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Database: UniProt/TrEMBL
Entry: F0L5S0_AGRSH
LinkDB: F0L5S0_AGRSH
Original site: F0L5S0_AGRSH 
ID   F0L5S0_AGRSH            Unreviewed;       427 AA.
AC   F0L5S0;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   01-OCT-2014, entry version 26.
DE   RecName: Full=Serine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00176};
DE            EC=6.1.1.11 {ECO:0000256|HAMAP-Rule:MF_00176};
DE   AltName: Full=Seryl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00176};
DE   AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000256|HAMAP-Rule:MF_00176};
GN   Name=serS {ECO:0000256|HAMAP-Rule:MF_00176,
GN   ECO:0000313|EMBL:ADY64632.1};
GN   OrderedLocusNames=AGROH133_06621 {ECO:0000313|EMBL:ADY64632.1};
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 {ECO:0000313|EMBL:ADY64632.1, ECO:0000313|Proteomes:UP000007455};
RN   [1] {ECO:0000313|EMBL:ADY64632.1, ECO:0000313|Proteomes:UP000007455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H13-3 {ECO:0000313|EMBL:ADY64632.1,
RC   ECO:0000313|Proteomes:UP000007455};
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). {ECO:0000256|HAMAP-
CC       Rule:MF_00176}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Sec) = AMP + diphosphate
CC       + L-seryl-tRNA(Sec). {ECO:0000256|HAMAP-Rule:MF_00176}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Ser) = AMP + diphosphate
CC       + L-seryl-tRNA(Ser). {ECO:0000256|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
CC       1/1. {ECO:0000256|HAMAP-Rule:MF_00176}.
CC   -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer.
CC       {ECO:0000256|HAMAP-Rule:MF_00176}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176}.
CC   -!- DOMAIN: Consists of two distinct domains, a catalytic core and a
CC       N-terminal extension that is involved in tRNA binding.
CC       {ECO:0000256|HAMAP-Rule:MF_00176}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. Type-1 seryl-tRNA synthetase subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00176}.
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DR   EMBL; CP002248; ADY64632.1; -; Genomic_DNA.
DR   RefSeq; WP_013636277.1; NC_015183.1.
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   OMA; QMRTEEL; -.
DR   BioCyc; ASP861208:GH59-1665-MONOMER; -.
DR   UniPathway; UPA00906; UER00895.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-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; SSF46589; 1.
DR   TIGRFAMs; TIGR00414; serS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00176,
KW   ECO:0000313|EMBL:ADY64632.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007455};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00176}.
FT   NP_BIND     262    264       ATP. {ECO:0000256|HAMAP-Rule:MF_00176}.
FT   NP_BIND     349    352       ATP. {ECO:0000256|HAMAP-Rule:MF_00176}.
FT   REGION      231    233       Serine binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00176}.
FT   BINDING     285    285       Serine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00176}.
FT   BINDING     385    385       Serine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00176}.
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
//
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