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Conserved domains on  [gi|1996008064|ref|XP_039714156|]
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ras GTPase-activating-like protein IQGAP1 [Pteropus giganteus]

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 ...
1123-1502 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: 794.63  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1123 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 1202
Cdd:cd05133      1 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1203 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALAHEEVKTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRF 1282
Cdd:cd05133     81 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQAMSHEEVRTRLDASIKNMRMVTDKFLSAIISSVDKIPYGMRF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1283 IAKVLKDSLHEKFPDAGEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 1362
Cdd:cd05133    161 IAKVLKDTLHEKFPDAGEDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1363 GDNAHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 1442
Cdd:cd05133    241 GDNAHLSPINEYLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 320
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1443 PIHELLDDLGEVPTIESLIGESAGNLNDPNKEALAKTEVSLTLTNKFDVPGDENAEMDAR 1502
Cdd:cd05133    321 PIHELLDDLGEVPTIESLIGENPGPPGDPNRETLAKTEVSLTLTNKFDVPGDENAEMDAR 380
CH_IQGAP1 cd21274
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif ...
157-310 1.03e-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: 339.28  E-value: 1.03e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  157 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 236
Cdd:cd21274      1 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1996008064  237 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKIELE 310
Cdd:cd21274     81 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTELE 154
IQG1 super family cl34962
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
996-1777 8.46e-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: 241.33  E-value: 8.46e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  996 LDQSDQDFQEELDLMKMREEVITLIRSNQQLENDLNLMDIKIGLLVKnkITLQDVVSHskkltkknKEQLSDMMMLNKQK 1075
Cdd:COG5261    290 SNVEQAFFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKRGNKIR--LLIQNRMPQ--------EEDTKFAERLQSNI 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1076 GGLKALSKEKReKLEAYQHLFYLLQTN-PTYL--------------AKLIFQMPQNKSTKFMdsvIFTLYNYASNQREEY 1140
Cdd:COG5261    360 NGRKKYFPLDR-RLSLFGPLFFLLQSSiPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE---IRKLYSLGKSNCEEH 435
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1141 LLLRLFKTALQEEIKSKVDqIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPVDIYKSWVN 1220
Cdd:COG5261    436 LSVSLFQMLLRTEVEATSL-VQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHEDLEVDINPLLVYRALLN 514
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1221 QmesqtgeasklpYDVTPEQALAHEEVKTRLDNSIRNMRAV-----------TDKFLSAIISSVDKIPYGMRFIAKVLK- 1288
Cdd:COG5261    515 K------------GQLSPDKDLELLTSNEEVSEFLAVMNAVqessakllelsTERILDAVYNSLDEIGYGIRFVCELIRv 582
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1289 ------DSLHEKFPDA--------GEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSaggqlTTDQRRNLGSIAKMLQH 1354
Cdd:COG5261    583 vfeltpNRLFPSISDSrclrticfAEIDSLGLIGGFFFLRFVNEALVSPQTSMLKDSC-----PSDNVRKLATLSKILQS 657
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1355 AASNKMFLGdnaHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYIsIGEIINTHTLLLDHQD 1434
Cdd:COG5261    658 VFEITSSDK---FDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYL-VNEIYLTHEIIIEYLD 733
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1435 AI--APEHNDPIHELLDDLGEVPtiesligesagnlnDPNKEALAKTEvSLTLTNKFDVPgdenaemdARTILLNTKRLI 1512
Cdd:COG5261    734 NLydPDSLVDLLLQELGELCSFP--------------QDQRDTLNCLV-TLPLFNRSDDP--------IRDLKQQLKRTR 790
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1513 VDVIRFQPGETLTEILETPATSEQEAEHQRAMQRRAIRDAKTPDKMKkskfvkedsNLTLQEKKEKIQSGLKKLTELGTV 1592
Cdd:COG5261    791 VYIIYVDAGTNLFEQLLRLLPSDEPATRNPLDLNPNIRDDPSVSSLK---------SMSLMKLKIRAIELLDELETLGFV 861
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1593 NPKNKYQELINDIARDIRNQRRYRQRRKAELVKLQQTYAALNSKATFYGEQVDYYKSYIKTCLDNLASKGK----VSKKP 1668
Cdd:COG5261    862 SRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKSklkgFSRGV 941
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1669 REMKGKKSKK--ISLKYTAARLHEKGVLLEIEDLQANqFKNVIFEISpTEEVGDFEVKAKFMG--VQMETFMLHYQDLLQ 1744
Cdd:COG5261    942 GVVRDKPKSIssGTFKYSAQQLYKRGVLVNITIPEPN-VSNIYFTFS-SDSTDNFVIEVYQPGhsVSLPEVSFCFDDLLK 1019
                          810       820       830
                   ....*....|....*....|....*....|...
gi 1996008064 1745 LQYEGVAVMKLFDRAKVNVNLLIFLLNKKFYGK 1777
Cdd:COG5261   1020 RQYNKNPVVDLGGFLTFNANKLLHLIESKFYRK 1052
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
805-832 5.02e-05

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: 41.74  E-value: 5.02e-05
                           10        20
                   ....*....|....*....|....*...
gi 1996008064  805 WAKHWVKGGYYYYHNLETQEGGWDEPPG 832
Cdd:cd00201      4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
894-916 2.62e-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: 2.62e-03
                            10        20
                    ....*....|....*....|...
gi 1996008064   894 KQIPAITCIQSQWRGYKQKKAYQ 916
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 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 ...
1123-1502 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: 794.63  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1123 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 1202
Cdd:cd05133      1 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1203 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALAHEEVKTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRF 1282
Cdd:cd05133     81 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQAMSHEEVRTRLDASIKNMRMVTDKFLSAIISSVDKIPYGMRF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1283 IAKVLKDSLHEKFPDAGEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 1362
Cdd:cd05133    161 IAKVLKDTLHEKFPDAGEDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1363 GDNAHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 1442
Cdd:cd05133    241 GDNAHLSPINEYLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 320
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1443 PIHELLDDLGEVPTIESLIGESAGNLNDPNKEALAKTEVSLTLTNKFDVPGDENAEMDAR 1502
Cdd:cd05133    321 PIHELLDDLGEVPTIESLIGENPGPPGDPNRETLAKTEVSLTLTNKFDVPGDENAEMDAR 380
CH_IQGAP1 cd21274
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif ...
157-310 1.03e-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: 339.28  E-value: 1.03e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  157 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 236
Cdd:cd21274      1 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1996008064  237 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKIELE 310
Cdd:cd21274     81 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTELE 154
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
1145-1357 9.41e-78

