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Conserved domains on  [gi|40674640|gb|AAH64971|]
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IQGAP1 protein, partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_IQGAP1 cd21274
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif ...
 37-190 7.12e-111

calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif containing GTPase activating protein 1 (IQGAP1), also called p195, is a homodimeric protein that is widely expressed among vertebrate cell types from early embryogenesis. It plays a crucial role in regulating the dynamics and assembly of the actin cytoskeleton. It belongs to the IQGAP family, which consists of multi-domain proteins having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity. It lacks GAP activity. Both, IQGAP1 and IQGAP2, specifically bind to Cdc42 and Rac1, but not to RhoA. Despite similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP1 contains a single copy of the CH domain at the N-terminus.


:

Pssm-ID: 409123 [Multi-domain]  Cd Length: 154  Bit Score: 337.73  E-value: 7.12e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  37 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 116
Cdd:cd21274   1 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40674640 117 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTELE 190
Cdd:cd21274  81 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTELE 154
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 685-710 7.27e-06

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: 7.27e-06
                        10        20
                ....*....|....*....|....*.
gi 40674640 685 WVKHWVKGGYYYYHNLETQEGGWDEP 710
Cdd:cd00201   4 WEERWDPDGRVYYYNHNTKETQWEDP 29
IQG1 super family cl34962
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
 749-933 1.29e-04

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: 46.03  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  749 ITRLQARCRGYLVRQEFRSRMnFLKKQIPAITCIQSQWRGYKQKKAYQDRL-------------------AYLR------ 803
Cdd:COG5261  323 DIRLLIQKRGNKIRLLIQNRM-PQEEDTKFAERLQSNINGRKKYFPLDRRLslfgplffllqssiplfsiAICVgrvkrf 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  804 --SHKDEVVKIQSLARMHQARKRYRDRLQYFRDHINdIIKIQAFIRAN-KARDDYKTLINAEdppMVVVRKFVHLLDQSd 880
Cdd:COG5261  402 siDALLNIVKLQILGNGYEIRKLYSLGKSNCEEHLS-VSLFQMLLRTEvEATSLVQSLLRGN---LPVHRNMTNYFRRS- 476

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 40674640  881 qdfQEELDLMKMREEVITLIRSNQQLENDLNLMDIKIGLLVKNKITLQDVVSH 933
Cdd:COG5261  477 ---QGQAALREIRYQIINDVAIHEDLEVDINPLLVYRALLNKGQLSPDKDLEL 526
 
Name Accession Description Interval E-value
CH_IQGAP1 cd21274
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif ...
 37-190 7.12e-111

calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif containing GTPase activating protein 1 (IQGAP1), also called p195, is a homodimeric protein that is widely expressed among vertebrate cell types from early embryogenesis. It plays a crucial role in regulating the dynamics and assembly of the actin cytoskeleton. It belongs to the IQGAP family, which consists of multi-domain proteins having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity. It lacks GAP activity. Both, IQGAP1 and IQGAP2, specifically bind to Cdc42 and Rac1, but not to RhoA. Despite similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP1 contains a single copy of the CH domain at the N-terminus.


Pssm-ID: 409123 [Multi-domain]  Cd Length: 154  Bit Score: 337.73  E-value: 7.12e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  37 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 116
Cdd:cd21274   1 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40674640 117 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTELE 190
Cdd:cd21274  81 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTELE 154
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
 26-214 4.18e-36

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: 148.11  E-value: 4.18e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640   26 LTAEEMDERRRQNVAYEYLCHLEEAKRWMEACLGEDLPpTTELEEGLRNGVYLAKLGNFFSPKvvSLKKIYdreqtryKA 105
Cdd:COG5261   25 LKTKTSAKNRSALRAYEYLCRVSEAKIWIEEVIEEALP-ELCFEDSLRNGVFLAKLTQRFNPD--LTTVIF-------PA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  106 TGLHFRHTDNVIQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVdFTEEEINNM 185
Cdd:COG5261   95 DKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTPLINSSGQIS-FTKEDIAAC 173

