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Conserved domains on  [gi|330443491|ref|NP_010041|]
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GTPase-activating protein LRG1 [Saccharomyces cerevisiae S288C]

Protein Classification

LIM domain-containing protein( domain architecture ID 10175085)

LIM (LIN-11, Isl1 and MEC-3) domain-containing protein; LIM is a small protein-protein interaction domain containing two zinc fingers; similar to Homo sapiens LIM domain only 7

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 ...
 728-959 1.18e-125

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: 380.56  E-value: 1.18e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  728 FGAPLDVLCEKWGVDSDLGVGPVKIRIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPTEAPDFSKENA 807
Cdd:cd04397     1 FGVPLEILVEKFGADSTLGVGPGKLRIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVPDLSKENP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  808 IQLSALLKKFIRELPQPILSTDLYELWIKAAKIDLEDEKQRVILLIYSLLPTYNRNLLEALLSFLHWTSSFSYIENEMGS 887
Cdd:cd04397    81 VQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSFSHIDEETGS 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 330443491  888 KMDIHNLSTVITPNILYLRHKEisndnvpdepesglvdsfaQNKGENYFLAIEIVDYLITHNEEMAMVPKFL 959
Cdd:cd04397   161 KMDIHNLATVITPNILYSKTDN-------------------PNTGDEYFLAIEAVNYLIENNEEFCEVPDEL 213
LIM1_Lrg1p_like cd09391
The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The first LIM ...
 28-90 2.15e-25

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: 99.68  E-value: 2.15e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330443491   28 CARCNKLVipdsqrTKTTLKALGKYYHESCFTCQDCQKPLKPKYFPYQVDKTSESILLCQYDY 90
Cdd:cd09391     1 CAKCGKPI------TGQFVRALGDVYHLDCFTCHDCGKPVASKFFPVDDPDTSEQVPLCETDY 57
LIM3_Lrg1p_like cd09393
The third LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The third LIM ...
 419-475 1.43e-24

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: 97.39  E-value: 1.43e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 330443491  419 CAGCNKYIQEECIQFYEHRWHIACFTCSSCHKNINPRSLTDPTFNKEkKKILCSHCS 475
Cdd:cd09393     1 CASCGKSIEDECIKFEDKRWHLKCFTCSRCHREISSELSDAAFNNKD-QRILCSNCS 56
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
 98-149 6.37e-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).


:

Pssm-ID: 259829 [Multi-domain]  Cd Length: 53  Bit Score: 58.48  E-value: 6.37e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 330443491   98 CHVCDTPLRGLYY-TAFGYRYDEEHFSCTICATPCGVKKCFMYGNQLYCKYHF 149
Cdd:cd08368     1 CAGCGKPIEGRELlRALGKKWHPECFKCAECGKPLGGDSFYEKDGKPYCEKCY 53
 
Name Accession Description Interval E-value
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 728-959 1.18e-125

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: 380.56  E-value: 1.18e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  728 FGAPLDVLCEKWGVDSDLGVGPVKIRIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPTEAPDFSKENA 807
Cdd:cd04397     1 FGVPLEILVEKFGADSTLGVGPGKLRIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVPDLSKENP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  808 IQLSALLKKFIRELPQPILSTDLYELWIKAAKIDLEDEKQRVILLIYSLLPTYNRNLLEALLSFLHWTSSFSYIENEMGS 887
Cdd:cd04397    81 VQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSFSHIDEETGS 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 330443491  888 KMDIHNLSTVITPNILYLRHKEisndnvpdepesglvdsfaQNKGENYFLAIEIVDYLITHNEEMAMVPKFL 959
Cdd:cd04397   161 KMDIHNLATVITPNILYSKTDN-------------------PNTGDEYFLAIEAVNYLIENNEEFCEVPDEL 213
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 755-907 4.68e-45

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 159.25  E-value: 4.68e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491   755 PIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPTEAPDFSKENAIQLSALLKKFIRELPQPILSTDLYELW 834
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330443491   835 IKAAKIDLEDEKQRVILLIYSLLPTYNRNLLEALLSFLHWTSSFSYIenemgSKMDIHNLSTVITPNILYLRH 907
Cdd:pfam00620   81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDV-----NKMNAHNLAIVFGPTLLRPPD 148
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 752-935 2.67e-44

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: 158.20  E-value: 2.67e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491    752 IRIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPTEAPDFSKENAIQLSALLKKFIRELPQPILSTDLY 831
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491    832 ELWIKAAKIDLEDEKQRVILLIYSLLPTYNRNLLEALLSFLHWTSsfsyiENEMGSKMDIHNLSTVITPNILYLRHKEis 911
Cdd:smart00324   81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVA-----EHSEENKMTARNLAIVFGPTLLRPPDGE-- 153

                           170       180
                    ....*....|....*....|....
gi 330443491    912 ndnVPDEPESGLVDSFAQNKGENY 935
Cdd:smart00324  154 ---VASLKDIRHQNTVIEFLIENA 174
LIM1_Lrg1p_like cd09391
The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The first LIM ...
 28-90 2.15e-25

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: 99.68  E-value: 2.15e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330443491   28 CARCNKLVipdsqrTKTTLKALGKYYHESCFTCQDCQKPLKPKYFPYQVDKTSESILLCQYDY 90
Cdd:cd09391     1 CAKCGKPI------TGQFVRALGDVYHLDCFTCHDCGKPVASKFFPVDDPDTSEQVPLCETDY 57
LIM3_Lrg1p_like cd09393
The third LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The third LIM ...
 419-475 1.43e-24

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: 97.39  E-value: 1.43e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 330443491  419 CAGCNKYIQEECIQFYEHRWHIACFTCSSCHKNINPRSLTDPTFNKEkKKILCSHCS 475
Cdd:cd09393     1 CASCGKSIEDECIKFEDKRWHLKCFTCSRCHREISSELSDAAFNNKD-QRILCSNCS 56
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
 28-94 2.51e-14

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


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 68.13  E-value: 2.51e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330443491    28 CARCNKLvIPDSQRTKttlkALGKYYHESCFTCQDCQKPLKPKYFpYQVDKTsesiLLCQYDYFRRH 94
Cdd:pfam00412    1 CAGCNRP-IYDRELVR----ALGKVWHPECFRCAVCGKPLTTGDF-YEKDGK----LYCKHDYYKLF 57
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
 419-477 6.93e-13

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


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 64.28  E-value: 6.93e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491   419 CAGCNKYIQEECI-QFYEHRWHIACFTCSSCHKNINPRSLtdptFNKEkKKILCSHCSID 477
Cdd:pfam00412    1 CAGCNRPIYDRELvRALGKVWHPECFRCAVCGKPLTTGDF----YEKD-GKLYCKHDYYK 55
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
 98-149 6.37e-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).


Pssm-ID: 259829 [Multi-domain]  Cd Length: 53  Bit Score: 58.48  E-value: 6.37e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 330443491   98 CHVCDTPLRGLYY-TAFGYRYDEEHFSCTICATPCGVKKCFMYGNQLYCKYHF 149
Cdd:cd08368     1 CAGCGKPIEGRELlRALGKKWHPECFKCAECGKPLGGDSFYEKDGKPYCEKCY 53
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
 27-89 1.20e-10

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: 57.78  E-value: 1.20e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330443491     27 ICARCNKLVIPDSQRtkttLKALGKYYHESCFTCQDCQKPLKPKYFpyqvdKTSESILLCQYD 89
Cdd:smart00132    1 KCAGCGKPIYGTERV----LRALGKVWHPECFKCATCGKPLSGDTF-----FEKDGKLYCKDC 54
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
 418-474 3.56e-10

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: 56.24  E-value: 3.56e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 330443491    418 SCAGCNKYIQ--EECIQFYEHRWHIACFTCSSCHKninprSLTDPTFNKEKKKILCSHC 474
Cdd:smart00132    1 KCAGCGKPIYgtERVLRALGKVWHPECFKCATCGK-----PLSGDTFFEKDGKLYCKDC 54
 
Name Accession Description Interval E-value
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 728-959 1.18e-125

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: 380.56  E-value: 1.18e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  728 FGAPLDVLCEKWGVDSDLGVGPVKIRIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPTEAPDFSKENA 807
Cdd:cd04397     1 FGVPLEILVEKFGADSTLGVGPGKLRIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVPDLSKENP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  808 IQLSALLKKFIRELPQPILSTDLYELWIKAAKIDLEDEKQRVILLIYSLLPTYNRNLLEALLSFLHWTSSFSYIENEMGS 887
Cdd:cd04397    81 VQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSFSHIDEETGS 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 330443491  888 KMDIHNLSTVITPNILYLRHKEisndnvpdepesglvdsfaQNKGENYFLAIEIVDYLITHNEEMAMVPKFL 959
Cdd:cd04397   161 KMDIHNLATVITPNILYSKTDN-------------------PNTGDEYFLAIEAVNYLIENNEEFCEVPDEL 213
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 755-907 4.68e-45

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 159.25  E-value: 4.68e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491   755 PIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPTEAPDFSKENAIQLSALLKKFIRELPQPILSTDLYELW 834
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330443491   835 IKAAKIDLEDEKQRVILLIYSLLPTYNRNLLEALLSFLHWTSSFSYIenemgSKMDIHNLSTVITPNILYLRH 907
Cdd:pfam00620   81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDV-----NKMNAHNLAIVFGPTLLRPPD 148
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 752-935 2.67e-44

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: 158.20  E-value: 2.67e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491    752 IRIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPTEAPDFSKENAIQLSALLKKFIRELPQPILSTDLY 831
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491    832 ELWIKAAKIDLEDEKQRVILLIYSLLPTYNRNLLEALLSFLHWTSsfsyiENEMGSKMDIHNLSTVITPNILYLRHKEis 911
Cdd:smart00324   81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVA-----EHSEENKMTARNLAIVFGPTLLRPPDGE-- 153

                           170       180
                    ....*....|....*....|....
gi 330443491    912 ndnVPDEPESGLVDSFAQNKGENY 935
Cdd:smart00324  154 ---VASLKDIRHQNTVIEFLIENA 174
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 755-948 5.96e-34

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: 128.19  E-value: 5.96e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  755 PIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNpTEAPDFSKENAIQLSALLKKFIRELPQPILSTDLYELW 834
Cdd:cd00159     1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRG-EDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  835 IKAAKIDLEDEKQRVILLIYSLLPTYNRNLLEALLSFLHWTSSFSYIenemgSKMDIHNLSTVITPNIlyLRHKEISNDN 914
Cdd:cd00159    80 IELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEV-----NKMTASNLAIVFAPTL--LRPPDSDDEL 152

                         170       180       190
                  ....*....|....*....|....*....|....
gi 330443491  915 VPDEPesglvdsfaqnkgenyfLAIEIVDYLITH 948
Cdd:cd00159   153 LEDIK-----------------KLNEIVEFLIEN 169
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 747-959 1.15e-27

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: 111.38  E-value: 1.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  747 VGPVKIRIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPTEAPDfSKENAIQLSALLKKFIRELPQPIL 826
Cdd:cd04376     2 LNPIARQVPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLD-ENHSVHDVAALLKEFFRDMPDPLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  827 STDLYELWIKAAKIDLEDEKQRVILLIYsLLPTYNRNLLEALLSFLHWTSSFSYI------ENEMGSKMDIHNLSTVITP 900
Cdd:cd04376    81 PRELYTAFIGTALLEPDEQLEALQLLIY-LLPPCNCDTLHRLLKFLHTVAEHAADsidedgQEVSGNKMTSLNLATIFGP 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 330443491  901 NILylrHKEISNDNVPDEPESGLVDSFAQnkgenyflaIEIVDYLITHNEEMAMVPKFL 959
Cdd:cd04376   160 NLL---HKQKSGEREFVQASLRIEESTAI---------INVVQTMIDNYEELFMVSPEL 206
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 727-964 1.50e-26

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: 108.59  E-value: 1.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  727 VFGAPLDVLcekwgVDSDLGVGPvKIRIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPTEApDFSKEN 806
Cdd:cd04391     1 LFGVPLSTL-----LERDQKKVP-GSKVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAKFYEG-TFLWDQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  807 AIQ--LSALLKKFIRELPQPILSTDLYELWIKAAKI-DLEDEKQRVILLIYsLLPTYNRNLLEALLSFLHwtssfSYIEN 883
Cdd:cd04391    74 VKQhdAASLLKLFIRELPQPLLTVEYLPAFYSVQGLpSKKDQLQALNLLVL-LLPEANRDTLKALLEFLQ-----KVVDH 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  884 EMGSKMDIHNLSTVITPNILYLRHKEiSNDNVPDEPESGLVDSFAQnkgenyflaieIVDYLITHNEEMAMVPKFLMNLL 963
Cdd:cd04391   148 EEKNKMNLWNVAMIMAPNLFPPRGKH-SKDNESLQEEVNMAAGCAN-----------IMRLLIRYQDLLWTVPSFLINQV 215


