Reviewed, UniProtKB/Swiss-Prot Q82YY9 (SYS2_ENTFA)

Names and origin

Protein names

Recommended name:
    Seryl-tRNA synthetase 2
    EC=6.1.1.11
Alternative name(s):
    Seryl-tRNA(Ser/Sec) synthetase 2
    Serine--tRNA ligase 2
      Short name=SerRS 2

Gene names

Name:	serS2
Synonyms:	serS-2
Ordered Locus Names:	EF_3292

Organism

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

Taxonomic identifier

1351 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Enterococcaceae › Enterococcus

Protein attributes

Sequence length	423 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 serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) By similarity.
Catalytic activity	ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). HAMAP MF_00176 ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP MF_00176
Pathway	Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. HAMAP MF_00176
Subunit structure	Homodimer. The tRNA molecule binds across the dimer By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	selenocysteine biosynthetic process Inferred from electronic annotation. Source: HAMAP seryl-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 serine-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 – 423	423	Seryl-tRNA synthetase 2 HAMAP MF_00176		PRO_0000122048
Regions
	Nucleotide binding	262 – 264	3	ATP By similarity
	Nucleotide binding	349 – 352	4	ATP By similarity
	Region	231 – 233	3	Serine binding By similarity
Sites
	Binding site	285	1	Serine By similarity
	Binding site	384	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q82YY9-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: B70A4BB73C4C36AE	FASTA	423	48,123
	10 20 30 40 50 60 MLDVKMMRQN FDEVKAKLQT RGVKEEILVE FLRLDESRRD LLVKVEEMKK YRNDVSAEIA 70 80 90 100 110 120 QLKRNKEDAT AKIAEMKEVG GNIKALDAEI NAIDEELRGI TTTLPNLPDD SVPVGAGEEE 130 140 150 160 170 180 NVEVRRWSEP RTFAFEPKPH WEVAENLGIL DFERGAKVAG SRFVYYKGLG ARLERALYNF 190 200 210 220 230 240 MLDLHVYEHG YTEMITPYIV NDTAMFGTGQ FPKFKEDVFQ LQDTDLTLIP TAEVPLTNYY 250 260 270 280 290 300 NNEILDGKDL PIYFTALSPS FRSEAGSAGR DTRGLIRLHQ FNKVEMVKFS DAEHSYEELE 310 320 330 340 350 360 KMTNNAEEIL QKLGLPYRVM ALSTGDMGFS AAKTYDLEVW IPAQETYREI SSCSNCEDFQ 370 380 390 400 410 420 ARRAMIRYRD ENDKVQYAHT LNGSGLAVGR TVAAILENYQ NEDGSVTVPE VLVPYMGNLT VIK

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: V583 / ATCC 700802.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016830 Genomic DNA. Translation: AAO82957.1.
RefSeq	NP_816887.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1202135.
GenomeReviews	Gene locus EF_3292 in contig AE016830_GR.
KEGG	efa:EF3292.
NMPDR	fig|226185.1.peg.3072.
TIGR	EF_3292.
Phylogenomic databases
HOGENOM	Q82YY9.
OMA	Q82YY9. IFKESEL.
Enzyme and pathway databases
BioCyc	EFAE226185:EF_3292-MON.
BRENDA	6.1.1.11. 704.
Family and domain databases
HAMAP	MF_00176. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-reg. IPR006195. aa-tRNA-synth_II_cons-reg. IPR002317. Ser-tRNA-synth_IIa. IPR018156. Ser-tRNA-synth_IIa_C. IPR015866. Ser-tRNA-synth_IIa_N. [Graphical view]
Gene3D	G3DSA:1.10.287.40. Ser-tRNA-synth_IIa_N. 1 hit.
PANTHER	PTHR11778. tRNA-synt_ser. 1 hit.
Pfam	PF02403. Seryl_tRNA_N. 1 hit. PF00587. tRNA-synt_2b. 1 hit. [Graphical view]
PIRSF	PIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
PRINTS	PR00981. TRNASYNTHSER.
TIGRFAMs	TIGR00414. serS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYS2_ENTFA

Accession

Primary (citable) accession number: Q82YY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	June 1, 2003
Last modified:	June 16, 2009
This is version 37 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)