Reviewed, UniProtKB/Swiss-Prot Q29465 (SYYC_BOVIN)

Names and origin

Protein names

Recommended name:
    Tyrosyl-tRNA synthetase, cytoplasmic
    EC=6.1.1.1
Alternative name(s):
    Tyrosyl--tRNA ligase
      Short name=TyrRS

Gene names

Name:	YARS
Synonyms:	TYRS

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	528 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (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) By similarity.
Catalytic activity	ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr).
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. Contains 1 tRNA-binding domain.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding RNA-binding tRNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation
Gene Ontology (GO)
Biological process	tyrosyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from sequence or structural similarity. Source: AgBase tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW tyrosine-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 528	527	Tyrosyl-tRNA synthetase, cytoplasmic		PRO_0000055672
Regions
	Domain	364 – 468	105	tRNA-binding
	Motif	44 – 52	9	"HIGH" region
	Motif	222 – 226	5	"KMSKS" region
Sites
	Binding site	39	1	Tyrosine By similarity
	Binding site	166	1	Tyrosine By similarity
	Binding site	170	1	Tyrosine By similarity
	Binding site	173	1	Tyrosine By similarity
	Binding site	188	1	Tyrosine By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylglycine By similarity
Experimental info
	Sequence conflict	21	1	V → A in CAA65245. Ref.2
	Sequence conflict	202	1	L → P in CAA65245. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q29465-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 44D16CB9F75EA7C3	FASTA	528	59,149
	10 20 30 40 50 60 MGDSLSPEEK LSLITRNLQE VLGEEKLKEI LKERELKVYW GTATTGKPHV AYFVPMSKIA 70 80 90 100 110 120 DFLKAGCEVT ILFADLHAYL DNMKAPWDVL ELRTSYYENV IKAMLESIGV PLEKLRFIKG 130 140 150 160 170 180 TDYQLSKEYT LDVYRLSSVV TQHDAKKAGA EVVKQVEHPL LSGLLYPGLQ ALDEEYLKVD 190 200 210 220 230 240 AQFGGVDQRK IFTFAEKYLP ALGYSKRIHL MNPMVPGLTG SKMSSSEEES KIDLLDRKED 250 260 270 280 290 300 VKKKLKKAFC EPGNVENNGV LAFIRHVLFP LKSEFVILRD EKWGGNKTYT AYLDLEKDFA 310 320 330 340 350 360 DEVVHPGDLK NSVEVALNKL LDPIREKFNT PALKKLSSAA YPDPSKQKPA VKGPAKNSEP 370 380 390 400 410 420 EEVIPSRLDI RVGKVISVDK HPDADSLYVE KIDVGEAEPR TVVSGLVQFV PKEELQDRLV 430 440 450 460 470 480 VVLCNLKPQK MRGVKSQGML LCASVEGVNR KVEPLDPPAG SAPGERVFVK GYEKGQPDEE 490 500 510 520 LKPKKKVFEK LQADFKISDE YIAQWKQTNF MTKMGSVSCK SLKGGNIS

References

[1]

"Amino acid sequence of bovine tyrosyl-tRNA synthetase. Possible generation of the isolated cytokine-like C-terminal domain via proteolytic cleavage at the 'PEST'-like sequence." Levanets O.V., Naidenov V.G., Odynets K.A., Woodmaska M.I., Matsuka G.K.H., Wientjes F.-J., Gassen H.G., Kornelyuk A.I. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.

[2]

"PCR-amplification, cloning and sequencing of nucleotide-binding domain of mammalian tyrosyl-tRNA synthetase." Levanets O.V., Naidenov V.G., Woodmaska M.I., Odynets K.A., Matsuka G.H., Kornelyuk A.I. Biopolim. Kletka 12:66-71(1996) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-212. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF087021 mRNA. Translation: AAC82467.1. X96373 Genomic DNA. Translation: CAA65245.1.
IPI	IPI00687540.
RefSeq	NP_776645.1.
UniGene	Bt.4535
3D structure databases
HSSP	HSSP built from PDB template 1N3L based on UniProtKB P54577.
SMR	Q29465. Positions 5-341, 6-342, 359-527, 360-528.
ModBase	Search...
Genome annotation databases
Ensembl	ENSBTAG00000018065. Bos taurus. [Contig view]
GeneID	281581.
KEGG	bta:281581.
Phylogenomic databases
HOVERGEN	Q29465.
Enzyme and pathway databases
BRENDA	6.1.1.1. 251.
Family and domain databases
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002305. aa-tRNA-synth_Ib. IPR012340. NA-bd_OB-fold. IPR014729. Rossmann-like_a/b/a_fold. IPR002547. tRNA_bd. IPR015624. Tyr-tRNA-synth_Ib_arc/euk. IPR002307. Tyr-tRNA-synth_Ib_bac/mito. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHER	PTHR11946:SF8. Tyr-tRNA_synth. 1 hit.
Pfam	PF00579. tRNA-synt_1b. 1 hit. PF01588. tRNA_bind. 1 hit. [Graphical view]
PRINTS	PR01040. TRNASYNTHTYR.
TIGRFAMs	TIGR00234. tyrS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. False negative. PS50886. TRBD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYYC_BOVIN

Accession

Primary (citable) accession number: Q29465
Secondary accession number(s): Q9TSJ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 64 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)