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Conserved domains on  [gi|118344446|ref|NP_001028656|]
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ras GTPase-activating-like protein IQGAP3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RasGAP super family cl02569
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
988-1337 0e+00

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.


The actual alignment was detected with superfamily member cd12207:

Pssm-ID: 470620 [Multi-domain]  Cd Length: 350  Bit Score: 623.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  988 EGVIFSLYNYASNRREAYLLLQLFRTALQEEIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLED 1067
Cdd:cd12207     1 ESVIFSLYNYASNRREAYLLLQLFKTALQEEISSKVEKPQDVITGNPTVIRLLVSFYRSARGQNALRHILGPVVQDVLQD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1068 RSVSIHTDPVHIYKSWINQEEAQTGQRSHLPYDVTPEQALSHSEVQRRLDISLRSLLTLTEKFFVAISSSVDHIPYGMRY 1147
Cdd:cd12207    81 KGLSIRTDPVQIYKAWINQTETQSGCRSSLPYEVSPEQALSHPEVQRRLDIAIRNLLAVTDKFLSAITSSVDKIPYGMRY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1148 MAKVLKTTLEKKFPNATERDIYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGSTLAAPQRHALGAVAQLLQHAAAGQIFS 1227
Cdd:cd12207   161 VAKVLRDSLQEKFPGASEDEVYKVVGNLLYYRFMNPAVVAPDGFDIVDCSAGGALQPEQRRMLGSVAKVLQHAAANKHFQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1228 GESRHLRVLNDYLEDLHLKFRKFICRACRVPEPEERFAIDEYSDMVAVAKPMVYITVGELIGTHRLLLEHQDQLAPGHQD 1307
Cdd:cd12207   241 GDSEHLQALNQYLEETHVKFRKFILQACCVPEPEERFNVDEYSEMVAVAKPVIYITVGELINTHKLLLEHQDSIAPDHSD 320
                         330       340       350
                  ....*....|....*....|....*....|
gi 118344446 1308 PLHQLLEDLGEPPTISDLIGDNIATDGHVD 1337
Cdd:cd12207   321 PLHELLEDLGEVPTVQSLIGESWADLGDDP 350
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
28-179 7.94e-107

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: 469584 [Multi-domain]  Cd Length: 152  Bit Score: 336.18  E-value: 7.94e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   28 NVAYQYLCRLEEAKRWMEVCLKEELPSPVELEESLRNGVLLAKLGHCFAPSVVPLKKIYDVEQLRYQATGLHFRHTDNIN 107
Cdd:cd21276     1 NVAYQYLCRLEEAKRWMEACLKEELPPPTELEESLRNGVYLAKLGHCFAPRVVPLKKIYDLEQMRYQATGLHFRHTDNIN 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118344446  108 FWLSAVAHIGLPSIFLPETTDIYDKKNMPRVIYCIHALSLFLFRLGLAPQIHDLYGKVKFTAEELGNIASEL 179
Cdd:cd21276    81 HWRNAMMHIGLPSIFHPETTDIYDKKNMPRVVYCIHALSLYLFRLGLAPQIHDLYGKVKFTEEEINNMKLEL 152
IQG1 super family cl34962
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
862-1632 1.14e-52

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: 202.81  E-value: 1.14e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  862 LNQSQEDFSAESELLKLQEEVVRKIRSNQQLEQDLNLMDIK----IGLLVKNRITLQEVVSHCKKLtkknkeqlsdmmiL 937
Cdd:COG5261   290 SNVEQAFFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFAERL-------------Q 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  938 DKQKGLKSLSREKRqKLEAYQHLFYLLQT-QPIYL--------------AKLIFQMPQNKTTKFMegvIFSLYNYASNRR 1002
Cdd:COG5261   357 SNINGRKKYFPLDR-RLSLFGPLFFLLQSsIPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE---IRKLYSLGKSNC 432
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1003 EAYLLLQLFrtalQEEIKSKVEQPQDVVT---GNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDRSVSIHTDPVHI 1079
Cdd:COG5261   433 EEHLSVSLF----QMLLRTEVEATSLVQSllrGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHEDLEVDINPLLV 508
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1080 YKSWINQeeAQTGQRSHLPYDVTPEQALSHSEVQRRLDISLRSLLTL-TEKFFVAISSSVDHIPYGMRYMAKVLKTTLE- 1157
Cdd:COG5261   509 YRALLNK--GQLSPDKDLELLTSNEEVSEFLAVMNAVQESSAKLLELsTERILDAVYNSLDEIGYGIRFVCELIRVVFEl 586
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1158 ---KKFPN-----------ATERDIYKVVGNLLYYRFLNPAVVAPDAFdivaMAAGSTLAAPQRhALGAVAQLLQhaaag 1223
Cdd:COG5261   587 tpnRLFPSisdsrclrticFAEIDSLGLIGGFFFLRFVNEALVSPQTS----MLKDSCPSDNVR-KLATLSKILQ----- 656
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1224 QIFSGES--RHLRVLNDYLEDLHLKFRKFICRACRVPEPEERFAIDEYSDMVAVAKPMVYiTVGELIGTHRLLLEHQDQL 1301
Cdd:COG5261   657 SVFEITSsdKFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEY-LVNEIYLTHEIIIEYLDNL 735
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1302 --APGHQDPLHQLLEDLGEPPTisdligdniatDGHVDLSRLEvSLTLTNKFEgletdadhNSNQSLLLSTKQMLADLIQ 1379
Cdd:COG5261   736 ydPDSLVDLLLQELGELCSFPQ-----------DQRDTLNCLV-TLPLFNRSD--------DPIRDLKQQLKRTRVYIIY 795
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1380 FHPGESLEEILTSSAPrEHEEAHRRLMcwrqacdtqKPEPLRRHhSLMAHSLLSLS--EKQQRVLRNLRRLQGLGLVRAS 1457
Cdd:COG5261   796 VDAGTNLFEQLLRLLP-SDEPATRNPL---------DLNPNIRD-DPSVSSLKSMSlmKLKIRAIELLDELETLGFVSRE 864
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1458 DCYQGLVDELAKDICNQRRHRQRRKAEMLRLRTTLQGLDAKTIFYEEQGDYYNQYIQACLDHLAPKPKSSGKGKKQ---- 1533
Cdd:COG5261   865 NRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKSKLKGFSRGvgvv 944
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1534 ---------PSLHYTAAQLLEKGVLVEIEDlPVSHFRNVIFDITpGDEAGRFFVNAKFLG--VDMEKFQLHYQDLLQLQY 1602
Cdd:COG5261   945 rdkpksissGTFKYSAQQLYKRGVLVNITI-PEPNVSNIYFTFS-SDSTDNFVIEVYQPGhsVSLPEVSFCFDDLLKRQY 1022
                         810       820       830
                  ....*....|....*....|....*....|
gi 118344446 1603 EGVAVMKLFNKAKVNVNLLIFLLNKKFLRK 1632
Cdd:COG5261  1023 NKNPVVDLGGFLTFNANKLLHLIESKFYRK 1052
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
764-782 6.27e-05

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


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 41.16  E-value: 6.27e-05
                            10
                    ....*....|....*....
gi 118344446    764 AVIKIQAHWRGYRQRKAYQ 782
Cdd:smart00015    5 AAIIIQAAWRGYLARKRYK 23
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
671-696 6.99e-03

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


:

Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 35.58  E-value: 6.99e-03
                          10        20
                  ....*....|....*....|....*.
gi 118344446  671 WVQHDMKDGTAYYLHLQTFQGTWEHP 696
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQWEDP 29
 
