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HAMAP annotation rule: MF_00036
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General rule information

Accession MF_00036
Dates 1-JUN-2001 (Created)
21-NOV-2011 (Last updated, Version 35)
Data class Protein

case <OC:Bacteria>
Predictors HAMAP; MF_00036_B; [distribution of match scores in UniProtKB];[seed alignment for MF_00036_B]
end case


case <OC:Archaea>
Predictors HAMAP; MF_00036_A; [distribution of match scores in UniProtKB];[seed alignment for MF_00036_A]
end case

Names Ala_tRNA_synth


Propagated annotation

Identifier, protein and gene names
Identifier SYA
Protein name
RecName: Full=Alanine--tRNA ligase;
EC=6.1.1.7;
AltName: Full=Alanyl-tRNA synthetase;
Short=AlaRS;
Gene name alaS
Comments
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 (By similarity).
CATALYTIC ACTIVITY: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).

case <FTGroup:1> or <FTGroup:2>
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
end case


case <OC:Enterobacteriaceae>
SUBUNIT: Homotetramer (By similarity).
end case

SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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 (By similarity).
SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
Cross-references
Pfam PF01411; tRNA-synt_2c; 1;
PRINTS PR00980; TRNASYNTHALA; 1;
TIGRFAMs TIGR00344; AlaS; 1;
PROSITE PS50860; AA_TRNA_LIGASE_II_ALA; 1;
Keywords

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
GO:0004813; Molecular function: alanine-tRNA ligase activity.
GO:0005524; Molecular function: ATP binding.
GO:0006419; Biological process: alanyl-tRNA aminoacylation.

case <FT:1> or <FT:2>
GO:0008270; Molecular function: zinc ion binding.
end case

GO:0005737; Cellular component: cytoplasm.
Features

case <OC:Escherichia> or <OC:Shigella>
From: SYA_ECOLI (P00957)
Key     From     To       Description   Condition   FTGroup
MOD_RES     74     74       N6-acetyllysine (By similarity)   K  
end case

case <OC:Bacteria>
Key     From     To       Description   Condition   FTGroup
 
METAL     564     564       Zinc (Potential)   H   1
METAL     568     568       Zinc (Potential)   H   1
METAL     666     666       Zinc (Potential)   C   1
METAL     670     670       Zinc (Potential)   H   1
end case

case <OC:Archaea>
From: SYA_ARCFU (O28029)
Key     From     To       Description   Condition   FTGroup
METAL     600     600       Zinc (By similarity)   H   2
METAL     604     604       Zinc (By similarity)   H   2
METAL     703     703       Zinc (By similarity)   C   2
METAL     707     707       Zinc (By similarity)   H   2
end case



Additional information


case <OC:Bacteria>
Size range: 842-977 amino acids
end case


case <OC:Archaea>
Size range: 870-932 amino acids
end case

Related UniRules: MF_04134 (SYAP (supersedes the current rule))
Template: P00957 (SYA_ECOLI)
Scope: Bacteria
Archaea
Fusion: Nter: None; Cter: None
Duplicate: in CLOPH
Plasmid encoded: 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, BORGA, BORHD, TREDE, TREPA and the second copy of CLOPH 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. LACC3, LACPL, LEUCK, LEUMM, OENOB are missing one of the conserved zinc-binding residues and are atypical.

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UniProtKB rule member sequences