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Conserved domains on  [gi|210032529|ref|NP_001101959|]
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ras GTPase-activating-like protein IQGAP1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RasGAP_IQGAP1 cd05133
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...
1003-1382 0e+00

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a homodimeric protein that is widely expressed among vertebrate cell types from early embryogenesis. Mammalian IQGAP1 protein is the best characterized member of the IQGAP family, and contains several protein-interacting domains. Human IQGAP1 is most similar to mouse Iqgap1 (94% identity) and has 62% identity to human IQGAP2. IQGAP1 binds and cross-links actin filaments in vitro and has been implicated in Ca2+/calmodulin signaling, E-cadherin-dependent cell adhesion, cell motility, and invasion. Yeast IQGAP homologs have a role in the recruitment of actin filaments, are components of the spindle pole body, and are required for actomyosin ring assembly and cytokinesis. Furthermore, IQGAP1 over-expression has also been detected in gastric and colorectal carcinomas and gastric cancer cell lines.


:

Pssm-ID: 213335  Cd Length: 380  Bit Score: 783.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1003 DSVIFTLYNYASNQREEYLLLRLFQTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 1082
Cdd:cd05133     1 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1083 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALSHEEVKTRLDNSIRNMRAVTDKFLSAIVSSVDKIPYGMRF 1162
Cdd:cd05133    81 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQAMSHEEVRTRLDASIKNMRMVTDKFLSAIISSVDKIPYGMRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1163 IAKVLKDSLHEKFPDAAEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 1242
Cdd:cd05133   161 IAKVLKDTLHEKFPDAGEDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1243 GDNAHLSIINEYLSQSYQKFRRFFQAACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 1322
Cdd:cd05133   241 GDNAHLSPINEYLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1323 PIHELLDDLGEVPTIESLIGESCGNSNDPSKEALAKTEVSLTLTNKFDVPGDENAEMDAR 1382
Cdd:cd05133   321 PIHELLDDLGEVPTIESLIGENPGPPGDPNRETLAKTEVSLTLTNKFDVPGDENAEMDAR 380
CH_IQGAP1 cd21274
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif ...
37-190 3.17e-107

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: 337.35  E-value: 3.17e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   37 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 116
Cdd:cd21274     1 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 210032529  117 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKIELE 190
Cdd:cd21274    81 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTELE 154
IQG1 super family cl34962
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
876-1657 8.68e-65

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: 240.94  E-value: 8.68e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529  876 LDQSDQDFQEELDLMKMREEVITLIRSNQQLENDLNLMDIK----IGLLVKNKITLQDVVSHSKKLtkknkeqlsdMMMI 951
Cdd:COG5261   290 SNVEQAFFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFAERL----------QSNI 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529  952 NKQKGGLKALskekrEKLEAYQHLFYLLQTN-PTYL--------------AKLIFQMPQNKSTKFMdsvIFTLYNYASNQ 1016
Cdd:COG5261   360 NGRKKYFPLD-----RRLSLFGPLFFLLQSSiPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE---IRKLYSLGKSN 431
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1017 REEYLLLRLFQTALQEEIKSKVDqIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPVDIYK 1096
Cdd:COG5261   432 CEEHLSVSLFQMLLRTEVEATSL-VQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHEDLEVDINPLLVYR 510
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1097 SWVNQmesqtgeaSKLPYDVTPEQALSHEEVKTRL------DNSIRN-MRAVTDKFLSAIVSSVDKIPYGMRFIAKVLK- 1168
Cdd:COG5261   511 ALLNK--------GQLSPDKDLELLTSNEEVSEFLavmnavQESSAKlLELSTERILDAVYNSLDEIGYGIRFVCELIRv 582
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1169 ------DSLHEKFPDA--------AEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSaggqlTTDQRRNLGSIAKMLQH 1234
Cdd:COG5261   583 vfeltpNRLFPSISDSrclrticfAEIDSLGLIGGFFFLRFVNEALVSPQTSMLKDSC-----PSDNVRKLATLSKILQS 657
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1235 AASNKMFLGdnaHLSIINEYLSQSYQKFRRFFQAACDVPELQDKFNVDEYSDLVTLTKPVIYIsIGEIINTHTLLLDHQD 1314
Cdd:COG5261   658 VFEITSSDK---FDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYL-VNEIYLTHEIIIEYLD 733
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1315 AI--APEHNDPIHELLDDLGEVPtiesligescgnsnDPSKEALAKTEvSLTLTNKFDVPgdenaemdARTILLNTKRLI 1392
Cdd:COG5261   734 NLydPDSLVDLLLQELGELCSFP--------------QDQRDTLNCLV-TLPLFNRSDDP--------IRDLKQQLKRTR 790
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1393 VDVIRFQPGETLTEIL--ETPatnEQEAEHQRAM-QRRAIRDAKTPDKMKkskpmkednNLSLQEKKEKIQTGLKKLTEL 1469
Cdd:COG5261   791 VYIIYVDAGTNLFEQLlrLLP---SDEPATRNPLdLNPNIRDDPSVSSLK---------SMSLMKLKIRAIELLDELETL 858
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1470 GTVDPKNRYQELINDIAKDIRNQRRYRQRRKAELVKLQQTYSALNSKATFYGEQVDYYKSYIKTCLDNLASKGK----VS 1545
Cdd:COG5261   859 GFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKSklkgFS 938
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1546 KKPREMKGKKSKK--ISLKYTAARLHEKGVLLEIEDLQANqFKNVIFEIGpTEEVGDFEVKAKFMG--VQMETFMLHYQD 1621
Cdd:COG5261   939 RGVGVVRDKPKSIssGTFKYSAQQLYKRGVLVNITIPEPN-VSNIYFTFS-SDSTDNFVIEVYQPGhsVSLPEVSFCFDD 1016
                         810       820       830
                  ....*....|....*....|....*....|....*.
gi 210032529 1622 LLQLQYEGVAVMKLFDRAKVNVNLLIFLLNKKFYGK 1657
Cdd:COG5261  1017 LLKRQYNKNPVVDLGGFLTFNANKLLHLIESKFYRK 1052
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
685-712 6.84e-04

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: 38.66  E-value: 6.84e-04
                          10        20
                  ....*....|....*....|....*...
gi 210032529  685 WVKHWVKGGYHYYHNLETQAGGWaEPPD 712
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQW-EDPR 30
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
774-796 1.89e-03

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


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.92  E-value: 1.89e-03
                            10        20
                    ....*....|....*....|...
gi 210032529    774 KQIPAITCIQSQWRGYKQKKAYQ 796
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
749-766 9.55e-03

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


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 34.99  E-value: 9.55e-03
                            10
                    ....*....|....*...
gi 210032529    749 ITKLQACCRGYLVRQEFR 766
Cdd:smart00015    6 AIIIQAAWRGYLARKRYK 23
 
Name Accession Description Interval E-value
RasGAP_IQGAP1 cd05133
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...
1003-1382 0e+00

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a homodimeric protein that is widely expressed among vertebrate cell types from early embryogenesis. Mammalian IQGAP1 protein is the best characterized member of the IQGAP family, and contains several protein-interacting domains. Human IQGAP1 is most similar to mouse Iqgap1 (94% identity) and has 62% identity to human IQGAP2. IQGAP1 binds and cross-links actin filaments in vitro and has been implicated in Ca2+/calmodulin signaling, E-cadherin-dependent cell adhesion, cell motility, and invasion. Yeast IQGAP homologs have a role in the recruitment of actin filaments, are components of the spindle pole body, and are required for actomyosin ring assembly and cytokinesis. Furthermore, IQGAP1 over-expression has also been detected in gastric and colorectal carcinomas and gastric cancer cell lines.