Name Accession Description Interval E-value
RasGAP_IQGAP3 cd12207
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ...
988-1337 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 [Multi-domain]  Cd Length: 350  Bit Score: 623.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  988 EGVIFSLYNYASNRREAYLLLQLFRTALQEEIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLED 1067
Cdd:cd12207     1 ESVIFSLYNYASNRREAYLLLQLFKTALQEEISSKVEKPQDVITGNPTVIRLLVSFYRSARGQNALRHILGPVVQDVLQD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1068 RSVSIHTDPVHIYKSWINQEEAQTGQRSHLPYDVTPEQALSHSEVQRRLDISLRSLLTLTEKFFVAISSSVDHIPYGMRY 1147
Cdd:cd12207    81 KGLSIRTDPVQIYKAWINQTETQSGCRSSLPYEVSPEQALSHPEVQRRLDIAIRNLLAVTDKFLSAITSSVDKIPYGMRY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1148 MAKVLKTTLEKKFPNATERDIYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGSTLAAPQRHALGAVAQLLQHAAAGQIFS 1227
Cdd:cd12207   161 VAKVLRDSLQEKFPGASEDEVYKVVGNLLYYRFMNPAVVAPDGFDIVDCSAGGALQPEQRRMLGSVAKVLQHAAANKHFQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1228 GESRHLRVLNDYLEDLHLKFRKFICRACRVPEPEERFAIDEYSDMVAVAKPMVYITVGELIGTHRLLLEHQDQLAPGHQD 1307
Cdd:cd12207   241 GDSEHLQALNQYLEETHVKFRKFILQACCVPEPEERFNVDEYSEMVAVAKPVIYITVGELINTHKLLLEHQDSIAPDHSD 320
                         330       340       350
                  ....*....|....*....|....*....|
gi 118344446 1308 PLHQLLEDLGEPPTISDLIGDNIATDGHVD 1337
Cdd:cd12207   321 PLHELLEDLGEVPTVQSLIGESWADLGDDP 350
CH_IQGAP3 cd21276
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP3; IQ motif ...
28-179 7.94e-107

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: 336.18  E-value: 7.94e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   28 NVAYQYLCRLEEAKRWMEVCLKEELPSPVELEESLRNGVLLAKLGHCFAPSVVPLKKIYDVEQLRYQATGLHFRHTDNIN 107
Cdd:cd21276     1 NVAYQYLCRLEEAKRWMEACLKEELPPPTELEESLRNGVYLAKLGHCFAPRVVPLKKIYDLEQMRYQATGLHFRHTDNIN 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118344446  108 FWLSAVAHIGLPSIFLPETTDIYDKKNMPRVIYCIHALSLFLFRLGLAPQIHDLYGKVKFTAEELGNIASEL 179
Cdd:cd21276    81 HWRNAMMHIGLPSIFHPETTDIYDKKNMPRVVYCIHALSLYLFRLGLAPQIHDLYGKVKFTEEEINNMKLEL 152
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
1010-1221 3.99e-66

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: 222.55  E-value: 3.99e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  1010 LFRTALQEEIKSkVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDRSVSIHTDPVHIYKSWINQEEA 1089
Cdd:pfam00616    1 LISELIEEEIES-SDNPNDLLRGNSLVSKLLETYNRRPRGQEYLKKVLGPLVRKIIEDEDLDLESDPRKIYESLINQEEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  1090 QTGqRSHLPYDVTPEQALSHSEVQRRLDISLRSLLTLTEKFFVAISSSVDHIPYGMRYMAKVLKTTLEKKFPNATERDIY 1169
Cdd:pfam00616   80 KTG-RSDLPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEIL 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 118344446  1170 KVVGNLLYYRFLNPAVVAPDAFDIVAmaagSTLAAPQRHALGAVAQLLQHAA 1221
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVD----HQISPKQRRNLTLIAKVLQNLA 206
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
977-1328 2.68e-53

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: 190.98  E-value: 2.68e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446    977 QMPQNKTTKFMEGVIFSLYNYASNRREAYLLLQLFRTALQeeIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEI 1056
Cdd:smart00323    1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLS--LASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRAL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   1057 LGKVIQDVLED----RSVSIHTDPVHIYKSWINQEEAQTGQRSHLPYDVTPEQALSHSEV---QRRLDISLRSLLTLTEK 1129
Cdd:smart00323   79 IDPEVERTDDPntifRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAkleGEDLETNLENLLQYVER 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   1130 FFVAISSSVDHIPYGMRYMAKVLKTTLEKKFPNATERdiYKVVGNLLYYRFLNPAVVAPDAFDIVamaaGSTLAAPQRHA 1209
Cdd:smart00323  159 LFDAIINSSDRLPYGLRDICKQLRQAAEKRFPDADVI--YKAVSSFVFLRFFCPAIVSPKLFNLV----DEHPDPTTRRT 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   1210 LGAVAQLLQHAAAGQIFSGESRHLRVLNDYLEDLHLKFRKFICRACRVPEPeerfAIDEYSDMVAVakpmvyiTVGELIG 1289
Cdd:smart00323  233 LTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEI----LVDKVSDSTTI-------SGRELSL 301
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|.
gi 118344446   1290 THRLLLEHQDQLAP--GHQDPLHQLLEDLGEPPTISDLIGD 1328
Cdd:smart00323  302 LHSLLLENGDALKRelNNEDPLGKLLFKLRYFGLTTHELTY 342
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
862-1632 1.14e-52

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: 202.81  E-value: 1.14e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  862 LNQSQEDFSAESELLKLQEEVVRKIRSNQQLEQDLNLMDIK----IGLLVKNRITLQEVVSHCKKLtkknkeqlsdmmiL 937
Cdd:COG5261   290 SNVEQAFFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFAERL-------------Q 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  938 DKQKGLKSLSREKRqKLEAYQHLFYLLQT-QPIYL--------------AKLIFQMPQNKTTKFMegvIFSLYNYASNRR 1002
Cdd:COG5261   357 SNINGRKKYFPLDR-RLSLFGPLFFLLQSsIPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE---IRKLYSLGKSNC 432
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1003 EAYLLLQLFrtalQEEIKSKVEQPQDVVT---GNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDRSVSIHTDPVHI 1079
Cdd:COG5261   433 EEHLSVSLF----QMLLRTEVEATSLVQSllrGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHEDLEVDINPLLV 508
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1080 YKSWINQeeAQTGQRSHLPYDVTPEQALSHSEVQRRLDISLRSLLTL-TEKFFVAISSSVDHIPYGMRYMAKVLKTTLE- 1157
Cdd:COG5261   509 YRALLNK--GQLSPDKDLELLTSNEEVSEFLAVMNAVQESSAKLLELsTERILDAVYNSLDEIGYGIRFVCELIRVVFEl 586
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1158 ---KKFPN-----------ATERDIYKVVGNLLYYRFLNPAVVAPDAFdivaMAAGSTLAAPQRhALGAVAQLLQhaaag 1223
Cdd:COG5261   587 tpnRLFPSisdsrclrticFAEIDSLGLIGGFFFLRFVNEALVSPQTS----MLKDSCPSDNVR-KLATLSKILQ----- 656
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1224 QIFSGES--RHLRVLNDYLEDLHLKFRKFICRACRVPEPEERFAIDEYSDMVAVAKPMVYiTVGELIGTHRLLLEHQDQL 1301
Cdd:COG5261   657 SVFEITSsdKFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEY-LVNEIYLTHEIIIEYLDNL 735
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1302 --APGHQDPLHQLLEDLGEPPTisdligdniatDGHVDLSRLEvSLTLTNKFEgletdadhNSNQSLLLSTKQMLADLIQ 1379
Cdd:COG5261   736 ydPDSLVDLLLQELGELCSFPQ-----------DQRDTLNCLV-TLPLFNRSD--------DPIRDLKQQLKRTRVYIIY 795
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1380 FHPGESLEEILTSSAPrEHEEAHRRLMcwrqacdtqKPEPLRRHhSLMAHSLLSLS--EKQQRVLRNLRRLQGLGLVRAS 1457
Cdd:COG5261   796 VDAGTNLFEQLLRLLP-SDEPATRNPL---------DLNPNIRD-DPSVSSLKSMSlmKLKIRAIELLDELETLGFVSRE 864
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1458 DCYQGLVDELAKDICNQRRHRQRRKAEMLRLRTTLQGLDAKTIFYEEQGDYYNQYIQACLDHLAPKPKSSGKGKKQ---- 1533
Cdd:COG5261   865 NRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKSKLKGFSRGvgvv 944
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1534 ---------PSLHYTAAQLLEKGVLVEIEDlPVSHFRNVIFDITpGDEAGRFFVNAKFLG--VDMEKFQLHYQDLLQLQY 1602
Cdd:COG5261   945 rdkpksissGTFKYSAQQLYKRGVLVNITI-PEPNVSNIYFTFS-SDSTDNFVIEVYQPGhsVSLPEVSFCFDDLLKRQY 1022
                         810       820       830
                  ....*....|....*....|....*....|
gi 118344446 1603 EGVAVMKLFNKAKVNVNLLIFLLNKKFLRK 1632
Cdd:COG5261  1023 NKNPVVDLGGFLTFNANKLLHLIESKFYRK 1052
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
6-204 4.28e-38

