Reviewed, UniProtKB/Swiss-Prot Q838D7 (SYY1_ENTFA)

Names and origin

Protein names

Recommended name:
    Tyrosyl-tRNA synthetase 1
    EC=6.1.1.1
Alternative name(s):
    Tyrosine--tRNA ligase 1
      Short name=TyrRS 1

Gene names

Name:	tyrS1
Synonyms:	tyrS-1
Ordered Locus Names:	EF_0633

Organism

Enterococcus faecalis (Streptococcus faecalis) [Complete proteome] [HAMAP]

Taxonomic identifier

1351 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Enterococcaceae › Enterococcus

Protein attributes

Sequence length	418 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 – 418	418	Tyrosyl-tRNA synthetase 1 HAMAP MF_02006		PRO_0000234708
Regions
	Domain	350 – 416	67	S4 RNA-binding
	Motif	39 – 48	10	"HIGH" region HAMAP MF_02006
	Motif	228 – 232	5	"KMSKS" region HAMAP MF_02006
Sites
	Binding site	34	1	Tyrosine By similarity
	Binding site	166	1	Tyrosine By similarity
	Binding site	170	1	Tyrosine By similarity
	Binding site	231	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q838D7-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 3136B3CBB783F9F8	FASTA	418	47,261
	10 20 30 40 50 60 MNIIDELAWR DAINQQTNEE GLRELTENTS ISLYCGVDPT GDSMHIGHLI PFMMMKRFQL 70 80 90 100 110 120 AGHHPYILIG GGTGTIGDPS GRTTERVLQT MEAVQHNVDS LSNQMKKLFG KDAEVTMVNN 130 140 150 160 170 180 YDWLSELSLL DFLRDYGKNF NVNTMLAKDI VASRLESGIS FTEFTYQILQ SIDFYTLHKK 190 200 210 220 230 240 HNIQLQIGGA DQWGNITAGL DLIRKKEGPE AKVFGLTIPL MLKADGTKFG KTAGGAIWLD 250 260 270 280 290 300 PKKTSPFEFY QFWLNQDDRD VIKYLKFFTF LDKEEIDALA EKVEKEPGKR EAQRRLAEEV 310 320 330 340 350 360 TRFVHDDAAL EEAQKISEAL FSGNIKDLTI EEIEQGLEHV PTVEITKDAK NIVDWLVDTE 370 380 390 400 410 IEPSKRQARE DVSGGAISIN GDRVTDLDFA VDPTQHFDGK FVVVRKGKKN YFLAKVMD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of the Enterococcus faecalis tyrosine decarboxylase operon involved in tyramine production." Connil N., Le Breton Y., Dousset X., Auffray Y., Rince A., Prevost H. Appl. Environ. Microbiol. 68:3537-3544(2002) [PubMed: 12089039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: JH2-2.
[2]	"Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis." Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin S.A. , Kolonay J.F., Madupu R., Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M. Science 299:2071-2074(2003) [PubMed: 12663927] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: V583 / ATCC 700802.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF354231 Genomic DNA. Translation: AAM46083.1. Different initiation. AE016830 Genomic DNA. Translation: AAO80458.1.
RefSeq	NP_814387.1.
3D structure databases
HSSP	HSSP built from PDB template 2TS1 based on UniProtKB P00952.
ModBase	Search...
Genome annotation databases
GeneID	1199534.
GenomeReviews	Gene locus EF_0633 in contig AE016830_GR.
KEGG	efa:EF0633.
NMPDR	fig|226185.1.peg.573.
TIGR	EF_0633.
Phylogenomic databases
HOGENOM	Q838D7.
OMA	ISLYCGV.
Enzyme and pathway databases
BioCyc	EFAE226185:EF_0633-MON.
BRENDA	6.1.1.1. 704.
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...

Entry information

Entry name

SYY1_ENTFA

Accession

Primary (citable) accession number: Q838D7
Secondary accession number(s): Q8KXD3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
This is version 39 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)