Pssm-ID: 213335  Cd Length: 380  Bit Score: 783.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1003 DSVIFTLYNYASNQREEYLLLRLFQTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 1082
Cdd:cd05133     1 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1083 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALSHEEVKTRLDNSIRNMRAVTDKFLSAIVSSVDKIPYGMRF 1162
Cdd:cd05133    81 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQAMSHEEVRTRLDASIKNMRMVTDKFLSAIISSVDKIPYGMRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1163 IAKVLKDSLHEKFPDAAEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 1242
Cdd:cd05133   161 IAKVLKDTLHEKFPDAGEDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1243 GDNAHLSIINEYLSQSYQKFRRFFQAACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 1322
Cdd:cd05133   241 GDNAHLSPINEYLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1323 PIHELLDDLGEVPTIESLIGESCGNSNDPSKEALAKTEVSLTLTNKFDVPGDENAEMDAR 1382
Cdd:cd05133   321 PIHELLDDLGEVPTIESLIGENPGPPGDPNRETLAKTEVSLTLTNKFDVPGDENAEMDAR 380
CH_IQGAP1 cd21274
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif ...
37-190 3.17e-107

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: 337.35  E-value: 3.17e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   37 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 116
Cdd:cd21274     1 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 210032529  117 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKIELE 190
Cdd:cd21274    81 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTELE 154
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
1025-1237 6.33e-77

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: 253.36  E-value: 6.33e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529  1025 LFQTALQEEIKSkVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPVDIYKSWVNQMES 1104
Cdd:pfam00616    1 LISELIEEEIES-SDNPNDLLRGNSLVSKLLETYNRRPRGQEYLKKVLGPLVRKIIEDEDLDLESDPRKIYESLINQEEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529  1105 QTGEaSKLPYDVTPEQALSHEEVKTRLDNSIRNMRAVTDKFLSAIVSSVDKIPYGMRFIAKVLKDSLHEKFPDAAEDELL 1184
Cdd:pfam00616   80 KTGR-SDLPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEIL 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 210032529  1185 KIIGNLLYYRYMNPAIVAPDAFDIIDlsagGQLTTDQRRNLGSIAKMLQHAAS 1237
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVD----HQISPKQRRNLTLIAKVLQNLAN 207
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
992-1344 3.21e-73

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: 248.38  E-value: 3.21e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529    992 QMPQNKSTKFMDSVIFTLYNYASNQREEYLLLRLFQTALQeeIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQI 1071
Cdd:smart00323    1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLS--LASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRAL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   1072 LAPVVKEIMDD----KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALSHEEVKTR---LDNSIRNMRAVTDK 1144
Cdd:smart00323   79 IDPEVERTDDPntifRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEgedLETNLENLLQYVER 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   1145 FLSAIVSSVDKIPYGMRFIAKVLKDSLHEKFPDAaeDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLsaggQLTTDQRRN 1224
Cdd:smart00323  159 LFDAIINSSDRLPYGLRDICKQLRQAAEKRFPDA--DVIYKAVSSFVFLRFFCPAIVSPKLFNLVDE----HPDPTTRRT 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   1225 LGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQAACDVPElqdkFNVDEYSDLVTLTkpviyisIGEIIN 1304
Cdd:smart00323  233 LTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPE----ILVDKVSDSTTIS-------GRELSL 301
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|..
gi 210032529   1305 THTLLLDHQDAIAPEHN--DPIHELLDDLGEVPTIESLIGES 1344
Cdd:smart00323  302 LHSLLLENGDALKRELNneDPLGKLLFKLRYFGLTTHELTYG 343
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
876-1657 8.68e-65

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: 240.94  E-value: 8.68e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529  876 LDQSDQDFQEELDLMKMREEVITLIRSNQQLENDLNLMDIK----IGLLVKNKITLQDVVSHSKKLtkknkeqlsdMMMI 951
Cdd:COG5261   290 SNVEQAFFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFAERL----------QSNI 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529  952 NKQKGGLKALskekrEKLEAYQHLFYLLQTN-PTYL--------------AKLIFQMPQNKSTKFMdsvIFTLYNYASNQ 1016
Cdd:COG5261   360 NGRKKYFPLD-----RRLSLFGPLFFLLQSSiPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE---IRKLYSLGKSN 431
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1017 REEYLLLRLFQTALQEEIKSKVDqIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPVDIYK 1096
Cdd:COG5261   432 CEEHLSVSLFQMLLRTEVEATSL-VQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHEDLEVDINPLLVYR 510
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1097 SWVNQmesqtgeaSKLPYDVTPEQALSHEEVKTRL------DNSIRN-MRAVTDKFLSAIVSSVDKIPYGMRFIAKVLK- 1168
Cdd:COG5261   511 ALLNK--------GQLSPDKDLELLTSNEEVSEFLavmnavQESSAKlLELSTERILDAVYNSLDEIGYGIRFVCELIRv 582
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1169 ------DSLHEKFPDA--------AEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSaggqlTTDQRRNLGSIAKMLQH 1234
Cdd:COG5261   583 vfeltpNRLFPSISDSrclrticfAEIDSLGLIGGFFFLRFVNEALVSPQTSMLKDSC-----PSDNVRKLATLSKILQS 657
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1235 AASNKMFLGdnaHLSIINEYLSQSYQKFRRFFQAACDVPELQDKFNVDEYSDLVTLTKPVIYIsIGEIINTHTLLLDHQD 1314
Cdd:COG5261   658 VFEITSSDK---FDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYL-VNEIYLTHEIIIEYLD 733
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1315 AI--APEHNDPIHELLDDLGEVPtiesligescgnsnDPSKEALAKTEvSLTLTNKFDVPgdenaemdARTILLNTKRLI 1392
Cdd:COG5261   734 NLydPDSLVDLLLQELGELCSFP--------------QDQRDTLNCLV-TLPLFNRSDDP--------IRDLKQQLKRTR 790
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1393 VDVIRFQPGETLTEIL--ETPatnEQEAEHQRAM-QRRAIRDAKTPDKMKkskpmkednNLSLQEKKEKIQTGLKKLTEL 1469
Cdd:COG5261   791 VYIIYVDAGTNLFEQLlrLLP---SDEPATRNPLdLNPNIRDDPSVSSLK---------SMSLMKLKIRAIELLDELETL 858
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1470 GTVDPKNRYQELINDIAKDIRNQRRYRQRRKAELVKLQQTYSALNSKATFYGEQVDYYKSYIKTCLDNLASKGK----VS 1545
Cdd:COG5261   859 GFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKSklkgFS 938
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1546 KKPREMKGKKSKK--ISLKYTAARLHEKGVLLEIEDLQANqFKNVIFEIGpTEEVGDFEVKAKFMG--VQMETFMLHYQD 1621
Cdd:COG5261   939 RGVGVVRDKPKSIssGTFKYSAQQLYKRGVLVNITIPEPN-VSNIYFTFS-SDSTDNFVIEVYQPGhsVSLPEVSFCFDD 1016
                         810       820       830
                  ....*....|....*....|....*....|....*.
gi 210032529 1622 LLQLQYEGVAVMKLFDRAKVNVNLLIFLLNKKFYGK 1657
Cdd:COG5261  1017 LLKRQYNKNPVVDLGGFLTFNANKLLHLIESKFYRK 1052
RasGAP_C pfam03836
RasGAP C-terminus; This domain can be found in the C terminus of the IQGAP family members, ...
1452-1581 7.04e-38

