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Conserved domains on  [gi|1959422415|gb|KAG2021437|]
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hypothetical protein GB937_004774 [Aspergillus fischeri]

Protein Classification

LIM1_Lrg1p_like and RhoGAP_fLRG1 domain-containing protein( domain architecture ID 10175094)

protein containing domains LIM1_Lrg1p_like, LIM2_Lrg1p_like, LIM, and RhoGAP_fLRG1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
860-1070 2.79e-138

RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal LRG1-like proteins. Yeast Lrg1p is required for efficient cell fusion, and mother-daughter cell separation, possibly through acting as a RhoGAP specifically regulating 1,3-beta-glucan synthesis. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


:

Pssm-ID: 239862  Cd Length: 213  Bit Score: 418.31  E-value: 2.79e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  860 FGVSLDFLVEKEGTESTHGVGPGALRVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYDQV-DLTKETP 938
Cdd:cd04397      1 FGVPLEILVEKFGADSTLGVGPGKLRIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVpDLSKENP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  939 VQIAALLKKFLREMPDPLLTFKLHNLFVISQKIPDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSSFSHVDEDTGS 1018
Cdd:cd04397     81 VQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSFSHIDEETGS 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1959422415 1019 KMDIHNLATVITPNILYPNTKNS-TVDESFLAIEAVNALITYNDTMCEIPEDL 1070
Cdd:cd04397    161 KMDIHNLATVITPNILYSKTDNPnTGDEYFLAIEAVNYLIENNEEFCEVPDEL 213
LIM1_Lrg1p_like cd09391
The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The first LIM ...
126-182 4.12e-35

The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


:

Pssm-ID: 188777  Cd Length: 57  Bit Score: 127.42  E-value: 4.12e-35
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGQIVASKFFPVDAEDGSGQYPLCETDY 182
Cdd:cd09391      1 CAKCGKPITGQFVRALGDVYHLDCFTCHDCGKPVASKFFPVDDPDTSEQVPLCETDY 57
LIM2_Lrg1p_like cd09392
The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The second LIM ...
190-242 1.23e-33

The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


:

Pssm-ID: 188778 [Multi-domain]  Cd Length: 53  Bit Score: 123.24  E-value: 1.23e-33
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFGAQDSYYEHEGRVYCHFHY 242
Cdd:cd09392      1 CFKCGGALRGSYITALGRKYHVEHFTCSVCPTVFGPNDSYYEHEGKIYCHYHY 53
LIM super family cl02475
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
501-558 2.02e-11

LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).


The actual alignment was detected with superfamily member cd09393:

Pssm-ID: 413332  Cd Length: 56  Bit Score: 60.02  E-value: 2.02e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1959422415  501 CAACKEPIDDECIMLGESRWHLKPphLTCAACQTDLTDTCQEALWSPRIKKVFCNSCA 558
Cdd:cd09393      1 CASCGKSIEDECIKFEDKRWHLKC--FTCSRCHREISSELSDAAFNNKDQRILCSNCS 56
 
Name Accession Description Interval E-value
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
860-1070 2.79e-138

RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal LRG1-like proteins. Yeast Lrg1p is required for efficient cell fusion, and mother-daughter cell separation, possibly through acting as a RhoGAP specifically regulating 1,3-beta-glucan synthesis. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239862  Cd Length: 213  Bit Score: 418.31  E-value: 2.79e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  860 FGVSLDFLVEKEGTESTHGVGPGALRVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYDQV-DLTKETP 938
Cdd:cd04397      1 FGVPLEILVEKFGADSTLGVGPGKLRIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVpDLSKENP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  939 VQIAALLKKFLREMPDPLLTFKLHNLFVISQKIPDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSSFSHVDEDTGS 1018
Cdd:cd04397     81 VQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSFSHIDEETGS 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1959422415 1019 KMDIHNLATVITPNILYPNTKNS-TVDESFLAIEAVNALITYNDTMCEIPEDL 1070
Cdd:cd04397    161 KMDIHNLATVITPNILYSKTDNPnTGDEYFLAIEAVNYLIENNEEFCEVPDEL 213
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
887-1038 1.93e-44

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 459875  Cd Length: 148  Bit Score: 157.71  E-value: 1.93e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  887 PALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMID-NKYDQVDLTKETPVQIAALLKKFLREMPDPLLTFKLHNLF 965
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDrGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1959422415  966 VISQKIPDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSSFSHVdedtgSKMDIHNLATVITPNILYPNT 1038
Cdd:pfam00620   81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDV-----NKMNAHNLAIVFGPTLLRPPD 148
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
885-1041 1.41e-43

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 156.27  E-value: 1.41e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415   885 RVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDN-KYDQVDLTKETPVQIAALLKKFLREMPDPLLTFKLHN 963
Cdd:smart00324    2 PIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSgPDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELYE 81
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1959422415   964 LFVISQKIPDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSSFSHVdedtgSKMDIHNLATVITPNILYPNTKNS 1041
Cdd:smart00324   82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEE-----NKMTARNLAIVFGPTLLRPPDGEV 154
LIM1_Lrg1p_like cd09391
The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The first LIM ...
126-182 4.12e-35

The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188777  Cd Length: 57  Bit Score: 127.42  E-value: 4.12e-35
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGQIVASKFFPVDAEDGSGQYPLCETDY 182
Cdd:cd09391      1 CAKCGKPITGQFVRALGDVYHLDCFTCHDCGKPVASKFFPVDDPDTSEQVPLCETDY 57
LIM2_Lrg1p_like cd09392
The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The second LIM ...
190-242 1.23e-33

The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188778 [Multi-domain]  Cd Length: 53  Bit Score: 123.24  E-value: 1.23e-33
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFGAQDSYYEHEGRVYCHFHY 242
Cdd:cd09392      1 CFKCGGALRGSYITALGRKYHVEHFTCSVCPTVFGPNDSYYEHEGKIYCHYHY 53
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
190-246 2.14e-13

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 65.82  E-value: 2.14e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1959422415  190 CHECGGALRGSYIT-ALDHKYHIEHFTCSVCPTVFGAQDsYYEHEGRVYCHFHYSTQF 246
Cdd:pfam00412    1 CAGCNRPIYDRELVrALGKVWHPECFRCAVCGKPLTTGD-FYEKDGKLYCKHDYYKLF 57
LIM3_Lrg1p_like cd09393
The third LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The third LIM ...
501-558 2.02e-11

The third LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The third LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188779  Cd Length: 56  Bit Score: 60.02  E-value: 2.02e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1959422415  501 CAACKEPIDDECIMLGESRWHLKPphLTCAACQTDLTDTCQEALWSPRIKKVFCNSCA 558
Cdd:cd09393      1 CASCGKSIEDECIKFEDKRWHLKC--FTCSRCHREISSELSDAAFNNKDQRILCSNCS 56
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
126-185 5.09e-11

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 58.88  E-value: 5.09e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1959422415  126 CKKCGEPLTGQF-VRALGATYHLECFKCEDCGQIVASK-FFPVDAEdgsgqyPLCETDYFRR 185
Cdd:pfam00412    1 CAGCNRPIYDRElVRALGKVWHPECFRCAVCGKPLTTGdFYEKDGK------LYCKHDYYKL 56
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
125-181 5.65e-09

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 53.16  E-value: 5.65e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1959422415   125 ICKKCGEPLTG--QFVRALGATYHLECFKCEDCGQIVASKFFpvDAEDGSgqyPLCETD 181
Cdd:smart00132    1 KCAGCGKPIYGteRVLRALGKVWHPECFKCATCGKPLSGDTF--FEKDGK---LYCKDC 54
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
190-238 1.46e-08

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 52.00  E-value: 1.46e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1959422415   190 CHECGGALRGS--YITALDHKYHIEHFTCSVCPTVFGaQDSYYEHEGRVYC 238
Cdd:smart00132    2 CAGCGKPIYGTerVLRALGKVWHPECFKCATCGKPLS-GDTFFEKDGKLYC 51
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
501-557 2.65e-06

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 45.79  E-value: 2.65e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1959422415  501 CAACKEPIDDECIMLG-ESRWHlkPPHLTCAACQTDLTDTCQealwSPRIKKVFCNSC 557
Cdd:pfam00412    1 CAGCNRPIYDRELVRAlGKVWH--PECFRCAVCGKPLTTGDF----YEKDGKLYCKHD 52
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
500-557 1.91e-04

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 40.44  E-value: 1.91e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1959422415   500 CCAACKEPIDDECIML--GESRWHlkPPHLTCAACQTDLT-DTCQEalwspRIKKVFCNSC 557
Cdd:smart00132    1 KCAGCGKPIYGTERVLraLGKVWH--PECFKCATCGKPLSgDTFFE-----KDGKLYCKDC 54
 
Name Accession Description Interval E-value
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
860-1070 2.79e-138

RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal LRG1-like proteins. Yeast Lrg1p is required for efficient cell fusion, and mother-daughter cell separation, possibly through acting as a RhoGAP specifically regulating 1,3-beta-glucan synthesis. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239862  Cd Length: 213  Bit Score: 418.31  E-value: 2.79e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  860 FGVSLDFLVEKEGTESTHGVGPGALRVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYDQV-DLTKETP 938
Cdd:cd04397      1 FGVPLEILVEKFGADSTLGVGPGKLRIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVpDLSKENP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  939 VQIAALLKKFLREMPDPLLTFKLHNLFVISQKIPDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSSFSHVDEDTGS 1018
Cdd:cd04397     81 VQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSFSHIDEETGS 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1959422415 1019 KMDIHNLATVITPNILYPNTKNS-TVDESFLAIEAVNALITYNDTMCEIPEDL 1070
Cdd:cd04397    161 KMDIHNLATVITPNILYSKTDNPnTGDEYFLAIEAVNYLIENNEEFCEVPDEL 213
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
887-1038 1.93e-44

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 459875  Cd Length: 148  Bit Score: 157.71  E-value: 1.93e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  887 PALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMID-NKYDQVDLTKETPVQIAALLKKFLREMPDPLLTFKLHNLF 965
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDrGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1959422415  966 VISQKIPDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSSFSHVdedtgSKMDIHNLATVITPNILYPNT 1038
Cdd:pfam00620   81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDV-----NKMNAHNLAIVFGPTLLRPPD 148
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
885-1041 1.41e-43

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 156.27  E-value: 1.41e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415   885 RVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDN-KYDQVDLTKETPVQIAALLKKFLREMPDPLLTFKLHN 963
Cdd:smart00324    2 PIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSgPDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELYE 81
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1959422415   964 LFVISQKIPDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSSFSHVdedtgSKMDIHNLATVITPNILYPNTKNS 1041
Cdd:smart00324   82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEE-----NKMTARNLAIVFGPTLLRPPDGEV 154
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
887-1059 2.88e-39

RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like small GTPases. Small GTPases (G proteins) cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when bound to GDP. The Rho family of small G proteins, which includes Cdc42Hs, activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. G proteins generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude. The RhoGAPs are one of the major classes of regulators of Rho G proteins.


Pssm-ID: 238090 [Multi-domain]  Cd Length: 169  Bit Score: 143.60  E-value: 2.88e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  887 PALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYDQVDLTKETPVQIAALLKKFLREMPDPLLTFKLHNLFV 966
Cdd:cd00159      1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  967 ISQKIPDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSSFSHVdedtgSKMDIHNLATVITPNILYPNTKNSTVDES 1046
Cdd:cd00159     81 ELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEV-----NKMTASNLAIVFAPTLLRPPDSDDELLED 155
                          170
                   ....*....|....
gi 1959422415 1047 F-LAIEAVNALITY 1059
Cdd:cd00159    156 IkKLNEIVEFLIEN 169
LIM1_Lrg1p_like cd09391
The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The first LIM ...
126-182 4.12e-35

The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188777  Cd Length: 57  Bit Score: 127.42  E-value: 4.12e-35
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGQIVASKFFPVDAEDGSGQYPLCETDY 182
Cdd:cd09391      1 CAKCGKPITGQFVRALGDVYHLDCFTCHDCGKPVASKFFPVDDPDTSEQVPLCETDY 57
LIM2_Lrg1p_like cd09392
The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The second LIM ...
190-242 1.23e-33

The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188778 [Multi-domain]  Cd Length: 53  Bit Score: 123.24  E-value: 1.23e-33
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFGAQDSYYEHEGRVYCHFHY 242
Cdd:cd09392      1 CFKCGGALRGSYITALGRKYHVEHFTCSVCPTVFGPNDSYYEHEGKIYCHYHY 53
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
859-1072 3.64e-31

RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP18-like proteins. The function of ArhGAP18 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239856  Cd Length: 216  Bit Score: 122.07  E-value: 3.64e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  859 VFGVSLDFLVEKEGTESthgvgPGaLRVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKY--DQVDLTKE 936
Cdd:cd04391      1 LFGVPLSTLLERDQKKV-----PG-SKVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAKFyeGTFLWDQV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  937 TPVQIAALLKKFLREMPDPLLTFKLHNLFVISQKIPDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTssfshVDEDT 1016
Cdd:cd04391     75 KQHDAASLLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKV-----VDHEE 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1959422415 1017 GSKMDIHNLATVITPNILYPNTKNSTVDES-----FLAIEA---VNALITYNDTMCEIPEDLQA 1072
Cdd:cd04391    150 KNKMNLWNVAMIMAPNLFPPRGKHSKDNESlqeevNMAAGCaniMRLLIRYQDLLWTVPSFLIN 213
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
879-1070 3.91e-29

RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP6-like proteins. ArhGAP6 shows GAP activity towards RhoA, but not towards Cdc42 and Rac1. ArhGAP6 is often deleted in microphthalmia with linear skin defects syndrome (MLS); MLS is a severe X-linked developmental disorder. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239841  Cd Length: 206  Bit Score: 116.00  E-value: 3.91e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  879 VGPGALRVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYDQVDLTKETPVQIAALLKKFLREMPDPLLT 958
Cdd:cd04376      2 LNPIARQVPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENHSVHDVAALLKEFFRDMPDPLLP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  959 FKLHNLFVISQKIpDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTS--SFSHVDED----TGSKMDIHNLATVITPN 1032
Cdd:cd04376     82 RELYTAFIGTALL-EPDEQLEALQLLIYLLPPCNCDTLHRLLKFLHTVAehAADSIDEDgqevSGNKMTSLNLATIFGPN 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1959422415 1033 ILY--------PNTKNSTVDESFLAIEAVNALITYNDTMCEIPEDL 1070
Cdd:cd04376    161 LLHkqksgereFVQASLRIEESTAIINVVQTMIDNYEELFMVSPEL 206
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
859-1068 6.74e-29

RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP11A-like proteins. The mouse homolog of human ArhGAP11A has been detected as a gene exclusively expressed in immature ganglion cells, potentially playing a role in retinal development. The exact function of ArhGAP11A is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239859 [Multi-domain]  Cd Length: 202  Bit Score: 115.26  E-value: 6.74e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  859 VFGVSLDFLVEKEGTESTHgvgpgalrVPALVDDAVSAMRQmDMSVEGVFRKNGNIRRLKEISEMIDNKYDQvdLTKETP 938
Cdd:cd04394      1 VFGVPLHSLPHSTVPEYGN--------VPKFLVDACTFLLD-HLSTEGLFRKSGSVVRQKELKAKLEGGEAC--LSSALP 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  939 VQIAALLKKFLREMPDPLLTFKLHNLFVISQKIPDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSsfSHVDEDtgs 1018
Cdd:cd04394     70 CDVAGLLKQFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVA--QRCSEN--- 144
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1959422415 1019 KMDIHNLATVITPNILYPNTKNSTVDESF---LAIEA--VNALITYNDTMCEIPE 1068
Cdd:cd04394    145 KMDSSNLAVIFAPNLFQSEEGGEKMSSSTekrLRLQAavVQTLIDNASNIGIVPD 199
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
860-1057 1.41e-25

RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p50RhoGAP-like proteins; p50RhoGAP, also known as RhoGAP-1, contains a C-terminal RhoGAP domain and an N-terminal Sec14 domain which binds phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). It is ubiquitously expressed and preferentially active on Cdc42. This subgroup also contains closely related ARHGAP8. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239869 [Multi-domain]  Cd Length: 195  Bit Score: 105.50  E-value: 1.41e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  860 FGVSLDFLVEKegtesthgvGPGALRVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIdNKYDQVDLTKETPV 939
Cdd:cd04404      6 FGVSLQFLKEK---------NPEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKY-NMGEPVDFDQYEDV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  940 QIAA-LLKKFLREMPDPLLTFKLHNLFVISQKIPDPEKQKRLLHLTcCLLPKAHRDTMEVLFAFLNWTSSFSHVDedtgs 1018
Cdd:cd04404     76 HLPAvILKTFLRELPEPLLTFDLYDDIVGFLNVDKEERVERVKQLL-QTLPEENYQVLKYLIKFLVQVSAHSDQN----- 149
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1959422415 1019 KMDIHNLATVITPNILYPntKNSTVdeSFLAIEAVNALI 1057
Cdd:cd04404    150 KMTNSNLAVVFGPNLLWA--KDASM--SLSAINPINTFT 184
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
860-1034 7.89e-24

RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in class IX myosins. Class IX myosins contain a characteristic head domain, a neck domain, a tail domain which contains a C6H2-zinc binding motif and a RhoGAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239842  Cd Length: 186  Bit Score: 100.21  E-value: 7.89e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  860 FGVSLDFLVEKEGTesthgvgpgalrVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYDQVDLTKETPV 939
Cdd:cd04377      1 FGVSLSSLTSEDRS------------VPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIH 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  940 QIAALLKKFLREMPDPLLTFKLHNLFVISQKIPDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSsfshvDEDTGSK 1019
Cdd:cd04377     69 VITSVLKQWLRELPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVA-----LQEEVNR 143
                          170
                   ....*....|....*
gi 1959422415 1020 MDIHNLATVITPNIL 1034
Cdd:cd04377    144 MSANALAIVFAPCIL 158
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
859-1057 1.73e-23

RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Nadrin-like proteins. Nadrin, also named Rich-1, has been shown to be involved in the regulation of Ca2+-dependent exocytosis in neurons and recently has been implicated in tight junction maintenance in mammalian epithelium. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239851  Cd Length: 203  Bit Score: 99.45  E-value: 1.73e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  859 VFGVSLDFLVEKEGTEsthgvgpgalrVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYDQVDLTKE-- 936
Cdd:cd04386      4 VFGTPLEEHLKRTGRE-----------IALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSLPLDEFys 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  937 TPVQIAALLKKFLREMPDPLLTFKLHNLFVISQKIPDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSSFSHVDedt 1016
Cdd:cd04386     73 DPHAVASALKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDEN--- 149
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1959422415 1017 gsKMDIHNLATVITPNILYPNTKNSTVDESFLAIEAVNALI 1057
Cdd:cd04386    150 --KMSPSNIAIVLAPNLLWAKNEGSLAEMAAGTSVHVVAIV 188
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
860-1062 8.53e-20

RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD1-like proteins. Yeast Rgd1 is a GAP protein for Rho3 and Rho4 and plays a role in low-pH response. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239863  Cd Length: 192  Bit Score: 88.61  E-value: 8.53e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  860 FGVSLDFLVEKEGtesthgvgpgaLRVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYDQVDLTK---- 935
Cdd:cd04398      1 FGVPLEDLILREG-----------DNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLLISpedy 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  936 ETPVQ-IAALLKKFLREMPDPLLTFKLHNLFVISQKIPDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSSFSHVDe 1014
Cdd:cd04398     70 ESDIHsVASLLKLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVN- 148
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1959422415 1015 dtgsKMDIHNLATVITPNILYPNTKNSTvDESFlAIEAVNALITYNDT 1062
Cdd:cd04398    149 ----RMSVNNLAIIWGPTLMNAAPDNAA-DMSF-QSRVIETLLDNAYQ 190
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
860-1043 2.55e-19

RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP27 (also called CAMGAP1), ARHGAP15, 12 and 9-like proteins; This subgroup of ARHGAPs are multidomain proteins that contain RhoGAP, PH, SH3 and WW domains. Most members that are studied show GAP activity towards Rac1, some additionally show activity towards Cdc42. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239868 [Multi-domain]  Cd Length: 187  Bit Score: 87.06  E-value: 2.55e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  860 FGVSLDFLVEKEGTesthgvgpgalRVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMID-NKYDQVDLTKETP 938
Cdd:cd04403      1 FGCHLEALCQRENS-----------TVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDhDEKLDLDDSKWED 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  939 VQ-IAALLKKFLREMPDPLLTFKLHNLFVISQKIPDPEkqKRLLHLTCCL--LPKAHRDTMEVLFAFLNwtSSFSHVDED 1015
Cdd:cd04403     70 IHvITGALKLFFRELPEPLFPYSLFNDFVAAIKLSDYE--QRVSAVKDLIksLPKPNHDTLKMLFRHLC--RVIEHGEKN 145
                          170       180
                   ....*....|....*....|....*...
gi 1959422415 1016 tgsKMDIHNLATVITPNILYPNTKNSTV 1043
Cdd:cd04403    146 ---RMTTQNLAIVFGPTLLRPEQETGNI 170
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
885-1063 7.93e-19

RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP21-like proteins. ArhGAP21 is a multi-domain protein, containing RhoGAP, PH and PDZ domains, and is believed to play a role in the organization of the cell-cell junction complex. It has been shown to function as a GAP of Cdc42 and RhoA, and to interact with alpha-catenin and Arf6. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239860  Cd Length: 196  Bit Score: 85.91  E-value: 7.93e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  885 RVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYDQVDLT----KETPVqIAALLKKFLREMPDPLLTFK 960
Cdd:cd04395     17 YVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGFDIDLQdprwRDVNV-VSSLLKSFFRKLPEPLFTNE 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  961 LHNLFVISQKIPDPEKQ----KRLLHltccLLPKAHRDTMEVLFAFLNWTSSFSHVDedtgsKMDIHNLATVITPNILYP 1036
Cdd:cd04395     96 LYPDFIEANRIEDPVERlkelRRLIH----SLPDHHYETLKHLIRHLKTVADNSEVN-----KMEPRNLAIVFGPTLVRT 166
                          170       180
                   ....*....|....*....|....*....
gi 1959422415 1037 NTKNST--VDESFLAIEAVNALITYNDTM 1063
Cdd:cd04395    167 SDDNMEtmVTHMPDQCKIVETLIQHYDWF 195
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
896-1059 1.14e-18

RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP19-like proteins. The function of ArhGAP19 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239857  Cd Length: 208  Bit Score: 85.98  E-value: 1.14e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  896 AMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYD-QVDLTKETPVQIAALLKKFLREMPDPLLT-------FKLHNLFVI 967
Cdd:cd04392     18 EYLEKNLRVEGLFRKPGNSARQQELRDLLNSGTDlDLESGGFHAHDCATVLKGFLGELPEPLLThahypahLQIADLCQF 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  968 SQK-----IPDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSSFshvdEDTgSKMDIHNLATVITPNILYPntKNST 1042
Cdd:cd04392     98 DEKgnktsAPDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKH----EDK-NKMSADNLALLFTPHLICP--RNLT 170
                          170
                   ....*....|....*..
gi 1959422415 1043 VDESFLAIEAVNALITY 1059
Cdd:cd04392    171 PEDLHENAQKLNSIVTF 187
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
859-1040 2.17e-18

RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of DLC1-like proteins. DLC1 shows in vitro GAP activity towards RhoA and CDC42. Beside its C-terminal GAP domain, DLC1 also contains a SAM (sterile alpha motif) and a START (StAR-related lipid transfer action) domain. DLC1 has tumor suppressor activity in cell culture. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239840  Cd Length: 220  Bit Score: 85.16  E-value: 2.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  859 VFGVSLDFLVEKEGTEsthgvgpgalrVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYDQVDLTKETP 938
Cdd:cd04375      4 VFGVPLLVNLQRTGQP-----------LPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQA 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  939 VQIAALLKKFLREMPDPLLTFKLHNLFV-ISQKIPdPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSSFSHVDEDTG 1017
Cdd:cd04375     73 YDVADMLKQYFRDLPEPLLTNKLSETFIaIFQYVP-KEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTA 151
                          170       180
                   ....*....|....*....|...
gi 1959422415 1018 SkmdihNLATVITPNILYPNTKN 1040
Cdd:cd04375    152 T-----NLAVCLAPSLFHLNTSR 169
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
886-1038 5.91e-18

RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP20-like proteins. ArhGAP20, also known as KIAA1391 and RA-RhoGAP, contains a RhoGAP, a RA, and a PH domain, and ANXL repeats. ArhGAP20 is activated by Rap1 and induces inactivation of Rho, which in turn leads to neurite outgrowth. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239867  Cd Length: 192  Bit Score: 83.12  E-value: 5.91e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  886 VPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKyDQVDLTKETPVQIAALLKKFLREMPDPLLTFKLHNLF 965
Cdd:cd04402     15 LPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSG-VEVDLKAEPVLLLASVLKDFLRNIPGSLLSSDLYEEW 93
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1959422415  966 --VISQKiPDPEKQ---KRLLHltccLLPKAHRDTMEVLFAFLNWTSSFSHVdedtgSKMDIHNLATVITPNILYPNT 1038
Cdd:cd04402     94 msALDQE-NEEEKIaelQRLLD----KLPRPNVLLLKHLICVLHNISQNSET-----NKMDAFNLAVCIAPSLLWPPA 161
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
859-1035 7.35e-18

RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of FAM13A1, isoform a-like proteins. The function of FAM13A1a is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by up several orders of magnitude.


Pssm-ID: 239858 [Multi-domain]  Cd Length: 189  Bit Score: 82.90  E-value: 7.35e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  859 VFGVSLDFLvEKEGtESTHGVgpgalrvPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYDqVDLTKETP 938
Cdd:cd04393      2 VFGVPLQEL-QQAG-QPENGV-------PAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEE-VDLSKEAD 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  939 V-QIAALLKKFLREMPDPLLTFKLHNLFV-ISQKIPDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSSFSHVDedt 1016
Cdd:cd04393     72 VcSAASLLRLFLQELPEGLIPASLQIRLMqLYQDYNGEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHEN--- 148
                          170
                   ....*....|....*....
gi 1959422415 1017 gsKMDIHNLATVITPNILY 1035
Cdd:cd04393    149 --RMTAENLAAVFGPDVFH 165
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
883-1033 8.02e-18

RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in MgcRacGAP proteins. MgcRacGAP plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling. ii) after phosphorylation by aurora B MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain a N-terminal C1-like domain, and a C-terminal RhoGAP domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239847  Cd Length: 193  Bit Score: 82.73  E-value: 8.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  883 ALRVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYDQVDLTK-ETPVqIAALLKKFLREMPDPLLTFKL 961
Cdd:cd04382     14 SPMIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKvDIHV-ICGCLKDFLRSLKEPLITFAL 92
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1959422415  962 HNLFVISQKIPDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSSFSHVdedtgsKMDIHNLATVITPNI 1033
Cdd:cd04382     93 WKEFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQSPEC------KMDINNLARVFGPTI 158
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
860-1063 1.56e-17

RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of chimaerins. Chimaerins are a family of phorbolester- and diacylglycerol-responsive GAPs specific for the Rho-like GTPase Rac. Chimaerins exist in two alternative splice forms that each contain a C-terminal GAP domain, and a central C1 domain which binds phorbol esters, inducing a conformational change that activates the protein; one splice form is lacking the N-terminal Src homology-2 (SH2) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239837 [Multi-domain]  Cd Length: 194  Bit Score: 82.18  E-value: 1.56e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  860 FGVSLDFLVEKEGTesthgvgpgalRVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYDQVDLTKETPV 939
Cdd:cd04372      1 YGCDLTTLVKAHNT-----------QRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKADISATVYP 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  940 Q---IAALLKKFLREMPDPLLTFKLHNLFVISQKIPDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSSFSHVDedt 1016
Cdd:cd04372     70 DinvITGALKLYFRDLPIPVITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDN--- 146
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1959422415 1017 gsKMDIHNLATVITPNILYPNTKNS--TVDESFLAIEAVNALITYNDTM 1063
Cdd:cd04372    147 --KMNAENLGIVFGPTLMRPPEDSAltTLNDMRYQILIVQLLITNEDVL 193
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
886-1059 5.32e-16

RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein) and PARG1 (PTPL1-associated RhoGAP1). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239843  Cd Length: 203  Bit Score: 77.85  E-value: 5.32e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  886 VPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYDQVDLTKETPVQIAALLKKFLREMPDPLLTFKLHNLF 965
Cdd:cd04378     16 VPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLRQLPEPLILFRLYNDF 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  966 VI----SQKIPDPEKQ--------------KRLLhltcCLLPKAHRDTMEVLFAFLNWTSsfSHVDEDtgsKMDIHNLAT 1027
Cdd:cd04378     96 IAlakeIQRDTEEDKApntpievnriirklKDLL----RQLPASNYNTLQHLIAHLYRVA--EQFEEN---KMSPNNLGI 166
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1959422415 1028 VITPNILYPNTKNSTVDESFLA-----IEAVNALITY 1059
Cdd:cd04378    167 VFGPTLIRPRPGDADVSLSSLVdygyqARLVEFLITN 203
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
886-1059 6.60e-16

RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in ARAPs. ARAPs (also known as centaurin deltas) contain, besides the RhoGAP domain, an Arf GAP, ankyrin repeat ras-associating, and PH domains. Since their ArfGAP activity is PIP3-dependent, ARAPs are considered integration points for phosphoinositide, Arf and Rho signaling. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239850  Cd Length: 184  Bit Score: 76.96  E-value: 6.60e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  886 VPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYDQVDLT--KETPVQIAALLKKFLREMPDPLLTFKLHN 963
Cdd:cd04385     15 IPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARSVQLRegEYTVHDVADVLKRFLRDLPDPLLTSELHA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  964 LFVISQKIPD-PEKQKRLLHLTCClLPKAHRDTMEVLFAFLNWTSSFShvDEDtgsKMDIHNLATVITPNILYPNTKNST 1042
Cdd:cd04385     95 EWIEAAELENkDERIARYKELIRR-LPPINRATLKVLIGHLYRVQKHS--DEN---QMSVHNLALVFGPTLFQTDEHSVG 168
                          170
                   ....*....|....*..
gi 1959422415 1043 VDESflAIEAVNALITY 1059
Cdd:cd04385    169 QTSH--EVKVIEDLIDN 183
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
860-1034 1.65e-15

RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXB. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239872 [Multi-domain]  Cd Length: 186  Bit Score: 76.18  E-value: 1.65e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  860 FGVSLDFLVEKEGTesthgvgpgalrVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYDQVDLtKETPV 939
Cdd:cd04407      1 FGVRVGSLTSNKTS------------VPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKL-ENYPI 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  940 Q-IAALLKKFLREMPDPLLTFKLHNLFVISQKIpdPEKQKRLLHLTCCL--LPKAHRDTMEVLFAFLNWTSSFSHVDedt 1016
Cdd:cd04407     68 HaITGLLKQWLRELPEPLMTFAQYNDFLRAVEL--PEKQEQLQAIYRVLeqLPTANHNTLERLIFHLVKVALEEDVN--- 142
                          170
                   ....*....|....*...
gi 1959422415 1017 gsKMDIHNLATVITPNIL 1034
Cdd:cd04407    143 --RMSPNALAIVFAPCLL 158
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
882-1040 1.73e-15

RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP22, 24 and 25-like proteins; longer isoforms of these proteins contain an additional N-terminal pleckstrin homology (PH) domain. ARHGAP25 (KIA0053) has been identified as a GAP for Rac1 and Cdc42. Short isoforms (without the PH domain) of ARHGAP24, called RC-GAP72 and p73RhoGAP, and of ARHGAP22, called p68RacGAP, has been shown to be involved in angiogenesis and endothelial cell capillary formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239855 [Multi-domain]  Cd Length: 199  Bit Score: 76.33  E-value: 1.73e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  882 GALRVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKyDQVDLTKETPVQ-IAALLKKFLREMPDPLLTFK 960
Cdd:cd04390     18 GPRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAG-ERPSFDSDTDVHtVASLLKLYLRELPEPVIPWA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  961 LHNLFVISQKIPDPEKQKRLLHLT--CCLLPKAHRDTMEVLFAFLNWTSSFSHVDedtgsKMDIHNLATVITPNILYPNT 1038
Cdd:cd04390     97 QYEDFLSCAQLLSKDEEKGLGELMkqVSILPKVNYNLLSYICRFLDEVQSNSSVN-----KMSVQNLATVFGPNILRPKV 171

                   ..
gi 1959422415 1039 KN 1040
Cdd:cd04390    172 ED 173
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
860-1033 3.24e-15

RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in RalBP1 proteins, also known as RLIP, RLIP76 or cytocentrin. RalBP1 plays an important role in endocytosis during interphase. During mitosis, RalBP1 transiently associates with the centromere and has been shown to play an essential role in the proper assembly of the mitotic apparatus. RalBP1 is an effector of the Ral GTPase which itself is an effector of Ras. RalBP1 contains a RhoGAP domain, which shows weak activity towards Rac1 and Cdc42, but not towards Ral, and a Ral effector domain binding motif. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239846 [Multi-domain]  Cd Length: 182  Bit Score: 75.16  E-value: 3.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  860 FGVSLDFLVEKegTESTHGVgpgalRVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKyDQVDLTKETPV 939
Cdd:cd04381      1 FGASLSLAVER--SRCHDGI-----DLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRR-ESPNLEEYEPP 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  940 QIAALLKKFLREMPDPLLTFKLHNLFVISQKIPD-PEKQKRLLHLTcCLLPKAHRdtmeVLFAFLnwTSSFSHV-DEDTG 1017
Cdd:cd04381     73 TVASLLKQYLRELPEPLLTKELMPRFEEACGRPTeAEREQELQRLL-KELPECNR----LLLAWL--IVHMDHViAQELE 145
                          170
                   ....*....|....*.
gi 1959422415 1018 SKMDIHNLATVITPNI 1033
Cdd:cd04381    146 TKMNIQNISIVLSPTV 161
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
190-242 3.08e-14

LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).


