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Conserved domains on  [gi|560951910|ref|XP_006198488|]
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LOW QUALITY PROTEIN: ras GTPase-activating-like protein IQGAP1 [Vicugna pacos]

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 ...
 970-1349 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: 792.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  970 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 1049
Cdd:cd05133     1 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1050 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALAHEEVRTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRF 1129
Cdd:cd05133    81 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQAMSHEEVRTRLDASIKNMRMVTDKFLSAIISSVDKIPYGMRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1130 IAKVLKDSLHEKFPDAGEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 1209
Cdd:cd05133   161 IAKVLKDTLHEKFPDAGEDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1210 GDNAHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 1289
Cdd:cd05133   241 GDNAHLSPINEYLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1290 PIHELLDDLGEVPTIESLIGESSGNLNDPNKEALAKTEVSLTLTNKFDVPGDENAEMDAR 1349
Cdd:cd05133   321 PIHELLDDLGEVPTIESLIGENPGPPGDPNRETLAKTEVSLTLTNKFDVPGDENAEMDAR 380
CH_IQGAP1 cd21274
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif ...
 7-160 1.57e-106

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: 335.42  E-value: 1.57e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910    7 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 86
Cdd:cd21274     1 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 560951910   87 IQWLNAMGEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKIELE 160
Cdd:cd21274    81 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTELE 154
IQG1 super family cl34962
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
 843-1624 1.50e-63

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: 237.09  E-value: 1.50e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  843 LDQSDQDFQEELDLMKMREEVITLIRSNQQLENDLNLMDIKIGLLVKnkITLQDVVSHskklt*knKEQLSDMMMLNKQK 922
Cdd:COG5261   290 SNVEQAFFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKRGNKIR--LLIQNRMPQ--------EEDTKFAERLQSNI 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  923 GGLKALSKEKReKLEAYQHLFYLLQTN-PTYL--------------AKLIFQMPQNKSTKFMdsvIFTLYNYASNQREEY 987
Cdd:COG5261   360 NGRKKYFPLDR-RLSLFGPLFFLLQSSiPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE---IRKLYSLGKSNCEEH 435

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  988 LLLRLFKTALQEEIKSKVDqIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPVDIYKSWVN 1067
Cdd:COG5261   436 LSVSLFQMLLRTEVEATSL-VQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHEDLEVDINPLLVYRALLN 514

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1068 QmesqtgeasklpYDVTPEQALAHEEVRTRLDNSIRNMRAV-----------TDKFLSAIISSVDKIPYGMRFIAKVLK- 1135
Cdd:COG5261   515 K------------GQLSPDKDLELLTSNEEVSEFLAVMNAVqessakllelsTERILDAVYNSLDEIGYGIRFVCELIRv 582

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1136 ------DSLHEKFPDA--------GEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSaggqlTTDQRRNLGSIAKMLQH 1201
Cdd:COG5261   583 vfeltpNRLFPSISDSrclrticfAEIDSLGLIGGFFFLRFVNEALVSPQTSMLKDSC-----PSDNVRKLATLSKILQS 657

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1202 AASNKMFLGdnaHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYIsIGEIINTHTLLLDHQD 1281
Cdd:COG5261   658 VFEITSSDK---FDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYL-VNEIYLTHEIIIEYLD 733

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1282 AI--APEHNDPIHELLDDLGEVPtiesligessgnlnDPNKEALAKTEvSLTLTNKFDVPgdenaemdARTILLNTKRLI 1359
Cdd:COG5261   734 NLydPDSLVDLLLQELGELCSFP--------------QDQRDTLNCLV-TLPLFNRSDDP--------IRDLKQQLKRTR 790

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1360 VDVIRFQPGETLTEILETPATSEQEAEHQRAMQRRAIRDAKTPDKMKksktikedsNLTLQEKKEKIQSGLKKLTELGTV 1439
Cdd:COG5261   791 VYIIYVDAGTNLFEQLLRLLPSDEPATRNPLDLNPNIRDDPSVSSLK---------SMSLMKLKIRAIELLDELETLGFV 861

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1440 DPKNRYQELINDIAKDIRNQRRYRQRRKAELVKLQQTYAALNSKATFYGEQVDYYKSYIKTCLDNLASKGK----VSKKP 1515
Cdd:COG5261   862 SRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKSklkgFSRGV 941

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1516 REMKGKKSKK--ISLKYTAARLHEKGVLLEIEDLQVNqFKNVIFEISpTEEVGDFEVKAKFMG--VQMETFMLHYQDLLQ 1591
Cdd:COG5261   942 GVVRDKPKSIssGTFKYSAQQLYKRGVLVNITIPEPN-VSNIYFTFS-SDSTDNFVIEVYQPGhsVSLPEVSFCFDDLLK 1019

                         810       820       830
                  ....*....|....*....|....*....|...
gi 560951910 1592 LQYEGVAVMKLFDRAKVNVNLLIFLLNKKFYGK 1624
Cdd:COG5261  1020 RQYNKNPVVDLGGFLTFNANKLLHLIESKFYRK 1052
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 652-679 1.55e-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: 43.29  E-value: 1.55e-05
                          10        20
                  ....*....|....*....|....*...
gi 560951910  652 WVKHWVKGGYHYYHNLETQEGGWDEPPD 679
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 745-763 2.21e-04

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


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 39.62  E-value: 2.21e-04
                            10
                    ....*....|....*....
gi 560951910    745 AITCIQSQWRGYKQRKAYQ 763
Cdd:smart00015    5 AAIIIQAAWRGYLARKRYK 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 ...
 970-1349 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: 792.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  970 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 1049
Cdd:cd05133     1 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1050 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALAHEEVRTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRF 1129
Cdd:cd05133    81 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQAMSHEEVRTRLDASIKNMRMVTDKFLSAIISSVDKIPYGMRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1130 IAKVLKDSLHEKFPDAGEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 1209
Cdd:cd05133   161 IAKVLKDTLHEKFPDAGEDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1210 GDNAHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 1289
Cdd:cd05133   241 GDNAHLSPINEYLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1290 PIHELLDDLGEVPTIESLIGESSGNLNDPNKEALAKTEVSLTLTNKFDVPGDENAEMDAR 1349
Cdd:cd05133   321 PIHELLDDLGEVPTIESLIGENPGPPGDPNRETLAKTEVSLTLTNKFDVPGDENAEMDAR 380
CH_IQGAP1 cd21274
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif ...
 7-160 1.57e-106

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: 335.42  E-value: 1.57e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910    7 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 86
Cdd:cd21274     1 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 560951910   87 IQWLNAMGEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKIELE 160
Cdd:cd21274    81 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTELE 154
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
 992-1204 9.19e-77

GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position.


Pssm-ID: 459871  Cd Length: 207  Bit Score: 252.98  E-value: 9.19e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910   992 LFKTALQEEIKSkVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPVDIYKSWVNQMES 1071
Cdd:pfam00616    1 LISELIEEEIES-SDNPNDLLRGNSLVSKLLETYNRRPRGQEYLKKVLGPLVRKIIEDEDLDLESDPRKIYESLINQEEL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  1072 QTGEaSKLPYDVTPEQALAHEEVRTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRFIAKVLKDSLHEKFPDAGEDELL 1151
Cdd:pfam00616   80 KTGR-SDLPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEIL 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 560951910  1152 KIIGNLLYYRYMNPAIVAPDAFDIIDlsagGQLTTDQRRNLGSIAKMLQHAAS 1204
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVD----HQISPKQRRNLTLIAKVLQNLAN 207
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
 959-1311 8.44e-73

GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position. Improved domain limits from structure.


