Reviewed, UniProtKB/Swiss-Prot A8Z2P6 (SYY_STAAT)

Names and origin

Protein names

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

Gene names

Name:	tyrS
Ordered Locus Names:	USA300HOU_1717

Organism

Staphylococcus aureus (strain USA300 / TCH1516) [Complete proteome] [HAMAP]

Taxonomic identifier

451516 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	420 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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). HAMAP MF_02006
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily. Contains 1 S4 RNA-binding domain.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	tyrosyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP RNA binding Inferred from electronic annotation. Source: UniProtKB-KW tyrosine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 420	420	Tyrosyl-tRNA synthetase HAMAP MF_02006		PRO_1000088631
Regions
	Domain	353 – 420	68	S4 RNA-binding
	Motif	41 – 50	10	"HIGH" region HAMAP MF_02006
	Motif	231 – 235	5	"KMSKS" region HAMAP MF_02006
Sites
	Binding site	36	1	Tyrosine By similarity
	Binding site	170	1	Tyrosine By similarity
	Binding site	174	1	Tyrosine By similarity
	Binding site	234	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8Z2P6-1 [UniParc]. Last modified January 15, 2008. Version 1. Checksum: B6916EA4BE4B21B2	FASTA	420	47,598
	10 20 30 40 50 60 MTNVLIEDLK WRGLIYQQTD EQGIEDLLNK EQVTLYCGAD PTADSLHIGH LLPFLTLRRF 70 80 90 100 110 120 QEHGHRPIVL IGGGTGMIGD PSGKSEERVL QTEEQVDKNI EGISKQMHNI FEFGTDHGAV 130 140 150 160 170 180 LVNNRDWLGQ ISLISFLRDY GKHVGVNYML GKDSIQSRLE HGISYTEFTY TILQAIDFGH 190 200 210 220 230 240 LNRELNCKIQ VGGSDQWGNI TSGIELMRRM YGQTDAYGLT IPLVTKSDGK KFGKSESGAV 250 260 270 280 290 300 WLDAEKTSPY EFYQFWINQS DEDVIKFLKY FTFLGKEEID RLEQSKNEAP HLREAQKTLA 310 320 330 340 350 360 EEVTKFIHGE DALNDAIRIS QALFSGDLKS LSAKELKDGF KDVPQVTLSN DTTNIVEVLI 370 380 390 400 410 420 ETGISPSKRQ AREDVNNGAI YINGERQQDV NYALAPEDKI DGEFTIIRRG KKKYFMVNYQ

References

[1]

"Subtle genetic changes enhance virulence of methicillin resistant and sensitive Staphylococcus aureus." Highlander S.K., Hulten K.G., Qin X., Jiang H., Yerrapragada S., Mason E.O. Jr., Shang Y., Williams T.M., Fortunov R.M., Liu Y., Igboeli O., Petrosino J., Tirumalai M., Uzman A., Fox G.E., Cardenas A.M., Muzny D.M., Hemphill L. , Ding Y., Dugan S., Blyth P.R., Buhay C.J., Dinh H.H., Hawes A.C., Holder M., Kovar C.L., Lee S.L., Liu W., Nazareth L.V., Wang Q., Zhou J., Kaplan S.L., Weinstock G.M. BMC Microbiol. 7:99-99(2007) [PubMed: 17986343] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000730 Genomic DNA. Translation: ABX29724.1.
RefSeq	YP_001575603.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5775803.
GenomeReviews	Gene locus USA300HOU_1717 in contig CP000730_GR.
KEGG	sax:USA300HOU_1717.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A8Z2P6. TFYIGFD.
Family and domain databases
HAMAP	MF_02006. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002305. aa-tRNA-synth_Ib. IPR014729. Rossmann-like_a/b/a_fold. IPR002942. S4_RNA_bd. IPR002307. Tyr-tRNA-synth_Ib_bac/mito. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHER	PTHR11766. Tyr_tRNA-synt_1b. 1 hit.
Pfam	PF01479. S4. 1 hit. PF00579. tRNA-synt_1b. 1 hit. [Graphical view]
PRINTS	PR01040. TRNASYNTHTYR.
SMART	SM00363. S4. 1 hit. [Graphical view]
TIGRFAMs	TIGR00234. tyrS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. PS50889. S4. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
BindingDB	A8Z2P6.

Entry information

Entry name

SYY_STAAT

Accession

Primary (citable) accession number: A8Z2P6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	January 15, 2008
Last modified:	June 16, 2009
This is version 13 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)