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: 138.84  E-value: 7.04e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529  1452 LQEKKEKIQTGLKKLTELGTVDPKNRYQELINDIAKDIRNQRRYRQRRKAELVKLQQTYSALNSKATFYGEQVDYYKSYI 1531
Cdd:pfam03836    1 YVELKKKALENLLELESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYI 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 210032529  1532 KTCLDNLASKGKVS-------KKPREMKGKKSKKISLKYTAARLHEKGVLLEIEDLQ 1581
Cdd:pfam03836   81 ENCLDNLQKKKKKLfskqyfhYRKLQKRGKLPKFGSYKYSARQLYEKGVLLEIEGVP 137
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
26-214 6.40e-35

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


Pssm-ID: 227586 [Multi-domain]  Cd Length: 1054  Bit Score: 145.80  E-value: 6.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   26 LTAEEMDERRRQNVAYEYLCHLEEAKRWMEACLGEDLPpTTELEEGLRNGVYLAKLGNFFSPKvvSLKKIYdreqtryKA 105
Cdd:COG5261    25 LKTKTSAKNRSALRAYEYLCRVSEAKIWIEEVIEEALP-ELCFEDSLRNGVFLAKLTQRFNPD--LTTVIF-------PA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529  106 TGLHFRHTDNVIQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVdFTEEEINNM 185
Cdd:COG5261    95 DKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTPLINSSGQIS-FTKEDIAAC 173
                         170       180
                  ....*....|....*....|....*....
gi 210032529  186 KIELEkygiQMPAFSKIGGILANELSVDE 214
Cdd:COG5261   174 KKAWP----RIPDFKSLGTNINTAASPEE 198
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
48-158 6.85e-15

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: 72.32  E-value: 6.85e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529    48 EEAKRWMEACLGEDLPPT--TELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREqtrykatglhFRHTDNVIQWLN-AMD 124
Cdd:pfam00307    5 KELLRWINSHLAEYGPGVrvTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSE----------FDKLENINLALDvAEK 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 210032529   125 EIGLPKIFyPETTDIYDRKNMpRCIYCIHALSLY 158
Cdd:pfam00307   75 KLGVPKVL-IEPEDLVEGDNK-SVLTYLASLFRR 106
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
48-155 1.15e-14

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: 71.19  E-value: 1.15e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529     48 EEAKRWMEACLGEDLPPT-TELEEGLRNGVYLAKLGNFFSPKVVSLKKIydreqtryKATGLHFRHTDNVIQWLNAMDEI 126
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPvTNFSSDLKDGVALCALLNSLSPGLVDKKKV--------AASLSRFKKIENINLALSFAEKL 72
                            90       100       110
                    ....*....|....*....|....*....|
gi 210032529    127 GlPKIFYPETTDIYD-RKNMPRCIYCIHAL 155
Cdd:smart00033   73 G-GKVVLFEPEDLVEgPKLILGVIWTLISL 101
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
685-712 6.84e-04

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: 38.66  E-value: 6.84e-04
                          10        20
                  ....*....|....*....|....*...
gi 210032529  685 WVKHWVKGGYHYYHNLETQAGGWaEPPD 712
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQW-EDPR 30
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
774-796 1.89e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.92  E-value: 1.89e-03
                            10        20
                    ....*....|....*....|...
gi 210032529    774 KQIPAITCIQSQWRGYKQKKAYQ 796
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
778-796 9.08e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.99  E-value: 9.08e-03
                           10
                   ....*....|....*....
gi 210032529   778 AITCIQSQWRGYKQKKAYQ 796
Cdd:pfam00612    3 AAIKIQAAWRGYLARKRYK 21
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
749-766 9.55e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 34.99  E-value: 9.55e-03
                            10
                    ....*....|....*...
gi 210032529    749 ITKLQACCRGYLVRQEFR 766
Cdd:smart00015    6 AIIIQAAWRGYLARKRYK 23
 
Name Accession Description Interval E-value
RasGAP_IQGAP1 cd05133
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...
1003-1382 0e+00

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a homodimeric protein that is widely expressed among vertebrate cell types from early embryogenesis. Mammalian IQGAP1 protein is the best characterized member of the IQGAP family, and contains several protein-interacting domains. Human IQGAP1 is most similar to mouse Iqgap1 (94% identity) and has 62% identity to human IQGAP2. IQGAP1 binds and cross-links actin filaments in vitro and has been implicated in Ca2+/calmodulin signaling, E-cadherin-dependent cell adhesion, cell motility, and invasion. Yeast IQGAP homologs have a role in the recruitment of actin filaments, are components of the spindle pole body, and are required for actomyosin ring assembly and cytokinesis. Furthermore, IQGAP1 over-expression has also been detected in gastric and colorectal carcinomas and gastric cancer cell lines.


Pssm-ID: 213335  Cd Length: 380  Bit Score: 783.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1003 DSVIFTLYNYASNQREEYLLLRLFQTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 1082
Cdd:cd05133     1 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1083 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALSHEEVKTRLDNSIRNMRAVTDKFLSAIVSSVDKIPYGMRF 1162
Cdd:cd05133    81 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQAMSHEEVRTRLDASIKNMRMVTDKFLSAIISSVDKIPYGMRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1163 IAKVLKDSLHEKFPDAAEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 1242
Cdd:cd05133   161 IAKVLKDTLHEKFPDAGEDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1243 GDNAHLSIINEYLSQSYQKFRRFFQAACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 1322
Cdd:cd05133   241 GDNAHLSPINEYLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1323 PIHELLDDLGEVPTIESLIGESCGNSNDPSKEALAKTEVSLTLTNKFDVPGDENAEMDAR 1382
Cdd:cd05133   321 PIHELLDDLGEVPTIESLIGENPGPPGDPNRETLAKTEVSLTLTNKFDVPGDENAEMDAR 380
RasGAP_IQGAP2 cd05131
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...
1003-1354 0e+00

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a member of the IQGAP family that contains a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeat, a single WW domain, four IQ motifs which mediate interactions with calmodulin, and a Ras-GTPase-activating protein (GAP)-related domain that binds Rho family GTPases. IQGAP2 and IQGAP3 play important roles in the regulation of the cytoskeleton for axon outgrowth in hippocampal neurons and are thought to stay in a common regulatory pathway. The results of RNA interference studies indicated that IQGAP3 partially compensates functions of IQGAP2, but has lesser ability than IQGAP2 to promote axon outgrowth in hippocampal neuron. Moreover, IQGAP2 is required for the cadherin-mediated cell-to-cell adhesion in Xenopus laevis embryos.


Pssm-ID: 213333 [Multi-domain]  Cd Length: 359  Bit Score: 663.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1003 DSVIFTLYNYASNQREEYLLLRLFQTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 1082
Cdd:cd05131     1 DTVIFTLYNYASNQREEYLLLKLFETALEEEIKSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1083 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALSHEEVKTRLDNSIRNMRAVTDKFLSAIVSSVDKIPYGMRF 1162
Cdd:cd05131    81 KSLIINTNPVEVYKAWVNQLETATGEASKLPYDVTTEQALTHPEVVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1163 IAKVLKDSLHEKFPDAAEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 1242
Cdd:cd05131   161 IAKVLKNSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHSEQRRNLGSVAKVLQHAASNKLFE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1243 GDNAHLSIINEYLSQSYQKFRRFFQAACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 1322
Cdd:cd05131   241 GENAHLSSMNSYLSQTYQKFRKFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIAPDQND 320
                         330       340       350
                  ....*....|....*....|....*....|..
gi 210032529 1323 PIHELLDDLGEVPTIESLIGESCGNSNDPSKE 1354
Cdd:cd05131   321 LLHELLKDLGEVPDVESFLGEGTVDPNDPNKE 352
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
1013-1343 0e+00