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: 156.20  E-value: 4.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446    6 AGRARTAYERLTAEEMDEQRRQNVAYQYLCRLEEAKRWMEVCLKEELPSpVELEESLRNGVLLAKLGHCFAPSVVplKKI 85
Cdd:COG5261    15 LGRPIGTPSHLKTKTSAKNRSALRAYEYLCRVSEAKIWIEEVIEEALPE-LCFEDSLRNGVFLAKLTQRFNPDLT--TVI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   86 YdveqlryQATGLHFRHTDNINFWLSAVAHIGLPSIFLPETTDIYDKKNMPRVIYCIHALSLFLFRLGLAPQIHDLYGKV 165
Cdd:COG5261    92 F-------PADKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTPLINSSGQIS 164
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 118344446  166 kFTAEELGNIASELAkyglQLPAFSKIGGILANEFSADE 204
Cdd:COG5261   165 -FTKEDIAACKKAWP----RIPDFKSLGTNINTAASPEE 198
RasGAP_C pfam03836
RasGAP C-terminus; This domain can be found in the C terminus of the IQGAP family members, ...
1434-1556 3.13e-36

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: 134.21  E-value: 3.13e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  1434 LSEKQQRVLRNLRRLQGLGLVRASDCYQGLVDELAKDICNQRRHRQRRKAEMLRLRTTLQGLDAKTIFYEEQGDYYNQYI 1513
Cdd:pfam03836    1 YVELKKKALENLLELESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYI 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 118344446  1514 QACLDHLAP--------------KPKSSGKGKKQPSLHYTAAQLLEKGVLVEIEDLP 1556
Cdd:pfam03836   81 ENCLDNLQKkkkklfskqyfhyrKLQKRGKLPKFGSYKYSARQLYEKGVLLEIEGVP 137
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
34-147 4.03e-14

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: 70.01  E-value: 4.03e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446    34 LCRLEEAKRWMEVCLKEELPSPV--ELEESLRNGVLLAKLGHCFAPSVVPLKKIYDVEqlryqatglhFRHTDNINFWLS 111
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGPGVRvtNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSE----------FDKLENINLALD 70
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 118344446   112 -AVAHIGLPsIFLPETTDIYDKKNMpRVIYCIHALSL 147
Cdd:pfam00307   71 vAEKKLGVP-KVLIEPEDLVEGDNK-SVLTYLASLFR 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
38-145 1.42e-13

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: 68.11  E-value: 1.42e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446     38 EEAKRWMEVCLKEELPSPVE-LEESLRNGVLLAKLGHCFAPSVVPLKKIydveqlryQATGLHFRHTDNINFWLSAVAHI 116
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTnFSSDLKDGVALCALLNSLSPGLVDKKKV--------AASLSRFKKIENINLALSFAEKL 72
                            90       100       110
                    ....*....|....*....|....*....|
gi 118344446    117 GlPSIFLPETTDIYD-KKNMPRVIYCIHAL 145
Cdd:smart00033   73 G-GKVVLFEPEDLVEgPKLILGVIWTLISL 101
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
764-782 6.27e-05

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 41.16  E-value: 6.27e-05
                            10
                    ....*....|....*....
gi 118344446    764 AVIKIQAHWRGYRQRKAYQ 782
Cdd:smart00015    5 AAIIIQAAWRGYLARKRYK 23
COG5022 COG5022
Myosin heavy chain [General function prediction only];
735-958 4.14e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 45.45  E-value: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  735 VIKLQARLRGFLVRQKFAESSHVFRTL------------------LPAVIKIQAHWRGYRQRKAYQERLQhfkanldAII 796
Cdd:COG5022   748 ATRIQRAIRGRYLRRRYLQALKRIKKIqviqhgfrlrrlvdyelkWRLFIKLQPLLSLLGSRKEYRSYLA-------CII 820
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  797 KIQawARMWAARRRYLRRLRYFqkNVDSVVKIQAFFRARKARDDYRMLVHARHPPLCV----------------VRKFAH 860
Cdd:COG5022   821 KLQ--KTIKREKKLRETEEVEF--SLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAqrvelaerqlqelkidVKSISS 896
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  861 LLNQSQEDFSAESELLK-----LQEEVVRKIRSNQQLEQDLNLMDIKIGL---LVKNRItLQEVVSHCKKLTKKNKEQls 932
Cdd:COG5022   897 LKLVNLELESEIIELKKslssdLIENLEFKTELIARLKKLLNNIDLEEGPsieYVKLPE-LNKLHEVESKLKETSEEY-- 973
                         250       260
                  ....*....|....*....|....*.
gi 118344446  933 dMMILDKQKGLKSLSREKRQKLEAYQ 958
Cdd:COG5022   974 -EDLLKKSTILVREGNKANSELKNFK 998
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
764-782 4.32e-04

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 38.84  E-value: 4.32e-04
                           10
                   ....*....|....*....
gi 118344446   764 AVIKIQAHWRGYRQRKAYQ 782
Cdd:pfam00612    3 AAIKIQAAWRGYLARKRYK 21
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
671-696 6.99e-03

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 35.58  E-value: 6.99e-03
                          10        20
                  ....*....|....*....|....*.
gi 118344446  671 WVQHDMKDGTAYYLHLQTFQGTWEHP 696
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQWEDP 29
 
Name Accession Description Interval E-value
RasGAP_IQGAP3 cd12207
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ...
988-1337 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 [Multi-domain]  Cd Length: 350  Bit Score: 623.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  988 EGVIFSLYNYASNRREAYLLLQLFRTALQEEIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLED 1067
Cdd:cd12207     1 ESVIFSLYNYASNRREAYLLLQLFKTALQEEISSKVEKPQDVITGNPTVIRLLVSFYRSARGQNALRHILGPVVQDVLQD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1068 RSVSIHTDPVHIYKSWINQEEAQTGQRSHLPYDVTPEQALSHSEVQRRLDISLRSLLTLTEKFFVAISSSVDHIPYGMRY 1147
Cdd:cd12207    81 KGLSIRTDPVQIYKAWINQTETQSGCRSSLPYEVSPEQALSHPEVQRRLDIAIRNLLAVTDKFLSAITSSVDKIPYGMRY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1148 MAKVLKTTLEKKFPNATERDIYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGSTLAAPQRHALGAVAQLLQHAAAGQIFS 1227
Cdd:cd12207   161 VAKVLRDSLQEKFPGASEDEVYKVVGNLLYYRFMNPAVVAPDGFDIVDCSAGGALQPEQRRMLGSVAKVLQHAAANKHFQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1228 GESRHLRVLNDYLEDLHLKFRKFICRACRVPEPEERFAIDEYSDMVAVAKPMVYITVGELIGTHRLLLEHQDQLAPGHQD 1307
Cdd:cd12207   241 GDSEHLQALNQYLEETHVKFRKFILQACCVPEPEERFNVDEYSEMVAVAKPVIYITVGELINTHKLLLEHQDSIAPDHSD 320
                         330       340       350
                  ....*....|....*....|....*....|
gi 118344446 1308 PLHQLLEDLGEPPTISDLIGDNIATDGHVD 1337
Cdd:cd12207   321 PLHELLEDLGEVPTVQSLIGESWADLGDDP 350
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
998-1327 2.20e-171

