNYASNRREAYLLLQLFKTALQEEISSKVEKPQDVITGNPTVIRLLVSFYRSARGQNALRHILGPVVQDVLQD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  940 KVLSVHTDPVHLYKNWINQTEAQTGQRSHLPYDVTPEQALSHPEVQRRLDIALRNLLAMTDKFLLAITSSVDQIPYGMRY 1019
Cdd:cd12207     81 KGLSIRTDPVQIYKAWINQTETQSGCRSSLPYEVSPEQALSHPEVQRRLDIAIRNLLAVTDKFLSAITSSVDKIPYGMRY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1020 VAKVLKATLAEKFPDATDSEVYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGGALAAPQRHALGAVAQLLQHAAAGKAFS 1099
Cdd:cd12207    161 VAKVLRDSLQEKFPGASEDEVYKVVGNLLYYRFMNPAVVAPDGFDIVDCSAGGALQPEQRRMLGSVAKVLQHAAANKHFQ 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1100 GQSQHLRVLNDYLEETHLKFRKFIHRACQVPEPEERFAVDEYSDMVAVAKPMVYITVGELVNTHRLLLEHQDCIAPDHQD 1179
Cdd:cd12207    241 GDSEHLQALNQYLEETHVKFRKFILQACCVPEPEERFNVDEYSEMVAVAKPVIYITVGELINTHKLLLEHQDSIAPDHSD 320
                          330       340       350
                   ....*....|....*....|....*....|
gi 1370451976 1180 PLHELLEDLGELPTIPDLIGESIAADGHTD 1209
Cdd:cd12207    321 PLHELLEDLGEVPTVQSLIGESWADLGDDP 350
IQG1 super family cl34962
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
734-1504 1.44e-58

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


The actual alignment was detected with superfamily member COG5261:

Pssm-ID: 227586 [Multi-domain]  Cd Length: 1054  Bit Score: 221.30  E-value: 1.44e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  734 LNQSQQDFLAEAELLKLQEEVVRKIRSNQQLEQDLNIMDIK----IGLLVKNRITLQEVVSHCKKLtkrnkeqlsdmmvL 809
Cdd:COG5261    290 SNVEQAFFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFAERL-------------Q 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  810 DKQKGLKSLSKEKRqKLEAYQHLFYLLQT-QPIYL--------------AKLIFQMPQNKTTKFMeavIFSLYNYASSRR 874
Cdd:COG5261    357 SNINGRKKYFPLDR-RLSLFGPLFFLLQSsIPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE---IRKLYSLGKSNC 432
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  875 EAYLLLQLFktalQEEIKSKVEQPQDVVT---GNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDKVLSVHTDPVHL 951
Cdd:COG5261    433 EEHLSVSLF----QMLLRTEVEATSLVQSllrGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHEDLEVDINPLLV 508
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  952 YKNWINQTeaQTGQRSHLPYDVTPEQALSHPEVQRRLDIALRNLLAM-TDKFLLAITSSVDQIPYGMRYVAKVLKA---- 1026
Cdd:COG5261    509 YRALLNKG--QLSPDKDLELLTSNEEVSEFLAVMNAVQESSAKLLELsTERILDAVYNSLDEIGYGIRFVCELIRVvfel 586
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1027 ---TLAEKFPDATD--------SEVYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGGAlaapQRhALGAVAQLLQHAAAG 1095
Cdd:COG5261    587 tpnRLFPSISDSRClrticfaeIDSLGLIGGFFFLRFVNEALVSPQTSMLKDSCPSDN----VR-KLATLSKILQSVFEI 661
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1096 KAFSGqsqHLRVLNDYLEETHLKFRKFIHRACQVPEPEERFAVDEYSDMVAVAKPMVYiTVGELVNTHRLLLEH-QDCIA 1174
Cdd:COG5261    662 TSSDK---FDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEY-LVNEIYLTHEIIIEYlDNLYD 737
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1175 PDhqDPLHELLEDLGELPTIPDligesiaaDGHTDLSKLevsltltnkFEGLEADADDSNTRSLLLSTKQLLADIIQFHP 1254
Cdd:COG5261    738 PD--SLVDLLLQELGELCSFPQ--------DQRDTLNCL---------VTLPLFNRSDDPIRDLKQQLKRTRVYIIYVDA 798
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1255 GDTLKEILsLSASREQEAAHKQLMSRrqactaqtpEPLRRHrSLTAHSLLPL--AEKQRRVLRNLRRLEALGLVSARNGY 1332
Cdd:COG5261    799 GTNLFEQL-LRLLPSDEPATRNPLDL---------NPNIRD-DPSVSSLKSMslMKLKIRAIELLDELETLGFVSRENRY 867
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1333 QGLVDELAKDIRNQHRHRHRRKAELVKLQATLQGLSTKTTFYEEQGDYYSQYIRACLDHLAPDSKSSGKGKKQ------- 1405
Cdd:COG5261    868 QPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKSKLKGFSRGvgvvrdk 947
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1406 ------PSLHYTAAQLLEKGVLVEIEDlPASHFRNVIFDITpGDEAGKF--EVNAKFLGVDMERFQLHYQDLLQLQYEGV 1477
Cdd:COG5261    948 pksissGTFKYSAQQLYKRGVLVNITI-PEPNVSNIYFTFS-SDSTDNFviEVYQPGHSVSLPEVSFCFDDLLKRQYNKN 1025
                          810       820
                   ....*....|....*....|....*..
gi 1370451976 1478 AVMKLFNKAKVNVNLLIFLLNKKFLRK 1504
Cdd:COG5261   1026 PVVDLGGFLTFNANKLLHLIESKFYRK 1052
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
1-45 3.45e-25

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 cd21276:

Pssm-ID: 444660  Cd Length: 152  Bit Score: 103.13  E-value: 3.45e-25
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1370451976    1 MPRVVYCIHALSLFLFRLGLAPQIHDLYGKVKFTAEELSNMASEL 45
Cdd:cd21276    108 MPRVVYCIHALSLYLFRLGLAPQIHDLYGKVKFTEEEINNMKLEL 152
COG5022 super family cl34868
Myosin heavy chain [General function prediction only];
607-830 6.81e-07

Myosin heavy chain [General function prediction only];


The actual alignment was detected with superfamily member COG5022:

Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 54.31  E-value: 6.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  607 VIQLQARLRGFLVRQKFAEHSHFLR------------------TWLPAVIKIQAHWRGYRQRKiylewlqYFKANLDAII 668
Cdd:COG5022    748 ATRIQRAIRGRYLRRRYLQALKRIKkiqviqhgfrlrrlvdyeLKWRLFIKLQPLLSLLGSRK-------EYRSYLACII 820
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  669 KIQAwarmwAARRQYLRRLHYFQK-NVNSIVKIQAFFRARKAQDDYRIL------------VHAPHPPLSV----VRRFA 731
Cdd:COG5022    821 KLQK-----TIKREKKLRETEEVEfSLKAEVLIQKFGRSLKAKKRFSLLkketiylqsaqrVELAERQLQElkidVKSIS 895
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  732 HLLNQSQQDflaEAELLKL--------QEEVVRKIRSNQQLEQDLNIMDIKIGL---LVKNRItLQEVVSHCKKLtKRNK 800
Cdd:COG5022    896 SLKLVNLEL---ESEIIELkkslssdlIENLEFKTELIARLKKLLNNIDLEEGPsieYVKLPE-LNKLHEVESKL-KETS 970
                          250       260       270
                   ....*....|....*....|....*....|
gi 1370451976  801 EQLSDMmvLDKQKGLKSLSKEKRQKLEAYQ 830
Cdd:COG5022    971 EEYEDL--LKKSTILVREGNKANSELKNFK 998
 