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


Pssm-ID: 213329 [Multi-domain]  Cd Length: 331  Bit Score: 603.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1013 ASNQREEYLLLRLFQTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPV 1092
Cdd:cd05127     1 ASNRREEYLLLKLFKTALREEIESKVSLPEDIVTGNPTVIKLVVNYNRGPRGQKYLRELLGPVVKEILDDDDLDLETDPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1093 DIYKSWVNQMESQTGEASKLPYDVTPEQALSHEEVKTRLDNSIRNMRAVTDKFLSAIVSSVDKIPYGMRFIAKVLKDSLH 1172
Cdd:cd05127    81 DIYKAWINQEESRTGEPSKLPYDVTREQALKDPEVRKRLIEHLEKLRAITDKFLTAITESLDKMPYGMRYIAKVLKEALR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1173 EKFPDAAEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFLGDNAHLSIIN 1252
Cdd:cd05127   161 EKFPDAPEEEILKIVGNLLYYRYMNPAIVAPEAFDIIDLSVGGQLSPLQRRNLGSIAKVLQQAASGKLFGGENPYLSPLN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1253 EYLSQSYQKFRRFFQAACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHNDPIHELLDDLG 1332
Cdd:cd05127   241 PYISESHEKFKKFFLEACTVPEAEEHFNIDEYSDLTMLTKPTIYISLQEIFATHKLLLEHQDEIAPDPDDPLRELLDDLG 320
                         330
                  ....*....|.
gi 210032529 1333 EVPTIESLIGE 1343
Cdd:cd05127   321 PAPTIESLLGS 331
RasGAP_IQGAP3 cd12207
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ...
1003-1350 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: 582.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1003 DSVIFTLYNYASNQREEYLLLRLFQTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 1082
Cdd:cd12207     1 ESVIFSLYNYASNRREAYLLLQLFKTALQEEISSKVEKPQDVITGNPTVIRLLVSFYRSARGQNALRHILGPVVQDVLQD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1083 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALSHEEVKTRLDNSIRNMRAVTDKFLSAIVSSVDKIPYGMRF 1162
Cdd:cd12207    81 KGLSIRTDPVQIYKAWINQTETQSGCRSSLPYEVSPEQALSHPEVQRRLDIAIRNLLAVTDKFLSAITSSVDKIPYGMRY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1163 IAKVLKDSLHEKFPDAAEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 1242
Cdd:cd12207   161 VAKVLRDSLQEKFPGASEDEVYKVVGNLLYYRFMNPAVVAPDGFDIVDCSAGGALQPEQRRMLGSVAKVLQHAAANKHFQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1243 GDNAHLSIINEYLSQSYQKFRRFFQAACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 1322
Cdd:cd12207   241 GDSEHLQALNQYLEETHVKFRKFILQACCVPEPEERFNVDEYSEMVAVAKPVIYITVGELINTHKLLLEHQDSIAPDHSD 320
                         330       340
                  ....*....|....*....|....*...
gi 210032529 1323 PIHELLDDLGEVPTIESLIGESCGNSND 1350
Cdd:cd12207   321 PLHELLEDLGEVPTVQSLIGESWADLGD 348
CH_IQGAP1 cd21274
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif ...
37-190 3.17e-107

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: 337.35  E-value: 3.17e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   37 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 116
Cdd:cd21274     1 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 210032529  117 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKIELE 190
Cdd:cd21274    81 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTELE 154
CH_IQGAP2 cd21275
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP2; IQ motif ...
14-169 3.95e-105

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: 331.60  E-value: 3.95e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   14 RPHYGSVLDNERLTAEEMDERRRQNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLK 93
Cdd:cd21275     1 RPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKQWIEACLNEELPPTTELEEGLRNGVYLVKLAKFFAPKLVSEK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 210032529   94 KIYDREQTRYKATGLHFRHTDNVIQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQ 169
Cdd:cd21275    81 KIYDVDQVRYKRSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNMPRVIYCIHALSLYLFKLGIAPQIQ 156
CH_IQGAP3 cd21276
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP3; IQ motif ...
38-189 2.71e-98

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: 312.30  E-value: 2.71e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   38 NVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNVI 117
Cdd:cd21276     1 NVAYQYLCRLEEAKRWMEACLKEELPPPTELEESLRNGVYLAKLGHCFAPRVVPLKKIYDLEQMRYQATGLHFRHTDNIN 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 210032529  118 QWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKIEL 189
Cdd:cd21276    81 HWRNAMMHIGLPSIFHPETTDIYDKKNMPRVVYCIHALSLYLFRLGLAPQIHDLYGKVKFTEEEINNMKLEL 152
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
1025-1237 6.33e-77

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: 253.36  E-value: 6.33e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529  1025 LFQTALQEEIKSkVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPVDIYKSWVNQMES 1104
Cdd:pfam00616    1 LISELIEEEIES-SDNPNDLLRGNSLVSKLLETYNRRPRGQEYLKKVLGPLVRKIIEDEDLDLESDPRKIYESLINQEEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529  1105 QTGEaSKLPYDVTPEQALSHEEVKTRLDNSIRNMRAVTDKFLSAIVSSVDKIPYGMRFIAKVLKDSLHEKFPDAAEDELL 1184
Cdd:pfam00616   80 KTGR-SDLPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEIL 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 210032529  1185 KIIGNLLYYRYMNPAIVAPDAFDIIDlsagGQLTTDQRRNLGSIAKMLQHAAS 1237
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVD----HQISPKQRRNLTLIAKVLQNLAN 207
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
992-1344 3.21e-73

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: 248.38  E-value: 3.21e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529    992 QMPQNKSTKFMDSVIFTLYNYASNQREEYLLLRLFQTALQeeIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQI 1071
Cdd:smart00323    1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLS--LASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRAL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   1072 LAPVVKEIMDD----KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALSHEEVKTR---LDNSIRNMRAVTDK 1144
Cdd:smart00323   79 IDPEVERTDDPntifRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEgedLETNLENLLQYVER 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   1145 FLSAIVSSVDKIPYGMRFIAKVLKDSLHEKFPDAaeDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLsaggQLTTDQRRN 1224
Cdd:smart00323  159 LFDAIINSSDRLPYGLRDICKQLRQAAEKRFPDA--DVIYKAVSSFVFLRFFCPAIVSPKLFNLVDE----HPDPTTRRT 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   1225 LGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQAACDVPElqdkFNVDEYSDLVTLTkpviyisIGEIIN 1304
Cdd:smart00323  233 LTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPE----ILVDKVSDSTTIS-------GRELSL 301
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|..
gi 210032529   1305 THTLLLDHQDAIAPEHN--DPIHELLDDLGEVPTIESLIGES 1344
Cdd:smart00323  302 LHSLLLENGDALKRELNneDPLGKLLFKLRYFGLTTHELTYG 343
CH_IQGAP cd21206
calponin homology (CH) domain found in the IQ motif containing GTPase activating protein ...
38-163 1.86e-70

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: 231.35  E-value: 1.86e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   38 NVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDreqtrykaTGLHFRHTDNVI 117
Cdd:cd21206     1 TIAYEYLCRLEEAKQWIEACLNEELPPTTEFEEELRNGVVLAKLANKFAPKLVPLKKIYD--------VGLQFRHTDNIN 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 210032529  118 QWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLG 163
Cdd:cd21206    73 HFLRALKKIGLPKIFHFETTDLYEKKNIPKVIYCLHALSLLLFKLG 118
RasGAP_GAPA cd05132
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...
1001-1335 1.13e-68

