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Conserved domains on  [gi|699017682|gb|AIU36568|]
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four and a half lim domains 2a, partial [Interochromis loocki]

Protein Classification

LIM domain-containing protein( domain architecture ID 10242179)

LIM (LIN-11, Isl1 and MEC-3) domain-containing protein; LIM is a small protein-protein interaction domain containing two zinc fingers; similar to Mus musculus four and a half LIM domains protein 2 that may function as a molecular transmitter linking various signaling pathways to transcriptional regulation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LIM4_FHL2 cd09433
The fourth LIM domain of Four and a half LIM domains protein 2 (FHL2); The fourth LIM domain ...
221-278 1.09e-30

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: 109.31  E-value: 1.09e-30
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 699017682 221 CASCTTPISGLGGSKYISFEERQWHNDCFNCKKCSVSLVGRGFLTERDDILCPECGKD 278
Cdd:cd09433    1 CAGCTNPISGLGGTKYISFEERQWHNDCFNCKKCSLSLVGRGFLTERDDILCPECGKD 58
LIM2_FHL2 cd09426
The second LIM domain of Four and a half LIM domains protein 2 (FHL2); The second LIM domain ...
101-157 2.69e-29

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: 105.52  E-value: 2.69e-29
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 699017682 101 CHECKKTIMPGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCYEKQ 157
Cdd:cd09426    1 CSECKKTIMPGTRKMEYKGNSWHETCFICQRCQQPIGTKSFIPKDNQNFCVPCYEKQ 57
LIM super family cl02475
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
36-97 7.45e-29

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


The actual alignment was detected with superfamily member cd09422:

Pssm-ID: 413332  Cd Length: 62  Bit Score: 104.60  E-value: 7.45e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 699017682  36 YSNTCEECKKPIGCNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECYSNEY 97
Cdd:cd09422    1 YSNTCEECKKPIGCDCKDLSYKDRHWHESCFHCFQCKNSLVDKPFAAKEEHLLCTECYSNEY 62
LIM super family cl02475
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
162-218 4.35e-28

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


The actual alignment was detected with superfamily member cd09431:

Pssm-ID: 413332  Cd Length: 57  Bit Score: 102.38  E-value: 4.35e-28
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 699017682 162 CVHCKKPITTGGVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCFCNLYA 218
Cdd:cd09431    1 CVQCKKPITTGGVTYRDQPWHKECFVCTGCKKQLSGQRFTSRDDFAYCLNCFCNLYA 57
LIM super family cl02475
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
7-33 3.62e-05

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


The actual alignment was detected with superfamily member cd09417:

Pssm-ID: 413332  Cd Length: 56  Bit Score: 40.59  E-value: 3.62e-05
                         10        20
                 ....*....|....*....|....*..
gi 699017682   7 CHYCKESLFGKKYVLREENPYCVKCYE 33
Cdd:cd09417   30 CWQCDESLTGQRYVLRDEHPYCIKCYE 56
 
Name Accession Description Interval E-value
LIM4_FHL2 cd09433
The fourth LIM domain of Four and a half LIM domains protein 2 (FHL2); The fourth LIM domain ...
221-278 1.09e-30

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: 109.31  E-value: 1.09e-30
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 699017682 221 CASCTTPISGLGGSKYISFEERQWHNDCFNCKKCSVSLVGRGFLTERDDILCPECGKD 278
Cdd:cd09433    1 CAGCTNPISGLGGTKYISFEERQWHNDCFNCKKCSLSLVGRGFLTERDDILCPECGKD 58
LIM2_FHL2 cd09426
The second LIM domain of Four and a half LIM domains protein 2 (FHL2); The second LIM domain ...
101-157 2.69e-29

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: 105.52  E-value: 2.69e-29
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 699017682 101 CHECKKTIMPGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCYEKQ 157
Cdd:cd09426    1 CSECKKTIMPGTRKMEYKGNSWHETCFICQRCQQPIGTKSFIPKDNQNFCVPCYEKQ 57
LIM1_FHL2 cd09422
The first LIM domain of Four and a half LIM domains protein 2 (FHL2); The first LIM domain of ...
36-97 7.45e-29

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: 104.60  E-value: 7.45e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 699017682  36 YSNTCEECKKPIGCNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECYSNEY 97
Cdd:cd09422    1 YSNTCEECKKPIGCDCKDLSYKDRHWHESCFHCFQCKNSLVDKPFAAKEEHLLCTECYSNEY 62
LIM3_Fhl2 cd09431
The third LIM domain of Four and a half LIM domains protein 2 (FHL2); The third LIM domain of ...
162-218 4.35e-28

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: 102.38  E-value: 4.35e-28
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 699017682 162 CVHCKKPITTGGVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCFCNLYA 218
Cdd:cd09431    1 CVQCKKPITTGGVTYRDQPWHKECFVCTGCKKQLSGQRFTSRDDFAYCLNCFCNLYA 57
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
40-92 3.99e-09

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


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 51.62  E-value: 3.99e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 699017682    40 CEECKKPIGCNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTEC 92
Cdd:smart00132   2 CAGCGKPIYGTERVLRALGKVWHPECFKCATCGKPLSGDTFFEKDGKLYCKDC 54
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
100-153 5.86e-08

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


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 48.53  E-value: 5.86e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 699017682   100 KCHECKKTIMPGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPC 153
Cdd:smart00132   1 KCAGCGKPIYGTERVLRALGKVWHPECFKCATCGKPLSGDTFFEKDGKLYCKDC 54
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
162-212 5.02e-06

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: 43.14  E-value: 5.02e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 699017682   162 CVHCKKPITTG--GVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNC 212
Cdd:smart00132   2 CAGCGKPIYGTerVLRALGKVWHPECFKCATCGKPLSGDTFFEKDGKLYCKDC 54
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
162-217 7.96e-06

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


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 42.32  E-value: 7.96e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 699017682  162 CVHCKKPITTGGVTY-RDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCFCNLY 217
Cdd:pfam00412   1 CAGCNRPIYDRELVRaLGKVWHPECFRCAVCGKPLTTGDFYEKDGKLYCKHDYYKLF 57
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
220-275 1.31e-05

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: 41.60  E-value: 1.31e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 699017682   220 KCASCTTPISGlgGSKYISFEERQWHNDCFNCKKCSVSLVGRGFLTERDDILCPEC 275
Cdd:smart00132   1 KCAGCGKPIYG--TERVLRALGKVWHPECFKCATCGKPLSGDTFFEKDGKLYCKDC 54
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
40-97 2.47e-05

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


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 41.16  E-value: 2.47e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 699017682   40 CEECKKPIgcNTRDLSY-KDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECYSNEY 97
Cdd:pfam00412   1 CAGCNRPI--YDRELVRaLGKVWHPECFRCAVCGKPLTTGDFYEKDGKLYCKHDYYKLF 57
LIM2_LIMPETin_like cd09417
The second LIM domain of protein LIMPETin and related proteins; The second LIM domain of ...
7-33 3.62e-05

The second LIM domain of protein LIMPETin and related proteins; The second 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: 188801  Cd Length: 56  Bit Score: 40.59  E-value: 3.62e-05
                         10        20
                 ....*....|....*....|....*..
gi 699017682   7 CHYCKESLFGKKYVLREENPYCVKCYE 33
Cdd:cd09417   30 CWQCDESLTGQRYVLRDEHPYCIKCYE 56
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
101-158 5.30e-04

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


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 37.31  E-value: 5.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 699017682  101 CHECKKTIMPGSRKMEhKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCYEKQF 158
Cdd:pfam00412   1 CAGCNRPIYDRELVRA-LGKVWHPECFRCAVCGKPLTTGDFYEKDGKLYCKHDYYKLF 57
 
Name Accession Description Interval E-value
LIM4_FHL2 cd09433
The fourth LIM domain of Four and a half LIM domains protein 2 (FHL2); The fourth LIM domain ...
221-278 1.09e-30