                        170       180
                 ....*....|....*....|....*....
gi 40674640  186 KTELEkygiQMPAFSKIGGILANELSVDE 214
Cdd:COG5261  174 KKAWP----RIPDFKSLGTNINTAASPEE 198
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 48-158 3.07e-15

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 72.32  E-value: 3.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640    48 EEAKRWMEACLGEDLPPT--TELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREqtrykatglhFRHTDNVIQWLN-AMD 124
Cdd:pfam00307   5 KELLRWINSHLAEYGPGVrvTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSE----------FDKLENINLALDvAEK 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 40674640   125 EIGLPKIFyPETTDIYDRKNMpRCIYCIHALSLY 158
Cdd:pfam00307  75 KLGVPKVL-IEPEDLVEGDNK-SVLTYLASLFRR 106
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 48-155 4.03e-15

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 71.96  E-value: 4.03e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640     48 EEAKRWMEACLGEDLPPT-TELEEGLRNGVYLAKLGNFFSPKVVSLKKIydreqtryKATGLHFRHTDNVIQWLNAMDEI 126
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPvTNFSSDLKDGVALCALLNSLSPGLVDKKKV--------AASLSRFKKIENINLALSFAEKL 72

                           90       100       110
                   ....*....|....*....|....*....|
gi 40674640    127 GlPKIFYPETTDIYD-RKNMPRCIYCIHAL 155
Cdd:smart00033  73 G-GKVVLFEPEDLVEgPKLILGVIWTLISL 101
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 685-710 7.27e-06

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: 7.27e-06
                        10        20
                ....*....|....*....|....*.
gi 40674640 685 WVKHWVKGGYYYYHNLETQEGGWDEP 710
Cdd:cd00201   4 WEERWDPDGRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 685-712 1.09e-05

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 42.97  E-value: 1.09e-05
                           10        20
                   ....*....|....*....|....*...
gi 40674640    685 WVKHWVKGGYYYYHNLETQEGGWDEPPN 712
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
 749-933 1.29e-04

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: 46.03  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  749 ITRLQARCRGYLVRQEFRSRMnFLKKQIPAITCIQSQWRGYKQKKAYQDRL-------------------AYLR------ 803
Cdd:COG5261  323 DIRLLIQKRGNKIRLLIQNRM-PQEEDTKFAERLQSNINGRKKYFPLDRRLslfgplffllqssiplfsiAICVgrvkrf 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  804 --SHKDEVVKIQSLARMHQARKRYRDRLQYFRDHINdIIKIQAFIRAN-KARDDYKTLINAEdppMVVVRKFVHLLDQSd 880
Cdd:COG5261  402 siDALLNIVKLQILGNGYEIRKLYSLGKSNCEEHLS-VSLFQMLLRTEvEATSLVQSLLRGN---LPVHRNMTNYFRRS- 476

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 40674640  881 qdfQEELDLMKMREEVITLIRSNQQLENDLNLMDIKIGLLVKNKITLQDVVSH 933
Cdd:COG5261  477 ---QGQAALREIRYQIINDVAIHEDLEVDINPLLVYRALLNKGQLSPDKDLEL 526
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 685-710 2.00e-04

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: 39.41  E-value: 2.00e-04
                          10        20
                  ....*....|....*....|....*.
gi 40674640   685 WVKHWVKGGYYYYHNLETQEGGWDEP 710
Cdd:pfam00397   5 WEERWDPDGRVYYYNHETGETQWEKP 30
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 774-796 2.35e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.15  E-value: 2.35e-03
                           10        20
                   ....*....|....*....|...
gi 40674640    774 KQIPAITCIQSQWRGYKQKKAYQ 796
Cdd:smart00015   1 RLTRAAIIIQAAWRGYLARKRYK 23
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 778-796 9.65e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.22  E-value: 9.65e-03
                          10
                  ....*....|....*....
gi 40674640   778 AITCIQSQWRGYKQKKAYQ 796
Cdd:pfam00612   3 AAIKIQAAWRGYLARKRYK 21
 