Pssm-ID: 259829 [Multi-domain]  Cd Length: 53  Bit Score: 68.11  E-value: 3.08e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1959422415  190 CHECGGALRGSYI-TALDHKYHIEHFTCSVCPTVFGaQDSYYEHEGRVYCHFHY 242
Cdd:cd08368      1 CAGCGKPIEGRELlRALGKKWHPECFKCAECGKPLG-GDSFYEKDGKPYCEKCY 53
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
886-1036 8.35e-14

RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239873  Cd Length: 200  Bit Score: 71.39  E-value: 8.35e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  886 VPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYDQVDLTKETPVQIAALLKKFLREMPDPLLTFKLHNLF 965
Cdd:cd04408     16 VPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLKELPEPVLPFQLYDDF 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  966 V--------ISQKIPD----PEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSS-FshvdEDtgSKMDIHNLATVITPN 1032
Cdd:cd04408     96 IalakelqrDSEKAAEspsiVENIIRSLKELLGRLPVSNYNTLRHLMAHLYRVAErF----ED--NKMSPNNLGIVFGPT 169

                   ....
gi 1959422415 1033 ILYP 1036
Cdd:cd04408    170 LLRP 173
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
860-1040 8.88e-14

RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXA. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239871  Cd Length: 186  Bit Score: 71.19  E-value: 8.88e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  860 FGVSLDFLVEKEGTesthgvgpgalrVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYDQVDLTKETPV 939
Cdd:cd04406      1 FGVELSRLTSEDRS------------VPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIH 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  940 QIAALLKKFLREMPDPLLTFKLHNLFVISQKIPDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSsfshVDEDTgSK 1019
Cdd:cd04406     69 VIASVFKQWLRDLPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIA----LQEET-NR 143
                          170       180
                   ....*....|....*....|..
gi 1959422415 1020 MDIHNLATVITPNILY-PNTKN 1040
Cdd:cd04406    144 MSANALAIVFAPCILRcPDTTD 165
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
190-246 2.14e-13

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 65.82  E-value: 2.14e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1959422415  190 CHECGGALRGSYIT-ALDHKYHIEHFTCSVCPTVFGAQDsYYEHEGRVYCHFHYSTQF 246
Cdd:pfam00412    1 CAGCNRPIYDRELVrALGKVWHPECFRCAVCGKPLTTGD-FYEKDGKLYCKHDYYKLF 57
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
860-1060 2.33e-13

RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in SYD-1_like proteins. Syd-1, first identified and best studied in C.elegans, has been shown to play an important role in neuronal development by specifying axonal properties. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239844  Cd Length: 207  Bit Score: 70.19  E-value: 2.33e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  860 FGVSLDFLVEKEgtesthgvgPGALRVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYDQVDLTKE--- 936
Cdd:cd04379      1 FGVPLSRLVERE---------GESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELSEElyp 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  937 -TPVqIAALLKKFLREMPDPLLTFKLHN--LFVISQKIPDPEKQKR---LLHLTCCllPKAHRDTMEVLFAFLNWTSSFS 1010
Cdd:cd04379     72 dINV-ITGVLKDYLRELPEPLITPQLYEmvLEALAVALPNDVQTNThltLSIIDCL--PLSAKATLLLLLDHLSLVLSNS 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1959422415 1011 HVDedtgsKMDIHNLATVITPNILYPNTKNSTVDESFLAIEAVNALITYN 1060
Cdd:cd04379    149 ERN-----KMTPQNLAVCFGPVLMFCSQEFSRYGISPTSKMAAVSTVDFK 193
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
905-1050 3.05e-13

RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of fungal BEM3-like proteins. Bem3 is a GAP protein of Cdc42, and is specifically involved in the control of the initial assembly of the septin ring in yeast bud formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239865 [Multi-domain]  Cd Length: 190  Bit Score: 69.69  E-value: 3.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  905 EGVFRKNGNIRRLKEISEMIDNKYDqVDLTKET----PVQIAALLKKFLREMPDPLLTFKLHNLFvisQKIPD--PEKQK 978
Cdd:cd04400     42 EGIFRLSGSASVIKQLKERFNTEYD-VDLFSSSlypdVHTVAGLLKLYLRELPTLILGGELHNDF---KRLVEenHDRSQ 117
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1959422415  979 RLLHLTCCL--LPKAHRDTMEVLFAFLNWTSSFSHVDedtgsKMDIHNLATVITPNILYPNTKNSTVDESFLAI 1050
Cdd:cd04400    118 RALELKDLVsqLPQANYDLLYVLFSFLRKIIEHSDVN-----KMNLRNVCIVFSPTLNIPAGIFVLFLTDFDCI 186
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
905-1034 1.07e-12

RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in KIAA1688-like proteins; KIAA1688 is a protein of unknown function that contains a RhoGAP domain and a myosin tail homology 4 (MyTH4) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239854  Cd Length: 187  Bit Score: 67.80  E-value: 1.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  905 EGVFRKNGNIRRLKEISEMIDnKYDQVDLTKETPVQIAALLKKFLREMPDPLLTFKLHNLFVISQKipDPEKQKRLLHLt 984
Cdd:cd04389     41 EGIFRVPGDIDEVNELKLRVD-QWDYPLSGLEDPHVPASLLKLWLRELEEPLIPDALYQQCISASE--DPDKAVEIVQK- 116
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1959422415  985 cclLPKAHRDTMEVLFAFLNWTSSFSHVDEdtgSKMDIHNLATVITPNIL 1034
Cdd:cd04389    117 ---LPIINRLVLCYLINFLQVFAQPENVAH---TKMDVSNLAMVFAPNIL 160
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
126-182 2.11e-12

LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).


Pssm-ID: 259829 [Multi-domain]  Cd Length: 53  Bit Score: 62.72  E-value: 2.11e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1959422415  126 CKKCGEPLTGQFV-RALGATYHLECFKCEDCG-QIVASKFFPVDAEdgsgqyPLCETDY 182
Cdd:cd08368      1 CAGCGKPIEGRELlRALGKKWHPECFKCAECGkPLGGDSFYEKDGK------PYCEKCY 53
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
886-1059 2.56e-12

RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of PARG1 (PTPL1-associated RhoGAP1). PARG1 was originally cloned as an interaction partner of PTPL1, an intracellular protein-tyrosine phosphatase. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239874  Cd Length: 211  Bit Score: 67.53  E-value: 2.56e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  886 VPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKYDQVDLTKETPVQIAALLKKFLREMPDPLLTFKLHNLF 965
Cdd:cd04409     16 IPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLKLYLRQLPEPLILFRLYNEF 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  966 V----ISQKIPDPEKQKRLLH---LTCCL---------------LPKAHRDTMEVLFAFLNWTSsfSHVDEDtgsKMDIH 1023
Cdd:cd04409     96 IglakESQHVNETQEAKKNSDkkwPNMCTelnrillkskdllrqLPAPNYNTLQFLIVHLHRVS--EQAEEN---KMSAS 170
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1959422415 1024 NLATVITPNILYPNTKNSTVDESFLA-----IEAVNALITY 1059
Cdd:cd04409    171 NLGIIFGPTLIRPRPTDATVSLSSLVdyphqARLVELLITY 211
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
904-1036 4.63e-12

RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of CdGAP-like proteins; CdGAP contains an N-terminal RhoGAP domain and a C-terminal proline-rich region, and it is active on both Cdc42 and Rac1 but not RhoA. CdGAP is recruited to focal adhesions via the interaction with the scaffold protein actopaxin (alpha-parvin). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239849 [Multi-domain]  Cd Length: 195  Bit Score: 66.37  E-value: 4.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  904 VEGVFRKNG---NIRRLKEisemidnKYD--QV-DLTKETPVQ----IAALLKKFLREMPDPLLTFKLHNLFVISQKIPD 973
Cdd:cd04384     35 VDGIYRLSGiasNIQRLRH-------EFDseQIpDLTKDVYIQdihsVSSLCKLYFRELPNPLLTYQLYEKFSEAVSAAS 107
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1959422415  974 PEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSSFShvdedtgSKMDIH--NLATVITPNILYP 1036
Cdd:cd04384    108 DEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYC-------SITNMHakNLAIVWAPNLLRS 165
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
885-1041 1.48e-11

RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr (breakpoint cluster region protein)-like proteins. Bcr is a multidomain protein with a variety of enzymatic functions. It contains a RhoGAP and a Rho GEF domain, a Ser/Thr kinase domain, an N-terminal oligomerization domain, and a C-terminal PDZ binding domain, in addition to PH and C2 domains. Bcr is a negative regulator of: i) RacGTPase, via the Rho GAP domain, ii) the Ras-Raf-MEK-ERK pathway, via phosphorylation of the Ras binding protein AF-6, and iii) the Wnt signaling pathway through binding beta-catenin. Bcr can form a complex with beta-catenin and Tcf1. The Wnt signaling pathway is involved in cell proliferation, differentiation, and cell renewal. Bcr was discovered as a fusion partner of Abl. The Bcr-Abl fusion is characteristic for a large majority of chronic myelogenous leukemias (CML). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239852 [Multi-domain]  Cd Length: 196  Bit Score: 64.95  E-value: 1.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  885 RVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMID-NKYDQVDLTKETPVQ-IAALLKKFLREMPDPLLTFKLH 962
Cdd:cd04387     15 KVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDtNNKDVSVMLSEMDVNaIAGTLKLYFRELPEPLFTDELY 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  963 NLFVISQKIPDP-EKQKRLLHLTCCLlPKAHRDTMEVLFAFLNWTSSFSHVDedtgsKMDIHNLATVITPNILYPNTKNS 1041
Cdd:cd04387     95 PNFAEGIALSDPvAKESCMLNLLLSL-PDPNLVTFLFLLHHLKRVAEREEVN-----KMSLHNLATVFGPTLLRPSEKES 168
LIM3_Lrg1p_like cd09393
The third LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The third LIM ...
501-558 2.02e-11

The third LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The third LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188779  Cd Length: 56  Bit Score: 60.02  E-value: 2.02e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1959422415  501 CAACKEPIDDECIMLGESRWHLKPphLTCAACQTDLTDTCQEALWSPRIKKVFCNSCA 558
Cdd:cd09393      1 CASCGKSIEDECIKFEDKRWHLKC--FTCSRCHREISSELSDAAFNNKDQRILCSNCS 56
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
886-1065 3.15e-11

RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p190-like proteins. p190, also named RhoGAP5, plays a role in neuritogenesis and axon branch stability. p190 shows a preference for Rho, over Rac and Cdc42, and consists of an N-terminal GTPase domain and a C-terminal GAP domain. The central portion of p190 contains important regulatory phosphorylation sites. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239838  Cd Length: 185  Bit Score: 63.63  E-value: 3.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  886 VPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDnKYDQVDL-TKETPVQIAA-LLKKFLREMPDPLLTFKLHN 963
Cdd:cd04373     15 IPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFD-QDHNLDLvSKDFTVNAVAgALKSFFSELPDPLIPYSMHL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  964 LFVISQKIPDpeKQKRLLHLTCCL--LPKAHRDTMEVLFAFLNWTSSFSHVDedtgsKMDIHNLATVITPNILYPNtkns 1041
Cdd:cd04373     94 ELVEAAKIND--REQRLHALKELLkkFPPENFDVFKYVITHLNKVSQNSKVN-----LMTSENLSICFWPTLMRPD---- 162
                          170       180
                   ....*....|....*....|....
gi 1959422415 1042 tvdesFLAIEAVNALITYNdTMCE 1065
Cdd:cd04373    163 -----FTSMEALSATRIYQ-TIIE 180
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
126-185 5.09e-11

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 58.88  E-value: 5.09e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1959422415  126 CKKCGEPLTGQF-VRALGATYHLECFKCEDCGQIVASK-FFPVDAEdgsgqyPLCETDYFRR 185
Cdd:pfam00412    1 CAGCNRPIYDRElVRALGKVWHPECFRCAVCGKPLTTGdFYEKDGK------LYCKHDYYKL 56
LIM3_Paxillin_like cd09338
The third LIM domain of the paxillin like protein family; The third LIM domain of the paxillin ...
190-242 1.06e-10

The third LIM domain of the paxillin like protein family; The third LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188724 [Multi-domain]  Cd Length: 53  Bit Score: 58.12  E-value: 1.06e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFGAQdSYYEHEGRVYCHFHY 242
Cdd:cd09338      1 CGGCNKPILENYISALNTQWHPECFVCRECHKPFING-SFFEHEGLPYCETHY 52
LIM2_Paxillin_like cd09337
The second LIM domain of the paxillin like protein family; The second LIM domain of the ...
190-242 3.19e-10

The second LIM domain of the paxillin like protein family; The second LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188723 [Multi-domain]  Cd Length: 52  Bit Score: 56.63  E-value: 3.19e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFGaQDSYYEHEGRVYCHFHY 242
Cdd:cd09337      1 CAYCNGPILDKCVTALDKTWHPEHFFCAQCGKPFG-DEGFHEKDGKPYCREDY 52
LIM4_PINCH cd09334
The fourth LIM domain of protein PINCH; The fourth LIM domain of protein PINCH: PINCH plays a ...
190-242 2.12e-09

The fourth LIM domain of protein PINCH; The fourth LIM domain of protein PINCH: PINCH plays a pivotal role in the assembly of focal adhesions (FAs), regulating diverse functions in cell adhesion, growth, and differentiation through LIM-mediated protein-protein interactions. PINCH comprises an array of five LIM domains that interact with integrin-linked kinase (ILK), Nck2 (also called Nckbeta or Grb4) and other interaction partners. These interactions are essential for triggering the FA assembly and for relaying diverse mechanical and biochemical signals between Cell-extracellular matrix and the actin cytoskeleton. The PINCH LIM4 domain recognizes the third SH3 domain of another adaptor protein, Nck2. This step is an important component of integrin signaling event. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assem bly of multimeric protein complexes.


Pssm-ID: 188720 [Multi-domain]  Cd Length: 54  Bit Score: 54.28  E-value: 2.12e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFgAQDSYYEHEGRVYCHFHY 242
Cdd:cd09334      3 CGACRRPIEGRVVTALGKHWHVEHFVCAKCEKPF-LGHRHYEKKGLAYCETHY 54
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
871-1036 3.33e-09

RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase regulator associated with focal adhesion kinase); Graf is a multi-domain protein, containing SH3 and PH domains, that binds focal adhesion kinase and influences cytoskeletal changes mediated by Rho proteins. Graf exhibits GAP activity toward RhoA and Cdc42, but only weakly activates Rac1. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239839  Cd Length: 203  Bit Score: 58.17  E-value: 3.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  871 EGTESTH---GVGPGALRVPALVDDA--------VSAMRQMDMSVEGVFRKNG-NIRRLKEISEMIDNK--------YDQ 930
Cdd:cd04374      2 DGKEPVYhspGRLQSEVEGEAQLDDIgfkfvrkcIEAVETRGINEQGLYRVVGvNSKVQKLLSLGLDPKtstpgdvdLDN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  931 VDLTKETpvqIAALLKKFLREMPDPLLTFKLHNLFVISQKIPDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLnwTSSFS 1010
Cdd:cd04374     82 SEWEIKT---ITSALKTYLRNLPEPLMTYELHNDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHL--TNVSD 156
                          170       180
                   ....*....|....*....|....*.
gi 1959422415 1011 HVDEDtgsKMDIHNLATVITPNILYP 1036
Cdd:cd04374    157 HSKKN---LMTVSNLGVVFGPTLLRP 179
LIM1_Paxillin_like cd09336
The first LIM domain of the paxillin like protein family; The first LIM domain of the paxillin ...
190-242 5.28e-09

The first LIM domain of the paxillin like protein family; The first LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 259830 [Multi-domain]  Cd Length: 53  Bit Score: 53.16  E-value: 5.28e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFGAQdSYYEHEGRVYCHFHY 242
Cdd:cd09336      1 CAACNKPIVGQVVTALGKTWHPEHFVCVHCQTELGTS-NFFERDGKPYCEKDY 52
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
125-181 5.65e-09

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 53.16  E-value: 5.65e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1959422415   125 ICKKCGEPLTG--QFVRALGATYHLECFKCEDCGQIVASKFFpvDAEDGSgqyPLCETD 181
Cdd:smart00132    1 KCAGCGKPIYGteRVLRALGKVWHPECFKCATCGKPLSGDTF--FEKDGK---LYCKDC 54
LIM1_Paxillin_like cd09336
The first LIM domain of the paxillin like protein family; The first LIM domain of the paxillin ...
126-183 1.27e-08

The first LIM domain of the paxillin like protein family; The first LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 259830 [Multi-domain]  Cd Length: 53  Bit Score: 52.01  E-value: 1.27e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGQIVASK-FFPVDAEdgsgqyPLCETDYF 183
Cdd:cd09336      1 CAACNKPIVGQVVTALGKTWHPEHFVCVHCQTELGTSnFFERDGK------PYCEKDYH 53
LIM3_Paxillin_like cd09338
The third LIM domain of the paxillin like protein family; The third LIM domain of the paxillin ...
126-182 1.38e-08

The third LIM domain of the paxillin like protein family; The third LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188724 [Multi-domain]  Cd Length: 53  Bit Score: 51.95  E-value: 1.38e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGQ-IVASKFFPVDaedgsGQyPLCETDY 182
Cdd:cd09338      1 CGGCNKPILENYISALNTQWHPECFVCRECHKpFINGSFFEHE-----GL-PYCETHY 52
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
190-238 1.46e-08

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 52.00  E-value: 1.46e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1959422415   190 CHECGGALRGS--YITALDHKYHIEHFTCSVCPTVFGaQDSYYEHEGRVYC 238
Cdd:smart00132    2 CAGCGKPIYGTerVLRALGKVWHPECFKCATCGKPLS-GDTFFEKDGKLYC 51
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
886-1034 2.35e-08

RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in srGAPs. srGAPs are components of the intracellular part of Slit-Robo signalling pathway that is important for axon guidance and cell migration. srGAPs contain an N-terminal FCH domain, a central RhoGAP domain and a C-terminal SH3 domain; this SH3 domain interacts with the intracellular proline-rich-tail of the Roundabout receptor (Robo). This interaction with Robo then activates the rhoGAP domain which in turn inhibits Cdc42 activity. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239848  Cd Length: 188  Bit Score: 55.12  E-value: 2.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  886 VPALVDDAVSAMRQMDMSVEGVFRKNGN---IRRLKEISEMIDN--KYDQVDLTKETpvqIAALLKKFLREMPDPLLTFK 960
Cdd:cd04383     18 IPLVVESCIRFINLYGLQHQGIFRVSGSqveVNDIKNAFERGEDplADDQNDHDINS---VAGVLKLYFRGLENPLFPKE 94
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1959422415  961 LHNLFVISQKIPDPEKQKRLLHLTCCLLPKAHRDTMEVLFAFLNWTSSFShvDEDTgskMDIHNLATVITPNIL 1034
Cdd:cd04383     95 RFEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFS--DENM---MDPYNLAICFGPTLM 163
LIM1_Enigma_like cd09361
The first LIM domain of Enigma-like family; The first LIM domain of Enigma-like family: The ...
190-242 3.21e-08

The first LIM domain of Enigma-like family; The first LIM domain of Enigma-like family: The Enigma LIM domain family is comprised of three members: Enigma, ENH, and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. Enigma was initially characterized in humans and is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. The second member, ENH protein, was first identified in rat brain. It has been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188747 [Multi-domain]  Cd Length: 52  Bit Score: 50.82  E-value: 3.21e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFgAQDSYYEHEGRVYCHFHY 242
Cdd:cd09361      1 CAHCNQVIRGPFLVALGRSWHPEEFTCSHCHCSL-AEIGFVEEKGSLYCELCY 52
LIM2_Paxillin cd09407
The second LIM domain of paxillin; The second LIM domain of paxillin: Paxillin is an adaptor ...
190-242 4.73e-08

The second LIM domain of paxillin; The second LIM domain of paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188791 [Multi-domain]  Cd Length: 52  Bit Score: 50.34  E-value: 4.73e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFGAQdSYYEHEGRVYCHFHY 242
Cdd:cd09407      1 CYYCNGPILDKVVTALDRTWHPEHFFCAQCGAFFGPE-GFHEKDGKAYCRKDY 52
LIM2_Leupaxin cd09408
The second LIM domain of Leupaxin; The second LIM domain of Leupaxin: Leupaxin is a ...
190-239 1.03e-07

The second LIM domain of Leupaxin; The second LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188792 [Multi-domain]  Cd Length: 52  Bit Score: 49.43  E-value: 1.03e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFGAqDSYYEHEGRVYCH 239
Cdd:cd09408      1 CAYCAGPILQNVLTAMDQTWHPEHFFCSHCGELFGD-EGFLERDGKPYCR 49
LIM1_Enigma cd09452
The first LIM domain of Enigma; The first LIM domain of Enigma: Enigma was initially ...
190-238 1.06e-07

The first LIM domain of Enigma; The first LIM domain of Enigma: Enigma was initially characterized in humans as a protein containing three LIM domains at the C-terminus and a PDZ domain at N-terminus. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes such as mitogenic activity, insulin related actin organization, and glucose metabolism. Enigma is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188836 [Multi-domain]  Cd Length: 52  Bit Score: 49.41  E-value: 1.06e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFgAQDSYYEHEGRVYC 238
Cdd:cd09452      1 CAQCNKIIRGRYLVALGRSYHPEEFTCSQCKKVL-DEGGFFEEKGSIFC 48
LIM4_Paxillin_like cd09339
The fourth LIM domain of the Paxillin-like protein family; The fourth LIM domain of the ...
190-239 1.07e-07

The fourth LIM domain of the Paxillin-like protein family; The fourth LIM domain of the Paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188725 [Multi-domain]  Cd Length: 52  Bit Score: 49.64  E-value: 1.07e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFgAQDSYYEHEGRVYCH 239
Cdd:cd09339      1 CAGCGKPITGRCITAMGRKFHPEHFVCAFCLKQL-SKGTFKEQDDKPYCH 49
LIM2_Enigma cd09456
The second LIM domain of Enigma; The second LIM domain of Enigma: Enigma was initially ...
126-182 1.16e-07

The second LIM domain of Enigma; The second LIM domain of Enigma: Enigma was initially characterized in humans as a protein containing three LIM domains at the C-terminus and a PDZ domain at N-terminus. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. Enigma is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188840 [Multi-domain]  Cd Length: 52  Bit Score: 49.61  E-value: 1.16e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGQIVASKFFPVdaEDGSgqyPLCETDY 182
Cdd:cd09456      1 CAKCKKKITGEIMHALKMTWHVHCFTCAACKTPIRNRAFYM--EEGA---PYCERDY 52
LIM1_Paxillin cd09405
The first LIM domain of paxillin; The first LIM domain of paxillin: Paxillin is an adaptor ...
125-182 1.44e-07

The first LIM domain of paxillin; The first LIM domain of paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight cons erved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188789 [Multi-domain]  Cd Length: 54  Bit Score: 49.24  E-value: 1.44e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1959422415  125 ICKKCGEPLTGQFVRALGATYHLECFKCEDCGQIVASK-FFPVDAEdgsgqyPLCETDY 182
Cdd:cd09405      1 VCGACKKPIAGQVVTAMGKTWHPEHFVCTHCQEEIGSRnFFERDGQ------PYCEKDY 53
LIM2_FBLP-1 cd09372
The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1); The second LIM domain of ...
126-167 1.82e-07

The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1); The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1): Fblp-1 contains a proline-rich domain near its N terminus and two LIM domains at its C terminus. FBLP-1 mRNA was detected in a variety of tissues and cells including platelets and endothelial cells. FBLP-1 binds to Filamins. The association between filamin B and FBLP-1 may play an unknown role in cytoskeletal function, cell adhesion, and cell motility. As in other LIM domains, this domain family is 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188758 [Multi-domain]  Cd Length: 53  Bit Score: 48.96  E-value: 1.82e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGQIVASKFFPVD 167
Cdd:cd09372      1 CAKCQGVITEHIIRALGKGYHPPCFTCVTCGRRIGDESFAVD 42
LIM4_Leupaxin cd09412
The fourth LIM domain of Leupaxin; The fourth LIM domain of Leupaxin: Leupaxin is a ...
190-239 2.00e-07

The fourth LIM domain of Leupaxin; The fourth LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188796 [Multi-domain]  Cd Length: 52  Bit Score: 48.58  E-value: 2.00e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFgAQDSYYEHEGRVYCH 239
Cdd:cd09412      1 CGSCGLPITGRCISALGRKFHPEHFVCAFCLRPL-TQGSFKEQSGKPYCS 49
LIM3_Paxillin cd09409
The third LIM domain of paxillin; The third LIM domain of paxillin: Paxillin is an adaptor ...
190-242 2.31e-07

The third LIM domain of paxillin; The third LIM domain of paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188793 [Multi-domain]  Cd Length: 53  Bit Score: 48.68  E-value: 2.31e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFgAQDSYYEHEGRVYCHFHY 242
Cdd:cd09409      1 CGGCARAILENYISALNTLWHPECFVCRECFTPF-VNGSFFEHDGQPYCEAHY 52
LIM2_ENH cd09457
The second LIM domain of the Enigma Homolog (ENH) family; The second LIM domain of the Enigma ...
126-182 2.55e-07

The second LIM domain of the Enigma Homolog (ENH) family; The second LIM domain of the Enigma Homolog (ENH) family: ENH was initially identified in rat brain. Same as enigma, it contains three LIM domains at the C-terminus and a PDZ domain at N-terminus. ENH is implicated in signal transduction processes involving protein kinases. It has also been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ENH is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188841 [Multi-domain]  Cd Length: 52  Bit Score: 48.49  E-value: 2.55e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGQIVASKFFPVdaEDGSgqyPLCETDY 182
Cdd:cd09457      1 CGRCQRKILGEVINALKQTWHVSCFVCVACHNPIRNNVFHL--EDGE---PYCETDY 52
LIM1_Zyxin cd09349
The first LIM domain of Zyxin; The first LIM domain of Zyxin: Zyxin exhibits three copies of ...
114-182 2.61e-07

The first LIM domain of Zyxin; The first LIM domain of Zyxin: Zyxin exhibits three copies of the LIM domain, an extensive proline-rich domain and a nuclear export signal. Localized at sites of cell substratum adhesion in fibroblasts, Zyxin interacts with alpha-actinin, members of the cysteine-rich protein (CRP) family, proteins that display Src homology 3 (SH3) domains and Ena/VASP family members. Zyxin and its partners have been implicated in the spatial control of actin filament assembly as well as in pathways important for cell differentiation. In addition to its functions at focal adhesion plaques, recent work has shown that zyxin moves from the sites of cell contacts to the nucleus, where it directly participates in the regulation of gene expression. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188735 [Multi-domain]  Cd Length: 87  Bit Score: 49.47  E-value: 2.61e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1959422415  114 RPPTKSPGSSRICKKCGEPL--TGQFVRALGATYHLECFKCEDCG-QIVASKFFPVDAEdgsgqyPLCETDY 182
Cdd:cd09349     22 HPPAAEAATNELCGICGQPLsrTQPAVRALGHLFHVTCFTCHQCEqQLQGQQFYSLEGK------PYCEECY 87
LIM3_Zyxin_like cd09357
The third LIM domain of Zyxin-like family; The third LIM domain of Zyxin like family: This ...
126-193 2.99e-07

The third LIM domain of Zyxin-like family; The third LIM domain of Zyxin like family: This family includes Ajuba, Limd1, WTIP, Zyxin, LPP, and Trip6 LIM proteins. Members of Zyxin family contain three tandem C-terminal LIM domains, and a proline-rich N-terminal region. Zyxin proteins are detected primarily in focal adhesion plaques. They function as scaffolds, participating in the assembly of multiple interactions and signal transduction networks, which regulate cell adhesion, spreading, and motility. They can also shuffle into nucleus. In nucleus, zyxin proteins affect gene transcription by interaction with a variety of nuclear proteins, including several transcription factors, playing regulating roles in cell proliferation, differentiation and apoptosis. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188743  Cd Length: 63  Bit Score: 48.57  E-value: 2.99e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1959422415  126 CKKCGEPLT---GQ--FVR--ALGATYHLECFKCEDCGQIVASKffpvdaEDGSGQYPlcetdyfrrLD--LLCHEC 193
Cdd:cd09357      1 CSVCGEPIMpepGQdeTVRivALDRSFHVNCYKCEDCGMLLSSE------DEGQGCYP---------LDghLLCKSC 62
LIM_ALP_like cd09360
The LIM domain of ALP (actinin-associated LIM protein) family; This family represents the LIM ...
126-156 3.16e-07

The LIM domain of ALP (actinin-associated LIM protein) family; This family represents the LIM domain of ALP (actinin-associated LIM protein) family. Four proteins: ALP, CLP36, RIL, and Mystique have been classified into the ALP subfamily of LIM domain proteins. Each member of the subfamily contains an N-terminal PDZ domain and a C-terminal LIM domain. Functionally, these proteins bind to alpha-actinin through their PDZ domains and bind or other signaling molecules through their LIM domains. ALP proteins have been implicated in cardiac and skeletal muscle structure, function and disease, platelet, and epithelial cell motility. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188746 [Multi-domain]  Cd Length: 52  Bit Score: 48.14  E-value: 3.16e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCG 156
Cdd:cd09360      1 CDKCGNGIVGVVVKARDKNRHPECFVCADCG 31
LIM2_Enigma_like cd09362
The second LIM domain of Enigma-like family; The second LIM domain of Enigma-like family: The ...
126-182 3.27e-07

The second LIM domain of Enigma-like family; The second LIM domain of Enigma-like family: The Enigma LIM domain family is comprised of three members: Enigma, ENH, and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. Enigma was initially characterized in humans and is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. The second member, ENH protein, was first identified in rat brain. It has been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188748 [Multi-domain]  Cd Length: 52  Bit Score: 48.24  E-value: 3.27e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGQIVASKFFPVdaEDGSgqyPLCETDY 182
Cdd:cd09362      1 CARCHKKILGEVMHALKQTWHVSCFVCAACKQPIGNSLFHM--EDGE---PYCEKDY 52
LIM1_Leupaxin cd09406
The first LIM domain of Leupaxin; The first LIM domain of Leupaxin: Leupaxin is a cytoskeleton ...
126-182 3.36e-07

The first LIM domain of Leupaxin; The first LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188790 [Multi-domain]  Cd Length: 55  Bit Score: 48.33  E-value: 3.36e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGQIVASK-FFpvdaEDGSGQYplCETDY 182
Cdd:cd09406      3 CASCQKPIAGQVVTALGQTWHPEHFVCCQCGKELGSRpFF----ERNGQAY--CEEDY 54
LIM1_LIMK2 cd09463
The first LIM domain of LIMK2 (LIM domain Kinase 2); The first LIM domain of LIMK2 (LIM domain ...
190-242 6.92e-07

The first LIM domain of LIMK2 (LIM domain Kinase 2); The first LIM domain of LIMK2 (LIM domain Kinase 2): LIMK2 is a member of the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, altering the rate of actin depolymerization. LIMK activity is activated by phosphorylation of a threonine residue within the activation loop of the kinase by p21-activated kinases 1 and 4 and by Rho kinase. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK2 is expressed in all tissues. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The activity of LIM kinase 2 to regulate cofilin phosphorylation is inhibited by the direct binding of Par-3. LIMK2 activation promotes cell cycle progression. The phenotype of Limk2 knockout mice shows a defect in spermatogenesis. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188847 [Multi-domain]  Cd Length: 53  Bit Score: 47.17  E-value: 6.92e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1959422415  190 CHECGGALRGSY-ITALDHKYHIEHFTCSVCptvfgaQDS----YYEHEGRVYCHFHY 242
Cdd:cd09463      1 CTGCGGRIQDSFhYRVVQEAWHNSCFQCSVC------QDLltnwYYEKDGKLYCHKHY 52
LIM1_LIMK cd09364
The first LIM domain of LIMK (LIM domain Kinase ); The first LIM domain of LIMK (LIM domain ...
190-242 7.43e-07

The first LIM domain of LIMK (LIM domain Kinase ); The first LIM domain of LIMK (LIM domain Kinase ): LIMK protein family is comprised of two members LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerisation. LIMKs can function in both cytoplasm and nucleus and are expressed in all tissues. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. However, LIMK1 and LIMk2 have different cellular locations. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The LIM domains of LIMK have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188750 [Multi-domain]  Cd Length: 53  Bit Score: 47.10  E-value: 7.43e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1959422415  190 CHECGGALR-GSYITALDHKYHIEHFTCSVCPTVFGAQdsYYEHEGRVYCHFHY 242
Cdd:cd09364      1 CAGCRGKILdSQYVQALNQDWHCDCFRCSVCSDSLSNW--YFEKDGKLYCRKDY 52
LIM1_Leupaxin cd09406
The first LIM domain of Leupaxin; The first LIM domain of Leupaxin: Leupaxin is a cytoskeleton ...
190-242 8.28e-07

The first LIM domain of Leupaxin; The first LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188790 [Multi-domain]  Cd Length: 55  Bit Score: 47.17  E-value: 8.28e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFGAQdSYYEHEGRVYCHFHY 242
Cdd:cd09406      3 CASCQKPIAGQVVTALGQTWHPEHFVCCQCGKELGSR-PFFERNGQAYCEEDY 54
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
859-1061 1.12e-06

RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal SAC7 and BAG7-like proteins. Both proteins are GTPase activating proteins of Rho1, but differ functionally in vivo: SAC7, but not BAG7, is involved in the control of Rho1-mediated activation of the PKC-MPK1 pathway. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239861  Cd Length: 225  Bit Score: 50.87  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  859 VFGVSLD----------FLVEKEGTESTHGvgpgalRVPALVDDAVSAMRQMDMSVEGVFRKNGNIRRLKEISEMIDNKY 928
Cdd:cd04396      1 VFGVSLEeslkyasvaiSIVDEDGEQYVYG------YIPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPP 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  929 D---QVDLTKETPVQIAALLKKFLREMPDPLLTFKLHNLF----VISQKIPDPEKQKRLLHLT-------------CCLL 988
Cdd:cd04396     75 DygkSFDWDGYTVHDAASVLRRYLNNLPEPLVPLDLYEEFrnplRKRPRILQYMKGRINEPLNtdidqaikeyrdlITRL 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1959422415  989 PKAHRDTMEVLFAFLNWTSSFSHVDEDTGSkmdihNLATVITPNILYPNTKNSTVDESFLAIEAVNALITYND 1061
Cdd:cd04396    155 PNLNRQLLLYLLDLLAVFARNSDKNLMTAS-----NLAAIFQPGILSHPDHEMDPKEYKLSRLVVEFLIEHQD 222
LIM3_abLIM cd09329
The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin ...
126-182 1.17e-06

The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188715 [Multi-domain]  Cd Length: 52  Bit Score: 46.54  E-value: 1.17e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1959422415  126 CKKCGEPLT-GQFVRALGATYHLECFKCEDCGQIVASKFFPVDAEdgsgqyPLCETDY 182
Cdd:cd09329      1 CAGCGQEIKnGQALLALDKQWHVWCFKCKECGKVLTGEYMGKDGK------PYCERDY 52
LIM2_Lhx2_Lhx9 cd09377
The second LIM domain of Lhx2 and Lhx9 family; The second LIM domain of Lhx2 and Lhx9 family: ...
190-242 1.19e-06