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: 109.31  E-value: 1.09e-30
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 699017682 221 CASCTTPISGLGGSKYISFEERQWHNDCFNCKKCSVSLVGRGFLTERDDILCPECGKD 278
Cdd:cd09433    1 CAGCTNPISGLGGTKYISFEERQWHNDCFNCKKCSLSLVGRGFLTERDDILCPECGKD 58
LIM2_FHL2 cd09426
The second LIM domain of Four and a half LIM domains protein 2 (FHL2); The second LIM domain ...
101-157 2.69e-29

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: 105.52  E-value: 2.69e-29
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 699017682 101 CHECKKTIMPGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCYEKQ 157
Cdd:cd09426    1 CSECKKTIMPGTRKMEYKGNSWHETCFICQRCQQPIGTKSFIPKDNQNFCVPCYEKQ 57
LIM1_FHL2 cd09422
The first LIM domain of Four and a half LIM domains protein 2 (FHL2); The first LIM domain of ...
36-97 7.45e-29

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: 104.60  E-value: 7.45e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 699017682  36 YSNTCEECKKPIGCNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECYSNEY 97
Cdd:cd09422    1 YSNTCEECKKPIGCDCKDLSYKDRHWHESCFHCFQCKNSLVDKPFAAKEEHLLCTECYSNEY 62
LIM3_Fhl2 cd09431
The third LIM domain of Four and a half LIM domains protein 2 (FHL2); The third LIM domain of ...
162-218 4.35e-28

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: 102.38  E-value: 4.35e-28
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 699017682 162 CVHCKKPITTGGVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCFCNLYA 218
Cdd:cd09431    1 CVQCKKPITTGGVTYRDQPWHKECFVCTGCKKQLSGQRFTSRDDFAYCLNCFCNLYA 57
LIM4_FHL cd09347
The fourth LIM domain of Four and a half LIM domains protein (FHL); The fourth LIM domain of ...
221-276 7.30e-28

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: 101.65  E-value: 7.30e-28
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 699017682 221 CASCTTPISGLGGSKYISFEERQWHNDCFNCKKCSVSLVGRGFLTERDDILCPECG 276
Cdd:cd09347    1 CAACTKPITGLGGAKFISFEERQWHSDCFNCGKCSVSLVGQGFLTQRDEILCPECG 56
LIM1_FHL cd09343
The first LIM domain of Four and a half LIM domains protein (FHL); The first LIM domain of ...
36-94 2.25e-26

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: 97.89  E-value: 2.25e-26
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 699017682  36 YSNTCEECKKPIGCNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECYS 94
Cdd:cd09343    1 FANTCEECKKKIGCDSKDLSYKDRHWHEGCFKCFKCQRSLVDKPFAAKDEDLLCTECYS 59
LIM3_FHL cd09346
The third LIM domain of Four and a half LIM domains protein (FHL); The third LIM domain of ...
162-213 2.49e-23

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: 89.69  E-value: 2.49e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 699017682 162 CVHCKKPITTGGVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd09346    1 CAKCKKAITSGGVTYRDQPWHKECFVCTGCKKQLAGQRFTSRDEYPYCVDCF 52
LIM2_FHL cd09345
The second LIM domain of Four and a half LIM domains protein (FHL); The second LIM domain of ...
101-154 1.97e-22

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: 87.35  E-value: 1.97e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682 101 CHECKKTIMPGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCY 154
Cdd:cd09345    1 CKACGKAIMPGSKKMEYKGKFWHEKCFTCSECKKPIGTKSFIPKDDKIYCVPCY 54
LIM4_FHL3 cd09434
The fourth LIM domain of Four and a half LIM domains protein 3 (FHL3); The fourth LIM domain ...
221-275 3.00e-21

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: 84.43  E-value: 3.00e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 699017682 221 CASCTTPISGLGGSKYISFEERQWHNDCFNCKKCSVSLVGRGFLTERDDILCPEC 275
Cdd:cd09434    1 CAACNKPITGFGGGKYVSFEDRQWHQPCFKCSRCSVSLVGAGFFPDGDQILCRDC 55
LIM6_LIMPETin cd09432
The sixth LIM domain of protein LIMPETin; The sixth LIM domain of protein LIMPETin: LIMPETin ...
221-275 3.16e-20

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: 81.75  E-value: 3.16e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 699017682 221 CASCTTPISGLGGSKYISFEERQWHNDCFNCKKCSVSLVGRGFLTERDDILCPEC 275
Cdd:cd09432    1 CAACGKPITGIGGTKFISFEDRHWHNDCFNCAGCRTSLVGKGFITDGGRILCPDC 55
LIM2_FHL3 cd09427
The second LIM domain of Four and a half LIM domains protein 3 (FHL3); The second LIM domain ...
98-155 9.55e-19

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: 77.97  E-value: 9.55e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 699017682  98 SSKCHECKKTIMPGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCYE 155
Cdd:cd09427    1 SSKCVACGKTVMPGSRKLEYEGQTWHEHCFICHGCEQPIGSRSFIPDKDEHYCVPCYE 58
LIM2_FHL5 cd09428
The second LIM domain of Four and a half LIM domains protein 5 (FHL5); The second LIM domain ...
101-154 2.40e-18

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: 76.80  E-value: 2.40e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682 101 CHECKKTIMPGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCY 154
Cdd:cd09428    1 CFHCKKTIMPGSRKLEFEGNEWHETCFVCQSCQQPIGTKPLITKENKNYCVPCF 54
LIM3_LIMPETin cd09421
The third LIM domain of protein LIMPETin; The third LIM domain of protein LIMPETin: LIMPETin ...
36-93 3.13e-17

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: 73.76  E-value: 3.13e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 699017682  36 YSNTCEECKKPIGCNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECY 93
Cdd:cd09421    1 FANQCEECSKIIGIDSKDLSYKDKHWHEACFLCSKCKISLVDKPFGSKADRIYCGNCY 58
LIM2_FHL1 cd09424
The second LIM domain of Four and a half LIM domains protein 1 (FHL1); The second LIM domain ...
101-158 3.14e-17

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: 73.64  E-value: 3.14e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 699017682 101 CHECKKTIMPGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCYEKQF 158
Cdd:cd09424    1 CKGCYKDILAGDQNVEYKGNVWHKDCFTCSNCKQPIGTKSFFPKGEDFYCVPCHEKKF 58
LIM3_FHL1 cd09429
The third LIM domain of Four and a half LIM domains protein 1 (FHL1); The third LIM domain of ...
162-213 7.80e-17

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: 72.54  E-value: 7.80e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 699017682 162 CVHCKKPITTGGVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd09429    1 CVKCNKPITSGGVTYQDQPWHSECFVCSSCSKKLAGQRFTAVEDQYYCVDCY 52
LIM5_LIMPETin cd09430
The fifth LIM domain of protein LIMPETin; The fifth LIM domain of protein LIMPETin: LIMPETin ...
162-213 3.71e-16

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: 70.97  E-value: 3.71e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 699017682 162 CVHCKKPITTGGVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd09430    1 CSKCNKIINSGGVTYKNEPWHRECFTCTNCSKSLAGQRFTSRDEKPYCADCF 52
LIM1_FHL3 cd09423
The first LIM domain of Four and a half LIM domains protein 3 (FHL3); The first LIM domain of ...
36-94 7.79e-16

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: 69.95  E-value: 7.79e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 699017682  36 YSNTCEECKKPIGCNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECYS 94
Cdd:cd09423    1 FANTCDECKELIGHDSRELYYEDRHYHEHCFRCFRCDRSLADEPFTCQDEELLCNDCYC 59
LIM4_LIMPETin cd09425
The fourth LIM domain of protein LIMPETin; The fourth LIM domain of protein LIMPETin: LIMPETin ...
101-154 2.93e-14

The fourth LIM domain of protein LIMPETin; The fourth 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: 188809  Cd Length: 54  Bit Score: 65.54  E-value: 2.93e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682 101 CHECKKTIMPGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCY 154
Cdd:cd09425    1 CDGCGEIFRAGMKKMEYKGQQWHEKCFCCCECKQPIGTKSFIPKDDDVYCVPCY 54
LIM1_FHL1 cd09344
The first LIM domain of Four and a half LIM domains protein 1; The first LIM domain of Four ...
40-92 4.27e-13