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: 256.06  E-value: 9.41e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1145 LFKTALQEEIKSkVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPVDIYKSWVNQMES 1224
Cdd:pfam00616    1 LISELIEEEIES-SDNPNDLLRGNSLVSKLLETYNRRPRGQEYLKKVLGPLVRKIIEDEDLDLESDPRKIYESLINQEEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1225 QTGEaSKLPYDVTPEQALAHEEVKTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRFIAKVLKDSLHEKFPDAGEDELL 1304
Cdd:pfam00616   80 KTGR-SDLPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEIL 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1996008064 1305 KIIGNLLYYRYMNPAIVAPDAFDIIDlsagGQLTTDQRRNLGSIAKMLQHAAS 1357
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVD----HQISPKQRRNLTLIAKVLQNLAN 207
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
1112-1464 2.58e-74

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: 251.84  E-value: 2.58e-74
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  1112 QMPQNKSTKFMDSVIFTLYNYASNQREEYLLLRLFKTALQeeIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQI 1191
Cdd:smart00323    1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLS--LASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRAL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  1192 LAPVVKEIMDD----KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALAHEEVKTR---LDNSIRNMRAVTDK 1264
Cdd:smart00323   79 IDPEVERTDDPntifRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEgedLETNLENLLQYVER 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  1265 FLSAIISSVDKIPYGMRFIAKVLKDSLHEKFPDAgeDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLsaggQLTTDQRRN 1344
Cdd:smart00323  159 LFDAIINSSDRLPYGLRDICKQLRQAAEKRFPDA--DVIYKAVSSFVFLRFFCPAIVSPKLFNLVDE----HPDPTTRRT 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  1345 LGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQTACDVPElqdkFNVDEYSDLVTLTkpviyisIGEIIN 1424
Cdd:smart00323  233 LTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPE----ILVDKVSDSTTIS-------GRELSL 301
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|..
gi 1996008064  1425 THTLLLDHQDAIAPEHN--DPIHELLDDLGEVPTIESLIGES 1464
Cdd:smart00323  302 LHSLLLENGDALKRELNneDPLGKLLFKLRYFGLTTHELTYG 343
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
996-1777 8.46e-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: 241.33  E-value: 8.46e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  996 LDQSDQDFQEELDLMKMREEVITLIRSNQQLENDLNLMDIKIGLLVKnkITLQDVVSHskkltkknKEQLSDMMMLNKQK 1075
Cdd:COG5261    290 SNVEQAFFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKRGNKIR--LLIQNRMPQ--------EEDTKFAERLQSNI 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1076 GGLKALSKEKReKLEAYQHLFYLLQTN-PTYL--------------AKLIFQMPQNKSTKFMdsvIFTLYNYASNQREEY 1140
Cdd:COG5261    360 NGRKKYFPLDR-RLSLFGPLFFLLQSSiPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE---IRKLYSLGKSNCEEH 435
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1141 LLLRLFKTALQEEIKSKVDqIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPVDIYKSWVN 1220
Cdd:COG5261    436 LSVSLFQMLLRTEVEATSL-VQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHEDLEVDINPLLVYRALLN 514
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1221 QmesqtgeasklpYDVTPEQALAHEEVKTRLDNSIRNMRAV-----------TDKFLSAIISSVDKIPYGMRFIAKVLK- 1288
Cdd:COG5261    515 K------------GQLSPDKDLELLTSNEEVSEFLAVMNAVqessakllelsTERILDAVYNSLDEIGYGIRFVCELIRv 582
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1289 ------DSLHEKFPDA--------GEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSaggqlTTDQRRNLGSIAKMLQH 1354
Cdd:COG5261    583 vfeltpNRLFPSISDSrclrticfAEIDSLGLIGGFFFLRFVNEALVSPQTSMLKDSC-----PSDNVRKLATLSKILQS 657
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1355 AASNKMFLGdnaHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYIsIGEIINTHTLLLDHQD 1434
Cdd:COG5261    658 VFEITSSDK---FDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYL-VNEIYLTHEIIIEYLD 733
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1435 AI--APEHNDPIHELLDDLGEVPtiesligesagnlnDPNKEALAKTEvSLTLTNKFDVPgdenaemdARTILLNTKRLI 1512
Cdd:COG5261    734 NLydPDSLVDLLLQELGELCSFP--------------QDQRDTLNCLV-TLPLFNRSDDP--------IRDLKQQLKRTR 790
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1513 VDVIRFQPGETLTEILETPATSEQEAEHQRAMQRRAIRDAKTPDKMKkskfvkedsNLTLQEKKEKIQSGLKKLTELGTV 1592
Cdd:COG5261    791 VYIIYVDAGTNLFEQLLRLLPSDEPATRNPLDLNPNIRDDPSVSSLK---------SMSLMKLKIRAIELLDELETLGFV 861
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1593 NPKNKYQELINDIARDIRNQRRYRQRRKAELVKLQQTYAALNSKATFYGEQVDYYKSYIKTCLDNLASKGK----VSKKP 1668
Cdd:COG5261    862 SRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKSklkgFSRGV 941
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1669 REMKGKKSKK--ISLKYTAARLHEKGVLLEIEDLQANqFKNVIFEISpTEEVGDFEVKAKFMG--VQMETFMLHYQDLLQ 1744
Cdd:COG5261    942 GVVRDKPKSIssGTFKYSAQQLYKRGVLVNITIPEPN-VSNIYFTFS-SDSTDNFVIEVYQPGhsVSLPEVSFCFDDLLK 1019
                          810       820       830
                   ....*....|....*....|....*....|...
gi 1996008064 1745 LQYEGVAVMKLFDRAKVNVNLLIFLLNKKFYGK 1777
Cdd:COG5261   1020 RQYNKNPVVDLGGFLTFNANKLLHLIESKFYRK 1052
RasGAP_C pfam03836
RasGAP C-terminus; This domain can be found in the C terminus of the IQGAP family members, ...
1572-1701 9.75e-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: 138.45  E-value: 9.75e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1572 LQEKKEKIQSGLKKLTELGTVNPKNKYQELINDIARDIRNQRRYRQRRKAELVKLQQTYAALNSKATFYGEQVDYYKSYI 1651
Cdd:pfam03836    1 YVELKKKALENLLELESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYI 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1996008064 1652 KTCLDNLASKGKVS-------KKPREMKGKKSKKISLKYTAARLHEKGVLLEIEDLQ 1701
Cdd:pfam03836   81 ENCLDNLQKKKKKLfskqyfhYRKLQKRGKLPKFGSYKYSARQLYEKGVLLEIEGVP 137
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
146-334 3.77e-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: 146.95  E-value: 3.77e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  146 LTAEEMDERRRQNVAYEYLCHLEEAKRWMEACLGEDLPpTTELEEGLRNGVYLAKLGNFFSPKvvSLKKIYdreqtryKA 225
Cdd:COG5261     25 LKTKTSAKNRSALRAYEYLCRVSEAKIWIEEVIEEALP-ELCFEDSLRNGVFLAKLTQRFNPD--LTTVIF-------PA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  226 TGLHFRHTDNVIQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVdFTEEEINNM 305
Cdd:COG5261     95 DKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTPLINSSGQIS-FTKEDIAAC 173
                          170       180
                   ....*....|....*....|....*....
gi 1996008064  306 KIELEkygiQMPAFSKIGGILANELSVDE 334
Cdd:COG5261    174 KKAWP----RIPDFKSLGTNINTAASPEE 198
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
168-278 2.48e-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: 73.47  E-value: 2.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  168 EEAKRWMEACLGEDLPPT--TELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREqtrykatglhFRHTDNVIQWLN-AMD 244
Cdd:pfam00307    5 KELLRWINSHLAEYGPGVrvTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSE----------FDKLENINLALDvAEK 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1996008064  245 EIGLPKIFyPETTDIYDRKNMpRCIYCIHALSLY 278
Cdd:pfam00307   75 KLGVPKVL-IEPEDLVEGDNK-SVLTYLASLFRR 106
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
168-275 4.79e-15

