Reviewed, UniProtKB/Swiss-Prot Q4KM49 (SYYC_RAT)

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

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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 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_0000239691
Regions
	Domain	364 – 468	105	tRNA-binding
	Motif	44 – 52	9	"HIGH" region By similarity
	Motif	222 – 226	5	"KMSKS" region By similarity
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
	Modified residue	197	1	N6-acetyllysine By similarity
	Modified residue	206	1	N6-acetyllysine By similarity
	Modified residue	272	1	N6-acetyllysine By similarity
	Modified residue	474	1	N6-acetyllysine By similarity
	Modified residue	482	1	N6-acetyllysine By similarity
	Modified residue	490	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4KM49-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: AD79FC551BEC9CBA	FASTA	528	59,115
	10 20 30 40 50 60 MGDAPSPEEK LHLITRNLQE VLGEEKLKEI LKERELKVYW GTATTGKPHV AYFVPMSKIA 70 80 90 100 110 120 DFLKAGCEVT ILFADLHAYL DNMKAPWELL ELRTSYYENV IKAMLESIGV PLEKLKFTKG 130 140 150 160 170 180 TDYQLSKEYT LDVYRLSSLV TQHDAKKAGA EVVKQVEHPL LSGLLYPGLQ ALDEEYLKVD 190 200 210 220 230 240 AQFGGIDQRK IFTFAEKYLP TLGYSKRVHL MNPMVPGLTG SKMSSSEEES KIDLLDRKED 250 260 270 280 290 300 VKKKLKKAFC EPGNVENNGV LSFVKHVLFP LKSEFVILRD EKWGGNKTYT IYQELEKDFA 310 320 330 340 350 360 AEVVHPGDLK NSVEVALNKL LDPIREKFNT PALKKLASAA YPDPSKQKPT AKGPAKSSEP 370 380 390 400 410 420 EEIIPSRLDI RVGKILSVEK HPDADSLYVE KIDVGEAEPR TVVSGLVQFV PKEELQDRLV 430 440 450 460 470 480 VVLCNLKPQK MRGVDSQGML LCASVEGVSR QVEPLDPPAG SAPGERVFVQ GYEKGQPDEE 490 500 510 520 LKPKKKVFEK LQADFKISDD CVAQWKQTNF MTKLGFVSCK SLKGGNIS

References

[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Spleen.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC098795 mRNA. Translation: AAH98795.1.
IPI	IPI00366785.
RefSeq	NP_001020867.1.
UniGene	Rn.41002
3D structure databases
SMR	Q4KM49. Positions 4-342, 360-528.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4KM49.
PTM databases
PhosphoSite	Q4KM49.
Genome annotation databases
Ensembl	ENSRNOT00000010674; ENSRNOP00000010674; ENSRNOG00000007213; Rattus norvegicus. [Genome view]
GeneID	313047.
KEGG	rno:313047.
NMPDR	fig|10116.3.peg.23990.
UCSC	NM_001025696. rat.
Organism-specific databases
CTD	313047.
RGD	1307616. Yars.
Phylogenomic databases
eggNOG	roNOG09132.
HOVERGEN	Q4KM49.
InParanoid	Q4KM49.
OMA	LCASIEG.
OrthoDB	EOG9THZCN.
PhylomeDB	Q4KM49.
Enzyme and pathway databases
BRENDA	6.1.1.1. 248.
Gene expression databases
ArrayExpress	Q4KM49.
Genevestigator	Q4KM49.
GermOnline	ENSRNOG00000007213. Rattus norvegicus.
Family and domain databases
InterPro	IPR002305. aa-tRNA-synth_Ib. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR014729. Rossmann-like_a/b/a_fold. IPR002547. tRNA-bd_dom. 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	PS50886. TRBD. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	665526.

Entry information

Entry name

SYYC_RAT

Accession

Primary (citable) accession number: Q4KM49

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 13, 2006
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 39 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)