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Conserved domains on  [gi|157823865|ref|NP_001102513|]
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zinc finger protein 185 isoform b [Mus musculus]

Protein Classification

LIM domain-containing protein( domain architecture ID 10639037)

LIM (LIN-11, Isl1 and MEC-3) domain-containing protein; LIM is a small protein-protein interaction domain containing two zinc fingers; similar to mammalian sciellin and zinc finger protein 185

CATH:  2.10.110.10
Gene Ontology:  GO:0046872|GO:0005515
PubMed:  15520811|10704826|7954790|9594664|8506279
SCOP:  4003634

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
 424-480 5.26e-11

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


:

Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 57.78  E-value: 5.26e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157823865   424 VCTYCSHEIQDCPKItLEHLGICCHEYCFKCGICNKPMGDllDQIFIHRDTIHCGKC 480
Cdd:smart00132   1 KCAGCGKPIYGTERV-LRALGKVWHPECFKCATCGKPLSG--DTFFEKDGKLYCKDC 54
PLN03240 super family cl42905
putative Low-temperature-induced protein; Provisional
 97-200 7.92e-03

putative Low-temperature-induced protein; Provisional


The actual alignment was detected with superfamily member PLN03240:

Pssm-ID: 178778 [Multi-domain]  Cd Length: 626  Bit Score: 38.65  E-value: 7.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823865  97 SSSHSQHrpsktnGAPRSASGQLGAAnsgHPLQSSGY--KMTTEDYKKLAPYNIRRSSISGTEEEEVPFTPDEQKRRSQA 174
Cdd:PLN03240 118 SSSHTKH------SEPIRGVGHEAMS---HPIKHSGVpdKEERRGAATLTPHNTPVSLLSATEDVTRTFVPDEDKSRDQR 188

                         90       100       110
                 ....*....|....*....|....*....|...
gi 157823865 175 ALGVLR-------KTAPREHSYVLSAAKKTTSP 200
Cdd:PLN03240 189 KVNIDRpkgldqdPAAPGSHGGLSNDQSKVTDP 221
 
Name Accession Description Interval E-value
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
 424-480 5.26e-11

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


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 57.78  E-value: 5.26e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157823865   424 VCTYCSHEIQDCPKItLEHLGICCHEYCFKCGICNKPMGDllDQIFIHRDTIHCGKC 480
Cdd:smart00132   1 KCAGCGKPIYGTERV-LRALGKVWHPECFKCATCGKPLSG--DTFFEKDGKLYCKDC 54
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
 425-481 4.30e-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: 46.54  E-value: 4.30e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157823865 425 CTYCSHEIQDcpKITLEHLGICCHEYCFKCGICNKPMGDllDQIFIHRDTIHCGKCY 481
Cdd:cd08368    1 CAGCGKPIEG--RELLRALGKKWHPECFKCAECGKPLGG--DSFYEKDGKPYCEKCY 53
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
 425-485 5.73e-06

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


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 43.48  E-value: 5.73e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157823865  425 CTYCSHEIQDCPKITLehLGICCHEYCFKCGICNKPMGDllDQIFIHRDTIHCGKCYEKLF 485
Cdd:pfam00412   1 CAGCNRPIYDRELVRA--LGKVWHPECFRCAVCGKPLTT--GDFYEKDGKLYCKHDYYKLF 57
PLN03240 PLN03240
putative Low-temperature-induced protein; Provisional
 97-200 7.92e-03

putative Low-temperature-induced protein; Provisional


Pssm-ID: 178778 [Multi-domain]  Cd Length: 626  Bit Score: 38.65  E-value: 7.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823865  97 SSSHSQHrpsktnGAPRSASGQLGAAnsgHPLQSSGY--KMTTEDYKKLAPYNIRRSSISGTEEEEVPFTPDEQKRRSQA 174
Cdd:PLN03240 118 SSSHTKH------SEPIRGVGHEAMS---HPIKHSGVpdKEERRGAATLTPHNTPVSLLSATEDVTRTFVPDEDKSRDQR 188

                         90       100       110
                 ....*....|....*....|....*....|...
gi 157823865 175 ALGVLR-------KTAPREHSYVLSAAKKTTSP 200
Cdd:PLN03240 189 KVNIDRpkgldqdPAAPGSHGGLSNDQSKVTDP 221
 
Name Accession Description Interval E-value
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
 424-480 5.26e-11

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


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 57.78  E-value: 5.26e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157823865   424 VCTYCSHEIQDCPKItLEHLGICCHEYCFKCGICNKPMGDllDQIFIHRDTIHCGKC 480
Cdd:smart00132   1 KCAGCGKPIYGTERV-LRALGKVWHPECFKCATCGKPLSG--DTFFEKDGKLYCKDC 54
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
 425-481 4.30e-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: 46.54  E-value: 4.30e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157823865 425 CTYCSHEIQDcpKITLEHLGICCHEYCFKCGICNKPMGDllDQIFIHRDTIHCGKCY 481
Cdd:cd08368    1 CAGCGKPIEG--RELLRALGKKWHPECFKCAECGKPLGG--DSFYEKDGKPYCEKCY 53
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
 425-485 5.73e-06

