(data stored in SCRATCH zone)

SWISSPROT: D6XV08_BACIE

ID   D6XV08_BACIE            Unreviewed;       424 AA.
AC   D6XV08;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 66.
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            Short=SerRS {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   OrderedLocusNames=Bsel_0015 {ECO:0000313|EMBL:ADH97566.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97566.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97566.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) 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). {ECO:0000256|HAMAP-
CC       Rule:MF_00176}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) +
CC         L-seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742,
CC         Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00176};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) +
CC         L-seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669,
CC         Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC         Evidence={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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00176}.
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DR   EMBL; CP001791; ADH97566.1; -; Genomic_DNA.
DR   RefSeq; WP_013170996.1; NC_014219.1.
DR   STRING; 439292.Bsel_0015; -.
DR   EnsemblBacteria; ADH97566; ADH97566; Bsel_0015.
DR   KEGG; bse:Bsel_0015; -.
DR   eggNOG; ENOG4105CGR; Bacteria.
DR   eggNOG; COG0172; LUCA.
DR   HOGENOM; HOG000035937; -.
DR   KO; K01875; -.
DR   OMA; SPCFRRE; -.
DR   OrthoDB; 353391at2; -.
DR   BioCyc; BSEL439292:G1GLR-18-MONOMER; -.
DR   UniPathway; UPA00906; UER00895.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00770; SerRS_core; 1.
DR   Gene3D; 1.10.287.40; -; 1.
DR   HAMAP; MF_00176; Ser_tRNA_synth_type1; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
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; IPR042103; SerRS_1_N_sf.
DR   InterPro; IPR033729; SerRS_core.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   PANTHER; PTHR43697; PTHR43697; 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;
DR   PRODOM; D6XV08.
DR   SWISS-2DPAGE; D6XV08.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00176,
KW   ECO:0000313|EMBL:ADH97566.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00176, ECO:0000313|EMBL:ADH97566.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   DOMAIN      166    410       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
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   COILED       31     96       {ECO:0000256|SAM:Coils}.
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   424 AA;  48452 MW;  9625A5F8C86BF290 CRC64;
     MLDMKRLRAD FEGVREKLAT RNEDISALDD FQKLDEERRQ VIQKVEELKG KRNTVSEEIS
     KMKRNKEDAS DVIAEMKDVS AEIKALDEKQ RDVDEKMKTL MLSIPNIPHE SAPVGLDETE
     NEEIRTWGER PAFDFEGKAH WDLAVTHDIV DFERASKITG SRFAIYKGAG ARLERALMNF
     MMDFHEDKHG YTEVLPPYMV NRDSMTGTGQ LPKFEEDAFQ IREEDYFLIP TAEVPVTNMH
     RDEILTADEL PIAYSAFSAC FRSEAGSAGR DTRGLIRQHQ FNKVELVRFV KPEDSYAELE
     KLTGHAEKIL QQLNLPYRVL NMCTGDLGFT AAKKYDIEVW LPSYGEYKEI SSCSNFEDFQ
     ARRANIRFKR DQKGKAEFVH TLNGSGLAIG RTVAAILENY QQADGTIKIP KVLQPYMGGK
     TRIG
//

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