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: 62.46  E-value: 4.27e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 699017682  40 CEECKKPIGCNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTEC 92
Cdd:cd09344    1 CAECRKPIGADSKELHHKNRYWHETCFRCAKCYKPLANEPFVAKDNKILCGKC 53
LIM4_FHL1 cd09348
The fourth LIM domain of Four and a half LIM domains protein 1 (FHL1); The fourth LIM domain ...
218-279 5.15e-12

The fourth LIM domain of Four and a half LIM domains protein 1 (FHL1); The fourth 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: 188734  Cd Length: 64  Bit Score: 59.78  E-value: 5.15e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 699017682 218 AKKCASCTTPISGLG-GSKYISFEERQWHNDCFNCKKCSVSLVGRGFLTERDDILCPECGKDI 279
Cdd:cd09348    2 AKKCSGCQNPITGFGkGTNVVNYEGSSWHDYCFNCKKCSLNLANKRFVFHNGQIYCSDCAKKL 64
LIM4_FHL cd09347
The fourth LIM domain of Four and a half LIM domains protein (FHL); The fourth LIM domain of ...
40-92 1.47e-10

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: 55.81  E-value: 1.47e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 699017682  40 CEECKKPIGC--NTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTEC 92
Cdd:cd09347    1 CAACTKPITGlgGAKFISFEERQWHSDCFNCGKCSVSLVGQGFLTQRDEILCPEC 55
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
40-92 3.99e-09

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


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 51.62  E-value: 3.99e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 699017682    40 CEECKKPIGCNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTEC 92
Cdd:smart00132   2 CAGCGKPIYGTERVLRALGKVWHPECFKCATCGKPLSGDTFFEKDGKLYCKDC 54
LIM6_LIMPETin cd09432
The sixth LIM domain of protein LIMPETin; The sixth LIM domain of protein LIMPETin: LIMPETin ...
40-92 5.40e-09

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: 51.32  E-value: 5.40e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 699017682  40 CEECKKPIGC--NTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTEC 92
Cdd:cd09432    1 CAACGKPITGigGTKFISFEDRHWHNDCFNCAGCRTSLVGKGFITDGGRILCPDC 55
LIM1_FHL1 cd09344
The first LIM domain of Four and a half LIM domains protein 1; The first LIM domain of Four ...
101-153 3.59e-08

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: 48.98  E-value: 3.59e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 699017682 101 CHECKKTIMPGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPC 153
Cdd:cd09344    1 CAECRKPIGADSKELHHKNRYWHETCFRCAKCYKPLANEPFVAKDNKILCGKC 53
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
100-153 5.86e-08

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


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 48.53  E-value: 5.86e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 699017682   100 KCHECKKTIMPGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPC 153
Cdd:smart00132   1 KCAGCGKPIYGTERVLRALGKVWHPECFKCATCGKPLSGDTFFEKDGKLYCKDC 54
LIM3_FHL cd09346
The third LIM domain of Four and a half LIM domains protein (FHL); The third LIM domain of ...
40-93 1.13e-07

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: 47.32  E-value: 1.13e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682  40 CEECKKPIgcNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECY 93
Cdd:cd09346    1 CAKCKKAI--TSGGVTYRDQPWHKECFVCTGCKKQLAGQRFTSRDEYPYCVDCF 52
LIM2_FHL1 cd09424
The second LIM domain of Four and a half LIM domains protein 1 (FHL1); The second LIM domain ...
40-93 1.72e-07

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: 47.06  E-value: 1.72e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682  40 CEECKKPIGCNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECY 93
Cdd:cd09424    1 CKGCYKDILAGDQNVEYKGNVWHKDCFTCSNCKQPIGTKSFFPKGEDFYCVPCH 54
LIM3_Testin_like cd09342
The third LIM domain of Testin-like family; The third LIM domain of Testin_like family: This ...
40-90 2.36e-07

The third LIM domain of Testin-like family; The third 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: 188728  Cd Length: 57  Bit Score: 46.62  E-value: 2.36e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 699017682  40 CEECKKPIGCNTRDLSYKDRHWH--EECFKCFQCKRSLVDKPFSTKDEQLLCT 90
Cdd:cd09342    1 CDACGEPIGPDVQRVAHNGQHWHatEECFCCSNCKKSLLGQPFLPKNGQIFCS 53
LIM1_FHL cd09343
The first LIM domain of Four and a half LIM domains protein (FHL); The first LIM domain of ...
217-275 2.65e-07

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: 46.66  E-value: 2.65e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 699017682 217 YAKKCASCTTPISGlgGSKYISFEERQWHNDCFNCKKCSVSLVGRGFLTERDDILCPEC 275
Cdd:cd09343    1 FANTCEECKKKIGC--DSKDLSYKDRHWHEGCFKCFKCQRSLVDKPFAAKDEDLLCTEC 57
LIM1_FHL2 cd09422
The first LIM domain of Four and a half LIM domains protein 2 (FHL2); The first LIM domain of ...
97-158 3.10e-07

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: 46.44  E-value: 3.10e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 699017682  97 YSSKCHECKKTIMPGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCYEKQF 158
Cdd:cd09422    1 YSNTCEECKKPIGCDCKDLSYKDRHWHESCFHCFQCKNSLVDKPFAAKEEHLLCTECYSNEY 62
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
101-154 5.00e-07

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: 45.77  E-value: 5.00e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682 101 CHECKKTIMpGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCY 154
Cdd:cd08368    1 CAGCGKPIE-GRELLRALGKKWHPECFKCAECGKPLGGDSFYEKDGKPYCEKCY 53
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
162-213 7.06e-07

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: 45.39  E-value: 7.06e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 699017682 162 CVHCKKPITTGGV-TYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd08368    1 CAGCGKPIEGRELlRALGKKWHPECFKCAECGKPLGGDSFYEKDGKPYCEKCY 53
LIM4_FHL3 cd09434
The fourth LIM domain of Four and a half LIM domains protein 3 (FHL3); The fourth LIM domain ...
40-92 7.10e-07

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: 7.10e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 699017682  40 CEECKKPIGC--NTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTEC 92
Cdd:cd09434    1 CAACNKPITGfgGGKYVSFEDRQWHQPCFKCSRCSVSLVGAGFFPDGDQILCRDC 55
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
40-93 9.79e-07

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: 45.00  E-value: 9.79e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682  40 CEECKKPIgCNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECY 93
Cdd:cd08368    1 CAGCGKPI-EGRELLRALGKKWHPECFKCAECGKPLGGDSFYEKDGKPYCEKCY 53
LIM3_Fhl2 cd09431
The third LIM domain of Four and a half LIM domains protein 2 (FHL2); The third LIM domain of ...
40-98 1.13e-06

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: 44.98  E-value: 1.13e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 699017682  40 CEECKKPIgcNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECYSNEYS 98
Cdd:cd09431    1 CVQCKKPI--TTGGVTYRDQPWHKECFVCTGCKKQLSGQRFTSRDDFAYCLNCFCNLYA 57
LIM1_Paxillin_like cd09336
The first LIM domain of the paxillin like protein family; The first LIM domain of the paxillin ...
162-213 1.86e-06

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: 44.30  E-value: 1.86e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 699017682 162 CVHCKKPITTGGVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd09336    1 CAACNKPIVGQVVTALGKTWHPEHFVCVHCQTELGTSNFFERDGKPYCEKDY 52
LIM1_Leupaxin cd09406
The first LIM domain of Leupaxin; The first LIM domain of Leupaxin: Leupaxin is a cytoskeleton ...
161-211 2.19e-06

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: 44.09  E-value: 2.19e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 699017682 161 HCVHCKKPITTGGVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLN 211
Cdd:cd09406    2 DCASCQKPIAGQVVTALGQTWHPEHFVCCQCGKELGSRPFFERNGQAYCEE 52
LIM3_Prickle cd09420
The third LIM domain of Prickle; The third LIM domain of Prickle: Prickle contains three ...
40-90 2.42e-06