                  .
gi 330443491  964 K 964
Cdd:cd04391   216 R 216
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 728-905 4.58e-26

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: 106.23  E-value: 4.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  728 FGAPLDVLCEkwgvDSDLgvgpvkiriPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNptEAPDFSKENA 807
Cdd:cd04402     2 FGQPLSNICE----DDNL---------PKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSG--VEVDLKAEPV 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  808 IQLSALLKKFIRELPQPILSTDLYELWIKAAKIDLEDEKQRVILLIYSLLPTYNRNLLEALLSFLHWTSsfsyiENEMGS 887
Cdd:cd04402    67 LLLASVLKDFLRNIPGSLLSSDLYEEWMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNIS-----QNSETN 141

                         170
                  ....*....|....*...
gi 330443491  888 KMDIHNLSTVITPNILYL 905
Cdd:cd04402   142 KMDAFNLAVCIAPSLLWP 159
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 727-960 1.14e-25

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: 105.63  E-value: 1.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  727 VFGAPLDVLCEKWGvdsdlgvgPVKIRIPIIIDELISSLRQmDMSVEGIFRKNGNIRRLRELTANIDSNptEAPDfSKEN 806
Cdd:cd04394     1 VFGVPLHSLPHSTV--------PEYGNVPKFLVDACTFLLD-HLSTEGLFRKSGSVVRQKELKAKLEGG--EACL-SSAL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  807 AIQLSALLKKFIRELPQPILSTDLYELWIKAAKIDLEDEKQRVILLIYSLLPTYNRNLLEALLSFLHWTSSFSyIENemg 886
Cdd:cd04394    69 PCDVAGLLKQFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRC-SEN--- 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330443491  887 sKMDIHNLSTVITPNILylrhkeisndnvpdePESGLVDSFAQNKGENYFLAIEIVDYLITHNEEMAMVPKFLM 960
Cdd:cd04394   145 -KMDSSNLAVIFAPNLF---------------QSEEGGEKMSSSTEKRLRLQAAVVQTLIDNASNIGIVPDFIL 202
LIM1_Lrg1p_like cd09391
The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The first LIM ...
 28-90 2.15e-25

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: 99.68  E-value: 2.15e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330443491   28 CARCNKLVipdsqrTKTTLKALGKYYHESCFTCQDCQKPLKPKYFPYQVDKTSESILLCQYDY 90
Cdd:cd09391     1 CAKCGKPI------TGQFVRALGDVYHLDCFTCHDCGKPVASKFFPVDDPDTSEQVPLCETDY 57
LIM3_Lrg1p_like cd09393
The third LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The third LIM ...
 419-475 1.43e-24

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: 97.39  E-value: 1.43e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 330443491  419 CAGCNKYIQEECIQFYEHRWHIACFTCSSCHKNINPRSLTDPTFNKEkKKILCSHCS 475
Cdd:cd09393     1 CASCGKSIEDECIKFEDKRWHLKCFTCSRCHREISSELSDAAFNNKD-QRILCSNCS 56
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 728-911 3.33e-23

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: 98.18  E-value: 3.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  728 FGAPLDVLCEKwgvdsdlgvGPVKIRIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIdsNPTEAPDFSKENA 807
Cdd:cd04404     6 FGVSLQFLKEK---------NPEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKY--NMGEPVDFDQYED 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  808 IQLSA-LLKKFIRELPQPILSTDLYELWIKAAKIDlEDEKQRVILLIYSLLPTYNRNLLEALLSFLHWTSSFSyIENEMG 886
Cdd:cd04404    75 VHLPAvILKTFLRELPEPLLTFDLYDDIVGFLNVD-KEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHS-DQNKMT 152

                         170       180
                  ....*....|....*....|....*
gi 330443491  887 SKmdihNLSTVITPNILYLRHKEIS 911
Cdd:cd04404   153 NS----NLAVVFGPNLLWAKDASMS 173
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 725-906 6.75e-21

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: 91.75  E-value: 6.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  725 KTVFGAPLDvlcekwgvdSDLGVgpVKIRIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSN---PTEAPD 801
Cdd:cd04386     2 KPVFGTPLE---------EHLKR--TGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGtfsLPLDEF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  802 FSKENAIqlSALLKKFIRELPQPILSTDLYELWIKAAKIDLEDEKQRVILLIYSLLPTYNRNLLEALLSFLhwtssfSYI 881
Cdd:cd04386    71 YSDPHAV--ASALKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFL------SKL 142

                         170       180
                  ....*....|....*....|....*.
gi 330443491  882 ENEMG-SKMDIHNLSTVITPNILYLR 906
Cdd:cd04386   143 AQKSDeNKMSPSNIAIVLAPNLLWAK 168
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 728-903 3.75e-19

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: 86.34  E-value: 3.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  728 FGAPLDVLcekwgVDSDLGVgpvkiriPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPtEAPDFSKENA 807
Cdd:cd04377     1 FGVSLSSL-----TSEDRSV-------PLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDP-DSVNLEDYPI 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  808 IQLSALLKKFIRELPQPILSTDLYELWIKAakIDLEDEKQRV--ILLIYSLLPTYNRNLLEALLSFLHWTSsfsyiENEM 885
Cdd:cd04377    68 HVITSVLKQWLRELPEPLMTFELYENFLRA--MELEEKQERVraLYSVLEQLPRANLNTLERLIFHLVRVA-----LQEE 140

                         170
                  ....*....|....*...
gi 330443491  886 GSKMDIHNLSTVITPNIL 903
Cdd:cd04377   141 VNRMSANALAIVFAPCIL 158
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 754-903 6.25e-19

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: 85.44  E-value: 6.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  754 IPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNP-TEAPDFSKENAIQLSALLKKFIRELPQPILSTDLYE 832
Cdd:cd04385    15 IPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDArSVQLREGEYTVHDVADVLKRFLRDLPDPLLTSELHA 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 330443491  833 LWIKAAKIDLEDEK-QRVILLIySLLPTYNRNLLEALLSFLHWTSSFSYiENemgsKMDIHNLSTVITPNIL 903
Cdd:cd04385    95 EWIEAAELENKDERiARYKELI-RRLPPINRATLKVLIGHLYRVQKHSD-EN----QMSVHNLALVFGPTLF 160
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 728-902 6.32e-18

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: 82.48  E-value: 6.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  728 FGAPLDVLCEKwgvdSDLGVGpvkIRIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNptEAPDFSKENA 807
Cdd:cd04381     1 FGASLSLAVER----SRCHDG---IDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRR--ESPNLEEYEP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  808 IQLSALLKKFIRELPQPILSTDLYELWIKAAKIDLEDEKQRVILLIYSLLPTYNRNLLEALLSFLHwtssfSYIENEMGS 887
Cdd:cd04381    72 PTVASLLKQYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMD-----HVIAQELET 146

                         170
                  ....*....|....*
gi 330443491  888 KMDIHNLSTVITPNI 902
Cdd:cd04381   147 KMNIQNISIVLSPTV 161
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 725-957 2.82e-17

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: 81.70  E-value: 2.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  725 KTVFGAPLDVLCEKWGVDsdlgvgpvkirIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPTEApDFSK 804
Cdd:cd04375     2 KNVFGVPLLVNLQRTGQP-----------LPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNV-NYDG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  805 ENAIQLSALLKKFIRELPQPILSTDLYELWIKAAKIDLEDEKQRVILLIYSLLPTYNRNLLEALLSFLHWTSSFSYiENE 884
Cdd:cd04375    70 QQAYDVADMLKQYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQ-ENQ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  885 MGSKmdihNLSTVITPNILYL------------RHKEISNDNVPDEPEsglvdsFAQNKGENYFLAieivdYLITHNEEM 952
Cdd:cd04375   149 MTAT----NLAVCLAPSLFHLntsrrenssparRMQRKKSLGKPDQKE------LSENKAAHQCLA-----YMIEECNTL 213


                  ....*
gi 330443491  953 AMVPK 957
Cdd:cd04375   214 FMVPK 218
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 728-903 1.30e-16

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: 78.98  E-value: 1.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  728 FGAPLDVLCEKWGVDsdlgvgpvkirIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPT-----EAPDF 802
Cdd:cd04398     1 FGVPLEDLILREGDN-----------VPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLnvlliSPEDY 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  803 skENAIQLSA-LLKKFIRELPQPILSTDLYELWIKAAKIdlEDEKQRVILL---IYSlLPTYNRNLLEALLSFLHwtssf 878
Cdd:cd04398    70 --ESDIHSVAsLLKLFFRELPEPLLTKALSREFIEAAKI--EDESRRRDALhglIND-LPDANYATLRALMFHLA----- 139

                         170       180
                  ....*....|....*....|....*
gi 330443491  879 SYIENEMGSKMDIHNLSTVITPNIL 903
Cdd:cd04398   140 RIKEHESVNRMSVNNLAIIWGPTLM 164
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 754-903 1.45e-16

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: 79.02  E-value: 1.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  754 IPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNptEAPDFSKENAIQLSA-LLKKFIRELPQPILSTDLYE 832
Cdd:cd04390    22 VPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAG--ERPSFDSDTDVHTVAsLLKLYLRELPEPVIPWAQYE 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330443491  833 LWIKAAKIDLEDEKQRVILLI--YSLLPTYNRNLLEALLSFLHWTSSFSYIenemgSKMDIHNLSTVITPNIL 903
Cdd:cd04390   100 DFLSCAQLLSKDEEKGLGELMkqVSILPKVNYNLLSYICRFLDEVQSNSSV-----NKMSVQNLATVFGPNIL 167
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 728-946 3.38e-16

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: 78.28  E-value: 3.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  728 FGAPLDVLCEKwgvdsdlgvGPVKIRIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPTeAPDFSKE-- 805
Cdd:cd04379     1 FGVPLSRLVER---------EGESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSA-AVELSEEly 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  806 ---NAIqlSALLKKFIRELPQPILSTDLYELWIKAAKIDLEDEKQ---RVILLIYSLLPTYNRNLLEALLSFLHWTSSFS 879
Cdd:cd04379    71 pdiNVI--TGVLKDYLRELPEPLITPQLYEMVLEALAVALPNDVQtntHLTLSIIDCLPLSAKATLLLLLDHLSLVLSNS 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330443491  880 yieneMGSKMDIHNLSTVITPnILYLRHKEISNDNVPDEPESGLVDSFAQNKgenyflAIEIVDYLI 946
Cdd:cd04379   149 -----ERNKMTPQNLAVCFGP-VLMFCSQEFSRYGISPTSKMAAVSTVDFKQ------HIEVLHYLL 203
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 758-959 4.03e-16

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: 78.27  E-value: 4.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  758 IDELISSLRQmDMSVEGIFRKNGNIRRLRELTANIDSN---PTEAPDFSKENaiqLSALLKKFIRELPQPILSTDLYELW 834
Cdd:cd04392    13 IYQLIEYLEK-NLRVEGLFRKPGNSARQQELRDLLNSGtdlDLESGGFHAHD---CATVLKGFLGELPEPLLTHAHYPAH 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  835 IKAAKIDLEDEKQR------------VILLIYSLLPTYNRNLLEALLSFLHWTSSFsyienEMGSKMDIHNLSTVITPNI 902
Cdd:cd04392    89 LQIADLCQFDEKGNktsapdkerlleALQLLLLLLPEENRNLLKLILDLLYQTAKH-----EDKNKMSADNLALLFTPHL 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 330443491  903 LYLRhkeisndNVPDEpesglvDSFAQNKGENyflaiEIVDYLITHNEEMAMVPKFL 959
Cdd:cd04392   164 ICPR-------NLTPE------DLHENAQKLN-----SIVTFMIKHSQKLFKAPAYL 202
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 753-903 3.18e-15

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: 75.12  E-value: 3.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  753 RIPIIIDELISSLRQMDMSV-EGIFRKNGNIRRLRELTANIDSnpTEAPDFSKENAIQLSALLKKFIRELPQPILSTDLY 831
Cdd:cd04389    20 KLPWILTFLSEKVLALGGFQtEGIFRVPGDIDEVNELKLRVDQ--WDYPLSGLEDPHVPASLLKLWLRELEEPLIPDALY 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 330443491  832 ELWIKAAkidledEKQRVILLIYSLLPTYNRNLLEALLSFLHwtsSFSYIENEMGSKMDIHNLSTVITPNIL 903
Cdd:cd04389    98 QQCISAS------EDPDKAVEIVQKLPIINRLVLCYLINFLQ---VFAQPENVAHTKMDVSNLAMVFAPNIL 160
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 727-906 9.70e-15

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: 73.65  E-value: 9.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  727 VFGAPLDVLCEKwgvdsdlgvGPVKIRIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNptEAPDFSKEN 806
Cdd:cd04393     2 VFGVPLQELQQA---------GQPENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSG--EEVDLSKEA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  807 AIQLSA-LLKKFIRELPQPILSTDLYELWIKA-AKIDLEDEKQRVILLIYSLLPTYNRNLLEALLSFLHWTSSFSYIEne 884
Cdd:cd04393    71 DVCSAAsLLRLFLQELPEGLIPASLQIRLMQLyQDYNGEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHEN-- 148

