ID   SYS_BLOPB               Reviewed;         428 AA.
AC   Q492S4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 35.
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=BPEN_395;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ41019.1; -; Genomic_DNA.
DR   RefSeq; YP_277894.1; -.
DR   GeneID; 3562760; -.
DR   GenomeReviews; CP000016_GR; BPEN_395.
DR   KEGG; bpn:BPEN_395; -.
DR   HOGENOM; Q492S4; -.
DR   OMA; Q492S4; LKPYMGG.
DR   BioCyc; CBLO291272:BPEN_395-MON; -.
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    428       Seryl-tRNA synthetase.
FT                                /FTId=PRO_1000019620.
FT   NP_BIND     266    268       ATP (By similarity).
FT   NP_BIND     353    356       ATP (By similarity).
FT   REGION      235    237       Serine binding (By similarity).
FT   BINDING     289    289       Serine (By similarity).
FT   BINDING     389    389       Serine (By similarity).
SQ   SEQUENCE   428 AA;  49049 MW;  8F15902A6680B518 CRC64;
     MIDPNLLRSN LDLVAKKLAR RKFILNINKF RQQESLRKIL QKKTESLQTE RKAKAKIIGV
     AKSRGENVEF LCQEAYVLGK KLTSLKLENK ELKNRIKQFE LSLPNIPDDQ VPYGFRDQDN
     LEIMRWGKPG QYNFPIRDHV ALGALTNGLD FSNATKLTGS RFIVMKGQIA HLHRALSQFM
     IDLHVKRHGY EEYYLPYLVN QDSLYGAGQL PKFYEDLFHI QHLQSGTNPY ALIPTAEVPL
     INLVRDVILD EEELPIKMVA HTPCFRYEAG SYGHHTRGLI RMHQFDKVEM VQVVHPDKSM
     QILEEITSHA EQVLQLLKLP YRKILLCTGN IGFSSCKTYD LEVWLPAYNA YCEVSSCSNV
     GDFQARRIRA RYKGRMNRKA RLLHTLNASG VAIGRALAAV LENYQLEDGR VAIPSVLSPY
     MSDITHIN
//