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| Annotation rule MF_01833 |
General rule information
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| Accession | MF_01833 |
| Dates | 30-SEP-2004 (Created) 19-NOV-2019 (Last updated, Version 13) |
| Name | EndA_short |
| Scope | Archaea |
| Template | Q58819 (ENDA_METJA) |
| Triggered by |
Propagated annotation
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Identifier, protein and gene names
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| Identifier |
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| Protein name |
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| Gene name |
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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.
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 (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. |