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Database: UniProt
Entry: A0A0G0TP27_9BACT
LinkDB: A0A0G0TP27_9BACT
Original site: A0A0G0TP27_9BACT 
ID   A0A0G0TP27_9BACT        Unreviewed;       410 AA.
AC   A0A0G0TP27;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
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};
GN   ORFNames=UU21_C0007G0044 {ECO:0000313|EMBL:KKR76581.1};
OS   Candidatus Levybacteria bacterium GW2011_GWA2_40_8.
OC   Bacteria; Candidatus Levybacteria.
OX   NCBI_TaxID=1618459 {ECO:0000313|EMBL:KKR76581.1, ECO:0000313|Proteomes:UP000034541};
RN   [1] {ECO:0000313|EMBL:KKR76581.1, ECO:0000313|Proteomes:UP000034541}
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:KKR76581.1}.
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DR   EMBL; LBZT01000007; KKR76581.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0TP27; -.
DR   PATRIC; fig|1618459.3.peg.425; -.
DR   Proteomes; UP000034541; 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   CDD; cd00770; SerRS_core; 1.
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; IPR033729; SerRS_core.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKR76581.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          126..394
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   COILED          30..90
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   410 AA;  46757 MW;  671915726F8C9C88 CRC64;
     MLDIQFIREN PSLVQKSSIN KGININIDHV LEIDRKYREL QAKVQEIRAK RNTVAKEQNI
     EEGKKLKVQL EKEENALNAV GEELKEWLLK IPNLSKDDVK VGKDESDNEV VRKEGSPRKF
     VFTPKDHLAL GKSLEVIDVE RAAKISGSRF YFLKNEVVLL SFALKQLAFE TLIREGFIPV
     LPPVLINLEI MRGLGYMEGG GDEDMYVFEK DGLVLVGTSE QSLVAMHKDE TFNLSDLPKR
     YVGFSTCFRR EAGSYGKDTR GIIRAHQFDK VEMVSFIEKG QDDKEQEYLL SLEEKLLGLL
     NIPYQVVKVC SGELGYPAAR KYDLEAWIPS EGKYREVTSV STTTDFQSRR LNIKYQDKGK
     TEFVDILNGT AFSTRPIVSI LENYQNEDGS VSIPKALQKY LNFERISPKK
//
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