Pssm-ID: 214617  Cd Length: 344  Bit Score: 247.22  E-value: 8.44e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910    959 QMPQNKSTKFMDSVIFTLYNYASNQREEYLLLRLFKTALQeeIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQI 1038
Cdd:smart00323    1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLS--LASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRAL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910   1039 LAPVVKEIMDD----KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALAHEEVRTR---LDNSIRNMRAVTDK 1111
Cdd:smart00323   79 IDPEVERTDDPntifRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEgedLETNLENLLQYVER 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910   1112 FLSAIISSVDKIPYGMRFIAKVLKDSLHEKFPDAgeDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLsaggQLTTDQRRN 1191
Cdd:smart00323  159 LFDAIINSSDRLPYGLRDICKQLRQAAEKRFPDA--DVIYKAVSSFVFLRFFCPAIVSPKLFNLVDE----HPDPTTRRT 232

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910   1192 LGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQTACDVPElqdkFNVDEYSDLVTLTkpviyisIGEIIN 1271
Cdd:smart00323  233 LTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPE----ILVDKVSDSTTIS-------GRELSL 301

                           330       340       350       360
                    ....*....|....*....|....*....|....*....|..
gi 560951910   1272 THTLLLDHQDAIAPEHN--DPIHELLDDLGEVPTIESLIGES 1311
Cdd:smart00323  302 LHSLLLENGDALKRELNneDPLGKLLFKLRYFGLTTHELTYG 343
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
 843-1624 1.50e-63

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: 237.09  E-value: 1.50e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  843 LDQSDQDFQEELDLMKMREEVITLIRSNQQLENDLNLMDIKIGLLVKnkITLQDVVSHskklt*knKEQLSDMMMLNKQK 922
Cdd:COG5261   290 SNVEQAFFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKRGNKIR--LLIQNRMPQ--------EEDTKFAERLQSNI 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  923 GGLKALSKEKReKLEAYQHLFYLLQTN-PTYL--------------AKLIFQMPQNKSTKFMdsvIFTLYNYASNQREEY 987
Cdd:COG5261   360 NGRKKYFPLDR-RLSLFGPLFFLLQSSiPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE---IRKLYSLGKSNCEEH 435

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  988 LLLRLFKTALQEEIKSKVDqIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPVDIYKSWVN 1067
Cdd:COG5261   436 LSVSLFQMLLRTEVEATSL-VQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHEDLEVDINPLLVYRALLN 514

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1068 QmesqtgeasklpYDVTPEQALAHEEVRTRLDNSIRNMRAV-----------TDKFLSAIISSVDKIPYGMRFIAKVLK- 1135
Cdd:COG5261   515 K------------GQLSPDKDLELLTSNEEVSEFLAVMNAVqessakllelsTERILDAVYNSLDEIGYGIRFVCELIRv 582

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1136 ------DSLHEKFPDA--------GEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSaggqlTTDQRRNLGSIAKMLQH 1201
Cdd:COG5261   583 vfeltpNRLFPSISDSrclrticfAEIDSLGLIGGFFFLRFVNEALVSPQTSMLKDSC-----PSDNVRKLATLSKILQS 657

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1202 AASNKMFLGdnaHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYIsIGEIINTHTLLLDHQD 1281
Cdd:COG5261   658 VFEITSSDK---FDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYL-VNEIYLTHEIIIEYLD 733

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1282 AI--APEHNDPIHELLDDLGEVPtiesligessgnlnDPNKEALAKTEvSLTLTNKFDVPgdenaemdARTILLNTKRLI 1359
Cdd:COG5261   734 NLydPDSLVDLLLQELGELCSFP--------------QDQRDTLNCLV-TLPLFNRSDDP--------IRDLKQQLKRTR 790

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1360 VDVIRFQPGETLTEILETPATSEQEAEHQRAMQRRAIRDAKTPDKMKksktikedsNLTLQEKKEKIQSGLKKLTELGTV 1439
Cdd:COG5261   791 VYIIYVDAGTNLFEQLLRLLPSDEPATRNPLDLNPNIRDDPSVSSLK---------SMSLMKLKIRAIELLDELETLGFV 861

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1440 DPKNRYQELINDIAKDIRNQRRYRQRRKAELVKLQQTYAALNSKATFYGEQVDYYKSYIKTCLDNLASKGK----VSKKP 1515
Cdd:COG5261   862 SRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKSklkgFSRGV 941

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1516 REMKGKKSKK--ISLKYTAARLHEKGVLLEIEDLQVNqFKNVIFEISpTEEVGDFEVKAKFMG--VQMETFMLHYQDLLQ 1591
Cdd:COG5261   942 GVVRDKPKSIssGTFKYSAQQLYKRGVLVNITIPEPN-VSNIYFTFS-SDSTDNFVIEVYQPGhsVSLPEVSFCFDDLLK 1019

                         810       820       830
                  ....*....|....*....|....*....|...
gi 560951910 1592 LQYEGVAVMKLFDRAKVNVNLLIFLLNKKFYGK 1624
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, ...
 1419-1548 1.14e-37

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: 138.07  E-value: 1.14e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  1419 LQEKKEKIQSGLKKLTELGTVDPKNRYQELINDIAKDIRNQRRYRQRRKAELVKLQQTYAALNSKATFYGEQVDYYKSYI 1498
Cdd:pfam03836    1 YVELKKKALENLLELESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYI 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 560951910  1499 KTCLDNLASKGK-------VSKKPREMKGKKSKKISLKYTAARLHEKGVLLEIEDLQ 1548
Cdd:pfam03836   81 ENCLDNLQKKKKklfskqyFHYRKLQKRGKLPKFGSYKYSARQLYEKGVLLEIEGVP 137
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
 1-161 4.22e-32

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: 136.55  E-value: 4.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910    1 MDERRRQNVAYEYLCHLEEAKRWMEACLGEDLPpTTELEEGLRNGVYLAKLGNFFSPKvvSLKKIYdreqtryKATGLHF 80
Cdd:COG5261    30 SAKNRSALRAYEYLCRVSEAKIWIEEVIEEALP-ELCFEDSLRNGVFLAKLTQRFNPD--LTTVIF-------PADKLQF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910   81 RHTDNVIQWLNAMGEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVdFTEEEINNMKIELE 160
Cdd:COG5261   100 RHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTPLINSSGQIS-FTKEDIAACKKAWP 178


                  .
gi 560951910  161 K 161
Cdd:COG5261   179 R 179
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 18-128 2.37e-14

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 70.78  E-value: 2.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910    18 EEAKRWMEACLGEDLPPT--TELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREqtrykatglhFRHTDNVIQWLN-AMG 94
Cdd:pfam00307    5 KELLRWINSHLAEYGPGVrvTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSE----------FDKLENINLALDvAEK 74

                           90       100       110
                   ....*....|....*....|....*....|....
gi 560951910    95 EIGLPKIFyPETTDIYDRKNMpRCIYCIHALSLY 128
Cdd:pfam00307   75 KLGVPKVL-IEPEDLVEGDNK-SVLTYLASLFRR 106
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 18-125 6.66e-14