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: 72.35  E-value: 4.79e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064   168 EEAKRWMEACLGEDLPPT-TELEEGLRNGVYLAKLGNFFSPKVVSLKKIydreqtryKATGLHFRHTDNVIQWLNAMDEI 246
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPvTNFSSDLKDGVALCALLNSLSPGLVDKKKV--------AASLSRFKKIENINLALSFAEKL 72
                            90       100       110
                    ....*....|....*....|....*....|
gi 1996008064   247 GlPKIFYPETTDIYD-RKNMPRCIYCIHAL 275
Cdd:smart00033   73 G-GKVVLFEPEDLVEgPKLILGVIWTLISL 101
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
805-832 5.02e-05

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: 41.74  E-value: 5.02e-05
                           10        20
                   ....*....|....*....|....*...
gi 1996008064  805 WAKHWVKGGYYYYHNLETQEGGWDEPPG 832
Cdd:cd00201      4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
805-832 9.29e-05

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 41.05  E-value: 9.29e-05
                            10        20
                    ....*....|....*....|....*...
gi 1996008064   805 WAKHWVKGGYYYYHNLETQEGGWDEPPG 832
Cdd:smart00456    6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
894-916 2.62e-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: 2.62e-03
                            10        20
                    ....*....|....*....|...
gi 1996008064   894 KQIPAITCIQSQWRGYKQKKAYQ 916
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 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 ...
1123-1502 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: 794.63  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1123 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 1202
Cdd:cd05133      1 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1203 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALAHEEVKTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRF 1282
Cdd:cd05133     81 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQAMSHEEVRTRLDASIKNMRMVTDKFLSAIISSVDKIPYGMRF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1283 IAKVLKDSLHEKFPDAGEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 1362
Cdd:cd05133    161 IAKVLKDTLHEKFPDAGEDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1363 GDNAHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 1442
Cdd:cd05133    241 GDNAHLSPINEYLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 320
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1443 PIHELLDDLGEVPTIESLIGESAGNLNDPNKEALAKTEVSLTLTNKFDVPGDENAEMDAR 1502
Cdd:cd05133    321 PIHELLDDLGEVPTIESLIGENPGPPGDPNRETLAKTEVSLTLTNKFDVPGDENAEMDAR 380
RasGAP_IQGAP2 cd05131
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...
1123-1474 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: 668.24  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1123 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 1202
Cdd:cd05131      1 DTVIFTLYNYASNQREEYLLLKLFETALEEEIKSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1203 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALAHEEVKTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRF 1282
Cdd:cd05131     81 KSLIINTNPVEVYKAWVNQLETATGEASKLPYDVTTEQALTHPEVVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1283 IAKVLKDSLHEKFPDAGEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 1362
Cdd:cd05131    161 IAKVLKNSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHSEQRRNLGSVAKVLQHAASNKLFE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1363 GDNAHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 1442
Cdd:cd05131    241 GENAHLSSMNSYLSQTYQKFRKFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIAPDQND 320
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1996008064 1443 PIHELLDDLGEVPTIESLIGESAGNLNDPNKE 1474
Cdd:cd05131    321 LLHELLKDLGEVPDVESFLGEGTVDPNDPNKE 352
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
1133-1463 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: 604.19  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1133 ASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPV 1212
Cdd:cd05127      1 ASNRREEYLLLKLFKTALREEIESKVSLPEDIVTGNPTVIKLVVNYNRGPRGQKYLRELLGPVVKEILDDDDLDLETDPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1213 DIYKSWVNQMESQTGEASKLPYDVTPEQALAHEEVKTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRFIAKVLKDSLH 1292
Cdd:cd05127     81 DIYKAWINQEESRTGEPSKLPYDVTREQALKDPEVRKRLIEHLEKLRAITDKFLTAITESLDKMPYGMRYIAKVLKEALR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1293 EKFPDAGEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFLGDNAHLSIIN 1372
Cdd:cd05127    161 EKFPDAPEEEILKIVGNLLYYRYMNPAIVAPEAFDIIDLSVGGQLSPLQRRNLGSIAKVLQQAASGKLFGGENPYLSPLN 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1373 EYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHNDPIHELLDDLG 1452
Cdd:cd05127    241 PYISESHEKFKKFFLEACTVPEAEEHFNIDEYSDLTMLTKPTIYISLQEIFATHKLLLEHQDEIAPDPDDPLRELLDDLG 320
                          330
                   ....*....|.
gi 1996008064 1453 EVPTIESLIGE 1463
Cdd:cd05127    321 PAPTIESLLGS 331
RasGAP_IQGAP3 cd12207
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ...
1123-1470 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: 584.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1123 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 1202
Cdd:cd12207      1 ESVIFSLYNYASNRREAYLLLQLFKTALQEEISSKVEKPQDVITGNPTVIRLLVSFYRSARGQNALRHILGPVVQDVLQD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1203 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALAHEEVKTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRF 1282
Cdd:cd12207     81 KGLSIRTDPVQIYKAWINQTETQSGCRSSLPYEVSPEQALSHPEVQRRLDIAIRNLLAVTDKFLSAITSSVDKIPYGMRY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1283 IAKVLKDSLHEKFPDAGEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 1362
Cdd:cd12207    161 VAKVLRDSLQEKFPGASEDEVYKVVGNLLYYRFMNPAVVAPDGFDIVDCSAGGALQPEQRRMLGSVAKVLQHAAANKHFQ 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1363 GDNAHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 1442
Cdd:cd12207    241 GDSEHLQALNQYLEETHVKFRKFILQACCVPEPEERFNVDEYSEMVAVAKPVIYITVGELINTHKLLLEHQDSIAPDHSD 320
                          330       340
                   ....*....|....*....|....*...
gi 1996008064 1443 PIHELLDDLGEVPTIESLIGESAGNLND 1470
Cdd:cd12207    321 PLHELLEDLGEVPTVQSLIGESWADLGD 348
CH_IQGAP1 cd21274
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif ...
157-310 1.03e-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: 339.28  E-value: 1.03e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  157 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 236
Cdd:cd21274      1 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1996008064  237 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKIELE 310
Cdd:cd21274     81 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTELE 154
CH_IQGAP2 cd21275
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP2; IQ motif ...
134-289 5.38e-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: 5.38e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  134 RPHYGSVLDNERLTAEEMDERRRQNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLK 213
Cdd:cd21275      1 RPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKQWIEACLNEELPPTTELEEGLRNGVYLVKLAKFFAPKLVSEK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1996008064  214 KIYDREQTRYKATGLHFRHTDNVIQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQ 289
Cdd:cd21275     81 KIYDVDQVRYKRSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNMPRVIYCIHALSLYLFKLGIAPQIQ 156
CH_IQGAP3 cd21276
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP3; IQ motif ...
158-309 3.28e-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: 3.28e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  158 NVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNVI 237
Cdd:cd21276      1 NVAYQYLCRLEEAKRWMEACLKEELPPPTELEESLRNGVYLAKLGHCFAPRVVPLKKIYDLEQMRYQATGLHFRHTDNIN 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1996008064  238 QWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKIEL 309
Cdd:cd21276     81 HWRNAMMHIGLPSIFHPETTDIYDKKNMPRVVYCIHALSLYLFRLGLAPQIHDLYGKVKFTEEEINNMKLEL 152
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
1145-1357 9.41e-78