                         170       180
                  ....*....|....*....|..
gi 330443491  885 mgsKMDIHNLSTVITPNILYLR 906
Cdd:cd04393   149 ---RMTAENLAAVFGPDVFHVY 167
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
 28-94 2.51e-14

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


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 68.13  E-value: 2.51e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330443491    28 CARCNKLvIPDSQRTKttlkALGKYYHESCFTCQDCQKPLKPKYFpYQVDKTsesiLLCQYDYFRRH 94
Cdd:pfam00412    1 CAGCNRP-IYDRELVR----ALGKVWHPECFRCAVCGKPLTTGDF-YEKDGK----LYCKHDYYKLF 57
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 772-912 1.76e-13

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: 70.22  E-value: 1.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  772 VEGIFRKNG---NIRRLReltANIDSNptEAPDFSKENAIQ----LSALLKKFIRELPQPILSTDLYELWIKAAKIDLED 844
Cdd:cd04384    35 VDGIYRLSGiasNIQRLR---HEFDSE--QIPDLTKDVYIQdihsVSSLCKLYFRELPNPLLTYQLYEKFSEAVSAASDE 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330443491  845 EKQRVILLIYSLLPTYNRNLLEALLSFLHWTSSFSYIENeMGSKmdihNLSTVITPNIlyLRHKEISN 912
Cdd:cd04384   110 ERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITN-MHAK----NLAIVWAPNL--LRSKQIES 170
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 751-903 3.67e-13

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: 68.87  E-value: 3.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  751 KIRIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPtEAPDFSKENAIQLSALLKKFIRELPQPILSTDL 830
Cdd:cd04407    12 KTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADP-ENVKLENYPIHAITGLLKQWLRELPEPLMTFAQ 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330443491  831 YELWIKAAKIdleDEKQRVILLIYSL---LPTYNRNLLEALLSFLhwtSSFSYIENEmgSKMDIHNLSTVITPNIL 903
Cdd:cd04407    91 YNDFLRAVEL---PEKQEQLQAIYRVleqLPTANHNTLERLIFHL---VKVALEEDV--NRMSPNALAIVFAPCLL 158
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 754-948 4.59e-13

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: 68.99  E-value: 4.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  754 IPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDsNPTEAPDFSKENAIQLSALLKKFIRELPQPILSTDLYEL 833
Cdd:cd04378    16 VPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFE-NGKDLVELSELSPHDISSVLKLFLRQLPEPLILFRLYND 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  834 WIKAAK-----------IDLEDEKQRVILLIYSL---LPTYNRNLLEALLSFLHWTSsfsyiENEMGSKMDIHNLSTVIT 899
Cdd:cd04378    95 FIALAKeiqrdteedkaPNTPIEVNRIIRKLKDLlrqLPASNYNTLQHLIAHLYRVA-----EQFEENKMSPNNLGIVFG 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 330443491  900 PNILYLRHKEisndnvPDEPESGLVDSFAQNKgenyflaieIVDYLITH 948
Cdd:cd04378   170 PTLIRPRPGD------ADVSLSSLVDYGYQAR---------LVEFLITN 203
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
 419-477 6.93e-13

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


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 64.28  E-value: 6.93e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491   419 CAGCNKYIQEECI-QFYEHRWHIACFTCSSCHKNINPRSLtdptFNKEkKKILCSHCSID 477
Cdd:pfam00412    1 CAGCNRPIYDRELvRALGKVWHPECFRCAVCGKPLTTGDF----YEKD-GKLYCKHDYYK 55
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 751-903 6.66e-12

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: 65.72  E-value: 6.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  751 KIRIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPTEAPDFSKE---NAIqlSALLKKFIRELPQPILS 827
Cdd:cd04387    13 RSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMLSEmdvNAI--AGTLKLYFRELPEPLFT 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330443491  828 TDLYELWIKAakIDLEDE--KQRVILLIYSLLPTYNRNLLEALLSFLHWTSsfsyiENEMGSKMDIHNLSTVITPNIL 903
Cdd:cd04387    91 DELYPNFAEG--IALSDPvaKESCMLNLLLSLPDPNLVTFLFLLHHLKRVA-----EREEVNKMSLHNLATVFGPTLL 161
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 754-903 2.27e-11

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: 63.87  E-value: 2.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  754 IPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNpTEAPDFSKENAIQLSALLKKFIRELPQPILSTDLYEL 833
Cdd:cd04406    15 VPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTD-ANSVNLDDYNIHVIASVFKQWLRDLPNPLMTFELYEE 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  834 WIKAAKIdleDEKQRVILLIYSLLPTYNRNLLEALLSFLHWTSSFSYieNEMGSKMDIHNLSTVITPNIL 903
Cdd:cd04406    94 FLRAMGL---QERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIAL--QEETNRMSANALAIVFAPCIL 158
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 727-950 2.50e-11

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: 63.96  E-value: 2.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  727 VFGAPLDvlcekwgvdsDLGVGPVKIRIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPTEAP--DFSK 804
Cdd:cd04395     1 TFGVPLD----------DCPPSSENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGFDIDlqDPRW 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  805 ENAIQLSALLKKFIRELPQPILSTDLYELWIKAAKIdlEDEKQRVILL--IYSLLPTYNRNLLEALLSFLHWTSsfsyiE 882
Cdd:cd04395    71 RDVNVVSSLLKSFFRKLPEPLFTNELYPDFIEANRI--EDPVERLKELrrLIHSLPDHHYETLKHLIRHLKTVA-----D 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330443491  883 NEMGSKMDIHNLSTVITPNILylrhkEISNDNVpdepESGLVDSFAQNKgenyflaieIVDYLITHNE 950
Cdd:cd04395   144 NSEVNKMEPRNLAIVFGPTLV-----RTSDDNM----ETMVTHMPDQCK---------IVETLIQHYD 193
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
 98-149 6.37e-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).


Pssm-ID: 259829 [Multi-domain]  Cd Length: 53  Bit Score: 58.48  E-value: 6.37e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 330443491   98 CHVCDTPLRGLYY-TAFGYRYDEEHFSCTICATPCGVKKCFMYGNQLYCKYHF 149
Cdd:cd08368     1 CAGCGKPIEGRELlRALGKKWHPECFKCAECGKPLGGDSFYEKDGKPYCEKCY 53
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 753-903 7.84e-11

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: 62.53  E-value: 7.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  753 RIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPTEApDFSKE---NAIQLSALLKKFIRELPQPILSTD 829
Cdd:cd04372    15 QRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKA-DISATvypDINVITGALKLYFRDLPIPVITYD 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330443491  830 LYELWIKAAKIDLEDEKQRVILLIYSLLPTYNRNLLEALLSFLHWTSSfsyieNEMGSKMDIHNLSTVITPNIL 903
Cdd:cd04372    94 TYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTL-----HEKDNKMNAENLGIVFGPTLM 162
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
 27-89 1.20e-10

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: 57.78  E-value: 1.20e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330443491     27 ICARCNKLVIPDSQRtkttLKALGKYYHESCFTCQDCQKPLKPKYFpyqvdKTSESILLCQYD 89
Cdd:smart00132    1 KCAGCGKPIYGTERV----LRALGKVWHPECFKCATCGKPLSGDTF-----FEKDGKLYCKDC 54
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
 28-90 1.54e-10

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: 57.33  E-value: 1.54e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330443491   28 CARCNKLVIPdsqrtKTTLKALGKYYHESCFTCQDCQKPLKPKYFpYQVDKTsesiLLCQYDY 90
Cdd:cd08368     1 CAGCGKPIEG-----RELLRALGKKWHPECFKCAECGKPLGGDSF-YEKDGK----PYCEKCY 53
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
 419-474 1.54e-10

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: 57.33  E-value: 1.54e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 330443491  419 CAGCNKYIQEECIQFY-EHRWHIACFTCSSCHKNinprsLTDPTFNKEKKKILCSHC 474
Cdd:cd08368     1 CAGCGKPIEGRELLRAlGKKWHPECFKCAECGKP-----LGGDSFYEKDGKPYCEKC 52
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 753-902 2.03e-10

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: 61.16  E-value: 2.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  753 RIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPTeAPDFSKENAIQLSALLKKFIRELPQPILSTDLYE 832
Cdd:cd04382    16 MIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKT-VPNLSKVDIHVICGCLKDFLRSLKEPLITFALWK 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  833 LWIKAAKIDLEDEKQRVILLIYSLLPTYNRNLLeALLsFLHWTSSFSYIENemgsKMDIHNLSTVITPNI 902
Cdd:cd04382    95 EFMEAAEILDEDNSRAALYQAISELPQPNRDTL-AFL-ILHLQRVAQSPEC----KMDINNLARVFGPTI 158
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
 773-902 2.10e-10

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: 61.22  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  773 EGIFRKNGN---IRRLRE-LTANIDSNPTEAPDFSKENAIqlSALLKKFIRELPQPILSTDLYELWIKAAKIdLEDEKQR 848
Cdd:cd04400    42 EGIFRLSGSasvIKQLKErFNTEYDVDLFSSSLYPDVHTV--AGLLKLYLRELPTLILGGELHNDFKRLVEE-NHDRSQR 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 330443491  849 VILL--IYSLLPTYNRNLLEALLSFLHwtssfSYIENEMGSKMDIHNLSTVITP--NI 902
Cdd:cd04400   119 ALELkdLVSQLPQANYDLLYVLFSFLR-----KIIEHSDVNKMNLRNVCIVFSPtlNI 171
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
 418-474 3.56e-10

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: 56.24  E-value: 3.56e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 330443491    418 SCAGCNKYIQ--EECIQFYEHRWHIACFTCSSCHKninprSLTDPTFNKEKKKILCSHC 474
Cdd:smart00132    1 KCAGCGKPIYgtERVLRALGKVWHPECFKCATCGK-----PLSGDTFFEKDGKLYCKDC 54
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 728-916 1.15e-09

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: 58.94  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  728 FGAPLDVLCEKWGVdsdlgvgpvkiRIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPTEAPDFSKENA 807
Cdd:cd04403     1 FGCHLEALCQRENS-----------TVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEKLDLDDSKWED 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  808 IQ-LSALLKKFIRELPQPILSTDLYELWIKAakIDLEDEKQRV--ILLIYSLLPTYNRNLLEALLSFLHwtssfSYIENE 884
Cdd:cd04403    70 IHvITGALKLFFRELPEPLFPYSLFNDFVAA--IKLSDYEQRVsaVKDLIKSLPKPNHDTLKMLFRHLC-----RVIEHG 142

                         170       180       190
                  ....*....|....*....|....*....|..
gi 330443491  885 MGSKMDIHNLSTVITPNILylrHKEISNDNVP 916
Cdd:cd04403   143 EKNRMTTQNLAIVFGPTLL---RPEQETGNIA 171
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 754-909 1.31e-09

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: 59.05  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  754 IPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDsNPTEAPDFSKENAIQLSALLKKFIRELPQPILSTDLYEL 833
Cdd:cd04409    16 IPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFE-NGKDLVELSELSPHDISNVLKLYLRQLPEPLILFRLYNE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  834 WIKAAK-------------------IDLEDEKQRVILLIYSL---LPTYNRNLLEALLSFLHWTSsfsyiENEMGSKMDI 891
Cdd:cd04409    95 FIGLAKesqhvnetqeakknsdkkwPNMCTELNRILLKSKDLlrqLPAPNYNTLQFLIVHLHRVS-----EQAEENKMSA 169

                         170
                  ....*....|....*...
gi 330443491  892 HNLSTVITPNILYLRHKE 909
Cdd:cd04409   170 SNLGIIFGPTLIRPRPTD 187
LIM2_Lrg1p_like cd09392
The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The second LIM ...
 98-149 1.84e-09

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: 54.29  E-value: 1.84e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 330443491   98 CHVCDTPLRGLYYTAFGYRYDEEHFSCTICATPCGVKKCFM-YGNQLYCKYHF 149
Cdd:cd09392     1 CFKCGGALRGSYITALGRKYHVEHFTCSVCPTVFGPNDSYYeHEGKIYCHYHY 53
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 727-903 4.21e-09

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: 57.81  E-value: 4.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  727 VFGAPLD----VLCEKWGVDSDLGVGPVKIRIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPTEAPDF 802
Cdd:cd04396     1 VFGVSLEeslkYASVAISIVDEDGEQYVYGYIPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPDYGKSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  803 --SKENAIQLSALLKKFIRELPQPILSTDLYE-------------LWIKAAKIDLEDEKQRVILLIY----SLLPTYNRN 863
Cdd:cd04396    81 dwDGYTVHDAASVLRRYLNNLPEPLVPLDLYEefrnplrkrprilQYMKGRINEPLNTDIDQAIKEYrdliTRLPNLNRQ 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 330443491  864 LLEALLSFLHWTSSFSYiENEMGSKmdihNLSTVITPNIL 903
Cdd:cd04396   161 LLLYLLDLLAVFARNSD-KNLMTAS----NLAAIFQPGIL 195
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 754-948 1.06e-08