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: 519.06  E-value: 2.20e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  998 ASNRREAYLLLQLFRTALQEEIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDRSVSIHTDPV 1077
Cdd:cd05127     1 ASNRREEYLLLKLFKTALREEIESKVSLPEDIVTGNPTVIKLVVNYNRGPRGQKYLRELLGPVVKEILDDDDLDLETDPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1078 HIYKSWINQEEAQTGQRSHLPYDVTPEQALSHSEVQRRLDISLRSLLTLTEKFFVAISSSVDHIPYGMRYMAKVLKTTLE 1157
Cdd:cd05127    81 DIYKAWINQEESRTGEPSKLPYDVTREQALKDPEVRKRLIEHLEKLRAITDKFLTAITESLDKMPYGMRYIAKVLKEALR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1158 KKFPNATERDIYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGSTLAAPQRHALGAVAQLLQHAAAGQIFSGESRHLRVLN 1237
Cdd:cd05127   161 EKFPDAPEEEILKIVGNLLYYRYMNPAIVAPEAFDIIDLSVGGQLSPLQRRNLGSIAKVLQQAASGKLFGGENPYLSPLN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1238 DYLEDLHLKFRKFICRACRVPEPEERFAIDEYSDMVAVAKPMVYITVGELIGTHRLLLEHQDQLAPGHQDPLHQLLEDLG 1317
Cdd:cd05127   241 PYISESHEKFKKFFLEACTVPEAEEHFNIDEYSDLTMLTKPTIYISLQEIFATHKLLLEHQDEIAPDPDDPLRELLDDLG 320
                         330
                  ....*....|
gi 118344446 1318 EPPTISDLIG 1327
Cdd:cd05127   321 PAPTIESLLG 330
RasGAP_IQGAP1 cd05133
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...
988-1352 2.86e-165

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: 504.96  E-value: 2.86e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  988 EGVIFSLYNYASNRREAYLLLQLFRTALQEEIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLED 1067
Cdd:cd05133     1 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1068 RSVSIHTDPVHIYKSWINQEEAQTGQRSHLPYDVTPEQALSHSEVQRRLDISLRSLLTLTEKFFVAISSSVDHIPYGMRY 1147
Cdd:cd05133    81 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQAMSHEEVRTRLDASIKNMRMVTDKFLSAIISSVDKIPYGMRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1148 MAKVLKTTLEKKFPNATERDIYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGSTLAAPQRHALGAVAQLLQHAAAGQIFS 1227
Cdd:cd05133   161 IAKVLKDTLHEKFPDAGEDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1228 GESRHLRVLNDYLEDLHLKFRKFICRACRVPEPEERFAIDEYSDMVAVAKPMVYITVGELIGTHRLLLEHQDQLAPGHQD 1307
Cdd:cd05133   241 GDNAHLSPINEYLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 118344446 1308 PLHQLLEDLGEPPTISDLIGDNIATDGHVD---LSRLEVSLTLTNKFE 1352
Cdd:cd05133   321 PIHELLDDLGEVPTIESLIGENPGPPGDPNretLAKTEVSLTLTNKFD 368
RasGAP_IQGAP2 cd05131
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...
990-1328 2.92e-160

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: 490.66  E-value: 2.92e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  990 VIFSLYNYASNRREAYLLLQLFRTALQEEIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDRS 1069
Cdd:cd05131     3 VIFTLYNYASNQREEYLLLKLFETALEEEIKSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIEDKS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1070 VSIHTDPVHIYKSWINQEEAQTGQRSHLPYDVTPEQALSHSEVQRRLDISLRSLLTLTEKFFVAISSSVDHIPYGMRYMA 1149
Cdd:cd05131    83 LIINTNPVEVYKAWVNQLETATGEASKLPYDVTTEQALTHPEVVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRYIA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1150 KVLKTTLEKKFPNATERDIYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGSTLAAPQRHALGAVAQLLQHAAAGQIFSGE 1229
Cdd:cd05131   163 KVLKNSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHSEQRRNLGSVAKVLQHAASNKLFEGE 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1230 SRHLRVLNDYLEDLHLKFRKFICRACRVPEPEERFAIDEYSDMVAVAKPMVYITVGELIGTHRLLLEHQDQLAPGHQDPL 1309
Cdd:cd05131   243 NAHLSSMNSYLSQTYQKFRKFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIAPDQNDLL 322
                         330
                  ....*....|....*....
gi 118344446 1310 HQLLEDLGEPPTISDLIGD 1328
Cdd:cd05131   323 HELLKDLGEVPDVESFLGE 341
CH_IQGAP3 cd21276
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP3; IQ motif ...
28-179 7.94e-107

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: 336.18  E-value: 7.94e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   28 NVAYQYLCRLEEAKRWMEVCLKEELPSPVELEESLRNGVLLAKLGHCFAPSVVPLKKIYDVEQLRYQATGLHFRHTDNIN 107
Cdd:cd21276     1 NVAYQYLCRLEEAKRWMEACLKEELPPPTELEESLRNGVYLAKLGHCFAPRVVPLKKIYDLEQMRYQATGLHFRHTDNIN 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118344446  108 FWLSAVAHIGLPSIFLPETTDIYDKKNMPRVIYCIHALSLFLFRLGLAPQIHDLYGKVKFTAEELGNIASEL 179
Cdd:cd21276    81 HWRNAMMHIGLPSIFHPETTDIYDKKNMPRVVYCIHALSLYLFRLGLAPQIHDLYGKVKFTEEEINNMKLEL 152
CH_IQGAP2 cd21275
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP2; IQ motif ...
14-159 1.18e-81

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: 264.96  E-value: 1.18e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   14 ERLTAEEMDEQRRQNVAYQYLCRLEEAKRWMEVCLKEELPSPVELEESLRNGVLLAKLGHCFAPSVVPLKKIYDVEQLRY 93
Cdd:cd21275    11 ERLSAEEMDERRRQNIAYEYLCHLEEAKQWIEACLNEELPPTTELEEGLRNGVYLVKLAKFFAPKLVSEKKIYDVDQVRY 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118344446   94 QATGLHFRHTDNINFWLSAVAHIGLPSIFLPETTDIYDKKNMPRVIYCIHALSLFLFRLGLAPQIH 159
Cdd:cd21275    91 KRSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNMPRVIYCIHALSLYLFKLGIAPQIQ 156
CH_IQGAP1 cd21274
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif ...
27-179 3.61e-79

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: 257.61  E-value: 3.61e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   27 QNVAYQYLCRLEEAKRWMEVCLKEELPSPVELEESLRNGVLLAKLGHCFAPSVVPLKKIYDVEQLRYQATGLHFRHTDNI 106
Cdd:cd21274     1 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118344446  107 NFWLSAVAHIGLPSIFLPETTDIYDKKNMPRVIYCIHALSLFLFRLGLAPQIHDLYGKVKFTAEELGNIASEL 179
Cdd:cd21274    81 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTEL 153
CH_IQGAP cd21206
calponin homology (CH) domain found in the IQ motif containing GTPase activating protein ...
28-153 6.73e-69

calponin homology (CH) domain found in the IQ motif containing GTPase activating protein family; Members of the IQ motif containing GTPase activating protein (IQGAP) family are associated with the Ras GTP-binding protein and act as essential regulators of cytoskeletal function. There are three known IQGAP family members: IQGAP1, IQGAP2, and IQGAP3. They are multi-domain molecules having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity. It lacks GAP activity. Both IQGAP1 and IQGAP2 specifically bind to Cdc42 and Rac1, but not to RhoA. Despite similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP3 regulates the organization of the cytoskeleton under the regulation of Rac1 and Cdc42 in neuronal cells. The depletion of IQGAP3 is shown to impair neurite or axon outgrowth in neuronal cells with disorganized cytoskeleton.