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 69.27  E-value: 6.66e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910     18 EEAKRWMEACLGEDLPPT-TELEEGLRNGVYLAKLGNFFSPKVVSLKKIydreqtryKATGLHFRHTDNVIQWLNAMGEI 96
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPvTNFSSDLKDGVALCALLNSLSPGLVDKKKV--------AASLSRFKKIENINLALSFAEKL 72

                            90       100       110
                    ....*....|....*....|....*....|
gi 560951910     97 GlPKIFYPETTDIYD-RKNMPRCIYCIHAL 125
Cdd:smart00033   73 G-GKVVLFEPEDLVEgPKLILGVIWTLISL 101
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 652-679 1.55e-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: 43.29  E-value: 1.55e-05
                          10        20
                  ....*....|....*....|....*...
gi 560951910  652 WVKHWVKGGYHYYHNLETQEGGWDEPPD 679
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 745-763 2.21e-04

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 39.62  E-value: 2.21e-04
                            10
                    ....*....|....*....
gi 560951910    745 AITCIQSQWRGYKQRKAYQ 763
Cdd:smart00015    5 AAIIIQAAWRGYLARKRYK 23
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 652-679 3.89e-04

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: 39.12  E-value: 3.89e-04
                            10        20
                    ....*....|....*....|....*...
gi 560951910    652 WVKHWVKGGYHYYHNLETQEGGWDEPPD 679
Cdd:smart00456    6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 745-763 1.19e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 37.68  E-value: 1.19e-03
                           10
                   ....*....|....*....
gi 560951910   745 AITCIQSQWRGYKQRKAYQ 763
Cdd:pfam00612    3 AAIKIQAAWRGYLARKRYK 21
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 652-677 1.25e-03

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 37.87  E-value: 1.25e-03
                           10        20
                   ....*....|....*....|....*.
gi 560951910   652 WVKHWVKGGYHYYHNLETQEGGWDEP 677
Cdd:pfam00397    5 WEERWDPDGRVYYYNHETGETQWEKP 30
COG5022 COG5022
Myosin heavy chain [General function prediction only];
715-940 6.54e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.22  E-value: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  715 LVTKLQACCRGYLVRQEFRSRMNFLKKqvpaitcIQSQWRGYKQRKAYQDRLAYLRShkdevVKIQSLARMHQARKRYRD 794
Cdd:COG5022   747 IATRIQRAIRGRYLRRRYLQALKRIKK-------IQVIQHGFRLRRLVDYELKWRLF-----IKLQPLLSLLGSRKEYRS 814

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  795 RLQYFRDHINDIIK-------------------IQAFIRANKARDDYKTLIN---AEDPPMIV-------------VRKF 839
Cdd:COG5022   815 YLACIIKLQKTIKRekklreteevefslkaevlIQKFGRSLKAKKRFSLLKKetiYLQSAQRVelaerqlqelkidVKSI 894

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  840 VHLLDQSDQDFQEELDLMK-----MREEVITLIRSNQQLENDLNLMDIKIGL---LVKNKItLQDVVSHSKKLt*knKEQ 911
Cdd:COG5022   895 SSLKLVNLELESEIIELKKslssdLIENLEFKTELIARLKKLLNNIDLEEGPsieYVKLPE-LNKLHEVESKL----KET 969

                         250       260
                  ....*....|....*....|....*....
gi 560951910  912 LSDMMMLNKQKGGLKALSKEKREKLEAYQ 940
Cdd:COG5022   970 SEEYEDLLKKSTILVREGNKANSELKNFK 998
 
Name Accession Description Interval E-value
RasGAP_IQGAP1 cd05133
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...
 970-1349 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: 792.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  970 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 1049
Cdd:cd05133     1 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1050 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALAHEEVRTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRF 1129
Cdd:cd05133    81 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQAMSHEEVRTRLDASIKNMRMVTDKFLSAIISSVDKIPYGMRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1130 IAKVLKDSLHEKFPDAGEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 1209
Cdd:cd05133   161 IAKVLKDTLHEKFPDAGEDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1210 GDNAHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 1289
Cdd:cd05133   241 GDNAHLSPINEYLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1290 PIHELLDDLGEVPTIESLIGESSGNLNDPNKEALAKTEVSLTLTNKFDVPGDENAEMDAR 1349
Cdd:cd05133   321 PIHELLDDLGEVPTIESLIGENPGPPGDPNRETLAKTEVSLTLTNKFDVPGDENAEMDAR 380
RasGAP_IQGAP2 cd05131
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...
 970-1321 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: 662.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  970 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 1049
Cdd:cd05131     1 DTVIFTLYNYASNQREEYLLLKLFETALEEEIKSKVDQIQDIVTGNPTVIKMVVSFNRGARGQNTLRQLLAPVVKEIIED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1050 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALAHEEVRTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRF 1129
Cdd:cd05131    81 KSLIINTNPVEVYKAWVNQLETATGEASKLPYDVTTEQALTHPEVVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1130 IAKVLKDSLHEKFPDAGEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 1209
Cdd:cd05131   161 IAKVLKNSLHEKFPDATEDELLKIVGNLLYYRYMNPAIVAPDGFDIIDMTAGGQIHSEQRRNLGSVAKVLQHAASNKLFE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1210 GDNAHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 1289
Cdd:cd05131   241 GENAHLSSMNSYLSQTYQKFRKFFQAACDVPEPEEKFNIDEYSDMVTLSKPVIYISIEEIINTHSLLLEHQDAIAPDQND 320

                         330       340       350
                  ....*....|....*....|....*....|..
gi 560951910 1290 PIHELLDDLGEVPTIESLIGESSGNLNDPNKE 1321
Cdd:cd05131   321 LLHELLKDLGEVPDVESFLGEGTVDPNDPNKE 352
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
 980-1310 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: 600.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  980 ASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPV 1059
Cdd:cd05127     1 ASNRREEYLLLKLFKTALREEIESKVSLPEDIVTGNPTVIKLVVNYNRGPRGQKYLRELLGPVVKEILDDDDLDLETDPV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1060 DIYKSWVNQMESQTGEASKLPYDVTPEQALAHEEVRTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRFIAKVLKDSLH 1139
Cdd:cd05127    81 DIYKAWINQEESRTGEPSKLPYDVTREQALKDPEVRKRLIEHLEKLRAITDKFLTAITESLDKMPYGMRYIAKVLKEALR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1140 EKFPDAGEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFLGDNAHLSIIN 1219
Cdd:cd05127   161 EKFPDAPEEEILKIVGNLLYYRYMNPAIVAPEAFDIIDLSVGGQLSPLQRRNLGSIAKVLQQAASGKLFGGENPYLSPLN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1220 EYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHNDPIHELLDDLG 1299
Cdd:cd05127   241 PYISESHEKFKKFFLEACTVPEAEEHFNIDEYSDLTMLTKPTIYISLQEIFATHKLLLEHQDEIAPDPDDPLRELLDDLG 320