Name Accession Description Interval E-value
CH_IQGAP1 cd21274
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif ...
 37-190 7.12e-111

calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif containing GTPase activating protein 1 (IQGAP1), also called p195, is a homodimeric protein that is widely expressed among vertebrate cell types from early embryogenesis. It plays a crucial role in regulating the dynamics and assembly of the actin cytoskeleton. It belongs to the IQGAP family, which consists of multi-domain proteins having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity. It lacks GAP activity. Both, IQGAP1 and IQGAP2, specifically bind to Cdc42 and Rac1, but not to RhoA. Despite similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP1 contains a single copy of the CH domain at the N-terminus.


Pssm-ID: 409123 [Multi-domain]  Cd Length: 154  Bit Score: 337.73  E-value: 7.12e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  37 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 116
Cdd:cd21274   1 QNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNV 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40674640 117 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTELE 190
Cdd:cd21274  81 IQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTELE 154
CH_IQGAP2 cd21275
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP2; IQ motif ...
 14-169 1.67e-108

calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP2; IQ motif containing GTPase activating protein 2 (IQGAP2) is a member of the IQGAP family, which consists of multi-domain proteins having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP2 binds to activated Cdc42 and Rac1 but does not seem to stimulate their GTPase activity. It associates with calmodulin. IQGAP2 contains a single copy of the CH domain at the N-terminus.


Pssm-ID: 409124 [Multi-domain]  Cd Length: 156  Bit Score: 331.60  E-value: 1.67e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  14 RPHYGSVLDNERLTAEEMDERRRQNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLK 93
Cdd:cd21275   1 RPRYGSIVDDERLSAEEMDERRRQNIAYEYLCHLEEAKQWIEACLNEELPPTTELEEGLRNGVYLVKLAKFFAPKLVSEK 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40674640  94 KIYDREQTRYKATGLHFRHTDNVIQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQ 169
Cdd:cd21275  81 KIYDVDQVRYKRSGLHFRHTDNTVQWLRAMESIGLPKIFYPETTDVYDRKNMPRVIYCIHALSLYLFKLGIAPQIQ 156
CH_IQGAP3 cd21276
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP3; IQ motif ...
 38-189 3.18e-101

calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP3; IQ motif containing GTPase activating protein 3 (IQGAP3) associates with Ras GTP-binding proteins. It regulates the organization of the cytoskeleton under the regulation of Rac1 and Cdc42 in neuronal cells. The depletion of IQGAP3 is shown to impair neurite or axon outgrowth in neuronal cells with disorganized cytoskeleton. It belongs to the IQGAP family, which consists of multi-domain proteins having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP3 contains a single copy of the CH domain at the N-terminus.


Pssm-ID: 409125 [Multi-domain]  Cd Length: 152  Bit Score: 312.30  E-value: 3.18e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  38 NVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNVI 117
Cdd:cd21276   1 NVAYQYLCRLEEAKRWMEACLKEELPPPTELEESLRNGVYLAKLGHCFAPRVVPLKKIYDLEQMRYQATGLHFRHTDNIN 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40674640 118 QWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTEL 189
Cdd:cd21276  81 HWRNAMMHIGLPSIFHPETTDIYDKKNMPRVVYCIHALSLYLFRLGLAPQIHDLYGKVKFTEEEINNMKLEL 152
CH_IQGAP cd21206
calponin homology (CH) domain found in the IQ motif containing GTPase activating protein ...
 38-163 1.17e-71

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


Pssm-ID: 409055 [Multi-domain]  Cd Length: 118  Bit Score: 232.12  E-value: 1.17e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  38 NVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDreqtrykaTGLHFRHTDNVI 117
Cdd:cd21206   1 TIAYEYLCRLEEAKQWIEACLNEELPPTTEFEEELRNGVVLAKLANKFAPKLVPLKKIYD--------VGLQFRHTDNIN 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 40674640 118 QWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLG 163
Cdd:cd21206  73 HFLRALKKIGLPKIFHFETTDLYEKKNIPKVIYCLHALSLLLFKLG 118
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
 26-214 4.18e-36