Pssm-ID: 409055 [Multi-domain]  Cd Length: 118  Bit Score: 226.72  E-value: 6.73e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   28 NVAYQYLCRLEEAKRWMEVCLKEELPSPVELEESLRNGVLLAKLGHCFAPSVVPLKKIYDVeqlryqatGLHFRHTDNIN 107
Cdd:cd21206     1 TIAYEYLCRLEEAKQWIEACLNEELPPTTEFEEELRNGVVLAKLANKFAPKLVPLKKIYDV--------GLQFRHTDNIN 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 118344446  108 FWLSAVAHIGLPSIFLPETTDIYDKKNMPRVIYCIHALSLFLFRLG 153
Cdd:cd21206    73 HFLRALKKIGLPKIFHFETTDLYEKKNIPKVIYCLHALSLLLFKLG 118
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
1010-1221 3.99e-66

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: 222.55  E-value: 3.99e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  1010 LFRTALQEEIKSkVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDRSVSIHTDPVHIYKSWINQEEA 1089
Cdd:pfam00616    1 LISELIEEEIES-SDNPNDLLRGNSLVSKLLETYNRRPRGQEYLKKVLGPLVRKIIEDEDLDLESDPRKIYESLINQEEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  1090 QTGqRSHLPYDVTPEQALSHSEVQRRLDISLRSLLTLTEKFFVAISSSVDHIPYGMRYMAKVLKTTLEKKFPNATERDIY 1169
Cdd:pfam00616   80 KTG-RSDLPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEIL 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 118344446  1170 KVVGNLLYYRFLNPAVVAPDAFDIVAmaagSTLAAPQRHALGAVAQLLQHAA 1221
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVD----HQISPKQRRNLTLIAKVLQNLA 206
RasGAP_GAPA cd05132
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...
986-1352 6.87e-60

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: 210.29  E-value: 6.87e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  986 FMEGVIFSLYNYASNRREAYLLLQLFRTALQEEIKSKVEqPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVL 1065
Cdd:cd05132     5 LLQTVMFTLYGNQYESREEHLLLSMFQSVLTYEFDETTE-FGSLLRANTAVSRMMTTYTRRGPGQSYLKTVLADRINDLI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1066 EDRSVSIHTDPVHIYKSWINQEEAQTGQRSHLPYDVTPEQALSHSEVQRRLDISLRSLLTLTEKFFVAISSSVDHIPYGM 1145
Cdd:cd05132    84 SLKDLNLEINPLKVYEQMINDIELDTGLPSNLPRGITPEEAAENPAVQNIIEPRLEMLEEITNSFLEAIINSLDEVPYGI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1146 RYMAKVLKTTLEKKFPNATERDIYKVVGNLLYYRFLNPAVVAPDAFDIVAmaagSTLAAPQRHALGAVAQLLQHAAAGQI 1225
Cdd:cd05132   164 RWICKQIRSLTRRKFPDASDETICSLIGGFFLLRFINPAIVSPQAYMLVD----GKPSDNTRRTLTLIAKLLQNLANKPS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1226 FSGESrHLRVLNDYLEDLHLKFRKFICRACRVPEPEERFAIDEYsdmVAVAKP--MVYITVGELIGTHRLLLEHQDQLAP 1303
Cdd:cd05132   240 YSKEP-YMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQY---IALSKKdlSINITLNEIYNTHSLLVKHLAELAP 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 118344446 1304 GHQDPLHQLLEDLGEPPtisdligdniatdghVDLSRLE---VSLTLTNKFE 1352
Cdd:cd05132   316 DHNDHLRLILQELGPAP---------------PQVPRKEnrtIELPLYSRWE 352
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
977-1328 2.68e-53

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: 190.98  E-value: 2.68e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446    977 QMPQNKTTKFMEGVIFSLYNYASNRREAYLLLQLFRTALQeeIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEI 1056
Cdd:smart00323    1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLS--LASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRAL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   1057 LGKVIQDVLED----RSVSIHTDPVHIYKSWINQEEAQTGQRSHLPYDVTPEQALSHSEV---QRRLDISLRSLLTLTEK 1129
Cdd:smart00323   79 IDPEVERTDDPntifRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAkleGEDLETNLENLLQYVER 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   1130 FFVAISSSVDHIPYGMRYMAKVLKTTLEKKFPNATERdiYKVVGNLLYYRFLNPAVVAPDAFDIVamaaGSTLAAPQRHA 1209
Cdd:smart00323  159 LFDAIINSSDRLPYGLRDICKQLRQAAEKRFPDADVI--YKAVSSFVFLRFFCPAIVSPKLFNLV----DEHPDPTTRRT 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   1210 LGAVAQLLQHAAAGQIFSGESRHLRVLNDYLEDLHLKFRKFICRACRVPEPeerfAIDEYSDMVAVakpmvyiTVGELIG 1289
Cdd:smart00323  233 LTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEI----LVDKVSDSTTI-------SGRELSL 301
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|.
gi 118344446   1290 THRLLLEHQDQLAP--GHQDPLHQLLEDLGEPPTISDLIGD 1328
Cdd:smart00323  302 LHSLLLENGDALKRelNNEDPLGKLLFKLRYFGLTTHELTY 342
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
862-1632 1.14e-52

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: 202.81  E-value: 1.14e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  862 LNQSQEDFSAESELLKLQEEVVRKIRSNQQLEQDLNLMDIK----IGLLVKNRITLQEVVSHCKKLtkknkeqlsdmmiL 937
Cdd:COG5261   290 SNVEQAFFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFAERL-------------Q 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  938 DKQKGLKSLSREKRqKLEAYQHLFYLLQT-QPIYL--------------AKLIFQMPQNKTTKFMegvIFSLYNYASNRR 1002
Cdd:COG5261   357 SNINGRKKYFPLDR-RLSLFGPLFFLLQSsIPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE---IRKLYSLGKSNC 432
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1003 EAYLLLQLFrtalQEEIKSKVEQPQDVVT---GNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDRSVSIHTDPVHI 1079
Cdd:COG5261   433 EEHLSVSLF----QMLLRTEVEATSLVQSllrGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHEDLEVDINPLLV 508
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1080 YKSWINQeeAQTGQRSHLPYDVTPEQALSHSEVQRRLDISLRSLLTL-TEKFFVAISSSVDHIPYGMRYMAKVLKTTLE- 1157
Cdd:COG5261   509 YRALLNK--GQLSPDKDLELLTSNEEVSEFLAVMNAVQESSAKLLELsTERILDAVYNSLDEIGYGIRFVCELIRVVFEl 586
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1158 ---KKFPN-----------ATERDIYKVVGNLLYYRFLNPAVVAPDAFdivaMAAGSTLAAPQRhALGAVAQLLQhaaag 1223
Cdd:COG5261   587 tpnRLFPSisdsrclrticFAEIDSLGLIGGFFFLRFVNEALVSPQTS----MLKDSCPSDNVR-KLATLSKILQ----- 656
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1224 QIFSGES--RHLRVLNDYLEDLHLKFRKFICRACRVPEPEERFAIDEYSDMVAVAKPMVYiTVGELIGTHRLLLEHQDQL 1301
Cdd:COG5261   657 SVFEITSsdKFDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEY-LVNEIYLTHEIIIEYLDNL 735
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1302 --APGHQDPLHQLLEDLGEPPTisdligdniatDGHVDLSRLEvSLTLTNKFEgletdadhNSNQSLLLSTKQMLADLIQ 1379
Cdd:COG5261   736 ydPDSLVDLLLQELGELCSFPQ-----------DQRDTLNCLV-TLPLFNRSD--------DPIRDLKQQLKRTRVYIIY 795
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1380 FHPGESLEEILTSSAPrEHEEAHRRLMcwrqacdtqKPEPLRRHhSLMAHSLLSLS--EKQQRVLRNLRRLQGLGLVRAS 1457
Cdd:COG5261   796 VDAGTNLFEQLLRLLP-SDEPATRNPL---------DLNPNIRD-DPSVSSLKSMSlmKLKIRAIELLDELETLGFVSRE 864
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1458 DCYQGLVDELAKDICNQRRHRQRRKAEMLRLRTTLQGLDAKTIFYEEQGDYYNQYIQACLDHLAPKPKSSGKGKKQ---- 1533
Cdd:COG5261   865 NRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKSKLKGFSRGvgvv 944
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1534 ---------PSLHYTAAQLLEKGVLVEIEDlPVSHFRNVIFDITpGDEAGRFFVNAKFLG--VDMEKFQLHYQDLLQLQY 1602
Cdd:COG5261   945 rdkpksissGTFKYSAQQLYKRGVLVNITI-PEPNVSNIYFTFS-SDSTDNFVIEVYQPGhsVSLPEVSFCFDDLLKRQY 1022
                         810       820       830
                  ....*....|....*....|....*....|
gi 118344446 1603 EGVAVMKLFNKAKVNVNLLIFLLNKKFLRK 1632
Cdd:COG5261  1023 NKNPVVDLGGFLTFNANKLLHLIESKFYRK 1052
RasGAP_IQGAP_related cd12206
Ras-GTPase Activating Domain of proteins related to IQGAPs; RasGAP: Ras-GTPase Activating ...
996-1332 6.00e-40