                         330
                  ....*....|.
gi 560951910 1300 EVPTIESLIGE 1310
Cdd:cd05127   321 PAPTIESLLGS 331
RasGAP_IQGAP3 cd12207
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ...
 970-1317 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 560951910  970 DSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDD 1049
Cdd:cd12207     1 ESVIFSLYNYASNRREAYLLLQLFKTALQEEISSKVEKPQDVITGNPTVIRLLVSFYRSARGQNALRHILGPVVQDVLQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1050 KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALAHEEVRTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRF 1129
Cdd:cd12207    81 KGLSIRTDPVQIYKAWINQTETQSGCRSSLPYEVSPEQALSHPEVQRRLDIAIRNLLAVTDKFLSAITSSVDKIPYGMRY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1130 IAKVLKDSLHEKFPDAGEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFL 1209
Cdd:cd12207   161 VAKVLRDSLQEKFPGASEDEVYKVVGNLLYYRFMNPAVVAPDGFDIVDCSAGGALQPEQRRMLGSVAKVLQHAAANKHFQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1210 GDNAHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHND 1289
Cdd:cd12207   241 GDSEHLQALNQYLEETHVKFRKFILQACCVPEPEERFNVDEYSEMVAVAKPVIYITVGELINTHKLLLEHQDSIAPDHSD 320

                         330       340
                  ....*....|....*....|....*...
gi 560951910 1290 PIHELLDDLGEVPTIESLIGESSGNLND 1317
Cdd:cd12207   321 PLHELLEDLGEVPTVQSLIGESWADLGD 348
CH_IQGAP1 cd21274
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif ...
 7-160 1.57e-106

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: 335.42  E-value: 1.57e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910    7 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 86
Cdd:cd21274     1 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 560951910   87 IQWLNAMGEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKIELE 160
Cdd:cd21274    81 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTELE 154
CH_IQGAP3 cd21276
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP3; IQ motif ...
 8-159 1.87e-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: 312.68  E-value: 1.87e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910    8 NVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNVI 87
Cdd:cd21276     1 NVAYQYLCRLEEAKRWMEACLKEELPPPTELEESLRNGVYLAKLGHCFAPRVVPLKKIYDLEQMRYQATGLHFRHTDNIN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 560951910   88 QWLNAMGEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKIEL 159
Cdd:cd21276    81 HWRNAMMHIGLPSIFHPETTDIYDKKNMPRVVYCIHALSLYLFRLGLAPQIHDLYGKVKFTEEEINNMKLEL 152
CH_IQGAP2 cd21275
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP2; IQ motif ...
 1-139 1.70e-93

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: 298.85  E-value: 1.70e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910    1 MDERRRQNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHF 80
Cdd:cd21275    18 MDERRRQNIAYEYLCHLEEAKQWIEACLNEELPPTTELEEGLRNGVYLVKLAKFFAPKLVSEKKIYDVDQVRYKRSGLHF 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 560951910   81 RHTDNVIQWLNAMGEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQ 139
Cdd:cd21275    98 RHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNMPRVIYCIHALSLYLFKLGIAPQIQ 156
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
 992-1204 9.19e-77

GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position.


Pssm-ID: 459871  Cd Length: 207  Bit Score: 252.98  E-value: 9.19e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910   992 LFKTALQEEIKSkVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPVDIYKSWVNQMES 1071
Cdd:pfam00616    1 LISELIEEEIES-SDNPNDLLRGNSLVSKLLETYNRRPRGQEYLKKVLGPLVRKIIEDEDLDLESDPRKIYESLINQEEL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  1072 QTGEaSKLPYDVTPEQALAHEEVRTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRFIAKVLKDSLHEKFPDAGEDELL 1151
Cdd:pfam00616   80 KTGR-SDLPRDVSPEEAIEDPEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEIL 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 560951910  1152 KIIGNLLYYRYMNPAIVAPDAFDIIDlsagGQLTTDQRRNLGSIAKMLQHAAS 1204
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVD----HQISPKQRRNLTLIAKVLQNLAN 207
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
 959-1311 8.44e-73

GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position. Improved domain limits from structure.


Pssm-ID: 214617  Cd Length: 344  Bit Score: 247.22  E-value: 8.44e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910    959 QMPQNKSTKFMDSVIFTLYNYASNQREEYLLLRLFKTALQeeIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQI 1038
Cdd:smart00323    1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLS--LASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRAL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910   1039 LAPVVKEIMDD----KSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALAHEEVRTR---LDNSIRNMRAVTDK 1111
Cdd:smart00323   79 IDPEVERTDDPntifRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEgedLETNLENLLQYVER 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910   1112 FLSAIISSVDKIPYGMRFIAKVLKDSLHEKFPDAgeDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLsaggQLTTDQRRN 1191
Cdd:smart00323  159 LFDAIINSSDRLPYGLRDICKQLRQAAEKRFPDA--DVIYKAVSSFVFLRFFCPAIVSPKLFNLVDE----HPDPTTRRT 232

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910   1192 LGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQTACDVPElqdkFNVDEYSDLVTLTkpviyisIGEIIN 1271
Cdd:smart00323  233 LTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPE----ILVDKVSDSTTIS-------GRELSL 301

                           330       340       350       360
                    ....*....|....*....|....*....|....*....|..
gi 560951910   1272 THTLLLDHQDAIAPEHN--DPIHELLDDLGEVPTIESLIGES 1311
Cdd:smart00323  302 LHSLLLENGDALKRELNneDPLGKLLFKLRYFGLTTHELTYG 343
CH_IQGAP cd21206
calponin homology (CH) domain found in the IQ motif containing GTPase activating protein ...
 8-133 2.37e-69

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


Pssm-ID: 409055 [Multi-domain]  Cd Length: 118  Bit Score: 228.26  E-value: 2.37e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910    8 NVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDreqtrykaTGLHFRHTDNVI 87
Cdd:cd21206     1 TIAYEYLCRLEEAKQWIEACLNEELPPTTEFEEELRNGVVLAKLANKFAPKLVPLKKIYD--------VGLQFRHTDNIN 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 560951910   88 QWLNAMGEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLG 133
Cdd:cd21206    73 HFLRALKKIGLPKIFHFETTDLYEKKNIPKVIYCLHALSLLLFKLG 118
RasGAP_GAPA cd05132
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...
 968-1302 1.39e-67

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: 232.63  E-value: 1.39e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  968 FMDSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDqIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIM 1047
Cdd:cd05132     5 LLQTVMFTLYGNQYESREEHLLLSMFQSVLTYEFDETTE-FGSLLRANTAVSRMMTTYTRRGPGQSYLKTVLADRINDLI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1048 DDKSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALAHEEVRTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGM 1127
Cdd:cd05132    84 SLKDLNLEINPLKVYEQMINDIELDTGLPSNLPRGITPEEAAENPAVQNIIEPRLEMLEEITNSFLEAIINSLDEVPYGI 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1128 RFIAKVLKDSLHEKFPDAGEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDlsagGQLTTDQRRNLGSIAKMLQHAASNKM 1207
Cdd:cd05132   164 RWICKQIRSLTRRKFPDASDETICSLIGGFFLLRFINPAIVSPQAYMLVD----GKPSDNTRRTLTLIAKLLQNLANKPS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1208 FlGDNAHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYsdlVTLTKPVIYISI--GEIINTHTLLLDHQDAIAP 1285
Cdd:cd05132   240 Y-SKEPYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQY---IALSKKDLSINItlNEIYNTHSLLVKHLAELAP 315