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: 235.71  E-value: 1.13e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1001 FMDSVIFTLYNYASNQREEYLLLRLFQTALQEEIKSKVDqIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIM 1080
Cdd:cd05132     5 LLQTVMFTLYGNQYESREEHLLLSMFQSVLTYEFDETTE-FGSLLRANTAVSRMMTTYTRRGPGQSYLKTVLADRINDLI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1081 DDKSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALSHEEVKTRLDNSIRNMRAVTDKFLSAIVSSVDKIPYGM 1160
Cdd:cd05132    84 SLKDLNLEINPLKVYEQMINDIELDTGLPSNLPRGITPEEAAENPAVQNIIEPRLEMLEEITNSFLEAIINSLDEVPYGI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1161 RFIAKVLKDSLHEKFPDAAEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDlsagGQLTTDQRRNLGSIAKMLQHAASNKM 1240
Cdd:cd05132   164 RWICKQIRSLTRRKFPDASDETICSLIGGFFLLRFINPAIVSPQAYMLVD----GKPSDNTRRTLTLIAKLLQNLANKPS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1241 FlGDNAHLSIINEYLSQSYQKFRRFFQAACDVPELQDKFNVDEYsdlVTLTKPVIYISI--GEIINTHTLLLDHQDAIAP 1318
Cdd:cd05132   240 Y-SKEPYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQY---IALSKKDLSINItlNEIYNTHSLLVKHLAELAP 315
                         330
                  ....*....|....*..
gi 210032529 1319 EHNDPIHELLDDLGEVP 1335
Cdd:cd05132   316 DHNDHLRLILQELGPAP 332
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
876-1657 8.68e-65

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: 240.94  E-value: 8.68e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529  876 LDQSDQDFQEELDLMKMREEVITLIRSNQQLENDLNLMDIK----IGLLVKNKITLQDVVSHSKKLtkknkeqlsdMMMI 951
Cdd:COG5261   290 SNVEQAFFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKrgnkIRLLIQNRMPQEEDTKFAERL----------QSNI 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529  952 NKQKGGLKALskekrEKLEAYQHLFYLLQTN-PTYL--------------AKLIFQMPQNKSTKFMdsvIFTLYNYASNQ 1016
Cdd:COG5261   360 NGRKKYFPLD-----RRLSLFGPLFFLLQSSiPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE---IRKLYSLGKSN 431
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1017 REEYLLLRLFQTALQEEIKSKVDqIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPVDIYK 1096
Cdd:COG5261   432 CEEHLSVSLFQMLLRTEVEATSL-VQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHEDLEVDINPLLVYR 510
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1097 SWVNQmesqtgeaSKLPYDVTPEQALSHEEVKTRL------DNSIRN-MRAVTDKFLSAIVSSVDKIPYGMRFIAKVLK- 1168
Cdd:COG5261   511 ALLNK--------GQLSPDKDLELLTSNEEVSEFLavmnavQESSAKlLELSTERILDAVYNSLDEIGYGIRFVCELIRv 582
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1169 ------DSLHEKFPDA--------AEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSaggqlTTDQRRNLGSIAKMLQH 1234
Cdd:COG5261   583 vfeltpNRLFPSISDSrclrticfAEIDSLGLIGGFFFLRFVNEALVSPQTSMLKDSC-----PSDNVRKLATLSKILQS 657
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1235 AASNKMFLGdnaHLSIINEYLSQSYQKFRRFFQAACDVPELQDKFNVDEYSDLVTLTKPVIYIsIGEIINTHTLLLDHQD 1314
Cdd:COG5261   658 VFEITSSDK---FDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYL-VNEIYLTHEIIIEYLD 733
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1315 AI--APEHNDPIHELLDDLGEVPtiesligescgnsnDPSKEALAKTEvSLTLTNKFDVPgdenaemdARTILLNTKRLI 1392
Cdd:COG5261   734 NLydPDSLVDLLLQELGELCSFP--------------QDQRDTLNCLV-TLPLFNRSDDP--------IRDLKQQLKRTR 790
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1393 VDVIRFQPGETLTEIL--ETPatnEQEAEHQRAM-QRRAIRDAKTPDKMKkskpmkednNLSLQEKKEKIQTGLKKLTEL 1469
Cdd:COG5261   791 VYIIYVDAGTNLFEQLlrLLP---SDEPATRNPLdLNPNIRDDPSVSSLK---------SMSLMKLKIRAIELLDELETL 858
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1470 GTVDPKNRYQELINDIAKDIRNQRRYRQRRKAELVKLQQTYSALNSKATFYGEQVDYYKSYIKTCLDNLASKGK----VS 1545
Cdd:COG5261   859 GFVSRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKSklkgFS 938
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1546 KKPREMKGKKSKK--ISLKYTAARLHEKGVLLEIEDLQANqFKNVIFEIGpTEEVGDFEVKAKFMG--VQMETFMLHYQD 1621
Cdd:COG5261   939 RGVGVVRDKPKSIssGTFKYSAQQLYKRGVLVNITIPEPN-VSNIYFTFS-SDSTDNFVIEVYQPGhsVSLPEVSFCFDD 1016
                         810       820       830
                  ....*....|....*....|....*....|....*.
gi 210032529 1622 LLQLQYEGVAVMKLFDRAKVNVNLLIFLLNKKFYGK 1657
Cdd:COG5261  1017 LLKRQYNKNPVVDLGGFLTFNANKLLHLIESKFYRK 1052
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
1018-1271 5.92e-38

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: 143.40  E-value: 5.92e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1018 EEYLLLRLFQTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSL----NIKTDPVD 1093
Cdd:cd04519     1 EEYRLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNTKNPNTLfrgnSLATKLLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1094 IYKSWVNQmESQTGEASKLPYDVTPEQAL----SHEEVKTRLDNSIRNMRAVTDKFLSAIVSSVDKIPYGMRFIAKVLKD 1169
Cdd:cd04519    81 QYMKLVGQ-EYLKETLSPLIREILESKESceidTKLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILRE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1170 SLHEKFPDaAEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDlsagGQLTTDQRRNLGSIAKMLQHAASNKMFLGDNAHLS 1249
Cdd:cd04519   160 FLAERFPE-EPDEAYQAVSGFLFLRFICPAIVSPELFGLVP----DEPSEQARRNLTLISKVLQSLANGVEFGDKEPFMK 234
                         250       260
                  ....*....|....*....|..
gi 210032529 1250 IINEYLSQSYQKFRRFFQAACD 1271
Cdd:cd04519   235 PLNDFIKSNKPKLKQFLDELSS 256
RasGAP_C pfam03836
RasGAP C-terminus; This domain can be found in the C terminus of the IQGAP family members, ...
1452-1581 7.04e-38

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: 138.84  E-value: 7.04e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529  1452 LQEKKEKIQTGLKKLTELGTVDPKNRYQELINDIAKDIRNQRRYRQRRKAELVKLQQTYSALNSKATFYGEQVDYYKSYI 1531
Cdd:pfam03836    1 YVELKKKALENLLELESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYI 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 210032529  1532 KTCLDNLASKGKVS-------KKPREMKGKKSKKISLKYTAARLHEKGVLLEIEDLQ 1581
Cdd:pfam03836   81 ENCLDNLQKKKKKLfskqyfhYRKLQKRGKLPKFGSYKYSARQLYEKGVLLEIEGVP 137
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
26-214 6.40e-35

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


Pssm-ID: 227586 [Multi-domain]  Cd Length: 1054  Bit Score: 145.80  E-value: 6.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   26 LTAEEMDERRRQNVAYEYLCHLEEAKRWMEACLGEDLPpTTELEEGLRNGVYLAKLGNFFSPKvvSLKKIYdreqtryKA 105
Cdd:COG5261    25 LKTKTSAKNRSALRAYEYLCRVSEAKIWIEEVIEEALP-ELCFEDSLRNGVFLAKLTQRFNPD--LTTVIF-------PA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529  106 TGLHFRHTDNVIQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVdFTEEEINNM 185
Cdd:COG5261    95 DKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTPLINSSGQIS-FTKEDIAAC 173
                         170       180
                  ....*....|....*....|....*....
gi 210032529  186 KIELEkygiQMPAFSKIGGILANELSVDE 214
Cdd:COG5261   174 KKAWP----RIPDFKSLGTNINTAASPEE 198
RasGAP_IQGAP_related cd12206
Ras-GTPase Activating Domain of proteins related to IQGAPs; RasGAP: Ras-GTPase Activating ...
1011-1334 6.27e-34

Ras-GTPase Activating Domain of proteins related to IQGAPs; RasGAP: Ras-GTPase Activating Domain. RasGAP functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Proteins having a RasGAP domain include p120GAP, IQGAP, Rab5-activating protein 6, and Neurofibromin. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a myriad of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGap domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator.