The third LIM domain of Prickle; The third LIM domain of Prickle: Prickle contains three C-terminal LIM domains and a N-terminal PET domain. Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). PCP establishment requires the conserved Frizzled/Dishevelled PCP pathway. Prickle interacts with Dishevelled, thereby modulating Frizzled/Dishevelled activity and PCP signaling. Two forms of prickles have been identified; namely prickle 1 and prickle 2. Prickle 1 and prickle 2 are differentially expressed. While prickle 1 is expressed in fetal heart and hematological malignancies, prickle 2 is found in fetal brain, adult cartilage, pancreatic islet, and some types of timorous cells. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188804  Cd Length: 59  Bit Score: 43.97  E-value: 2.42e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 699017682  40 CEECKKPIGCNTRDLSYKDRHWH--EECFKCFQCKRSLVDKPFSTKDEQLLCT 90
Cdd:cd09420    3 CDTCGEHIGVDQGQMTYDGQHWHatEKCFCCAQCKKSLLGRPFLPKQGQIYCS 55
LIM3_FHL1 cd09429
The third LIM domain of Four and a half LIM domains protein 1 (FHL1); The third LIM domain of ...
40-93 3.74e-06

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: 43.26  E-value: 3.74e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682  40 CEECKKPIgcNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECY 93
Cdd:cd09429    1 CVKCNKPI--TSGGVTYQDQPWHSECFVCSSCSKKLAGQRFTAVEDQYYCVDCY 52
LIM6_LIMPETin cd09432
The sixth LIM domain of protein LIMPETin; The sixth LIM domain of protein LIMPETin: LIMPETin ...
162-212 3.90e-06

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: 43.23  E-value: 3.90e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 699017682 162 CVHCKKPITTGG----VTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNC 212
Cdd:cd09432    1 CAACGKPITGIGgtkfISFEDRHWHNDCFNCAGCRTSLVGKGFITDGGRILCPDC 55
LIM2_FHL cd09345
The second LIM domain of Four and a half LIM domains protein (FHL); The second LIM domain of ...
162-213 4.35e-06

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: 43.05  E-value: 4.35e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682 162 CVHCKKPITTGG--VTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd09345    1 CKACGKAIMPGSkkMEYKGKFWHEKCFTCSECKKPIGTKSFIPKDDKIYCVPCY 54
LIM1_FHL1 cd09344
The first LIM domain of Four and a half LIM domains protein 1; The first LIM domain of Four ...
221-276 4.36e-06

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: 43.20  E-value: 4.36e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 699017682 221 CASCTTPISGlgGSKYISFEERQWHNDCFNCKKCSVSLVGRGFLTERDDILCPECG 276
Cdd:cd09344    1 CAECRKPIGA--DSKELHHKNRYWHETCFRCAKCYKPLANEPFVAKDNKILCGKCT 54
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
162-212 5.02e-06

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: 43.14  E-value: 5.02e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 699017682   162 CVHCKKPITTG--GVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNC 212
Cdd:smart00132   2 CAGCGKPIYGTerVLRALGKVWHPECFKCATCGKPLSGDTFFEKDGKLYCKDC 54
LIM4_FHL1 cd09348
The fourth LIM domain of Four and a half LIM domains protein 1 (FHL1); The fourth LIM domain ...
40-95 5.16e-06

The fourth LIM domain of Four and a half LIM domains protein 1 (FHL1); The fourth 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: 188734  Cd Length: 64  Bit Score: 43.21  E-value: 5.16e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 699017682  40 CEECKKPI---GCNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECYSN 95
Cdd:cd09348    5 CSGCQNPItgfGKGTNVVNYEGSSWHDYCFNCKKCSLNLANKRFVFHNGQIYCSDCAKK 63
LIM1_FHL cd09343
The first LIM domain of Four and a half LIM domains protein (FHL); The first LIM domain of ...
158-214 5.44e-06

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: 43.19  E-value: 5.44e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 699017682 158 FAMHCVHCKKPITTGG--VTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCFC 214
Cdd:cd09343    1 FANTCEECKKKIGCDSkdLSYKDRHWHEGCFKCFKCQRSLVDKPFAAKDEDLLCTECYS 59
LIM1_FHL2 cd09422
The first LIM domain of Four and a half LIM domains protein 2 (FHL2); The first LIM domain of ...
158-217 5.54e-06

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: 42.97  E-value: 5.54e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 699017682 158 FAMHCVHCKKPITTGG--VTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCFCNLY 217
Cdd:cd09422    1 YSNTCEECKKPIGCDCkdLSYKDRHWHESCFHCFQCKNSLVDKPFAAKEEHLLCTECYSNEY 62
LIM3_LIMPETin cd09421
The third LIM domain of protein LIMPETin; The third LIM domain of protein LIMPETin: LIMPETin ...
158-213 5.64e-06

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: 42.94  E-value: 5.64e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 699017682 158 FAMHCVHCKKPI--TTGGVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd09421    1 FANQCEECSKIIgiDSKDLSYKDKHWHEACFLCSKCKISLVDKPFGSKADRIYCGNCY 58
LIM1_Paxillin_like cd09336
The first LIM domain of the paxillin like protein family; The first LIM domain of the paxillin ...
101-154 7.56e-06

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: 42.38  E-value: 7.56e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682 101 CHECKKTIMpgSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCY 154
Cdd:cd09336    1 CAACNKPIV--GQVVTALGKTWHPEHFVCVHCQTELGTSNFFERDGKPYCEKDY 52
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
162-217 7.96e-06

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


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 42.32  E-value: 7.96e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 699017682  162 CVHCKKPITTGGVTY-RDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCFCNLY 217
Cdd:pfam00412   1 CAGCNRPIYDRELVRaLGKVWHPECFRCAVCGKPLTTGDFYEKDGKLYCKHDYYKLF 57
LIM4_FHL2 cd09433
The fourth LIM domain of Four and a half LIM domains protein 2 (FHL2); The fourth LIM domain ...
40-92 8.68e-06

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: 42.28  E-value: 8.68e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 699017682  40 CEECKKPIGC--NTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTEC 92
Cdd:cd09433    1 CAGCTNPISGlgGTKYISFEERQWHNDCFNCKKCSLSLVGRGFLTERDDILCPEC 55
LIM4_FHL1 cd09348
The fourth LIM domain of Four and a half LIM domains protein 1 (FHL1); The fourth LIM domain ...
100-156 8.70e-06

The fourth LIM domain of Four and a half LIM domains protein 1 (FHL1); The fourth 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: 188734  Cd Length: 64  Bit Score: 42.44  E-value: 8.70e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 699017682 100 KCHECKKTIM---PGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCYEK 156
Cdd:cd09348    4 KCSGCQNPITgfgKGTNVVNYEGSSWHDYCFNCKKCSLNLANKRFVFHNGQIYCSDCAKK 63
LIM2_FHL1 cd09424
The second LIM domain of Four and a half LIM domains protein 1 (FHL1); The second LIM domain ...
162-213 1.09e-05

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: 42.06  E-value: 1.09e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682 162 CVHCKKPITTGG--VTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd09424    1 CKGCYKDILAGDqnVEYKGNVWHKDCFTCSNCKQPIGTKSFFPKGEDFYCVPCH 54
LIM2_FHL cd09345
The second LIM domain of Four and a half LIM domains protein (FHL); The second LIM domain of ...
40-93 1.18e-05

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: 41.89  E-value: 1.18e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682  40 CEECKKPIGCNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECY 93
Cdd:cd09345    1 CKACGKAIMPGSKKMEYKGKFWHEKCFTCSECKKPIGTKSFIPKDDKIYCVPCY 54
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
220-275 1.31e-05