                         330
                  ....*....|....*..
gi 560951910 1286 EHNDPIHELLDDLGEVP 1302
Cdd:cd05132   316 DHNDHLRLILQELGPAP 332
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
 843-1624 1.50e-63

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: 237.09  E-value: 1.50e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  843 LDQSDQDFQEELDLMKMREEVITLIRSNQQLENDLNLMDIKIGLLVKnkITLQDVVSHskklt*knKEQLSDMMMLNKQK 922
Cdd:COG5261   290 SNVEQAFFHLDRELHRLKQSISSQSKQVVVLERDIRLLIQKRGNKIR--LLIQNRMPQ--------EEDTKFAERLQSNI 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  923 GGLKALSKEKReKLEAYQHLFYLLQTN-PTYL--------------AKLIFQMPQNKSTKFMdsvIFTLYNYASNQREEY 987
Cdd:COG5261   360 NGRKKYFPLDR-RLSLFGPLFFLLQSSiPLFSiaicvgrvkrfsidALLNIVKLQILGNGYE---IRKLYSLGKSNCEEH 435

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  988 LLLRLFKTALQEEIKSKVDqIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPVDIYKSWVN 1067
Cdd:COG5261   436 LSVSLFQMLLRTEVEATSL-VQSLLRGNLPVHRNMTNYFRRSQGQAALREIRYQIINDVAIHEDLEVDINPLLVYRALLN 514

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1068 QmesqtgeasklpYDVTPEQALAHEEVRTRLDNSIRNMRAV-----------TDKFLSAIISSVDKIPYGMRFIAKVLK- 1135
Cdd:COG5261   515 K------------GQLSPDKDLELLTSNEEVSEFLAVMNAVqessakllelsTERILDAVYNSLDEIGYGIRFVCELIRv 582

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1136 ------DSLHEKFPDA--------GEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSaggqlTTDQRRNLGSIAKMLQH 1201
Cdd:COG5261   583 vfeltpNRLFPSISDSrclrticfAEIDSLGLIGGFFFLRFVNEALVSPQTSMLKDSC-----PSDNVRKLATLSKILQS 657

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1202 AASNKMFLGdnaHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYIsIGEIINTHTLLLDHQD 1281
Cdd:COG5261   658 VFEITSSDK---FDVPLQPFLKEYKEKVHNLLRKLGNVGDFEEYFEFDQYIDLVKKSRALEYL-VNEIYLTHEIIIEYLD 733

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1282 AI--APEHNDPIHELLDDLGEVPtiesligessgnlnDPNKEALAKTEvSLTLTNKFDVPgdenaemdARTILLNTKRLI 1359
Cdd:COG5261   734 NLydPDSLVDLLLQELGELCSFP--------------QDQRDTLNCLV-TLPLFNRSDDP--------IRDLKQQLKRTR 790

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1360 VDVIRFQPGETLTEILETPATSEQEAEHQRAMQRRAIRDAKTPDKMKksktikedsNLTLQEKKEKIQSGLKKLTELGTV 1439
Cdd:COG5261   791 VYIIYVDAGTNLFEQLLRLLPSDEPATRNPLDLNPNIRDDPSVSSLK---------SMSLMKLKIRAIELLDELETLGFV 861

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1440 DPKNRYQELINDIAKDIRNQRRYRQRRKAELVKLQQTYAALNSKATFYGEQVDYYKSYIKTCLDNLASKGK----VSKKP 1515
Cdd:COG5261   862 SRENRYQPLLNEIAKDIINLDALYERRRAELDILQDSLRNICEHNEYLDSQLQIYGSYLNNARSQLQPKKSklkgFSRGV 941

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1516 REMKGKKSKK--ISLKYTAARLHEKGVLLEIEDLQVNqFKNVIFEISpTEEVGDFEVKAKFMG--VQMETFMLHYQDLLQ 1591
Cdd:COG5261   942 GVVRDKPKSIssGTFKYSAQQLYKRGVLVNITIPEPN-VSNIYFTFS-SDSTDNFVIEVYQPGhsVSLPEVSFCFDDLLK 1019

                         810       820       830
                  ....*....|....*....|....*....|...
gi 560951910 1592 LQYEGVAVMKLFDRAKVNVNLLIFLLNKKFYGK 1624
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, ...
 1419-1548 1.14e-37

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: 138.07  E-value: 1.14e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  1419 LQEKKEKIQSGLKKLTELGTVDPKNRYQELINDIAKDIRNQRRYRQRRKAELVKLQQTYAALNSKATFYGEQVDYYKSYI 1498
Cdd:pfam03836    1 YVELKKKALENLLELESLGVISRENNYQDLLNDIANDIRNKHRRREQRQAELESLRQTLKKLCEKNKYLEEQLDSYNDYI 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 560951910  1499 KTCLDNLASKGK-------VSKKPREMKGKKSKKISLKYTAARLHEKGVLLEIEDLQ 1548
Cdd:pfam03836   81 ENCLDNLQKKKKklfskqyFHYRKLQKRGKLPKFGSYKYSARQLYEKGVLLEIEGVP 137
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
 985-1238 1.51e-37

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


Pssm-ID: 213328  Cd Length: 256  Bit Score: 142.25  E-value: 1.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  985 EEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSL----NIKTDPVD 1060
Cdd:cd04519     1 EEYRLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNTKNPNTLfrgnSLATKLLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1061 IYKSWVNQmESQTGEASKLPYDVTPEQAL----AHEEVRTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRFIAKVLKD 1136
Cdd:cd04519    81 QYMKLVGQ-EYLKETLSPLIREILESKESceidTKLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILRE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1137 SLHEKFPDAgEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDlsagGQLTTDQRRNLGSIAKMLQHAASNKMFLGDNAHLS 1216
Cdd:cd04519   160 FLAERFPEE-PDEAYQAVSGFLFLRFICPAIVSPELFGLVP----DEPSEQARRNLTLISKVLQSLANGVEFGDKEPFMK 234

                         250       260
                  ....*....|....*....|..
gi 560951910 1217 IINEYLSQSYQKFRRFFQTACD 1238
Cdd:cd04519   235 PLNDFIKSNKPKLKQFLDELSS 256
RasGAP_IQGAP_related cd12206
Ras-GTPase Activating Domain of proteins related to IQGAPs; RasGAP: Ras-GTPase Activating ...
 978-1301 6.01e-33

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: 132.07  E-value: 6.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  978 NYASNQREEYLLLRLFKTALQEEIKsKVDQIQEIVTGNPTV-IKMVVSFNRgaRGQNALRQ-ILAPVVKEIMDDKSLNIK 1055
Cdd:cd12206    20 NGKMDSREEFLFIKFILELLKSDIE-NSNSNQDFLANSDNFwILLLVTFNN--LRERSELKsIFGPLLVQYLENQEIDFE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1056 TDPVDIYKSWVNQMesqtgeasklpyDVTPEQALAHEEVRTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRFIAKVLK 1135
Cdd:cd12206    97 SDPSVIYKSLHGRP------------PLSSEEAIEDDRVSDKFVENLTNLREAVEMVAEIIFKNVDKIPVEIRYLCTKAY 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1136 DSLHEKFPDAGEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDlsaggqlttDQRRNLGSIAKMLQHAASNKMFLG-DNAH 1214
Cdd:cd12206   165 IAFADKFPDESEEDILRAISKILIKSYVAPILVNPENYGFVD---------NEEDNLNEKARVLLQILSMVFFLKnFDGY 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1215 LSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPehNDPIHEL 1294
Cdd:cd12206   236 LKPLNQYIEEIKPSIRDLLKELLDVPEEEQEYDKLIYYDIMSTTRPCLEILLDKVIEIIQILKENLDEFTP--DDQLVQL 313