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: 56.36  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  754 IPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDsNPTEAPDFSKENAIQLSALLKKFIRELPQPILSTDLYEL 833
Cdd:cd04408    16 VPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFE-NGRDLVDLSGHSPHDITSVLKHFLKELPEPVLPFQLYDD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  834 WIKAAKIDLEDEKQRVIL------LIYSL------LPTYNRNLLEALLSFLHWTSsfsyiENEMGSKMDIHNLSTVITPN 901
Cdd:cd04408    95 FIALAKELQRDSEKAAESpsivenIIRSLkellgrLPVSNYNTLRHLMAHLYRVA-----ERFEDNKMSPNNLGIVFGPT 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 330443491  902 ILylrhKEISNdnvPDEPESGLVDSFAQNkgenyflaiEIVDYLITH 948
Cdd:cd04408   170 LL----RPLVG---GDVSMICLLDTGYQA---------QLVEFLISN 200
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 754-903 4.78e-08

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: 54.00  E-value: 4.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  754 IPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNpTEAPDFSKENAIQLSA-LLKKFIRELPQPILSTDLYE 832
Cdd:cd04373    15 IPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQD-HNLDLVSKDFTVNAVAgALKSFFSELPDPLIPYSMHL 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330443491  833 LWIKAAKIDleDEKQRVILL--IYSLLPTYNRNLLEALLSFLHWTSSFSYIeNEMGSKmdihNLSTVITPNIL 903
Cdd:cd04373    94 ELVEAAKIN--DREQRLHALkeLLKKFPPENFDVFKYVITHLNKVSQNSKV-NLMTSE----NLSICFWPTLM 159
LIM2_abLIM cd09328
The second LIM domain on actin binding LIM (abLIM) proteins; The second LIM domain of actin ...
 419-475 3.98e-07

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: 47.73  E-value: 3.98e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 330443491  419 CAGCNKYIQEECIQFYEHRWHIACFTCSSCHKNINPRSLTdpTFNkeKKKILCSHCS 475
Cdd:cd09328     4 CDSCQDFVEGEVVSALGKTYHPKCFVCSVCRQPFPPGDRV--TFN--GKECLCQKCS 56
LIM2_FHL cd09345
The second LIM domain of Four and a half LIM domains protein (FHL); The second LIM domain of ...
 28-72 5.12e-07

The second LIM domain of Four and a half LIM domains protein (FHL); The second 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 int eracts 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: 188731 [Multi-domain]  Cd Length: 54  Bit Score: 47.29  E-value: 5.12e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 330443491   28 CARCNKLVIPDSQRtkttLKALGKYYHESCFTCQDCQKPLKPKYF 72
Cdd:cd09345     1 CKACGKAIMPGSKK----MEYKGKFWHEKCFTCSECKKPIGTKSF 41
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 754-903 7.94e-07

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: 50.50  E-value: 7.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  754 IPIIIDELISSLRQMDMSVEGIFRKNGN---IRRLRELTANIDSNPTEAPDFSKENAIqlSALLKKFIRELPQPILSTDL 830
Cdd:cd04383    18 IPLVVESCIRFINLYGLQHQGIFRVSGSqveVNDIKNAFERGEDPLADDQNDHDINSV--AGVLKLYFRGLENPLFPKER 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330443491  831 YELWIKAAKIDLEDEKQRVILLIYSLLPTYNRNLLEALLSFLHWTSSFSyiENEMgskMDIHNLSTVITPNIL 903
Cdd:cd04383    96 FEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFS--DENM---MDPYNLAICFGPTLM 163
LIM4_FHL cd09347
The fourth LIM domain of Four and a half LIM domains protein (FHL); The fourth LIM domain of ...
 419-474 2.24e-06

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: 45.80  E-value: 2.24e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  419 CAGCNKYI--QEEC--IQFYEHRWHIACFTCSSCHKninprSLTDPTFNKEKKKILCSHC 474
Cdd:cd09347     1 CAACTKPItgLGGAkfISFEERQWHSDCFNCGKCSV-----SLVGQGFLTQRDEILCPEC 55
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
 757-909 2.68e-06

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: 49.31  E-value: 2.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  757 IIDELISSLRQMDMSVEGIFRKNG-NIRRLRELTANID---SNPTEAPDFSKENAIQ-LSALLKKFIRELPQPILSTDLY 831
Cdd:cd04374    31 FVRKCIEAVETRGINEQGLYRVVGvNSKVQKLLSLGLDpktSTPGDVDLDNSEWEIKtITSALKTYLRNLPEPLMTYELH 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  832 ELWIKAAKidLEDEKQRVI---LLIYSlLPTYNRNLLEALLSFLHWTSSFSYiENemgsKMDIHNLSTVITPNIlyLRHK 908
Cdd:cd04374   111 NDFINAAK--SENLESRVNaihSLVHK-LPEKNREMLELLIKHLTNVSDHSK-KN----LMTVSNLGVVFGPTL--LRPQ 180


                  .
gi 330443491  909 E 909
Cdd:cd04374   181 E 181
LIM4_FHL3 cd09434
The fourth LIM domain of Four and a half LIM domains protein 3 (FHL3); The fourth LIM domain ...
 419-475 2.87e-06

The fourth LIM domain of Four and a half LIM domains protein 3 (FHL3); The fourth LIM domain of Four and a half LIM domains protein 3 (FHL3): FHL3 is highly expressed in the skeleton and cardiac muscles and possesses the transactivation and repression activities. FHL3 interacts with many transcription factors, such as CREB, BKLF/KLF3, CtBP2, MyoD, and MZF_1. Moreover, FHL3 interacts with alpha- and beta-subunits of the muscle alpha7beta1 integrin receptor. FHL3 was also proved to possess the auto-activation ability and was confirmed that the second zinc finger motif in fourth LIM domain was responsible for the auto-activation of FHL3. 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: 188818  Cd Length: 56  Bit Score: 45.52  E-value: 2.87e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 330443491  419 CAGCNKYI----QEECIQFYEHRWHIACFTCSSCHKninprSLTDPTFNKEKKKILCSHCS 475
Cdd:cd09434     1 CAACNKPItgfgGGKYVSFEDRQWHQPCFKCSRCSV-----SLVGAGFFPDGDQILCRDCN 56
LIM2_FHL5 cd09428
The second LIM domain of Four and a half LIM domains protein 5 (FHL5); The second LIM domain ...
 28-70 6.63e-06

The second LIM domain of Four and a half LIM domains protein 5 (FHL5); The second LIM domain of Four and a half LIM domains protein 5 (FHL5): FHL5 is a tissue-specific coactivator of CREB/CREM family transcription factors , which are highly expressed in male germ cells and is required for post-meiotic gene expression. FHL5 associates with CREM and confers a powerful transcriptional activation function. Activation by CREB has known to occur upon phosphorylation at an essential regulatory site and the subsequent interaction with the ubiquitous coactivator CREB-binding protein (CBP). However, the activation by FHL5 is independent of phosphorylation and CBP association. It represents a new route for transcriptional activation by CREM and CREB. 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: 188812  Cd Length: 54  Bit Score: 44.45  E-value: 6.63e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 330443491   28 CARCNKLVIPDSQRtkttLKALGKYYHESCFTCQDCQKPLKPK 70
Cdd:cd09428     1 CFHCKKTIMPGSRK----LEFEGNEWHETCFVCQSCQQPIGTK 39
LIM1_Rga cd09394
The first LIM domain of Rga GTPase-Activating Proteins; The first LIM domain of Rga ...
 419-475 7.22e-06

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: 44.27  E-value: 7.22e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 330443491  419 CAGCNKYIQEE-CIQFYEHRWHIACFTCSSCHKNINprslTDPTF-NKEKKKILCSHCS 475
Cdd:cd09394     1 CVGCKESITEGhAYELGGDRWHIHCFKCYKCDKKLS----CDSNFlVLGDGSLICSDCS 55
LIM2_FHL2 cd09426
The second LIM domain of Four and a half LIM domains protein 2 (FHL2); The second LIM domain ...
 28-72 8.81e-06

The second LIM domain of Four and a half LIM domains protein 2 (FHL2); The second LIM domain of Four and a half LIM domains protein 2 (FHL2): FHL2 is one of the best studied FHL proteins. FHL2 expression is most abundant in the heart, and in brain, liver and lung to a lesser extent. FHL2 participates in a wide range of cellular processes, such as transcriptional regulation, signal transduction, and cell survival by binding to various protein partners. 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. Although FHL2 is abundantly expressed in heart, the fhl2 null mice are viable and had no detectable abnormal cardiac phenotype. 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 s upport the assembly of multimeric protein complexes.


Pssm-ID: 188810  Cd Length: 57  Bit Score: 43.88  E-value: 8.81e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 330443491   28 CARCNKLVIPDSQRtkttLKALGKYYHESCFTCQDCQKPLKPKYF 72
Cdd:cd09426     1 CSECKKTIMPGTRK----MEYKGNSWHETCFICQRCQQPIGTKSF 41
LIM2_Zyxin cd09353
The second LIM domain of Zyxin; The second LIM domain of Zyxin: Zyxin exhibits three copies of ...
 28-94 8.93e-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: 44.15  E-value: 8.93e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330443491   28 CARCNKLVipdsqrTKTTLKALGKYYHESCFTCQDCQKPLKPKyfPYQVDKTSESilLCQYDYFRRH 94
Cdd:cd09353     1 CAVCDQKI------TDRMLKATGKSYHPQCFTCVVCKCPLEGE--SFIVDQANQP--HCVNDYHRRY 57
LIM1_abLIM cd09327
The first LIM domain of actin binding LIM (abLIM) proteins; The first LIM domain of actin ...
 28-90 9.57e-06

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: 43.78  E-value: 9.57e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330443491   28 CARCNKLVIpdsqrtKTTLKALGKYYHESCFTCQDCQKPLKPKYFpyqvdKTSESILLCQYDY 90
Cdd:cd09327     1 CYKCGKKCK------GEVLRVQDKYFHIKCFTCKVCGCDLAQGGF-----FVKEGEYYCTDDY 52
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 726-909 1.12e-05

RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in OCRL1-like proteins. OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins contain two conserved domains: a central inositol polyphosphate 5-phosphatase domain and a C-terminal Rho GAP domain, this GAP domain lacks the catalytic residue and therefore maybe inactive. OCRL-like proteins are type II inositol polyphosphate 5-phosphatases that can hydrolyze lipid PI(4,5)P2 and PI(3,4,5)P3 and soluble Ins(1,4,5)P3 and Ins(1,3,4,5)P4, but their individual specificities vary. The functionality of the RhoGAP domain is still unclear. 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: 239845  Cd Length: 220  Bit Score: 47.72  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  726 TVFGAPLDVLC-----------EKWGVDSDLGVGPVKIRIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANI-D 793
Cdd:cd04380    11 SCFGSSLETLIrlpdpgirnliDQLELGDNPDYSEVPLSIPKEIWRLVDYLYTRGLAQEGLFEEPGLPSEPGELLAEIrD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  794 SNPTEAPDFSKENA-IQLSALLKkFIRELPQPILSTDLYELWIKAAKIDLEDEKQrvilLIYSLLPTYNRNLLEALLSFL 872
Cdd:cd04380    91 ALDTGSPFNSPGSAeSVAEALLL-FLESLPDPIIPYSLYERLLEAVANNEEDKRQ----VIRISLPPVHRNVFVYLCSFL 165

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 330443491  873 HWTssFSYIENemgSKMDIHNLSTVITPniLYLRHKE 909
Cdd:cd04380   166 REL--LSESAD---RGLDENTLATIFGR--VLLRDPP 195
LIM3_FHL1 cd09429
The third LIM domain of Four and a half LIM domains protein 1 (FHL1); The third LIM domain of ...
 419-474 1.88e-05

The third LIM domain of Four and a half LIM domains protein 1 (FHL1); The third LIM domain of Four and a half LIM domains protein 1 (FHL1): FHL1 is heavily expressed in skeletal and cardiac muscles. It plays important roles in muscle growth, differentiation, and sarcomere assembly by acting as a modulator of transcription factors. Defects in FHL1 gene are responsible for a number of Muscular dystrophy-like muscle disorders. It has been detected that FHL1 binds to Myosin-binding protein C, regulating myosin filament formation and sarcomere assembly. 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: 188813  Cd Length: 53  Bit Score: 42.88  E-value: 1.88e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 330443491  419 CAGCNKYIQEECIQFYEHRWHIACFTCSSCHKninprSLTDPTFNKEKKKILCSHC 474
Cdd:cd09429     1 CVKCNKPITSGGVTYQDQPWHSECFVCSSCSK-----KLAGQRFTAVEDQYYCVDC 51
LIM1_FHL cd09343
The first LIM domain of Four and a half LIM domains protein (FHL); The first LIM domain of ...
 419-474 2.28e-05

