AC   MF_02006;
DC   Protein; auto
TR   HAMAP; MF_02006; -; 1; level=0
XX
Names: Tyr_tRNA_synth_type1
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 1 subfamily.
XX
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1; trigger=no
DR   PROSITE; PS50889; S4; 1; trigger=yes
DR   Pfam; PF01479; S4; 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
case <FT:7>
KW   Acetylation
end case
KW   Aminoacyl-tRNA synthetase
KW   ATP-binding
KW   Cytoplasm
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_ECOLI (P0AGJ9)
FT   MOTIF           42..51
FT                   /note="'HIGH' region"
FT   Condition: [PCATI]-[TS]-[AGES]-x-[SA]-[LMI]-[HT]-[ILVA]-G-[HNSG]
FT   MOTIF           235..239
FT                   /note="'KMSKS' region"
FT   Condition: K-[FMILY]-G-K-[ST]
FT   BINDING         37
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT   Condition: Y
FT   BINDING         175
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT   Condition: Y
FT   BINDING         179
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT   Condition: Q
FT   BINDING         238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: K
case <OC:Escherichia> or <OC:Shigella>
FT   MOD_RES         144
FT                   /note="N6-acetyllysine"
FT   Condition: K
end case
XX
Size: 391-471;
Related: MF_02007; MF_02008;
Template: P0AGJ9; P00952; P41256; Q57834;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in BACAN, BACC1, BACCR, BACCZ, BACHK, ENTFA, STRT1, STRT2
Plasmid: None
Comments: Some species have a second copy of TyrRS in another subfamily (MF_02007).
 Shorter sequences in second copy of STRT1 and STRT2; sequences not included in
 alignment and not taken into account in size range.
XX
# Revision 1.25 2023/06/01
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