Conserved Protein Domain Family
LIM2_dLMO

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cd09390: LIM2_dLMO 
The second LIM domain of dLMO (Beaderx)
The second LIM domain of dLMO (Beaderx): dLMO is a nuclear protein that plays important roles in transcriptional regulation and development. In Drosophila dLMO modulates the activity of LIM-homeodomain protein Apterous (Ap), which regulates the formation of the dorsal-ventral axis of the Drosophila wing. Biochemical analysis shows that dLMO protein influences the activity of Apterous by binding of its cofactor Chip. Further studies shown that dLMO proteins might function in an evolutionarily conserved mechanism involved in patterning the appendages. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.
Statistics
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PSSM-Id: 188776
Aligned: 5 rows
Threshold Bit Score: 94.5389
Created: 8-Sep-2010
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
Zn binding site
Feature 1:Zn binding site [ion binding site]
Evidence:
  • Comment:The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The Zn binding residues of LIM domain are highly conserved.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1        #  #                  #  #  #  #                  #  # 
XP_002134510 250 CAACSKVIPAFEMVMRARTNVYHLECFACQQCNHRFCVGDRFYLCENKILCEYDY 304 Drosophila pseudoobscura pseudoobscura
XP_002414040 130 CSACSKTIPAFEMVMRARGNVYHLECFACQHCNHRFCVGDRFYLFDNKILCEYDY 184 black-legged tick
NP_523402    227 CAACSKVIPAFEMVMRARTNVYHLECFACQQCNHRFCVGDRFYLCENKILCEYDY 281 fruit fly
XP_001640872  84 CSVCCKTIPAFEMVMRARDNVYHLECFSCQRCNQRFCVGDKFYLFNNRILCVDDY 138 starlet sea anemone
XP_002587981 115 CAVCAKIIPAFEIVMRAGNNVYHLDCFACQRCNHRFCVGDKFFLCENTILCQLDY 169 Florida lancelet

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