HAMAP rule MF_01834
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_01834 |
| Accession | MF_01834 |
| Dates | 28-FEB-2005 (Created)
12-JUN-2025 (Last updated, Version 17) |
| Name | EndA_long |
| Scope(s) |
Archaea |
| Template(s) | O07118; O29362; [ Recover all ] |
| Triggered by |
HAMAP; MF_01834 (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 | Homodimer. |
| SIMILARITY | Belongs to the tRNA-intron endonuclease family. Archaeal long subfamily. |
Keywords
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Gene Ontology
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| GO:0000213; Molecular function:tRNA-intron lyase 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_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
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| 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. |