The first LIM domain of Four and a half LIM domains protein (FHL); The first 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 int eracts 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: 188729  Cd Length: 59  Bit Score: 42.81  E-value: 2.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 330443491  419 CAGCNKYIQEECIQ-FYEHR-WHIACFTCSSCHkninpRSLTDPTFNKEKKKILCSHC 474
Cdd:cd09343     5 CEECKKKIGCDSKDlSYKDRhWHEGCFKCFKCQ-----RSLVDKPFAAKDEDLLCTEC 57
LIM1_Paxillin_like cd09336
The first LIM domain of the paxillin like protein family; The first LIM domain of the paxillin ...
 98-148 2.49e-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: 42.76  E-value: 2.49e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 330443491   98 CHVCDTPLRGLYYTAFGYRYDEEHFSCTICATPCGVKKCFMYGNQLYCK--YH 148
Cdd:cd09336     1 CAACNKPIVGQVVTALGKTWHPEHFVCVHCQTELGTSNFFERDGKPYCEkdYH 53
LIM_CRP_like cd09326
The LIM domains of Cysteine Rich Protein (CRP) family; The LIM domains of Cysteine Rich ...
 28-67 3.60e-05

The LIM domains of Cysteine Rich Protein (CRP) family; The LIM domains of Cysteine Rich Protein (CRP) family: Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to a short glycine-rich repeats (GRRs). The known CRP family members include CRP1, CRP2, and CRP3/MLP. CRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription control, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network. CRP1, CRP2, and CRP3/MLP are involved in promoting protein assembly along the actin-based cytoskeleton. 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: 188712  Cd Length: 53  Bit Score: 42.20  E-value: 3.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 330443491   28 CARCNKLVIPDSQRTkttlkALGKYYHESCFTCQDCQKPL 67
Cdd:cd09326     1 CPRCGKSVYAAEEVI-----AAGKSWHKSCFTCAVCNKRL 35
LIM1_LIMK cd09364
The first LIM domain of LIMK (LIM domain Kinase ); The first LIM domain of LIMK (LIM domain ...
 419-467 3.75e-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: 3.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 330443491  419 CAGCNKYIQE-ECIQFYEHRWHIACFTCSSCHKninprSLTDPTFNKEKK 467
Cdd:cd09364     1 CAGCRGKILDsQYVQALNQDWHCDCFRCSVCSD-----SLSNWYFEKDGK 45
LIM3_LIMPETin cd09421
The third LIM domain of protein LIMPETin; The third LIM domain of protein LIMPETin: LIMPETin ...
 417-474 4.05e-05

The third LIM domain of protein LIMPETin; The third LIM domain of protein LIMPETin: LIMPETin contains 6 LIM domains at the C-terminal and an N-terminal PET domain. Four of the six LIM domains are highly homologous to the four and half LIM domain protein family and two of them show sequence similarity to the LIM domains of the testin family. Thus, LIMPETin may be the recombinant product of genes coding testin and FHL proteins. In Schistosoma mansoni, where LIMPETin was first identified, LIMPETin is down regulated in sexually mature adult Schistosoma females compared to sexually immature adult females and adult male. Its differential expression indicates that it is a transcription regulator. 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: 188805  Cd Length: 59  Bit Score: 42.17  E-value: 4.05e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443491  417 DSCAGCNKYI--QEECIQFYEHRWHIACFTCSSCHKninprSLTDPTFNKEKKKILCSHC 474
Cdd:cd09421     3 NQCEECSKIIgiDSKDLSYKDKHWHEACFLCSKCKI-----SLVDKPFGSKADRIYCGNC 57
LIM2_FHL3 cd09427
The second LIM domain of Four and a half LIM domains protein 3 (FHL3); The second LIM domain ...
 28-72 4.76e-05

The second LIM domain of Four and a half LIM domains protein 3 (FHL3); The second LIM domain of Four and a half LIM domains protein 3 (FHL3): FHL3 is highly expressed in the skeleton and cardiac muscles and possesses the transactivation and repression activities. FHL3 interacts with many transcription factors, such as CREB, BKLF/KLF3, CtBP2, MyoD, and MZF_1. Moreover, FHL3 interacts with alpha- and beta-subunits of the muscle alpha7beta1 integrin receptor. FHL3 was also proved to possess the auto-activation ability and was confirmed that the second zinc finger motif in fourth LIM domain was responsible for the auto-activation of FHL3. 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: 188811  Cd Length: 58  Bit Score: 42.15  E-value: 4.76e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 330443491   28 CARCNKLVIPDSQRtkttLKALGKYYHESCFTCQDCQKPLKPKYF 72
Cdd:cd09427     4 CVACGKTVMPGSRK----LEYEGQTWHEHCFICHGCEQPIGSRSF 44
LIM1_FHL3 cd09423
The first LIM domain of Four and a half LIM domains protein 3 (FHL3); The first LIM domain of ...
 416-474 5.08e-05

The first LIM domain of Four and a half LIM domains protein 3 (FHL3); The first LIM domain of Four and a half LIM domains protein 3 (FHL3): FHL3 is highly expressed in the skeleton and cardiac muscles and possesses the transactivation and repression activities. FHL3 interacts with many transcription factors, such as CREB, BKLF/KLF3, CtBP2, MyoD, and MZF_1. Moreover, FHL3 interacts with alpha- and beta-subunits of the muscle alpha7beta1 integrin receptor. FHL3 was also proved to possess the auto-activation ability and was confirmed that the second zinc finger motif in fourth LIM domain was responsible for the auto-activation of FHL3. 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: 188807  Cd Length: 59  Bit Score: 41.83  E-value: 5.08e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 330443491  416 TDSCAGCNKYIQEECIQ-FYEHR-WHIACFTCSSCHkninpRSLTDPTFNKEKKKILCSHC 474
Cdd:cd09423     2 ANTCDECKELIGHDSRElYYEDRhYHEHCFRCFRCD-----RSLADEPFTCQDEELLCNDC 57
LIM1_Zyxin cd09349
The first LIM domain of Zyxin; The first LIM domain of Zyxin: Zyxin exhibits three copies of ...
 28-77 5.41e-05

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: 42.92  E-value: 5.41e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 330443491   28 CARCNKLVIpdsqRTKTTLKALGKYYHESCFTCQDCQKPLKPKYFpYQVD 77
Cdd:cd09349    34 CGICGQPLS----RTQPAVRALGHLFHVTCFTCHQCEQQLQGQQF-YSLE 78
LIM_DA1 cd09396
The Lim domain of DA1; The Lim domain of DA1: DA1 contains one copy of LIM domain and a domain ...
 419-452 5.65e-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: 41.47  E-value: 5.65e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 330443491  419 CAGCNKYIQE-ECIQFYEHRWHIACFTCSSCHKNI 452
Cdd:cd09396     1 CAGCKSEIGHgRFLSALGAVWHPECFRCHACRKPI 35
LIM2_FBLP-1 cd09372
The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1); The second LIM domain of ...
 28-90 6.05e-05

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: 41.64  E-value: 6.05e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330443491   28 CARCNKLVipdsqrTKTTLKALGKYYHESCFTCQDCQKPLKPKYFpyQVDKTSEsiLLCQYDY 90
Cdd:cd09372     1 CAKCQGVI------TEHIIRALGKGYHPPCFTCVTCGRRIGDESF--AVDEQNE--VYCLDDY 53
LIM4_FHL2 cd09433
The fourth LIM domain of Four and a half LIM domains protein 2 (FHL2); The fourth LIM domain ...
 419-477 6.28e-05

The fourth LIM domain of Four and a half LIM domains protein 2 (FHL2); The fourth LIM domain of Four and a half LIM domains protein 2 (FHL2): FHL2 is one of the best studied FHL proteins. FHL2 expression is most abundant in the heart, and in brain, liver and lung to a lesser extent. FHL2 participates in a wide range of cellular processes, such as transcriptional regulation, signal transduction, and cell survival by binding to various protein partners. 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. Although FHL2 is abundantly expressed in heart, the fhl2 null mice are viable and had no detectable abnormal cardiac phenotype. 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 s upport the assembly of multimeric protein complexes.


Pssm-ID: 188817  Cd Length: 58  Bit Score: 41.51  E-value: 6.28e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330443491  419 CAGCNKYIQ----EECIQFYEHRWHIACFTCSSChkninPRSLTDPTFNKEKKKILCSHCSID 477
Cdd:cd09433     1 CAGCTNPISglggTKYISFEERQWHNDCFNCKKC-----SLSLVGRGFLTERDDILCPECGKD 58
LIM1_Paxillin cd09405
The first LIM domain of paxillin; The first LIM domain of paxillin: Paxillin is an adaptor ...
 97-148 8.89e-05

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: 41.15  E-value: 8.89e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 330443491   97 LCHVCDTPLRGLYYTAFGYRYDEEHFSCTICATPCGVKKCFMYGNQLYCK--YH 148
Cdd:cd09405     1 VCGACKKPIAGQVVTAMGKTWHPEHFVCTHCQEEIGSRNFFERDGQPYCEkdYH 54
LIM1_FHL2 cd09422
The first LIM domain of Four and a half LIM domains protein 2 (FHL2); The first LIM domain of ...
 416-474 9.71e-05

The first LIM domain of Four and a half LIM domains protein 2 (FHL2); The first LIM domain of Four and a half LIM domains protein 2 (FHL2): FHL2 is one of the best studied FHL proteins. FHL2 expression is most abundant in the heart, and in brain, liver and lung at lesser extent. FHL2 participates in a wide range of cellular processes, such as transcriptional regulation, signal transduction, and cell survival by binding to various protein partners. 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. Although FHL2 is abundantly expressed in heart, the fhl2 null mice are viable and had no detectable abnormal cardiac phenotype. 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: 188806  Cd Length: 62  Bit Score: 41.43  E-value: 9.71e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 330443491  416 TDSCAGCNKYIQEEC--IQFYEHRWHIACFTCSSCHkninpRSLTDPTFNKEKKKILCSHC 474
Cdd:cd09422     2 SNTCEECKKPIGCDCkdLSYKDRHWHESCFHCFQCK-----NSLVDKPFAAKEEHLLCTEC 57
LIM1_LPP cd09351
The first LIM domain of lipoma preferred partner (LPP); The first LIM domain of lipoma ...
 28-90 1.21e-04

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: 40.87  E-value: 1.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330443491   28 CARCNKLVIPDSqrtkTTLKALGKYYHESCFTCQDCQKPLKPKYFpYQVDKTSesilLCQYDY 90
Cdd:cd09351     1 CVKCGEKVLGEG----SGCTAMDQVYHISCFTCHQCQINLQGKPF-YALDGKP----YCEEDY 54
LIM1_FHL1 cd09344
The first LIM domain of Four and a half LIM domains protein 1; The first LIM domain of Four ...
 419-475 1.34e-04

The first LIM domain of Four and a half LIM domains protein 1; The first LIM domain of Four and a half LIM domains protein 1 (FHL1): FHL1 is heavily expressed in skeletal and cardiac muscles. It plays important roles in muscle growth, differentiation, and sarcomere assembly by acting as a modulator of transcription factors. Defects in FHL1 gene are responsible for a number of Muscular dystrophy-like muscle disorders. It has been detected that FHL1 binds to Myosin-binding protein C, regulating myosin filament formation and sarcomere assembly. 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: 188730  Cd Length: 54  Bit Score: 40.51  E-value: 1.34e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 330443491  419 CAGCNKYIQEEC--IQFYEHRWHIACFTCSSCHKNinprsLTDPTFNKEKKKILCSHCS 475
Cdd:cd09344     1 CAECRKPIGADSkeLHHKNRYWHETCFRCAKCYKP-----LANEPFVAKDNKILCGKCT 54
LIM6_LIMPETin cd09432
The sixth LIM domain of protein LIMPETin; The sixth LIM domain of protein LIMPETin: LIMPETin ...
 419-475 1.45e-04

The sixth LIM domain of protein LIMPETin; The sixth LIM domain of protein LIMPETin: LIMPETin contains 6 LIM domains at the C-terminal and an N-terminal PET domain. Four of the six LIM domains are highly homologous to the four and half LIM domain protein family and two of them show sequence similarity to the LIM domains of the testin family. Thus, LIMPETin may be the recombinant product of genes coding testin and FHL proteins. In Schistosoma mansoni, where LIMPETin was first identified, LIMPETin is down regulated in sexually mature adult Schistosoma females compared to sexually immature adult females and adult male. Its differential expression indicates that it is a transcription regulator. 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: 188816  Cd Length: 56  Bit Score: 40.54  E-value: 1.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 330443491  419 CAGCNKYIQ----EECIQFYEHRWHIACFTCSSCHKninprSLTDPTFNKEKKKILCSHCS 475
Cdd:cd09432     1 CAACGKPITgiggTKFISFEDRHWHNDCFNCAGCRT-----SLVGKGFITDGGRILCPDCA 56
LIM3_Paxillin_like cd09338
The third LIM domain of the paxillin like protein family; The third LIM domain of the paxillin ...
 419-450 1.53e-04

