AC   MF_01833;
DC   Protein; auto
TR   HAMAP; MF_01833; -; 1; level=0
XX
Names: EndA_short
XX
ID   ENDA
DE   RecName: Full=tRNA-splicing endonuclease;
DE            EC=4.6.1.16;
DE   AltName: Full=tRNA-intron endonuclease;
GN   Name=endA;
XX
CC   -!- FUNCTION: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at
CC       the 5'- and 3'-splice sites to release the intron. The products are an
CC       intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and
CC       5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged
CC       loops of 3 bases are separated by a stem of 4 bp.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=pretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-
CC         half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with
CC         a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.; EC=4.6.1.16;
CC   -!- SUBUNIT: Homotetramer; although the tetramer contains four active
CC       sites, only two participate in the cleavage. Therefore, it should be
CC       considered as a dimer of dimers.
CC   -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family. Archaeal
CC       short subfamily.
XX
DR   Pfam; PF01974; tRNA_int_endo; 1; trigger=no
DR   Pfam; PF02778; tRNA_int_endo_N; 1; trigger=no
DR   NCBIfam; TIGR00324; EndA; 1; trigger=no
XX
KW   Lyase
KW   tRNA processing
XX
GO   GO:0000213; F:tRNA-intron endonuclease activity
GO   GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation
XX
FT   From: ENDA_METJA (Q58819)
FT   ACT_SITE        115
FT   Condition: Y
FT   ACT_SITE        125
FT   Condition: H
FT   ACT_SITE        156
FT   Condition: K
XX
Size: 154-187;
Related: MF_01834;
Template: Q58819;
Scope:
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: 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.
XX
# Revision 1.15 2023/06/01
//