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: 41.60  E-value: 1.31e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 699017682   220 KCASCTTPISGlgGSKYISFEERQWHNDCFNCKKCSVSLVGRGFLTERDDILCPEC 275
Cdd:smart00132   1 KCAGCGKPIYG--TERVLRALGKVWHPECFKCATCGKPLSGDTFFEKDGKLYCKDC 54
LIM1_FHL2 cd09422
The first LIM domain of Four and a half LIM domains protein 2 (FHL2); The first LIM domain of ...
217-275 1.43e-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: 41.82  E-value: 1.43e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 699017682 217 YAKKCASCTTPISGlgGSKYISFEERQWHNDCFNCKKCSVSLVGRGFLTERDDILCPEC 275
Cdd:cd09422    1 YSNTCEECKKPIGC--DCKDLSYKDRHWHESCFHCFQCKNSLVDKPFAAKEEHLLCTEC 57
LIM4_Paxillin_like cd09339
The fourth LIM domain of the Paxillin-like protein family; The fourth LIM domain of the ...
162-213 1.48e-05

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


Pssm-ID: 188725 [Multi-domain]  Cd Length: 52  Bit Score: 41.56  E-value: 1.48e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 699017682 162 CVHCKKPITTGGVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd09339    1 CAGCGKPITGRCITAMGRKFHPEHFVCAFCLKQLSKGTFKEQDDKPYCHPCF 52
LIM4_LIMPETin cd09425
The fourth LIM domain of protein LIMPETin; The fourth LIM domain of protein LIMPETin: LIMPETin ...
40-93 1.78e-05

The fourth LIM domain of protein LIMPETin; The fourth 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: 188809  Cd Length: 54  Bit Score: 41.27  E-value: 1.78e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682  40 CEECKKPIGCNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECY 93
Cdd:cd09425    1 CDGCGEIFRAGMKKMEYKGQQWHEKCFCCCECKQPIGTKSFIPKDDDVYCVPCY 54
LIM2_Zyxin cd09353
The second LIM domain of Zyxin; The second LIM domain of Zyxin: Zyxin exhibits three copies of ...
101-159 2.37e-05

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: 41.45  E-value: 2.37e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 699017682 101 CHECKKTIMpgSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKD-NQNFCVPCYEKQFA 159
Cdd:cd09353    1 CAVCDQKIT--DRMLKATGKSYHPQCFTCVVCKCPLEGESFIVDQaNQPHCVNDYHRRYA 58
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
40-97 2.47e-05

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


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 41.16  E-value: 2.47e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 699017682   40 CEECKKPIgcNTRDLSY-KDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECYSNEY 97
Cdd:pfam00412   1 CAGCNRPI--YDRELVRaLGKVWHPECFRCAVCGKPLTTGDFYEKDGKLYCKHDYYKLF 57
LIM1_FHL3 cd09423
The first LIM domain of Four and a half LIM domains protein 3 (FHL3); The first LIM domain of ...
97-154 2.68e-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: 41.06  E-value: 2.68e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 699017682  97 YSSKCHECKKTIMPGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCY 154
Cdd:cd09423    1 FANTCDECKELIGHDSRELYYEDRHYHEHCFRCFRCDRSLADEPFTCQDEELLCNDCY 58
LIM2_LIMPETin_like cd09417
The second LIM domain of protein LIMPETin and related proteins; The second LIM domain of ...
7-33 3.62e-05

The second LIM domain of protein LIMPETin and related proteins; The second 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: 188801  Cd Length: 56  Bit Score: 40.59  E-value: 3.62e-05
                         10        20
                 ....*....|....*....|....*..
gi 699017682   7 CHYCKESLFGKKYVLREENPYCVKCYE 33
Cdd:cd09417   30 CWQCDESLTGQRYVLRDEHPYCIKCYE 56
LIM1_Paxillin cd09405
The first LIM domain of paxillin; The first LIM domain of paxillin: Paxillin is an adaptor ...
162-209 4.60e-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: 40.38  E-value: 4.60e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 699017682 162 CVHCKKPITTGGVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYC 209
Cdd:cd09405    2 CGACKKPIAGQVVTAMGKTWHPEHFVCTHCQEEIGSRNFFERDGQPYC 49
LIM5_LIMPETin cd09430
The fifth LIM domain of protein LIMPETin; The fifth LIM domain of protein LIMPETin: LIMPETin ...
40-93 5.96e-05

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: 39.77  E-value: 5.96e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682  40 CEECKKPIgcNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECY 93
Cdd:cd09430    1 CSKCNKII--NSGGVTYKNEPWHRECFTCTNCSKSLAGQRFTSRDEKPYCADCF 52
LIM3_LIMPETin cd09421
The third LIM domain of protein LIMPETin; The third LIM domain of protein LIMPETin: LIMPETin ...
97-155 7.03e-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: 39.86  E-value: 7.03e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 699017682  97 YSSKCHECKKTIMPGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCYE 155
Cdd:cd09421    1 FANQCEECSKIIGIDSKDLSYKDKHWHEACFLCSKCKISLVDKPFGSKADRIYCGNCYD 59
LIM3_Paxillin_like cd09338
The third LIM domain of the paxillin like protein family; The third LIM domain of the paxillin ...
162-209 7.95e-05

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: 39.63  E-value: 7.95e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 699017682 162 CVHCKKPITTGGVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYC 209
Cdd:cd09338    1 CGGCNKPILENYISALNTQWHPECFVCRECHKPFINGSFFEHEGLPYC 48
LIM3_LIMPETin cd09421
The third LIM domain of protein LIMPETin; The third LIM domain of protein LIMPETin: LIMPETin ...
217-275 9.73e-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: 39.48  E-value: 9.73e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 699017682 217 YAKKCASCTTPISGlgGSKYISFEERQWHNDCFNCKKCSVSLVGRGFLTERDDILCPEC 275
Cdd:cd09421    1 FANQCEECSKIIGI--DSKDLSYKDKHWHEACFLCSKCKISLVDKPFGSKADRIYCGNC 57
LIM3_Enigma_like cd09363
The third LIM domain of Enigma-like family; The third LIM domain of Enigma-like family: The ...
101-150 1.06e-04

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


Pssm-ID: 188749 [Multi-domain]  Cd Length: 54  Bit Score: 39.34  E-value: 1.06e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 699017682 101 CHECKKTIMPGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFC 150
Cdd:cd09363    1 CHGCDFPIEAGDRFLEALGHTWHDTCFVCAVCHVNLEGQTFYSKKDKPLC 50
LIM3_Testin_like cd09342
The third LIM domain of Testin-like family; The third LIM domain of Testin_like family: This ...
101-152 1.13e-04

The third LIM domain of Testin-like family; The third 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: 188728  Cd Length: 57  Bit Score: 39.30  E-value: 1.13e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682 101 CHECKKTIMPGSRKMEHKGNSWH--ETCFTCKRCQQPIGTKSFIPKDNQNFCVP 152
Cdd:cd09342    1 CDACGEPIGPDVQRVAHNGQHWHatEECFCCSNCKKSLLGQPFLPKNGQIFCSP 54
LIM2_FHL3 cd09427
The second LIM domain of Four and a half LIM domains protein 3 (FHL3); The second LIM domain ...
162-213 1.24e-04

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: 39.06  E-value: 1.24e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682 162 CVHCKKPITTGG--VTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd09427    4 CVACGKTVMPGSrkLEYEGQTWHEHCFICHGCEQPIGSRSFIPDKDEHYCVPCY 57
LIM2_FHL5 cd09428
The second LIM domain of Four and a half LIM domains protein 5 (FHL5); The second LIM domain ...
40-93 1.32e-04

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: 39.05  E-value: 1.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682  40 CEECKKPIGCNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECY 93
Cdd:cd09428    1 CFHCKKTIMPGSRKLEFEGNEWHETCFVCQSCQQPIGTKPLITKENKNYCVPCF 54
LIM4_FHL1 cd09348
The fourth LIM domain of Four and a half LIM domains protein 1 (FHL1); The fourth LIM domain ...
159-216 1.46e-04

