HAMAP rule MF_02006

General rule information [?]

Accession	MF_02006
Dates	24-APR-2006 (Created) 1-JUN-2023 (Last updated, Version 25)

Name	Tyr_tRNA_synth_type1

Scope

Bacteria

Templates

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

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	RHEA:10220: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr) 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>

Acetylation

end case

Aminoacyl-tRNA synthetase
ATP-binding
Cytoplasm
Ligase
Nucleotide-binding
Protein biosynthesis

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;
NCBIfam	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 /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 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.

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