Name Accession Description Interval E-value
RasGAP_IQGAP3 cd12207
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ...
860-1209 0e+00

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  Cd Length: 350  Bit Score: 663.06  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  860 EAVIFSLYNYASSRREAYLLLQLFKTALQEEIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLED 939
Cdd:cd12207      1 ESVIFSLYNYASNRREAYLLLQLFKTALQEEISSKVEKPQDVITGNPTVIRLLVSFYRSARGQNALRHILGPVVQDVLQD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  940 KVLSVHTDPVHLYKNWINQTEAQTGQRSHLPYDVTPEQALSHPEVQRRLDIALRNLLAMTDKFLLAITSSVDQIPYGMRY 1019
Cdd:cd12207     81 KGLSIRTDPVQIYKAWINQTETQSGCRSSLPYEVSPEQALSHPEVQRRLDIAIRNLLAVTDKFLSAITSSVDKIPYGMRY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1020 VAKVLKATLAEKFPDATDSEVYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGGALAAPQRHALGAVAQLLQHAAAGKAFS 1099
Cdd:cd12207    161 VAKVLRDSLQEKFPGASEDEVYKVVGNLLYYRFMNPAVVAPDGFDIVDCSAGGALQPEQRRMLGSVAKVLQHAAANKHFQ 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1100 GQSQHLRVLNDYLEETHLKFRKFIHRACQVPEPEERFAVDEYSDMVAVAKPMVYITVGELVNTHRLLLEHQDCIAPDHQD 1179
Cdd:cd12207    241 GDSEHLQALNQYLEETHVKFRKFILQACCVPEPEERFNVDEYSEMVAVAKPVIYITVGELINTHKLLLEHQDSIAPDHSD 320
                          330       340       350
                   ....*....|....*....|....*....|
gi 1370451976 1180 PLHELLEDLGELPTIPDLIGESIAADGHTD 1209
Cdd:cd12207    321 PLHELLEDLGEVPTVQSLIGESWADLGDDP 350
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
882-1093 6.99e-67

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: 395491  Cd Length: 206  Bit Score: 224.47  E-value: 6.99e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  882 LFKTALQEEIKSkVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDKVLSVHTDPVHLYKNWINQTEA 961
Cdd:pfam00616    1 LISELIEEEIES-SDNPNDLLRGNSLVSKLLETYNRRPRGQEYLKKVLGPLVRKIIEDEDLDLESDPRKIYESLINQEEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  962 QTGqRSHLPYDVTPEQALSHPEVQRRLDIALRNLLAMTDKFLLAITSSVDQIPYGMRYVAKVLKATLAEKFPDATDSEVY 1041
Cdd:pfam00616   80 KTG-RSDLPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEDEIL 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1370451976 1042 KVVGNLLYYRFLNPAVVAPDAFDIVAMAAGGAlaapQRHALGAVAQLLQHAA 1093
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVDHQISPK----QRRNLTLIAKVLQNLA 206
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
734-1504 1.44e-58

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


Pssm-ID: 227586 [Multi-domain]  Cd Length: 1054  Bit Score: 221.30  E-value: 1.44e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  734 LNQSQQDFLAEAELLKLQEEVVRKIRSNQQLEQDLNIMDIK----IGLLVKNRITLQEVVSHCKKLtkrnkeqlsdmmvL 809
Cdd:COG5261    290 SNVEQAFFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFAERL-------------Q 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  810 DKQKGLKSLSKEKRqKLEAYQHLFYLLQT-QPIYL--------------AKLIFQMPQNKTTKFMeavIFSLYNYASSRR 874
Cdd:COG5261    357 SNINGRKKYFPLDR-RLSLFGPLFFLLQSsIPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE---IRKLYSLGKSNC 432
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  875 EAYLLLQLFktalQEEIKSKVEQPQDVVT---GNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDKVLSVHTDPVHL 951
Cdd:COG5261    433 EEHLSVSLF----QMLLRTEVEATSLVQSllrGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHEDLEVDINPLLV 508
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  952 YKNWINQTeaQTGQRSHLPYDVTPEQALSHPEVQRRLDIALRNLLAM-TDKFLLAITSSVDQIPYGMRYVAKVLKA---- 1026
Cdd:COG5261    509 YRALLNKG--QLSPDKDLELLTSNEEVSEFLAVMNAVQESSAKLLELsTERILDAVYNSLDEIGYGIRFVCELIRVvfel 586
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1027 ---TLAEKFPDATD--------SEVYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGGAlaapQRhALGAVAQLLQHAAAG 1095
Cdd:COG5261    587 tpnRLFPSISDSRClrticfaeIDSLGLIGGFFFLRFVNEALVSPQTSMLKDSCPSDN----VR-KLATLSKILQSVFEI 661
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1096 KAFSGqsqHLRVLNDYLEETHLKFRKFIHRACQVPEPEERFAVDEYSDMVAVAKPMVYiTVGELVNTHRLLLEH-QDCIA 1174
Cdd:COG5261    662 TSSDK---FDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEY-LVNEIYLTHEIIIEYlDNLYD 737
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1175 PDhqDPLHELLEDLGELPTIPDligesiaaDGHTDLSKLevsltltnkFEGLEADADDSNTRSLLLSTKQLLADIIQFHP 1254
Cdd:COG5261    738 PD--SLVDLLLQELGELCSFPQ--------DQRDTLNCL---------VTLPLFNRSDDPIRDLKQQLKRTRVYIIYVDA 798
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1255 GDTLKEILsLSASREQEAAHKQLMSRrqactaqtpEPLRRHrSLTAHSLLPL--AEKQRRVLRNLRRLEALGLVSARNGY 1332
Cdd:COG5261    799 GTNLFEQL-LRLLPSDEPATRNPLDL---------NPNIRD-DPSVSSLKSMslMKLKIRAIELLDELETLGFVSRENRY 867
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1333 QGLVDELAKDIRNQHRHRHRRKAELVKLQATLQGLSTKTTFYEEQGDYYSQYIRACLDHLAPDSKSSGKGKKQ------- 1405
Cdd:COG5261    868 QPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKSKLKGFSRGvgvvrdk 947
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1406 ------PSLHYTAAQLLEKGVLVEIEDlPASHFRNVIFDITpGDEAGKF--EVNAKFLGVDMERFQLHYQDLLQLQYEGV 1477
Cdd:COG5261    948 pksissGTFKYSAQQLYKRGVLVNITI-PEPNVSNIYFTFS-SDSTDNFviEVYQPGHSVSLPEVSFCFDDLLKRQYNKN 1025
                          810       820
                   ....*....|....*....|....*..
gi 1370451976 1478 AVMKLFNKAKVNVNLLIFLLNKKFLRK 1504
Cdd:COG5261   1026 PVVDLGGFLTFNANKLLHLIESKFYRK 1052
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
849-1202 6.61e-55