Pssm-ID: 213345 [Multi-domain]  Cd Length: 359  Bit Score: 135.15  E-value: 6.27e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1011 NYASNQREEYLLLRLFQTALQEEIKsKVDQIQEIVTGNPTV-IKMVVSFNRgaRGQNALRQ-ILAPVVKEIMDDKSLNIK 1088
Cdd:cd12206    20 NGKMDSREEFLFIKFILELLKSDIE-NSNSNQDFLANSDNFwILLLVTFNN--LRERSELKsIFGPLLVQYLENQEIDFE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1089 TDPVDIYKSWVNQMesqtgeasklpyDVTPEQALSHEEVKTRLDNSIRNMRAVTDKFLSAIVSSVDKIPYGMRFIAKVLK 1168
Cdd:cd12206    97 SDPSVIYKSLHGRP------------PLSSEEAIEDDRVSDKFVENLTNLREAVEMVAEIIFKNVDKIPVEIRYLCTKAY 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1169 DSLHEKFPDAAEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDlsaggqlttDQRRNLGSIAKMLQHAASNKMFLG-DNAH 1247
Cdd:cd12206   165 IAFADKFPDESEEDILRAISKILIKSYVAPILVNPENYGFVD---------NEEDNLNEKARVLLQILSMVFFLKnFDGY 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1248 LSIINEYLSQSYQKFRRFFQAACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPehNDPIHEL 1327
Cdd:cd12206   236 LKPLNQYIEEIKPSIRDLLKELLDVPEEEQEYDKLIYYDIMSTTRPCLEILLDKVIEIIQILKENLDEFTP--DDQLVQL 313

                  ....*..
gi 210032529 1328 LDDLGEV 1334
Cdd:cd12206   314 LEKIVDL 320
RasGAP_Neurofibromin_like cd05392
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...
967-1345 3.09e-32

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: 128.94  E-value: 3.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529  967 EKLEAYQHLFYLLQTNPTylakLIFQMPQNKSTKFMDS---VIFTLYNYASNqreeylLLRLFQTALQEEIkSKVDQIQE 1043
Cdd:cd05392     1 KKSEAYDELLELLIEDPQ----LLLAIAEVCPSSEVDLlaqSLLNLFETRNR------LLPLISWLIEDEI-SHTSRAAD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1044 IVTGNPTVIKMVVSFNRgARGQNALRQILAPVVKEIMDDKSLN--IKTDPVDiykswvnqmesqtgeasklpydvtpeqa 1121
Cdd:cd05392    70 LFRRNSVATRLLTLYAK-SVGNKYLRKVLRPLLTEIVDNKDYFevEKIKPDD---------------------------- 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1122 lshEEVKTRLDNsirnMRAVTDKFLSAIVSSVDKIPYGMRFIAKVLKDSLHEKFPDAAedelLKIIGNLLYYRYMNPAIV 1201
Cdd:cd05392   121 ---ENLEENADL----LMKYAQMLLDSITDSVDQLPPSFRYICNTIYESVSKKFPDAA----LIAVGGFLFLRFICPAIV 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1202 APDAFDIIDLSAggqlTTDQRRNLGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQAACDVPElqdkfnv 1281
Cdd:cd05392   190 SPESENLLDPPP----TPEARRSLILIAKVLQNIANGVLFSLKEPYLESLNEFLKKNSDRIQQFLSEVSTIPP------- 258
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 210032529 1282 DEYSDLVTLTKPViyisIGEIINTHTLLLDHQDAIAPEHNDPIhELLDDLGEVPTIESLIGESC 1345
Cdd:cd05392   259 TDPIFDESDEEPI----TADLRYLHKFLYLHFLEIRKEVLKGS-SSQGSDKELVETFKLIDEIL 317
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
47-157 1.62e-25

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 102.42  E-value: 1.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   47 LEEAKRWMEACLGEDLP-PTTELEEGLRNGVYLAKLGNFFSPKVVSLKKiydreqtryKATGLHFRHTDNVIQWLNAMDE 125
Cdd:cd00014     1 EEELLKWINEVLGEELPvSITDLFESLRDGVLLCKLINKLSPGSIPKIN---------KKPKSPFKKRENINLFLNACKK 71
                          90       100       110
                  ....*....|....*....|....*....|..
gi 210032529  126 IGLPKIFYPETTDIYDRKNMPRCIYCIHALSL 157
Cdd:cd00014    72 LGLPELDLFEPEDLYEKGNLKKVLGTLWALAL 103
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
1116-1317 2.87e-15

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


Pssm-ID: 213332 [Multi-domain]  Cd Length: 332  Bit Score: 78.90  E-value: 2.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1116 VTPEQALSHEEVKTRLDNS------IRNMRAVTDKFLSAIVSSVDKIPYGMRFIAKVLKDSLHEKFPDAAedelLKIIGN 1189
Cdd:cd05130   112 ITSSEWVSYEVDPTRLEGNenleenQRNLLQLTEKFFHAIISSSDEFPPQLRSVCHCLYQVVSHRFPNSG----LGAVGS 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1190 LLYYRYMNPAIVAPDAFDIIDlsagGQLTTDQRRNLGSIAKMLQHAASNKMFLGDnAHLSIINEYLSQSYQKFRRFFQAA 1269
Cdd:cd05130   188 AIFLRFINPAIVSPYEYGILD----REPPPRVKRGLKLMSKILQNIANHVLFTKE-AHMLPFNDFLRNHFEAGRRFFSSI 262
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 210032529 1270 CDvpelqDKFNVDEYSDlvtltKPVIYISIGEIINTHTLLLDHQDAIA 1317
Cdd:cd05130   263 AS-----DCGAVDGPSS-----KYLSFINDANVLALHRLLWNNQEKIG 300
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
48-158 6.85e-15

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: 72.32  E-value: 6.85e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529    48 EEAKRWMEACLGEDLPPT--TELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREqtrykatglhFRHTDNVIQWLN-AMD 124
Cdd:pfam00307    5 KELLRWINSHLAEYGPGVrvTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSE----------FDKLENINLALDvAEK 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 210032529   125 EIGLPKIFyPETTDIYDRKNMpRCIYCIHALSLY 158
Cdd:pfam00307   75 KLGVPKVL-IEPEDLVEGDNK-SVLTYLASLFRR 106
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
48-155 1.15e-14

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: 71.19  E-value: 1.15e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529     48 EEAKRWMEACLGEDLPPT-TELEEGLRNGVYLAKLGNFFSPKVVSLKKIydreqtryKATGLHFRHTDNVIQWLNAMDEI 126
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPvTNFSSDLKDGVALCALLNSLSPGLVDKKKV--------AASLSRFKKIENINLALSFAEKL 72
                            90       100       110
                    ....*....|....*....|....*....|
gi 210032529    127 GlPKIFYPETTDIYD-RKNMPRCIYCIHAL 155
Cdd:smart00033   73 G-GKVVLFEPEDLVEgPKLILGVIWTLISL 101
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
49-155 8.22e-14