                  ....*..
gi 560951910 1295 LDDLGEV 1301
Cdd:cd12206   314 LEKIVDL 320
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
 1-161 4.22e-32

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: 136.55  E-value: 4.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910    1 MDERRRQNVAYEYLCHLEEAKRWMEACLGEDLPpTTELEEGLRNGVYLAKLGNFFSPKvvSLKKIYdreqtryKATGLHF 80
Cdd:COG5261    30 SAKNRSALRAYEYLCRVSEAKIWIEEVIEEALP-ELCFEDSLRNGVFLAKLTQRFNPD--LTTVIF-------PADKLQF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910   81 RHTDNVIQWLNAMGEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVdFTEEEINNMKIELE 160
Cdd:COG5261   100 RHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTPLINSSGQIS-FTKEDIAACKKAWP 178


                  .
gi 560951910  161 K 161
Cdd:COG5261   179 R 179
RasGAP_Neurofibromin_like cd05392
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...
 934-1311 1.20e-31

Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins include the Saccharomyces cerevisiae RasGAP proteins Ira1 and Ira2, the closest homolog of neurofibromin, which is responsible for the human autosomal dominant disease neurofibromatosis type I (NF1). The RasGAP Ira1/2 proteins are negative regulators of the Ras-cAMP signaling pathway and conserved from yeast to human. In yeast Ras proteins are activated by GEFs, and inhibited by two GAPs, Ira1 and Ira2. Ras proteins activate the cAMP/protein kinase A (PKA) pathway, which controls metabolism, stress resistance, growth, and meiosis. Recent studies showed that the kelch proteins Gpb1 and Gpb2 inhibit Ras activity via association with Ira1 and Ira2. Gpb1/2 bind to a conserved C-terminal domain of Ira1/2, and loss of Gpb1/2 results in a destabilization of Ira1 and Ira2, leading to elevated levels of Ras2-GTP and uninhibited cAMP-PKA signaling. Since the Gpb1/2 binding domain on Ira1/2 is conserved in the human neurofibromin protein, the studies suggest that an analogous signaling mechanism may contribute to the neoplastic development of NF1.


Pssm-ID: 213341  Cd Length: 317  Bit Score: 127.02  E-value: 1.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  934 EKLEAYQHLFYLLQTNPTylakLIFQMPQNKSTKFMDS---VIFTLYNYASNqreeylLLRLFKTALQEEIkSKVDQIQE 1010
Cdd:cd05392     1 KKSEAYDELLELLIEDPQ----LLLAIAEVCPSSEVDLlaqSLLNLFETRNR------LLPLISWLIEDEI-SHTSRAAD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1011 IVTGNPTVIKMVVSFNRgARGQNALRQILAPVVKEIMDDKslniKTDPVDIYKSWVNQMESQtgeasklpydvtpeqala 1090
Cdd:cd05392    70 LFRRNSVATRLLTLYAK-SVGNKYLRKVLRPLLTEIVDNK----DYFEVEKIKPDDENLEEN------------------ 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1091 heevrtrldnsIRNMRAVTDKFLSAIISSVDKIPYGMRFIAKVLKDSLHEKFPDAGedelLKIIGNLLYYRYMNPAIVAP 1170
Cdd:cd05392   127 -----------ADLLMKYAQMLLDSITDSVDQLPPSFRYICNTIYESVSKKFPDAA----LIAVGGFLFLRFICPAIVSP 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1171 DAFDIIDLSAggqlTTDQRRNLGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQTACDVPElqdkfnvDE 1250
Cdd:cd05392   192 ESENLLDPPP----TPEARRSLILIAKVLQNIANGVLFSLKEPYLESLNEFLKKNSDRIQQFLSEVSTIPP-------TD 260

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 560951910 1251 YSDLVTLTKPViyisIGEIINTHTLLLDHQDAIAPEHNDPIhELLDDLGEVPTIESLIGES 1311
Cdd:cd05392   261 PIFDESDEEPI----TADLRYLHKFLYLHFLEIRKEVLKGS-SSQGSDKELVETFKLIDEI 316
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 17-127 7.43e-25

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 100.49  E-value: 7.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910   17 LEEAKRWMEACLGEDLP-PTTELEEGLRNGVYLAKLGNFFSPKVVSLKKiydreqtryKATGLHFRHTDNVIQWLNAMGE 95
Cdd:cd00014     1 EEELLKWINEVLGEELPvSITDLFESLRDGVLLCKLINKLSPGSIPKIN---------KKPKSPFKKRENINLFLNACKK 71

                          90       100       110
                  ....*....|....*....|....*....|..
gi 560951910   96 IGLPKIFYPETTDIYDRKNMPRCIYCIHALSL 127
Cdd:cd00014    72 LGLPELDLFEPEDLYEKGNLKKVLGTLWALAL 103
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
 1093-1284 8.27e-16

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


Pssm-ID: 213332 [Multi-domain]  Cd Length: 332  Bit Score: 80.44  E-value: 8.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1093 EV-RTRLDNS------IRNMRAVTDKFLSAIISSVDKIPYGMRFIAKVLKDSLHEKFPDAGedelLKIIGNLLYYRYMNP 1165
Cdd:cd05130   121 EVdPTRLEGNenleenQRNLLQLTEKFFHAIISSSDEFPPQLRSVCHCLYQVVSHRFPNSG----LGAVGSAIFLRFINP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1166 AIVAPDAFDIIDlsagGQLTTDQRRNLGSIAKMLQHAASNKMFLGDnAHLSIINEYLSQSYQKFRRFFQTACDvpelqDK 1245
Cdd:cd05130   197 AIVSPYEYGILD----REPPPRVKRGLKLMSKILQNIANHVLFTKE-AHMLPFNDFLRNHFEAGRRFFSSIAS-----DC 266

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 560951910 1246 FNVDEYSDlvtltKPVIYISIGEIINTHTLLLDHQDAIA 1284
Cdd:cd05130   267 GAVDGPSS-----KYLSFINDANVLALHRLLWNNQEKIG 300
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 18-128 2.37e-14

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 70.78  E-value: 2.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910    18 EEAKRWMEACLGEDLPPT--TELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREqtrykatglhFRHTDNVIQWLN-AMG 94
Cdd:pfam00307    5 KELLRWINSHLAEYGPGVrvTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSE----------FDKLENINLALDvAEK 74

                           90       100       110
                   ....*....|....*....|....*....|....
gi 560951910    95 EIGLPKIFyPETTDIYDRKNMpRCIYCIHALSLY 128
Cdd:pfam00307   75 KLGVPKVL-IEPEDLVEGDNK-SVLTYLASLFRR 106
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 18-125 6.66e-14

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 69.27  E-value: 6.66e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910     18 EEAKRWMEACLGEDLPPT-TELEEGLRNGVYLAKLGNFFSPKVVSLKKIydreqtryKATGLHFRHTDNVIQWLNAMGEI 96
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPvTNFSSDLKDGVALCALLNSLSPGLVDKKKV--------AASLSRFKKIENINLALSFAEKL 72