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: 195.22  E-value: 6.61e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976   849 QMPQNKTTKFMEAVIFSLYNYASSRREAYLLLQLFKTALQeeIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEI 928
Cdd:smart00323    1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLS--LASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRAL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976   929 LGKVIQDVLEDKVL----SVHTDPVHLYKNWINQTEAQTGQRSHLPYDVTPEQALSHPEVQRRLDIA---LRNLLAMTDK 1001
Cdd:smart00323   79 IDPEVERTDDPNTIfrgnSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEGEDLetnLENLLQYVER 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  1002 FLLAITSSVDQIPYGMRYVAKVLKATLAEKFPDATdsEVYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGGAlaapQRHA 1081
Cdd:smart00323  159 LFDAIINSSDRLPYGLRDICKQLRQAAEKRFPDAD--VIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPT----TRRT 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  1082 LGAVAQLLQHAAAGKAFSGQSQHLRVLNDYLEETHLKFRKFIHRACQVPEPeerfAVDEYSDMVAVakpmvyiTVGELVN 1161
Cdd:smart00323  233 LTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEI----LVDKVSDSTTI-------SGRELSL 301
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|...
gi 1370451976  1162 THRLLLEHQDCIAP--DHQDPLHELLEDLGELPTIPDLIGESI 1202
Cdd:smart00323  302 LHSLLLENGDALKRelNNEDPLGKLLFKLRYFGLTTHELTYGK 344
RasGAP_C pfam03836
RasGAP C-terminus; This domain can be found in the C-terminus of the IQGAP family members, ...
1321-1428 8.99e-31

RasGAP C-terminus; This domain can be found in the C-terminus of the IQGAP family members, including human IQGAP1/2/3, S. cerevisiae Iqg1 and S. pombe Rng2. Some members function in cytoskeletal remodelling. Human IQGAP1 is a scaffolding protein that can assemble multi-protein complexes involved in cell-cell interaction, cell adherence, and movement via actin/tubulin-based cytoskeletal reorganization. IQGAP1 is also a regulator of the MAPK and Wnt/beta-catenin signaling pathways.Iqg1 and Rng2 are required for actomyosin ring construction during cytokinesis.


Pssm-ID: 427540  Cd Length: 137  Bit Score: 118.42  E-value: 8.99e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1321 EALGLVSARNGYQGLVDELAKDIRNQHRHRHRRKAELVKLQATLQGLSTKTTFYEEQGDYYSQYIRACLDHLAP------ 1394
Cdd:pfam03836   16 ESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYIENCLENLQKkkkklf 95
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1370451976 1395 --------DSKSSGKGKKQPSLHYTAAQLLEKGVLVEIEDLP 1428
Cdd:pfam03836   96 skqkfhyrKLQKRGKLPKFGSYKYSARQLYEKGVLLEIEGVP 137
CH_IQGAP3 cd21276
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP3; IQ motif ...
1-45 3.45e-25

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  Cd Length: 152  Bit Score: 103.13  E-value: 3.45e-25
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1370451976    1 MPRVVYCIHALSLFLFRLGLAPQIHDLYGKVKFTAEELSNMASEL 45
Cdd:cd21276    108 MPRVVYCIHALSLYLFRLGLAPQIHDLYGKVKFTEEEINNMKLEL 152
COG5022 COG5022
Myosin heavy chain [General function prediction only];
607-830 6.81e-07

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 54.31  E-value: 6.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  607 VIQLQARLRGFLVRQKFAEHSHFLR------------------TWLPAVIKIQAHWRGYRQRKiylewlqYFKANLDAII 668
Cdd:COG5022    748 ATRIQRAIRGRYLRRRYLQALKRIKkiqviqhgfrlrrlvdyeLKWRLFIKLQPLLSLLGSRK-------EYRSYLACII 820
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  669 KIQAwarmwAARRQYLRRLHYFQK-NVNSIVKIQAFFRARKAQDDYRIL------------VHAPHPPLSV----VRRFA 731
Cdd:COG5022    821 KLQK-----TIKREKKLRETEEVEfSLKAEVLIQKFGRSLKAKKRFSLLkketiylqsaqrVELAERQLQElkidVKSIS 895
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  732 HLLNQSQQDflaEAELLKL--------QEEVVRKIRSNQQLEQDLNIMDIKIGL---LVKNRItLQEVVSHCKKLtKRNK 800
Cdd:COG5022    896 SLKLVNLEL---ESEIIELkkslssdlIENLEFKTELIARLKKLLNNIDLEEGPsieYVKLPE-LNKLHEVESKL-KETS 970
                          250       260       270
                   ....*....|....*....|....*....|
gi 1370451976  801 EQLSDMmvLDKQKGLKSLSKEKRQKLEAYQ 830
Cdd:COG5022    971 EEYEDL--LKKSTILVREGNKANSELKNFK 998
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
636-653 3.23e-04

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 39.23  E-value: 3.23e-04
                            10
                    ....*....|....*...
gi 1370451976   636 AVIKIQAHWRGYRQRKIY 653
Cdd:smart00015    5 AAIIIQAAWRGYLARKRY 22
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
636-653 1.58e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 425778  Cd Length: 21  Bit Score: 36.91  E-value: 1.58e-03
                           10
                   ....*....|....*...
gi 1370451976  636 AVIKIQAHWRGYRQRKIY 653
Cdd:pfam00612    3 AAIKIQAAWRGYLARKRY 20
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
666-806 2.24e-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: 40.18  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  666 AIIKIQAWARMWAARRQY------LRRLHYFQKNVNSIVKIqaffrarkaqddyrilvhaphpplsvvrrfAHLLNQSQQ 739
Cdd:cd21759     47 ALIKIQKTVRGYLARKKHrprikgLRKIRALEKQLKEMEEI------------------------------ASQLKKDKD 96
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370451976  740 DFLAEAELLKLQ-EEVVRKIRSNqqleqdlnimdikigllvkNRITLQEVVSHCKKLTKRNKEQLSDM 806
Cdd:cd21759     97 KWTKQVKELKKEiDALIKKIKTN-------------------DMITRKEIDKLYNALVKKVDKQLAEL 145
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
1-70 9.12e-03

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: 40.64  E-value: 9.12e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976    1 MPRVVYCIHALSLFLFRLGLAPQIHDLYGKVkFTAEELSNMASELAkyglQLPAFSKIGGILANELSVDE 70
Cdd:COG5261    134 IPKVIYCIHALISMLSWPGKTPLINSSGQIS-FTKEDIAACKKAWP----RIPDFKSLGTNINTAASPEE 198
 