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: 40.40  E-value: 1.53e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 330443491  419 CAGCNKYIQEECIQFYEHRWHIACFTCSSCHK 450
Cdd:cd09338     1 CGGCNKPILENYISALNTQWHPECFVCRECHK 32
LIM1_LIMK cd09364
The first LIM domain of LIMK (LIM domain Kinase ); The first LIM domain of LIMK (LIM domain ...
 28-91 1.76e-04

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: 40.17  E-value: 1.76e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330443491   28 CARCNKlVIPDSQrtktTLKALGKYYHESCFTCQDCQKPLKPKYFpyqvdkTSESILLCQYDYF 91
Cdd:cd09364     1 CAGCRG-KILDSQ----YVQALNQDWHCDCFRCSVCSDSLSNWYF------EKDGKLYCRKDYW 53
LIM2_Enigma_like cd09362
The second LIM domain of Enigma-like family; The second LIM domain of Enigma-like family: The ...
 419-471 1.91e-04

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: 40.15  E-value: 1.91e-04
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gi 330443491  419 CAGCNKYIQEECIQFYEHRWHIACFTCSSCHKNINPRsltdpTFNKEKKKILC 471
Cdd:cd09362     1 CARCHKKILGEVMHALKQTWHVSCFVCAACKQPIGNS-----LFHMEDGEPYC 48
LIM4_Paxillin cd09411
The fourth LIM domain of Paxillin; The fourth LIM domain of Paxillin: Paxillin is an adaptor ...
 419-474 1.95e-04

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: 39.93  E-value: 1.95e-04
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gi 330443491  419 CAGCNKYIQEECIQFYEHRWHIACFTCSSCHKNINprsltDPTFNKEKKKILCSHC 474
Cdd:cd09411     1 CSGCQKPITGRCITAMGKKFHPEHFVCAFCLKQLN-----KGTFKEQNDKPYCHNC 51
LIM3_abLIM cd09329
The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin ...
 28-90 2.32e-04

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: 39.99  E-value: 2.32e-04
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gi 330443491   28 CARCNKlVIPDSQrtktTLKALGKYYHESCFTCQDCQKPLKPKYFpyqvdkTSESILLCQYDY 90
Cdd:cd09329     1 CAGCGQ-EIKNGQ----ALLALDKQWHVWCFKCKECGKVLTGEYM------GKDGKPYCERDY 52
LIM_TLP_like cd09401
The LIM domains of thymus LIM protein (TLP); The LIM domain of thymus LIM protein (TLP) like ...
 28-69 2.33e-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: 40.02  E-value: 2.33e-04
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gi 330443491   28 CARCNKLVIPDSQRTkttlkALGKYYHESCFTCQDCQKPLKP 69
Cdd:cd09401     1 CPKCGKPVYFAEKKT-----SLGRDWHKPCLRCEKCKKTLTP 37
LIM1_Leupaxin cd09406
The first LIM domain of Leupaxin; The first LIM domain of Leupaxin: Leupaxin is a cytoskeleton ...
 98-148 2.63e-04

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: 39.85  E-value: 2.63e-04
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gi 330443491   98 CHVCDTPLRGLYYTAFGYRYDEEHFSCTICATPCGVKKCFMYGNQLYCK--YH 148
Cdd:cd09406     3 CASCQKPIAGQVVTALGQTWHPEHFVCCQCGKELGSRPFFERNGQAYCEedYH 55
LIM2_ENH cd09457
The second LIM domain of the Enigma Homolog (ENH) family; The second LIM domain of the Enigma ...
 419-452 2.77e-04

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: 39.63  E-value: 2.77e-04
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gi 330443491  419 CAGCNKYIQEECIQFYEHRWHIACFTCSSCHKNI 452
Cdd:cd09457     1 CGRCQRKILGEVINALKQTWHVSCFVCVACHNPI 34
LIM3_abLIM cd09329
The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin ...
 419-450 2.78e-04

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: 39.61  E-value: 2.78e-04
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gi 330443491  419 CAGCNKYIQE-ECIQFYEHRWHIACFTCSSCHK 450
Cdd:cd09329     1 CAGCGQEIKNgQALLALDKQWHVWCFKCKECGK 33
LIM1_Enigma_like cd09361
The first LIM domain of Enigma-like family; The first LIM domain of Enigma-like family: The ...
 419-474 2.89e-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: 39.65  E-value: 2.89e-04
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gi 330443491  419 CAGCNKYIQEECIQFYEHRWHIACFTCSSCHKninprSLTDPTFNKEKKKILCSHC 474
Cdd:cd09361     1 CAHCNQVIRGPFLVALGRSWHPEEFTCSHCHC-----SLAEIGFVEEKGSLYCELC 51
LIM2_abLIM cd09328
The second LIM domain on actin binding LIM (abLIM) proteins; The second LIM domain of actin ...
 28-69 2.96e-04

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: 39.64  E-value: 2.96e-04
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gi 330443491   28 CARCNKLVipdsqrTKTTLKALGKYYHESCFTCQDCQKPLKP 69
Cdd:cd09328     4 CDSCQDFV------EGEVVSALGKTYHPKCFVCSVCRQPFPP 39
LIM3_Zyxin_like cd09357
The third LIM domain of Zyxin-like family; The third LIM domain of Zyxin like family: This ...
 28-67 3.04e-04

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: 39.71  E-value: 3.04e-04
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gi 330443491   28 CARCNKLVIP-DSQRTKTTLKALGKYYHESCFTCQDCQKPL 67
Cdd:cd09357     1 CSVCGEPIMPePGQDETVRIVALDRSFHVNCYKCEDCGMLL 41
LIM_Mical_like cd09358
The LIM domain of Mical (molecule interacting with CasL) like family; The LIM domain of Mical ...
 28-69 3.10e-04

The LIM domain of Mical (molecule interacting with CasL) like family; The LIM domain of Mical (molecule interacting with CasL) like family: Known members of this family includes LIM domain containing proteins; Mical (molecule interacting with CasL), pollen specific protein SF3, Eplin, xin actin-binding repeat-containing protein 2 (XIRP2) and Ltd-1. The members of this family function mainly at the cytoskeleton and focal adhesions. They interact with transcription factors or other signaling molecules to play roles in muscle development, neuronal differentiation, cell growth and mobility. Eplin has also found to be tumor suppressor. 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: 188744 [Multi-domain]  Cd Length: 53  Bit Score: 39.56  E-value: 3.10e-04
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gi 330443491   28 CARCNKLVIPDSQrtkttLKALGKYYHESCFTCQDCQKPLKP 69
Cdd:cd09358     1 CAVCGKTVYPMER-----LVADGKLFHKSCFRCSHCNKTLRL 37
LIM1_Ajuba_like cd09352
The first LIM domain of Ajuba-like proteins; The first LIM domain of Ajuba-like proteins: ...
 28-90 3.77e-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: 39.34  E-value: 3.77e-04
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gi 330443491   28 CARCNKLVIPDSQrtktTLKALGKYYHESCFTCQDCQKPLKPKYFpYQVDKTsesiLLCQYDY 90
Cdd:cd09352     1 CVKCGKGVYGASQ----ACQAMGNLYHTNCFTCCSCGRTLRGKAF-YNVNGK----VYCEEDY 54
LIM1_Lhx3b cd09467
The first LIM domain of Lhx3b; The first LIM domain of Lhx3b. Lhx3b is a member of LHX protein ...
 27-72 4.15e-04

The first LIM domain of Lhx3b; The first LIM domain of Lhx3b. Lhx3b is a member of 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. Lhx3b is one of the two isoforms of Lhx3. The Lhx3 gene is expressed in the ventral spinal cord, the pons, the medulla oblongata, and the pineal gland of the developing nervous system during mouse embryogenesis, and transcripts are found in the emergent pituitary gland. Lhx3 functions in concert with other transcription factors to specify interneuron and motor neuron fates during development. Lhx3 proteins have been demonstrated to directly bind to the promoters of several pituitary hormone gene promoters. The Lhx3 gene encodes two isoforms, LHX3a and LHX3b that differ in their amino-terminal sequences, where Lhx3a has longer N-terminal. They show differential activation of pituitary hormone genes and distinct DNA binding properties. In human, Lhx3a trans-activated the alpha-glycoprotein subunit promoter and genes containing a high-affinity Lhx3 binding site more effectively than the hLhx3b isoform. In addition, hLhx3a induce transcription of the TSHbeta-subunit gene by acting on pituitary POU domain factor, Pit-1, while hLhx3b does not. 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: 188851 [Multi-domain]  Cd Length: 55  Bit Score: 39.15  E-value: 4.15e-04
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gi 330443491   27 ICARCNKLVIpdsqrTKTTLKALGKYYHESCFTCQDCQKPLKPKYF 72
Cdd:cd09467     3 LCAGCNQHIV-----DRFILKVLDRHWHSKCLKCSDCQTQLAEKCF 43
LIM1_Enigma cd09452
The first LIM domain of Enigma; The first LIM domain of Enigma: Enigma was initially ...
 419-474 5.30e-04

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: 39.01  E-value: 5.30e-04
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gi 330443491  419 CAGCNKYIQEECIQFYEHRWHIACFTCSSCHKninprSLTDPTFNKEKKKILCSHC 474
Cdd:cd09452     1 CAQCNKIIRGRYLVALGRSYHPEEFTCSQCKK-----VLDEGGFFEEKGSIFCPKC 51
LIM2_PINCH cd09332
The second LIM domain of protein PINCH; The second LIM domain of protein PINCH: PINCH plays a ...
 419-474 5.41e-04

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: 38.86  E-value: 5.41e-04
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                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 330443491  419 CAGCNKYIQEECIQFYEHRWHIACFTCSSCHKninprSLTDPTFNKEKKKILCSHC 474
Cdd:cd09332     1 CGKCGEFVIGRVIKAMNNNWHPDCFRCEICNK-----ELADIGFVKNAGRALCHPC 51
LIM1_Lhx4 cd09468
The first LIM domain of Lhx4; The first LIM domain of Lhx4. Lhx4 belongs to the LHX protein ...
 28-72 6.08e-04

The first LIM domain of Lhx4; The first LIM domain of Lhx4. Lhx4 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. LHX4 plays essential roles in pituitary gland and nervous system development. In mice, the lhx4 gene is expressed in the developing hindbrain, cerebral cortex, pituitary gland, and spinal cord. LHX4 shows significant sequence similarity to LHX3, particularly to isoforms Lhx3a. In gene regulation experiments, the LHX4 protein exhibits regulation roles towards pituitary genes, acting on their promoters/enhancers. 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: 188852  Cd Length: 52  Bit Score: 38.80  E-value: 6.08e-04
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gi 330443491   28 CARCNKLVIpdsqrTKTTLKALGKYYHESCFTCQDCQKPLKPKYF 72
Cdd:cd09468     1 CAGCNQHIL-----DKFILKVLDRHWHSSCLKCADCQMQLAERCF 40
LIM2_Enigma cd09456
The second LIM domain of Enigma; The second LIM domain of Enigma: Enigma was initially ...
 419-457 7.13e-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: 38.44  E-value: 7.13e-04
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gi 330443491  419 CAGCNKYIQEECIQFYEHRWHIACFTCSSCHKNINPRSL 457
Cdd:cd09456     1 CAKCKKKITGEIMHALKMTWHVHCFTCAACKTPIRNRAF 39
LIM3_Zyxin cd09435
The third LIM domain of Zyxin; The third LIM domain of Zyxin: Zyxin exhibits three copies of ...
 28-67 7.32e-04

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: 39.08  E-value: 7.32e-04
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gi 330443491   28 CARCNKLVIPDSQRTKTT-LKALGKYYHESCFTCQDCQKPL 67
Cdd:cd09435     1 CCVCSEPIMPEPGRDETVrVVALEKNFHMKCYKCEDCGRPL 41
LIM_TLP_like cd09401
The LIM domains of thymus LIM protein (TLP); The LIM domain of thymus LIM protein (TLP) like ...
 419-474 7.50e-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: 7.50e-04
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gi 330443491  419 CAGCNK--YIQEEcIQFYEHRWHIACFTCSSCHKNINPRSLTDptfnkEKKKILCSHC 474
Cdd:cd09401     1 CPKCGKpvYFAEK-KTSLGRDWHKPCLRCEKCKKTLTPGQHSE-----HEGKPYCNKC 52
LIM5_LIMPETin cd09430
The fifth LIM domain of protein LIMPETin; The fifth LIM domain of protein LIMPETin: LIMPETin ...
 419-474 7.80e-04