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: 148.11  E-value: 4.18e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640   26 LTAEEMDERRRQNVAYEYLCHLEEAKRWMEACLGEDLPpTTELEEGLRNGVYLAKLGNFFSPKvvSLKKIYdreqtryKA 105
Cdd:COG5261   25 LKTKTSAKNRSALRAYEYLCRVSEAKIWIEEVIEEALP-ELCFEDSLRNGVFLAKLTQRFNPD--LTTVIF-------PA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  106 TGLHFRHTDNVIQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVdFTEEEINNM 185
Cdd:COG5261   95 DKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPGKTPLINSSGQIS-FTKEDIAAC 173

                        170       180
                 ....*....|....*....|....*....
gi 40674640  186 KTELEkygiQMPAFSKIGGILANELSVDE 214
Cdd:COG5261  174 KKAWP----RIPDFKSLGTNINTAASPEE 198
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 47-157 5.18e-26

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 102.80  E-value: 5.18e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  47 LEEAKRWMEACLGEDLP-PTTELEEGLRNGVYLAKLGNFFSPKVVSLKKiydreqtryKATGLHFRHTDNVIQWLNAMDE 125
Cdd:cd00014   1 EEELLKWINEVLGEELPvSITDLFESLRDGVLLCKLINKLSPGSIPKIN---------KKPKSPFKKRENINLFLNACKK 71

                        90       100       110
                ....*....|....*....|....*....|..
gi 40674640 126 IGLPKIFYPETTDIYDRKNMPRCIYCIHALSL 157
Cdd:cd00014  72 LGLPELDLFEPEDLYEKGNLKKVLGTLWALAL 103
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 48-158 3.07e-15

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 72.32  E-value: 3.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640    48 EEAKRWMEACLGEDLPPT--TELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREqtrykatglhFRHTDNVIQWLN-AMD 124
Cdd:pfam00307   5 KELLRWINSHLAEYGPGVrvTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSE----------FDKLENINLALDvAEK 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 40674640   125 EIGLPKIFyPETTDIYDRKNMpRCIYCIHALSLY 158
Cdd:pfam00307  75 KLGVPKVL-IEPEDLVEGDNK-SVLTYLASLFRR 106
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 48-155 4.03e-15

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 71.96  E-value: 4.03e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640     48 EEAKRWMEACLGEDLPPT-TELEEGLRNGVYLAKLGNFFSPKVVSLKKIydreqtryKATGLHFRHTDNVIQWLNAMDEI 126
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPvTNFSSDLKDGVALCALLNSLSPGLVDKKKV--------AASLSRFKKIENINLALSFAEKL 72

                           90       100       110
                   ....*....|....*....|....*....|
gi 40674640    127 GlPKIFYPETTDIYD-RKNMPRCIYCIHAL 155
Cdd:smart00033  73 G-GKVVLFEPEDLVEgPKLILGVIWTLISL 101
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
 49-155 2.86e-14

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


Pssm-ID: 409056 [Multi-domain]  Cd Length: 107  Bit Score: 69.65  E-value: 2.86e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  49 EAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKvvSLKKIydreqtryKATGLHFRHTDNVIQWLNAMDEIGL 128
Cdd:cd21207   9 EALDWIEAVTGEKLDDGKDYEDVLKDGVILCKLINILKPG--SVKKI--------NTSKMAFKLMENIENFLTACKGYGV 78

                        90       100
                ....*....|....*....|....*..
gi 40674640 129 PKIFYPETTDIYDRKNMPRCIYCIHAL 155
Cdd:cd21207  79 PKTDLFQTVDLYEKKNIPQVTNCLFAL 105
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
 48-156 3.66e-13

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


Pssm-ID: 409059 [Multi-domain]  Cd Length: 101  Bit Score: 66.24  E-value: 3.66e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  48 EEAKRWMEACLGEDLPPTTeLEEGLRNGVYLAKLGNffspkvvslkKIYDREQTRYKATGLHFRHTDNVIQWLNAMDEIG 127
Cdd:cd21210   3 QEAREWIEEVLGEKLAQGD-LLDALKDGVVLCKLAN----------RILPADIRKYKESKMPFVQMENISAFLNAARKLG 71