The second LIM domain of Lhx2 and Lhx9 family; The second LIM domain of Lhx2 and Lhx9 family: Lhx2 and Lhx9 are highly homologous LHX regulatory proteins. They belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Although Lhx2 and Lhx9 are highly homologous, they seems to play regulatory roles in different organs. In animals, Lhx2 plays important roles in eye, cerebral cortex, limb, the olfactory organs, and erythrocyte development. Lhx2 gene knockout mice exhibit impaired patterning of the cortical hem and the telencephalon of the developing brain, and a lack of development in olfactory structures. Lhx9 is expressed in several regions of the developing mouse brain, the spinal cord, the pancreas, in limb mesenchyme, and in the urogenital region. Lhx9 plays critical roles in gonad development. Homozygous mice lacking functional Lhx9 alleles exhibit numerous urogenital defects, such as gonadal agenesis, infertility, and undetectable levels of testosterone and estradiol coupled with high FSH levels. Lhx9 null mice are phenotypically female, even those that are genotypically male. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188763  Cd Length: 59  Bit Score: 46.88  E-value: 1.19e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1959422415  190 CHECGGALRGSYIT--ALDHKYHIEHFTCSVCPTVFGAQDSYYEHEGRVYCHFHY 242
Cdd:cd09377      5 CARCHLGISASELVmrARDLVFHLNCFTCATCNKPLTKGDHFGMRDGLVYCRLHY 59
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
501-557 2.65e-06

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 45.79  E-value: 2.65e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1959422415  501 CAACKEPIDDECIMLG-ESRWHlkPPHLTCAACQTDLTDTCQealwSPRIKKVFCNSC 557
Cdd:pfam00412    1 CAGCNRPIYDRELVRAlGKVWH--PECFRCAVCGKPLTTGDF----YEKDGKLYCKHD 52
LIM2_Zyxin cd09353
The second LIM domain of Zyxin; The second LIM domain of Zyxin: Zyxin exhibits three copies of ...
126-185 4.47e-06

The second LIM domain of Zyxin; The second LIM domain of Zyxin: Zyxin exhibits three copies of the LIM domain, an extensive proline-rich domain and a nuclear export signal. Localized at sites of cellsubstratum adhesion in fibroblasts, Zyxin interacts with alpha-actinin, members of the cysteine-rich protein (CRP) family, proteins that display Src homology 3 (SH3) domains and Ena/VASP family members. Zyxin and its partners have been implicated in the spatial control of actin filament assembly as well as in pathways important for cell differentiation. In addition to its functions at focal adhesion plaques, recent work has shown that zyxin moves from the sites of cell contacts to the nucleus, where it directly participates in the regulation of gene expression. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors o r scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188739 [Multi-domain]  Cd Length: 60  Bit Score: 45.31  E-value: 4.47e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGQIVASKFFPVDaedgSGQYPLCETDYFRR 185
Cdd:cd09353      1 CAVCDQKITDRMLKATGKSYHPQCFTCVVCKCPLEGESFIVD----QANQPHCVNDYHRR 56
LIM2_abLIM cd09328
The second LIM domain on actin binding LIM (abLIM) proteins; The second LIM domain of actin ...
126-157 1.07e-05

The second LIM domain on actin binding LIM (abLIM) proteins; The second LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188714  Cd Length: 56  Bit Score: 43.87  E-value: 1.07e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGQ 157
Cdd:cd09328      4 CDSCQDFVEGEVVSALGKTYHPKCFVCSVCRQ 35
LIM1_ZASP_Cypher cd09454
The first LIM domain of ZASP/Cypher family; The first LIM domain of ZASP/Cypher family: ZASP ...
190-242 1.10e-05

The first LIM domain of ZASP/Cypher family; The first LIM domain of ZASP/Cypher family: ZASP was identified in human heart and skeletal muscle and Cypher is a mice ortholog of ZASP. ZASP/Cyppher contains three LIM domains at the C-terminus and a PDZ domain at N-terminus. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188838 [Multi-domain]  Cd Length: 52  Bit Score: 43.81  E-value: 1.10e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFgAQDSYYEHEGRVYCHFHY 242
Cdd:cd09454      1 CGHCNNIIRGPFLVALGRSWHPEEFTCHYCHTSL-ADVSFVEEQNNVYCENCY 52
LIM2_LIMK cd09365
The second LIM domain of LIMK (LIM domain Kinase ); The second LIM domain of LIMK (LIM domain ...
190-239 1.13e-05

The second LIM domain of LIMK (LIM domain Kinase ); The second LIM domain of LIMK (LIM domain Kinase ): LIMK protein family is comprised of two members LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerization. LIMKs can function in both cytoplasm and nucleus and are expressed in all tissues. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. However, LIMK1 and LIMk2 have different cellular locations. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The LIM domains of LIMK have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188751 [Multi-domain]  Cd Length: 54  Bit Score: 43.89  E-value: 1.13e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFGAQDSYYEHEG-RVYCH 239
Cdd:cd09365      1 CHGCSQIITGPVMVAGDHKFHPECFSCSSCKAFIGDGDSYALVERsKLYCG 51
LIM3_Leupaxin cd09410
The third LIM domain of Leupaxin; The third LIM domain of Leupaxin: Leupaxin is a cytoskeleton ...
190-242 1.21e-05

The third LIM domain of Leupaxin; The third LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188794 [Multi-domain]  Cd Length: 53  Bit Score: 43.66  E-value: 1.21e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFgAQDSYYEHEGRVYCHFHY 242
Cdd:cd09410      1 CSGCGRPVKENYLSAANGVWHPECFVCSDCLKPF-TDGSFFELDGRPLCELHY 52
LIM3_Leupaxin cd09410
The third LIM domain of Leupaxin; The third LIM domain of Leupaxin: Leupaxin is a cytoskeleton ...
126-182 1.36e-05

The third LIM domain of Leupaxin; The third LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188794 [Multi-domain]  Cd Length: 53  Bit Score: 43.66  E-value: 1.36e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDC-GQIVASKFFPVDAEdgsgqyPLCETDY 182
Cdd:cd09410      1 CSGCGRPVKENYLSAANGVWHPECFVCSDClKPFTDGSFFELDGR------PLCELHY 52
LIM_DA1 cd09396
The Lim domain of DA1; The Lim domain of DA1: DA1 contains one copy of LIM domain and a domain ...
126-167 1.63e-05

The Lim domain of DA1; The Lim domain of DA1: DA1 contains one copy of LIM domain and a domain of unknown function. DA1 is predicted as an ubiquitin receptor, which sets final seed and organ size by restricting the period of cell proliferation. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188782 [Multi-domain]  Cd Length: 53  Bit Score: 43.40  E-value: 1.63e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1959422415  126 CKKCGEPLT-GQFVRALGATYHLECFKCEDCGQIVASKFFPVD 167
Cdd:cd09396      1 CAGCKSEIGhGRFLSALGAVWHPECFRCHACRKPIAEHEFSVS 43
LIM3_Ajuba_like cd09438
The third LIM domain of Ajuba-like proteins; The third LIM domain of Ajuba-like proteins: ...
126-193 1.66e-05

The third LIM domain of Ajuba-like proteins; The third LIM domain of Ajuba-like proteins: Ajuba like LIM protein family includes three highly homologous proteins Ajuba, Limd1, and WTIP. Members of the family contain three tandem C-terminal LIM domains and a proline-rich N-terminal region. This family of proteins functions as scaffolds, participating in the assembly of numerous protein complexes. In the cytoplasm, Ajuba binds Grb2 to modulate serum-stimulated ERK activation. Ajuba also recruits the TNF receptor-associated factor 6 (TRAF6) to p62 and activates PKCKappa activity. Ajuba interacts with alpha-catenin and F-actin to contribute to the formation or stabilization of adheren junctions by linking adhesive receptors to the actin cytoskeleton. Although Ajuba is a cytoplasmic protein, it can shuttle into the nucleus. In nucleus, Ajuba functions as a corepressor for the zinc finger-protein Snail. It binds to the SNAG repression domain of Snail through its LIM region. Arginine methyltransferase-5 (Prmt5), a protein in the complex, is recruited to Snai l through an interaction with Ajuba. This ternary complex functions to repress E-cadherin, a Snail target gene. In addition, Ajuba contains functional nuclear-receptor interacting motifs and selectively interacts with retinoic acid receptors (RARs) and rexinoid receptor (RXRs) to negatively regulate retinoic acid signaling. Wtip, the Wt1-interacting protein, was originally identified as an interaction partner of the Wilms tumour protein 1 (WT1). Wtip is involved in kidney and neural crest development. Wtip interacts with the receptor tyrosine kinase Ror2 and inhibits canonical Wnt signaling. LIMD1 was reported to inhibit cell growth and metastases. The inhibition may be mediated through an interaction with the protein barrier-to-autointegration (BAF), a component of SWI/SNF chromatin-remodeling protein; or through the interaction with retinoblastoma protein (pRB), resulting in inhibition of E2F-mediated transcription, and expression of the majority of genes with E2F1- responsive elements. Recently, Limd1 was shown to interact with the p62/sequestosome protein and influence IL-1 and RANKL signaling by facilitating the assembly of a p62/TRAF6/a-PKC multi-protein complex. The Limd1-p62 interaction affects both NF-kappaB and AP-1 activity in epithelial cells and osteoclasts. Moreover, LIMD1 functions as tumor repressor to block lung tumor cell line in vitro and in vivo. Recent studies revealed that LIM proteins Wtip, LIMD1 and Ajuba interact with components of RNA induced silencing complexes (RISC) as well as eIF4E and the mRNA m7GTP cap-protein complex and are required for microRNA-mediated gene silencing. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188822  Cd Length: 62  Bit Score: 43.53  E-value: 1.66e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1959422415  126 CKKCGEPL-----TGQFVR--ALGATYHLECFKCEDCGqivaskfFPVDAEDGSGQYPLceTDYfrrldLLCHEC 193
Cdd:cd09438      1 CAACGQPIlpaegSEETIRvvSMDKDYHVECYHCEDCG-------LQLNDEEGHRCYPL--DGH-----LLCHSC 61
LIM4_Paxillin cd09411
The fourth LIM domain of Paxillin; The fourth LIM domain of Paxillin: Paxillin is an adaptor ...
190-239 1.83e-05

The fourth LIM domain of Paxillin; The fourth LIM domain of Paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188795 [Multi-domain]  Cd Length: 52  Bit Score: 43.01  E-value: 1.83e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFGaQDSYYEHEGRVYCH 239
Cdd:cd09411      1 CSGCQKPITGRCITAMGKKFHPEHFVCAFCLKQLN-KGTFKEQNDKPYCH 49
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
501-558 2.07e-05

LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).


Pssm-ID: 259829 [Multi-domain]  Cd Length: 53  Bit Score: 43.08  E-value: 2.07e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  501 CAACKEPIDDECIML-GESRWHLKppHLTCAACQTDL-TDTCQEalwspRIKKVFCNSCA 558
Cdd:cd08368      1 CAGCGKPIEGRELLRaLGKKWHPE--CFKCAECGKPLgGDSFYE-----KDGKPYCEKCY 53
LIM2_PINCH cd09332
The second LIM domain of protein PINCH; The second LIM domain of protein PINCH: PINCH plays a ...
126-160 2.22e-05

The second LIM domain of protein PINCH; The second LIM domain of protein PINCH: PINCH plays a pivotal role in the assembly of focal adhesions (FAs), regulating diverse functions in cell adhesion, growth, and differentiation through LIM-mediated protein-protein interactions. PINCH comprises an array of five LIM domains that interact with integrin-linked kinase (ILK), Nck2 (also called Nckbeta or Grb4) and other interaction partners. These interactions are essential for triggering the FA assembly and for relaying diverse mechanical and biochemical signals between Cell-extracellular matrix and the actin cytoskeleton. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188718 [Multi-domain]  Cd Length: 52  Bit Score: 43.09  E-value: 2.22e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGQIVA 160
Cdd:cd09332      1 CGKCGEFVIGRVIKAMNNNWHPDCFRCEICNKELA 35
LIM1_ENH cd09453
The first LIM domain of the Enigma Homolog (ENH) family; The first LIM domain of the Enigma ...
190-242 2.40e-05

The first LIM domain of the Enigma Homolog (ENH) family; The first LIM domain of the Enigma Homolog (ENH) family: ENH was initially identified in rat brain. Same as enigma, it contains three LIM domains at the C-terminus and a PDZ domain at N-terminus. ENH is implicated in signal transduction processes involving protein kinases. It has also been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ENH is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188837 [Multi-domain]  Cd Length: 52  Bit Score: 42.70  E-value: 2.40e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFgAQDSYYEHEGRVYCHFHY 242
Cdd:cd09453      1 CATCNQVIRGPFLVALGKSWHPEEFNCAHCKSSM-AYIGFVEEKGALYCEICY 52
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
933-1062 2.73e-05

RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD2-like proteins. Yeast Rgd2 is a GAP protein for Cdc42 and Rho5. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239864  Cd Length: 212  Bit Score: 46.56  E-value: 2.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  933 LTKETPVQIAALLKKFLREMPDPLLTfklHNLFVI---------SQKIPDPEKQKRLLHLTCCLLPKAHRDTMEVL---F 1000
Cdd:cd04399     73 LKKFEPSTVASVLKLYLLELPDSLIP---HDIYDLirslysaypPSQEDSDTARIQGLQSTLSQLPKSHIATLDAIithF 149
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1959422415 1001 AFLNWTSSFSHVDEDtgskmDIHNLATVITPNILYPNTKNSTVDESFLAIEAVNALITYNDT 1062
Cdd:cd04399    150 YRLIEITKMGESEEE-----YADKLATSLSREILRPIIESLLTIGDKHGYKFFRDLLTHKDQ 206
LIM1_abLIM cd09327
The first LIM domain of actin binding LIM (abLIM) proteins; The first LIM domain of actin ...
126-182 3.35e-05

The first LIM domain of actin binding LIM (abLIM) proteins; The first LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188713 [Multi-domain]  Cd Length: 52  Bit Score: 42.24  E-value: 3.35e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCG-QIVASKFFPVDaedgsGQYpLCETDY 182
Cdd:cd09327      1 CYKCGKKCKGEVLRVQDKYFHIKCFTCKVCGcDLAQGGFFVKE-----GEY-YCTDDY 52
LIM2_LPP cd09354
The second LIM domain of lipoma preferred partner (LPP); The second LIM domain of lipoma ...
126-168 3.79e-05

The second LIM domain of lipoma preferred partner (LPP); The second LIM domain of lipoma preferred partner (LPP): LPP is a member of the zyxin LIM protein family and contains three LIM zinc-binding domains at the C-terminal and proline-rich region at the N-terminal. LPP initially identified as the most frequent translocation partner of HMGA2 (High Mobility Group A2) in a subgroup of benign tumors of adipose tissue (lipomas). It was also shown to be rearranged in a number of other soft tissues, as well as in a case of acute monoblastic leukemia. In addition to its involvement in tumors, LPP was inedited as a smooth muscle restricted LIM protein that plays an important role in SMC migration. LPP is localized at sites of cell adhesion, cell-cell contacts and transiently in the nucleus. In nucleus, it acts as a coactivator for the ETS domain transcription factor PEA3. In addition to PEA3, it interacts with alpha-actinin,vasodilator stimulated phosphoprotein (VASP),Palladin, and Scrib. The LIM domains are the main focal adhesion targeting elements and that the proline- rich region, which harbors binding sites for alpha-actinin and vasodilator- stimulated phosphoprotein (VASP), has a weak targeting capacity. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188740 [Multi-domain]  Cd Length: 60  Bit Score: 42.53  E-value: 3.79e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGQIVASKFFPVDA 168
Cdd:cd09354      1 CSVCSKPILDRILRATGKPYHPQCFTCVVCGKSLDGIPFTVDA 43
LIM1_LIMK cd09364
The first LIM domain of LIMK (LIM domain Kinase ); The first LIM domain of LIMK (LIM domain ...
126-183 4.20e-05

The first LIM domain of LIMK (LIM domain Kinase ); The first LIM domain of LIMK (LIM domain Kinase ): LIMK protein family is comprised of two members LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerisation. LIMKs can function in both cytoplasm and nucleus and are expressed in all tissues. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. However, LIMK1 and LIMk2 have different cellular locations. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The LIM domains of LIMK have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188750 [Multi-domain]  Cd Length: 53  Bit Score: 42.09  E-value: 4.20e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1959422415  126 CKKCGEPLT-GQFVRALGATYHLECFKCEDCGQIVASKFFPVDaedgsGQYpLCETDYF 183
Cdd:cd09364      1 CAGCRGKILdSQYVQALNQDWHCDCFRCSVCSDSLSNWYFEKD-----GKL-YCRKDYW 53
LIM3_LPP cd09437
The third LIM domain of lipoma preferred partner (LPP); The third LIM domain of lipoma ...
125-195 4.82e-05

The third LIM domain of lipoma preferred partner (LPP); The third LIM domain of lipoma preferred partner (LPP): LPP is a member of the zyxin LIM protein family and contains three LIM zinc-binding domains at the C-terminal and proline-rich region at the N-terminal. LPP initially identified as the most frequent translocation partner of HMGA2 (High Mobility Group A2) in a subgroup of benign tumors of adipose tissue (lipomas). It was also shown to be rearranged in a number of other soft tissues, as well as in a case of acute monoblastic leukemia. In addition to its involvement in tumors, LPP was inedited as a smooth muscle restricted LIM protein that plays an important role in SMC migration. LPP is localized at sites of cell adhesion, cell-cell contacts and transiently in the nucleus. In nucleus, it acts as a coactivator for the ETS domain transcription factor PEA3. In addition to PEA3, it interacts with alpha-actinin,vasodilator stimulated phosphoprotein (VASP), Palladin, and Scrib. The LIM domains are the main focal adhesion targeting elements and that the proline- rich region, which harbors binding sites for alpha-actinin and vasodilator- stimulated phosphoprotein (VASP), has a weak targeting capacity. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188821  Cd Length: 68  Bit Score: 42.45  E-value: 4.82e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1959422415  125 ICKKCGEPLTGQ----FVRALGATYHLECFKCEDCGQIVASKffpvdaEDGSGQYPLceTDYfrrldLLCHECGG 195
Cdd:cd09437      3 VCKLPIMPEPGQdetvRVVALDRSFHVQCYKCEDCGLLLSSE------AEGRGCYPL--DDH-----VLCKSCNA 64
LIM1_Paxillin_like cd09336
The first LIM domain of the paxillin like protein family; The first LIM domain of the paxillin ...
501-536 5.43e-05