The fourth LIM domain of Four and a half LIM domains protein 1 (FHL1); The fourth 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: 188734  Cd Length: 64  Bit Score: 38.98  E-value: 1.46e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 699017682 159 AMHCVHCKKPITTGG-----VTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCFCNL 216
Cdd:cd09348    2 AKKCSGCQNPITGFGkgtnvVNYEGSSWHDYCFNCKKCSLNLANKRFVFHNGQIYCSDCAKKL 64
LIM1_Paxillin cd09405
The first LIM domain of paxillin; The first LIM domain of paxillin: Paxillin is an adaptor ...
101-150 1.58e-04

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: 38.84  E-value: 1.58e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 699017682 101 CHECKKTImpGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFC 150
Cdd:cd09405    2 CGACKKPI--AGQVVTAMGKTWHPEHFVCTHCQEEIGSRNFFERDGQPYC 49
LIM2_Testin_like cd09341
The second LIM domain of Testin-like family; The second LIM domain of Testin-like family: This ...
7-33 1.63e-04

The second LIM domain of Testin-like family; The second 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: 188727  Cd Length: 56  Bit Score: 38.74  E-value: 1.63e-04
                         10        20
                 ....*....|....*....|....*..
gi 699017682   7 CHYCKESLFGKKYVLREENPYCVKCYE 33
Cdd:cd09341   30 CFQCDEPLGGQRYVLREGKPYCLDCYE 56
LIM1_FHL1 cd09344
The first LIM domain of Four and a half LIM domains protein 1; The first LIM domain of Four ...
162-212 2.45e-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: 38.20  E-value: 2.45e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 699017682 162 CVHCKKPITTGG--VTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNC 212
Cdd:cd09344    1 CAECRKPIGADSkeLHHKNRYWHETCFRCAKCYKPLANEPFVAKDNKILCGKC 53
LIM_TLP_like cd09401
The LIM domains of thymus LIM protein (TLP); The LIM domain of thymus LIM protein (TLP) like ...
40-93 3.02e-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: 38.09  E-value: 3.02e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682  40 CEECKKPIGCNTRDLSYKdRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECY 93
Cdd:cd09401    1 CPKCGKPVYFAEKKTSLG-RDWHKPCLRCEKCKKTLTPGQHSEHEGKPYCNKCY 53
LIM5_LIMPETin cd09430
The fifth LIM domain of protein LIMPETin; The fifth LIM domain of protein LIMPETin: LIMPETin ...
101-154 3.24e-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: 37.84  E-value: 3.24e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682 101 CHECKKTIMPGSrkMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCY 154
Cdd:cd09430    1 CSKCNKIINSGG--VTYKNEPWHRECFTCTNCSKSLAGQRFTSRDEKPYCADCF 52
LIM3_ENH cd09459
The third LIM domain of the Enigma Homolog (ENH) family; The third LIM domain of the Enigma ...
101-150 4.12e-04

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: 37.64  E-value: 4.12e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 699017682 101 CHECKKTIMPGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFC 150
Cdd:cd09459    1 CHGCEFPIEAGDRFLEALGHTWHDTCFVCSVCCESLEGQTFFSKKDKPLC 50
LIM3_Enigma cd09458
The third LIM domain of Enigma; The third LIM domain of Enigma: Enigma was initially ...
101-150 5.06e-04

The third LIM domain of Enigma; The third 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: 188842  Cd Length: 55  Bit Score: 37.33  E-value: 5.06e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 699017682 101 CHECKKTIMPGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFC 150
Cdd:cd09458    1 CHGCDFKIDAGDRFLEALGFSWHDTCFVCAICQINLEGKTFYSKKDKPLC 50
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
101-158 5.30e-04

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


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 37.31  E-value: 5.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 699017682  101 CHECKKTIMPGSRKMEhKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCYEKQF 158
Cdd:pfam00412   1 CAGCNRPIYDRELVRA-LGKVWHPECFRCAVCGKPLTTGDFYEKDGKLYCKHDYYKLF 57
LIM3_FHL cd09346
The third LIM domain of Four and a half LIM domains protein (FHL); The third LIM domain of ...
101-154 6.56e-04

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: 36.92  E-value: 6.56e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682 101 CHECKKTIMPGSrkMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCY 154
Cdd:cd09346    1 CAKCKKAITSGG--VTYRDQPWHKECFVCTGCKKQLAGQRFTSRDEYPYCVDCF 52
LIM3_FHL1 cd09429
The third LIM domain of Four and a half LIM domains protein 1 (FHL1); The third LIM domain of ...
101-155 7.01e-04

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: 37.10  E-value: 7.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 699017682 101 CHECKKTIMPGSrkMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCYE 155
Cdd:cd09429    1 CVKCNKPITSGG--VTYQDQPWHSECFVCSSCSKKLAGQRFTAVEDQYYCVDCYK 53
LIM_DA1 cd09396
The Lim domain of DA1; The Lim domain of DA1: DA1 contains one copy of LIM domain and a domain ...
40-93 7.80e-04

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: 36.85  E-value: 7.80e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682  40 CEECKKPIGcNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECY 93
Cdd:cd09396    1 CAGCKSEIG-HGRFLSALGAVWHPECFRCHACRKPIAEHEFSVSGNDPYHKSCY 53
LIM3_FHL1 cd09429
The third LIM domain of Four and a half LIM domains protein 1 (FHL1); The third LIM domain of ...
221-277 7.97e-04

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: 36.72  E-value: 7.97e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 699017682 221 CASCTTPISGLGgskyISFEERQWHNDCFNCKKCSVSLVGRGFLTERDDILCPECGK 277
Cdd:cd09429    1 CVKCNKPITSGG----VTYQDQPWHSECFVCSSCSKKLAGQRFTAVEDQYYCVDCYK 53
LIM2_LIMPETin_like cd09417
The second LIM domain of protein LIMPETin and related proteins; The second LIM domain of ...
161-213 8.48e-04

The second LIM domain of protein LIMPETin and related proteins; The second 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: 188801  Cd Length: 56  Bit Score: 36.74  E-value: 8.48e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682 161 HCVHCKKPITTGGVT-YRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd09417    2 RSVQCDELIFSGEYTkAMNKDWHSGHFCCWQCDESLTGQRYVLRDEHPYCIKCY 55
LIM2_FHL3 cd09427
The second LIM domain of Four and a half LIM domains protein 3 (FHL3); The second LIM domain ...
37-93 8.98e-04

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: 36.75  E-value: 8.98e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 699017682  37 SNTCEECKKPIGCNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECY 93
Cdd:cd09427    1 SSKCVACGKTVMPGSRKLEYEGQTWHEHCFICHGCEQPIGSRSFIPDKDEHYCVPCY 57
LIM3_Enigma_like_1 cd09461
The third LIM domain of an Enigma subfamily with unknown function; The third LIM domain of an ...
101-150 1.00e-03

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


Pssm-ID: 188845  Cd Length: 54  Bit Score: 36.37  E-value: 1.00e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 699017682 101 CHECKKTIMPGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFC 150
Cdd:cd09461    1 CVSCGFPIEAGDRWVEALNNNYHSQCFNCTRCNVNLEGQSFYAKGGRPFC 50
LIM1_PINCH cd09331
The first LIM domain of protein PINCH; The first LIM domain of paxillin: Paxillin is an ...
174-218 1.04e-03

The first LIM domain of protein PINCH; 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 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: 188717  Cd Length: 59  Bit Score: 36.54  E-value: 1.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 699017682 174 VTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCFCNLYA 218
Cdd:cd09331   15 VNSNGELYHEQCFVCAQCFQPFPDGLFYEFEGRKYCEHDFQVLFA 59
LIM1_Zyxin cd09349
The first LIM domain of Zyxin; The first LIM domain of Zyxin: Zyxin exhibits three copies of ...
162-213 1.31e-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: 37.14  E-value: 1.31e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682 162 CVHCKKPI--TTGGVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd09349   34 CGICGQPLsrTQPAVRALGHLFHVTCFTCHQCEQQLQGQQFYSLEGKPYCEECY 87
LIM2_Enigma_like cd09362
The second LIM domain of Enigma-like family; The second LIM domain of Enigma-like family: The ...
101-150 1.39e-03

