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Annotation rule MF_02006
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General rule information [?]

Accession MF_02006
Dates 24-APR-2006 (Created)
5-AUG-2019 (Last updated, Version 21)
Name Tyr_tRNA_synth_type1
Scope
Bacteria
Templates P0AGJ9 (SYY_ECOLI); P00952 (SYY_GEOSE); P41256 (SYY_ACIFR); Q57834 (SYY_METJA): [Recover all]

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
tyrS

Comments [?]

Function Catalyzes 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;.
Subunit Homodimer.
Subcellular location Cytoplasm.
Similarity Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily.

Keywords [?]

case <FT:7>
end case

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;
PS50889; S4; 1; trigger=PRU00182;
Pfam PF01479; S4; 1;
PF00579; tRNA-synt_1b; 1;
PRINTS PR01040; TRNASYNTHTYR; 1;
TIGRFAMs TIGR00234; TyrS; 1;

Features [?]

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

Additional information [?]

Size range 391-471 amino acids
Related rules MF_02007 (SYY); MF_02008 (SYY)
Fusion 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.