                            90       100       110
                    ....*....|....*....|....*....|
gi 560951910     97 GlPKIFYPETTDIYD-RKNMPRCIYCIHAL 125
Cdd:smart00033   73 G-GKVVLFEPEDLVEgPKLILGVIWTLISL 101
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
 19-125 1.65e-13

calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 (dMP20) and similar domains; This subfamily contains Drosophila melanogaster muscle-specific protein 20 (dMP20), Echinococcus granulosus myophilin, Dictyostelium discoideum Rac guanine nucleotide exchange factor B (also called Trix), and similar proteins. dMP20 is present only in the synchronous muscles of D. melanogaster. It may be involved in the system linking the nerve impulse with the contraction or the relaxation process. Trix is involved in the regulation of the late steps of the endocytic pathway. dMP20 contains a single copy of the CH domain, while Trix (triple CH-domain array exchange factor) contains three, two type 3 CH domains which are included in this model, and one type 1 CH domain that is not included in this subfamily, but is part of the superfamily. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409056 [Multi-domain]  Cd Length: 107  Bit Score: 68.11  E-value: 1.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910   19 EAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKvvSLKKIydreqtryKATGLHFRHTDNVIQWLNAMGEIGL 98
Cdd:cd21207     9 EALDWIEAVTGEKLDDGKDYEDVLKDGVILCKLINILKPG--SVKKI--------NTSKMAFKLMENIENFLTACKGYGV 78

                          90       100
                  ....*....|....*....|....*..
gi 560951910   99 PKIFYPETTDIYDRKNMPRCIYCIHAL 125
Cdd:cd21207    79 PKTDLFQTVDLYEKKNIPQVTNCLFAL 105
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
 18-126 1.39e-12

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


Pssm-ID: 409059 [Multi-domain]  Cd Length: 101  Bit Score: 65.47  E-value: 1.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910   18 EEAKRWMEACLGEDLPPTTeLEEGLRNGVYLAKLGNffspkvvslkKIYDREQTRYKATGLHFRHTDNVIQWLNAMGEIG 97
Cdd:cd21210     3 QEAREWIEEVLGEKLAQGD-LLDALKDGVVLCKLAN----------RILPADIRKYKESKMPFVQMENISAFLNAARKLG 71

                          90       100
                  ....*....|....*....|....*....
gi 560951910   98 LPKIFYPETTDIYDRKNMPRCIYCIHALS 126
Cdd:cd21210    72 VPENDLFQTVDLFERKNPAQVLQCLHALS 100
RasGAP_RAP6 cd05129
Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is ...
 937-1289 1.40e-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: 61.97  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  937 EAYQHLFY----------LLQTNPTYLAKLIFQMPQ--NKSTKFMDSVIFT-LYNYASNQREEYLLLRLFKTALQEEIKS 1003
Cdd:cd05129     1 DAYKLLGYqlshygeflrILRENPQLLAECLARGEKlsLEQTQNVIQTIVTsLYGNCIMPEDERLLLQLLRELMELQLKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1004 KVDQIQEIVTGNPTVIKMVVSFNRGARGQN-----ALRQilaPVVKEIMDDkSLNIKTDPVD-IYKSWVNQMESQTGEas 1077
Cdd:cd05129    81 SDNPRRLLRKGSCAFSRVFKLFTELLFSAKlyltaALHK---PIMQVLVDD-EIFLETDPQKaLCRFSPAEQEKRFGE-- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1078 klpyDVTPEQALAHEEVRTRLdnsIRNMRAVTDKFLSAIISSVDKIPYGMRFIAKVLKDSLHEKFpDAGEDELLKIIGNL 1157
Cdd:cd05129   155 ----EGTPEQQRKLQQYRAEF---LSRLVALVNKFISSLRQSVYCFPQSLRWIVRQLRKILTRSG-DDEEAEARALCTDL 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1158 LYYRYMNPAIVAPDAFDIIDLSAGGQLTtdqRRNLGSIAKMLQHAASNKMFLGDNahlsiineYLSQSYQKFRR----FF 1233
Cdd:cd05129   227 LFTNFICPAIVNPEQYGIISDAPISEVA---RHNLMQVAQILQVLALTEFESPDP--------RLKELLSKFDKdcvsAF 295

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 560951910 1234 QTACDVPELQDKFNVDEySDLVTLTKPVIYISIGEiINTHTLLLDHQDAIAPEHND 1289
Cdd:cd05129   296 LDVVIVGRAVETPPPSS-SALLEGSRTAVLITESD-LATLVEFLRSVKTGDEEKED 349
SCP1 COG5199
Calponin [Cytoskeleton];
18-138 2.83e-09

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 58.01  E-value: 2.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910   18 EEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVslkkiydreqtRYKATGLHFRHTDNVIQWLNAMGEIG 97
Cdd:COG5199    16 KEVTLWIETVLGEKFEPPGDLLSLLKDGVRLCRILNEASPLDI-----------KYKESKMPFVQMENISSFINGLKKLR 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 560951910   98 LPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKL------GLAPQI 138
Cdd:COG5199    85 VPEYELFQTNDLFEAKDLRQVVICLYSLSRYAQKErmfsgpFLGPHL 131
RasGAP_RASAL cd05135
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...
 1035-1200 4.18e-09

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: 59.83  E-value: 4.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1035 LRQILAPVVKEIMDDKSLnIKTDPVDIykswvnqMESQTGEASKlpydvtpEQALAHEEVRtrlDNSIRNMRAVTDKFLS 1114
Cdd:cd05135   101 LHEVLKPVINRIFEEKKY-VELDPCKI-------DLNRTRRISF-------KGSLSEAQVR---ESSLELLQGYLGSIID 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1115 AIISSVDKIPYGMRFIAKVLKDSLHEKFPDAGEDELLKI-IGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTtdqrRNLG 1193
Cdd:cd05135   163 AIVGSVDQCPPVMRVAFKQLHKRVEERFPEAEHQDVKYLaISGFLFLRFFAPAILTPKLFQLREQHADPRTS----RTLL 238


                  ....*..
gi 560951910 1194 SIAKMLQ 1200
Cdd:cd05135   239 LLAKAVQ 245
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
 18-125 1.75e-08