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: 35.92  E-value: 1.39e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 699017682 101 CHECKKTIMpgSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFC 150
Cdd:cd09362    1 CARCHKKIL--GEVMHALKQTWHVSCFVCAACKQPIGNSLFHMEDGEPYC 48
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
221-275 1.42e-03

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: 36.14  E-value: 1.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 699017682 221 CASCTTPISGlggSKYISFEERQWHNDCFNCKKCSVSLVGRGFLTERDDILCPEC 275
Cdd:cd08368    1 CAGCGKPIEG---RELLRALGKKWHPECFKCAECGKPLGGDSFYEKDGKPYCEKC 52
LIM2_Testin_like cd09341
The second LIM domain of Testin-like family; The second LIM domain of Testin-like family: This ...
178-213 1.69e-03

The second LIM domain of Testin-like family; The second 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: 188727  Cd Length: 56  Bit Score: 36.04  E-value: 1.69e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 699017682 178 DQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd09341   20 GKNWHLKHFCCFQCDEPLGGQRYVLREGKPYCLDCY 55
LIM2_FHL5 cd09428
The second LIM domain of Four and a half LIM domains protein 5 (FHL5); The second LIM domain ...
162-213 1.83e-03

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: 35.59  E-value: 1.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682 162 CVHCKKPITTGG--VTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd09428    1 CFHCKKTIMPGSrkLEFEGNEWHETCFVCQSCQQPIGTKPLITKENKNYCVPCF 54
LIM3_FHL cd09346
The third LIM domain of Four and a half LIM domains protein (FHL); The third LIM domain of ...
221-275 2.04e-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: 35.38  E-value: 2.04e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 699017682 221 CASCTTPISGLGgskyISFEERQWHNDCFNCKKCSVSLVGRGFLTERDDILCPEC 275
Cdd:cd09346    1 CAKCKKAITSGG----VTYRDQPWHKECFVCTGCKKQLAGQRFTSRDEYPYCVDC 51
LIM4_FHL3 cd09434
The fourth LIM domain of Four and a half LIM domains protein 3 (FHL3); The fourth LIM domain ...
162-212 2.07e-03

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: 35.51  E-value: 2.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 699017682 162 CVHCKKPITTGG----VTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNC 212
Cdd:cd09434    1 CAACNKPITGFGggkyVSFEDRQWHQPCFKCSRCSVSLVGAGFFPDGDQILCRDC 55
LIM4_Paxillin cd09411
The fourth LIM domain of Paxillin; The fourth LIM domain of Paxillin: Paxillin is an adaptor ...
162-213 2.10e-03

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


Pssm-ID: 188795 [Multi-domain]  Cd Length: 52  Bit Score: 35.70  E-value: 2.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 699017682 162 CVHCKKPITTGGVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd09411    1 CSGCQKPITGRCITAMGKKFHPEHFVCAFCLKQLNKGTFKEQNDKPYCHNCF 52
LIM2_Paxillin_like cd09337
The second LIM domain of the paxillin like protein family; The second LIM domain of the ...
162-209 2.18e-03

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


Pssm-ID: 188723 [Multi-domain]  Cd Length: 52  Bit Score: 35.44  E-value: 2.18e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 699017682 162 CVHCKKPITTGGVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYC 209
Cdd:cd09337    1 CAYCNGPILDKCVTALDKTWHPEHFFCAQCGKPFGDEGFHEKDGKPYC 48
LIM1_abLIM cd09327
The first LIM domain of actin binding LIM (abLIM) proteins; The first LIM domain of actin ...
40-93 2.25e-03

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: 35.31  E-value: 2.25e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682  40 CEECKKPigCNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECY 93
Cdd:cd09327    1 CYKCGKK--CKGEVLRVQDKYFHIKCFTCKVCGCDLAQGGFFVKEGEYYCTDDY 52
LIM2_Leupaxin cd09408
The second LIM domain of Leupaxin; The second LIM domain of Leupaxin: Leupaxin is a ...
162-213 2.74e-03

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


Pssm-ID: 188792 [Multi-domain]  Cd Length: 52  Bit Score: 35.18  E-value: 2.74e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 699017682 162 CVHCKKPITTGGVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd09408    1 CAYCAGPILQNVLTAMDQTWHPEHFFCSHCGELFGDEGFLERDGKPYCRRDF 52
LIM1_Enigma_like cd09361
The first LIM domain of Enigma-like family; The first LIM domain of Enigma-like family: The ...
221-275 3.26e-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: 35.03  E-value: 3.26e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 699017682 221 CASCTTPISGlggsKYISFEERQWHNDCFNCKKCSVSLVGRGFLTERDDILCPEC 275
Cdd:cd09361    1 CAHCNQVIRG----PFLVALGRSWHPEEFTCSHCHCSLAEIGFVEEKGSLYCELC 51
LIM2_Prickle cd09418
The second LIM domain of Prickle; The second LIM domain of Prickle: Prickle contains three ...
178-213 3.28e-03

The second LIM domain of Prickle; The second LIM domain of Prickle: Prickle contains three C-terminal LIM domains and a N-terminal PET domain. Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). PCP establishment requires the conserved Frizzled/Dishevelled PCP pathway. Prickle interacts with Dishevelled, thereby modulating Frizzled/Dishevelled activity and PCP signaling. Two forms of prickles have been identified; namely prickle 1 and prickle 2. Prickle 1 and prickle 2 are differentially expressed. While prickle 1 is expressed in fetal heart and hematological malignancies, prickle 2 is found in fetal brain, adult cartilage, pancreatic islet, and some types of timorous cells. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188802  Cd Length: 56  Bit Score: 35.10  E-value: 3.28e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 699017682 178 DQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd09418   20 GRHWHMKHFCCFECECQLGGQRYIMREGRPYCCHCF 55
LIM1_TRIP6 cd09350
The first LIM domain of Thyroid receptor-interacting protein 6 (TRIP6); The first LIM domain ...
173-213 3.77e-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: 34.69  E-value: 3.77e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 699017682 173 GVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd09350   14 GCTAMDQVFHVDCFTCMTCNGKLRGQPFYAVEKKAYCEPCY 54
LIM3_Prickle cd09420
The third LIM domain of Prickle; The third LIM domain of Prickle: Prickle contains three ...
101-150 4.08e-03

The third LIM domain of Prickle; The third LIM domain of Prickle: Prickle contains three C-terminal LIM domains and a N-terminal PET domain. Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). PCP establishment requires the conserved Frizzled/Dishevelled PCP pathway. Prickle interacts with Dishevelled, thereby modulating Frizzled/Dishevelled activity and PCP signaling. Two forms of prickles have been identified; namely prickle 1 and prickle 2. Prickle 1 and prickle 2 are differentially expressed. While prickle 1 is expressed in fetal heart and hematological malignancies, prickle 2 is found in fetal brain, adult cartilage, pancreatic islet, and some types of timorous cells. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188804  Cd Length: 59  Bit Score: 35.11  E-value: 4.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 699017682 101 CHECKKTIMPGSRKMEHKGNSWH--ETCFTCKRCQQPIGTKSFIPKDNQNFC 150
Cdd:cd09420    3 CDTCGEHIGVDQGQMTYDGQHWHatEKCFCCAQCKKSLLGRPFLPKQGQIYC 54
LIM2_Testin_like cd09341
The second LIM domain of Testin-like family; The second LIM domain of Testin-like family: This ...
58-93 4.14e-03