The fifth LIM domain of protein LIMPETin; The fifth LIM domain of protein LIMPETin: LIMPETin contains 6 LIM domains at the C-terminal and an N-terminal PET domain. Four of the six LIM domains are highly homologous to the four and half LIM domain protein family and two of them show sequence similarity to the LIM domains of the testin family. Thus, LIMPETin may be the recombinant product of genes coding testin and FHL proteins. In Schistosoma mansoni, where LIMPETin was first identified, LIMPETin is down regulated in sexually mature adult Schistosoma females compared to sexually immature adult females and adult male. Its differential expression indicates that it is a transcription regulator. 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: 188814  Cd Length: 52  Bit Score: 38.23  E-value: 7.80e-04
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gi 330443491  419 CAGCNKYIQEECIQFYEHRWHIACFTCSSCHKninprSLTDPTFNKEKKKILCSHC 474
Cdd:cd09430     1 CSKCNKIINSGGVTYKNEPWHRECFTCTNCSK-----SLAGQRFTSRDEKPYCADC 51
LIM_LASP cd09447
The LIM domain of LIM and SH3 Protein (LASP); The LIM domain of LIM and SH3 Protein (LASP): ...
 28-67 8.66e-04

The LIM domain of LIM and SH3 Protein (LASP); The LIM domain of LIM and SH3 Protein (LASP): LASP family contains two highly homologous members, LASP-1 and LASP-2. LASP contains a LIM motif at its amino terminus, a src homology 3 (SH3) domains at its C-terminal part, and a nebulin-like region in the middle. LASP-1 and -2 are highly conserved in their LIM, nebulin-like, and SH3 domains ,but differ significantly at their linker regions. Both proteins are ubiquitously expressed and involved in cytoskeletal architecture, especially in the organization of focal adhesions. LASP-1 and LASP-2, are important during early embryo- and fetogenesis and are highly expressed in the central nervous system of the adult. However, only LASP-1 seems to participate significantly in neuronal differentiation and plays an important functional role in migration and proliferation of certain cancer cells while the role of LASP-2 is more structural. The expression of LASP-1 in breast tumors is increased significantly. 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: 188831  Cd Length: 53  Bit Score: 38.13  E-value: 8.66e-04
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gi 330443491   28 CARCNKLVIPDSQrtkttLKALGKYYHESCFTCQDCQKPL 67
Cdd:cd09447     1 CARCGKTVYPTEK-----LNCLDKIWHKGCFKCEVCGMTL 35
LIM3_FHL cd09346
The third LIM domain of Four and a half LIM domains protein (FHL); The third LIM domain of ...
 419-452 1.01e-03

The third LIM domain of Four and a half LIM domains protein (FHL); The third 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 int eracts 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: 188732  Cd Length: 52  Bit Score: 38.08  E-value: 1.01e-03
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gi 330443491  419 CAGCNKYIQEECIQFYEHRWHIACFTCSSCHKNI 452
Cdd:cd09346     1 CAKCKKAITSGGVTYRDQPWHKECFVCTGCKKQL 34
LIM1_Enigma_like cd09361
The first LIM domain of Enigma-like family; The first LIM domain of Enigma-like family: The ...
 98-149 1.28e-03

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: 37.73  E-value: 1.28e-03
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gi 330443491   98 CHVCDTPLRGLYYTAFGYRYDEEHFSCTICATPCGVKKCFMYGNQLYCKYHF 149
Cdd:cd09361     1 CAHCNQVIRGPFLVALGRSWHPEEFTCSHCHCSLAEIGFVEEKGSLYCELCY 52
LIM2_Enigma cd09456
The second LIM domain of Enigma; The second LIM domain of Enigma: Enigma was initially ...
 28-90 1.37e-03

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: 37.67  E-value: 1.37e-03
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gi 330443491   28 CARCNKLVipdsqrTKTTLKALGKYYHESCFTCQDCQKPLKPKYFPYQvdktsESILLCQYDY 90
Cdd:cd09456     1 CAKCKKKI------TGEIMHALKMTWHVHCFTCAACKTPIRNRAFYME-----EGAPYCERDY 52
LIM2_TRIP6 cd09356
The second LIM domain of Thyroid receptor-interacting protein 6 (TRIP6); The second LIM domain ...
 28-81 1.46e-03

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: 37.54  E-value: 1.46e-03
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gi 330443491   28 CARCNKLVIpdsqrtKTTLKALGKYYHESCFTCQDCQKPLKPkyFPYQVDKTSE 81
Cdd:cd09356     1 CSVCSKPIM------ERILRATGKAYHPHCFTCVVCHRSLDG--IPFTVDATGQ 46
LIM_CRP_like cd09326
The LIM domains of Cysteine Rich Protein (CRP) family; The LIM domains of Cysteine Rich ...
 419-474 2.01e-03

The LIM domains of Cysteine Rich Protein (CRP) family; The LIM domains of Cysteine Rich Protein (CRP) family: Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to a short glycine-rich repeats (GRRs). The known CRP family members include CRP1, CRP2, and CRP3/MLP. CRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription control, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network. CRP1, CRP2, and CRP3/MLP are involved in promoting protein assembly along the actin-based cytoskeleton. 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: 188712  Cd Length: 53  Bit Score: 37.19  E-value: 2.01e-03
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gi 330443491  419 CAGCNK--YIQEECIQfYEHRWHIACFTCSSCHKNINPRSLTDPtfnkeKKKILCSHC 474
Cdd:cd09326     1 CPRCGKsvYAAEEVIA-AGKSWHKSCFTCAVCNKRLDSTTLAEH-----DGEIYCKSC 52
LIM1_Testin_like cd09340
The first LIM domain of Testin-like family; The first LIM domain of Testin_like family: This ...
 419-449 2.10e-03

The first LIM domain of Testin-like family; The first LIM domain of Testin_like family: This family includes testin, prickle, dyxin and LIMPETin. Structurally, testin and prickle proteins contain three LIM domains at C-terminal; LIMPETin has six LIM domains; and dyxin presents only two LIM domains. However, all members of the family contain a PET protein-protein interaction domain. Testin is a cytoskeleton associated focal adhesion protein that localizes along actin stress fibers, at cell-cell-contact areas, and at focal adhesion plaques. Testin interacts with a variety of cytoskeletal proteins, including zyxin, mena, VASP, talin, and actin and it is involved in cell motility and adhesion events. Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). Dyxin involves in lung and heart development by interaction with GATA6 and blocking GATA6 activated target genes. LIMPETin might be the recombinant product of genes coding testin and four and half LIM proteins and its function is not well understood. 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 complexes.


Pssm-ID: 188726  Cd Length: 58  Bit Score: 37.20  E-value: 2.10e-03
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gi 330443491  419 CAGCNKYIQEECIQFYEHR------WHIACFTCSSCH 449
Cdd:cd09340     1 CEKCKEPINPGEVAVFAERagedacWHPGCFVCETCN 37
LIM1_ZASP_Cypher cd09454
The first LIM domain of ZASP/Cypher family; The first LIM domain of ZASP/Cypher family: ZASP ...
 419-474 2.11e-03

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: 37.27  E-value: 2.11e-03
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gi 330443491  419 CAGCNKYIQEECIQFYEHRWHIACFTCSSCHKninprSLTDPTFNKEKKKILCSHC 474
Cdd:cd09454     1 CGHCNNIIRGPFLVALGRSWHPEEFTCHYCHT-----SLADVSFVEEQNNVYCENC 51
LIM2_Ajuba_like cd09355
The second LIM domain of Ajuba-like proteins; The second LIM domain of Ajuba-like proteins: ...
 28-90 3.06e-03

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: 36.55  E-value: 3.06e-03
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gi 330443491   28 CARCNKLVIPdsqrtkTTLKALGKYYHESCFTCQDCQKPLKPkyFPYQVDktSESILLCQYDY 90
Cdd:cd09355     1 CAVCGHLIME------MILQALGKSYHPGCFRCCVCNECLDG--VPFTVD--VENNIYCVKDY 53
LIM1_Zyxin cd09349
The first LIM domain of Zyxin; The first LIM domain of Zyxin: Zyxin exhibits three copies of ...
 392-474 3.56e-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: 37.53  E-value: 3.56e-03
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gi 330443491  392 LREVEKNELFENNPFQYIKTP----VNATDSCAGCNKYI--QEECIQFYEHRWHIACFTCSSCHkninpRSLTDPTFNKE 465
Cdd:cd09349     3 MKEVEELEMLTQQLMQDMDHPpaaeAATNELCGICGQPLsrTQPAVRALGHLFHVTCFTCHQCE-----QQLQGQQFYSL 77


                  ....*....
gi 330443491  466 KKKILCSHC 474
Cdd:cd09349    78 EGKPYCEEC 86
LIM_Mical_like_2 cd09445
This domain belongs to the LIM domain family which are found on Mical (molecule interacting ...
 28-86 3.57e-03

This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL) like proteins; The LIM domain on proteins of unknown function: This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL)-like proteins. Known members of the Mical-like family includes single LIM domain containing proteins, Mical (molecule interacting with CasL), pollen specific protein SF3, Eplin, xin actin-binding repeat-containing protein 2 (XIRP2), and Ltd-1. The members of this family function mainly at the cytoskeleton and focal adhesions. They interact with transcription factors or other signaling molecules to play roles in muscle development, neuronal differentiation, cell growth, and mobility. 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: 188829 [Multi-domain]  Cd Length: 53  Bit Score: 36.67  E-value: 3.57e-03
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gi 330443491   28 CARCNKLVIPDSQrtkttLKALGKYYHESCFTCQDCQKPLKPKyfPYQVdktSESILLC 86
Cdd:cd09445     1 CRSCGKPVYKMEE-----IIAEKHIYHKNCFRCKDCNKQLKVD--NYQS---HEGNLYC 49
LIM2_FHL cd09345
The second LIM domain of Four and a half LIM domains protein (FHL); The second LIM domain of ...
 419-474 3.70e-03

The second LIM domain of Four and a half LIM domains protein (FHL); The second 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 int eracts 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: 188731 [Multi-domain]  Cd Length: 54  Bit Score: 36.50  E-value: 3.70e-03
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gi 330443491  419 CAGCNKYIQ--EECIQFYEHRWHIACFTCSSCHKNINPRSltdptFNKEKKKILCSHC 474
Cdd:cd09345     1 CKACGKAIMpgSKKMEYKGKFWHEKCFTCSECKKPIGTKS-----FIPKDDKIYCVPC 53
LIM3_Enigma_like cd09363
The third LIM domain of Enigma-like family; The third LIM domain of Enigma-like family: The ...
 419-472 4.00e-03

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: 36.26  E-value: 4.00e-03
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gi 330443491  419 CAGCNKYIQ--EECIQFYEHRWHIACFTCSSCHKNinprsLTDPTFNKEKKKILCS 472
Cdd:cd09363     1 CHGCDFPIEagDRFLEALGHTWHDTCFVCAVCHVN-----LEGQTFYSKKDKPLCK 51
LIM4_Leupaxin cd09412
The fourth LIM domain of Leupaxin; The fourth LIM domain of Leupaxin: Leupaxin is a ...
 419-474 4.10e-03

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: 36.25  E-value: 4.10e-03
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                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 330443491  419 CAGCNKYIQEECIQFYEHRWHIACFTCSSChkninPRSLTDPTFNKEKKKILCSHC 474
Cdd:cd09412     1 CGSCGLPITGRCISALGRKFHPEHFVCAFC-----LRPLTQGSFKEQSGKPYCSTC 51
LIM1_Lhx4 cd09468
The first LIM domain of Lhx4; The first LIM domain of Lhx4. Lhx4 belongs to the LHX protein ...
 419-449 4.24e-03

The first LIM domain of Lhx4; The first LIM domain of Lhx4. Lhx4 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. LHX4 plays essential roles in pituitary gland and nervous system development. In mice, the lhx4 gene is expressed in the developing hindbrain, cerebral cortex, pituitary gland, and spinal cord. LHX4 shows significant sequence similarity to LHX3, particularly to isoforms Lhx3a. In gene regulation experiments, the LHX4 protein exhibits regulation roles towards pituitary genes, acting on their promoters/enhancers. 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: 188852  Cd Length: 52  Bit Score: 36.49  E-value: 4.24e-03
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gi 330443491  419 CAGCNKYIQEECI-QFYEHRWHIACFTCSSCH 449
Cdd:cd09468     1 CAGCNQHILDKFIlKVLDRHWHSSCLKCADCQ 32
LIM2_Lhx2_Lhx9 cd09377
The second LIM domain of Lhx2 and Lhx9 family; The second LIM domain of Lhx2 and Lhx9 family: ...
 26-90 4.98e-03

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: 36.10  E-value: 4.98e-03
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gi 330443491   26 KICARCNkLVIPDSQrtkTTLKALGKYYHESCFTCQDCQKPL-KPKYFPYQvdktsESILLCQYDY 90
Cdd:cd09377     3 KRCARCH-LGISASE---LVMRARDLVFHLNCFTCATCNKPLtKGDHFGMR-----DGLVYCRLHY 59
LIM1_FHL1 cd09344
The first LIM domain of Four and a half LIM domains protein 1; The first LIM domain of Four ...
 28-72 5.49e-03