Name Accession Description Interval E-value
RasGAP_IQGAP3 cd12207
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ...
860-1209 0e+00

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  Cd Length: 350  Bit Score: 663.06  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  860 EAVIFSLYNYASSRREAYLLLQLFKTALQEEIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLED 939
Cdd:cd12207      1 ESVIFSLYNYASNRREAYLLLQLFKTALQEEISSKVEKPQDVITGNPTVIRLLVSFYRSARGQNALRHILGPVVQDVLQD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  940 KVLSVHTDPVHLYKNWINQTEAQTGQRSHLPYDVTPEQALSHPEVQRRLDIALRNLLAMTDKFLLAITSSVDQIPYGMRY 1019
Cdd:cd12207     81 KGLSIRTDPVQIYKAWINQTETQSGCRSSLPYEVSPEQALSHPEVQRRLDIAIRNLLAVTDKFLSAITSSVDKIPYGMRY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1020 VAKVLKATLAEKFPDATDSEVYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGGALAAPQRHALGAVAQLLQHAAAGKAFS 1099
Cdd:cd12207    161 VAKVLRDSLQEKFPGASEDEVYKVVGNLLYYRFMNPAVVAPDGFDIVDCSAGGALQPEQRRMLGSVAKVLQHAAANKHFQ 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1100 GQSQHLRVLNDYLEETHLKFRKFIHRACQVPEPEERFAVDEYSDMVAVAKPMVYITVGELVNTHRLLLEHQDCIAPDHQD 1179
Cdd:cd12207    241 GDSEHLQALNQYLEETHVKFRKFILQACCVPEPEERFNVDEYSEMVAVAKPVIYITVGELINTHKLLLEHQDSIAPDHSD 320
                          330       340       350
                   ....*....|....*....|....*....|
gi 1370451976 1180 PLHELLEDLGELPTIPDLIGESIAADGHTD 1209
Cdd:cd12207    321 PLHELLEDLGEVPTVQSLIGESWADLGDDP 350
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
870-1200 2.75e-176

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  Cd Length: 331  Bit Score: 529.08  E-value: 2.75e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  870 ASSRREAYLLLQLFKTALQEEIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDKVLSVHTDPV 949
Cdd:cd05127      1 ASNRREEYLLLKLFKTALREEIESKVSLPEDIVTGNPTVIKLVVNYNRGPRGQKYLRELLGPVVKEILDDDDLDLETDPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  950 HLYKNWINQTEAQTGQRSHLPYDVTPEQALSHPEVQRRLDIALRNLLAMTDKFLLAITSSVDQIPYGMRYVAKVLKATLA 1029
Cdd:cd05127     81 DIYKAWINQEESRTGEPSKLPYDVTREQALKDPEVRKRLIEHLEKLRAITDKFLTAITESLDKMPYGMRYIAKVLKEALR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1030 EKFPDATDSEVYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGGALAAPQRHALGAVAQLLQHAAAGKAFSGQSQHLRVLN 1109
Cdd:cd05127    161 EKFPDAPEEEILKIVGNLLYYRYMNPAIVAPEAFDIIDLSVGGQLSPLQRRNLGSIAKVLQQAASGKLFGGENPYLSPLN 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1110 DYLEETHLKFRKFIHRACQVPEPEERFAVDEYSDMVAVAKPMVYITVGELVNTHRLLLEHQDCIAPDHQDPLHELLEDLG 1189
Cdd:cd05127    241 PYISESHEKFKKFFLEACTVPEAEEHFNIDEYSDLTMLTKPTIYISLQEIFATHKLLLEHQDEIAPDPDDPLRELLDDLG 320
                          330
                   ....*....|.
gi 1370451976 1190 ELPTIPDLIGE 1200
Cdd:cd05127    321 PAPTIESLLGS 331
RasGAP_IQGAP1 cd05133
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...
860-1224 2.50e-168

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: 510.36  E-value: 2.50e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  860 EAVIFSLYNYASSRREAYLLLQLFKTALQEEIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLED 939
Cdd:cd05133      1 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  940 KVLSVHTDPVHLYKNWINQTEAQTGQRSHLPYDVTPEQALSHPEVQRRLDIALRNLLAMTDKFLLAITSSVDQIPYGMRY 1019
Cdd:cd05133     81 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQAMSHEEVRTRLDASIKNMRMVTDKFLSAIISSVDKIPYGMRF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1020 VAKVLKATLAEKFPDATDSEVYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGGALAAPQRHALGAVAQLLQHAAAGKAFS 1099
Cdd:cd05133    161 IAKVLKDTLHEKFPDAGEDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1100 GQSQHLRVLNDYLEETHLKFRKFIHRACQVPEPEERFAVDEYSDMVAVAKPMVYITVGELVNTHRLLLEHQDCIAPDHQD 1179
Cdd:cd05133    241 GDNAHLSPINEYLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 320
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1370451976 1180 PLHELLEDLGELPTIPDLIGESIAADGHTD---LSKLEVSLTLTNKFE 1224
Cdd:cd05133    321 PIHELLDDLGEVPTIESLIGENPGPPGDPNretLAKTEVSLTLTNKFD 368
RasGAP_IQGAP2 cd05131
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...
860-1200 7.71e-166

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: 502.99  E-value: 7.71e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  860 EAVIFSLYNYASSRREAYLLLQLFKTALQEEIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLED 939
Cdd:cd05131      1 DTVIFTLYNYASNQREEYLLLKLFETALEEEIKSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  940 KVLSVHTDPVHLYKNWINQTEAQTGQRSHLPYDVTPEQALSHPEVQRRLDIALRNLLAMTDKFLLAITSSVDQIPYGMRY 1019
Cdd:cd05131     81 KSLIINTNPVEVYKAWVNQLETATGEASKLPYDVTTEQALTHPEVVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1020 VAKVLKATLAEKFPDATDSEVYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGGALAAPQRHALGAVAQLLQHAAAGKAFS 1099
Cdd:cd05131    161 IAKVLKNSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHSEQRRNLGSVAKVLQHAASNKLFE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1100 GQSQHLRVLNDYLEETHLKFRKFIHRACQVPEPEERFAVDEYSDMVAVAKPMVYITVGELVNTHRLLLEHQDCIAPDHQD 1179
Cdd:cd05131    241 GENAHLSSMNSYLSQTYQKFRKFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIAPDQND 320
                          330       340
                   ....*....|....*....|.
gi 1370451976 1180 PLHELLEDLGELPTIPDLIGE 1200
Cdd:cd05131    321 LLHELLKDLGEVPDVESFLGE 341
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
882-1093 6.99e-67