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: 256.06  E-value: 9.41e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1145 LFKTALQEEIKSkVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPVDIYKSWVNQMES 1224
Cdd:pfam00616    1 LISELIEEEIES-SDNPNDLLRGNSLVSKLLETYNRRPRGQEYLKKVLGPLVRKIIEDEDLDLESDPRKIYESLINQEEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1225 QTGEaSKLPYDVTPEQALAHEEVKTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRFIAKVLKDSLHEKFPDAGEDELL 1304
Cdd:pfam00616   80 KTGR-SDLPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEIL 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1996008064 1305 KIIGNLLYYRYMNPAIVAPDAFDIIDlsagGQLTTDQRRNLGSIAKMLQHAAS 1357
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVD----HQISPKQRRNLTLIAKVLQNLAN 207
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
1112-1464 2.58e-74

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: 251.84  E-value: 2.58e-74
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  1112 QMPQNKSTKFMDSVIFTLYNYASNQREEYLLLRLFKTALQeeIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQI 1191
Cdd:smart00323    1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLS--LASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRAL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  1192 LAPVVKEIMDD----KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALAHEEVKTR---LDNSIRNMRAVTDK 1264
Cdd:smart00323   79 IDPEVERTDDPntifRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEgedLETNLENLLQYVER 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  1265 FLSAIISSVDKIPYGMRFIAKVLKDSLHEKFPDAgeDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLsaggQLTTDQRRN 1344
Cdd:smart00323  159 LFDAIINSSDRLPYGLRDICKQLRQAAEKRFPDA--DVIYKAVSSFVFLRFFCPAIVSPKLFNLVDE----HPDPTTRRT 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  1345 LGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQTACDVPElqdkFNVDEYSDLVTLTkpviyisIGEIIN 1424
Cdd:smart00323  233 LTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPE----ILVDKVSDSTTIS-------GRELSL 301
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|..
gi 1996008064  1425 THTLLLDHQDAIAPEHN--DPIHELLDDLGEVPTIESLIGES 1464
Cdd:smart00323  302 LHSLLLENGDALKRELNneDPLGKLLFKLRYFGLTTHELTYG 343
CH_IQGAP cd21206
calponin homology (CH) domain found in the IQ motif containing GTPase activating protein ...
158-283 3.70e-71

