ID   SYS_BAUCH               Reviewed;         430 AA.
AC   Q1LTE8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Seryl-tRNA synthetase;
DE            EC=6.1.1.11;
DE   AltName: Full=Seryl-tRNA(Ser/Sec) synthetase;
DE   AltName: Full=Serine--tRNA ligase;
DE            Short=SerRS;
GN   Name=serS; OrderedLocusNames=BCI_0318;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
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; CP000238; ABF14125.1; -; Genomic_DNA.
DR   RefSeq; YP_588766.1; -.
DR   GeneID; 4056311; -.
DR   GenomeReviews; CP000238_GR; BCI_0318.
DR   KEGG; bci:BCI_0318; -.
DR   HOGENOM; Q1LTE8; -.
DR   OMA; Q1LTE8; LKPYMGG.
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    430       Seryl-tRNA synthetase.
FT                                /FTId=PRO_1000019618.
FT   NP_BIND     268    270       ATP (By similarity).
FT   NP_BIND     355    358       ATP (By similarity).
FT   REGION      237    239       Serine binding (By similarity).
FT   BINDING     291    291       Serine (By similarity).
FT   BINDING     391    391       Serine (By similarity).
SQ   SEQUENCE   430 AA;  49484 MW;  90A8E0735E80F9E5 CRC64;
     MLDPYLLRHD IKIVAKKLAS KNFLLAVDKV NQQEALRKQL QIKKEHLQFI RKSKSRIVNL
     AKANGENITI LCQEINQINE QLKQTKSELS SLKQLINDYM LLLPNIPADD VPYGSDKKDN
     IEIKRWGEPR KYNFPIKDHV NLGYITGNID FTAGVKLAGT RFVVIRGQIA RLYRALSQFM
     LDLHTQQHGY EEYYLPYLVN RTSLYGTGHL PKFYEDLFHI QSINKENISN IYTLIPTAEV
     PLINLLRDKI FDENILPLKM TANTPCFRAE AGSYGRDTHG LIRMHQFDKV EMVQAIKPEH
     SMIALEEMTK HAEKVLQLLN LHYRKVLLCT GDTGFASSKT YDLEVWLPSQ NIYCEVSSCS
     NTSDFQTRRV LARYRNKKDK QLRFLHTING SGLAIGRTLI AILENYQLAD GRIEVPKSLR
     SYMQGLTILG
//