ID SYS_MYCSJ Reviewed; 417 AA.
AC A3Q7P6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 01-MAY-2013, entry version 51.
DE RecName: Full=Serine--tRNA ligase;
DE EC=6.1.1.11;
DE AltName: Full=Seryl-tRNA synthetase;
DE Short=SerRS;
DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase;
GN Name=serS; OrderedLocusNames=Mjls_5410;
OS Mycobacterium sp. (strain JLS).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX NCBI_TaxID=164757;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLS;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Miller C.D., Anderson A.J., Sims R.C., Richardson P.;
RT "Complete sequence of Mycobacterium sp. JLS.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000580; ABO01174.1; -; Genomic_DNA.
DR RefSeq; YP_001073664.1; NC_009077.1.
DR ProteinModelPortal; A3Q7P6; -.
DR STRING; 164757.Mjls_5410; -.
DR EnsemblBacteria; ABO01174; ABO01174; Mjls_5410.
DR GeneID; 4881107; -.
DR KEGG; mjl:Mjls_5410; -.
DR PATRIC; 18097101; VBIMycSp51234_5450.
DR eggNOG; COG0172; -.
DR HOGENOM; HOG000035937; -.
DR KO; K01875; -.
DR OMA; GPIRYAG; -.
DR ProtClustDB; PRK05431; -.
DR BioCyc; MSP164757:GHV3-5463-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 CHAIN 1 417 Serine--tRNA ligase.
FT /FTId=PRO_1000019739.
FT NP_BIND 257 259 ATP (By similarity).
FT NP_BIND 344 347 ATP (By similarity).
FT REGION 226 228 Serine binding (By similarity).
FT BINDING 273 273 ATP; via amide nitrogen and carbonyl
FT oxygen (By similarity).
FT BINDING 280 280 Serine (By similarity).
FT BINDING 379 379 Serine (By similarity).
SQ SEQUENCE 417 AA; 45304 MW; 4B47025B6AEA146F CRC64;
MIDLKFLREN PDAVRASQRS RGEDPALVDA LLDADAARRA AVSAADNLRA EQKAASKKVG
KASPEERPAL LTRAKELAEQ VKAAEAAQAD ADRTFTAAHM AISNVVIEGV PAGGEDCFAV
LDVVGEPRAI DDPKDHLELG EALGLIDMER GAKVAGSRFY FLTGRGALLQ LGLMQLAVRL
ATDNGFTLVI PPVLVRPEVM AGTGFLGAHA DEVYRLESDD MYLVGTSEVP LAGYHADEII
DLSAGPRRYA GWSSCFRREA GSYGKDTRGI IRVHQFDKVE GFIYCKPEDA AAEHDRLLGW
QREMLALIEV PYRVIDVAAG DLGSSAARKY DCEAWVPTQQ TYRELTSTSN CTTFQARRLS
TRYRDENGKP QIAATLNGTL ATTRWLVAIL ENHQQPDGSV RVPAALVPFV GTEVLEP
//