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: 233.27  E-value: 3.70e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  158 NVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDreqtrykaTGLHFRHTDNVI 237
Cdd:cd21206      1 TIAYEYLCRLEEAKQWIEACLNEELPPTTEFEEELRNGVVLAKLANKFAPKLVPLKKIYD--------VGLQFRHTDNIN 72
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1996008064  238 QWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLG 283
Cdd:cd21206     73 HFLRALKKIGLPKIFHFETTDLYEKKNIPKVIYCLHALSLLLFKLG 118
RasGAP_GAPA cd05132
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...
1121-1455 1.53e-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: 235.32  E-value: 1.53e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1121 FMDSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDqIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIM 1200
Cdd:cd05132      5 LLQTVMFTLYGNQYESREEHLLLSMFQSVLTYEFDETTE-FGSLLRANTAVSRMMTTYTRRGPGQSYLKTVLADRINDLI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1201 DDKSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALAHEEVKTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGM 1280
Cdd:cd05132     84 SLKDLNLEINPLKVYEQMINDIELDTGLPSNLPRGITPEEAAENPAVQNIIEPRLEMLEEITNSFLEAIINSLDEVPYGI 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1281 RFIAKVLKDSLHEKFPDAGEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDlsagGQLTTDQRRNLGSIAKMLQHAASNKM 1360
Cdd:cd05132    164 RWICKQIRSLTRRKFPDASDETICSLIGGFFLLRFINPAIVSPQAYMLVD----GKPSDNTRRTLTLIAKLLQNLANKPS 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1361 FlGDNAHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYsdlVTLTKPVIYISI--GEIINTHTLLLDHQDAIAP 1438
Cdd:cd05132    240 Y-SKEPYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQY---IALSKKDLSINItlNEIYNTHSLLVKHLAELAP 315
                          330
                   ....*....|....*..
gi 1996008064 1439 EHNDPIHELLDDLGEVP 1455
Cdd:cd05132    316 DHNDHLRLILQELGPAP 332
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
996-1777 8.46e-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: 241.33  E-value: 8.46e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  996 LDQSDQDFQEELDLMKMREEVITLIRSNQQLENDLNLMDIKIGLLVKnkITLQDVVSHskkltkknKEQLSDMMMLNKQK 1075
Cdd:COG5261    290 SNVEQAFFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKRGNKIR--LLIQNRMPQ--------EEDTKFAERLQSNI 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1076 GGLKALSKEKReKLEAYQHLFYLLQTN-PTYL--------------AKLIFQMPQNKSTKFMdsvIFTLYNYASNQREEY 1140
Cdd:COG5261    360 NGRKKYFPLDR-RLSLFGPLFFLLQSSiPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE---IRKLYSLGKSNCEEH 435
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1141 LLLRLFKTALQEEIKSKVDqIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPVDIYKSWVN 1220
Cdd:COG5261    436 LSVSLFQMLLRTEVEATSL-VQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHEDLEVDINPLLVYRALLN 514
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1221 QmesqtgeasklpYDVTPEQALAHEEVKTRLDNSIRNMRAV-----------TDKFLSAIISSVDKIPYGMRFIAKVLK- 1288
Cdd:COG5261    515 K------------GQLSPDKDLELLTSNEEVSEFLAVMNAVqessakllelsTERILDAVYNSLDEIGYGIRFVCELIRv 582
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1289 ------DSLHEKFPDA--------GEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSaggqlTTDQRRNLGSIAKMLQH 1354
Cdd:COG5261    583 vfeltpNRLFPSISDSrclrticfAEIDSLGLIGGFFFLRFVNEALVSPQTSMLKDSC-----PSDNVRKLATLSKILQS 657
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1355 AASNKMFLGdnaHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYIsIGEIINTHTLLLDHQD 1434
Cdd:COG5261    658 VFEITSSDK---FDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYL-VNEIYLTHEIIIEYLD 733
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1435 AI--APEHNDPIHELLDDLGEVPtiesligesagnlnDPNKEALAKTEvSLTLTNKFDVPgdenaemdARTILLNTKRLI 1512
Cdd:COG5261    734 NLydPDSLVDLLLQELGELCSFP--------------QDQRDTLNCLV-TLPLFNRSDDP--------IRDLKQQLKRTR 790
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1513 VDVIRFQPGETLTEILETPATSEQEAEHQRAMQRRAIRDAKTPDKMKkskfvkedsNLTLQEKKEKIQSGLKKLTELGTV 1592
Cdd:COG5261    791 VYIIYVDAGTNLFEQLLRLLPSDEPATRNPLDLNPNIRDDPSVSSLK---------SMSLMKLKIRAIELLDELETLGFV 861
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1593 NPKNKYQELINDIARDIRNQRRYRQRRKAELVKLQQTYAALNSKATFYGEQVDYYKSYIKTCLDNLASKGK----VSKKP 1668
Cdd:COG5261    862 SRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKSklkgFSRGV 941
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1669 REMKGKKSKK--ISLKYTAARLHEKGVLLEIEDLQANqFKNVIFEISpTEEVGDFEVKAKFMG--VQMETFMLHYQDLLQ 1744
Cdd:COG5261    942 GVVRDKPKSIssGTFKYSAQQLYKRGVLVNITIPEPN-VSNIYFTFS-SDSTDNFVIEVYQPGhsVSLPEVSFCFDDLLK 1019
                          810       820       830
                   ....*....|....*....|....*....|...
gi 1996008064 1745 LQYEGVAVMKLFDRAKVNVNLLIFLLNKKFYGK 1777
Cdd:COG5261   1020 RQYNKNPVVDLGGFLTFNANKLLHLIESKFYRK 1052
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
1138-1391 1.20e-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: 145.71  E-value: 1.20e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1138 EEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSL----NIKTDPVD 1213
Cdd:cd04519      1 EEYRLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNTKNPNTLfrgnSLATKLLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1214 IYKSWVNQmESQTGEASKLPYDVTPEQAL----AHEEVKTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRFIAKVLKD 1289
Cdd:cd04519     81 QYMKLVGQ-EYLKETLSPLIREILESKESceidTKLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILRE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1290 SLHEKFPDAgEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDlsagGQLTTDQRRNLGSIAKMLQHAASNKMFLGDNAHLS 1369
Cdd:cd04519    160 FLAERFPEE-PDEAYQAVSGFLFLRFICPAIVSPELFGLVP----DEPSEQARRNLTLISKVLQSLANGVEFGDKEPFMK 234
                          250       260
                   ....*....|....*....|..
gi 1996008064 1370 IINEYLSQSYQKFRRFFQTACD 1391
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, ...
1572-1701 9.75e-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: 138.45  E-value: 9.75e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1572 LQEKKEKIQSGLKKLTELGTVNPKNKYQELINDIARDIRNQRRYRQRRKAELVKLQQTYAALNSKATFYGEQVDYYKSYI 1651
Cdd:pfam03836    1 YVELKKKALENLLELESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYI 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1996008064 1652 KTCLDNLASKGKVS-------KKPREMKGKKSKKISLKYTAARLHEKGVLLEIEDLQ 1701
Cdd:pfam03836   81 ENCLDNLQKKKKKLfskqyfhYRKLQKRGKLPKFGSYKYSARQLYEKGVLLEIEGVP 137
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
146-334 3.77e-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: 146.95  E-value: 3.77e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  146 LTAEEMDERRRQNVAYEYLCHLEEAKRWMEACLGEDLPpTTELEEGLRNGVYLAKLGNFFSPKvvSLKKIYdreqtryKA 225
Cdd:COG5261     25 LKTKTSAKNRSALRAYEYLCRVSEAKIWIEEVIEEALP-ELCFEDSLRNGVFLAKLTQRFNPD--LTTVIF-------PA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  226 TGLHFRHTDNVIQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVdFTEEEINNM 305
Cdd:COG5261     95 DKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTPLINSSGQIS-FTKEDIAAC 173
                          170       180
                   ....*....|....*....|....*....
gi 1996008064  306 KIELEkygiQMPAFSKIGGILANELSVDE 334
Cdd:COG5261    174 KKAWP----RIPDFKSLGTNINTAASPEE 198
RasGAP_IQGAP_related cd12206
Ras-GTPase Activating Domain of proteins related to IQGAPs; RasGAP: Ras-GTPase Activating ...
1131-1454 1.34e-34

