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HAMAP rule MF_01834

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General rule information [?]

Accession MF_01834
Dates 30-SEP-2004 (Created)
1-JUN-2023 (Last updated, Version 15)
Name EndA_long
Scope(s) Archaea
Template(s) O07118 (ENDA_HALVD); O29362 (ENDA_ARCFU); [ Recover all ]
Triggered by HAMAP; MF_01834 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier ENDA
Protein name RecName: Full=tRNA-splicing endonuclease;
AltName: Full=tRNA-intron endonuclease;
Gene name Name=endA;

Comments [?]

FUNCTIONEndonuclease 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=;
SIMILARITYBelongs to the tRNA-intron endonuclease family. Archaeal long 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;
Pfam PF02778; tRNA_int_endo_N; 1;
NCBIfam TIGR00324; EndA; 1;

Features [?]

From: ENDA_HALVD (O07118)
Key From To Description Tag Condition FTGroup
ACT_SITE 274 274 Y
ACT_SITE 285 285 H
ACT_SITE 316 316 K

Additional information [?]

Size range 289-353 amino acids
Related rules MF_01833
Fusion Nter: None Cter: None
Comments In archaea, the tRNA-intron endonuclease enzyme is either composed of a homotetramer of a protein of 150-190 amino acids (MF_01833), or composed of a homodimer of a endA protein of 300-370 amino acids (this family), in which each protein of the dimer arose by tandem duplication of the endA protein of 150-190 amino acids.

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