HAMAP rule MF_01833
General rule information
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Accession | MF_01833 |
Dates | 30-SEP-2004 (Created)
1-JUN-2023 (Last updated, Version 15) |
Name | EndA_short |
Scope(s) |
Archaea |
Template(s) | Q58819 (ENDA_METJA); [ Recover all ] |
Triggered by |
HAMAP; MF_01833 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | ENDA |
Protein name | RecName: Full=tRNA-splicing endonuclease; EC=4.6.1.16; AltName: Full=tRNA-intron endonuclease; |
Gene name | Name=endA; |
Comments
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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=4.6.1.16; |
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
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Gene Ontology
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GO:0000213; Molecular function:tRNA-intron endonuclease activity |
GO:0006388; Biological process:tRNA splicing, via endonucleolytic cleavage and ligation |
Cross-references
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Features
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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
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Size range | 154-187 amino acids |
Related rules |
MF_01834 |
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 (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. |