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: 395491  Cd Length: 206  Bit Score: 224.47  E-value: 6.99e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  882 LFKTALQEEIKSkVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDKVLSVHTDPVHLYKNWINQTEA 961
Cdd:pfam00616    1 LISELIEEEIES-SDNPNDLLRGNSLVSKLLETYNRRPRGQEYLKKVLGPLVRKIIEDEDLDLESDPRKIYESLINQEEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  962 QTGqRSHLPYDVTPEQALSHPEVQRRLDIALRNLLAMTDKFLLAITSSVDQIPYGMRYVAKVLKATLAEKFPDATDSEVY 1041
Cdd:pfam00616   80 KTG-RSDLPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEDEIL 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1370451976 1042 KVVGNLLYYRFLNPAVVAPDAFDIVAMAAGGAlaapQRHALGAVAQLLQHAA 1093
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVDHQISPK----QRRNLTLIAKVLQNLA 206
RasGAP_GAPA cd05132
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...
858-1192 1.29e-63

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: 220.69  E-value: 1.29e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  858 FMEAVIFSLYNYASSRREAYLLLQLFKTALQEEIKSKVEqPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVL 937
Cdd:cd05132      5 LLQTVMFTLYGNQYESREEHLLLSMFQSVLTYEFDETTE-FGSLLRANTAVSRMMTTYTRRGPGQSYLKTVLADRINDLI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  938 EDKVLSVHTDPVHLYKNWINQTEAQTGQRSHLPYDVTPEQALSHPEVQRRLDIALRNLLAMTDKFLLAITSSVDQIPYGM 1017
Cdd:cd05132     84 SLKDLNLEINPLKVYEQMINDIELDTGLPSNLPRGITPEEAAENPAVQNIIEPRLEMLEEITNSFLEAIINSLDEVPYGI 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1018 RYVAKVLKATLAEKFPDATDSEVYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGGALaapqRHALGAVAQLLQHAAAGKA 1097
Cdd:cd05132    164 RWICKQIRSLTRRKFPDASDETICSLIGGFFLLRFINPAIVSPQAYMLVDGKPSDNT----RRTLTLIAKLLQNLANKPS 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1098 FSGQSqHLRVLNDYLEETHLKFRKFIHRACQVPEPEERFAVDEYsdmVAVAKP--MVYITVGELVNTHRLLLEHQDCIAP 1175
Cdd:cd05132    240 YSKEP-YMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQY---IALSKKdlSINITLNEIYNTHSLLVKHLAELAP 315
                          330
                   ....*....|....*..
gi 1370451976 1176 DHQDPLHELLEDLGELP 1192
Cdd:cd05132    316 DHNDHLRLILQELGPAP 332
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
734-1504 1.44e-58

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


Pssm-ID: 227586 [Multi-domain]  Cd Length: 1054  Bit Score: 221.30  E-value: 1.44e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  734 LNQSQQDFLAEAELLKLQEEVVRKIRSNQQLEQDLNIMDIK----IGLLVKNRITLQEVVSHCKKLtkrnkeqlsdmmvL 809
Cdd:COG5261    290 SNVEQAFFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFAERL-------------Q 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  810 DKQKGLKSLSKEKRqKLEAYQHLFYLLQT-QPIYL--------------AKLIFQMPQNKTTKFMeavIFSLYNYASSRR 874
Cdd:COG5261    357 SNINGRKKYFPLDR-RLSLFGPLFFLLQSsIPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE---IRKLYSLGKSNC 432
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  875 EAYLLLQLFktalQEEIKSKVEQPQDVVT---GNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDKVLSVHTDPVHL 951
Cdd:COG5261    433 EEHLSVSLF----QMLLRTEVEATSLVQSllrGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHEDLEVDINPLLV 508
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  952 YKNWINQTeaQTGQRSHLPYDVTPEQALSHPEVQRRLDIALRNLLAM-TDKFLLAITSSVDQIPYGMRYVAKVLKA---- 1026
Cdd:COG5261    509 YRALLNKG--QLSPDKDLELLTSNEEVSEFLAVMNAVQESSAKLLELsTERILDAVYNSLDEIGYGIRFVCELIRVvfel 586
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1027 ---TLAEKFPDATD--------SEVYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGGAlaapQRhALGAVAQLLQHAAAG 1095
Cdd:COG5261    587 tpnRLFPSISDSRClrticfaeIDSLGLIGGFFFLRFVNEALVSPQTSMLKDSCPSDN----VR-KLATLSKILQSVFEI 661
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1096 KAFSGqsqHLRVLNDYLEETHLKFRKFIHRACQVPEPEERFAVDEYSDMVAVAKPMVYiTVGELVNTHRLLLEH-QDCIA 1174
Cdd:COG5261    662 TSSDK---FDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEY-LVNEIYLTHEIIIEYlDNLYD 737
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1175 PDhqDPLHELLEDLGELPTIPDligesiaaDGHTDLSKLevsltltnkFEGLEADADDSNTRSLLLSTKQLLADIIQFHP 1254
Cdd:COG5261    738 PD--SLVDLLLQELGELCSFPQ--------DQRDTLNCL---------VTLPLFNRSDDPIRDLKQQLKRTRVYIIYVDA 798
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1255 GDTLKEILsLSASREQEAAHKQLMSRrqactaqtpEPLRRHrSLTAHSLLPL--AEKQRRVLRNLRRLEALGLVSARNGY 1332
Cdd:COG5261    799 GTNLFEQL-LRLLPSDEPATRNPLDL---------NPNIRD-DPSVSSLKSMslMKLKIRAIELLDELETLGFVSRENRY 867
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1333 QGLVDELAKDIRNQHRHRHRRKAELVKLQATLQGLSTKTTFYEEQGDYYSQYIRACLDHLAPDSKSSGKGKKQ------- 1405
Cdd:COG5261    868 QPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKSKLKGFSRGvgvvrdk 947
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1406 ------PSLHYTAAQLLEKGVLVEIEDlPASHFRNVIFDITpGDEAGKF--EVNAKFLGVDMERFQLHYQDLLQLQYEGV 1477
Cdd:COG5261    948 pksissGTFKYSAQQLYKRGVLVNITI-PEPNVSNIYFTFS-SDSTDNFviEVYQPGHSVSLPEVSFCFDDLLKRQYNKN 1025
                          810       820
                   ....*....|....*....|....*..
gi 1370451976 1478 AVMKLFNKAKVNVNLLIFLLNKKFLRK 1504
Cdd:COG5261   1026 PVVDLGGFLTFNANKLLHLIESKFYRK 1052
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
849-1202 6.61e-55

