ID F0L5S0_AGRSH Unreviewed; 427 AA.
AC F0L5S0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 03-APR-2013, entry version 17.
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=AGROH133_06621;
OS Agrobacterium sp. (strain H13-3) (Rhizobium lupini (strain H13-3)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX NCBI_TaxID=861208;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H13-3;
RX PubMed=21329740; DOI=10.1016/j.jbiotec.2011.01.010;
RA Wibberg D., Blom J., Jaenicke S., Kollin F., Rupp O., Scharf B.,
RA Schneiker-Bekel S., Sczcepanowski R., Goesmann A., Setubal J.C.,
RA Schmitt R., Puhler A., Schluter A.;
RT "Complete genome sequencing of Agrobacterium sp. H13-3, the former
RT Rhizobium lupini H13-3, reveals a tripartite genome consisting of a
RT circular and a linear chromosome and an accessory plasmid but lacking
RT a tumor-inducing Ti-plasmid.";
RL J. Biotechnol. 155:50-62(2011).
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; CP002248; ADY64632.1; -; Genomic_DNA.
DR RefSeq; YP_004278952.1; NC_015183.1.
DR EnsemblBacteria; ADY64632; ADY64632; AGROH133_06621.
DR GeneID; 10267421; -.
DR KEGG; agr:AGROH133_06621; -.
DR PATRIC; 46848147; VBIAgrSp164909_1678.
DR KO; K01875; -.
DR BioCyc; ASP861208:GH59-4283-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 262 264 ATP (By similarity).
FT NP_BIND 349 352 ATP (By similarity).
FT REGION 231 233 Serine binding (By similarity).
FT BINDING 285 285 Serine (By similarity).
FT BINDING 385 385 Serine (By similarity).
SQ SEQUENCE 427 AA; 47688 MW; 9D6E1F8C5B756073 CRC64;
MHDIKWIREN PEAFDAALAR RGAEPAASSL IALDEKRRSV IQSLQDMQSR RNAASKDIGA
AMAQKNMELA EKLKAEVADI KENMPRAEEE DRQVTAELND ALSRLPNIPF DDVPDGKDEH
DNVVTRVVGQ KPGWNHEAKE HFEIGEALGY MDFERAAKLS GSRFTVLTSQ LARLERALGQ
FMIDLHTSEH GYTEVSSPLM VRDEAMFGTG QLPKFSEDLF KTTDGRWLIP TAEVTLTNLV
SGEILEQEKL PLRFTALTPS FRSEAGSAGR DTRGMLRQHQ FWKCELVSIT DAESAVAEHE
RMTACAEEVL KRLGLHFRTM TLCTGDMGFS ARKTYDLEVW LPGQNTYREI SSCSVCGDFQ
ARRMNARYRG KDDKATKFVH TLNGSGTAVG RCLIAVLENY LNDDGSVTIP NVLLPYMGGL
KRIEKAA
//