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: 152.48  E-value: 6.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  996 NYASNRREAYLLLQLFRTALQEEIKsKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDRSVSIHTD 1075
Cdd:cd12206    20 NGKMDSREEFLFIKFILELLKSDIE-NSNSNQDFLANSDNFWILLLVTFNNLRERSELKSIFGPLLVQYLENQEIDFESD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1076 PVHIYKSWINQEeaqtgqrshlpyDVTPEQALSHSEVQRRLDISLRSLLTLTEKFFVAISSSVDHIPYGMRYMAKVLKTT 1155
Cdd:cd12206    99 PSVIYKSLHGRP------------PLSSEEAIEDDRVSDKFVENLTNLREAVEMVAEIIFKNVDKIPVEIRYLCTKAYIA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1156 LEKKFPNATERDIYKVVGNLLYYRFLNPAVVAPDAFDIVAMaagstlaapQRHALGAVAQLLQHAAAGQIFSGESR-HLR 1234
Cdd:cd12206   167 FADKFPDESEEDILRAISKILIKSYVAPILVNPENYGFVDN---------EEDNLNEKARVLLQILSMVFFLKNFDgYLK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1235 VLNDYLEDLHLKFRKFICRACRVPEPEERFAIDEYSDMVAVAKPMVYITVGELIGTHRLLLEHQDQLAPGhqDPLHQLLE 1314
Cdd:cd12206   238 PLNQYIEEIKPSIRDLLKELLDVPEEEQEYDKLIYYDIMSTTRPCLEILLDKVIEIIQILKENLDEFTPD--DQLVQLLE 315
                         330
                  ....*....|....*...
gi 118344446 1315 DLGEPPTISDLIGDNIAT 1332
Cdd:cd12206   316 KIVDLSSSSNDKRSGRVT 333
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
6-204 4.28e-38

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: 156.20  E-value: 4.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446    6 AGRARTAYERLTAEEMDEQRRQNVAYQYLCRLEEAKRWMEVCLKEELPSpVELEESLRNGVLLAKLGHCFAPSVVplKKI 85
Cdd:COG5261    15 LGRPIGTPSHLKTKTSAKNRSALRAYEYLCRVSEAKIWIEEVIEEALPE-LCFEDSLRNGVFLAKLTQRFNPDLT--TVI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   86 YdveqlryQATGLHFRHTDNINFWLSAVAHIGLPSIFLPETTDIYDKKNMPRVIYCIHALSLFLFRLGLAPQIHDLYGKV 165
Cdd:COG5261    92 F-------PADKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTPLINSSGQIS 164
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 118344446  166 kFTAEELGNIASELAkyglQLPAFSKIGGILANEFSADE 204
Cdd:COG5261   165 -FTKEDIAACKKAWP----RIPDFKSLGTNINTAASPEE 198
RasGAP_C pfam03836
RasGAP C-terminus; This domain can be found in the C terminus of the IQGAP family members, ...
1434-1556 3.13e-36

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: 134.21  E-value: 3.13e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  1434 LSEKQQRVLRNLRRLQGLGLVRASDCYQGLVDELAKDICNQRRHRQRRKAEMLRLRTTLQGLDAKTIFYEEQGDYYNQYI 1513
Cdd:pfam03836    1 YVELKKKALENLLELESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYI 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 118344446  1514 QACLDHLAP--------------KPKSSGKGKKQPSLHYTAAQLLEKGVLVEIEDLP 1556
Cdd:pfam03836   81 ENCLDNLQKkkkklfskqyfhyrKLQKRGKLPKFGSYKYSARQLYEKGVLLEIEGVP 137
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
1003-1255 6.99e-34

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: 131.84  E-value: 6.99e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1003 EAYLLLQLFRTALQEEIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLED----RSVSIHTDPVH 1078
Cdd:cd04519     1 EEYRLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNTKNPntlfRGNSLATKLLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1079 IYKSWINQEeAQTGQRSHLPYDVTPEQAL----SHSEVQRRLDISLRSLLTLTEKFFVAISSSVDHIPYGMRYMAKVLKT 1154
Cdd:cd04519    81 QYMKLVGQE-YLKETLSPLIREILESKESceidTKLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILRE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1155 TLEKKFPNATErDIYKVVGNLLYYRFLNPAVVAPDAFDIVAMaagsTLAAPQRHALGAVAQLLQHAAAGQIFSGESRHLR 1234
Cdd:cd04519   160 FLAERFPEEPD-EAYQAVSGFLFLRFICPAIVSPELFGLVPD----EPSEQARRNLTLISKVLQSLANGVEFGDKEPFMK 234
                         250       260
                  ....*....|....*....|.
gi 118344446 1235 VLNDYLEDLHLKFRKFICRAC 1255
Cdd:cd04519   235 PLNDFIKSNKPKLKQFLDELS 255
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
37-147 1.83e-27

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: 107.81  E-value: 1.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   37 LEEAKRWMEVCLKEELPSPV-ELEESLRNGVLLAKLGHCFAPSVVPLKKiydveqlryQATGLHFRHTDNINFWLSAVAH 115
Cdd:cd00014     1 EEELLKWINEVLGEELPVSItDLFESLRDGVLLCKLINKLSPGSIPKIN---------KKPKSPFKKRENINLFLNACKK 71
                          90       100       110
                  ....*....|....*....|....*....|..
gi 118344446  116 IGLPSIFLPETTDIYDKKNMPRVIYCIHALSL 147
Cdd:cd00014    72 LGLPELDLFEPEDLYEKGNLKKVLGTLWALAL 103
RasGAP_Neurofibromin_like cd05392
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...
987-1302 3.69e-23

