Q834C7 (SYY2_ENTFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine--tRNA ligase 2
EC=6.1.1.1

Alternative name(s):
Tyrosyl-tRNA synthetase 2
Short name=TyrRS 2

Gene names

Name:	tyrS2
Synonyms:	tyrS-2
Ordered Locus Names:	EF_1739

Organism

Enterococcus faecalis (Streptococcus faecalis)

Taxonomic identifier

1351 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Enterococcaceae › Enterococcus

Protein attributes

Sequence length	420 AA.
Sequence status	Complete.
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. HAMAP MF_02006
Catalytic activity	ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). HAMAP MF_02006
Subunit structure	Homodimer By similarity. HAMAP MF_02006
Subcellular location	Cytoplasm By similarity HAMAP MF_02006.
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 Reference proteome
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 RNA 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
	Chain	1 – 420	420	Tyrosine--tRNA ligase 2 HAMAP MF_02006		PRO_0000234709
Regions
	Domain	354 – 420	67	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	171	1	Tyrosine By similarity
	Binding site	175	1	Tyrosine By similarity
	Binding site	234	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q834C7 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 95F889502EB2E168	FASTA	420	47,637
	10 20 30 40 50 60 MNSAFFEELK ARGLVYQVTD EEALQKQLNE ESVKLYIGFD PTADSLHIGH LLPILMLRRF 70 80 90 100 110 120 QQNGHVPIAL VGGGTGMIGD PSFKDAERSL NTLDTVKAWS ESIKGQLSRF IDFEDEKNPA 130 140 150 160 170 180 ILANNYDWLG ELSLIDFLRD VGKNFTINYM MSKESVKRRI ETGISYTEFA YQLLQAYDFL 190 200 210 220 230 240 KLYETEGCLL QLGGSDQWGN ITSGIELLRR EQEVQGFGLT MPLITKADGT KFGKTEGNAV 250 260 270 280 290 300 WLDAEKTSPY EFYQFWINTD DRDVVKFLKY FTFLTLDEIA TIEEEFTANP GQRAAQKALA 310 320 330 340 350 360 KEVTTLVHGE AAYHQAVKIS EALFSGDIQS LTAEEIKQGF KDVPTYEVQP EDQLSLVDLL 370 380 390 400 410 420 VTSKIEPSKR QAREDVQNGA IYVNGERRQD LAAELTETDK IEGQFTVIRR GKKKYFLLKY

References

[1]

"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: ATCC 700802 / V583.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016830 Genomic DNA. Translation: AAO81513.1.
RefSeq	NP_815443.1. NC_004668.1.
3D structure databases
ProteinModelPortal	Q834C7.
SMR	Q834C7. Positions 8-320, 322-420.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1200630.
GenomeReviews	Gene locus EF_1739 in contig AE016830_GR.
KEGG	efa:EF1739.
NMPDR	fig|226185.1.peg.1628.
PATRIC	21853818. VBIEntFae7065_1635.
TIGR	EF_1739.
Phylogenomic databases
HOGENOM	HBG288125.
OMA	TFYIGFD.
ProtClustDB	PRK05912.
Enzyme and pathway databases
BioCyc	EFAE226185:EF_1739-MONOMER.
Family and domain databases
HAMAP	MF_02006. Tyr_tRNA_synth_type1. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002305. aa-tRNA-synth_Ic. IPR014729. Rossmann-like_a/b/a_fold. IPR002942. S4_RNA-bd. IPR002307. Tyr-tRNA-synth. IPR024088. Tyr-tRNA-synth_bac-type. IPR024107. Tyr-tRNA-synth_bac_1. [Graphical view]
Gene3D	G3DSA:3.10.290.10. G3DSA:3.10.290.10. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KO	K01866.
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

SYY2_ENTFA

Accession

Primary (citable) accession number: Q834C7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program