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


Pssm-ID: 213345 [Multi-domain]  Cd Length: 359  Bit Score: 137.07  E-value: 1.34e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1131 NYASNQREEYLLLRLFKTALQEEIKsKVDQIQEIVTGNPTV-IKMVVSFNRgaRGQNALRQ-ILAPVVKEIMDDKSLNIK 1208
Cdd:cd12206     20 NGKMDSREEFLFIKFILELLKSDIE-NSNSNQDFLANSDNFwILLLVTFNN--LRERSELKsIFGPLLVQYLENQEIDFE 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1209 TDPVDIYKSWVNQMesqtgeasklpyDVTPEQALAHEEVKTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRFIAKVLK 1288
Cdd:cd12206     97 SDPSVIYKSLHGRP------------PLSSEEAIEDDRVSDKFVENLTNLREAVEMVAEIIFKNVDKIPVEIRYLCTKAY 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1289 DSLHEKFPDAGEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDlsaggqlttDQRRNLGSIAKMLQHAASNKMFLG-DNAH 1367
Cdd:cd12206    165 IAFADKFPDESEEDILRAISKILIKSYVAPILVNPENYGFVD---------NEEDNLNEKARVLLQILSMVFFLKnFDGY 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1368 LSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPehNDPIHEL 1447
Cdd:cd12206    236 LKPLNQYIEEIKPSIRDLLKELLDVPEEEQEYDKLIYYDIMSTTRPCLEILLDKVIEIIQILKENLDEFTP--DDQLVQL 313

                   ....*..
gi 1996008064 1448 LDDLGEV 1454
Cdd:cd12206    314 LEKIVDL 320
RasGAP_Neurofibromin_like cd05392
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...
1087-1464 1.45e-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: 130.10  E-value: 1.45e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1087 EKLEAYQHLFYLLQTNPTylakLIFQMPQNKSTKFMDS---VIFTLYNYASNqreeylLLRLFKTALQEEIkSKVDQIQE 1163
Cdd:cd05392      1 KKSEAYDELLELLIEDPQ----LLLAIAEVCPSSEVDLlaqSLLNLFETRNR------LLPLISWLIEDEI-SHTSRAAD 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1164 IVTGNPTVIKMVVSFNRgARGQNALRQILAPVVKEIMDDKSLN--IKTDPVDiykswvnqmesqtgeasklpydvtpeqa 1241
Cdd:cd05392     70 LFRRNSVATRLLTLYAK-SVGNKYLRKVLRPLLTEIVDNKDYFevEKIKPDD---------------------------- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1242 lahEEVKTRLDNsirnMRAVTDKFLSAIISSVDKIPYGMRFIAKVLKDSLHEKFPDAGedelLKIIGNLLYYRYMNPAIV 1321
Cdd:cd05392    121 ---ENLEENADL----LMKYAQMLLDSITDSVDQLPPSFRYICNTIYESVSKKFPDAA----LIAVGGFLFLRFICPAIV 189
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1322 APDAFDIIDLSAggqlTTDQRRNLGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQTACDVPElqdkfnv 1401
Cdd:cd05392    190 SPESENLLDPPP----TPEARRSLILIAKVLQNIANGVLFSLKEPYLESLNEFLKKNSDRIQQFLSEVSTIPP------- 258
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1996008064 1402 DEYSDLVTLTKPViyisIGEIINTHTLLLDHQDAIAPEHNDPIhELLDDLGEVPTIESLIGES 1464
Cdd:cd05392    259 TDPIFDESDEEPI----TADLRYLHKFLYLHFLEIRKEVLKGS-SSQGSDKELVETFKLIDEI 316
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
167-277 4.78e-26

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: 103.96  E-value: 4.78e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  167 LEEAKRWMEACLGEDLP-PTTELEEGLRNGVYLAKLGNFFSPKVVSLKKiydreqtryKATGLHFRHTDNVIQWLNAMDE 245
Cdd:cd00014      1 EEELLKWINEVLGEELPvSITDLFESLRDGVLLCKLINKLSPGSIPKIN---------KKPKSPFKKRENINLFLNACKK 71
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1996008064  246 IGLPKIFYPETTDIYDRKNMPRCIYCIHALSL 277
Cdd:cd00014     72 LGLPELDLFEPEDLYEKGNLKKVLGTLWALAL 103
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
1249-1437 1.10e-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: 80.44  E-value: 1.10e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1249 TRLDNS------IRNMRAVTDKFLSAIISSVDKIPYGMRFIAKVLKDSLHEKFPDAGedelLKIIGNLLYYRYMNPAIVA 1322
Cdd:cd05130    125 TRLEGNenleenQRNLLQLTEKFFHAIISSSDEFPPQLRSVCHCLYQVVSHRFPNSG----LGAVGSAIFLRFINPAIVS 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1323 PDAFDIIDlsagGQLTTDQRRNLGSIAKMLQHAASNKMFLGDnAHLSIINEYLSQSYQKFRRFFQTACDvpelqDKFNVD 1402
Cdd:cd05130    201 PYEYGILD----REPPPRVKRGLKLMSKILQNIANHVLFTKE-AHMLPFNDFLRNHFEAGRRFFSSIAS-----DCGAVD 270
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1996008064 1403 EYSDlvtltKPVIYISIGEIINTHTLLLDHQDAIA 1437
Cdd:cd05130    271 GPSS-----KYLSFINDANVLALHRLLWNNQEKIG 300
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
168-278 2.48e-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: 73.47  E-value: 2.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  168 EEAKRWMEACLGEDLPPT--TELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREqtrykatglhFRHTDNVIQWLN-AMD 244
Cdd:pfam00307    5 KELLRWINSHLAEYGPGVrvTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSE----------FDKLENINLALDvAEK 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1996008064  245 EIGLPKIFyPETTDIYDRKNMpRCIYCIHALSLY 278
Cdd:pfam00307   75 KLGVPKVL-IEPEDLVEGDNK-SVLTYLASLFRR 106
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
168-275 4.79e-15

