ADAnticodon-binding domain |
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| SMART accession number: | SM00995
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| Description: |
This domain of approximately 100 residues is conserved from plants to humans. It is frequently found in association with Lsm domain-containing proteins. |
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| Interpro abstract (IPR019181): |
This domain of approximately 100 residues is conserved from plants to humans. It is an anticodon-binding domain of a prolyl-tRNA synthetase [(PUBMED:11399074)]. It is found in Lms12 and homologues. Lsm12 is a protein possibly involved in mRNA degradation or tRNA splicing [(PUBMED:15225602)].
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| Family alignment: |
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There are 150
AD domains in 150 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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- Cellular role (predicted cellular role)
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Cellular role: translation
- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Albrecht M, Lengauer T
- Novel Sm-like proteins with long C-terminal tails and associatedmethyltransferases.
- FEBS Lett. 2004; 569: 18-26
- Display abstract
Sm and Sm-like proteins of the Lsm (like Sm) domain family are generallyinvolved in essential RNA-processing tasks. While recent research hasfocused on the function and structure of small family members, little isknown about Lsm domain proteins carrying additional domains. Using anintegrative bioinformatics approach, we discovered five novel groups ofLsm domain proteins (Lsm12-16) with long C-terminal tails and investigatedtheir functions. All of them are evolutionarily conserved in eukaryoteswith an N-terminal Lsm domain to bind nucleic acids followed by as yetuncharacterized C-terminal domains and sequence motifs. Based on knownyeast interaction partners, Lsm12-16 may play important roles in RNAmetabolism. Particularly, Lsm12 is possibly involved in mRNA degradationor tRNA splicing, and Lsm13-16 in the regulation of the mitotic G2/Mphase. Lsm16 proteins have an additional C-terminal YjeF_N domain of asyet unknown function. The identification of an additionalmethyltransferase domain at the C-terminus of one of the Lsm12 proteinsalso led to the recognition of three new groups of methyltransferases,presumably dependent on S-adenosyl-l-methionine. Further computationalanalyses revealed that some methyltransferases contain putativeRNA-binding helix-turn-helix domains and zinc fingers.
- Links (links to other resources describing this domain)
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to expand nodes. To display all proteins with a AD domain in a specific node, click on it.