AC   MF_02009;
DC   Protein; auto
TR   HAMAP; MF_02009; -; 1; level=0
XX
Names: Tyr_tRNA_synth_type4
XX
ID   SYY
DE   RecName: Full=Tyrosine--tRNA ligase;
DE            EC=6.1.1.1;
DE   AltName: Full=Tyrosyl-tRNA synthetase;
DE            Short=TyrRS;
GN   Name=tyrS;
XX
CC   -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-
CC       step reaction: tyrosine is first activated by ATP to form Tyr-AMP and
CC       then transferred to the acceptor end of tRNA(Tyr).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-
CC         tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706,
CC         Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       TyrS type 4 subfamily.
XX
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1; trigger=no
DR   Pfam; PF00579; tRNA-synt_1b; 1; trigger=no
DR   PRINTS; PR01040; TRNASYNTHTYR; 1; trigger=no
DR   NCBIfam; TIGR00234; TyrS; 1; trigger=no
XX
KW   Cytoplasm
KW   Aminoacyl-tRNA synthetase
KW   ATP-binding
KW   Ligase
KW   Nucleotide-binding
KW   Protein biosynthesis
XX
GO   GO:0004831; F:tyrosine-tRNA ligase activity
GO   GO:0005524; F:ATP binding
GO   GO:0006437; P:tyrosyl-tRNA aminoacylation
GO   GO:0005737; C:cytoplasm
XX
FT   From: SYY_AERPE (Q9YA64)
FT   MOTIF           238..242
FT                   /note="'KMSKS' region"
FT   Condition: K-M-S-K-S
FT   BINDING         39
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT   Condition: Y
FT   BINDING         165
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT   Condition: Y
FT   BINDING         169
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT   Condition: Q
FT   BINDING         172
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT   Condition: D
FT   BINDING         187
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT   Condition: Q
FT   BINDING         241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: K
XX
Size: 316-376;
Related: MF_02006; MF_02007; MF_02008;
Template: P0AGJ9; P00952; P41256; Q57834; O29482; Q9YA64; O58739;
Scope:
 Archaea; Thermoproteota
 Archaea; Euryarchaeota
 Archaea; Nanoarchaeota
Fusion:
 Nter: None
 Cter: None
Duplicate: in PYRAE
Plasmid: None
Comments: None
XX
# Revision 1.16 2023/06/01
//