ID C7N3A7_SLAHD Unreviewed; 428 AA.
AC C7N3A7;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 29-MAY-2013, entry version 32.
DE RecName: Full=Serine--tRNA ligase;
DE EC=6.1.1.11;
DE AltName: Full=Seryl-tRNA synthetase;
DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase;
GN Name=serS; OrderedLocusNames=Shel_26270;
OS Slackia heliotrinireducens (strain ATCC 29202 / DSM 20476 / NCTC 11029
OS / RHS 1) (Peptococcus heliotrinreducens).
OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales;
OC Coriobacterineae; Coriobacteriaceae; Slackia.
OX NCBI_TaxID=471855;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29202 / DSM 20476 / NCTC 11029 / RHS 1;
RX PubMed=21304663; DOI=10.4056/sigs.37633;
RA Pukall R., Lapidus A., Nolan M., Copeland A., Glavina Del Rio T.,
RA Lucas S., Chen F., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA Goodwin L., Kuske C., Brettin T., Detter J.C., Han C., Pitluck S.,
RA Pati A., Mavrommatis K., Ivanova N., Ovchinnikova G., Chen A.,
RA Palaniappan K., Schneider S., Rohde M., Chain P., D'haeseleer P.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Kyrpides N.C.,
RA Klenk H.P., Hugenholtz P.;
RT "Complete genome sequence of Slackia heliotrinireducens type strain
RT (RHS 1).";
RL Stand. Genomic Sci. 1:234-241(2009).
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(Sec) = AMP + diphosphate
CC + L-seryl-tRNA(Sec).
CC -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Ser) = AMP + diphosphate
CC + L-seryl-tRNA(Ser).
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; CP001684; ACV23630.1; -; Genomic_DNA.
DR RefSeq; YP_003144979.1; NC_013165.1.
DR STRING; 471855.Shel_26270; -.
DR EnsemblBacteria; ACV23630; ACV23630; Shel_26270.
DR GeneID; 8396515; -.
DR KEGG; shi:Shel_26270; -.
DR PATRIC; 23644860; VBISlaHel66389_2613.
DR eggNOG; COG0172; -.
DR HOGENOM; HOG000035938; -.
DR KO; K01875; -.
DR OMA; EESWEWH; -.
DR ProtClustDB; PRK05431; -.
DR BioCyc; SHEL471855:GH2I-2627-MONOMER; -.
DR UniPathway; UPA00906; UER00895.
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:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:HAMAP.
DR Gene3D; 1.10.287.40; -; 1.
DR HAMAP; MF_00176; Ser_tRNA_synth_type1; 1; -.
DR InterPro; IPR002314; aa-tRNA-synt_IIb_cons-dom.
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; IPR010978; tRNA-bd_arm.
DR PANTHER; PTHR11778; PTHR11778; 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; tRNA_binding_arm; 1.
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 NP_BIND 261 263 ATP (By similarity).
FT NP_BIND 348 351 ATP (By similarity).
FT REGION 230 232 Serine binding (By similarity).
FT BINDING 277 277 ATP; via amide nitrogen and carbonyl
FT oxygen (By similarity).
FT BINDING 284 284 Serine (By similarity).
FT BINDING 385 385 Serine (By similarity).
SQ SEQUENCE 428 AA; 47979 MW; 3EDA0421A0B886C8 CRC64;
MLDIKFVREN QDVITQAMKN RNGSWDVDKF NELDESRRSY IADEEAMQAK RNTASKQIGA
LMREGKADEA EASKEEVRAL NEKIAEVSAK RSEAETALNE MLCRIPNIPH ESTPVGKDET
ENPEVRRWGT PRKFDFEFKA HWDLGADLNI IDSERATKLA GSRFVLLGGL GARLERALIN
FMADTHGSRG YKEWWCPVMA NGNTLYGTGQ LPKFEEDLFH TTEGLYLIPT AEVQLTNIHA
GDVLEASQLP LKYCGYTACF REEAGSAGRD TRGLIRVHQF DKVEMVKFAT PEDGFNQLEL
MVEDAENILQ LLGLPYRVIS LCTGDLGFSA AKTYDLEVWL PSYDAYKEIS SCSCCTDFQA
RRANIRYRDP NKFKGTRYVY TLNGSGLAVG RTMAAVMENY QQADGSIKVP DVLVPYMGGV
EVIAADQL
//
