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Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)

 SYS_ORITI               Reviewed;         429 AA.
B3CQX9;
24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
22-JUL-2008, sequence version 1.
07-JUN-2017, entry version 55.
RecName: Full=Serine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00176};
EC=6.1.1.11 {ECO:0000255|HAMAP-Rule:MF_00176};
AltName: Full=Seryl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00176};
Short=SerRS {ECO:0000255|HAMAP-Rule:MF_00176};
AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000255|HAMAP-Rule:MF_00176};
Name=serS {ECO:0000255|HAMAP-Rule:MF_00176};
OrderedLocusNames=OTT_0428;
Orientia tsutsugamushi (strain Ikeda) (Rickettsia tsutsugamushi).
Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
Rickettsiaceae; Rickettsieae; Orientia.
NCBI_TaxID=334380;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ikeda;
PubMed=18508905; DOI=10.1093/dnares/dsn011;
Nakayama K., Yamashita A., Kurokawa K., Morimoto T., Ogawa M.,
Fukuhara M., Urakami H., Ohnishi M., Uchiyama I., Ogura Y., Ooka T.,
Oshima K., Tamura A., Hattori M., Hayashi T.;
"The whole-genome sequencing of the obligate intracellular bacterium
Orientia tsutsugamushi revealed massive gene amplification during
reductive genome evolution.";
DNA Res. 15:185-199(2008).
-!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also
able to aminoacylate tRNA(Sec) with serine, to form the
misacylated tRNA L-seryl-tRNA(Sec), which will be further
converted into selenocysteinyl-tRNA(Sec). {ECO:0000255|HAMAP-
Rule:MF_00176}.
-!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Ser) = AMP + diphosphate
+ L-seryl-tRNA(Ser). {ECO:0000255|HAMAP-Rule:MF_00176}.
-!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Sec) = AMP + diphosphate
+ L-seryl-tRNA(Sec). {ECO:0000255|HAMAP-Rule:MF_00176}.
-!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step
1/1. {ECO:0000255|HAMAP-Rule:MF_00176}.
-!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer.
{ECO:0000255|HAMAP-Rule:MF_00176}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00176}.
-!- DOMAIN: Consists of two distinct domains, a catalytic core and a
N-terminal extension that is involved in tRNA binding.
{ECO:0000255|HAMAP-Rule:MF_00176}.
-!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
family. Type-1 seryl-tRNA synthetase subfamily.
{ECO:0000255|HAMAP-Rule:MF_00176}.
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EMBL; AP008981; BAG39886.1; -; Genomic_DNA.
RefSeq; WP_012461101.1; NC_010793.1.
SMR; B3CQX9; -.
EnsemblBacteria; BAG39886; BAG39886; OTT_0428.
KEGG; ott:OTT_0428; -.
HOGENOM; HOG000035938; -.
KO; K01875; -.
OMA; SPCFRRE; -.
OrthoDB; POG091H01YY; -.
UniPathway; UPA00906; UER00895.
Proteomes; UP000001033; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-EC.
GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:InterPro.
CDD; cd00770; SerRS_core; 1.
HAMAP; MF_00176; Ser_tRNA_synth_type1; 1.
InterPro; IPR002314; aa-tRNA-synt_IIb.
InterPro; IPR006195; aa-tRNA-synth_II.
InterPro; IPR002317; Ser-tRNA-ligase_type_1.
InterPro; IPR015866; Ser-tRNA-synth_1_N.
InterPro; IPR033729; SerRS_core.
InterPro; IPR010978; tRNA-bd_arm.
PANTHER; PTHR43697; PTHR43697; 1.
Pfam; PF02403; Seryl_tRNA_N; 1.
Pfam; PF00587; tRNA-synt_2b; 1.
PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1.
PRINTS; PR00981; TRNASYNTHSER.
SUPFAM; SSF46589; SSF46589; 1.
TIGRFAMs; TIGR00414; serS; 1.
PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
3: Inferred from homology;
Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
Ligase; Nucleotide-binding; Protein biosynthesis.
CHAIN 1 429 Serine--tRNA ligase.
/FTId=PRO_1000098104.
NP_BIND 260 262 ATP. {ECO:0000255|HAMAP-Rule:MF_00176}.
NP_BIND 347 350 ATP. {ECO:0000255|HAMAP-Rule:MF_00176}.
REGION 229 231 Serine binding. {ECO:0000255|HAMAP-
Rule:MF_00176}.
BINDING 283 283 Serine. {ECO:0000255|HAMAP-
Rule:MF_00176}.
BINDING 383 383 Serine. {ECO:0000255|HAMAP-
Rule:MF_00176}.
SEQUENCE 429 AA; 48618 MW; D2692EDD3F091BCF CRC64;
MLDIKWIRAN PDKLDESLSK RGIDSVSKSI IHIDSEKRTL ISLIQKLQHE RKEKSSSVAH
IYDKSSTDFE EIQNDVKLIN QKITELETSL LHHEKRLSEI MDNLPNLVAD DVPYGTNSDM
NKVLKECGTI QNIKFPKHHY EIGKNLGMMD FNTATKMSGS RFVILKHDLA KLERALINFM
IDVHTTEFNF FEVSPPCLVK DHAMYNVGQL PKFADASFET TTGYRLIPTA EVPLTNIFAN
TTLLEEKLPI RLVAFTPCFR SEVGSAGKDV KGMLRMHQFG KVELFTIATP KESNREFEYL
TAAAEKILEK LGLPYRVVLL CSGDIGFAAH KTYDLEVWLP AQNCYREISS CSHFSSFQAR
RSLSKYRELC SKKVNFLHTI NGSGLAVGRT IIAILENYQN SDGSVTIPEK LRNYMGGQKL
ITPLTETVF


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