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: 195.22  E-value: 6.61e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976   849 QMPQNKTTKFMEAVIFSLYNYASSRREAYLLLQLFKTALQeeIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEI 928
Cdd:smart00323    1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLS--LASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRAL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976   929 LGKVIQDVLEDKVL----SVHTDPVHLYKNWINQTEAQTGQRSHLPYDVTPEQALSHPEVQRRLDIA---LRNLLAMTDK 1001
Cdd:smart00323   79 IDPEVERTDDPNTIfrgnSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEGEDLetnLENLLQYVER 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  1002 FLLAITSSVDQIPYGMRYVAKVLKATLAEKFPDATdsEVYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGGAlaapQRHA 1081
Cdd:smart00323  159 LFDAIINSSDRLPYGLRDICKQLRQAAEKRFPDAD--VIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPT----TRRT 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  1082 LGAVAQLLQHAAAGKAFSGQSQHLRVLNDYLEETHLKFRKFIHRACQVPEPeerfAVDEYSDMVAVakpmvyiTVGELVN 1161
Cdd:smart00323  233 LTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEI----LVDKVSDSTTI-------SGRELSL 301
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|...
gi 1370451976  1162 THRLLLEHQDCIAP--DHQDPLHELLEDLGELPTIPDLIGESI 1202
Cdd:smart00323  302 LHSLLLENGDALKRelNNEDPLGKLLFKLRYFGLTTHELTYGK 344
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
875-1128 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 1370451976  875 EAYLLLQLFKTALQEEIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDKVL----SVHTDPVH 950
Cdd:cd04519      1 EEYRLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNTKNPNTLfrgnSLATKLLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  951 LYKNWINQtEAQTGQRSHLPYDVTPEQAL----SHPEVQRRLDIALRNLLAMTDKFLLAITSSVDQIPYGMRYVAKVLKA 1026
Cdd:cd04519     81 QYMKLVGQ-EYLKETLSPLIREILESKESceidTKLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILRE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1027 TLAEKFPDATDsEVYKVVGNLLYYRFLNPAVVAPDAFDIVamaaGGALAAPQRHALGAVAQLLQHAAAGKAFSGQSQHLR 1106
Cdd:cd04519    160 FLAERFPEEPD-EAYQAVSGFLFLRFICPAIVSPELFGLV----PDEPSEQARRNLTLISKVLQSLANGVEFGDKEPFMK 234
                          250       260
                   ....*....|....*....|..
gi 1370451976 1107 VLNDYLEETHLKFRKFIHRACQ 1128
Cdd:cd04519    235 PLNDFIKSNKPKLKQFLDELSS 256
RasGAP_IQGAP_related cd12206
Ras-GTPase Activating Domain of proteins related to IQGAPs; RasGAP: Ras-GTPase Activating ...
868-1202 1.08e-34

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: 137.07  E-value: 1.08e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  868 NYASSRREAYLLLQLFKTALQEEIKsKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDKVLSVHTD 947
Cdd:cd12206     20 NGKMDSREEFLFIKFILELLKSDIE-NSNSNQDFLANSDNFWILLLVTFNNLRERSELKSIFGPLLVQYLENQEIDFESD 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  948 PVHLYKNWINqteaqtgqrsHLPYDvtPEQALSHPEVQRRLDIALRNLLAMTDKFLLAITSSVDQIPYGMRYVAKVLKAT 1027
Cdd:cd12206     99 PSVIYKSLHG----------RPPLS--SEEAIEDDRVSDKFVENLTNLREAVEMVAEIIFKNVDKIPVEIRYLCTKAYIA 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1028 LAEKFPDATDSEVYKVVGNLLYYRFLNPAVVAPDAFDIVAMaaggalaapQRHALGAVAQLLQHAAAGKAFSGQSQ-HLR 1106
Cdd:cd12206    167 FADKFPDESEEDILRAISKILIKSYVAPILVNPENYGFVDN---------EEDNLNEKARVLLQILSMVFFLKNFDgYLK 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1107 VLNDYLEETHLKFRKFIHRACQVPEPEERFAVDEYSDMVAVAKPMVYITVGELVNTHRLLLEHQDCIAPDhqDPLHELLE 1186
Cdd:cd12206    238 PLNQYIEEIKPSIRDLLKELLDVPEEEQEYDKLIYYDIMSTTRPCLEILLDKVIEIIQILKENLDEFTPD--DQLVQLLE 315
                          330
                   ....*....|....*.
gi 1370451976 1187 DLGELPTIPDLIGESI 1202
Cdd:cd12206    316 KIVDLSSSSNDKRSGR 331
RasGAP_C pfam03836
RasGAP C-terminus; This domain can be found in the C-terminus of the IQGAP family members, ...
1321-1428 8.99e-31

RasGAP C-terminus; This domain can be found in the C-terminus of the IQGAP family members, including human IQGAP1/2/3, S. cerevisiae Iqg1 and S. pombe Rng2. Some members function in cytoskeletal remodelling. Human IQGAP1 is a scaffolding protein that can assemble multi-protein complexes involved in cell-cell interaction, cell adherence, and movement via actin/tubulin-based cytoskeletal reorganization. IQGAP1 is also a regulator of the MAPK and Wnt/beta-catenin signaling pathways.Iqg1 and Rng2 are required for actomyosin ring construction during cytokinesis.


Pssm-ID: 427540  Cd Length: 137  Bit Score: 118.42  E-value: 8.99e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1321 EALGLVSARNGYQGLVDELAKDIRNQHRHRHRRKAELVKLQATLQGLSTKTTFYEEQGDYYSQYIRACLDHLAP------ 1394
Cdd:pfam03836   16 ESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYIENCLENLQKkkkklf 95
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1370451976 1395 --------DSKSSGKGKKQPSLHYTAAQLLEKGVLVEIEDLP 1428
Cdd:pfam03836   96 skqkfhyrKLQKRGKLPKFGSYKYSARQLYEKGVLLEIEGVP 137
CH_IQGAP3 cd21276
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP3; IQ motif ...
1-45 3.45e-25

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  Cd Length: 152  Bit Score: 103.13  E-value: 3.45e-25
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1370451976    1 MPRVVYCIHALSLFLFRLGLAPQIHDLYGKVKFTAEELSNMASEL 45
Cdd:cd21276    108 MPRVVYCIHALSLYLFRLGLAPQIHDLYGKVKFTEEEINNMKLEL 152
RasGAP_Neurofibromin_like cd05392
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...
859-1202 9.64e-25

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: 106.60  E-value: 9.64e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  859 MEAVIFSLYNYASsrreayLLLQLFKTALQEEIkSKVEQPQDVVTGNPTVVRLVVRFYRNgRGQSALQEILGKVIQDVLE 938
Cdd:cd05392     35 LAQSLLNLFETRN------RLLPLISWLIEDEI-SHTSRAADLFRRNSVATRLLTLYAKS-VGNKYLRKVLRPLLTEIVD 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  939 DKVlsvhtdpvhlyknwinqteaqtgqrshlPYDVTPEQALSHPevqrrLDIALRNLLAMTDKFLLAITSSVDQIPYGMR 1018
Cdd:cd05392    107 NKD----------------------------YFEVEKIKPDDEN-----LEENADLLMKYAQMLLDSITDSVDQLPPSFR 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1019 YVAKVLKATLAEKFPDATDSevykVVGNLLYYRFLNPAVVAPDAFDIVamaaGGALAAPQRHALGAVAQLLQHAAAGKAF 1098
Cdd:cd05392    154 YICNTIYESVSKKFPDAALI----AVGGFLFLRFICPAIVSPESENLL----DPPPTPEARRSLILIAKVLQNIANGVLF 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1099 SGQSQHLRVLNDYLEETHLKFRKFIHRACQVPEPEERFAVDEYSDMVAvakpmvyitvgELVNTHRLLLEHQDCIAPDHQ 1178
Cdd:cd05392    226 SLKEPYLESLNEFLKKNSDRIQQFLSEVSTIPPTDPIFDESDEEPITA-----------DLRYLHKFLYLHFLEIRKEVL 294
                          330       340
                   ....*....|....*....|....
gi 1370451976 1179 DPLhELLEDLGELPTIPDLIGESI 1202
Cdd:cd05392    295 KGS-SSQGSDKELVETFKLIDEIL 317
CH_IQGAP1 cd21274
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif ...
1-45 5.23e-18

