(data stored in ACNUC7421 zone)

SWISSPROT: SYS_LEGPC

ID   SYS_LEGPC               Reviewed;         426 AA.
AC   A5IH84;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 79.
DE   RecName: Full=Serine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00176};
DE            EC=6.1.1.11 {ECO:0000255|HAMAP-Rule:MF_00176};
DE   AltName: Full=Seryl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00176};
DE            Short=SerRS {ECO:0000255|HAMAP-Rule:MF_00176};
DE   AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000255|HAMAP-Rule:MF_00176};
GN   Name=serS {ECO:0000255|HAMAP-Rule:MF_00176}; OrderedLocusNames=LPC_2833;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also able
CC       to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-
CC       seryl-tRNA(Sec), which will be further converted into selenocysteinyl-
CC       tRNA(Sec). {ECO:0000255|HAMAP-Rule:MF_00176}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-
CC         seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669,
CC         Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00176};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-
CC         seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742,
CC         Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00176};
CC   -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC       biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00176}.
CC   -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer.
CC       {ECO:0000255|HAMAP-Rule:MF_00176}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00176}.
CC   -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N-
CC       terminal extension that is involved in tRNA binding.
CC       {ECO:0000255|HAMAP-Rule:MF_00176}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type-1 seryl-tRNA synthetase subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00176}.
DR   EMBL; CP000675; ABQ56734.1; -; Genomic_DNA.
DR   RefSeq; WP_011945665.1; NC_009494.2.
DR   SMR; A5IH84; -.
DR   PRIDE; A5IH84; -.
DR   EnsemblBacteria; ABQ56734; ABQ56734; LPC_2833.
DR   KEGG; lpc:LPC_2833; -.
DR   HOGENOM; HOG000035938; -.
DR   KO; K01875; -.
DR   OMA; SPCFRRE; -.
DR   BioCyc; LPNE400673:LPC_RS02800-MONOMER; -.
DR   UniPathway; UPA00906; UER00895.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00770; SerRS_core; 1.
DR   Gene3D; 1.10.287.40; -; 1.
DR   HAMAP; MF_00176; Ser_tRNA_synth_type1; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR002317; Ser-tRNA-ligase_type_1.
DR   InterPro; IPR015866; Ser-tRNA-synth_1_N.
DR   InterPro; IPR042103; SerRS_1_N_sf.
DR   InterPro; IPR033729; SerRS_core.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   PANTHER; PTHR43697; PTHR43697; 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   SUPFAM; SSF46589; SSF46589; 1.
DR   TIGRFAMs; TIGR00414; serS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5IH84.
DR   SWISS-2DPAGE; A5IH84.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..426
FT                   /note="Serine--tRNA ligase"
FT                   /id="PRO_1000019715"
FT   NP_BIND         262..264
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   NP_BIND         349..352
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   REGION          231..233
FT                   /note="Serine binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   BINDING         285
FT                   /note="Serine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   BINDING         385
FT                   /note="Serine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
SQ   SEQUENCE   426 AA;  48153 MW;  011C0395EB8623E7 CRC64;
     MLDNQLLREN PQYVATQLLK RGFQFDAVTF SQLEEKRKAL QVSTQSLQNE RNLRSKAIGE
     AKSRGENIEP MREEVNKLGA KLEQQKTELD EVLKQIEVIS LSLPNIPHES VPVGKDELDN
     QEIRKWGDVP AFSFPVKSHD ELGEALGQMD FALAAKITGS RFVVMKGHLA RLHRALIQFM
     LDIHIQQHGY QEIYVPYIVN ADSLLGTGQL PKFEADLFKL TGDNGYYLTS TSEIPVTNTV
     REMILSAEQL PIRYVCHSPC FRSEAGSYGK DTKGMIRQHQ FEKVELVWIT KPEDSYNALE
     QLTQHAEVIL QRLNLPYRVV ALCTGDIGAG SAKTYDLEVW LPSQNTYREI SSCSNMEAFQ
     ARRMKARFRN PDTNEIQLVH TLNGSGLAVG RTLVAIMENY QDEHGNIHIP DALKPYLGGI
     DIISVK
//

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