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: 72.35  E-value: 4.79e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064   168 EEAKRWMEACLGEDLPPT-TELEEGLRNGVYLAKLGNFFSPKVVSLKKIydreqtryKATGLHFRHTDNVIQWLNAMDEI 246
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPvTNFSSDLKDGVALCALLNSLSPGLVDKKKV--------AASLSRFKKIENINLALSFAEKL 72
                            90       100       110
                    ....*....|....*....|....*....|
gi 1996008064   247 GlPKIFYPETTDIYD-RKNMPRCIYCIHAL 275
Cdd:smart00033   73 G-GKVVLFEPEDLVEgPKLILGVIWTLISL 101
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
169-275 5.87e-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: 69.65  E-value: 5.87e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  169 EAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKvvSLKKIydreqtryKATGLHFRHTDNVIQWLNAMDEIGL 248
Cdd:cd21207      9 EALDWIEAVTGEKLDDGKDYEDVLKDGVILCKLINILKPG--SVKKI--------NTSKMAFKLMENIENFLTACKGYGV 78
                           90       100
                   ....*....|....*....|....*..
gi 1996008064  249 PKIFYPETTDIYDRKNMPRCIYCIHAL 275
Cdd:cd21207     79 PKTDLFQTVDLYEKKNIPQVTNCLFAL 105
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
168-276 5.28e-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: 66.62  E-value: 5.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  168 EEAKRWMEACLGEDLPPTTeLEEGLRNGVYLAKLGNffspkvvslkKIYDREQTRYKATGLHFRHTDNVIQWLNAMDEIG 247
Cdd:cd21210      3 QEAREWIEEVLGEKLAQGD-LLDALKDGVVLCKLAN----------RILPADIRKYKESKMPFVQMENISAFLNAARKLG 71
                           90       100
                   ....*....|....*....|....*....
gi 1996008064  248 LPKIFYPETTDIYDRKNMPRCIYCIHALS 276
Cdd:cd21210     72 VPENDLFQTVDLFERKNPAQVLQCLHALS 100
RasGAP_RAP6 cd05129
Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is ...
1090-1442 1.15e-09

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: 62.36  E-value: 1.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1090 EAYQHLFY----------LLQTNPTYLAKLIFQMPQ--NKSTKFMDSVIFT-LYNYASNQREEYLLLRLFKTALQEEIKS 1156
Cdd:cd05129      1 DAYKLLGYqlshygeflrILRENPQLLAECLARGEKlsLEQTQNVIQTIVTsLYGNCIMPEDERLLLQLLRELMELQLKK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1157 KVDQIQEIVTGNPTVIKMVVSFNRGARGQN-----ALRQilaPVVKEIMDDkSLNIKTDPVD-IYKSWVNQMESQTGEas 1230
Cdd:cd05129     81 SDNPRRLLRKGSCAFSRVFKLFTELLFSAKlyltaALHK---PIMQVLVDD-EIFLETDPQKaLCRFSPAEQEKRFGE-- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1231 klpyDVTPEQalaHEEVKTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRFIAKVLKDSLHEKFPDagEDELLK-IIGN 1309
Cdd:cd05129    155 ----EGTPEQ---QRKLQQYRAEFLSRLVALVNKFISSLRQSVYCFPQSLRWIVRQLRKILTRSGDD--EEAEARaLCTD 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1310 LLYYRYMNPAIVAPDAFDIIDLSAGGQLTtdqRRNLGSIAKMLQHAASNKMFLGDNahlsiineYLSQSYQKFRR----F 1385
Cdd:cd05129    226 LLFTNFICPAIVNPEQYGIISDAPISEVA---RHNLMQVAQILQVLALTEFESPDP--------RLKELLSKFDKdcvsA 294
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1996008064 1386 FQTACDVPELQDKFNVDEySDLVTLTKPVIYISIGEiINTHTLLLDHQDAIAPEHND 1442
Cdd:cd05129    295 FLDVVIVGRAVETPPPSS-SALLEGSRTAVLITESD-LATLVEFLRSVKTGDEEKED 349
SCP1 COG5199
Calponin [Cytoskeleton];
168-288 1.69e-09

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 58.78  E-value: 1.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  168 EEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVslkkiydreqtRYKATGLHFRHTDNVIQWLNAMDEIG 247
Cdd:COG5199     16 KEVTLWIETVLGEKFEPPGDLLSLLKDGVRLCRILNEASPLDI-----------KYKESKMPFVQMENISSFINGLKKLR 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1996008064  248 LPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKL------GLAPQI 288
Cdd:COG5199     85 VPEYELFQTNDLFEAKDLRQVVICLYSLSRYAQKErmfsgpFLGPHL 131
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
168-275 2.33e-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: 2.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  168 EEAKRWMEACLGEDLPPTT---ELEEGLRNGVYLAKLGNFFSPKVVSlkKIYDREQTRYKATGLHFRHTDNVIQWLNAMD 244
Cdd:cd21203      3 YEAAEWIQNVLGVLVLPDPseeEFRLCLRDGVVLCKLLNKLQPGAVP--KVVESPDDPDGAAGSAFQYFENVRNFLVAIE 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1996008064  245 EIGLPkIFYPETTDIYDRKNMPRCIYCIHAL 275
Cdd:cd21203     81 EMGLP-TFEASDLEQGGGGSRPRVVDCILAL 110
RasGAP_RASAL cd05135
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...
1188-1353 1.22e-08

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


Pssm-ID: 213337  Cd Length: 287  Bit Score: 58.29  E-value: 1.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1188 LRQILAPVVKEIMDDKSLnIKTDPVDIykswvnqMESQTGEASKlpydvtpEQALAHEEVktrLDNSIRNMRAVTDKFLS 1267
Cdd:cd05135    101 LHEVLKPVINRIFEEKKY-VELDPCKI-------DLNRTRRISF-------KGSLSEAQV---RESSLELLQGYLGSIID 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1268 AIISSVDKIPYGMRFIAKVLKDSLHEKFPDAGEDELLKI-IGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTtdqrRNLG 1346
Cdd:cd05135    163 AIVGSVDQCPPVMRVAFKQLHKRVEERFPEAEHQDVKYLaISGFLFLRFFAPAILTPKLFQLREQHADPRTS----RTLL 238

                   ....*..
gi 1996008064 1347 SIAKMLQ 1353
Cdd:cd05135    239 LLAKAVQ 245
RasGAP_GAP1_like cd05128
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...
1141-1354 1.72e-07