The first LIM domain of the paxillin like protein family; The first LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 259830 [Multi-domain]  Cd Length: 53  Bit Score: 41.99  E-value: 5.43e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1959422415  501 CAACKEPIDDECIM-LGESrWHlkPPHLTCAACQTDL 536
Cdd:cd09336      1 CAACNKPIVGQVVTaLGKT-WH--PEHFVCVHCQTEL 34
LIM1_Lmx1b cd09371
The first LIM domain of Lmx1b; The first LIM domain of Lmx1b: Lmx1b belongs to the LHX protein ...
501-554 6.86e-05

The first LIM domain of Lmx1b; The first LIM domain of Lmx1b: Lmx1b belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. In mouse, Lmx1b functions in the developing limbs and eyes, the kidneys, the brain, and in cranial mesenchyme. The disruption of Lmx1b gene results kidney and limb defects. In the brain, Lmx1b is important for generation of mesencephalic dopamine neurons and the differentiation of serotonergic neurons. In the mouse eye, Lmx1b regulates anterior segment (cornea, iris, ciliary body, trabecular meshwork, and lens) development. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188757 [Multi-domain]  Cd Length: 53  Bit Score: 41.59  E-value: 6.86e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1959422415  501 CAACKEPIDDECIM-LGESRWHLKPphLTCAACQTDLTDTCQEalwspRIKKVFC 554
Cdd:cd09371      1 CAGCQRPISDRYLLrVNERSWHEEC--LQCSVCQQPLTTSCYF-----RDRKLYC 48
LIM1_LIMK1 cd09462
The first LIM domain of LIMK1 (LIM domain Kinase 1); The first LIM domain of LIMK1 (LIM domain ...
189-242 1.12e-04

The first LIM domain of LIMK1 (LIM domain Kinase 1); The first LIM domain of LIMK1 (LIM domain Kinase 1): LIMK1 belongs to the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerization. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK1 is expressed in all tissues and is localized to focal adhesions in the cell. LIMK1 can form homodimers upon binding of HSP90 and is activated by Rho effector Rho kinase and MAPKAPK2. LIMK1 is important for normal central nervous system development, and its deletion has been implicated in the development of the human genetic disorder Williams syndrome. Moreover, LIMK1 up-regulates the promoter activity of urokinase type plasminogen activator and induces its mRNA and protein expression in breast cancer cells. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188846 [Multi-domain]  Cd Length: 74  Bit Score: 41.80  E-value: 1.12e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1959422415  189 LCHECG-GALRGSYITALDHKYHIEHFTCSVCPTVFGAQdsYYEHEGRVYCHFHY 242
Cdd:cd09462     21 VCASCGqSIYDGQYLQALNSDWHADCFRCCECGASLSHW--YYEKDGRLFCKKDY 73
LIM1_LIMK1 cd09462
The first LIM domain of LIMK1 (LIM domain Kinase 1); The first LIM domain of LIMK1 (LIM domain ...
125-183 1.21e-04

The first LIM domain of LIMK1 (LIM domain Kinase 1); The first LIM domain of LIMK1 (LIM domain Kinase 1): LIMK1 belongs to the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerization. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK1 is expressed in all tissues and is localized to focal adhesions in the cell. LIMK1 can form homodimers upon binding of HSP90 and is activated by Rho effector Rho kinase and MAPKAPK2. LIMK1 is important for normal central nervous system development, and its deletion has been implicated in the development of the human genetic disorder Williams syndrome. Moreover, LIMK1 up-regulates the promoter activity of urokinase type plasminogen activator and induces its mRNA and protein expression in breast cancer cells. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188846 [Multi-domain]  Cd Length: 74  Bit Score: 41.41  E-value: 1.21e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959422415  125 ICKKCGEPL-TGQFVRALGATYHLECFKCEDCGQIVASKFFPVDaedgsGQYpLCETDYF 183
Cdd:cd09462     21 VCASCGQSIyDGQYLQALNSDWHADCFRCCECGASLSHWYYEKD-----GRL-FCKKDYW 74
LIM_RIL cd09451
The LIM domain of RIL; The LIM domain of RIL: RIL contains an N-terminal PDZ domain, a LIM ...
126-156 1.35e-04

The LIM domain of RIL; The LIM domain of RIL: RIL contains an N-terminal PDZ domain, a LIM domain, and a short consensus C-terminal region. It is the smallest molecule in the ALP LIM domain containing protein family. RIL was identified in rat fibroblasts and in human lymphocytes. The LIM domain interacts with the AMPA glutamate receptor in dendritic spines. The consensus C-terminus interacts with PTP-BL, a submembranous protein tyrosine phosphatase and the PDZ domain is responsible to interact with alpha-actinin molecules. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188835  Cd Length: 53  Bit Score: 40.68  E-value: 1.35e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCG 156
Cdd:cd09451      1 CTRCGNGIVGTIVKARDKLYHPECFMCDDCG 31
LIM4_Paxillin_like cd09339
The fourth LIM domain of the Paxillin-like protein family; The fourth LIM domain of the ...
501-557 1.66e-04

The fourth LIM domain of the Paxillin-like protein family; The fourth LIM domain of the Paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188725 [Multi-domain]  Cd Length: 52  Bit Score: 40.40  E-value: 1.66e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1959422415  501 CAACKEPIDDECIMLGESRWHlkPPHLTCAACQTDLTDTCqealWSPRIKKVFCNSC 557
Cdd:cd09339      1 CAGCGKPITGRCITAMGRKFH--PEHFVCAFCLKQLSKGT----FKEQDDKPYCHPC 51
LIM5_PINCH cd09335
The fifth LIM domain of protein PINCH; The fifth LIM domain of protein PINCH: PINCH plays ...
190-238 1.85e-04

The fifth LIM domain of protein PINCH; The fifth LIM domain of protein PINCH: PINCH plays pivotal roles in the assembly of focal adhesions (FAs), regulating diverse functions in cell adhesion, growth, and differentiation through LIM-mediated protein-protein interactions. PINCH comprises an array of five LIM domains that interact with integrin-linked kinase (ILK), Nck2 (also called Nckbeta or Grb4) and other interaction partners. These interactions are essential for triggering the FA assembly and for relaying diverse mechanical and biochemical signals between Cell-extracellular matrix and the actin cytoskeleton. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188721 [Multi-domain]  Cd Length: 54  Bit Score: 40.41  E-value: 1.85e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFGAQDSYYEHEGRVYC 238
Cdd:cd09335      1 CYHCNQVIEGDVVSALNKTWCVDHFSCSFCDTKLTLKSKFYEFDMKPVC 49
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
500-557 1.91e-04

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 40.44  E-value: 1.91e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1959422415   500 CCAACKEPIDDECIML--GESRWHlkPPHLTCAACQTDLT-DTCQEalwspRIKKVFCNSC 557
Cdd:smart00132    1 KCAGCGKPIYGTERVLraLGKVWH--PECFKCATCGKPLSgDTFFE-----KDGKLYCKDC 54
LIM4_PINCH cd09334
The fourth LIM domain of protein PINCH; The fourth LIM domain of protein PINCH: PINCH plays a ...
125-182 2.98e-04

The fourth LIM domain of protein PINCH; The fourth LIM domain of protein PINCH: PINCH plays a pivotal role in the assembly of focal adhesions (FAs), regulating diverse functions in cell adhesion, growth, and differentiation through LIM-mediated protein-protein interactions. PINCH comprises an array of five LIM domains that interact with integrin-linked kinase (ILK), Nck2 (also called Nckbeta or Grb4) and other interaction partners. These interactions are essential for triggering the FA assembly and for relaying diverse mechanical and biochemical signals between Cell-extracellular matrix and the actin cytoskeleton. The PINCH LIM4 domain recognizes the third SH3 domain of another adaptor protein, Nck2. This step is an important component of integrin signaling event. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assem bly of multimeric protein complexes.


Pssm-ID: 188720 [Multi-domain]  Cd Length: 54  Bit Score: 39.65  E-value: 2.98e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1959422415  125 ICKKCGEPLTGQFVRALGATYHLECFKCEDCGQivasKFFPVDAEDGSGQyPLCETDY 182
Cdd:cd09334      2 ICGACRRPIEGRVVTALGKHWHVEHFVCAKCEK----PFLGHRHYEKKGL-AYCETHY 54
LIM1_Ajuba_like cd09352
The first LIM domain of Ajuba-like proteins; The first LIM domain of Ajuba-like proteins: ...
126-164 2.99e-04

The first LIM domain of Ajuba-like proteins; The first LIM domain of Ajuba-like proteins: Ajuba like LIM protein family includes three highly homologous proteins Ajuba, Limd1, and WTIP. Members of the family contain three tandem C-terminal LIM domains and a proline-rich N-terminal region. This family of proteins functions as scaffolds, participating in the assembly of numerous protein complexes. In the cytoplasm, Ajuba binds Grb2 to modulate serum-stimulated ERK activation. Ajuba also recruits the TNF receptor-associated factor 6 (TRAF6) to p62 and activates PKCKappa activity. Ajuba interacts with alpha-catenin and F-actin to contribute to the formation or stabilization of adheren junctions by linking adhesive receptors to the actin cytoskeleton. Although Ajuba is a cytoplasmic protein, it can shuttle into the nucleus. In nucleus, Ajuba functions as a corepressor for the zinc finger-protein Snail. It binds to the SNAG repression domain of Snail through its LIM region. Arginine methyltransferase-5 (Prmt5), a protein in the complex, is recruited to Snai l through an interaction with Ajuba. This ternary complex functions to repress E-cadherin, a Snail target gene. In addition, Ajuba contains functional nuclear-receptor interacting motifs and selectively interacts with retinoic acid receptors (RARs) and rexinoid receptor (RXRs) to negatively regulate retinoic acid signaling. Wtip, the Wt1-interacting protein, was originally identified as an interaction partner of the Wilms tumour protein 1 (WT1). Wtip is involved in kidney and neural crest development. Wtip interacts with the receptor tyrosine kinase Ror2 and inhibits canonical Wnt signaling. LIMD1 was reported to inhibit cell growth and metastases. The inhibition may be mediated through an interaction with the protein barrier-to-autointegration (BAF), a component of SWI/SNF chromatin-remodeling protein; or through the interaction with retinoblastoma protein (pRB), resulting in inhibition of E2F-mediated transcription, and expression of the majority of genes with E2F1- responsive elements. Recently, Limd1 was shown to interact with the p62/sequestosome protein and influence IL-1 and RANKL signaling by facilitating the assembly of a p62/TRAF6/a-PKC multi-protein complex. The Limd1-p62 interaction affects both NF-kappaB and AP-1 activity in epithelial cells and osteoclasts. Moreover, LIMD1 functions as tumor repressor to block lung tumor cell line in vitro and in vivo. Recent studies revealed that LIM proteins Wtip, LIMD1 and Ajuba interact with components of RNA induced silencing complexes (RISC) as well as eIF4E and the mRNA m7GTP cap-protein complex and are required for microRNA-mediated gene silencing. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188738  Cd Length: 54  Bit Score: 39.72  E-value: 2.99e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1959422415  126 CKKCGEPLTG--QFVRALGATYHLECFKCEDCGQIVASKFF 164
Cdd:cd09352      1 CVKCGKGVYGasQACQAMGNLYHTNCFTCCSCGRTLRGKAF 41
LIM3_TRIP6 cd09436
The third LIM domain of Thyroid receptor-interacting protein 6 (TRIP6); The third LIM domain ...
126-177 3.10e-04

The third LIM domain of Thyroid receptor-interacting protein 6 (TRIP6); The third LIM domain of Thyroid receptor-interacting protein 6 (TRIP6): TRIP6 is a member of the zyxin LIM protein family and contains three LIM zinc-binding domains at the C-terminal. TRIP6 protein localizes to focal adhesion sites and along actin stress fibers. Recruitment of this protein to the plasma membrane occurs in a lysophosphatidic acid (LPA)-dependent manner. TRIP6 recruits a number of molecules involved in actin assembly, cell motility, survival and transcriptional control. The function of TRIP6 in cell motility is regulated by Src-dependent phosphorylation at a Tyr residue. The phosphorylation activates the coupling to the Crk SH2 domain, which is required for the function of TRIP6 in promoting lysophosphatidic acid (LPA)-induced cell migration. TRIP6 can shuttle to the nucleus to serve as a coactivator of AP-1 and NF-kappaB transcriptional factors. Moreover, TRIP6 can form a ternary complex with the NHERF2 PDZ protein and LPA2 receptor to regulate LPA-induced activation of ERK and AKT, rendering cells resistant to chemotherapy. Recent evidence shows that TRIP6 antagonizes Fas-Induced apoptosis by enhancing the antiapoptotic effect of LPA in cells. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188820  Cd Length: 66  Bit Score: 40.38  E-value: 3.10e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1959422415  126 CKKCGEPLT---GQ--FVR--ALGATYHLECFKCEDCGQIVASKffpvdaeDGSGQYPL 177
Cdd:cd09436      1 CSVCKEPIMpapGQeeTVRivALDRDFHVQCYRCEDCGSLLSEG-------DNQGCYPL 52
LIM2_Ajuba_like cd09355
The second LIM domain of Ajuba-like proteins; The second LIM domain of Ajuba-like proteins: ...
126-182 4.05e-04

The second LIM domain of Ajuba-like proteins; The second LIM domain of Ajuba-like proteins: Ajuba like LIM protein family includes three highly homologous proteins Ajuba, Limd1, and WTIP. Members of the family contain three tandem C-terminal LIM domains and a proline-rich N-terminal region. This family of proteins functions as scaffolds, participating in the assembly of numerous protein complexes. In the cytoplasm, Ajuba binds Grb2 to modulate serum-stimulated ERK activation. Ajuba also recruits the TNF receptor-associated factor 6 (TRAF6) to p62 and activates PKCKappa activity. Ajuba interacts with alpha-catenin and F-actin to contribute to the formation or stabilization of adheren junctions by linking adhesive receptors to the actin cytoskeleton. Although Ajuba is a cytoplasmic protein, it can shuttle into the nucleus. In nucleus, Ajuba functions as a corepressor for the zinc finger-protein Snail. It binds to the SNAG repression domain of Snail through its LIM region. Arginine methyltransferase-5 (Prmt5), a protein in the complex, is recruited to Snai l through an interaction with Ajuba. This ternary complex functions to repress E-cadherin, a Snail target gene. In addition, Ajuba contains functional nuclear-receptor interacting motifs and selectively interacts with retinoic acid receptors (RARs) and rexinoid receptor (RXRs) to negatively regulate retinoic acid signaling. Wtip, the Wt1-interacting protein, was originally identified as an interaction partner of the Wilms tumour protein 1 (WT1). Wtip is involved in kidney and neural crest development. Wtip interacts with the receptor tyrosine kinase Ror2 and inhibits canonical Wnt signaling. LIMD1 was reported to inhibit cell growth and metastases. The inhibition may be mediated through an interaction with the protein barrier-to-autointegration (BAF), a component of SWI/SNF chromatin-remodeling protein; or through the interaction with retinoblastoma protein (pRB), resulting in inhibition of E2F-mediated transcription, and expression of the majority of genes with E2F1- responsive elements. Recently, Limd1 was shown to interact with the p62/sequestosome protein and influence IL-1 and RANKL signaling by facilitating the assembly of a p62/TRAF6/a-PKC multi-protein complex. The Limd1-p62 interaction affects both NF-kappaB and AP-1 activity in epithelial cells and osteoclasts. Moreover, LIMD1 functions as tumor repressor to block lung tumor cell line in vitro and in vivo. Recent studies revealed that LIM proteins Wtip, LIMD1 and Ajuba interact with components of RNA induced silencing complexes (RISC) as well as eIF4E and the mRNA m7GTP cap-protein complex and are required for microRNA-mediated gene silencing. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188741 [Multi-domain]  Cd Length: 53  Bit Score: 39.25  E-value: 4.05e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGQIVASKFFPVDAEdgSGQYplCETDY 182
Cdd:cd09355      1 CAVCGHLIMEMILQALGKSYHPGCFRCCVCNECLDGVPFTVDVE--NNIY--CVKDY 53
LIM2_TRIP6 cd09356
The second LIM domain of Thyroid receptor-interacting protein 6 (TRIP6); The second LIM domain ...
126-168 4.96e-04

