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HAMAP rule MF_01833

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General rule information [?]

Accession MF_01833
Dates 30-SEP-2004 (Created)
1-JUN-2023 (Last updated, Version 15)
Name EndA_short
Template Q58819 (ENDA_METJA)

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name
RecName: Full=tRNA-splicing endonuclease;
AltName: Full=tRNA-intron endonuclease;
Gene name

Comments [?]

Function Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a stem of 4 bp.
Catalytic activity Reaction=pretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.; EC=;
Subunit Homotetramer; although the tetramer contains four active sites, only two participate in the cleavage. Therefore, it should be considered as a dimer of dimers.
Similarity Belongs to the tRNA-intron endonuclease family. Archaeal short subfamily.

Keywords [?]

Gene Ontology [?]

GO:0000213; Molecular function: tRNA-intron endonuclease activity.
GO:0006388; Biological process: tRNA splicing, via endonucleolytic cleavage and ligation.

Cross-references [?]

Pfam PF01974; tRNA_int_endo; 1;
PF02778; tRNA_int_endo_N; 1;
NCBIfam TIGR00324; EndA; 1;

Features [?]

From: ENDA_METJA (Q58819)
Key     From     To       Description   Tag   Condition   FTGroup
ACT_SITE     115     115             Y  
ACT_SITE     125     125             H  
ACT_SITE     156     156             K  

Additional information [?]

Size range 154-187 amino acids
Related rules MF_01834 (ENDA)
Fusion None
Comments In archaea, the tRNA-intron endonuclease enzyme is either composed of a homotetramer of a protein of 150-190 amino acids (this family), or composed of a homodimer of a endA protein of 300-370 amino acids (MF_01834), in which each protein of the dimer arose by tandem duplication of the endA protein of 150-190 amino acids.