                        90       100
                ....*....|....*....|....*....
gi 40674640 128 LPKIFYPETTDIYDRKNMPRCIYCIHALS 156
Cdd:cd21210  72 VPENDLFQTVDLFERKNPAQVLQCLHALS 100
SCP1 COG5199
Calponin [Cytoskeleton];
48-168 4.78e-10

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 59.55  E-value: 4.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  48 EEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVslkkiydreqtRYKATGLHFRHTDNVIQWLNAMDEIG 127
Cdd:COG5199  16 KEVTLWIETVLGEKFEPPGDLLSLLKDGVRLCRILNEASPLDI-----------KYKESKMPFVQMENISSFINGLKKLR 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 40674640 128 LPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKL------GLAPQI 168
Cdd:COG5199  85 VPEYELFQTNDLFEAKDLRQVVICLYSLSRYAQKErmfsgpFLGPHL 131
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
 48-155 1.20e-09

calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. This family includes a group of kinesin-like proteins belonging to KIN-14 protein family. They all contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409052 [Multi-domain]  Cd Length: 112  Bit Score: 56.65  E-value: 1.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  48 EEAKRWMEACLGEDLPPTT---ELEEGLRNGVYLAKLGNFFSPKVVSlkKIYDREQTRYKATGLHFRHTDNVIQWLNAMD 124
Cdd:cd21203   3 YEAAEWIQNVLGVLVLPDPseeEFRLCLRDGVVLCKLLNKLQPGAVP--KVVESPDDPDGAAGSAFQYFENVRNFLVAIE 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 40674640 125 EIGLPkIFYPETTDIYDRKNMPRCIYCIHAL 155
Cdd:cd21203  81 EMGLP-TFEASDLEQGGGGSRPRVVDCILAL 110
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
 47-141 1.85e-06

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


Pssm-ID: 409057 [Multi-domain]  Cd Length: 119  Bit Score: 47.72  E-value: 1.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  47 LEEAKRWMEACLGEDLPPtTELEEGLRNGVYLAKLGNFFSPKvvSLKKIyDREQTRYkaTGLhfrhtDNVIQWLNAMDEI 126
Cdd:cd21208   2 LKEARTWIEAVTGKKFPS-DDFRESLEDGILLCELINAIKPG--SIKKI-NRLPTPI--AGL-----DNLNLFLKACEDL 70

                        90
                ....*....|....*
gi 40674640 127 GLPKIFYPETTDIYD 141
Cdd:cd21208  71 GLKDSQLFDPTDLQD 85
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 685-710 7.27e-06

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: 7.27e-06
                        10        20
                ....*....|....*....|....*.
gi 40674640 685 WVKHWVKGGYYYYHNLETQEGGWDEP 710
Cdd:cd00201   4 WEERWDPDGRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 685-712 1.09e-05

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 42.97  E-value: 1.09e-05
                           10        20
                   ....*....|....*....|....*...
gi 40674640    685 WVKHWVKGGYYYYHNLETQEGGWDEPPN 712
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
 749-933 1.29e-04

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: 46.03  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  749 ITRLQARCRGYLVRQEFRSRMnFLKKQIPAITCIQSQWRGYKQKKAYQDRL-------------------AYLR------ 803
Cdd:COG5261  323 DIRLLIQKRGNKIRLLIQNRM-PQEEDTKFAERLQSNINGRKKYFPLDRRLslfgplffllqssiplfsiAICVgrvkrf 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  804 --SHKDEVVKIQSLARMHQARKRYRDRLQYFRDHINdIIKIQAFIRAN-KARDDYKTLINAEdppMVVVRKFVHLLDQSd 880
Cdd:COG5261  402 siDALLNIVKLQILGNGYEIRKLYSLGKSNCEEHLS-VSLFQMLLRTEvEATSLVQSLLRGN---LPVHRNMTNYFRRS- 476