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


Pssm-ID: 213330  Cd Length: 269  Bit Score: 54.56  E-value: 1.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1141 LLLRLFKTALQEEIkSKVDQIQEIVTGNPTVIKMVVSFNRGArGQNALRQILAPVVKEIMDD-KSLNIktDPvdiykswv 1219
Cdd:cd05128     51 QIVPLLRALASREI-SKTQDPNTLFRGNSLASKCMDEFMKLV-GMQYLHETLKPVIDEIFSEkKSCEI--DP-------- 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1220 nqmesqtgeaSKLPYdvtpeqalaheevKTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRFIAKVLKDSLHEKFPDAG 1299
Cdd:cd05128    119 ----------SKLKD-------------GEVLETNLANLRGYVERVFKAITSSARRCPTLMCEIFSDLRESAAQRFPDNE 175
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1300 EDELLKIIGnLLYYRYMNPAIVAPDAFDiidlsaggqLTTDQ-----RRNLGSIAKMLQH 1354
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 ...
167-261 2.52e-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: 2.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  167 LEEAKRWMEACLGEDLPPtTELEEGLRNGVYLAKLGNFFSPKvvSLKKIyDREQTRYkaTGLhfrhtDNVIQWLNAMDEI 246
Cdd:cd21208      2 LKEARTWIEAVTGKKFPS-DDFRESLEDGILLCELINAIKPG--SIKKI-NRLPTPI--AGL-----DNLNLFLKACEDL 70
                           90
                   ....*....|....*
gi 1996008064  247 GLPKIFYPETTDIYD 261
Cdd:cd21208     71 GLKDSQLFDPTDLQD 85
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
1256-1468 2.37e-05

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: 48.35  E-value: 2.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1256 RNMRAVTDKFLSAIISSVDKIPygmrfiaKVLKD---SLHEKFPDAGEDELL-KIIGNLLYYRYMNPAIVAPDAFDIIdl 1331
Cdd:cd05136    137 ANLRRSVELAWCKILSSHCVFP-------RELREvfsSWRERLEERGREDIAdRLISASLFLRFLCPAILSPSLFNLT-- 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1332 saggQLTTDQR--RNLGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVT 1409
Cdd:cd05136    208 ----QEYPSERaaRNLTLIAKVIQNLANFTRFGGKEEYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGR 283
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1996008064 1410 ltkpviyisigEIINTHTLLLdhqDAIAPEHNDPIHEllddLGEVPTIESLIGESAGNL 1468
Cdd:cd05136    284 -----------ELSLLHSLLV---EIISKLNQTTLDK----LGPLPRILNDITEALRNP 324
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
805-832 5.02e-05

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: 41.74  E-value: 5.02e-05
                           10        20
                   ....*....|....*....|....*...
gi 1996008064  805 WAKHWVKGGYYYYHNLETQEGGWDEPPG 832
Cdd:cd00201      4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
805-832 9.29e-05

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 41.05  E-value: 9.29e-05
                            10        20
                    ....*....|....*....|....*...
gi 1996008064   805 WAKHWVKGGYYYYHNLETQEGGWDEPPG 832
Cdd:smart00456    6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
RasGAP_p120GAP cd05391
Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ...
1230-1410 8.40e-04

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: 43.63  E-value: 8.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1230 SKLPYDVTPEQALAHEEVKTRLDNSIRNMRAVTDKflsaIISSVDKIPYGMRFIAKVLKDSLHEKFPDageDELL--KII 1307
Cdd:cd05391    111 SKQSCELNPSKLEKNEDVNTNLEHLLNILSELVEK----IFMAAEILPPTLRYIYGCLQKSVQQKWPT---NTTVrtRVV 183
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1308 GNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTtdqrRNLGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQ 1387
Cdd:cd05391    184 SGFVFLRLICPAILNPRMFNIISETPSPTAA----RTLTLVAKSLQNLANLVEFGAKEPYMEGVNPFIKKNKERMIMFLD 259
                          170       180
                   ....*....|....*....|....*.
gi 1996008064 1388 TACDVPELQD---KFNVDEYSDLVTL 1410
Cdd:cd05391    260 ELGNVPELPDtteHSRTDLSRDLAAL 285
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
894-916 2.62e-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: 2.62e-03
                            10        20
                    ....*....|....*....|...
gi 1996008064   894 KQIPAITCIQSQWRGYKQKKAYQ 916
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
RasGAP_CLA2_BUD2 cd05137
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ...
1184-1393 3.16e-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: 41.78  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1184 GQNALRQILAPVVKEIMDDKsLNIKTDPvdiykswvnqmesqtgeaSKLPYDvtpeqalAHEEVKTRLDNSIRNMRAVTD 1263
Cdd:cd05137    114 GKEYLEKSIGDVIRKICEEN-KDCEVDP------------------SRVKES-------DSIEKEEDLEENWENLISLTE 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1264 KFLSAIISSVDKIPYGMRFIAKVLKDSLHEKFPDAGEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDlsagGQLTTDQRR 1343
Cdd:cd05137    168 EIWNSIYITSNDCPPELRKILKHIRAKVEDRYGDFLRTVTLNSVSGFLFLRFFCPAILNPKLFGLLK----DHPRPRAQR 243
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1996008064 1344 NLGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQTACDVP 1393
Cdd:cd05137    244 TLTLIAKVLQNLANLTTFGQKEPWMEPMNEFLTTHREELKDYIDKITGIK 293
CH_VAV1 cd21262
calponin homology (CH) domain found in VAV1 protein; VAV1 is expressed predominantly in the ...
172-276 6.15e-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: 6.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  172 RWMEAClgEDLPPT----------TELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRykatglHFRHTDNVIQWLN 241
Cdd:cd21262      8 HWLIQC--RVLPPNhrvtwdsaqvCDLAQALRDGVLLCQLLNNLLPHAVNLREINLRPQMS------QFLCLKNIRTFLS 79
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1996008064  242 A-MDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALS 276
Cdd:cd21262     80 TcCEKFGLRKSELFEAFDLFDVRDFGKVIDTLSILS 115
CH_TAGLN-like cd21209
calponin homology (CH) domain found in the transgelin family; The transgelin (TAGLN) family ...
173-265 9.11e-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: 9.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996008064  173 WMEACLGEDL----PPTTELEEGLRNGVYLAKLGN-FFSPKVVSLKKIydreqtryKATGLHFRHTDNVIQWLNAMDEIG 247
Cdd:cd21209     11 WIVAQCGSDVgrpdPGRLGFQKWLKDGTVLCKLINsLYPEGSKPVKKI--------QSSKMAFKQMEQISQFLKAAEDYG 82
                           90
                   ....*....|....*...
gi 1996008064  248 LPKIFYPETTDIYDRKNM 265
Cdd:cd21209     83 VRTTDIFQTVDLWEGKDM 100
 
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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