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HAMAP rule MF_02006

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General rule information [?]

Accession MF_02006
Dates 24-APR-2006 (Created)
1-JUN-2023 (Last updated, Version 25)
Name Tyr_tRNA_synth_type1
Scope(s) Bacteria
Template(s) P0AGJ9 (SYY_ECOLI); P00952 (SYY_GEOSE); P41256 (SYY_ACIFR); Q57834 (SYY_METJA); [ Recover all ]
Triggered by HAMAP; MF_02006 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier SYY
Protein name RecName: Full=Tyrosine--tRNA ligase;
                 EC=6.1.1.1;
AltName: Full=Tyrosyl-tRNA synthetase;
                 Short=TyrRS;
Gene name Name=tyrS;

Comments [?]

FUNCTIONCatalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
CATALYTIC ACTIVITY Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L- tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706, Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442, ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1;
SUBUNITHomodimer.
SUBCELLULAR LOCATIONCytoplasm.
SIMILARITYBelongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily.

Keywords [?]


Gene Ontology [?]

GO:0004831; Molecular function:tyrosine-tRNA ligase activity
GO:0005524; Molecular function:ATP binding
GO:0006437; Biological process:tyrosyl-tRNA aminoacylation
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

PROSITE PS00178; AA_TRNA_LIGASE_I; 1;
PROSITE PS50889; S4; 1;
Pfam PF01479; S4; 1;
Pfam PF00579; tRNA-synt_1b; 1;
PRINTS PR01040; TRNASYNTHTYR; 1;
NCBIfam TIGR00234; TyrS; 1;

Features [?]

From: SYY_ECOLI (P0AGJ9)
Key From To Description Tag Condition FTGroup
MOTIF 42 51 /note="'HIGH' region" [PCATI]-[TS]-[AGES]-x-[SA]-[LMI]-[HT]-[ILVA]-G-[HNSG]
MOTIF 235 239 /note="'KMSKS' region" K-[FMILY]-G-K-[ST]
BINDING 37 37 /ligand="L-tyrosine"
/ligand_id="ChEBI:CHEBI:58315"
Y
BINDING 175 175 /ligand="L-tyrosine"
/ligand_id="ChEBI:CHEBI:58315"
Y
BINDING 179 179 /ligand="L-tyrosine"
/ligand_id="ChEBI:CHEBI:58315"
Q
BINDING 238 238 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
K
case <OC:Escherichia> or <OC:Shigella>
MOD_RES 144 144 /note="N6-acetyllysine" K
end case

Additional information [?]

Size range 391-471 amino acids
Related rules MF_02007
MF_02008
Fusion Nter: None Cter: 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.



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