Annotation rule MF_00036
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General rule information [?]

Accession MF_00036
Dates 1-JUN-2001 (Created)
10-OCT-2014 (Last updated, Version 39)
Name Ala_tRNA_synth
Scope Bacteria
Archaea
Template P00957 (SYA_ECOLI)
case <OC:Bacteria>
end case

case <OC:Archaea>
end case


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.
Catalytic activity ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).
case <FTGroup:1> or <FTGroup:2>
Cofactor Zn(2+)
Note: Binds 1 zinc ion per subunit.
end case
case <OC:Enterobacteriaceae>
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 [?]

case <FT:1>
end case
case <FTGroup:1> or <FTGroup:2>
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.

Cross-references [?]

Pfam PF01411; tRNA-synt_2c; 1;
PRINTS PR00980; TRNASYNTHALA; 1;
TIGRFAMs TIGR00344; AlaS; 1;
PROSITE PS50860; AA_TRNA_LIGASE_II_ALA; 1;

Features [?]

case <OC:Escherichia> or <OC:Shigella>
From: SYA_ECOLI (P00957)
Key     From     To       Description   Tag   Condition   FTGroup
MOD_RES     74     74       N6-acetyllysine     K  
end case
case <OC:Bacteria>
METAL     564     564       Zinc     H   1
METAL     568     568       Zinc     H   1
METAL     666     666       Zinc     C   1
METAL     670     670       Zinc     H   1
end case
case <OC:Archaea>
From: SYA_ARCFU (O28029)
METAL     600     600       Zinc     H   2
METAL     604     604       Zinc     H   2
METAL     703     703       Zinc     C   2
METAL     707     707       Zinc     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 rules MF_03134 (SYAP supersedes the current rule)
Fusion 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, BORGABORHD, 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.