HAMAP rule MF_00036
General rule information
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| Accession | MF_00036 |
| Dates | 1-JUN-2001 (Created)
3-SEP-2024 (Last updated, Version 52) |
| Name | Ala_tRNA_synth |
| Scope(s) |
Bacteria Archaea |
| Template(s) | P00957 (SYA_ECOLI); [ Recover all ] |
| Triggered by |
case c? <OC:Bacteria>
HAMAP; MF_00036_B (Get profile general information and statistics) end case
case c? <OC:Archaea>
HAMAP; MF_00036_A (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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| Identifier | SYA |
| Protein name | RecName: Full=Alanine--tRNA ligase; EC=6.1.1.7; AltName: Full=Alanyl-tRNA synthetase; Short=AlaRS; |
| Gene name | Name=alaS; |
Comments
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| FUNCTION | Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. |
| CATALYTIC ACTIVITY | Reaction=tRNA(Ala) + L-alanine + ATP = L-alanyl-tRNA(Ala) + AMP + diphosphate; Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA- COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972, ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7; |
| case <FTGroup:1> or <FTGroup:2> | |
| COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; |
| end case | |
| case <OC:Enterobacterales> | |
| SUBUNIT | Homotetramer. |
| end case | |
| SUBCELLULAR LOCATION | Cytoplasm. |
| DOMAIN | Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs. |
| SIMILARITY | Belongs to the class-II aminoacyl-tRNA synthetase family. |
Keywords
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| case <FT:1> | |
| Acetylation | |
| end case | |
| Cytoplasm | |
| Aminoacyl-tRNA synthetase | |
| Protein biosynthesis | |
| Ligase | |
| ATP-binding | |
| Nucleotide-binding | |
| RNA-binding | |
| tRNA-binding | |
| case <FTGroup:1> or <FTGroup:2> | |
| Metal-binding | |
| Zinc | |
| end case | |
Gene Ontology
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| GO:0004813; Molecular function:alanine-tRNA ligase activity | |
| GO:0005524; Molecular function:ATP binding | |
| GO:0006419; Biological process:alanyl-tRNA aminoacylation | |
| case <FTGroup:1> or <FTGroup:2> | |
| GO:0008270; Molecular function:zinc ion binding | |
| end case | |
| GO:0005737; Cellular component:cytoplasm | |
Cross-references
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| Pfam | PF01411; tRNA-synt_2c; 1; |
| PRINTS | PR00980; TRNASYNTHALA; 1; |
| NCBIfam | TIGR03683; A-tRNA_syn_arch; 0-1; |
| NCBIfam | TIGR00344; AlaS; 1; |
| PROSITE | PS50860; AA_TRNA_LIGASE_II_ALA; 1; |
Features
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| From: SYA_ECOLI (P00957) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| case <OC:Escherichia> or <OC:Shigella> | ||||||||||||
| MOD_RES | 74 | 74 | /note="N6-acetyllysine" | K | ||||||||
| end case | ||||||||||||
| case <OC:Bacteria> | ||||||||||||
| BINDING | 564 | 564 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
H | 1 | |||||||
| BINDING | 568 | 568 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
H | 1 | |||||||
| BINDING | 666 | 666 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 1 | |||||||
| BINDING | 670 | 670 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
H | 1 | |||||||
| end case | ||||||||||||
| From: SYA_ARCFU (O28029) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| case <OC:Archaea> | ||||||||||||
| BINDING | 600 | 600 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
H | 2 | |||||||
| BINDING | 604 | 604 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
H | 2 | |||||||
| BINDING | 703 | 703 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 2 | |||||||
| BINDING | 707 | 707 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
H | 2 | |||||||
| end case | ||||||||||||
Additional information
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| Size range | 870-932 amino acids |
| Related rules |
MF_03134 |
| Fusion | Nter: None Cter: None |
| Comments | Zinc-binding shown for Archaea (ARCFU and PYRHO crystals), the residues are (mostly) conserved in bacteria and ECOLI is known to bind zinc. KORVE has an insert in the catalytic domain, BORAP, BORBU, BORGP, BORHD, TREDE, TREPA and the second copy of LACP7 are missing part of the catalytic domain and all of the C-Ala domain and are marked as atypical. In YERPA the C-Ala domain is replaced by an unrelated sequence and is also considered atypical. LACP3, LACPL, LEUCK, LEUMM, OENOB are missing one of the conserved zinc-binding residues and are atypical. |