The first LIM domain of Four and a half LIM domains protein 1; The first LIM domain of Four and a half LIM domains protein 1 (FHL1): FHL1 is heavily expressed in skeletal and cardiac muscles. It plays important roles in muscle growth, differentiation, and sarcomere assembly by acting as a modulator of transcription factors. Defects in FHL1 gene are responsible for a number of Muscular dystrophy-like muscle disorders. It has been detected that FHL1 binds to Myosin-binding protein C, regulating myosin filament formation and sarcomere assembly. 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: 188730  Cd Length: 54  Bit Score: 35.89  E-value: 5.49e-03
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gi 330443491   28 CARCNKLVIPDSQRtkttLKALGKYYHESCFTCQDCQKPLKPKYF 72
Cdd:cd09344     1 CAECRKPIGADSKE----LHHKNRYWHETCFRCAKCYKPLANEPF 41
LIM1_Lhx3_Lhx4 cd09368
The first LIM domain of Lhx3 and Lhx4 family; The first LIM domain of Lhx3-Lhx4 family: Lhx3 ...
 28-72 5.59e-03

The first LIM domain of Lhx3 and Lhx4 family; The first LIM domain of Lhx3-Lhx4 family: Lhx3 and Lhx4 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. The LHX3 and LHX4 LIM-homeodomain transcription factors play essential roles in pituitary gland and nervous system development. Although LHX3 and LHX4 share marked sequence homology, the genes have different expression patterns. They play overlapping, but distinct functions during the establishment of the specialized cells of the mammalian pituitary gland and the nervous system. Lhx3 proteins have been demonstrated the ability to directly bind to the promoters/enhancers of several pituitary hormone gene promoters to cause increased transcription. Lhx3a and Lhx3b, whose mRNAs have distinct temporal expression profiles during development, are two isoforms of Lhx3. LHX4 plays essential roles in pituitary gland and nervous system development. In mice, the lhx4 gene is expressed in the developing hindbrain, cerebral cortex, pituitary gland, and spinal cord. LHX4 shows significant sequence similarity to LHX3, particularly to isoforms Lhx3a. In gene regulation experiments, the LHX4 protein exhibits regulation roles towards pituitary genes, acting on their promoters/enhancers. 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: 188754  Cd Length: 52  Bit Score: 35.86  E-value: 5.59e-03
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                  ....*....|....*....|....*....|....*....|....*
gi 330443491   28 CARCNKLVIpdsqrTKTTLKALGKYYHESCFTCQDCQKPLKPKYF 72
Cdd:cd09368     1 CGGCQEHIL-----DRFILKVLDRTWHAKCLKCNDCGAQLTDKCF 40
LIM_DA1 cd09396
The Lim domain of DA1; The Lim domain of DA1: DA1 contains one copy of LIM domain and a domain ...
 28-72 5.72e-03

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: 36.08  E-value: 5.72e-03
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gi 330443491   28 CARCNKLVIPdsqrtKTTLKALGKYYHESCFTCQDCQKPLKPKYF 72
Cdd:cd09396     1 CAGCKSEIGH-----GRFLSALGAVWHPECFRCHACRKPIAEHEF 40
LIM2_LPP cd09354
The second LIM domain of lipoma preferred partner (LPP); The second LIM domain of lipoma ...
 28-81 6.09e-03

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: 35.98  E-value: 6.09e-03
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gi 330443491   28 CARCNKlviPDSQRTkttLKALGKYYHESCFTCQDCQKPLKPkyFPYQVDKTSE 81
Cdd:cd09354     1 CSVCSK---PILDRI---LRATGKPYHPQCFTCVVCGKSLDG--IPFTVDATNQ 46
LIM1_LIMK2 cd09463
The first LIM domain of LIMK2 (LIM domain Kinase 2); The first LIM domain of LIMK2 (LIM domain ...
 419-467 6.13e-03

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: 36.00  E-value: 6.13e-03
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gi 330443491  419 CAGCNKYIQE-ECIQFYEHRWHIACFTCSSCHKninprSLTDPTFNKEKK 467
Cdd:cd09463     1 CTGCGGRIQDsFHYRVVQEAWHNSCFQCSVCQD-----LLTNWYYEKDGK 45
LIM_ALP cd09450
This family represents the LIM domain of ALP, actinin-associated LIM protein; This family ...
 28-72 6.82e-03

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: 35.65  E-value: 6.82e-03
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gi 330443491   28 CARCNKLVIpdsqrtKTTLKALGKYYHESCFTCQDCQKPLKPK-YF 72
Cdd:cd09450     1 CDKCGSGIV------GTVVKARDKYRHPECFVCSDCNLNLKQKgYF 40
LIM3_ENH cd09459
The third LIM domain of the Enigma Homolog (ENH) family; The third LIM domain of the Enigma ...
 419-471 6.87e-03

The third LIM domain of the Enigma Homolog (ENH) family; The third 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: 188843 [Multi-domain]  Cd Length: 55  Bit Score: 35.71  E-value: 6.87e-03
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gi 330443491  419 CAGCNKYIqEECIQFYE---HRWHIACFTCSSCHKninprSLTDPTFNKEKKKILC 471
Cdd:cd09459     1 CHGCEFPI-EAGDRFLEalgHTWHDTCFVCSVCCE-----SLEGQTFFSKKDKPLC 50
LIM3_ZASP_Cypher cd09460
The third LIM domain of ZASP/Cypher family; The third LIM domain of ZASP/Cypher family: ZASP ...
 419-473 7.07e-03

The third LIM domain of ZASP/Cypher family; The third 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: 188844  Cd Length: 55  Bit Score: 35.78  E-value: 7.07e-03
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gi 330443491  419 CAGCNKYIQ--EECIQFYEHRWHIACFTCSSCHKNINPRsltdPTFNKEKKKILCSH 473
Cdd:cd09460     1 CHGCDFPVEagDKFIEALGHTWHDTCFICAVCHVNLEGQ----PFYSKKDKPLCKKH 53
LIM1_Lhx3b cd09467
The first LIM domain of Lhx3b; The first LIM domain of Lhx3b. Lhx3b is a member of LHX protein ...
 419-458 7.23e-03

The first LIM domain of Lhx3b; The first LIM domain of Lhx3b. Lhx3b is a member of 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. Lhx3b is one of the two isoforms of Lhx3. The Lhx3 gene is expressed in the ventral spinal cord, the pons, the medulla oblongata, and the pineal gland of the developing nervous system during mouse embryogenesis, and transcripts are found in the emergent pituitary gland. Lhx3 functions in concert with other transcription factors to specify interneuron and motor neuron fates during development. Lhx3 proteins have been demonstrated to directly bind to the promoters of several pituitary hormone gene promoters. The Lhx3 gene encodes two isoforms, LHX3a and LHX3b that differ in their amino-terminal sequences, where Lhx3a has longer N-terminal. They show differential activation of pituitary hormone genes and distinct DNA binding properties. In human, Lhx3a trans-activated the alpha-glycoprotein subunit promoter and genes containing a high-affinity Lhx3 binding site more effectively than the hLhx3b isoform. In addition, hLhx3a induce transcription of the TSHbeta-subunit gene by acting on pituitary POU domain factor, Pit-1, while hLhx3b does not. 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: 188851 [Multi-domain]  Cd Length: 55  Bit Score: 35.68  E-value: 7.23e-03
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gi 330443491  419 CAGCNKYIQEECI-QFYEHRWHIACFTCSSCHKNINPRSLT 458
Cdd:cd09467     4 CAGCNQHIVDRFIlKVLDRHWHSKCLKCSDCQTQLAEKCFS 44
LIM3_Fhl2 cd09431
The third LIM domain of Four and a half LIM domains protein 2 (FHL2); The third LIM domain of ...
 419-458 7.25e-03

The third LIM domain of Four and a half LIM domains protein 2 (FHL2); The third LIM domain of Four and a half LIM domains protein 2 (FHL2): FHL2 is one of the best studied FHL proteins. FHL2 expression is most abundant in the heart, and in brain, liver and lung to a lesser extent. FHL2 participates in a wide range of cellular processes, such as transcriptional regulation, signal transduction, and cell survival by binding to various protein partners. 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. Although FHL2 is abundantly expressed in heart, the fhl2 null mice are viable and had no detectable abnormal cardiac phenotype. 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 s upport the assembly of multimeric protein complexes.


Pssm-ID: 188815  Cd Length: 57  Bit Score: 35.74  E-value: 7.25e-03
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gi 330443491  419 CAGCNKYIQEECIQFYEHRWHIACFTCSSCHKNINPRSLT 458
Cdd:cd09431     1 CVQCKKPITTGGVTYRDQPWHKECFVCTGCKKQLSGQRFT 40
LIM1_Lrg1p_like cd09391
The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The first LIM ...
 419-455 7.30e-03

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: 35.74  E-value: 7.30e-03
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                  ....*....|....*....|....*....|....*..
gi 330443491  419 CAGCNKYIQEECIQFYEHRWHIACFTCSSCHKNINPR 455
Cdd:cd09391     1 CAKCGKPITGQFVRALGDVYHLDCFTCHDCGKPVASK 37
LIM1_TRIP6 cd09350
The first LIM domain of Thyroid receptor-interacting protein 6 (TRIP6); The first LIM domain ...
 28-80 7.32e-03

The first LIM domain of Thyroid receptor-interacting protein 6 (TRIP6); The first 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: 188736  Cd Length: 54  Bit Score: 35.84  E-value: 7.32e-03
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gi 330443491   28 CARCNKLVIPDSqrtkTTLKALGKYYHESCFTCQDCQKPLKPKYFpYQVDKTS 80
Cdd:cd09350     1 CGRCGENVVGEG----TGCTAMDQVFHVDCFTCMTCNGKLRGQPF-YAVEKKA 48
LIM2_FBLP-1 cd09372
The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1); The second LIM domain of ...
 419-464 8.08e-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: 35.48  E-value: 8.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 330443491  419 CAGCNKYIQEECIQFYEHRWHIACFTCSSCHKNINPRSLTDPTFNK 464
Cdd:cd09372     1 CAKCQGVITEHIIRALGKGYHPPCFTCVTCGRRIGDESFAVDEQNE 46
LIM_LASP_like cd09359
The LIM domain of LIM and SH3 Protein (LASP)-like proteins; The LIM domain of LIM and SH3 ...
 28-72 9.46e-03

The LIM domain of LIM and SH3 Protein (LASP)-like proteins; The LIM domain of LIM and SH3 Protein (LASP) like proteins: This family contains two types of LIM containing proteins; LASP and N-RAP. LASP family contains two highly homologous members, LASP-1 and LASP-2. LASP contains a LIM motif at its amino terminus, a src homology 3 (SH3) domains at its C-terminal part, and a nebulin-like region in the middle. LASP-1 and -2 are highly conserved in their LIM, nebulin-like, and SH3 domains, but differ significantly at their linker regions. Both proteins are ubiquitously expressed and involved in cytoskeletal architecture, especially in the organization of focal adhesions. LASP-1 and LASP-2, are important during early embryo- and fetogenesis and are highly expressed in the central nervous system of the adult. However, only LASP-1 seems to participate significantly in neuronal differentiation and plays an important functional role in migration and proliferation of certain cancer cells while the role of LASP-2 is more structural. The expression of LASP-1 in breast tumors is increased significantly. 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: 188745  Cd Length: 53  Bit Score: 35.32  E-value: 9.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 330443491   28 CARCNKLVIPDSQrtkttLKALGKYYHESCFTCQDCQKPLKPKYF 72
Cdd:cd09359     1 CARCGKIVYPTEK-----VNCLDKTWHKACFHCEVCKMTLNMNNY 40
LIM2_FHL1 cd09424
The second LIM domain of Four and a half LIM domains protein 1 (FHL1); The second LIM domain ...
 419-456 1.00e-02

The second LIM domain of Four and a half LIM domains protein 1 (FHL1); The second LIM domain of Four and a half LIM domains protein 1 (FHL1): FHL1 is heavily expressed in skeletal and cardiac muscles. It plays important roles in muscle growth, differentiation, and sarcomere assembly by acting as a modulator of transcription factors. Defects in FHL1 gene are responsible for a number of Muscular dystrophy-like muscle disorders. It has been detected that FHL1 binds to Myosin-binding protein C, regulating myosin filament formation and sarcomere assembly. 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: 188808  Cd Length: 58  Bit Score: 35.51  E-value: 1.00e-02
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 330443491  419 CAGCNKYIQEEC--IQFYEHRWHIACFTCSSCHKNINPRS 456
Cdd:cd09424     1 CKGCYKDILAGDqnVEYKGNVWHKDCFTCSNCKQPIGTKS 40
 
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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