The second LIM domain of Thyroid receptor-interacting protein 6 (TRIP6); The second LIM domain of Thyroid receptor-interacting protein 6 (TRIP6): TRIP6 is a member of the zyxin LIM protein family and contains three LIM zinc-binding domains at the C-terminal. TRIP6 protein localizes to focal adhesion sites and along actin stress fibers. Recruitment of this protein to the plasma membrane occurs in a lysophosphatidic acid (LPA)-dependent manner. TRIP6 recruits a number of molecules involved in actin assembly, cell motility, survival and transcriptional control. The function of TRIP6 in cell motility is regulated by Src-dependent phosphorylation at a Tyr residue. The phosphorylation activates the coupling to the Crk SH2 domain, which is required for the function of TRIP6 in promoting lysophosphatidic acid (LPA)-induced cell migration. TRIP6 can shuttle to the nucleus to serve as a coactivator of AP-1 and NF-kappaB transcriptional factors. Moreover, TRIP6 can form a ternary complex with the NHERF2 PDZ protein and LPA2 receptor to regulate LPA-induced activation of ERK and AKT, rendering cells resistant to chemotherapy. Recent evidence shows that TRIP6 antagonizes Fas-Induced apoptosis by enhancing the antiapoptotic effect of LPA in cells. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188742  Cd Length: 53  Bit Score: 39.08  E-value: 4.96e-04
                           10        20        30        40
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gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGQIVASKFFPVDA 168
Cdd:cd09356      1 CSVCSKPIMERILRATGKAYHPHCFTCVVCHRSLDGIPFTVDA 43
LIM3_Enigma_like cd09363
The third LIM domain of Enigma-like family; The third LIM domain of Enigma-like family: The ...
190-241 5.23e-04

The third LIM domain of Enigma-like family; The third LIM domain of Enigma-like family: The Enigma LIM domain family is comprised of three members: Enigma, ENH, and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. Enigma was initially characterized in humans and is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. The second member, ENH protein, was first identified in rat brain. It has been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188749 [Multi-domain]  Cd Length: 54  Bit Score: 38.96  E-value: 5.23e-04
                           10        20        30        40        50
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gi 1959422415  190 CHECGGALRGS--YITALDHKYHIEHFTCSVCPTVFGAQdSYYEHEGRVYCHFH 241
Cdd:cd09363      1 CHGCDFPIEAGdrFLEALGHTWHDTCFVCAVCHVNLEGQ-TFYSKKDKPLCKNH 53
LIM2_LMO4 cd09387
The second LIM domain of LMO4 (LIM domain only protein 4); The second LIM domain of LMO4 (LIM ...
126-181 6.13e-04

The second LIM domain of LMO4 (LIM domain only protein 4); The second LIM domain of LMO4 (LIM domain only protein 4): LMO4 is a nuclear protein that plays important roles in transcriptional regulation and development. LMO4 is involved in various functions in tumorigenesis and cellular differentiation. LMO4 proteins regulate gene expression by interacting with a wide variety of transcription factors and cofactors to form large transcription complexes. It can interact with Smad proteins, and associate with the promoter of the PAI-1 (plasminogen activator inhibitor-1) gene in a TGFbeta (transforming growth factor beta)-dependent manner. LMO4 can also form a complex with transcription regulator CREB (cAMP response element-binding protein) and interact with CLIM1 and CLIM2. In breast tissue, LMO4 interacts with multiple proteins, including the cofactor CtIP [CtBP (C-terminal binding protein)-interacting protein], the breast and ovarian tumor suppressor BRCA1 (breast-cancer susceptibility gene 1) and the LIM-domain-binding protein LDB1. Functionally, LMO4 is shown to repress BRCA1-mediated transcription activation, thus invoking a potential role for LMO4 as a negative regulator of BRCA1 in sporadic breast cancer. LMO4 also forms complex to both ERa (oestrogen receptor alpha), MTA1 (metastasis tumor antigen 1), and HDACs (histone deacetylases), implying that LMO4 is also a component of the MTA1 corepressor complex. Over-expressed LMO4 represses ERa transactivation functions in an HDAC-dependent manner, and contributes to the process of breast cancer progression by allowing the development of Era-negative phenotypes. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188773  Cd Length: 55  Bit Score: 39.00  E-value: 6.13e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1959422415  126 CKKCGE--PLTGQFVRALGATYHLECFKCEDCG-QIVASKFFPVdaEDGSgqyPLCETD 181
Cdd:cd09387      1 CSACGQsiPASELVMRAQGNVYHLKCFTCSTCHnQLVPGDRFHY--VNGS---LFCEHD 54
LIM2_LIMK2 cd09465
The second LIM domain of LIMK2 (LIM domain Kinase 2); The second LIM domain of LIMK2 (LIM ...
189-238 7.05e-04

The second LIM domain of LIMK2 (LIM domain Kinase 2); The second LIM domain of LIMK2 (LIM domain Kinase 2): LIMK2 is a member of the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, altering the rate of actin depolymerisation. LIMK activity is activated by phosphorylation of a threonine residue within the activation loop of the kinase by p21-activated kinases 1 and 4 and by Rho kinase. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK2 is expressed in all tissues. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The activity of LIM kinase 2 to regulate cofilin phosphorylation is inhibited by the direct binding of Par-3. LIMK2 activation promotes cell cycle progression. The phenotype of Limk2 knockout mice shows a defect in spermatogenesis. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188849 [Multi-domain]  Cd Length: 59  Bit Score: 38.76  E-value: 7.05e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1959422415  189 LCHECGGALRGSYITALDHKYHIEHFTCSVCPTVFGAQDSY--YEHeGRVYC 238
Cdd:cd09465      5 LCHGCSLLMTGPAMVAGEYKYHPECFACMSCKVIIEDGDTYalVQH-TTLYC 55
LIM2_Enigma cd09456
The second LIM domain of Enigma; The second LIM domain of Enigma: Enigma was initially ...
190-242 7.45e-04

The second LIM domain of Enigma; The second LIM domain of Enigma: Enigma was initially characterized in humans as a protein containing three LIM domains at the C-terminus and a PDZ domain at N-terminus. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. Enigma is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188840 [Multi-domain]  Cd Length: 52  Bit Score: 38.82  E-value: 7.45e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFGAQdSYYEHEGRVYCHFHY 242
Cdd:cd09456      1 CAKCKKKITGEIMHALKMTWHVHCFTCAACKTPIRNR-AFYMEEGAPYCERDY 52
LIM_ALP cd09450
This family represents the LIM domain of ALP, actinin-associated LIM protein; This family ...
126-169 7.91e-04

This family represents the LIM domain of ALP, actinin-associated LIM protein; This family represents the LIM domain of ALP, actinin-associated LIM protein. ALP contains an N-terminal PDZ domain, a C-terminal LIM domain and an ALP-subfamily-specific 34-amino-acid motif termed ALP-like motif (AM), which contains a putative consensus protein kinase C (PKC) phosphorylation site and two alpha-helices. ALP proteins are found in heart and in skeletal muscle. ALP may act as a signaling molecule which is regulated by PKC-dependent signaling. ALP plays an essential role in the development of RV (right ventricle) chamber. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188834 [Multi-domain]  Cd Length: 53  Bit Score: 38.73  E-value: 7.91e-04
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gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGQIVASK-FFPVDAE 169
Cdd:cd09450      1 CDKCGSGIVGTVVKARDKYRHPECFVCSDCNLNLKQKgYFFVEGQ 45
LIM_TLP_like cd09401
The LIM domains of thymus LIM protein (TLP); The LIM domain of thymus LIM protein (TLP) like ...
126-161 8.08e-04

The LIM domains of thymus LIM protein (TLP); The LIM domain of thymus LIM protein (TLP) like proteins: This family includes the LIM domains of TLP and CRIP (Cysteine-Rich Intestinal Protein). TLP is the distant member of the CRP family of proteins. TLP has two isomers (TLP-A and TLP-B) and sharing approximately 30% with each of the three other CRPs. Like CRP1, CRP2 and CRP3/MLP, TLP has two LIM domains, connected by a flexible linker region. Unlike the CRPs, TLP lacks the nuclear targeting signal (K/R-K/R-Y-G-P-K) and is localized solely in the cytoplasm. TLP is specifically expressed in the thymus in a subset of cortical epithelial cells. TLP has a role in development of normal thymus and in controlling the development and differentiation of thymic epithelial cells. CRIP is a short LIM protein with only one LIM domain. CRIP gene is developmentally regulated and can be induced by glucocorticoid hormones during the first three postnatal weeks. The domain shows close sequence homology to LIM domain of thymus LIM protein. However, unlike the TLP proteins which have two LIM domains, the members of this family have only one LIM domain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188785 [Multi-domain]  Cd Length: 53  Bit Score: 38.48  E-value: 8.08e-04
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                   ....*....|....*....|....*....|....*..
gi 1959422415  126 CKKCGEPLTG-QFVRALGATYHLECFKCEDCGQIVAS 161
Cdd:cd09401      1 CPKCGKPVYFaEKKTSLGRDWHKPCLRCEKCKKTLTP 37
LIM_like_1 cd09400
LIM domain in proteins of unknown function; LIM domain in proteins of unknown function: LIM ...
126-180 8.53e-04

LIM domain in proteins of unknown function; LIM domain in proteins of unknown function: LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation, and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. The LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).


Pssm-ID: 188784  Cd Length: 61  Bit Score: 38.56  E-value: 8.53e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1959422415  126 CKKCGEPLT-GQFVRALGATYHLECFKCEDCG-QIVASKFFPVDaedgSGQYpLCET 180
Cdd:cd09400      5 CASCGLPVFlAERLLIEGKVYHRTCFKCARCGvQLTPGSFYETE----YGSY-CCET 56
LIM1_Enigma_like cd09361
The first LIM domain of Enigma-like family; The first LIM domain of Enigma-like family: The ...
126-155 8.82e-04

The first LIM domain of Enigma-like family; The first LIM domain of Enigma-like family: The Enigma LIM domain family is comprised of three members: Enigma, ENH, and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. Enigma was initially characterized in humans and is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. The second member, ENH protein, was first identified in rat brain. It has been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188747 [Multi-domain]  Cd Length: 52  Bit Score: 38.50  E-value: 8.82e-04
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gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDC 155
Cdd:cd09361      1 CAHCNQVIRGPFLVALGRSWHPEEFTCSHC 30
LIM_ALP cd09450
This family represents the LIM domain of ALP, actinin-associated LIM protein; This family ...
190-241 9.17e-04

This family represents the LIM domain of ALP, actinin-associated LIM protein; This family represents the LIM domain of ALP, actinin-associated LIM protein. ALP contains an N-terminal PDZ domain, a C-terminal LIM domain and an ALP-subfamily-specific 34-amino-acid motif termed ALP-like motif (AM), which contains a putative consensus protein kinase C (PKC) phosphorylation site and two alpha-helices. ALP proteins are found in heart and in skeletal muscle. ALP may act as a signaling molecule which is regulated by PKC-dependent signaling. ALP plays an essential role in the development of RV (right ventricle) chamber. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188834 [Multi-domain]  Cd Length: 53  Bit Score: 38.35  E-value: 9.17e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFgAQDSYYEHEGRVYCHFH 241
Cdd:cd09450      1 CDKCGSGIVGTVVKARDKYRHPECFVCSDCNLNL-KQKGYFFVEGQLYCEAH 51
LIM2_Paxillin_like cd09337
The second LIM domain of the paxillin like protein family; The second LIM domain of the ...
126-182 9.46e-04

The second LIM domain of the paxillin like protein family; The second LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188723 [Multi-domain]  Cd Length: 52  Bit Score: 38.52  E-value: 9.46e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGqivasKFFpvdAEDG----SGQyPLCETDY 182
Cdd:cd09337      1 CAYCNGPILDKCVTALDKTWHPEHFFCAQCG-----KPF---GDEGfhekDGK-PYCREDY 52
LIM_CLP36 cd09448
This family represents the LIM domain of CLP36; This family represents the LIM domain of CLP36. ...
126-167 9.68e-04

This family represents the LIM domain of CLP36; This family represents the LIM domain of CLP36. CLP36 has also been named as CLIM1, Elfin, or PDLIM1. CLP36 contains a C-terminal LIM domain and an N-terminal PDZ domain. CLP36 is highly expressed in heart and is present in many other tissues including lung, liver, spleen, and blood. CLP36 has been implicated in many processes including hypoxia and regulation of actin stress fibers. CLP36 co-localizes with alpha-actinin-2 at the Z-lines in myocardium. In addition, CLP36 binds to alpha-actinin-1 and alpha-actinin-4, and associates with F-actin filaments and stress fibers. CLP36 might be involved in not only the function of sarcomeres in muscle cells, but also in actin stress fiber-mediated cellular processes, such as cell shape, migration, polarit, and cytokinesis in non-muscle cells. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188832  Cd Length: 52  Bit Score: 38.36  E-value: 9.68e-04
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gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGQIVASK--FFPVD 167
Cdd:cd09448      1 CDKCGSGIVGVFVKIRDKPRHPECYVCTDCGTNLKQKghFFVED 44
LIM4_Leupaxin cd09412
The fourth LIM domain of Leupaxin; The fourth LIM domain of Leupaxin: Leupaxin is a ...
126-155 9.88e-04

The fourth LIM domain of Leupaxin; The fourth LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188796 [Multi-domain]  Cd Length: 52  Bit Score: 38.18  E-value: 9.88e-04
                           10        20        30
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gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDC 155
Cdd:cd09412      1 CGSCGLPITGRCISALGRKFHPEHFVCAFC 30
LIM2_FBLP-1 cd09372
The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1); The second LIM domain of ...
190-238 1.01e-03

The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1); The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1): Fblp-1 contains a proline-rich domain near its N terminus and two LIM domains at its C terminus. FBLP-1 mRNA was detected in a variety of tissues and cells including platelets and endothelial cells. FBLP-1 binds to Filamins. The association between filamin B and FBLP-1 may play an unknown role in cytoskeletal function, cell adhesion, and cell motility. As in other LIM domains, this domain family is 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188758 [Multi-domain]  Cd Length: 53  Bit Score: 38.17  E-value: 1.01e-03
                           10        20        30        40
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gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFGAQDSYYEHEGRVYC 238
Cdd:cd09372      1 CAKCQGVITEHIIRALGKGYHPPCFTCVTCGRRIGDESFAVDEQNEVYC 49
LIM1_Enigma_like_1 cd09455
The first LIM domain of an Enigma subfamily with unknown function; The first LIM domain of an ...
190-242 1.20e-03

The first LIM domain of an Enigma subfamily with unknown function; The first LIM domain of an Enigma subfamily with unknown function: The Enigma LIM domain family is comprised of three characterized members: Enigma, ENH and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. They serve as adaptor proteins, where the PDZ domain tethers the protein to the cytoskeleton and the LIM domains, recruit signaling proteins to implement corresponding functions. The members of the Enigma family have been implicated in regulating or organizing cytoskeletal structure, as well as involving multiple signaling pathways. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188839  Cd Length: 54  Bit Score: 38.21  E-value: 1.20e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFGAQD-SYYEHEGRVYCHFHY 242
Cdd:cd09455      1 CESCNQQIRGPFITALGKIWCPDHFICANASCRRPLQDiGFVEEKGQLYCEYCF 54
LIM1_Lhx7_Lhx8 cd09381
The first LIM domain of Lhx7 and Lhx8; The first LIM domain of Lhx7 and Lhx8: Lhx7 and Lhx8 ...
189-242 1.45e-03

The first LIM domain of Lhx7 and Lhx8; The first LIM domain of Lhx7 and Lhx8: Lhx7 and Lhx8 belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs such as the pituitary gland and the pancreas. Studies using mutant mice have revealed roles for Lhx7 and Lhx8 in the development of cholinergic neurons in the telencephalon and in basal forebrain development. Mice lacking alleles of the LIM-homeobox gene Lhx7 or Lhx8 display dramatically reduced number of forebrain cholinergic neurons. In addition, Lhx7 mutation affects male and female mice differently, with females appearing more affected than males. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188767 [Multi-domain]  Cd Length: 56  Bit Score: 38.03  E-value: 1.45e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1959422415  189 LCHECGGALRGSYITAL-DHKYHIEHFTCSVCPTVFGAQDSYYEHEGRVYCHFHY 242
Cdd:cd09381      1 VCSSCGLEIVDKYLLKVnDLCWHVRCLSCSVCRTSLGRHTSCYIKDKDIFCKLDY 55
LIM3_Zyxin cd09435
The third LIM domain of Zyxin; The third LIM domain of Zyxin: Zyxin exhibits three copies of ...
126-193 1.51e-03

The third LIM domain of Zyxin; The third LIM domain of Zyxin: Zyxin exhibits three copies of the LIM domain, an extensive proline-rich domain and a nuclear export signal. Localized at sites of cellsubstratum adhesion in fibroblasts, Zyxin interacts with alpha-actinin, members of the cysteine-rich protein (CRP) family, proteins that display Src homology 3 (SH3) domains and Ena/VASP family members. Zyxin and its partners have been implicated in the spatial control of actin filament assembly as well as in pathways important for cell differentiation. In addition to its functions at focal adhesion plaques, recent work has shown that zyxin moves from the sites of cell contacts to the nucleus, where it directly participates in the regulation of gene expression. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188819  Cd Length: 67  Bit Score: 38.31  E-value: 1.51e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1959422415  126 CKKCGEPLTGQ-------FVRALGATYHLECFKCEDCGQIVAskffpVDAEDgSGQYPLcetdyfrRLDLLCHEC 193
Cdd:cd09435      1 CCVCSEPIMPEpgrdetvRVVALEKNFHMKCYKCEDCGRPLS-----IEADD-NGCFPL-------DGHVLCMKC 62
LIM5_PINCH cd09335
The fifth LIM domain of protein PINCH; The fifth LIM domain of protein PINCH: PINCH plays ...
126-182 1.56e-03

The fifth LIM domain of protein PINCH; The fifth LIM domain of protein PINCH: PINCH plays pivotal roles in the assembly of focal adhesions (FAs), regulating diverse functions in cell adhesion, growth, and differentiation through LIM-mediated protein-protein interactions. PINCH comprises an array of five LIM domains that interact with integrin-linked kinase (ILK), Nck2 (also called Nckbeta or Grb4) and other interaction partners. These interactions are essential for triggering the FA assembly and for relaying diverse mechanical and biochemical signals between Cell-extracellular matrix and the actin cytoskeleton. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188721 [Multi-domain]  Cd Length: 54  Bit Score: 37.71  E-value: 1.56e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGQIVA--SKFFPVDAEdgsgqyPLCETDY 182
Cdd:cd09335      1 CYHCNQVIEGDVVSALNKTWCVDHFSCSFCDTKLTlkSKFYEFDMK------PVCKKCY 53
LIM4_PINCH cd09334
The fourth LIM domain of protein PINCH; The fourth LIM domain of protein PINCH: PINCH plays a ...
501-533 1.97e-03

The fourth LIM domain of protein PINCH; The fourth LIM domain of protein PINCH: PINCH plays a pivotal role in the assembly of focal adhesions (FAs), regulating diverse functions in cell adhesion, growth, and differentiation through LIM-mediated protein-protein interactions. PINCH comprises an array of five LIM domains that interact with integrin-linked kinase (ILK), Nck2 (also called Nckbeta or Grb4) and other interaction partners. These interactions are essential for triggering the FA assembly and for relaying diverse mechanical and biochemical signals between Cell-extracellular matrix and the actin cytoskeleton. The PINCH LIM4 domain recognizes the third SH3 domain of another adaptor protein, Nck2. This step is an important component of integrin signaling event. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assem bly of multimeric protein complexes.


