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Database: UniProt
Entry: A0A0G1VD56_9BACT
LinkDB: A0A0G1VD56_9BACT
Original site: A0A0G1VD56_9BACT 
ID   A0A0G1VD56_9BACT        Unreviewed;       359 AA.
AC   A0A0G1VD56;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Serine--tRNA ligase {ECO:0000256|ARBA:ARBA00039158};
DE            EC=6.1.1.11 {ECO:0000256|ARBA:ARBA00012840};
DE   AltName: Full=Seryl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031113};
DE   AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000256|ARBA:ARBA00033352};
DE   Flags: Fragment;
GN   ORFNames=UY03_C0047G0005 {ECO:0000313|EMBL:KKU76073.1};
OS   Parcubacteria group bacterium GW2011_GWA2_47_64.
OC   Bacteria.
OX   NCBI_TaxID=1618845 {ECO:0000313|EMBL:KKU76073.1, ECO:0000313|Proteomes:UP000034132};
RN   [1] {ECO:0000313|EMBL:KKU76073.1, ECO:0000313|Proteomes:UP000034132}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC       biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005045}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKU76073.1}.
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DR   EMBL; LCOL01000047; KKU76073.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1VD56; -.
DR   Proteomes; UP000034132; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 1.10.287.40; Serine-tRNA synthetase, tRNA binding domain; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
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; IPR010978; tRNA-bd_arm.
DR   NCBIfam; TIGR00414; serS; 1.
DR   PANTHER; PTHR43697:SF1; SERINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43697; SERYL-TRNA SYNTHETASE; 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; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF46589; tRNA-binding arm; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   4: Predicted;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKU76073.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          175..359
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          108..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         359
FT                   /evidence="ECO:0000313|EMBL:KKU76073.1"
SQ   SEQUENCE   359 AA;  41029 MW;  70AD031426BC9E95 CRC64;
     MLDIKFIREN KDLVAEAAKK KRVSFDVEEL LKLDDERRAL LTVVEKKRSE HNMKSNQMVR
     TSIPERRELL VEELRTQKSG LEEEETKLKG IMQKWQALML QAPNVPDISV PDGDSENDNS
     EVRTWGSIPE FSSPPKGHME IMESCDMADF LRGGDVSGFR GYFLKNEGAL LSFALWQFTL
     EHFAKKGFTF MMAPSLVRKQ TLLGTGYLPQ GEDDLYKTQD GDYLSGTSEV SAMSYFSETI
     LKKEELPKKI LAFSTCFRRE AGSYGKDTKG LIRVHEFFKL EQVMLCEASH EISVKFHEEL
     TGNAEELLQA LKLPYRVVIN CGGDLGLGQV KKYDIETWIP SDKAYRETHS SSYFHDFQT
//
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