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: 68.88  E-value: 8.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   49 EAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKvvSLKKIydreqtryKATGLHFRHTDNVIQWLNAMDEIGL 128
Cdd:cd21207     9 EALDWIEAVTGEKLDDGKDYEDVLKDGVILCKLINILKPG--SVKKI--------NTSKMAFKLMENIENFLTACKGYGV 78
                          90       100
                  ....*....|....*....|....*..
gi 210032529  129 PKIFYPETTDIYDRKNMPRCIYCIHAL 155
Cdd:cd21207    79 PKTDLFQTVDLYEKKNIPQVTNCLFAL 105
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
48-156 6.65e-13

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


Pssm-ID: 409059 [Multi-domain]  Cd Length: 101  Bit Score: 66.24  E-value: 6.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   48 EEAKRWMEACLGEDLPPTTeLEEGLRNGVYLAKLGNffspkvvslkKIYDREQTRYKATGLHFRHTDNVIQWLNAMDEIG 127
Cdd:cd21210     3 QEAREWIEEVLGEKLAQGD-LLDALKDGVVLCKLAN----------RILPADIRKYKESKMPFVQMENISAFLNAARKLG 71
                          90       100
                  ....*....|....*....|....*....
gi 210032529  128 LPKIFYPETTDIYDRKNMPRCIYCIHALS 156
Cdd:cd21210    72 VPENDLFQTVDLFERKNPAQVLQCLHALS 100
RasGAP_RAP6 cd05129
Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is ...
970-1322 3.37e-10

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: 63.90  E-value: 3.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529  970 EAYQHLFY----------LLQTNPTYLAKLIFQMPQ--NKSTKFMDSVIFT-LYNYASNQREEYLLLRLFQTALQEEIKS 1036
Cdd:cd05129     1 DAYKLLGYqlshygeflrILRENPQLLAECLARGEKlsLEQTQNVIQTIVTsLYGNCIMPEDERLLLQLLRELMELQLKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1037 KVDQIQEIVTGNPTVIKMVVSFNRGARGQN-----ALRQilaPVVKEIMDDkSLNIKTDPVD-IYKSWVNQMESQTGEas 1110
Cdd:cd05129    81 SDNPRRLLRKGSCAFSRVFKLFTELLFSAKlyltaALHK---PIMQVLVDD-EIFLETDPQKaLCRFSPAEQEKRFGE-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1111 klpyDVTPEQalsHEEVKTRLDNSIRNMRAVTDKFLSAIVSSVDKIPYGMRFIAKVLKDSLHEKFpDAAEDELLKIIGNL 1190
Cdd:cd05129   155 ----EGTPEQ---QRKLQQYRAEFLSRLVALVNKFISSLRQSVYCFPQSLRWIVRQLRKILTRSG-DDEEAEARALCTDL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1191 LYYRYMNPAIVAPDAFDIIDLSAGGQLTtdqRRNLGSIAKMLQHAASNKMFLGDNahlsiineYLSQSYQKFRR----FF 1266
Cdd:cd05129   227 LFTNFICPAIVNPEQYGIISDAPISEVA---RHNLMQVAQILQVLALTEFESPDP--------RLKELLSKFDKdcvsAF 295
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 210032529 1267 QAACDVPELQDKFNVDEySDLVTLTKPVIYISIGEiINTHTLLLDHQDAIAPEHND 1322
Cdd:cd05129   296 LDVVIVGRAVETPPPSS-SALLEGSRTAVLITESD-LATLVEFLRSVKTGDEEKED 349
RasGAP_RASAL cd05135
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...
1068-1233 6.43e-10

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: 62.14  E-value: 6.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1068 LRQILAPVVKEIMDDKSLnIKTDPVDIykswvnqMESQTGEASKlpydvtpEQALSHEEVktrLDNSIRNMRAVTDKFLS 1147
Cdd:cd05135   101 LHEVLKPVINRIFEEKKY-VELDPCKI-------DLNRTRRISF-------KGSLSEAQV---RESSLELLQGYLGSIID 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1148 AIVSSVDKIPYGMRFIAKVLKDSLHEKFPDAAEDELLKI-IGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTtdqrRNLG 1226
Cdd:cd05135   163 AIVGSVDQCPPVMRVAFKQLHKRVEERFPEAEHQDVKYLaISGFLFLRFFAPAILTPKLFQLREQHADPRTS----RTLL 238

                  ....*..
gi 210032529 1227 SIAKMLQ 1233
Cdd:cd05135   239 LLAKAVQ 245
SCP1 COG5199
Calponin [Cytoskeleton];
48-168 1.43e-09

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 59.16  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   48 EEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVslkkiydreqtRYKATGLHFRHTDNVIQWLNAMDEIG 127
Cdd:COG5199    16 KEVTLWIETVLGEKFEPPGDLLSLLKDGVRLCRILNEASPLDI-----------KYKESKMPFVQMENISSFINGLKKLR 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 210032529  128 LPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKL------GLAPQI 168
Cdd:COG5199    85 VPEYELFQTNDLFEAKDLRQVVICLYSLSRYAQKErmfsgpFLGPHL 131
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
48-155 2.17e-09

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: 56.65  E-value: 2.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   48 EEAKRWMEACLGEDLPPTT---ELEEGLRNGVYLAKLGNFFSPKVVSlkKIYDREQTRYKATGLHFRHTDNVIQWLNAMD 124
Cdd:cd21203     3 YEAAEWIQNVLGVLVLPDPseeEFRLCLRDGVVLCKLLNKLQPGAVP--KVVESPDDPDGAAGSAFQYFENVRNFLVAIE 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 210032529  125 EIGLPkIFYPETTDIYDRKNMPRCIYCIHAL 155
Cdd:cd21203    81 EMGLP-TFEASDLEQGGGGSRPRVVDCILAL 110
RasGAP_GAP1_like cd05128
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...
1021-1234 6.06e-08

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


Pssm-ID: 213330  Cd Length: 269  Bit Score: 55.72  E-value: 6.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1021 LLLRLFQTALQEEIkSKVDQIQEIVTGNPTVIKMVVSFNRGArGQNALRQILAPVVKEIMDD-KSLNIktDPvdiykswv 1099
Cdd:cd05128    51 QIVPLLRALASREI-SKTQDPNTLFRGNSLASKCMDEFMKLV-GMQYLHETLKPVIDEIFSEkKSCEI--DP-------- 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1100 nqmesqtgeaSKLPYdvtpeqalsheevKTRLDNSIRNMRAVTDKFLSAIVSSVDKIPYGMRFIAKVLKDSLHEKFPDAA 1179
Cdd:cd05128   119 ----------SKLKD-------------GEVLETNLANLRGYVERVFKAITSSARRCPTLMCEIFSDLRESAAQRFPDNE 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1180 EDELLKIIGnLLYYRYMNPAIVAPDAFDiidlsaggqLTTDQ-----RRNLGSIAKMLQH 1234
Cdd:cd05128   176 DVPYTAVSG-FIFLRFFAPAILNPKLFG---------LREEHpdpqtARTLTLISKTIQT 225
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
47-141 2.69e-06

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: 48.10  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   47 LEEAKRWMEACLGEDLPPtTELEEGLRNGVYLAKLGNFFSPKvvSLKKIyDREQTRYkaTGLhfrhtDNVIQWLNAMDEI 126
Cdd:cd21208     2 LKEARTWIEAVTGKKFPS-DDFRESLEDGILLCELINAIKPG--SIKKI-NRLPTPI--AGL-----DNLNLFLKACEDL 70
                          90
                  ....*....|....*
gi 210032529  127 GLPKIFYPETTDIYD 141
Cdd:cd21208    71 GLKDSQLFDPTDLQD 85
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
1136-1348 6.67e-04