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


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 43.48  E-value: 5.73e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157823865  425 CTYCSHEIQDCPKITLehLGICCHEYCFKCGICNKPMGDllDQIFIHRDTIHCGKCYEKLF 485
Cdd:pfam00412   1 CAGCNRPIYDRELVRA--LGKVWHPECFRCAVCGKPLTT--GDFYEKDGKLYCKHDYYKLF 57
LIM1_Testin_like cd09340
The first LIM domain of Testin-like family; The first LIM domain of Testin_like family: This ...
 425-481 7.21e-05

The first LIM domain of Testin-like family; The first LIM domain of Testin_like family: This family includes testin, prickle, dyxin and LIMPETin. Structurally, testin and prickle proteins contain three LIM domains at C-terminal; LIMPETin has six LIM domains; and dyxin presents only two LIM domains. However, all members of the family contain a PET protein-protein interaction domain. Testin is a cytoskeleton associated focal adhesion protein that localizes along actin stress fibers, at cell-cell-contact areas, and at focal adhesion plaques. Testin interacts with a variety of cytoskeletal proteins, including zyxin, mena, VASP, talin, and actin and it is involved in cell motility and adhesion events. Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). Dyxin involves in lung and heart development by interaction with GATA6 and blocking GATA6 activated target genes. LIMPETin might be the recombinant product of genes coding testin and four and half LIM proteins and its function is not well understood. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188726  Cd Length: 58  Bit Score: 40.66  E-value: 7.21e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823865 425 CTYCSHEIQ-DCPKITLEHLG--ICCHEYCFKCGICNKPMGDLLdqIFIHRDTIHCGKCY 481
Cdd:cd09340    1 CEKCKEPINpGEVAVFAERAGedACWHPGCFVCETCNELLVDLI--YFYHDGKIYCGRHY 58
LIM2_FHL cd09345
The second LIM domain of Four and a half LIM domains protein (FHL); The second LIM domain of ...
 440-481 1.26e-04

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: 39.58  E-value: 1.26e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 157823865 440 LEHLGICCHEYCFKCGICNKPMGdllDQIFIHRD-TIHCGKCY 481
Cdd:cd09345   15 MEYKGKFWHEKCFTCSECKKPIG---TKSFIPKDdKIYCVPCY 54
LIM2_FHL1 cd09424
The second LIM domain of Four and a half LIM domains protein 1 (FHL1); The second LIM domain ...
 439-485 3.07e-04

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: 38.59  E-value: 3.07e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 157823865 439 TLEHLGICCHEYCFKCGICNKPMGDlldQIFIHRDT-IHCGKCYEKLF 485
Cdd:cd09424   14 NVEYKGNVWHKDCFTCSNCKQPIGT---KSFFPKGEdFYCVPCHEKKF 58
LIM1_Prickle_1 cd09483
The first LIM domain of Prickle 1; The first LIM domain of Prickle 1. Prickle contains three ...
 444-479 1.69e-03

The first LIM domain of Prickle 1; The first LIM domain of Prickle 1. 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. Four forms of prickles have been identified: prickle 1-4. The best characterized is prickle 1 and prickle 2 which are differentially expressed. While prickle 1 is expressed in fetal heart and hematological malignancies, prickle 2 is found in mainly expressed in fetal brain, adult cartilage, pancreatic islet, and some types of timorous cells. In addition, Prickle 1 regulates cell movements during gastrulation and neuronal migration through interaction with the noncanonical Wnt11/Wnt5 pathway in zebrafish. Mutations in prickle 1 have been linked to progressive myoclonus epilepsy. 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: 188867  Cd Length: 59  Bit Score: 36.82  E-value: 1.69e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 157823865 444 GICCHEYCFKCGICNKPMGDLldqIFIHRD-TIHCGK 479
Cdd:cd09483   23 GVCWHPSCFVCFTCNELLVDL---IYFYQDgKIHCGR 56
PLN03240 PLN03240
putative Low-temperature-induced protein; Provisional
 97-200 7.92e-03

putative Low-temperature-induced protein; Provisional


Pssm-ID: 178778 [Multi-domain]  Cd Length: 626  Bit Score: 38.65  E-value: 7.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823865  97 SSSHSQHrpsktnGAPRSASGQLGAAnsgHPLQSSGY--KMTTEDYKKLAPYNIRRSSISGTEEEEVPFTPDEQKRRSQA 174
Cdd:PLN03240 118 SSSHTKH------SEPIRGVGHEAMS---HPIKHSGVpdKEERRGAATLTPHNTPVSLLSATEDVTRTFVPDEDKSRDQR 188

                         90       100       110
                 ....*....|....*....|....*....|...
gi 157823865 175 ALGVLR-------KTAPREHSYVLSAAKKTTSP 200
Cdd:PLN03240 189 KVNIDRpkgldqdPAAPGSHGGLSNDQSKVTDP 221
LIM1_Prickle cd09415
The first LIM domain of Prickle; The first LIM domain of Prickle: Prickle contains three ...
 444-479 8.59e-03

The first LIM domain of Prickle; The first 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. Four forms of prickles have been identified: prickle 1-4. The best characterized is prickle 1 and prickle 2 which 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. Mutations in prickle 1 have been linked to progressive myoclonus epilepsy. 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: 188799  Cd Length: 59  Bit Score: 34.54  E-value: 8.59e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 157823865 444 GICCHEYCFKCGICNKPMGDLldqIFIHRD-TIHCGK 479
Cdd:cd09415   23 GACWHPACFVCSTCKELLVDL---IYFYQDgKVYCGR 56
 
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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