ID SYS_MYCTA Reviewed; 419 AA.
AC A5U9G3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 01-MAY-2013, entry version 49.
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=MRA_3874;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RA Wang S.Y., Zheng H.J., Lv L.D., Wang B.F., Zhang X.L., Pu S.Y.,
RA Zhu G.F., Wang H.H., Zhao G.P., Zhang Y.;
RT "Complete genomic sequence of Mycobacterium tuberculosis strain H37Ra,
RT a non-pathogenic variant closely related to the well-characterized
RT pathogenic strain H37Rv.";
RL Submitted (MAR-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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP000611; ABQ75663.1; -; Genomic_DNA.
DR RefSeq; YP_001285225.1; NC_009525.1.
DR ProteinModelPortal; A5U9G3; -.
DR SMR; A5U9G3; 1-417.
DR STRING; 419947.MRA_3874; -.
DR EnsemblBacteria; ABQ75663; ABQ75663; MRA_3874.
DR GeneID; 5211930; -.
DR KEGG; mra:MRA_3874; -.
DR PATRIC; 18148277; VBIMycTub106795_4316.
DR eggNOG; COG0172; -.
DR HOGENOM; HOG000035937; -.
DR KO; K01875; -.
DR OMA; GPIRYAG; -.
DR ProtClustDB; PRK05431; -.
DR BioCyc; MTUB419947:GJ8N-3995-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 1 419 Serine--tRNA ligase.
FT /FTId=PRO_1000019742.
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 419 AA; 45324 MW; BC01C9FC2FF34FB5 CRC64;
MIDLKLLREN PDAVRRSQLS RGEDPALVDA LLTADAARRA VISTADSLRA EQKAASKSVG
GASPEERPPL LRRAKELAEQ VKAAEADEVE AEAAFTAAHL AISNVIVDGV PAGGEDDYAV
LDVVGEPSYL ENPKDHLELG ESLGLIDMQR GAKVSGSRFY FLTGRGALLQ LGLLQLALKL
AVDNGFVPTI PPVLVRPEVM VGTGFLGAHA EEVYRVEGDG LYLVGTSEVP LAGYHSGEIL
DLSRGPLRYA GWSSCFRREA GSHGKDTRGI IRVHQFDKVE GFVYCTPADA EHEHERLLGW
QRQMLARIEV PYRVIDVAAG DLGSSAARKF DCEAWIPTQG AYRELTSTSN CTTFQARRLA
TRYRDASGKP QIAATLNGTL ATTRWLVAIL ENHQRPDGSV RVPDALVPFV GVEVLEPVA
//