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: 102.36  E-value: 3.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  987 MEGVIFSLYNYASNrreaylLLQLFRTALQEEIkSKVEQPQDVVTGNPTVVRLVVRFYRNgRGQSALQEILGKVIQDVLE 1066
Cdd:cd05392    35 LAQSLLNLFETRNR------LLPLISWLIEDEI-SHTSRAADLFRRNSVATRLLTLYAKS-VGNKYLRKVLRPLLTEIVD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1067 DRsvsihtDPVHIYKSWINQEEAQTgqrshlpydvtpeqalshsevqrrldiSLRSLLTLTEKFFVAISSSVDHIPYGMR 1146
Cdd:cd05392   107 NK------DYFEVEKIKPDDENLEE---------------------------NADLLMKYAQMLLDSITDSVDQLPPSFR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1147 YMAKVLKTTLEKKFPNATerdiYKVVGNLLYYRFLNPAVVAPDAFDIVAmaagSTLAAPQRHALGAVAQLLQHAAAGQIF 1226
Cdd:cd05392   154 YICNTIYESVSKKFPDAA----LIAVGGFLFLRFICPAIVSPESENLLD----PPPTPEARRSLILIAKVLQNIANGVLF 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118344446 1227 SGESRHLRVLNDYLEDLHLKFRKFICRACRVPEPEERFAIDEYSDMVAvakpmvyitvgELIGTHRLLLEHQDQLA 1302
Cdd:cd05392   226 SLKEPYLESLNEFLKKNSDRIQQFLSEVSTIPPTDPIFDESDEEPITA-----------DLRYLHKFLYLHFLEIR 290
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
39-145 9.59e-17

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: 77.35  E-value: 9.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   39 EAKRWMEVCLKEELPSPVELEESLRNGVLLAKLGHCFAPSVVplKKIydveqlryQATGLHFRHTDNINFWLSAVAHIGL 118
Cdd:cd21207     9 EALDWIEAVTGEKLDDGKDYEDVLKDGVILCKLINILKPGSV--KKI--------NTSKMAFKLMENIENFLTACKGYGV 78
                          90       100
                  ....*....|....*....|....*..
gi 118344446  119 PSIFLPETTDIYDKKNMPRVIYCIHAL 145
Cdd:cd21207    79 PKTDLFQTVDLYEKKNIPQVTNCLFAL 105
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
1121-1321 3.54e-16

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: 81.60  E-value: 3.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1121 RSLLTLTEKFFVAISSSVDHIPYGMRYMAKVLKTTLEKKFPNATerdiYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGS 1200
Cdd:cd05130   138 RNLLQLTEKFFHAIISSSDEFPPQLRSVCHCLYQVVSHRFPNSG----LGAVGSAIFLRFINPAIVSPYEYGILDREPPP 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1201 TLaapqRHALGAVAQLLQHAAAGQIFSGESrHLRVLNDYLEDLHLKFRKFICrACRVPEPeerfAIDEysdmvAVAKPMV 1280
Cdd:cd05130   214 RV----KRGLKLMSKILQNIANHVLFTKEA-HMLPFNDFLRNHFEAGRRFFS-SIASDCG----AVDG-----PSSKYLS 278
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 118344446 1281 YITVGELIGTHRLLLEHQDQ-------------LAPGHQDPLHQLLEDLGEPPT 1321
Cdd:cd05130   279 FINDANVLALHRLLWNNQEKigqylassrdhkaVGRRPFDKMATLLAYLGPPGH 332
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
34-147 4.03e-14

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: 70.01  E-value: 4.03e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446    34 LCRLEEAKRWMEVCLKEELPSPV--ELEESLRNGVLLAKLGHCFAPSVVPLKKIYDVEqlryqatglhFRHTDNINFWLS 111
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGPGVRvtNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSE----------FDKLENINLALD 70
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 118344446   112 -AVAHIGLPsIFLPETTDIYDKKNMpRVIYCIHALSL 147
Cdd:pfam00307   71 vAEKKLGVP-KVLIEPEDLVEGDNK-SVLTYLASLFR 105
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
38-146 6.52e-14

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: 68.93  E-value: 6.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   38 EEAKRWMEVCLKEELPsPVELEESLRNGVLLAKLghcfapsvvpLKKIYDVEQLRYQATGLHFRHTDNINFWLSAVAHIG 117
Cdd:cd21210     3 QEAREWIEEVLGEKLA-QGDLLDALKDGVVLCKL----------ANRILPADIRKYKESKMPFVQMENISAFLNAARKLG 71
                          90       100
                  ....*....|....*....|....*....
gi 118344446  118 LPSIFLPETTDIYDKKNMPRVIYCIHALS 146
Cdd:cd21210    72 VPENDLFQTVDLFERKNPAQVLQCLHALS 100
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
38-145 1.42e-13

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: 68.11  E-value: 1.42e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446     38 EEAKRWMEVCLKEELPSPVE-LEESLRNGVLLAKLGHCFAPSVVPLKKIydveqlryQATGLHFRHTDNINFWLSAVAHI 116
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTnFSSDLKDGVALCALLNSLSPGLVDKKKV--------AASLSRFKKIENINLALSFAEKL 72
                            90       100       110
                    ....*....|....*....|....*....|
gi 118344446    117 GlPSIFLPETTDIYD-KKNMPRVIYCIHAL 145
Cdd:smart00033   73 G-GKVVLFEPEDLVEgPKLILGVIWTLISL 101
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
37-131 2.19e-09

calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This family includes LIM domain only protein 7 (LMO-7) and LIM and calponin homology domains-containing protein 1 (LIMCH1), and similar proteins. LMO-7, also called F-box only protein 20, or LOMP, is a transcription regulator for expression of many Emery-Dreifuss muscular dystrophy (EDMD)-relevant genes. It binds to alpha-actinin and AF6/afadin at adherens junctions for epithelial cell-cell adhesion. LIMCH1 acts as an actin stress fiber-associated protein that activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. It positively regulates actin stress fiber assembly and stabilizes focal adhesions, and therefore negatively regulates cell spreading and cell migration. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409057 [Multi-domain]  Cd Length: 119  Bit Score: 56.96  E-value: 2.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   37 LEEAKRWMEVCLKEELPSPvELEESLRNGVLLAKLGHCFAPSVVplKKIydvEQLRYQATGLhfrhtDNINFWLSAVAHI 116
Cdd:cd21208     2 LKEARTWIEAVTGKKFPSD-DFRESLEDGILLCELINAIKPGSI--KKI---NRLPTPIAGL-----DNLNLFLKACEDL 70
                          90
                  ....*....|....*
gi 118344446  117 GLPSIFLPETTDIYD 131
Cdd:cd21208    71 GLKDSQLFDPTDLQD 85
SCP1 COG5199
Calponin [Cytoskeleton];
38-172 2.28e-09

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 58.39  E-value: 2.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   38 EEAKRWMEVCLKEELPSPVELEESLRNGVLLAKLghcfapsvvpLKKIyDVEQLRYQATGLHFRHTDNINFWLSAVAHIG 117
Cdd:COG5199    16 KEVTLWIETVLGEKFEPPGDLLSLLKDGVRLCRI----------LNEA-SPLDIKYKESKMPFVQMENISSFINGLKKLR 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118344446  118 LPSIFLPETTDIYDKKNMPRVIYCIHALS-----LFLFRL-GLAPQIHDLYGKVKFTAEEL 172
Cdd:COG5199    85 VPEYELFQTNDLFEAKDLRQVVICLYSLSryaqkERMFSGpFLGPHLATKKPRVFSSQEVL 145
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
36-145 1.95e-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: 1.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   36 RLEEAKRWMEVCLKEEL---PSPVELEESLRNGVLLAKLGHCFAPSVVPlkKIYDVEQLRYQATGLHFRHTDNINFWLSA 112
Cdd:cd21203     1 RRYEAAEWIQNVLGVLVlpdPSEEEFRLCLRDGVVLCKLLNKLQPGAVP--KVVESPDDPDGAAGSAFQYFENVRNFLVA 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 118344446  113 VAHIGLPSiFLPETTDIYDKKNMPRVIYCIHAL 145
Cdd:cd21203    79 IEEMGLPT-FEASDLEQGGGGSRPRVVDCILAL 110
RasGAP_GAP1_like cd05128
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...
1006-1193 4.94e-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: 49.94  E-value: 4.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1006 LLLQLFRTALQEEIkSKVEQPQDVVTGNpTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDRsVSIHTDPVHiykswin 1085
Cdd:cd05128    51 QIVPLLRALASREI-SKTQDPNTLFRGN-SLASKCMDEFMKLVGMQYLHETLKPVIDEIFSEK-KSCEIDPSK------- 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1086 qeeaqtgqrshlpydvtpeqaLSHSEVqrrLDISLRSLLTLTEKFFVAISSSVDHIPYGMRYMAKVLKTTLEKKFPNAte 1165
Cdd:cd05128   121 ---------------------LKDGEV---LETNLANLRGYVERVFKAITSSARRCPTLMCEIFSDLRESAAQRFPDN-- 174
                         170       180
                  ....*....|....*....|....*....
gi 118344446 1166 RDI-YKVVGNLLYYRFLNPAVVAPDAFDI 1193
Cdd:cd05128   175 EDVpYTAVSGFIFLRFFAPAILNPKLFGL 203
RasGAP_RASAL cd05135
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...
1049-1193 1.10e-05