The second LIM domain of Testin-like family; The second 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: 188727  Cd Length: 56  Bit Score: 34.89  E-value: 4.14e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 699017682  58 DRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECY 93
Cdd:cd09341   20 GKNWHLKHFCCFQCDEPLGGQRYVLREGKPYCLDCY 55
LIM_DA1 cd09396
The Lim domain of DA1; The Lim domain of DA1: DA1 contains one copy of LIM domain and a domain ...
101-154 4.60e-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: 34.54  E-value: 4.60e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682 101 CHECKKTIMPGsRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCY 154
Cdd:cd09396    1 CAGCKSEIGHG-RFLSALGAVWHPECFRCHACRKPIAEHEFSVSGNDPYHKSCY 53
LIM1_Zyxin cd09349
The first LIM domain of Zyxin; The first LIM domain of Zyxin: Zyxin exhibits three copies of ...
91-154 4.79e-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: 35.60  E-value: 4.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 699017682  91 ECYSNEYSSKCHECKKTIMPGSRKMEHKgnsWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCY 154
Cdd:cd09349   27 EAATNELCGICGQPLSRTQPAVRALGHL---FHVTCFTCHQCEQQLQGQQFYSLEGKPYCEECY 87
LIM1_Zyxin cd09349
The first LIM domain of Zyxin; The first LIM domain of Zyxin: Zyxin exhibits three copies of ...
37-93 5.08e-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: 35.60  E-value: 5.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 699017682  37 SNTCEECKKPIGCNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECY 93
Cdd:cd09349   31 NELCGICGQPLSRTQPAVRALGHLFHVTCFTCHQCEQQLQGQQFYSLEGKPYCEECY 87
LIM4_Leupaxin cd09412
The fourth LIM domain of Leupaxin; The fourth LIM domain of Leupaxin: Leupaxin is a ...
162-213 5.21e-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: 34.32  E-value: 5.21e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 699017682 162 CVHCKKPITTGGVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd09412    1 CGSCGLPITGRCISALGRKFHPEHFVCAFCLRPLTQGSFKEQSGKPYCSTCF 52
LIM_TLP_like cd09401
The LIM domains of thymus LIM protein (TLP); The LIM domain of thymus LIM protein (TLP) like ...
101-154 5.88e-03

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: 34.24  E-value: 5.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682 101 CHECKKTIMPGSRKMEHkGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCY 154
Cdd:cd09401    1 CPKCGKPVYFAEKKTSL-GRDWHKPCLRCEKCKKTLTPGQHSEHEGKPYCNKCY 53
LIM3_ENH cd09459
The third LIM domain of the Enigma Homolog (ENH) family; The third LIM domain of the Enigma ...
221-272 5.96e-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: 34.56  E-value: 5.96e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 699017682 221 CASCTTPISGlgGSKYISFEERQWHNDCFNCKKCSVSLVGRGFLTERDDILC 272
Cdd:cd09459    1 CHGCEFPIEA--GDRFLEALGHTWHDTCFVCSVCCESLEGQTFFSKKDKPLC 50
LIM2_Testin_like cd09341
The second LIM domain of Testin-like family; The second LIM domain of Testin-like family: This ...
119-155 6.27e-03

The second LIM domain of Testin-like family; The second 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: 188727  Cd Length: 56  Bit Score: 34.12  E-value: 6.27e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 699017682 119 GNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCYE 155
Cdd:cd09341   20 GKNWHLKHFCCFQCDEPLGGQRYVLREGKPYCLDCYE 56
LIM2_CRP3 cd09482
The second LIM domain of Cysteine Rich Protein 3 (CRP3/MLP); The second LIM domain of Cysteine ...
101-154 7.57e-03

The second LIM domain of Cysteine Rich Protein 3 (CRP3/MLP); The second LIM domain of Cysteine Rich Protein 3 (CRP3/MLP): Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to short glycine-rich repeats (GRRs). The CRP family members include CRP1, CRP2, CRP3/MLP and TLPCRP1, 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 circuits, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network.CRP3 also called Muscle LIM Protein (MLP), which is a striated muscle-specific factor that enhances myogenic differentiation. The second LIM domain of CRP3/MLP interacts with cytoskeletal protein beta-spectrin. CRP3/MLP also interacts with the basic helix-loop-helix myogenic transcription factors MyoD, myogenin, and MRF4 thereby increasing their affinity for specific DNA regulatory elements. 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: 188866 [Multi-domain]  Cd Length: 54  Bit Score: 34.22  E-value: 7.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699017682 101 CHECKKTIMPGSRKMeHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFCVPCY 154
Cdd:cd09482    1 CPRCGKSVYAAEKVM-GGGKPWHKTCFRCAICGKSLESTTVTDKDGELYCKVCY 53
LIM4_LIMPETin cd09425
The fourth LIM domain of protein LIMPETin; The fourth LIM domain of protein LIMPETin: LIMPETin ...
176-213 7.63e-03

The fourth LIM domain of protein LIMPETin; The fourth 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: 188809  Cd Length: 54  Bit Score: 33.95  E-value: 7.63e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 699017682 176 YRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd09425   17 YKGQQWHEKCFCCCECKQPIGTKSFIPKDDDVYCVPCY 54
LIM3_ZASP_Cypher cd09460
The third LIM domain of ZASP/Cypher family; The third LIM domain of ZASP/Cypher family: ZASP ...
101-150 8.00e-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: 33.86  E-value: 8.00e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 699017682 101 CHECKKTIMPGSRKMEHKGNSWHETCFTCKRCQQPIGTKSFIPKDNQNFC 150
Cdd:cd09460    1 CHGCDFPVEAGDKFIEALGHTWHDTCFICAVCHVNLEGQPFYSKKDKPLC 50
LIM2_Paxillin cd09407
The second LIM domain of paxillin; The second LIM domain of paxillin: Paxillin is an adaptor ...
162-209 8.47e-03

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


Pssm-ID: 188791 [Multi-domain]  Cd Length: 52  Bit Score: 33.78  E-value: 8.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 699017682 162 CVHCKKPITTGGVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYC 209
Cdd:cd09407    1 CYYCNGPILDKVVTALDRTWHPEHFFCAQCGAFFGPEGFHEKDGKAYC 48
LIM1_PINCH cd09331
The first LIM domain of protein PINCH; The first LIM domain of paxillin: Paxillin is an ...
40-98 8.51e-03

The first LIM domain of protein PINCH; 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 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: 188717  Cd Length: 59  Bit Score: 33.85  E-value: 8.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 699017682  40 CEECKKPIGCNTRDLSYKDRHWHEECFKCFQCKRSLVDKPFSTKDEQLLCTECYSNEYS 98
Cdd:cd09331    1 CERCREGFEPDEKIVNSNGELYHEQCFVCAQCFQPFPDGLFYEFEGRKYCEHDFQVLFA 59
LIM2_CRP2 cd09840
The second LIM domain of Cysteine Rich Protein 2 (CRP2); The second LIM domain of Cysteine ...
179-213 9.73e-03

The second LIM domain of Cysteine Rich Protein 2 (CRP2); The second LIM domain of Cysteine Rich Protein 2 (CRP2): Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to short glycine-rich repeats (GRRs). The CRP family members include CRP1, CRP2, CRP3/MLP and TLPCRP1, 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 circuits, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network.CRP3 also called Muscle LIM Protein (MLP), which is a striated muscle-specific factor that enhances myogenic differentiation. The second LIM domain of CRP3/MLP interacts with cytoskeletal protein beta-spectrin. CRP3/MLP also interacts with the basic helix-loop-helix myogenic transcription factors MyoD, myogenin, and MRF4 thereby increasing their affinity for specific DNA regulatory elements. 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: 188871 [Multi-domain]  Cd Length: 54  Bit Score: 33.93  E-value: 9.73e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 699017682 179 QPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCF 213
Cdd:cd09840   19 KPWHKNCFRCAKCGKSLESTTLTEKEGEIYCKGCY 53
LIM1_FHL3 cd09423
The first LIM domain of Four and a half LIM domains protein 3 (FHL3); The first LIM domain of ...
158-214 9.80e-03

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: 33.74  E-value: 9.80e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 699017682 158 FAMHCVHCKKPI--TTGGVTYRDQPWHKDCFLCTSCKQQLSGQRFTSRDDFAYCLNCFC 214
Cdd:cd09423    1 FANTCDECKELIghDSRELYYEDRHYHEHCFRCFRCDRSLADEPFTCQDEELLCNDCYC 59
 
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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