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


Pssm-ID: 213338  Cd Length: 324  Bit Score: 43.73  E-value: 6.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1136 RNMRAVTDKFLSAIVSSVDKIPygmrfiaKVLKD---SLHEKF-----PDAAEdellKIIGNLLYYRYMNPAIVAPDAFD 1207
Cdd:cd05136   137 ANLRRSVELAWCKILSSHCVFP-------RELREvfsSWRERLeergrEDIAD----RLISASLFLRFLCPAILSPSLFN 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1208 IIdlsaggQLTTDQR--RNLGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQAACDVPELQDKFNVDEYS 1285
Cdd:cd05136   206 LT------QEYPSERaaRNLTLIAKVIQNLANFTRFGGKEEYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYI 279
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 210032529 1286 DLVTltkpviyisigEIINTHTLLLdhqDAIAPEHNDPIHEllddLGEVPTIESLIGESCGNS 1348
Cdd:cd05136   280 DLGR-----------ELSLLHSLLV---EIISKLNQTTLDK----LGPLPRILNDITEALRNP 324
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
685-712 6.84e-04

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: 38.66  E-value: 6.84e-04
                          10        20
                  ....*....|....*....|....*...
gi 210032529  685 WVKHWVKGGYHYYHNLETQAGGWaEPPD 712
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQW-EDPR 30
RasGAP_p120GAP cd05391
Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ...
1110-1290 1.21e-03

Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates hydrolysis of bound GTP to GDP. Once the Ras regulator p120GAP, a member of the GAP protein family, is recruited to the membrane, it is transiently immobilized to interact with Ras-GTP. The down-regulation of Ras by p120GAP is a critical step in the regulation of many cellular processes, which is disrupted in approximately 30% of human cancers. p120GAP contains SH2, SH3, PH, calcium- and lipid-binding domains, suggesting its involvement in a complex network of cellular interactions in vivo.


Pssm-ID: 213340  Cd Length: 328  Bit Score: 42.86  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1110 SKLPYDVTPEQALSHEEVKTRLDNSIRNMRAVTDKflsaIVSSVDKIPYGMRFIAKVLKDSLHEKFPDAAEDElLKIIGN 1189
Cdd:cd05391   111 SKQSCELNPSKLEKNEDVNTNLEHLLNILSELVEK----IFMAAEILPPTLRYIYGCLQKSVQQKWPTNTTVR-TRVVSG 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1190 LLYYRYMNPAIVAPDAFDIIDLSAGGQLTtdqrRNLGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQAA 1269
Cdd:cd05391   186 FVFLRLICPAILNPRMFNIISETPSPTAA----RTLTLVAKSLQNLANLVEFGAKEPYMEGVNPFIKKNKERMIMFLDEL 261
                         170       180
                  ....*....|....*....|....
gi 210032529 1270 CDVPELQD---KFNVDEYSDLVTL 1290
Cdd:cd05391   262 GNVPELPDtteHSRTDLSRDLAAL 285
RasGAP_CLA2_BUD2 cd05137
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ...
1064-1273 1.69e-03

Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein (GAP) for BUD1/RSR1 and is necessary for proper bud-site selection in yeast. BUD2 has sequence similarity to the catalytic domain of RasGAPs, and stimulates the hydrolysis of BUD1-GTP to BUD1-GDP. Elimination of Bud2p activity by mutation causes a random budding pattern with no growth defect. Overproduction of Bud2p also alters the budding pattern.


Pssm-ID: 213339 [Multi-domain]  Cd Length: 356  Bit Score: 42.55  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1064 GQNALRQILAPVVKEIMDDKsLNIKTDPvdiykswvnqmesqtgeaSKLPYDvtpeqalSHEEVKTRLDNSIRNMRAVTD 1143
Cdd:cd05137   114 GKEYLEKSIGDVIRKICEEN-KDCEVDP------------------SRVKES-------DSIEKEEDLEENWENLISLTE 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529 1144 KFLSAIVSSVDKIPYGMRfiaKVLKdSLHEKFPDAAEDELLKIIGN----LLYYRYMNPAIVAPDAFDIIDlsagGQLTT 1219
Cdd:cd05137   168 EIWNSIYITSNDCPPELR---KILK-HIRAKVEDRYGDFLRTVTLNsvsgFLFLRFFCPAILNPKLFGLLK----DHPRP 239
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 210032529 1220 DQRRNLGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQAACDVP 1273
Cdd:cd05137   240 RAQRTLTLIAKVLQNLANLTTFGQKEPWMEPMNEFLTTHREELKDYIDKITGIK 293
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
774-796 1.89e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.92  E-value: 1.89e-03
                            10        20
                    ....*....|....*....|...
gi 210032529    774 KQIPAITCIQSQWRGYKQKKAYQ 796
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
CH_VAV1 cd21262
calponin homology (CH) domain found in VAV1 protein; VAV1 is expressed predominantly in the ...
52-156 5.72e-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: 38.38  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   52 RWMEAClgEDLPPT----------TELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRykatglHFRHTDNVIQWLN 121
Cdd:cd21262     8 HWLIQC--RVLPPNhrvtwdsaqvCDLAQALRDGVLLCQLLNNLLPHAVNLREINLRPQMS------QFLCLKNIRTFLS 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 210032529  122 A-MDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALS 156
Cdd:cd21262    80 TcCEKFGLRKSELFEAFDLFDVRDFGKVIDTLSILS 115
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
778-796 9.08e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.99  E-value: 9.08e-03
                           10
                   ....*....|....*....
gi 210032529   778 AITCIQSQWRGYKQKKAYQ 796
Cdd:pfam00612    3 AAIKIQAAWRGYLARKRYK 21
CH_TAGLN-like cd21209
calponin homology (CH) domain found in the transgelin family; The transgelin (TAGLN) family ...
53-145 9.25e-03

calponin homology (CH) domain found in the transgelin family; The transgelin (TAGLN) family includes transgelin, transgelin-2 and transgelin-3. Transgelin, also called 22 kDa actin-binding protein, protein WS3-10, or smooth muscle protein 22-alpha (SM22-alpha), acts as an actin cross-linking/gelling protein that may be involved in calcium interactions and in regulating contractile properties of the cell. Transgelin-2, also called epididymis tissue protein Li 7e, or SM22-alpha homolog, acts as an actin-binding protein that induces actin gelation and regulates actin cytoskeleton. It may participate in the development and progression of multiple cancers. Transgelin-3, also called neuronal protein 22 (NP22), or neuronal protein NP25, may have a role in alcohol-related adaptations and may mediate regulatory signal transduction pathways in neurons. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409058 [Multi-domain]  Cd Length: 119  Bit Score: 37.88  E-value: 9.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210032529   53 WMEACLGEDL----PPTTELEEGLRNGVYLAKLGN-FFSPKVVSLKKIydreqtryKATGLHFRHTDNVIQWLNAMDEIG 127
Cdd:cd21209    11 WIVAQCGSDVgrpdPGRLGFQKWLKDGTVLCKLINsLYPEGSKPVKKI--------QSSKMAFKQMEQISQFLKAAEDYG 82
                          90
                  ....*....|....*...
gi 210032529  128 LPKIFYPETTDIYDRKNM 145
Cdd:cd21209    83 VRTTDIFQTVDLWEGKDM 100
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
749-766 9.55e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 34.99  E-value: 9.55e-03
                            10
                    ....*....|....*...
gi 210032529    749 ITKLQACCRGYLVRQEFR 766
Cdd:smart00015    6 AIIIQAAWRGYLARKRYK 23
 
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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