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: 53.96  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910   18 EEAKRWMEACLGEDLPPTT---ELEEGLRNGVYLAKLGNFFSPKVVSlkKIYDREQTRYKATGLHFRHTDNVIQWLNAMG 94
Cdd:cd21203     3 YEAAEWIQNVLGVLVLPDPseeEFRLCLRDGVVLCKLLNKLQPGAVP--KVVESPDDPDGAAGSAFQYFENVRNFLVAIE 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 560951910   95 EIGLPkIFYPETTDIYDRKNMPRCIYCIHAL 125
Cdd:cd21203    81 EMGLP-TFEASDLEQGGGGSRPRVVDCILAL 110
RasGAP_GAP1_like cd05128
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...
 988-1201 3.28e-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: 53.79  E-value: 3.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  988 LLLRLFKTALQEEIkSKVDQIQEIVTGNPTVIKMVVSFNRGArGQNALRQILAPVVKEIMDD-KSLNIktDPvdiykswv 1066
Cdd:cd05128    51 QIVPLLRALASREI-SKTQDPNTLFRGNSLASKCMDEFMKLV-GMQYLHETLKPVIDEIFSEkKSCEI--DP-------- 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1067 nqmesqtgeaSKLPYdvtpeqalaheevRTRLDNSIRNMRAVTDKFLSAIISSVDKIPYGMRFIAKVLKDSLHEKFPDAG 1146
Cdd:cd05128   119 ----------SKLKD-------------GEVLETNLANLRGYVERVFKAITSSARRCPTLMCEIFSDLRESAAQRFPDNE 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1147 EDELLKIIGnLLYYRYMNPAIVAPDAFDiidlsaggqLTTDQ-----RRNLGSIAKMLQH 1201
Cdd:cd05128   176 DVPYTAVSG-FIFLRFFAPAILNPKLFG---------LREEHpdpqtARTLTLISKTIQT 225
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 652-679 1.55e-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: 43.29  E-value: 1.55e-05
                          10        20
                  ....*....|....*....|....*...
gi 560951910  652 WVKHWVKGGYHYYHNLETQEGGWDEPPD 679
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
 17-111 1.62e-05

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: 45.79  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910   17 LEEAKRWMEACLGEDLPPtTELEEGLRNGVYLAKLGNFFSPKvvSLKKIyDREQTRYkaTGLhfrhtDNVIQWLNAMGEI 96
Cdd:cd21208     2 LKEARTWIEAVTGKKFPS-DDFRESLEDGILLCELINAIKPG--SIKKI-NRLPTPI--AGL-----DNLNLFLKACEDL 70

                          90
                  ....*....|....*
gi 560951910   97 GLPKIFYPETTDIYD 111
Cdd:cd21208    71 GLKDSQLFDPTDLQD 85
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
 1103-1315 3.45e-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: 47.96  E-value: 3.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1103 RNMRAVTDKFLSAIISSVDKIPygmrfiaKVLKD---SLHEKFPDAGEDELL-KIIGNLLYYRYMNPAIVAPDAFDIIdl 1178
Cdd:cd05136   137 ANLRRSVELAWCKILSSHCVFP-------RELREvfsSWRERLEERGREDIAdRLISASLFLRFLCPAILSPSLFNLT-- 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1179 saggQLTTDQR--RNLGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVT 1256
Cdd:cd05136   208 ----QEYPSERaaRNLTLIAKVIQNLANFTRFGGKEEYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGR 283

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 560951910 1257 ltkpviyisigEIINTHTLLLdhqDAIAPEHNDPIHEllddLGEVPTIESLIGESSGNL 1315
Cdd:cd05136   284 -----------ELSLLHSLLV---EIISKLNQTTLDK----LGPLPRILNDITEALRNP 324
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 745-763 2.21e-04

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 39.62  E-value: 2.21e-04
                            10
                    ....*....|....*....
gi 560951910    745 AITCIQSQWRGYKQRKAYQ 763
Cdd:smart00015    5 AAIIIQAAWRGYLARKRYK 23
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 652-679 3.89e-04

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: 39.12  E-value: 3.89e-04
                            10        20
                    ....*....|....*....|....*...
gi 560951910    652 WVKHWVKGGYHYYHNLETQEGGWDEPPD 679
Cdd:smart00456    6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
RasGAP_p120GAP cd05391
Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ...
 1110-1257 1.19e-03

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


Pssm-ID: 213340  Cd Length: 328  Bit Score: 42.86  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1110 DKFLSAIISSVDKIPYGMRFIAKVLKDSLHEKFPDageDELL--KIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTtd 1187
Cdd:cd05391   140 SELVEKIFMAAEILPPTLRYIYGCLQKSVQQKWPT---NTTVrtRVVSGFVFLRLICPAILNPRMFNIISETPSPTAA-- 214

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 560951910 1188 qrRNLGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQTACDVPELQD---KFNVDEYSDLVTL 1257
Cdd:cd05391   215 --RTLTLVAKSLQNLANLVEFGAKEPYMEGVNPFIKKNKERMIMFLDELGNVPELPDtteHSRTDLSRDLAAL 285
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 745-763 1.19e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 37.68  E-value: 1.19e-03
                           10
                   ....*....|....*....
gi 560951910   745 AITCIQSQWRGYKQRKAYQ 763
Cdd:pfam00612    3 AAIKIQAAWRGYLARKRYK 21
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 652-677 1.25e-03

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 37.87  E-value: 1.25e-03
                           10        20
                   ....*....|....*....|....*.
gi 560951910   652 WVKHWVKGGYHYYHNLETQEGGWDEP 677
Cdd:pfam00397    5 WEERWDPDGRVYYYNHETGETQWEKP 30
RasGAP_CLA2_BUD2 cd05137
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ...
 1031-1240 3.82e-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: 41.40  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1031 GQNALRQILAPVVKEIMDDKsLNIKTDPvdiykswvnqmesqtgeaSKLPYDvtpeqalAHEEVRTRLDNSIRNMRAVTD 1110
Cdd:cd05137   114 GKEYLEKSIGDVIRKICEEN-KDCEVDP------------------SRVKES-------DSIEKEEDLEENWENLISLTE 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910 1111 KFLSAIISSVDKIPYGMRFIAKVLKDSLHEKFPDAGEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDlsagGQLTTDQRR 1190
Cdd:cd05137   168 EIWNSIYITSNDCPPELRKILKHIRAKVEDRYGDFLRTVTLNSVSGFLFLRFFCPAILNPKLFGLLK----DHPRPRAQR 243

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 560951910 1191 NLGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQTACDVP 1240
Cdd:cd05137   244 TLTLIAKVLQNLANLTTFGQKEPWMEPMNEFLTTHREELKDYIDKITGIK 293
COG5022 COG5022
Myosin heavy chain [General function prediction only];
715-940 6.54e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.22  E-value: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  715 LVTKLQACCRGYLVRQEFRSRMNFLKKqvpaitcIQSQWRGYKQRKAYQDRLAYLRShkdevVKIQSLARMHQARKRYRD 794
Cdd:COG5022   747 IATRIQRAIRGRYLRRRYLQALKRIKK-------IQVIQHGFRLRRLVDYELKWRLF-----IKLQPLLSLLGSRKEYRS 814

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  795 RLQYFRDHINDIIK-------------------IQAFIRANKARDDYKTLIN---AEDPPMIV-------------VRKF 839
Cdd:COG5022   815 YLACIIKLQKTIKRekklreteevefslkaevlIQKFGRSLKAKKRFSLLKKetiYLQSAQRVelaerqlqelkidVKSI 894

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560951910  840 VHLLDQSDQDFQEELDLMK-----MREEVITLIRSNQQLENDLNLMDIKIGL---LVKNKItLQDVVSHSKKLt*knKEQ 911
Cdd:COG5022   895 SSLKLVNLELESEIIELKKslssdLIENLEFKTELIARLKKLLNNIDLEEGPsieYVKLPE-LNKLHEVESKL----KET 969

                         250       260
                  ....*....|....*....|....*....
gi 560951910  912 LSDMMMLNKQKGGLKALSKEKREKLEAYQ 940
Cdd:COG5022   970 SEEYEDLLKKSTILVREGNKANSELKNFK 998
 
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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