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  Cd Length: 154  Bit Score: 82.35  E-value: 5.23e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1370451976    1 MPRVVYCIHALSLFLFRLGLAPQIHDLYGKVKFTAEELSNMASEL 45
Cdd:cd21274    109 MPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTEL 153
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
993-1174 7.38e-14

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: 74.67  E-value: 7.38e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  993 RNLLAMTDKFLLAITSSVDQIPYGMRYVAKVLKATLAEKFPdatdSEVYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGG 1072
Cdd:cd05130    138 RNLLQLTEKFFHAIISSSDEFPPQLRSVCHCLYQVVSHRFP----NSGLGAVGSAIFLRFINPAIVSPYEYGILDREPPP 213
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1073 ALaapqRHALGAVAQLLQHAAAGKAFSGQsQHLRVLNDYLEETHLKFRKFIhraCQVpepeerfAVDEYSDMVAVAKPMV 1152
Cdd:cd05130    214 RV----KRGLKLMSKILQNIANHVLFTKE-AHMLPFNDFLRNHFEAGRRFF---SSI-------ASDCGAVDGPSSKYLS 278
                          170       180
                   ....*....|....*....|..
gi 1370451976 1153 YITVGELVNTHRLLLEHQDCIA 1174
Cdd:cd05130    279 FINDANVLALHRLLWNNQEKIG 300
CH_IQGAP2 cd21275
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP2; IQ motif ...
1-25 1.80e-09

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  Cd Length: 156  Bit Score: 58.11  E-value: 1.80e-09
                           10        20
                   ....*....|....*....|....*
gi 1370451976    1 MPRVVYCIHALSLFLFRLGLAPQIH 25
Cdd:cd21275    132 MPRVIYCIHALSLYLFKLGIAPQIQ 156
COG5022 COG5022
Myosin heavy chain [General function prediction only];
607-830 6.81e-07

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 54.31  E-value: 6.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  607 VIQLQARLRGFLVRQKFAEHSHFLR------------------TWLPAVIKIQAHWRGYRQRKiylewlqYFKANLDAII 668
Cdd:COG5022    748 ATRIQRAIRGRYLRRRYLQALKRIKkiqviqhgfrlrrlvdyeLKWRLFIKLQPLLSLLGSRK-------EYRSYLACII 820
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  669 KIQAwarmwAARRQYLRRLHYFQK-NVNSIVKIQAFFRARKAQDDYRIL------------VHAPHPPLSV----VRRFA 731
Cdd:COG5022    821 KLQK-----TIKREKKLRETEEVEfSLKAEVLIQKFGRSLKAKKRFSLLkketiylqsaqrVELAERQLQElkidVKSIS 895
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  732 HLLNQSQQDflaEAELLKL--------QEEVVRKIRSNQQLEQDLNIMDIKIGL---LVKNRItLQEVVSHCKKLtKRNK 800
Cdd:COG5022    896 SLKLVNLEL---ESEIIELkkslssdlIENLEFKTELIARLKKLLNNIDLEEGPsieYVKLPE-LNKLHEVESKL-KETS 970
                          250       260       270
                   ....*....|....*....|....*....|
gi 1370451976  801 EQLSDMmvLDKQKGLKSLSKEKRQKLEAYQ 830
Cdd:COG5022    971 EEYEDL--LKKSTILVREGNKANSELKNFK 998
RasGAP_GAP1_like cd05128
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...
878-1065 1.30e-06

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: 51.48  E-value: 1.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  878 LLLQLFKTALQEEIkSKVEQPQDVVTGNpTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDKVlSVHTDPVHLyknwin 957
Cdd:cd05128     51 QIVPLLRALASREI-SKTQDPNTLFRGN-SLASKCMDEFMKLVGMQYLHETLKPVIDEIFSEKK-SCEIDPSKL------ 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  958 qteaqtgqrshlpydvtpeqalSHPEVqrrLDIALRNLLAMTDKFLLAITSSVDQIPYGMRYVAKVLKATLAEKFPDatD 1037
Cdd:cd05128    122 ----------------------KDGEV---LETNLANLRGYVERVFKAITSSARRCPTLMCEIFSDLRESAAQRFPD--N 174
                          170       180
                   ....*....|....*....|....*....
gi 1370451976 1038 SEV-YKVVGNLLYYRFLNPAVVAPDAFDI 1065
Cdd:cd05128    175 EDVpYTAVSGFIFLRFFAPAILNPKLFGL 203
RasGAP_RASAL cd05135
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...
921-1065 2.34e-06

Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like protein (RASAL) or RASAL1 is a member of the GAP1 family, and a Ca2+ sensor responding in-phase to repetitive Ca2+ signals by associating with the plasma membrane and deactivating Ras. It contains a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. RASAL, like Ca2+ -promoted Ras inactivator (CAPRI, or RASAL4), is a cytosolic protein that undergoes a rapid translocation to the plasma membrane in response to receptor-mediated elevation in the concentration of intracellular free Ca2+, a translocation that activates its ability to function as a RasGAP. However, unlike RASAL4, RASAL undergoes an oscillatory translocation to the plasma membrane that occurs in synchrony with repetitive Ca2+ spikes.


Pssm-ID: 213337  Cd Length: 287  Bit Score: 50.97  E-value: 2.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  921 GQSALQEILGKVIQDVLEDKVLsVHTDPVHLyknwinqtEAQTGQRSHLPYDVTPEQALSHpevqrRLDIALRNLLAMTD 1000
Cdd:cd05135     97 GMPYLHEVLKPVINRIFEEKKY-VELDPCKI--------DLNRTRRISFKGSLSEAQVRES-----SLELLQGYLGSIID 162
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451976 1001 kfllAITSSVDQIPYGMRYVAKVLKATLAEKFPDATDSEV-YKVVGNLLYYRFLNPAVVAPDAFDI 1065
Cdd:cd05135    163 ----AIVGSVDQCPPVMRVAFKQLHKRVEERFPEAEHQDVkYLAISGFLFLRFFAPAILTPKLFQL 224
CH_IQGAP cd21206
calponin homology (CH) domain found in the IQ motif containing GTPase activating protein ...
1-19 4.03e-06

