ID   SYS2_ENTFA              Reviewed;         423 AA.
AC   Q82YY9;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-JUN-2009, entry version 37.
DE   RecName: Full=Seryl-tRNA synthetase 2;
DE            EC=6.1.1.11;
DE   AltName: Full=Seryl-tRNA(Ser/Sec) synthetase 2;
DE   AltName: Full=Serine--tRNA ligase 2;
DE            Short=SerRS 2;
GN   Name=serS2; Synonyms=serS-2; OrderedLocusNames=EF_3292;
OS   Enterococcus faecalis (Streptococcus faecalis).
OC   Bacteria; Firmicutes; Lactobacillales; Enterococcaceae; Enterococcus.
OX   NCBI_TaxID=1351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V583 / ATCC 700802;
RX   MEDLINE=22550857; PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F.,
RA   Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J.,
RA   Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A.,
RA   Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant
RT   Enterococcus faecalis.";
RL   Science 299:2071-2074(2003).
CC   -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also
CC       able to aminoacylate tRNA(Sec) with serine, to form the
CC       misacylated tRNA L-seryl-tRNA(Sec), which will be further
CC       converted into selenocysteinyl-tRNA(Sec) (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Ser) = AMP + diphosphate
CC       + L-seryl-tRNA(Ser).
CC   -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Sec) = AMP + diphosphate
CC       + L-seryl-tRNA(Sec).
CC   -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC       biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step
CC       1/1.
CC   -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- DOMAIN: Consists of two distinct domains, a catalytic core and a
CC       N-terminal extension that is involved in tRNA binding (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. Type-1 seryl-tRNA synthetase subfamily.
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DR   EMBL; AE016830; AAO82957.1; -; Genomic_DNA.
DR   RefSeq; NP_816887.1; -.
DR   GeneID; 1202135; -.
DR   GenomeReviews; AE016830_GR; EF_3292.
DR   KEGG; efa:EF3292; -.
DR   NMPDR; fig|226185.1.peg.3072; -.
DR   TIGR; EF_3292; -.
DR   HOGENOM; Q82YY9; -.
DR   OMA; Q82YY9; IFKESEL.
DR   BioCyc; EFAE226185:EF_3292-MON; -.
DR   BRENDA; 6.1.1.11; 704.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004828; F:serine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:HAMAP.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00176; -; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb_cons-reg.
DR   InterPro; IPR006195; aa-tRNA-synth_II_cons-reg.
DR   InterPro; IPR002317; Ser-tRNA-synth_IIa.
DR   InterPro; IPR018156; Ser-tRNA-synth_IIa_C.
DR   InterPro; IPR015866; Ser-tRNA-synth_IIa_N.
DR   Gene3D; G3DSA:1.10.287.40; Ser-tRNA-synth_IIa_N; 1.
DR   PANTHER; PTHR11778; tRNA-synt_ser; 1.
DR   Pfam; PF02403; Seryl_tRNA_N; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1.
DR   PRINTS; PR00981; TRNASYNTHSER.
DR   TIGRFAMs; TIGR00414; serS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    423       Seryl-tRNA synthetase 2.
FT                                /FTId=PRO_0000122048.
FT   NP_BIND     262    264       ATP (By similarity).
FT   NP_BIND     349    352       ATP (By similarity).
FT   REGION      231    233       Serine binding (By similarity).
FT   BINDING     285    285       Serine (By similarity).
FT   BINDING     384    384       Serine (By similarity).
SQ   SEQUENCE   423 AA;  48123 MW;  B70A4BB73C4C36AE CRC64;
     MLDVKMMRQN FDEVKAKLQT RGVKEEILVE FLRLDESRRD LLVKVEEMKK YRNDVSAEIA
     QLKRNKEDAT AKIAEMKEVG GNIKALDAEI NAIDEELRGI TTTLPNLPDD SVPVGAGEEE
     NVEVRRWSEP RTFAFEPKPH WEVAENLGIL DFERGAKVAG SRFVYYKGLG ARLERALYNF
     MLDLHVYEHG YTEMITPYIV NDTAMFGTGQ FPKFKEDVFQ LQDTDLTLIP TAEVPLTNYY
     NNEILDGKDL PIYFTALSPS FRSEAGSAGR DTRGLIRLHQ FNKVEMVKFS DAEHSYEELE
     KMTNNAEEIL QKLGLPYRVM ALSTGDMGFS AAKTYDLEVW IPAQETYREI SSCSNCEDFQ
     ARRAMIRYRD ENDKVQYAHT LNGSGLAVGR TVAAILENYQ NEDGSVTVPE VLVPYMGNLT
     VIK
//