AC   MF_03133;
DC   Protein; auto
c?   <OC:Eukaryota> or <OG:Plastid>
TR   HAMAP; MF_00036_B; -; 1; level=0
XX
Names: Ala_tRNA_synth_euk
XX
case (<OC:Metazoa> or <OC:Amoebozoa>) and not <AnyFeature:TransitM>
ID   SYAC
else case (<OC:Metazoa> or <OC:Amoebozoa>) and <AnyFeature:TransitM>
ID   SYAM
else
ID   SYA
end case
case <OG:Organellar chromatophore>
DE   RecName: Full=Alanine--tRNA ligase, organellar chromatophore;
DE            EC=6.1.1.7;
DE   AltName: Full=Alanyl-tRNA synthetase;
DE            Short=AlaRS;
else case (<OC:Metazoa> or <OC:Amoebozoa>) and not <AnyFeature:TransitM>
DE   RecName: Full=Alanine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.7;
DE   AltName: Full=Alanyl-tRNA synthetase;
DE            Short=AlaRS;
else case (<OC:Metazoa> or <OC:Amoebozoa>) and <AnyFeature:TransitM>
DE   RecName: Full=Alanine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.7;
DE   AltName: Full=Alanyl-tRNA synthetase;
DE            Short=AlaRS;
else
DE   RecName: Full=Alanine--tRNA ligase;
DE            EC=6.1.1.7;
DE   AltName: Full=Alanyl-tRNA synthetase;
DE            Short=AlaRS;
end case
case <OC:Vertebrata>
GN   Name=AARS;
else case <OC:Drosophilidae> and <AnyFeature:TransitM>
GN   Name=AlaRS-m;
else case <OC:Drosophilidae> and not <AnyFeature:TransitM>
GN   Name=AlaRS;
else case <OC:Caenorhabditis>
GN   Name=aars;
else case <OC:Fungi>
GN   Name=ALA1;
end case
XX
CC   -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-
CC       step reaction: alanine is first activated by ATP to form Ala-AMP and
CC       then transferred to the acceptor end of tRNA(Ala). Also edits
CC       incorrectly charged tRNA(Ala) via its editing domain.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-
CC         tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-
CC         COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
end case
case <OC:Vertebrata>
CC   -!- SUBUNIT: Monomer. Interacts with ANKRD16; the interaction is direct.
else
CC   -!- SUBUNIT: Monomer.
end case
case <OG:Organellar chromatophore>
CC   -!- SUBCELLULAR LOCATION: Plastid, organellar chromatophore.
else case (<OC:Metazoa> or <OC:Amoebozoa>) and not <AnyFeature:TransitM>
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
else case (<OC:Metazoa> or <OC:Amoebozoa>) and <AnyFeature:TransitM>
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
else
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm.
end case
CC   -!- DOMAIN: Consists of three domains; the N-terminal catalytic domain, the
CC       editing domain and the C-terminal C-Ala domain. The editing domain
CC       removes incorrectly charged amino acids, while the C-Ala domain, along
CC       with tRNA(Ala), serves as a bridge to cooperatively bring together the
CC       editing and aminoacylation centers thus stimulating deacylation of
CC       misacylated tRNAs.
case <OC:Mammalia>
CC   -!- PTM: ISGylated.
end case
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
XX
DR   Pfam; PF02272; DHHA1; 1; trigger=no
DR   Pfam; PF01411; tRNA-synt_2c; 1; trigger=no
DR   Pfam; PF07973; tRNA_SAD; 1; trigger=no
DR   PRINTS; PR00980; TRNASYNTHALA; 1; trigger=no
DR   NCBIfam; TIGR00344; AlaS; 1; trigger=no
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1; trigger=no
case (<OC:Metazoa> or <OC:Amoebozoa>)
DR   General; TransitM; -; 0-1; trigger=yes
end case
XX
KW   Aminoacyl-tRNA synthetase
KW   ATP-binding
KW   Ligase
KW   Nucleotide-binding
KW   Protein biosynthesis
KW   RNA-binding
KW   tRNA-binding
case <FTGroup:1>
KW   Metal-binding
KW   Zinc
end case
case <OG:Organellar chromatophore>
KW   Organellar chromatophore
KW   Plastid
else case (<OC:Metazoa> or <OC:Amoebozoa>) and not <AnyFeature:TransitM>
KW   Cytoplasm
else case (<OC:Metazoa> or <OC:Amoebozoa>) and <AnyFeature:TransitM>
KW   Mitochondrion
else
KW   Cytoplasm
KW   Mitochondrion
end case
case <FTTag:acetyl>
KW   Acetylation
end case
case <OC:Mammalia>
KW   Ubl conjugation
end case
XX
GO   GO:0004813; F:alanine-tRNA ligase activity
GO   GO:0005524; F:ATP binding
GO   GO:0008270; F:zinc ion binding
case <OG:Organellar chromatophore>
GO   GO:0006419; P:alanyl-tRNA aminoacylation
GO   GO:0070111; C:organellar chromatophore
else case (<OC:Metazoa> or <OC:Amoebozoa>) and not <AnyFeature:TransitM>
GO   GO:0006419; P:alanyl-tRNA aminoacylation
GO   GO:0005737; C:cytoplasm
else case (<OC:Metazoa> or <OC:Amoebozoa>) and <AnyFeature:TransitM>
GO   GO:0070143; P:mitochondrial alanyl-tRNA aminoacylation
GO   GO:0005739; C:mitochondrion
else
GO   GO:0006419; P:alanyl-tRNA aminoacylation
GO   GO:0070143; P:mitochondrial alanyl-tRNA aminoacylation
GO   GO:0005737; C:cytoplasm
GO   GO:0005739; C:mitochondrion
end case
XX
FT   From: SYAC_HUMAN (P49588)
FT   BINDING         605
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
FT   BINDING         609
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
FT   BINDING         723
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: C
FT   BINDING         727
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
case <OC:Mammalia>
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT   Tag: acetyl; Condition: M
end case
XX
Size: 433-1408;
Related: MF_03134!;
Template: P49588; P40825; P36428; Q5A8K2;
Scope:
 Eukaryota
 Plastid
Fusion:
 Nter: None
 Cter: None
Duplicate: in 9CHLO, AEDAE, ANOGA, ARATH, BRUMA, CAEBR, CAEEL, CHICK, CULQU,
 DANRE, DICDI, DROAN, DROER, DROGR, DROME, DROMO, DROPE, DROPS, DROSE, DROVI,
 DROWI, DROYA, EMENI, HUMAN, MICPS, MOUSE, ORYSI, ORYSJ, OSTLU, OSTTA, PHATR,
 PHYIN, PHYPA, POPTR, RAT, RICCO, SORBI, TOXGO, TRYCR, VANPO
Plasmid: None
Comments: None
XX
# Revision 1.12 2023/06/01
//