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  Cd Length: 118  Bit Score: 47.22  E-value: 4.03e-06
                           10
                   ....*....|....*....
gi 1370451976    1 MPRVVYCIHALSLFLFRLG 19
Cdd:cd21206    100 IPKVIYCLHALSLLLFKLG 118
RasGAP_p120GAP cd05391
Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ...
992-1198 4.06e-05

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: 47.48  E-value: 4.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  992 LRNLLAMTDKFLLAITSSVDQIPYGMRYVAKVLKATLAEKFPDATDSEVyKVVGNLLYYRFLNPAVVAPDAFDIVAMAAG 1071
Cdd:cd05391    132 LEHLLNILSELVEKIFMAAEILPPTLRYIYGCLQKSVQQKWPTNTTVRT-RVVSGFVFLRLICPAILNPRMFNIISETPS 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1072 GALAapqrHALGAVAQLLQHAAAGKAFSGQSQHLRVLNDYLEETHLKFRKFIHRACQVPEPE---ERFAVDEYSDMVAVa 1148
Cdd:cd05391    211 PTAA----RTLTLVAKSLQNLANLVEFGAKEPYMEGVNPFIKKNKERMIMFLDELGNVPELPdttEHSRTDLSRDLAAL- 285
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1370451976 1149 kpmvyitvgelvnthrllleHQDCIapDHQDPLHEL---LEDLGELPTIPDLI 1198
Cdd:cd05391    286 --------------------HEICV--AHSDELRTLsneRGALKKLLAVTELL 316
RasGAP_RAP6 cd05129
Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is ...
827-1090 8.47e-05

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: 46.57  E-value: 8.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  827 EAYQHLFY----------LLQTQPIYLAKLIF---QMPQNKTTKFMEAVIFSLYNYASSRREAYLLLQLFKTALQEEIKS 893
Cdd:cd05129      1 DAYKLLGYqlshygeflrILRENPQLLAECLArgeKLSLEQTQNVIQTIVTSLYGNCIMPEDERLLLQLLRELMELQLKK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  894 KVEQPQDVVTGNPTVVRLVVRF-YRNGRGQSALQEILGKVIQDVLEDKVLSVHTDPVHLYknwinQTEAQTGQRSHLPYD 972
Cdd:cd05129     81 SDNPRRLLRKGSCAFSRVFKLFtELLFSAKLYLTAALHKPIMQVLVDDEIFLETDPQKAL-----CRFSPAEQEKRFGEE 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  973 VTPEQalsHPEVQRRLDIALRNLLAMTDKFLLAITSSVDQIPYGMRYVAKVLKATLAEKFpDATDSEVYKVVGNLLYYRF 1052
Cdd:cd05129    156 GTPEQ---QRKLQQYRAEFLSRLVALVNKFISSLRQSVYCFPQSLRWIVRQLRKILTRSG-DDEEAEARALCTDLLFTNF 231
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1370451976 1053 LNPAVVAPDAFDIVAMAAGGALAapqRHALGAVAQLLQ 1090
Cdd:cd05129    232 ICPAIVNPEQYGIISDAPISEVA---RHNLMQVAQILQ 266
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
636-653 3.23e-04

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 39.23  E-value: 3.23e-04
                            10
                    ....*....|....*...
gi 1370451976   636 AVIKIQAHWRGYRQRKIY 653
Cdd:smart00015    5 AAIIIQAAWRGYLARKRY 22
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
921-1201 5.70e-04

Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras GTPase-activating proteins includes DAB2IP, nGAP, and Syn GAP. Disabled 2 interactive protein, (DAB2IP; also known as ASK-interacting protein 1 (AIP1)), is a member of the GTPase-activating proteins, down-regulates Ras-mediated signal pathways, and mediates TNF-induced activation of ASK1-JNK signaling pathways. The mechanism by which TNF signaling is coupled to DAB2IP is not known.


Pssm-ID: 213338 [Multi-domain]  Cd Length: 324  Bit Score: 43.73  E-value: 5.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  921 GQSALQEILGKVIQDVLEdkvlsvhtdpvhlyknwinqteaqtgqrSHLPYDVTPEQALSHPEVQRRLdialRNLLAMTD 1000
Cdd:cd05136     97 GQKYLQETLGEFIRALYE----------------------------SEEDCEVDPSKCPPSASLSRNQ----ANLRRSVE 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1001 KFLLAITSSVDQIPYGMRYVAKVLKATLAE-KFPDATDsevyKVVGNLLYYRFLNPAVVAPDAFDIVamaAGGALAAPQR 1079
Cdd:cd05136    145 LAWCKILSSHCVFPRELREVFSSWRERLEErGREDIAD----RLISASLFLRFLCPAILSPSLFNLT---QEYPSERAAR 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976 1080 hALGAVAQLLQHAAAGKAFSGQSQHLRVLNDYLEETHLKFRKFIHracQVPEPEERFAVDEYSDmvavakpmvYITVG-E 1158
Cdd:cd05136    218 -NLTLIAKVIQNLANFTRFGGKEEYMEFMNDFVEQEWPNMKQFLQ---EISSPSPSSNSSDFDG---------YIDLGrE 284
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1370451976 1159 LVNTHRLLLEhqdCIAPDHQDPLHElledLGELPTIPDLIGES 1201
Cdd:cd05136    285 LSLLHSLLVE---IISKLNQTTLDK----LGPLPRILNDITEA 320
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
636-653 1.58e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 425778  Cd Length: 21  Bit Score: 36.91  E-value: 1.58e-03
                           10
                   ....*....|....*...
gi 1370451976  636 AVIKIQAHWRGYRQRKIY 653
Cdd:pfam00612    3 AAIKIQAAWRGYLARKRY 20
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
666-806 2.24e-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: 40.18  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976  666 AIIKIQAWARMWAARRQY------LRRLHYFQKNVNSIVKIqaffrarkaqddyrilvhaphpplsvvrrfAHLLNQSQQ 739
Cdd:cd21759     47 ALIKIQKTVRGYLARKKHrprikgLRKIRALEKQLKEMEEI------------------------------ASQLKKDKD 96
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370451976  740 DFLAEAELLKLQ-EEVVRKIRSNqqleqdlnimdikigllvkNRITLQEVVSHCKKLTKRNKEQLSDM 806
Cdd:cd21759     97 KWTKQVKELKKEiDALIKKIKTN-------------------DMITRKEIDKLYNALVKKVDKQLAEL 145
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
1-70 9.12e-03

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: 40.64  E-value: 9.12e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451976    1 MPRVVYCIHALSLFLFRLGLAPQIHDLYGKVkFTAEELSNMASELAkyglQLPAFSKIGGILANELSVDE 70
Cdd:COG5261    134 IPKVIYCIHALISMLSWPGKTPLINSSGQIS-FTKEDIAACKKAWP----RIPDFKSLGTNINTAASPEE 198
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
665-683 9.43e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 425778  Cd Length: 21  Bit Score: 34.99  E-value: 9.43e-03
                           10
                   ....*....|....*....
gi 1370451976  665 DAIIKIQAWARMWAARRQY 683
Cdd:pfam00612    2 KAAIKIQAAWRGYLARKRY 20
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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