Pssm-ID: 188720 [Multi-domain]  Cd Length: 54  Bit Score: 37.33  E-value: 1.97e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1959422415  501 CAACKEPIDDECIM-LGESrWHlkPPHLTCAACQ 533
Cdd:cd09334      3 CGACRRPIEGRVVTaLGKH-WH--VEHFVCAKCE 33
LIM1_Zyxin cd09349
The first LIM domain of Zyxin; The first LIM domain of Zyxin: Zyxin exhibits three copies of ...
189-238 2.10e-03

The first LIM domain of Zyxin; The first LIM domain of Zyxin: Zyxin exhibits three copies of the LIM domain, an extensive proline-rich domain and a nuclear export signal. Localized at sites of cell substratum adhesion in fibroblasts, Zyxin interacts with alpha-actinin, members of the cysteine-rich protein (CRP) family, proteins that display Src homology 3 (SH3) domains and Ena/VASP family members. Zyxin and its partners have been implicated in the spatial control of actin filament assembly as well as in pathways important for cell differentiation. In addition to its functions at focal adhesion plaques, recent work has shown that zyxin moves from the sites of cell contacts to the nucleus, where it directly participates in the regulation of gene expression. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188735 [Multi-domain]  Cd Length: 87  Bit Score: 38.30  E-value: 2.10e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1959422415  189 LCHECGGALRGSY--ITALDHKYHIEHFTCSVCPTVFGAQdSYYEHEGRVYC 238
Cdd:cd09349     33 LCGICGQPLSRTQpaVRALGHLFHVTCFTCHQCEQQLQGQ-QFYSLEGKPYC 83
LIM1_Rga cd09394
The first LIM domain of Rga GTPase-Activating Proteins; The first LIM domain of Rga ...
126-156 2.43e-03

The first LIM domain of Rga GTPase-Activating Proteins; The first LIM domain of Rga GTPase-Activating Proteins: The members of this family contain two tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Rga activates GTPases during polarized morphogenesis. In yeast, a known regulating target of Rga is CDC42p, a small GTPase. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188780  Cd Length: 55  Bit Score: 37.34  E-value: 2.43e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1959422415  126 CKKCGEPLTGQFVRALGAT-YHLECFKCEDCG 156
Cdd:cd09394      1 CVGCKESITEGHAYELGGDrWHIHCFKCYKCD 32
LIM2_dLMO cd09390
The second LIM domain of dLMO (Beaderx); The second LIM domain of dLMO (Beaderx): dLMO is a ...
126-182 2.47e-03

The second LIM domain of dLMO (Beaderx); The second LIM domain of dLMO (Beaderx): dLMO is a nuclear protein that plays important roles in transcriptional regulation and development. In Drosophila dLMO modulates the activity of LIM-homeodomain protein Apterous (Ap), which regulates the formation of the dorsal-ventral axis of the Drosophila wing. Biochemical analysis shows that dLMO protein influences the activity of Apterous by binding of its cofactor Chip. Further studies shown that dLMO proteins might function in an evolutionarily conserved mechanism involved in patterning the appendages. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188776  Cd Length: 55  Bit Score: 37.14  E-value: 2.47e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1959422415  126 CKKCGE--PLTGQFVRALGATYHLECFKCEDCGQ--IVASKFFPVDAEdgsgqyPLCETDY 182
Cdd:cd09390      1 CAACSKtiPAFEMVMRARTNVYHLECFACQRCNHrfCVGDRFYLCENK------ILCEYDY 55
LIM2_Rga cd09395
The second LIM domain of Rga GTPase-Activating Proteins; The second LIM domain of Rga ...
126-175 2.57e-03

The second LIM domain of Rga GTPase-Activating Proteins; The second LIM domain of Rga GTPase-Activating Proteins: The members of this family contain two tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Rga activates GTPases during polarized morphogenesis. In yeast, a known regulating target of Rga is CDC42p, a small GTPase. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188781  Cd Length: 53  Bit Score: 37.07  E-value: 2.57e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1959422415  126 CKKCGEPLTGQFV-RALGATYHLECFKCEDCGQIVASKffpVDAEDGSGQY 175
Cdd:cd09395      1 CKNCGKKIDDTAIlLSSDEAYCSDCFRCRRCSRDITDL---KYAKTKRGLF 48
LIM1_LPP cd09351
The first LIM domain of lipoma preferred partner (LPP); The first LIM domain of lipoma ...
126-182 2.68e-03

The first LIM domain of lipoma preferred partner (LPP); The first LIM domain of lipoma preferred partner (LPP): LPP is a member of the zyxin LIM protein family and contains three LIM zinc-binding domains at the C-terminal and proline-rich region at the N-terminal. LPP initially identified as the most frequent translocation partner of HMGA2 (High Mobility Group A2) in a subgroup of benign tumors of adipose tissue (lipomas). It was also shown to be rearranged in a number of other soft tissues, as well as in a case of acute monoblastic leukemia. In addition to its involvement in tumors, LPP was inedited as a smooth muscle restricted LIM protein that plays an important role in SMC migration. LPP is localized at sites of cell adhesion, cell-cell contacts and transiently in the nucleus. In nucleus, it acts as a coactivator for the ETS domain transcription factor PEA3. In addition to PEA3, it interacts with alpha-actinin,vasodilator stimulated phosphoprotein (VASP),Palladin, and Scrib. The LIM domains are the main focal adhesion targeting elements and that the proline- rich region, which harbors binding sites for alpha-actinin and vasodilator- stimulated phosphoprotein (VASP), has a weak targeting capacity. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188737 [Multi-domain]  Cd Length: 54  Bit Score: 37.02  E-value: 2.68e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1959422415  126 CKKCGEPLTGQF--VRALGATYHLECFKCEDCGQIVASKffPVDAEDGSgqyPLCETDY 182
Cdd:cd09351      1 CVKCGEKVLGEGsgCTAMDQVYHISCFTCHQCQINLQGK--PFYALDGK---PYCEEDY 54
LIM1_Leupaxin cd09406
The first LIM domain of Leupaxin; The first LIM domain of Leupaxin: Leupaxin is a cytoskeleton ...
501-536 2.86e-03

The first LIM domain of Leupaxin; The first LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188790 [Multi-domain]  Cd Length: 55  Bit Score: 37.16  E-value: 2.86e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1959422415  501 CAACKEPIDDECIM-LGESrWHlkPPHLTCAACQTDL 536
Cdd:cd09406      3 CASCQKPIAGQVVTaLGQT-WH--PEHFVCCQCGKEL 36
LIM2_abLIM cd09328
The second LIM domain on actin binding LIM (abLIM) proteins; The second LIM domain of actin ...
190-227 3.66e-03

The second LIM domain on actin binding LIM (abLIM) proteins; The second LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188714  Cd Length: 56  Bit Score: 36.94  E-value: 3.66e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFGAQD 227
Cdd:cd09328      4 CDSCQDFVEGEVVSALGKTYHPKCFVCSVCRQPFPPGD 41
LIM2_LIMK cd09365
The second LIM domain of LIMK (LIM domain Kinase ); The second LIM domain of LIMK (LIM domain ...
126-193 4.22e-03

The second LIM domain of LIMK (LIM domain Kinase ); The second LIM domain of LIMK (LIM domain Kinase ): LIMK protein family is comprised of two members LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerization. LIMKs can function in both cytoplasm and nucleus and are expressed in all tissues. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. However, LIMK1 and LIMk2 have different cellular locations. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The LIM domains of LIMK have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188751 [Multi-domain]  Cd Length: 54  Bit Score: 36.57  E-value: 4.22e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1959422415  126 CKKCGEPLTGQFVRALGATYHLECFKCEDCGQIVAskffpvdaeDGSgQYPLCEtdyfrRLDLLCHEC 193
Cdd:cd09365      1 CHGCSQIITGPVMVAGDHKFHPECFSCSSCKAFIG---------DGD-SYALVE-----RSKLYCGVC 53
LIM_N_RAP cd09446
The LIM domain of N-RAP; The LIM domain of N-RAP: N-RAP is a muscle-specific protein ...
190-241 4.71e-03

The LIM domain of N-RAP; The LIM domain of N-RAP: N-RAP is a muscle-specific protein concentrated at myotendinous junctions in skeletal muscle and intercalated disks in cardiac muscle. LIM domain is found at the N-terminus of N-RAP and the C-terminal of N-RAP contains a region with multiple of nebulin repeats. N-RAP functions as a scaffolding protein that organizes alpha-actinin and actin into symmetrical I-Z-I structures in developing myofibrils. Nebulin repeat is known as actin binding domain. The N-RAP is hypothesized to form antiparallel dimerization via its LIM domain. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188830  Cd Length: 53  Bit Score: 36.44  E-value: 4.71e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1959422415  190 CHECG-GALRGSYITALDHKYHIEHFTCSVCPTVFGAqDSYYEHEGRVYCHFH 241
Cdd:cd09446      1 CARCGyGVYPAEKINCIDQTWHKACFHCEVCKMMLTV-NNFVSHQKKPYCQAH 52
LIM4_FHL cd09347
The fourth LIM domain of Four and a half LIM domains protein (FHL); The fourth LIM domain of ...
126-194 4.83e-03

The fourth LIM domain of Four and a half LIM domains protein (FHL); The fourth LIM domain of Four and a half LIM domains protein (FHL): LIM-only protein family consists of five members, designated FHL1, FHL2, FHL3, FHL5 and LIMPETin. The first four members are composed of four complete LIM domains arranged in tandem and an N-terminal single zinc finger domain with a consensus sequence equivalent to the C-terminal half of a LIM domain. LIMPETin is an exception, containing six LIM domains. FHL1, 2 and 3 are predominantly expressed in muscle tissues, and FHL5 is highly expressed in male germ cells. FHL proteins exert their roles as transcription co-activators or co-repressors through a wide array of interaction partners. For example, FHL1 binds to Myosin-binding protein C, regulating myosin filament formation and sarcomere assembly. FHL2 has shown to interact with more than 50 different proteins, including receptors, structural proteins, transcription factors and cofactors, signal transducers, splicing factors, DNA replication and repair enzymes, and metabolic enzymes. FHL3 interacts with many transcription factors, such as CREB, BKLF/KLF3, CtBP2, MyoD, and MZF_1. FHL5 is a tissue-specific coactivator of CREB/CREM family transcription factors. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188733  Cd Length: 56  Bit Score: 36.55  E-value: 4.83e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1959422415  126 CKKCGEPLTGQFvralGATY--------HLECFKCEDCG-QIVASKFFPvdaedgsgqyplcetdyfRRLDLLCHECG 194
Cdd:cd09347      1 CAACTKPITGLG----GAKFisfeerqwHSDCFNCGKCSvSLVGQGFLT------------------QRDEILCPECG 56
LIM4_Paxillin cd09411
The fourth LIM domain of Paxillin; The fourth LIM domain of Paxillin: Paxillin is an adaptor ...
501-557 5.11e-03

The fourth LIM domain of Paxillin; The fourth LIM domain of Paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188795 [Multi-domain]  Cd Length: 52  Bit Score: 36.47  E-value: 5.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1959422415  501 CAACKEPIDDECIMLGESRWHlkPPHLTCAACQTDLtdtcQEALWSPRIKKVFCNSC 557
Cdd:cd09411      1 CSGCQKPITGRCITAMGKKFH--PEHFVCAFCLKQL----NKGTFKEQNDKPYCHNC 51
LIM1_UF1 cd09397
LIM domain in proteins of unknown function; The first Lim domain of a LIM domain containing ...
190-242 5.43e-03

LIM domain in proteins of unknown function; The first Lim domain of a LIM domain containing protein: The functions of the proteins are unknown. The members of this family contain two copies of LIM domain. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188783 [Multi-domain]  Cd Length: 58  Bit Score: 36.47  E-value: 5.43e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1959422415  190 CHECGGALRGSYIT----ALDHKYHIEHFTCSVCPTVFGAQDSYYEHEGRVYCHFHY 242
Cdd:cd09397      1 CRKCGLEIEGKSISskdgELSGQWHRECFVCTTCGCPFQFSVPCYVLDDKPYCQQHY 57
LIM1_LPP cd09351
The first LIM domain of lipoma preferred partner (LPP); The first LIM domain of lipoma ...
190-242 6.76e-03

The first LIM domain of lipoma preferred partner (LPP); The first LIM domain of lipoma preferred partner (LPP): LPP is a member of the zyxin LIM protein family and contains three LIM zinc-binding domains at the C-terminal and proline-rich region at the N-terminal. LPP initially identified as the most frequent translocation partner of HMGA2 (High Mobility Group A2) in a subgroup of benign tumors of adipose tissue (lipomas). It was also shown to be rearranged in a number of other soft tissues, as well as in a case of acute monoblastic leukemia. In addition to its involvement in tumors, LPP was inedited as a smooth muscle restricted LIM protein that plays an important role in SMC migration. LPP is localized at sites of cell adhesion, cell-cell contacts and transiently in the nucleus. In nucleus, it acts as a coactivator for the ETS domain transcription factor PEA3. In addition to PEA3, it interacts with alpha-actinin,vasodilator stimulated phosphoprotein (VASP),Palladin, and Scrib. The LIM domains are the main focal adhesion targeting elements and that the proline- rich region, which harbors binding sites for alpha-actinin and vasodilator- stimulated phosphoprotein (VASP), has a weak targeting capacity. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188737 [Multi-domain]  Cd Length: 54  Bit Score: 35.86  E-value: 6.76e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1959422415  190 CHECGGAL--RGSYITALDHKYHIEHFTCSVCPTVFGAQdSYYEHEGRVYCHFHY 242
Cdd:cd09351      1 CVKCGEKVlgEGSGCTAMDQVYHISCFTCHQCQINLQGK-PFYALDGKPYCEEDY 54
LIM3_abLIM cd09329
The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin ...
190-238 7.34e-03

The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188715 [Multi-domain]  Cd Length: 52  Bit Score: 35.76  E-value: 7.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1959422415  190 CHECGGALR-GSYITALDHKYHIEHFTCSVCPTVFGAQdsYYEHEGRVYC 238
Cdd:cd09329      1 CAGCGQEIKnGQALLALDKQWHVWCFKCKECGKVLTGE--YMGKDGKPYC 48
LIM2_Paxillin_like cd09337
The second LIM domain of the paxillin like protein family; The second LIM domain of the ...
501-532 8.52e-03

The second LIM domain of the paxillin like protein family; The second LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188723 [Multi-domain]  Cd Length: 52  Bit Score: 35.83  E-value: 8.52e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1959422415  501 CAACKEPIDDECIMLGESRWHlkPPHLTCAAC 532
Cdd:cd09337      1 CAYCNGPILDKCVTALDKTWH--PEHFFCAQC 30
LIM1_UF1 cd09397
LIM domain in proteins of unknown function; The first Lim domain of a LIM domain containing ...
126-157 8.80e-03

LIM domain in proteins of unknown function; The first Lim domain of a LIM domain containing protein: The functions of the proteins are unknown. The members of this family contain two copies of LIM domain. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188783 [Multi-domain]  Cd Length: 58  Bit Score: 35.70  E-value: 8.80e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1959422415  126 CKKCGEPLTGQFVR----ALGATYHLECFKCEDCGQ 157
Cdd:cd09397      1 CRKCGLEIEGKSISskdgELSGQWHRECFVCTTCGC 36
LIM_RIL cd09451
The LIM domain of RIL; The LIM domain of RIL: RIL contains an N-terminal PDZ domain, a LIM ...
190-241 9.05e-03

The LIM domain of RIL; The LIM domain of RIL: RIL contains an N-terminal PDZ domain, a LIM domain, and a short consensus C-terminal region. It is the smallest molecule in the ALP LIM domain containing protein family. RIL was identified in rat fibroblasts and in human lymphocytes. The LIM domain interacts with the AMPA glutamate receptor in dendritic spines. The consensus C-terminus interacts with PTP-BL, a submembranous protein tyrosine phosphatase and the PDZ domain is responsible to interact with alpha-actinin molecules. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188835  Cd Length: 53  Bit Score: 35.68  E-value: 9.05e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1959422415  190 CHECGGALRGSYITALDHKYHIEHFTCSVCPTVFgAQDSYYEHEGRVYCHFH 241
Cdd:cd09451      1 CTRCGNGIVGTIVKARDKLYHPECFMCDDCGLNL-KQRGYFFIDEQLYCETH 51
 
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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