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


Pssm-ID: 213337  Cd Length: 287  Bit Score: 49.04  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1049 GQSALQEILGKVIQDVLEDRSVsIHTDPVHIykswinqeEAQTGQRSHLPYDVTPEQALSHSevqrrLDISLRSLLTLTE 1128
Cdd:cd05135    97 GMPYLHEVLKPVINRIFEEKKY-VELDPCKI--------DLNRTRRISFKGSLSEAQVRESS-----LELLQGYLGSIID 162
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118344446 1129 kffvAISSSVDHIPYGMRYMAKVLKTTLEKKFPNATERDI-YKVVGNLLYYRFLNPAVVAPDAFDI 1193
Cdd:cd05135   163 ----AIVGSVDQCPPVMRVAFKQLHKRVEERFPEAEHQDVkYLAISGFLFLRFFAPAILTPKLFQL 224
CH_VAV cd21201
calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic ...
54-146 1.84e-05

calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and as scaffold proteins, and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the CH domain, an actin-binding domain which is present as a single copy in VAV proteins.


Pssm-ID: 409050  Cd Length: 117  Bit Score: 45.32  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   54 SPVELEESLRNGVLLAKLGHCFAPSVVPLKKIydveQLRYQAtgLHFRHTDNINFWLSA-VAHIGLPSIFLPETTDIYDK 132
Cdd:cd21201    28 TVFDLAQALRDGVLLCQLLNRLSPGSVDDREI----NLRPQM--SQFLCLKNIRTFLQAcRTVFGLRSADLFEPEDLYDV 101
                          90
                  ....*....|....
gi 118344446  133 KNMPRVIYCIHALS 146
Cdd:cd21201   102 TNFGKVIRTLSKLS 115
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
764-782 6.27e-05

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 41.16  E-value: 6.27e-05
                            10
                    ....*....|....*....
gi 118344446    764 AVIKIQAHWRGYRQRKAYQ 782
Cdd:smart00015    5 AAIIIQAAWRGYLARKRYK 23
RasGAP_RAP6 cd05129
Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is ...
955-1218 3.35e-04

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: 45.03  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  955 EAYQHLFY----------LLQTQPIYLAKLIF---QMPQNKTTKFMEGVIFSLYNYASNRREAYLLLQLFRTALQEEIKS 1021
Cdd:cd05129     1 DAYKLLGYqlshygeflrILRENPQLLAECLArgeKLSLEQTQNVIQTIVTSLYGNCIMPEDERLLLQLLRELMELQLKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1022 KVEQPQDVVTGNPTVVRLVVRF-YRNGRGQSALQEILGKVIQDVLEDRSVSIHTDPVH-IYKSWINQEEAQTGQRshlpy 1099
Cdd:cd05129    81 SDNPRRLLRKGSCAFSRVFKLFtELLFSAKLYLTAALHKPIMQVLVDDEIFLETDPQKaLCRFSPAEQEKRFGEE----- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446 1100 dVTPEQalsHSEVQRRLDISLRSLLTLTEKFFVAISSSVDHIPYGMRYMAKVLKTTLEKKFpNATERDIYKVVGNLLYYR 1179
Cdd:cd05129   156 -GTPEQ---QRKLQQYRAEFLSRLVALVNKFISSLRQSVYCFPQSLRWIVRQLRKILTRSG-DDEEAEARALCTDLLFTN 230
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 118344446 1180 FLNPAVVAPDAFDIVAMAAGSTLAapqRHALGAVAQLLQ 1218
Cdd:cd05129   231 FICPAIVNPEQYGIISDAPISEVA---RHNLMQVAQILQ 266
COG5022 COG5022
Myosin heavy chain [General function prediction only];
735-958 4.14e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 45.45  E-value: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  735 VIKLQARLRGFLVRQKFAESSHVFRTL------------------LPAVIKIQAHWRGYRQRKAYQERLQhfkanldAII 796
Cdd:COG5022   748 ATRIQRAIRGRYLRRRYLQALKRIKKIqviqhgfrlrrlvdyelkWRLFIKLQPLLSLLGSRKEYRSYLA-------CII 820
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  797 KIQawARMWAARRRYLRRLRYFqkNVDSVVKIQAFFRARKARDDYRMLVHARHPPLCV----------------VRKFAH 860
Cdd:COG5022   821 KLQ--KTIKREKKLRETEEVEF--SLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAqrvelaerqlqelkidVKSISS 896
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446  861 LLNQSQEDFSAESELLK-----LQEEVVRKIRSNQQLEQDLNLMDIKIGL---LVKNRItLQEVVSHCKKLTKKNKEQls 932
Cdd:COG5022   897 LKLVNLELESEIIELKKslssdLIENLEFKTELIARLKKLLNNIDLEEGPsieYVKLPE-LNKLHEVESKLKETSEEY-- 973
                         250       260
                  ....*....|....*....|....*.
gi 118344446  933 dMMILDKQKGLKSLSREKRQKLEAYQ 958
Cdd:COG5022   974 -EDLLKKSTILVREGNKANSELKNFK 998
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
764-782 4.32e-04

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 38.84  E-value: 4.32e-04
                           10
                   ....*....|....*....
gi 118344446   764 AVIKIQAHWRGYRQRKAYQ 782
Cdd:pfam00612    3 AAIKIQAAWRGYLARKRYK 21
CH_VAV1 cd21262
calponin homology (CH) domain found in VAV1 protein; VAV1 is expressed predominantly in the ...
57-146 2.25e-03

calponin homology (CH) domain found in VAV1 protein; VAV1 is expressed predominantly in the hematopoietic system and it plays an important role in the development and activation of B and T cells. It is activated by tyrosine phosphorylation to function as a guanine nucleotide exchange factor (GEF) for Rho GTPases following cell surface receptor activation, triggering various effects such as cytoskeletal reorganization, transcription regulation, cell cycle progression, and calcium mobilization. It also serves as a scaffold protein and has been shown to interact with Ku70, Socs1, Janus kinase 2, SIAH2, S100B, Abl gene, ZAP-70, SLP76, and Syk, among others. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the CH domain, an actin-binding domain which is present as a single copy in VAV1 protein.


Pssm-ID: 409111  Cd Length: 120  Bit Score: 39.54  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344446   57 ELEESLRNGVLLAKLGHCFAPSVVPLKKIydveQLRYQATglHFRHTDNINFWLSAVAH-IGLPSIFLPETTDIYDKKNM 135
Cdd:cd21262    31 DLAQALRDGVLLCQLLNNLLPHAVNLREI----NLRPQMS--QFLCLKNIRTFLSTCCEkFGLRKSELFEAFDLFDVRDF 104
                          90
                  ....*....|.
gi 118344446  136 PRVIYCIHALS 146
Cdd:cd21262   105 GKVIDTLSILS 115
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
671-696 6.99e-03

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 35.58  E-value: 6.99e-03
                          10        20
                  ....*....|....*....|....*.
gi 118344446  671 WVQHDMKDGTAYYLHLQTFQGTWEHP 696
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQWEDP 29
 
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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