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Conserved domains on  [gi|530402759|ref|XP_005266635|]
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sciellin isoform X13 [Homo sapiens]

Protein Classification

LIM domain-containing protein( domain architecture ID 10639037)

LIM domain-containing protein; LIM is a small protein-protein interaction domain containing two zinc fingers; similar to mammalian sciellin and zinc finger protein 185

Gene Ontology:  GO:0046872
PubMed:  15520811

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 ...
 597-655 1.43e-07

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: 1.43e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 530402759   597 MCTYCRKPLgVETKMILDELQICCHSTCFKCEICKQPLEnlqaGDSIWIYRQTIHCEPC 655
Cdd:smart00132   1 KCAGCGKPI-YGTERVLRALGKVWHPECFKCATCGKPLS----GDTFFEKDGKLYCKDC 54
 
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 ...
 597-655 1.43e-07

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: 1.43e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 530402759   597 MCTYCRKPLgVETKMILDELQICCHSTCFKCEICKQPLEnlqaGDSIWIYRQTIHCEPC 655
Cdd:smart00132   1 KCAGCGKPI-YGTERVLRALGKVWHPECFKCATCGKPLS----GDTFFEKDGKLYCKDC 54
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
 598-656 1.50e-06

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: 1.50e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530402759 598 CTYCRKPlgVETKMILDELQICCHSTCFKCEICKQPLEnlqaGDSIWIYRQTIHCEPCY 656
Cdd:cd08368    1 CAGCGKP--IEGRELLRALGKKWHPECFKCAECGKPLG----GDSFYEKDGKPYCEKCY 53
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
 598-658 1.47e-03

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: 1.47e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530402759  598 CTYCRKP-LGVETKMILDElqiCCHSTCFKCEICKQPLENlqaGDSIWIYRQtIHCEPCYSK 658
Cdd:pfam00412   1 CAGCNRPiYDRELVRALGK---VWHPECFRCAVCGKPLTT---GDFYEKDGK-LYCKHDYYK 55
 
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 ...
 597-655 1.43e-07

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: 1.43e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 530402759   597 MCTYCRKPLgVETKMILDELQICCHSTCFKCEICKQPLEnlqaGDSIWIYRQTIHCEPC 655
Cdd:smart00132   1 KCAGCGKPI-YGTERVLRALGKVWHPECFKCATCGKPLS----GDTFFEKDGKLYCKDC 54
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
 598-656 1.50e-06

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: 1.50e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530402759 598 CTYCRKPlgVETKMILDELQICCHSTCFKCEICKQPLEnlqaGDSIWIYRQTIHCEPCY 656
Cdd:cd08368    1 CAGCGKP--IEGRELLRALGKKWHPECFKCAECGKPLG----GDSFYEKDGKPYCEKCY 53
LIM1_FHL1 cd09344
The first LIM domain of Four and a half LIM domains protein 1; The first LIM domain of Four ...
 598-655 1.74e-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: 39.74  E-value: 1.74e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402759 598 CTYCRKPLGVETKMILDELQICcHSTCFKCEICKQPL--ENLQAGDsiwiyrQTIHCEPC 655
Cdd:cd09344    1 CAECRKPIGADSKELHHKNRYW-HETCFRCAKCYKPLanEPFVAKD------NKILCGKC 53
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
 598-658 1.47e-03

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: 1.47e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530402759  598 CTYCRKP-LGVETKMILDElqiCCHSTCFKCEICKQPLENlqaGDSIWIYRQtIHCEPCYSK 658
Cdd:pfam00412   1 CAGCNRPiYDRELVRALGK---VWHPECFRCAVCGKPLTT---GDFYEKDGK-LYCKHDYYK 55
LIM1_Testin_like cd09340
The first LIM domain of Testin-like family; The first LIM domain of Testin_like family: This ...
 598-653 3.51e-03

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


Pssm-ID: 188726  Cd Length: 58  Bit Score: 36.04  E-value: 3.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530402759 598 CTYCRKPL-----GVETKMILDElqICCHSTCFKCEICKQPLENLqagdsIWIYRQ-TIHCE 653
Cdd:cd09340    1 CEKCKEPInpgevAVFAERAGED--ACWHPGCFVCETCNELLVDL-----IYFYHDgKIYCG 55
 
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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