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 40674640  881 qdfQEELDLMKMREEVITLIRSNQQLENDLNLMDIKIGLLVKNKITLQDVVSH 933
Cdd:COG5261  477 ---QGQAALREIRYQIINDVAIHEDLEVDINPLLVYRALLNKGQLSPDKDLEL 526
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 685-710 2.00e-04

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: 39.41  E-value: 2.00e-04
                          10        20
                  ....*....|....*....|....*.
gi 40674640   685 WVKHWVKGGYYYYHNLETQEGGWDEP 710
Cdd:pfam00397   5 WEERWDPDGRVYYYNHETGETQWEKP 30
CH_TAGLN cd21279
calponin homology (CH) domain found in transgelin; Transgelin, also called 22 kDa ...
 52-145 7.54e-04

calponin homology (CH) domain found in transgelin; Transgelin, also called 22 kDa actin-binding protein, protein WS3-10, or smooth muscle protein 22-alpha (SM22-alpha), acts as an actin cross-linking/gelling protein that may be involved in calcium interactions and in regulating contractile properties of the cell. It may also contribute to replicative senescence. Transgelin contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409128 [Multi-domain]  Cd Length: 121  Bit Score: 40.38  E-value: 7.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  52 RWMEACLGEDL--PPTTEL--EEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTrykatgLHFRHTDNVIQWLNAMDEIG 127
Cdd:cd21279  10 EWIVVQCGPDVgrPDRGRLgfQVWLKNGVVLSKLVNSLYPDGSKPVKIPDNPPS------MVFKQMEQVAQFLKAAEDYG 83

                        90
                ....*....|....*...
gi 40674640 128 LPKIFYPETTDIYDRKNM 145
Cdd:cd21279  84 VVKTDMFQTVDLYEGKDM 101
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 774-796 2.35e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.15  E-value: 2.35e-03
                           10        20
                   ....*....|....*....|...
gi 40674640    774 KQIPAITCIQSQWRGYKQKKAYQ 796
Cdd:smart00015   1 RLTRAAIIIQAAWRGYLARKRYK 23
CH_VAV1 cd21262
calponin homology (CH) domain found in VAV1 protein; VAV1 is expressed predominantly in the ...
 52-156 3.91e-03

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


Pssm-ID: 409111  Cd Length: 120  Bit Score: 38.38  E-value: 3.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  52 RWMEAClgEDLPPT----------TELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRykatglHFRHTDNVIQWLN 121
Cdd:cd21262   8 HWLIQC--RVLPPNhrvtwdsaqvCDLAQALRDGVLLCQLLNNLLPHAVNLREINLRPQMS------QFLCLKNIRTFLS 79

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 40674640 122 A-MDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALS 156
Cdd:cd21262  80 TcCEKFGLRKSELFEAFDLFDVRDFGKVIDTLSILS 115
CH_TAGLN-like cd21209
calponin homology (CH) domain found in the transgelin family; The transgelin (TAGLN) family ...
 53-145 5.74e-03

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


Pssm-ID: 409058 [Multi-domain]  Cd Length: 119  Bit Score: 37.88  E-value: 5.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40674640  53 WMEACLGEDL----PPTTELEEGLRNGVYLAKLGN-FFSPKVVSLKKIydreqtryKATGLHFRHTDNVIQWLNAMDEIG 127
Cdd:cd21209  11 WIVAQCGSDVgrpdPGRLGFQKWLKDGTVLCKLINsLYPEGSKPVKKI--------QSSKMAFKQMEQISQFLKAAEDYG 82

                        90
                ....*....|....*...
gi 40674640 128 LPKIFYPETTDIYDRKNM 145
Cdd:cd21209  83 VRTTDIFQTVDLWEGKDM 100
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 778-796 9.65e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.22  E-value: 9.65e-03
                          10
                  ....*....|....*....
gi 40674640   778 AITCIQSQWRGYKQKKAYQ 796
Cdd:pfam00612   3 AAIKIQAAWRGYLARKRYK 21
 
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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